|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-507 |
9.65e-170 |
|
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: 487.01 E-value: 9.65e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 4 FISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPIN 83
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 84 HKLQAPEVSYILRHSGARLclvdgarasLITAIqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaphal 163
Cdd:COG0318 81 PRLTAEELAYILEDSGARA---------LVTAL----------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 aeILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFL 243
Cdd:COG0318 105 --ILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 244 ETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYrSDRFMQVYGMTESGPLGTVLY 323
Cdd:COG0318 183 ELIERERVTVLFGVPTMLARLLRH-PEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 324 PEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGY 403
Cdd:COG0318 261 EDPGERRPGSVGR-PLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-GWLRTGDLGRLDEDGY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 404 LYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKI 483
Cdd:COG0318 339 LYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKV 418
|
490 500
....*....|....*....|....
gi 502603069 484 PRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:COG0318 419 PRRVEFVDELPRTASGKIDRRALR 442
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-507 |
8.45e-164 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 474.29 E-value: 8.45e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 1 MMNFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVV 80
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 81 PINHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPLADIQWLSTASATEGLD---CFDELLAqAAPCGDEHGR 157
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPevgEYEELLA-AASDTFDFPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 158 PAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREY 237
Cdd:PRK06187 164 IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWG-LPYLALMAGAKQVIPRRF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 238 APREFLETLAQERISFTFGAPiAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDrFMQVYGMTESGP 317
Cdd:PRK06187 243 DPENLLDLIETERVTFFFAVP-TIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGID-LVQGYGMTETSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 318 LGTVLYPEEAVV----KAGSIGRcAIPGVELEVRRQDGSLC--SSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYR 391
Cdd:PRK06187 321 VVSVLPPEDQLPgqwtKRRSAGR-PLPGVEARIVDDDGDELppDGGEVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 392 SGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLR 471
Cdd:PRK06187 399 TGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELR 478
|
490 500 510
....*....|....*....|....*....|....*.
gi 502603069 472 QFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK06187 479 AFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
8-503 |
1.17e-159 |
|
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: 460.54 E-value: 1.17e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQ 87
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 88 APEVSYILRHSGARLcLVDgaraslitaiqaepqplaDIQWlstasategldcfdellaqaapcgdehgrpaphalaeIL 167
Cdd:cd17631 81 PPEVAYILADSGAKV-LFD------------------DLAL-------------------------------------LM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 168 YTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLA 247
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 248 QERISFTFGAPIAFLApLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQvyRSDRFMQVYGMTESGPLGTVLYPEEA 327
Cdd:cd17631 185 RHRVTSFFLVPTMIQA-LLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA--RGVKFVQGYGMTETSPGVTFLSPEDH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 328 VVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIV 407
Cdd:cd17631 262 RRKLGSAGR-PVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 408 DRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIF 487
Cdd:cd17631 340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSV 419
|
490
....*....|....*.
gi 502603069 488 EVRDTLPRTATGKLLK 503
Cdd:cd17631 420 EFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
4-507 |
6.02e-148 |
|
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: 431.99 E-value: 6.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 4 FISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPIN 83
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 84 HKLQAPEVSYILRHSGARlclvdgarasliTAIQAEPqpladiqwlstasategldcFDELLAQAAPCGDEHGRPaPHAL 163
Cdd:cd05936 81 PLYTPRELEHILNDSGAK------------ALIVAVS--------------------FTDLLAAGAPLGERVALT-PEDV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 AEILYTSGTTGQPKGCLHSHANVFH--AALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPRE 241
Cdd:cd05936 128 AVLQYTSGTTGVPKGAMLTHRNLVAnaLQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 242 FLETLAQERISFTFGAPIAFLApLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRsDRFMQVYGMTESGPLGTV 321
Cdd:cd05936 208 VLKEIRKHRVTIFPGVPTMYIA-LLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTG-VPIVEGYGLTETSPVVAV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 322 lYPEEAVVKAGSIGrCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDED 401
Cdd:cd05936 286 -NPLDGPRKPGSIG-IPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYMDED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 402 GYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARY 481
Cdd:cd05936 363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGY 442
|
490 500
....*....|....*....|....*.
gi 502603069 482 KIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05936 443 KVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-508 |
2.57e-131 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 391.19 E-value: 2.57e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 1 MMNFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVV 80
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 81 PINHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPLADIQWLST---ASATEGLDCFDELLAQAAPcgDEHGR 157
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETeedDPHTEKMKTFTDFLAAGDP--AERAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 158 P-APHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMRE 236
Cdd:PRK07656 162 EvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 237 YAPREFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGgplgADMARKLAQVYRS----DRFMQVYGM 312
Cdd:PRK07656 242 FDPDEVFRLIETERITVLPGPPTMYNSLLQH-PDRSAEDLSSLRLAVTGA----ASMPVALLERFESelgvDIVLTGYGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 313 TESGPLGTVLYP-EEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYR 391
Cdd:PRK07656 317 SEASGVTTFNRLdDDRKTVAGTIGT-AIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 392 SGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLR 471
Cdd:PRK07656 396 TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELI 475
|
490 500 510
....*....|....*....|....*....|....*..
gi 502603069 472 QFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLRG 508
Cdd:PRK07656 476 AYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
7-507 |
1.55e-130 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 389.29 E-value: 1.55e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGARASLITAIQAEpQPLADIQW---LSTASATEGLDCFDELL-AQAAPCGDEHgrPAPHA 162
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAPTAEAALAL-LPVDTLILslvLGGREAPGGWLDFADWAeAGSVAEPDVE--LADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 LAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREF 242
Cdd:PRK08316 173 LAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISFTFGAPIAFLApLSVVPDVASYDFSAMRLWAYGG----GPLGADMARKLAQVyrsdRFMQVYGMTESGPL 318
Cdd:PRK08316 253 LRTIEAERITSFFAPPTVWIS-LLRHPDFDTRDLSSLRKGYYGAsimpVEVLKELRERLPGL----RFYNCYGQTEIAPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 319 GTVLYPEEAVVKAGSIGRCAIpGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARV 398
Cdd:PRK08316 328 ATVLGPEEHLRRPGSAGRPVL-NVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG-GWFHSGDLGVM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 399 DEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRL 478
Cdd:PRK08316 406 DEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARL 485
|
490 500
....*....|....*....|....*....
gi 502603069 479 ARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK08316 486 AGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
163-502 |
3.94e-122 |
|
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: 361.22 E-value: 3.94e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 LAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREYAPREF 242
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISFTFGAPiAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRsDRFMQVYGMTESGPLGTVL 322
Cdd:cd04433 81 LELIEREKVTILLGVP-TLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG-IKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 323 YPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDG 402
Cdd:cd04433 159 PPDDDARKPGSVGR-PVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-GWYRTGDLGRLDEDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 403 YLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYK 482
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYK 316
|
330 340
....*....|....*....|
gi 502603069 483 IPRIFEVRDTLPRTATGKLL 502
Cdd:cd04433 317 VPRRVVFVDALPRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
23-502 |
3.18e-113 |
|
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: 343.81 E-value: 3.18e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 23 ADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARL 102
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 103 CLVDGARASLITAIQAEPQPLADIqwLSTASATEGLDCFDELLAQAAPCGDEHGRPAPHALAE----ILYTSGTTGQPKG 178
Cdd:cd05911 86 IFTDPDGLEKVKEAAKELGPKDKI--IVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDdtaaILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 179 CLHSHANVF--HAALCAAAATSLAPTERTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTFG 256
Cdd:cd05911 164 VCLSHRNLIanLSQVQTFLYGNDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 257 APiAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPLGTVLYpeEAVVKAGSIGR 336
Cdd:cd05911 243 VP-PIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNP--DGDDKPGSVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 337 cAIPGVELEVRRQDG-SLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIV 415
Cdd:cd05911 320 -LLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 416 TGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYK--IPRIFEVrDTL 493
Cdd:cd05911 399 YKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKqlRGGVVFV-DEI 477
|
....*....
gi 502603069 494 PRTATGKLL 502
Cdd:cd05911 478 PKSASGKIL 486
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1-507 |
1.64e-112 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 342.25 E-value: 1.64e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 1 MMNFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVV 80
Cdd:PRK06145 1 MFNLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 81 PINHKLQAPEVSYILRHSGARLCLVDGARAslitAIQAEPQPLADIQWLSTASATEgldcfdeLLAQAAPCGDEHGRpAP 160
Cdd:PRK06145 81 PINYRLAADEVAYILGDAGAKLLLVDEEFD----AIVALETPKIVIDAAAQADSRR-------LAQGGLEIPPQAAV-AP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 161 HALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPR 240
Cdd:PRK06145 149 TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 EFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRlWAYGGGPLGADM-ARKLAQVYRSDRFMQVYGMTESGPLG 319
Cdd:PRK06145 229 AVLAAIERHRLTCAWMAPVMLSRVLTV-PDRDRFDLDSLA-WCIGGGEKTPESrIRDFTRVFTRARYIDAYGLTETCSGD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 320 TVLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVD 399
Cdd:PRK06145 307 TLMEAGREIEKIGSTGR-ALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG-DWFRSGDVGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 400 EDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLA 479
Cdd:PRK06145 385 EEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLA 464
|
490 500
....*....|....*....|....*...
gi 502603069 480 RYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK06145 465 SFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
2-507 |
4.15e-110 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 337.52 E-value: 4.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 2 MNFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:PRK07786 17 QNWVNQLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 INHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEpQPLADIQWLSTASATEGLDCFDELLAQAAPCgdehgrPAPH 161
Cdd:PRK07786 97 VNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDI-VPLLSTVVVAGGSSDDSVLGYEDLLAEAGPA------HAPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 162 ALAE-----ILYTSGTTGQPKGCLHSHAN-VFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGtLLMGGTAVL-- 233
Cdd:PRK07786 170 DIPNdspalIMYTSGTTGRPKGAVLTHANlTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPG-LLLGAPTVIyp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 234 MREYAPREFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFsAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMT 313
Cdd:PRK07786 249 LGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAE-QQARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 314 ESGPLGTVLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSG 393
Cdd:PRK07786 327 EMSPVTCMLLGEDAIRKLGSVGK-VIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 394 DLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPG-KTLVHEDLRQ 472
Cdd:PRK07786 405 DLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAE 484
|
490 500 510
....*....|....*....|....*....|....*
gi 502603069 473 FMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK07786 485 FLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
8-417 |
3.14e-106 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 323.50 E-value: 3.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLAL-RADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGA--RASLITAIQAEPQPLADIQWLSTASATEGLDCFDELLAQAAPCgdEHGRPAPHALA 164
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDAlkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP--PPPPPDPDDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 165 EILYTSGTTGQPKGCLHSHANVFH----AALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPR 240
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 ---EFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRsDRFMQVYGMTESGP 317
Cdd:pfam00501 239 dpaALLELIERYKVTVLYGVPTLLNMLLEA-GAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTETTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 318 LGT-VLYPEEAVVKAGSIGRcAIPGVELEVRRQD-GSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDL 395
Cdd:pfam00501 317 VVTtPLPLDEDLRSLGSVGR-PLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDL 395
|
410 420
....*....|....*....|..
gi 502603069 396 ARVDEDGYLYIVDRLKDMIVTG 417
Cdd:pfam00501 396 GRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
25-507 |
2.77e-105 |
|
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: 321.16 E-value: 2.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 25 GQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCL 104
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 105 VDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaphaLAEILYTSGTTGQPKGCLHSHA 184
Cdd:cd05934 81 VD--------------------------------------------------------PASILYTSGTTGPPKGVVITHA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 185 NVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQERISFT--FGAPIAFL 262
Cdd:cd05934 105 NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTnyLGAMLSYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 263 APLSVVPDVAsydfsAMRLWAYGGGPLGADMARKLaqvyrSDRF----MQVYGMTESGplGTVLYPEEAVVKAGSIGRcA 338
Cdd:cd05934 185 LAQPPSPDDR-----AHRLRAAYGAPNPPELHEEF-----EERFgvrlLEGYGMTETI--VGVIGPRDEPRRPGSIGR-P 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 339 IPGVELEVRRQDGSLCSSGEVGEICLRSA---AMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIV 415
Cdd:cd05934 252 APGYEVRIVDDDGQELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAMRN-GWFHTGDLGYRDADGFFYFVDRKKDMIR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 416 TGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPR 495
Cdd:cd05934 331 RRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPK 410
|
490
....*....|..
gi 502603069 496 TATGKLLKHMLR 507
Cdd:cd05934 411 TPTEKVAKAQLR 422
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
8-512 |
8.63e-105 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 322.58 E-value: 8.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALRADGQDWSYAAL-AQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLhEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGARASLITAIQAEPQpLADIQWLSTASATEgldcfdellaQAAPCG-DEHGRPAPHAlae 165
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSY-VQRVISITSLKEIE----------DRKIDNfVEKNESASFI--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLET 245
Cdd:PRK06839 154 ICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLGADMARKLAQvyRSDRFMQVYGMTESGPLGTVLYPE 325
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINC-SKFETTNLQSVRWFYNGGAPCPEELMREFID--RGFLFGQGFGMTETSPTVFMLSEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 326 EAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLY 405
Cdd:PRK06839 311 DARRKVGSIGK-PVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQD-GWLCTGDLARVDEDGFVY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 406 IVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPR 485
Cdd:PRK06839 389 IVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPK 468
|
490 500
....*....|....*....|....*..
gi 502603069 486 IFEVRDTLPRTATGKLLKHMLRGSTTS 512
Cdd:PRK06839 469 EIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
24-507 |
3.95e-98 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 305.29 E-value: 3.95e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 24 DGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLC 103
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 104 LVDGARASLITAIQAE-PQPLADIqwLSTASATEGLDCFDELLAQAAPcgdehGRPAPHAL-AEILYTSGTTGQPKGC-- 179
Cdd:PRK08276 88 IVSAALADTAAELAAElPAGVPLL--LVVAGPVPGFRSYEEALAAQPD-----TPIADETAgADMLYSSGTTGRPKGIkr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 180 ----LHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTF 255
Cdd:PRK08276 161 plpgLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLR-FGMSALALGGTVVVMEKFDAEEALALIERYRVTHSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 256 GAPIAFLAPLSVVPDV-ASYDFSAMRLWAYGGGPLGADMARKLAQ-----VYRSdrfmqvYGMTESGpLGTVLYPEEAVV 329
Cdd:PRK08276 240 LVPTMFVRMLKLPEEVrARYDVSSLRVAIHAAAPCPVEVKRAMIDwwgpiIHEY------YASSEGG-GVTVITSEDWLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 330 KAGSIGRcAIPGvELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDR 409
Cdd:PRK08276 313 HPGSVGK-AVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 410 LKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL---VHEDLRQFMETRLARYKIPRI 486
Cdd:PRK08276 391 KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAgdaLAAELIAWLRGRLAHYKCPRS 470
|
490 500
....*....|....*....|.
gi 502603069 487 FEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK08276 471 IDFEDELPRTPTGKLYKRRLR 491
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
7-507 |
4.36e-98 |
|
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: 305.71 E-value: 4.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQD----WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPI 82
Cdd:cd12119 1 LLEHAARLHGDREIVSRTHEGevhrYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 83 NHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPLADIQWLSTA-----SATEGLDCFDELLAQAA-----PCG 152
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDaampePAGVGVLAYEELLAAESpeydwPDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 153 DEHgrpaphALAEILYTSGTTGQPKGCLHSH-ANVFHAALCAAAATSLAPTERT-LIAMPIWHsspLNNW---FLGTllM 227
Cdd:cd12119 161 DEN------TAAAICYTSGTTGNPKGVVYSHrSLVLHAMAALLTDGLGLSESDVvLPVVPMFH---VNAWglpYAAA--M 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 228 GGTAVLM--REYAPREFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRsdR 305
Cdd:cd12119 230 VGAKLVLpgPYLDPASLAELIEREGVTFAAGVPTVWQGLLDH-LEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGV--R 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 306 FMQVYGMTESGPLGTVLYP---------EEAVVKAGSIGRcAIPGVELEVRRQDG-SLCSSGE-VGEICLRSAAMMQGYL 374
Cdd:cd12119 307 VIHAWGMTETSPLGTVARPpsehsnlseDEQLALRAKQGR-PVPGVELRIVDDDGrELPWDGKaVGELQVRGPWVTKSYY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 375 DNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVV 454
Cdd:cd12119 386 KNDEESEALTED-GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 502603069 455 AVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd12119 465 AVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
7-507 |
6.20e-98 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 306.65 E-value: 6.20e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQD-----WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 INHKLQAPEVSYILRHSGARL-----CLVDGARASLITAIQAEPQPLAD-------IQWLSTASATEGLDCFDELLAQAA 149
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVlitadGGLRGGKVIDLKEKVDEALEELPslehvivVGRTGADVPMEGDLDWDELLAAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 150 PCGDEHGRPAPHALAeILYTSGTTGQPKGCLHSHANVF-HAALCAAAATSLAPTERtliampIWHSSPLN------NWFL 222
Cdd:COG0365 174 AEFEPEPTDADDPLF-ILYTSGTTGKPKGVVHTHGGYLvHAATTAKYVLDLKPGDV------FWCTADIGwatghsYIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 223 GTLLMGGTAVLMRE----YAPREFLETLAQERISFTFGAPIAFLAPLSVVPD-VASYDFSAMRLWAYGGGPLGADmarkl 297
Cdd:COG0365 247 GPLLNGATVVLYEGrpdfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEpLKKYDLSSLRLLGSAGEPLNPE----- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 298 aqVYRsdRFMQV--------YGMTESG-PLGTVLYPEEavVKAGSIGrCAIPGVELEVRRQDGSLCSSGEVGEICLRSA- 367
Cdd:COG0365 322 --VWE--WWYEAvgvpivdgWGQTETGgIFISNLPGLP--VKPGSMG-KPVPGYDVAVVDEDGNPVPPGEEGELVIKGPw 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 368 -AMMQGYLDNREATAAVLDDQ--GWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGR 444
Cdd:COG0365 395 pGMFRGYWNDPERYRETYFGRfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGV 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502603069 445 PHPEWGETVVAVLTLKPGKTL---VHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:COG0365 475 PDEIRGQVVKAFVVLKPGVEPsdeLAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLR 540
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
12-506 |
1.80e-96 |
|
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: 301.08 E-value: 1.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 12 ARTRPEKLAL--RADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAP 89
Cdd:cd05904 15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 90 EVSYILRHSGARLCLVDGARASLITAIQAePQPLADiqwlstaSATEGLDCFDELLAqaapCGDEHGRPAP----HALAE 165
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELAEKLASLAL-PVVLLD-------SAEFDSLSFSDLLF----EADEAEPPVVvikqDDVAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSH----ANVfhAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPRE 241
Cdd:cd05904 163 LLYSSGTTGRSKGVMLTHrnliAMV--AQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 242 FLETLAQERISFTFGAPIAFLApLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPLGTV 321
Cdd:cd05904 241 LLAAIERYKVTHLPVVPPIVLA-LVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 322 LY-PEEAVVKAGSIGRCAiPGVELE-VRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVD 399
Cdd:cd05904 320 CFaPEKDRAKYGSVGRLV-PNVEAKiVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYID 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 400 EDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLA 479
Cdd:cd05904 399 EDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVA 478
|
490 500
....*....|....*....|....*...
gi 502603069 480 RYK-IPRIFEVrDTLPRTATGKLLKHML 506
Cdd:cd05904 479 PYKkVRKVAFV-DAIPKSPSGKILRKEL 505
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
13-508 |
1.43e-94 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 296.90 E-value: 1.43e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 13 RTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPInHKLQAPE-V 91
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL-HPLGSLDdH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 92 SYILRHSGARLCLVDGAR-ASLITAIQAEPQPLAdiQWLSTASATEGLDcfdeLLAQAAPCGDEHGRPA--PHALAEILY 168
Cdd:PRK06188 102 AYVLEDAGISTLIVDPAPfVERALALLARVPSLK--HVLTLGPVPDGVD----LLAAAAKFGPAPLVAAalPPDIAGLAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 169 TSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLnnWFLGTLLMGGTAVLMREYAPREFLETLAQ 248
Cdd:PRK06188 176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDPAEVLRAIEE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 249 ERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLG----ADMARKLAQVyrsdrFMQVYGMTESGPLGTVLYP 324
Cdd:PRK06188 254 QRITATFLVPTMIYALLDH-PDLRTRDLSSLETVYYGASPMSpvrlAEAIERFGPI-----FAQYYGQTEAPMVITYLRK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 325 EEAVVKA----GSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDE 400
Cdd:PRK06188 328 RDHDPDDpkrlTSCGR-PTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRD-GWLHTGDVAREDE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 401 DGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLAR 480
Cdd:PRK06188 406 DGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGS 485
|
490 500
....*....|....*....|....*...
gi 502603069 481 YKIPRIFEVRDTLPRTATGKLLKHMLRG 508
Cdd:PRK06188 486 VHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-507 |
1.50e-94 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 295.72 E-value: 1.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 1 MMNFislLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVV 80
Cdd:PRK03640 4 MPNW---LKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 81 PINHKLQAPEVSYILRHSGARLCLVDGARASLITAIQ------AEPQPLADIQWLSTasategldcFDEllaqaapcgDE 154
Cdd:PRK03640 81 LLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGIsvkfaeLMNGPKEEAEIQEE---------FDL---------DE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 155 hgrpaphaLAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLnnwflgTLLM-----GG 229
Cdd:PRK03640 143 --------VATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGL------SILMrsviyGM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 230 TAVLMREYAPREFLETLAQERISFtfgapiaflapLSVVP----------DVASY--DFSAMRLwayGGGPlgADMArKL 297
Cdd:PRK03640 209 RVVLVEKFDAEKINKLLQTGGVTI-----------ISVVStmlqrllerlGEGTYpsSFRCMLL---GGGP--APKP-LL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 298 AQ-------VYrsdrfmQVYGMTESGPLGTVLYPEEAVVKAGSIGRCAIPgVELEVRRqDGSLCSSGEVGEICLRSAAMM 370
Cdd:PRK03640 272 EQckekgipVY------QSYGMTETASQIVTLSPEDALTKLGSAGKPLFP-CELKIEK-DGVVVPPFEEGEIVVKGPNVT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 371 QGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWG 450
Cdd:PRK03640 344 KGYLNREDATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502603069 451 ETVVAVLTLkpGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK03640 423 QVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELK 477
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
7-507 |
1.70e-94 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 297.84 E-value: 1.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLAL--RADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINH 84
Cdd:PRK12583 23 AFDATVARFPDREALvvRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 85 KLQAPEVSYILRHSGAR-LCLVDGARASLITAI-------QAEPQP-------LADIQWLST--ASATEGLDCFDELLAQ 147
Cdd:PRK12583 103 AYRASELEYALGQSGVRwVICADAFKTSDYHAMlqellpgLAEGQPgalacerLPELRGVVSlaPAPPPGFLAWHELQAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 148 AAPCGDEHGRPAPHALA-----EILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFL 222
Cdd:PRK12583 183 GETVSREALAERQASLDrddpiNIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 223 GTLLMGGTAVLMREY-APREFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGP-LGADMARKLAQV 300
Cdd:PRK12583 263 GCMTVGACLVYPNEAfDPLATLQAVEEERCTALYGVPTMFIAELDH-PQRGNFDLSSLRTGIMAGAPcPIEVMRRVMDEM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 301 YRSDrfMQV-YGMTESGPLGTVLYPEEAV-VKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNRE 378
Cdd:PRK12583 342 HMAE--VQIaYGMTETSPVSLQTTAADDLeRRVETVGR-TQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 379 ATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLT 458
Cdd:PRK12583 419 ATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVR 498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502603069 459 LKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK12583 499 LHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
17-507 |
5.10e-92 |
|
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: 287.65 E-value: 5.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 17 EKLALRADGQDWSYAALAQAGRRAATVLYEQG-VRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYIL 95
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RHSGARLcLVDGARaslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaphalaeILYTSGTTGQ 175
Cdd:cd05941 81 TDSEPSL-VLDPAL--------------------------------------------------------ILYTSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 176 PKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTF 255
Cdd:cd05941 104 PKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 256 GAP------IAFLAPLSVVPDVAS-YDFSAMRLWAYGGGPLGADMARKLAQVYrSDRFMQVYGMTESGPLGTVlyPEEAV 328
Cdd:cd05941 184 GVPtiytrlLQYYEAHFTDPQFARaAAAERLRLMVSGSAALPVPTLEEWEAIT-GHTLLERYGMTEIGMALSN--PLDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 329 VKAGSIGRcAIPGVELEVRRQDGS-LCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIV 407
Cdd:cd05941 261 RRPGTVGM-PLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 408 DRLKDMIV-TGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGK-TLVHEDLRQFMETRLARYKIPR 485
Cdd:cd05941 340 GRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRLAPYKRPR 419
|
490 500
....*....|....*....|..
gi 502603069 486 IFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05941 420 RLILVDELPRNAMGKVNKKELR 441
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
7-507 |
5.59e-92 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 291.33 E-value: 5.59e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQD--WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINH 84
Cdd:PRK08315 21 LLDRTAARYPDREALVYRDQGlrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 85 KLQAPEVSYILRHSGAR-LCLVDGARAS------------LITA----IQAEPQP-LADIQWLSTAsATEGLDCFDELLA 146
Cdd:PRK08315 101 AYRLSELEYALNQSGCKaLIAADGFKDSdyvamlyelapeLATCepgqLQSARLPeLRRVIFLGDE-KHPGMLNFDELLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 147 QAAPCGDEhgrpaphALAEIL------------YTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHS 214
Cdd:PRK08315 180 LGRAVDDA-------ELAARQatldpddpiniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 215 splnnwF---LGTLLM---GGTAVLMRE-YAPREFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGG 287
Cdd:PRK08315 253 ------FgmvLGNLACvthGATMVYPGEgFDPLATLAAVEEERCTALYGVPTMFIAELDH-PDFARFDLSSLRTGIMAGS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 288 PLGADMARKLAqvyrSDRFMQ----VYGMTESGPLGT---VLYPEEAVVkaGSIGRcAIPGVELEVRRQD-GSLCSSGEV 359
Cdd:PRK08315 326 PCPIEVMKRVI----DKMHMSevtiAYGMTETSPVSTqtrTDDPLEKRV--TTVGR-ALPHLEVKIVDPEtGETVPRGEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 360 GEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDV 439
Cdd:PRK08315 399 GELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDV 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502603069 440 AVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK08315 479 QVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
16-501 |
9.29e-92 |
|
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: 288.83 E-value: 9.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQD--WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSY 93
Cdd:cd05926 1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 94 ILRHSGARLCLVD-GARASLITAIQAEPQPLADIQWLSTASATEGLDcfDEL--LAQAAPCGDEHGRPAPHALAEILYTS 170
Cdd:cd05926 81 YLADLGSKLVLTPkGELGPASRAASKLGLAILELALDVGVLIRAPSA--ESLsnLLADKKNAKSEGVPLPDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 171 GTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQER 250
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 251 ISFTFGAPIAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFmQVYGMTE------SGPLgtvlyp 324
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEaahqmtSNPL------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 325 EEAVVKAGSIGRCAipGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYL 404
Cdd:cd05926 312 PPGPRKPGSVGKPV--GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 405 YIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIP 484
Cdd:cd05926 390 FLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVP 469
|
490
....*....|....*..
gi 502603069 485 RIFEVRDTLPRTATGKL 501
Cdd:cd05926 470 KKVYFVDELPKTATGKI 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
9-507 |
1.70e-90 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 286.19 E-value: 1.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 9 DQQARTRPEKLAL-----RADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPIN 83
Cdd:PRK08008 14 DDLADVYGHKTALifessGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 84 HKLQAPEVSYILRHSGARLCLVDGARASLITAIQAE-PQPLADIqWL--STASATEGLDCFDELLAQAAPCGDEHGRPAP 160
Cdd:PRK08008 94 ARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEdATPLRHI-CLtrVALPADDGVSSFTQLKAQQPATLCYAPPLST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 161 HALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPR 240
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSAR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 EFLETLAQERISFTFGAPIaFLAPLSVVPDVASYDFSAMR-LWAYgggpLGADMARKLAQVYR-SDRFMQVYGMTES--G 316
Cdd:PRK08008 253 AFWGQVCKYRATITECIPM-MIRTLMVQPPSANDRQHCLReVMFY----LNLSDQEKDAFEERfGVRLLTSYGMTETivG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 317 PLGTvlYPEEAVvKAGSIGRCAIpGVELEVRRQDGSLCSSGEVGEICLRSAA---MMQGYLDNREATAAVLDDQGWYRSG 393
Cdd:PRK08008 328 IIGD--RPGDKR-RWPSIGRPGF-CYEAEIRDDHNRPLPAGEIGEICIKGVPgktIFKEYYLDPKATAKVLEADGWLHTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 394 DLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQF 473
Cdd:PRK08008 404 DTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAF 483
|
490 500 510
....*....|....*....|....*....|....
gi 502603069 474 METRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK08008 484 CEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
29-507 |
9.79e-90 |
|
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: 281.58 E-value: 9.79e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGA 108
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 109 RAslitaiQAEPQPLadiqwlstasategldcfdellaqaapcgdehgrpaPHALAEILYTSGTTGQPKGCLHSHANVFH 188
Cdd:cd05903 83 FR------QFDPAAM------------------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 189 AALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTFGAPiAFLAPLSVV 268
Cdd:cd05903 121 SIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGAT-PFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 269 PDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSdRFMQVYGMTESGPLGTVLYPEEAVVKAGSIGRcAIPGVELEVRR 348
Cdd:cd05903 200 VEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTECPGAVTSITPAPEDRRLYTDGR-PLPGVEIKVVD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 349 QDGSLCSSGEVGEICLRSAAMMQGYLDnREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVED 428
Cdd:cd05903 278 DTGATLAPGVEGELLSRGPSVFLGYLD-RPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 429 VLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFME-TRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05903 357 LLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
2-507 |
8.46e-88 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 279.62 E-value: 8.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 2 MNFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:PRK07470 7 MNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 INHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPLADIQWLSTASATEGldcFDELLAQAApcgdehGRPAPH 161
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLD---YEALVARHL------GARVAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 162 ALAE------ILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTE--RTLIAMPIWHSSPLNNwfLGTLLMGGTAVL 233
Cdd:PRK07470 158 AAVDhddpcwFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGTTEqdASLVVAPLSHGAGIHQ--LCQVARGAATVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 234 M--REYAPREFLETLAQERISFTFGAPiAFLAPLSVVPDVASYDFSAMRLWAYGGGPL-GADMARKLAQVYRSdrFMQVY 310
Cdd:PRK07470 236 LpsERFDPAEVWALVERHRVTNLFTVP-TILKMLVEHPAVDRYDHSSLRYVIYAGAPMyRADQKRALAKLGKV--LVQYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 311 GMTESGPLGTVLYP---EEAVVKAGSIGRCAIP--GVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLD 385
Cdd:PRK07470 313 GLGEVTGNITVLPPalhDAEDGPDARIGTCGFErtGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 386 DqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL 465
Cdd:PRK07470 393 D-GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPV 471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 502603069 466 VHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK07470 472 DEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
11-507 |
1.14e-87 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 277.84 E-value: 1.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 11 QARTRPEKLALR--ADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQA 88
Cdd:PRK09088 4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 89 PEVSYILRHSGARLCLVDGARAslitAIQAEPQPLADIqwlsTASAteglDCFDELLAQAAPcgdehgrpaPHALAEILY 168
Cdd:PRK09088 84 SELDALLQDAEPRLLLGDDAVA----AGRTDVEDLAAF----IASA----DALEPADTPSIP---------PERVSLILF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 169 TSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQ 248
Cdd:PRK09088 143 TSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 249 ERISFT--FGAPiAFLAPLSVVPDvasYDFSAMR-LWAY--GGGP-LGADMARKLAQvyrSDRFMQVYGMTESGP-LGTV 321
Cdd:PRK09088 223 PALGIThyFCVP-QMAQAFRAQPG---FDAAALRhLTALftGGAPhAAEDILGWLDD---GIPMVDGFGMSEAGTvFGMS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 322 LYPEEAVVKAGSIGRCAiPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDED 401
Cdd:PRK09088 296 VDCDVIRAKAGAAGIPT-PTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 402 GYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARY 481
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKY 454
|
490 500
....*....|....*....|....*.
gi 502603069 482 KIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK09088 455 KVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
27-508 |
7.35e-87 |
|
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: 273.45 E-value: 7.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 27 DWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLclvd 106
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 107 garaslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpapHALAEILYTSGTTGQPKGCLHSHANV 186
Cdd:cd05912 77 ------------------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNH 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 187 FHAALCAAAATSLAPTERTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTFGAPIAFLAPLS 266
Cdd:cd05912 103 WWSAIGSALNLGLTEDDNWLCALPLFHISGLS-ILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 267 VVPDVASYDFSAMRLwayGGGPLGADMARKLAQ----VYRSdrfmqvYGMTESGPLGTVLYPEEAVVKAGSIGRcAIPGV 342
Cdd:cd05912 182 ILGEGYPNNLRCILL---GGGPAPKPLLEQCKEkgipVYQS------YGMTETCSQIVTLSPEDALNKIGSAGK-PLFPV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 343 ELEVRRQDGSLcssGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVY 422
Cdd:cd05912 252 ELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 423 SKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKpgKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLL 502
Cdd:cd05912 328 PAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLL 405
|
....*.
gi 502603069 503 KHMLRG 508
Cdd:cd05912 406 RHELKQ 411
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
5-507 |
1.07e-86 |
|
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: 275.33 E-value: 1.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 5 ISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINH 84
Cdd:cd12118 7 LSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 85 KLQAPEVSYILRHSGARLCLVDgaRASLITAIQAEPQPLADIQWLStasategldcfdellaqaapcgDEHGrpaPHALA 164
Cdd:cd12118 87 RLDAEEIAFILRHSEAKVLFVD--REFEYEDLLAEGDPDFEWIPPA----------------------DEWD---PIALN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 165 eilYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSsplNNW-FLGTLLM-GGTAVLMREYAPREF 242
Cdd:cd12118 140 ---YTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHC---NGWcFPWTVAAvGGTNVCLRKVDAKAI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISFTFGAPIAfLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVyrSDRFMQVYGMTESGPLGTVL 322
Cdd:cd12118 214 YDLIEKHKVTHFCGAPTV-LNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL--GFDVTHVYGLTETYGPATVC 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 323 Y----------PEEAVVKA----GSIGRCAIPGVELEVRR---QDGSlcssgEVGEICLRSAAMMQGYLDNREATAAVLD 385
Cdd:cd12118 291 AwkpewdelptEERARLKArqgvRYVGLEEVDVLDPETMKpvpRDGK-----TIGEIVFRGNIVMKGYLKNPEATAEAFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 386 DqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL 465
Cdd:cd12118 366 G-GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKV 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 502603069 466 VHEDLRQFMETRLARYKIPRIFEVRDtLPRTATGKLLKHMLR 507
Cdd:cd12118 445 TEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
12-502 |
1.80e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 276.46 E-value: 1.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 12 ARTRPEKLALRADGQDWSYAAL-AQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPE 90
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELlEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 91 VSYILRHSGARL-----CLVDG-ARASLITAIQ-----------AEPQPLADIQWLSTASATEGLDCFD-ELLAQAAPCG 152
Cdd:PRK08314 100 LAHYVTDSGARVaivgsELAPKvAPAVGNLRLRhvivaqysdylPAEPEIAVPAWLRAEPPLQALAPGGvVAWKEALAAG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 153 DehgRPAPHA-----LAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLM 227
Cdd:PRK08314 180 L---APPPHTagpddLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 228 GGTAVLM----REYAPRefleTLAQERISFTFGAP---IAFLAPlsvvPDVASYDFSAMRLWAYGGGPLGADMARKLAQV 300
Cdd:PRK08314 257 GATVVLMprwdREAAAR----LIERYRVTHWTNIPtmvVDFLAS----PGLAERDLSSLRYIGGGGAAMPEAVAERLKEL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 301 YrSDRFMQVYGMTESGPlGTVLYPEEAvVKAGSIGrcaIPGVELEVRRQD---GSLCSSGEVGEICLRSAAMMQGYLDNR 377
Cdd:PRK08314 329 T-GLDYVEGYGLTETMA-QTHSNPPDR-PKLQCLG---IPTFGVDARVIDpetLEELPPGEVGEIVVHGPQVFKGYWNRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 378 EATAAV---LDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVV 454
Cdd:PRK08314 403 EATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVK 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502603069 455 AVLTLKPGK--TLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLL 502
Cdd:PRK08314 483 AVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
4-507 |
5.89e-86 |
|
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: 274.72 E-value: 5.89e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 4 FISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDK----LGllcfNTPGFVFALLGAWRLGAVv 79
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRvvvqLP----NVAEFVIVFFALFRAGAI- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 80 vPIN----HKLQapEVSYILRHSGARLCLVDGARA-----SLITAIQAEPQPLAdiQWLSTASATEGLDcFDELLAqaAP 150
Cdd:COG1021 102 -PVFalpaHRRA--EISHFAEQSEAVAYIIPDRHRgfdyrALARELQAEVPSLR--HVLVVGDAGEFTS-LDALLA--AP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 151 CGDEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWH----SSPlnnWFLGTLL 226
Cdd:COG1021 174 ADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHnfplSSP---GVLGVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 227 MGGTAVLMREYAPREFLETLAQERISFTfgapiaflaplSVVPDVAS----------YDFSAMRLWAYGGGPLGADMARK 296
Cdd:COG1021 251 AGGTVVLAPDPSPDTAFPLIERERVTVT-----------ALVPPLALlwldaaersrYDLSSLRVLQVGGAKLSPELARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 297 LAQVYrSDRFMQVYGMTEsgplGTVLY-----PEEAVVkaGSIGRCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQ 371
Cdd:COG1021 320 VRPAL-GCTLQQVFGMAE----GLVNYtrlddPEEVIL--TTQGRPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 372 GYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGE 451
Cdd:COG1021 393 GYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGE 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502603069 452 TVVAVLTLKpGKTLVHEDLRQFMETR-LARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:COG1021 473 RSCAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
20-507 |
1.25e-85 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 273.11 E-value: 1.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 20 ALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSG 99
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 100 ARLC-----LVDGARASLITAIQ----AEPQPLADIQWLSTASAT--EGLDCFDELLAQAAPcgdeHGRPAPHALAEILY 168
Cdd:PRK12406 84 ARVLiahadLLHGLASALPAGVTvlsvPTPPEIAAAYRISPALLTppAGAIDWEGWLAQQEP----YDGPPVPQPQSMIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 169 TSGTTGQPKGCLHSHANVFHAALCAAAATSL---APTERTLIAMPIWHSSPlNNWFLGTLLMGGTAVLMREYAPREFLET 245
Cdd:PRK12406 160 TSGTTGHPKGVRRAAPTPEQAAAAEQMRALIyglKPGIRALLTGPLYHSAP-NAYGLRAGRLGGVLVLQPRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQERISFTFGAPIAFLAPLSVVPDV-ASYDFSAMRLWAYGGGPLGADMARKLAQ-----VYrsdrfmQVYGMTESGPLg 319
Cdd:PRK12406 239 IERHRITHMHMVPTMFIRLLKLPEEVrAKYDVSSLRHVIHAAAPCPADVKRAMIEwwgpvIY------EYYGSTESGAV- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 320 TVLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVD 399
Cdd:PRK12406 312 TFATSEDALSHPGTVGK-AAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 400 EDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLA 479
Cdd:PRK12406 391 ADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLA 470
|
490 500
....*....|....*....|....*...
gi 502603069 480 RYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK12406 471 GYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-507 |
4.45e-84 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 270.09 E-value: 4.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPLADIQWLSTASATEGLDCFDEL----LAQAAPCGDehgrPAPHA 162
Cdd:PRK06155 106 RGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAplppLDAPAPAAA----VQPGD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 LAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNwFLGTLLMGGTAVLMREYAPREF 242
Cdd:PRK06155 182 TAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNA-FFQALLAGATYVLEPRFSASGF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISFTF--GAPIAFLapLSVVPDVASYDFSAMRLWAYGGGPlgadmarKLAQVYRsDRF----MQVYGMTESG 316
Cdd:PRK06155 261 WPAVRRHGATVTYllGAMVSIL--LSQPARESDRAHRVRVALGPGVPA-------ALHAAFR-ERFgvdlLDGYGSTETN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 317 PLGTVLYPEEavvKAGSIGRCAiPGVELEVRRQDGSLCSSGEVGEICLRSA---AMMQGYLDNREATAAVLDDQgWYRSG 393
Cdd:PRK06155 331 FVIAVTHGSQ---RPGSMGRLA-PGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNL-WFHTG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 394 DLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQF 473
Cdd:PRK06155 406 DRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRH 485
|
490 500 510
....*....|....*....|....*....|....
gi 502603069 474 METRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK06155 486 CEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-459 |
1.98e-83 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 270.05 E-value: 1.98e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 2 MNFISLLDQQARTRPEKLALR--ADG--QDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGA 77
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALRekEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 78 VVVPINHKLQAPEVSYILRHSGARLCLV-DGARASLITAIQAEpqpLADIQWL-----STASATEGLDCFDELLAQaapc 151
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDE---LPSLRHIvvldpRGLRDDPRLLSLDELLAL---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 152 GDEHGRPA----------PHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSspLNNWF 221
Cdd:COG1022 164 GREVADPAelearraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHV--FERTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 222 LGTLLMGGTAV-----------LMREY-------APReFLETL---AQERIS---------FTFGAPIA---FLA----- 263
Cdd:COG1022 242 SYYALAAGATVafaespdtlaeDLREVkptfmlaVPR-VWEKVyagIQAKAEeagglkrklFRWALAVGrryARArlagk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 264 --PLSVVPDVASYD---FSAMR-------LWAY-GGGPLGADMARklaqVYRSD--RFMQVYGMTESGPLGTVLYPEEav 328
Cdd:COG1022 321 spSLLLRLKHALADklvFSKLRealggrlRFAVsGGAALGPELAR----FFRALgiPVLEGYGLTETSPVITVNRPGD-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 329 VKAGSIGRcAIPGVELEVrrqdgslcssGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVD 408
Cdd:COG1022 395 NRIGTVGP-PLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502603069 409 RLKDMIVT-GGENVYSKEVEDVLCTHSDVQDVAVIG--RPHpewgetVVAVLTL 459
Cdd:COG1022 464 RKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVVGdgRPF------LAALIVP 511
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
160-507 |
2.55e-82 |
|
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: 259.52 E-value: 2.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 PHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMRE-YA 238
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPsFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 239 PREFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPL 318
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTMFIAELEH-PDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 319 GTVLYPEEAV-VKAGSIGRcAIPGVELE-VRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLA 396
Cdd:cd05917 160 STQTRTDDSIeKRVNTVGR-IMPHTEAKiVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 397 RVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMET 476
Cdd:cd05917 239 VMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKG 318
|
330 340 350
....*....|....*....|....*....|.
gi 502603069 477 RLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05917 319 KIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
6-507 |
1.42e-81 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 263.92 E-value: 1.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLD---QQARTRPEKLALRAD-GQDWSYAALAQAGRRAATVLYEQGVRQGDKLGllcFNTPG---FVFALLGAWRLGAV 78
Cdd:PRK06087 24 SLADywqQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVA---FQLPGwceFTIIYLACLKVGAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 79 VVPINHKLQAPEVSYILRHSGARLCLVDGARAS-----LITAIQAEPQPLADIQWLSTASATEGLDCFDELLAQAAPCGD 153
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQtrpvdLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYEPLTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 154 EhgrPAPHA--LAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLapTERTLIAMPiwhsSPLNN---WFLG---TL 225
Cdd:PRK06087 181 A---ITTHGdeLAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNL--TWQDVFMMP----APLGHatgFLHGvtaPF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 226 LMGGTAVLMREYAPREFLETLAQERISFTFGApIAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQvyRSDR 305
Cdd:PRK06087 252 LIGARSVLLDIFTPDACLALLEQQRCTCMLGA-TPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQ--RGIK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 306 FMQVYGMTESGPlGTVLYPEEAVVKAGSIGRCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLD 385
Cdd:PRK06087 329 LLSVYGSTESSP-HAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 386 DQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLK-PGKT 464
Cdd:PRK06087 408 EEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKaPHHS 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 502603069 465 LVHEDLRQFMET-RLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK06087 488 LTLEEVVAFFSRkRVAKYKYPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
3-507 |
2.54e-81 |
|
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: 261.92 E-value: 2.54e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 3 NFISLLDQQ-ARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:cd05959 4 NAATLVDLNlNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 INHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPlaDIQWLSTASATEGLDCFDeLLAQAAPCGDEHGRPAPH 161
Cdd:cd05959 84 VNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEH--TLVVLIVSGGAGPEAGAL-LLAELVAAEAEQLKPAAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 162 ALAEI---LYTSGTTGQPKGCLHSHANVFHAALC-AAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREY 237
Cdd:cd05959 161 HADDPafwLYSSGSTGRPKGVVHLHADIYWTAELyARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 238 -APREFLETLAQERISFTFGAPiAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVyGMTESG 316
Cdd:cd05959 241 pTPAAVFKRIRRYRPTVFFGVP-TLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGI-GSTEML 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 317 PLGTVLYPEEavVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLddQG-WYRSGDL 395
Cdd:cd05959 319 HIFLSNRPGR--VRYGTTGK-PVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF--QGeWTRTGDK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 396 ARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPG---KTLVHEDLRQ 472
Cdd:cd05959 394 YVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyedSEALEEELKE 473
|
490 500 510
....*....|....*....|....*....|....*
gi 502603069 473 FMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05959 474 FVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-508 |
1.71e-80 |
|
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: 257.27 E-value: 1.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 28 WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDG 107
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 108 ARASLItaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaphalaeiLYTSGTTGQPKGCLHSHANVF 187
Cdd:cd05972 81 EDPALI-----------------------------------------------------YFTSGTTGLPKGVLHTHSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 188 HAALCAAAATSLAPTERTL-IAMPIWhssPLNNW--FLGTLLMGGTAVL--MREYAPREFLETLAQERISFTFGAPIAFl 262
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWnIADPGW---AKGAWssFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGPPTAY- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 263 aPLSVVPDVASYDFSAMRLWAYGGGPLGADMARkLAQVYRSDRFMQVYGMTESG-PLGTVLYPEeavVKAGSIGRcAIPG 341
Cdd:cd05972 184 -RMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIE-WWRAATGLPIRDGYGQTETGlTVGNFPDMP---VKPGSMGR-PTPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 342 VELEVRRQDGSLCSSGEVGEICLRSA--AMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGE 419
Cdd:cd05972 258 YDVAIIDDDGRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASIRG-DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 420 NVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPG----KTLVhEDLRQFMETRLARYKIPRIFEVRDTLPR 495
Cdd:cd05972 337 RIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGyepsEELA-EELQGHVKKVLAPYKYPREIEFVEELPK 415
|
490
....*....|...
gi 502603069 496 TATGKLLKHMLRG 508
Cdd:cd05972 416 TISGKIRRVELRD 428
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
8-507 |
2.82e-80 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 260.37 E-value: 2.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLAL---RADGQ---DWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:PRK13295 30 LDACVASCPDKTAVtavRLGTGaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 INHKLQAPEVSYILRHSGARLCLV-----DGARASLITAIQAEpqpLADIQWLSTASAtEGLDCFDELL-------AQAA 149
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLRPE---LPALRHVVVVGG-DGADSFEALLitpaweqEPDA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 150 PCGDEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGG 229
Cdd:PRK13295 186 PAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 230 TAVLMREYAPREFLETLAQERISFTFGApIAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKlAQVYRSDRFMQV 309
Cdd:PRK13295 266 TAVLQDIWDPARAAELIRTEGVTFTMAS-TPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVER-ARAALGAKIVSA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 310 YGMTESGpLGTVLYPEEAVVKAGSIGRCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAvlDDQGW 389
Cdd:PRK13295 344 WGMTENG-AVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGW 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 390 YRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHED 469
Cdd:PRK13295 421 FDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEE 500
|
490 500 510
....*....|....*....|....*....|....*....
gi 502603069 470 LRQFMET-RLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK13295 501 MVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
5-503 |
3.72e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 258.01 E-value: 3.72e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 5 ISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINH 84
Cdd:PRK05605 35 VDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 85 KLQAPEVSYILRHSGARLCLVDGARASLITA---------------IQAEPQP-----------LADIQWLSTASATEGL 138
Cdd:PRK05605 115 LYTAHELEHPFEDHGARVAIVWDKVAPTVERlrrttpletivsvnmIAAMPLLqrlalrlpipaLRKARAALTGPAPGTV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 139 DcFDELLAQAAP---CGDEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAP--TERTLIAMPIWH 213
Cdd:PRK05605 195 P-WETLVDAAIGgdgSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGdgPERVLAALPMFH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 214 SSPLNnwFLGTL--LMGGTAVLMREYAPREFLETLAQERISFTFGAPIAF--LAPLSVVPDVasyDFSAMRLWAYGGGPL 289
Cdd:PRK05605 274 AYGLT--LCLTLavSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYekIAEAAEERGV---DLSGVRNAFSGAMAL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 290 GADMARKLAQVyRSDRFMQVYGMTESGPLgTVLYPEEAVVKAGSIGrcaIPGVELEVRRQD----GSLCSSGEVGEICLR 365
Cdd:PRK05605 349 PVSTVELWEKL-TGGLLVEGYGLTETSPI-IVGNPMSDDRRPGYVG---VPFPDTEVRIVDpedpDETMPDGEEGELLVR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 366 SAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRP 445
Cdd:PRK05605 424 GPQVFKGYWNRPEETAKSFLD-GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLP 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502603069 446 HPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLK 503
Cdd:PRK05605 503 REDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
29-506 |
5.46e-79 |
|
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: 253.91 E-value: 5.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDga 108
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 109 raSLITAIQAEPQPLADIqWLSTASATEGLDCFDellaqaapcGDehgrpaphALAEILYTSGTTGQPKGCLHSHANVFH 188
Cdd:TIGR01923 79 --SLLEEKDFQADSLDRI-EAAGRYETSLSASFN---------MD--------QIATLMFTSGTTGKPKAVPHTFRNHYA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 189 AALCAAAATSLAPTERTLIAMPIWHSSPLNNWFlGTLLMGGTAVLMREYAprEFLETLAQERISFtfgapiaflapLSVV 268
Cdd:TIGR01923 139 SAVGSKENLGFTEDDNWLLSLPLYHISGLSILF-RWLIEGATLRIVDKFN--QLLEMIANERVTH-----------ISLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 269 PDV------ASYDFSAMRLWAYGGGPLGADMARKlAQVYRSDRFmQVYGMTESGPLGTVLYPEEAVVKaGSIGRcAIPGV 342
Cdd:TIGR01923 205 PTQlnrlldEGGHNENLRKILLGGSAIPAPLIEE-AQQYGLPIY-LSYGMTETCSQVTTATPEMLHAR-PDVGR-PLAGR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 343 ELEVRRQDGSlcssgEVGEICLRSAAMMQGYLDNREATAAVlDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVY 422
Cdd:TIGR01923 281 EIKIKVDNKE-----GHGEIMVKGANLMKGYLYQGELTPAF-EQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 423 SKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKpgKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLL 502
Cdd:TIGR01923 355 PEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKIL 432
|
....
gi 502603069 503 KHML 506
Cdd:TIGR01923 433 RNQL 436
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
10-509 |
9.34e-79 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 256.39 E-value: 9.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 10 QQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAP 89
Cdd:PRK07788 57 HAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 90 EVSYILRHSGARLCLVDGARASLITAIqaePQPLADIQ-WLSTASATEGLDCFDELLAQAAPCGDEHGRPAP--HAlAEI 166
Cdd:PRK07788 137 QLAEVAAREGVKALVYDDEFTDLLSAL---PPDLGRLRaWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPpkPG-GIV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLmGGTAVLMREYAPREFLETL 246
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMAL-GSTVVLRRRFDPEATLEDI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 247 AQERISFTFGAPIAFLAPLSVVPDV-ASYDFSAMRLWAYGGGPLGADMARKLAQVYrSDRFMQVYGMTESGpLGTVLYPE 325
Cdd:PRK07788 292 AKHKATALVVVPVMLSRILDLGPEVlAKYDTSSLKIIFVSGSALSPELATRALEAF-GPVLYNLYGSTEVA-FATIATPE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 326 EAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNReaTAAVLDdqGWYRSGDLARVDEDGYLY 405
Cdd:PRK07788 370 DLAEAPGTVGR-PPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR--DKQIID--GLLSSGDVGYFDEDGLLF 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 406 IVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPR 485
Cdd:PRK07788 445 VDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPR 524
|
490 500
....*....|....*....|....
gi 502603069 486 IFEVRDTLPRTATGKLLKHMLRGS 509
Cdd:PRK07788 525 DVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
9-508 |
3.10e-77 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 251.53 E-value: 3.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 9 DQQARTRPEKLA--LRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK13391 4 GIHAQTTPDKPAviMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGARASLIT-AIQAEPQPLADIQwLSTASATEGLDCFDELLAQ--AAPCGDEH-GRPapha 162
Cdd:PRK13391 84 TPAEAAYIVDDSGARALITSAAKLDVARaLLKQCPGVRHRLV-LDGDGELEGFVGYAEAVAGlpATPIADESlGTD---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 laeILYTSGTTGQPKGCLH--SHANVFHAALCAAAATSL---APTERTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREY 237
Cdd:PRK13391 159 ---MLYSSGTTGRPKGIKRplPEQPPDTPLPLTAFLQRLwgfRSDMVYLSPAPLYHSAPQR-AVMLVIRLGGTVIVMEHF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 238 APREFLETLAQERISFTFGAPIAFLAPLSVVPDV-ASYDFSAMRLWAYGGGPLGADMARKLAQ-----VYrsdrfmQVYG 311
Cdd:PRK13391 235 DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVrDKYDLSSLEVAIHAAAPCPPQVKEQMIDwwgpiIH------EYYA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 312 MTEsGPLGTVLYPEEAVVKAGSIGRcAIPGVeLEVRRQDGSLCSSGEVGEICLRSAAMMQgYLDNREATAAVLDDQG-WY 390
Cdd:PRK13391 309 ATE-GLGFTACDSEEWLAHPGTVGR-AMFGD-LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 391 RSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTL----KPGKTLV 466
Cdd:PRK13391 385 TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPvdgvDPGPALA 464
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 502603069 467 HEdLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLRG 508
Cdd:PRK13391 465 AE-LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
29-506 |
5.22e-77 |
|
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: 248.55 E-value: 5.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARlclvdga 108
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 109 raslitaiqaepqpladiqwlsTASATEGLDcfdellaqaapcgdehgrpaphALAEILYTSGTTGQPKGCLHSHANVFH 188
Cdd:cd05935 76 ----------------------VAVVGSELD----------------------DLALIPYTSGTTGLPKGCMHTHFSAAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 189 AALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTFGAPIAFLAPLSvV 268
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLA-T 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 269 PDVASYDFSAMRLWAYGGGPLGADMARKLAQVYrSDRFMQVYGMTESGPLGTVLYPeeAVVKAGSIGrcaIPGVELEVR- 347
Cdd:cd05935 191 PEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQTHTNPP--LRPKLQCLG---IP*FGVDARv 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 348 --RQDGSLCSSGEVGEICLRSAAMMQGYLDNREATA-AVLDDQG--WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVY 422
Cdd:cd05935 265 idIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEeSFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 423 SKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGK--TLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGK 500
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGK 424
|
....*.
gi 502603069 501 LLKHML 506
Cdd:cd05935 425 ILWRLL 430
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
6-508 |
1.45e-75 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 247.39 E-value: 1.45e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHK 85
Cdd:TIGR03098 4 HLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 86 LQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPLA------DIQWLSTASATEGLDCFDELlaQAAPCGDEHGRPA 159
Cdd:TIGR03098 84 LKAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHDLRtliivgDPAHASEGHPGEEPASWPKL--LALGDADPPHPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 PHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNwFLGTLLMGGTAVLMREYAP 239
Cdd:TIGR03098 162 DSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQ-LTTAFYVGATVVLHDYLLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 240 REFLETLAQERIS-FTFGAPI-AFLAPLsvvpDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGP 317
Cdd:TIGR03098 241 RDVLKALEKHGITgLAAVPPLwAQLAQL----DWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEAFR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 318 lGTVLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA------------VLD 385
Cdd:TIGR03098 317 -STYLPPEEVDRRPDSIGK-AIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAErfrplppfpgelHLP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 386 DQGWYrSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL 465
Cdd:TIGR03098 395 ELAVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEEL 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 502603069 466 VHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLRG 508
Cdd:TIGR03098 474 DRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
15-507 |
3.50e-75 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 245.94 E-value: 3.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 15 RPEKLALRA-DGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSY 93
Cdd:PRK07514 15 DRDAPFIETpDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 94 ILRHSGARLCLVDGARASLITAIqAEPQPLADIqwlstasATEGLDCFDELLAQAAPCGDEHgRPAPHA---LAEILYTS 170
Cdd:PRK07514 95 FIGDAEPALVVCDPANFAWLSKI-AAAAGAPHV-------ETLDADGTGSLLEAAAAAPDDF-ETVPRGaddLAAILYTS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 171 GTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLnnwFL---GTLLMGGTAVLMREYAPREFLETLA 247
Cdd:PRK07514 166 GTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGL---FVatnVALLAGASMIFLPKFDPDAVLALMP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 248 qeRISFTFGAP---IAFLAPLSVVPDVASYdfsaMRLWAYGGGPLGADMARKLAQvyRS-DRFMQVYGMTESGPLGTVLY 323
Cdd:PRK07514 243 --RATVMMGVPtfyTRLLQEPRLTREAAAH----MRLFISGSAPLLAETHREFQE--RTgHAILERYGMTETNMNTSNPY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 324 PEEAVvkAGSIGRcAIPGVELEVR-RQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDG 402
Cdd:PRK07514 315 DGERR--AGTVGF-PLPGVSLRVTdPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 403 YLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYK 482
Cdd:PRK07514 392 YVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFK 471
|
490 500
....*....|....*....|....*
gi 502603069 483 IPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK07514 472 QPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
12-506 |
4.14e-75 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 247.26 E-value: 4.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 12 ARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEV 91
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 92 SYILRHSGARLCLVDGA--------------RASLITA----IQAEPQ-PLADIQWLSTASATEGLDCFDELLAQAAPCG 152
Cdd:PRK06178 123 SYELNDAGAEVLLALDQlapvveqvraetslRHVIVTSladvLPAEPTlPLPDSLRAPRLAAAGAIDLLPALRACTAPVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 153 DEhgRPAPHALAEILYTSGTTGQPKGCLHSHAN-VFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTA 231
Cdd:PRK06178 203 LP--PPALDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 232 VLMREYAPREFLETLAQERISFTFGaPIAFLAPLSVVPDVASYDFSAMRlwayggGPLGADMARKLAQVYR--------S 303
Cdd:PRK06178 281 VLLARWDAVAFMAAVERYRVTRTVM-LVDNAVELMDHPRFAEYDLSSLR------QVRVVSFVKKLNPDYRqrwraltgS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 304 DRFMQVYGMTESGPLGTV----------LYPEEAVVKagsigrCAIPGVELEVRRQD-GSLCSSGEVGEICLRSAAMMQG 372
Cdd:PRK06178 354 VLAEAAWGMTETHTCDTFtagfqdddfdLLSQPVFVG------LPVPGTEFKICDFEtGELLPLGAEGEIVVRTPSLLKG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 373 YLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGET 452
Cdd:PRK06178 428 YWNKPEATAEALRD-GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQV 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502603069 453 VVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIfEVRDTLPRTATGKLLKHML 506
Cdd:PRK06178 507 PVAFVQLKPGADLTAAALQAWCRENMAVYKVPEI-RIVDALPMTATGKVRKQDL 559
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
11-507 |
1.69e-74 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 244.15 E-value: 1.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 11 QARTRPEKLAL--RADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQA 88
Cdd:PRK13390 6 HAQIAPDRPAVivAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 89 PEVSYILRHSGARLCLVDGARASLITAIQAePQPLAdiqwLSTASATEGLDCFDELLAQAAP------CGdehgrpapha 162
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAKVGA-DLPLR----LSFGGEIDGFGSFEAALAGAGPrlteqpCG---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 lAEILYTSGTTGQPKGC---------------LHSHANVFHAALCaaaatslapTERTLIAMPIWHSSPLNnWFLGTLLM 227
Cdd:PRK13390 151 -AVMLYSSGTTGFPKGIqpdlpgrdvdapgdpIVAIARAFYDISE---------SDIYYSSAPIYHAAPLR-WCSMVHAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 228 GGTAVLMREYAPREFLETLAQERISFTFGAPIAFLAPLSVVPDVAS-YDFSAMRLWAYGGGPLGADMARKLAQ-----VY 301
Cdd:PRK13390 220 GGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTrYDVSSLRAVIHAAAPCPVDVKHAMIDwlgpiVY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 302 RSDRFMQVYGMTesgplgtVLYPEEAVVKAGSIGRCAIPgvELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATA 381
Cdd:PRK13390 300 EYYSSTEAHGMT-------FIDSPDWLAHPGSVGRSVLG--DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 382 AVLDDQG--WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTL 459
Cdd:PRK13390 371 AAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQL 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502603069 460 ----KPGKTLVHEdLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK13390 451 vegiRGSDELARE-LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
4-506 |
2.83e-74 |
|
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: 242.62 E-value: 2.83e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 4 FISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPIN 83
Cdd:cd05920 17 LGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 84 HKLQAPEVSYILRHSGARLCLVDGARASLitaiqaEPQPLADiqwlstasategldcfdELLAqaapcgdEHGRPAphal 163
Cdd:cd05920 97 PSHRRSELSAFCAHAEAVAYIVPDRHAGF------DHRALAR-----------------ELAE-------SIPEVA---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 aEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNN-WFLGTLLMGGTAVLMREYAPREF 242
Cdd:cd05920 143 -LFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDPSPDAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISFTfgapiaflaplSVVPDVAS----------YDFSAMRLWAYGGGPLGADMARKLAQVYRSdRFMQVYGM 312
Cdd:cd05920 222 FPLIEREGVTVT-----------ALVPALVSlwldaaasrrADLSSLRLLQVGGARLSPALARRVPPVLGC-TLQQVFGM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 313 TEsgplGTVLY-----PEEavVKAGSIGRCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQ 387
Cdd:cd05920 290 AE----GLLNYtrlddPDE--VIIHTQGRPMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 388 GWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVh 467
Cdd:cd05920 364 GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSA- 442
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 502603069 468 EDLRQFMETR-LARYKIPRIFEVRDTLPRTATGKLLKHML 506
Cdd:cd05920 443 AQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
8-506 |
5.77e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 244.17 E-value: 5.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQ 87
Cdd:PRK06710 30 VEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 88 APEVSYILRHSGARLCLVDGARASLITAIQAEPQ-------PLAD------------IQWLST-----ASATEGLDCFDE 143
Cdd:PRK06710 110 ERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKiehvivtRIADflpfpknllypfVQKKQSnlvvkVSESETIHLWNS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 144 L-----LAQAAPCGDEHGrpaphaLAEILYTSGTTGQPKGCLHSHANVFHAALCAAA--ATSLAPTERTLIAMPIWHSSP 216
Cdd:PRK06710 190 VekevnTGVEVPCDPEND------LALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwlYNCKEGEEVVLGVLPFFHVYG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 217 LNNWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLGADMARK 296
Cdd:PRK06710 264 MTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNS-PLLKEYDISSIRACISGSAPLPVEVQEK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 297 LAQVyRSDRFMQVYGMTESGPLGTVLYPEEAVVkAGSIGrcaIPGVELEVR---RQDGSLCSSGEVGEICLRSAAMMQGY 373
Cdd:PRK06710 343 FETV-TGGKLVEGYGLTESSPVTHSNFLWEKRV-PGSIG---VPWPDTEAMimsLETGEALPPGEIGEIVVKGPQIMKGY 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 374 LDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETV 453
Cdd:PRK06710 418 WNKPEETAAVLQD-GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 502603069 454 VAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHML 506
Cdd:PRK06710 497 KAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
3-507 |
2.01e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 237.35 E-value: 2.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 3 NFISLLDQQARTRPEKLALRADGQDWSYAAL-AQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:PRK05677 25 NIQAVLKQSCQRFADKPAFSNLGKTLTYGELyKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 INHKLQAPEVSYILRHSGAR--LCLVD------------GARASLITAIQAEPQPL------ADIQWLST---ASATEGL 138
Cdd:PRK05677 105 TNPLYTAREMEHQFNDSGAKalVCLANmahlaekvlpktGVKHVIVTEVADMLPPLkrllinAVVKHVKKmvpAYHLPQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 139 DCFDELLAQAAPCGDEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTE--RTLIA-MPIWHSS 215
Cdd:PRK05677 185 VKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgcEILIApLPLYHIY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 216 PLNNWFLGTLLMGGTAVLMREyaPRE---FLETLAQERISFTFGAPIAFLApLSVVPDVASYDFSAMRLWAYGGGPLGAD 292
Cdd:PRK05677 265 AFTFHCMAMMLIGNHNILISN--PRDlpaMVKELGKWKFSGFVGLNTLFVA-LCNNEAFRKLDFSALKLTLSGGMALQLA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 293 MARKLAQVYRSDrFMQVYGMTESGPLGTVlYPEEAVvKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQG 372
Cdd:PRK05677 342 TAERWKEVTGCA-ICEGYGMTETSPVVSV-NPSQAI-QVGTIGI-PVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 373 YLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGET 452
Cdd:PRK05677 418 YWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502603069 453 VVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK05677 498 IKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
16-501 |
1.18e-70 |
|
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: 232.03 E-value: 1.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYIL 95
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RHSGARLCLVDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaPHALAEILYTSGTTGQ 175
Cdd:cd05930 81 EDSGAKLVLTD-----------------------------------------------------PDDLAYVIYTSGSTGK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 176 PKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFlGTLLMGGTAVLMRE---YAPREFLETLAQERIS 252
Cdd:cd05930 108 PKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIF-GALLAGATLVVLPEevrKDPEALADLLAEEGIT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 253 FTFGAPiAFLAPLsvVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTES--GPLGTVLYPEEAVVK 330
Cdd:cd05930 187 VLHLTP-SLLRLL--LQELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEAtvDATYYRVPPDDEEDG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 331 AGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA---VLDDQGW---YRSGDLARVDEDGYL 404
Cdd:cd05930 264 RVPIGR-PIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAErfvPNPFGPGermYRTGDLVRWLPDGNL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 405 YIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIP 484
Cdd:cd05930 343 EFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVP 422
|
490
....*....|....*..
gi 502603069 485 RIFEVRDTLPRTATGKL 501
Cdd:cd05930 423 SAFVVLDALPLTPNGKV 439
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
163-503 |
1.32e-70 |
|
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: 228.54 E-value: 1.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 LAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREF 242
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGpLGTVL 322
Cdd:cd17638 82 LEAIERERITVLPGPPTLFQSLLDH-PGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAG-VATMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 323 YPEEAVVK-AGSIGRcAIPGVELEVrrqdgslcssGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDED 401
Cdd:cd17638 160 RPGDDAETvATTCGR-ACPGFEVRI----------ADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 402 GYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARY 481
Cdd:cd17638 229 GYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANY 308
|
330 340
....*....|....*....|..
gi 502603069 482 KIPRIFEVRDTLPRTATGKLLK 503
Cdd:cd17638 309 KVPRFVRFLDELPRNASGKVMK 330
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
26-501 |
1.53e-68 |
|
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: 226.71 E-value: 1.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 26 QDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLV 105
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 106 DGaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaPHALAEILYTSGTTGQPKGCLHSHAN 185
Cdd:cd05907 84 ED----------------------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRN 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 186 VFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVlmreYAPRE--FLETLAQERISFTFGAPIAFLA 263
Cdd:cd05907 112 ILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIY----FASSAetLLDDLSEVRPTVFLAVPRVWEK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 264 PLSVVPDVASYDF-SAMRLWAY---------GGGPLGADMARKLAQ----VYrsdrfmQVYGMTESGPLGTVLYPEEavV 329
Cdd:cd05907 188 VYAAIKVKAVPGLkRKLFDLAVggrlrfaasGGAPLPAELLHFFRAlgipVY------EGYGLTETSAVVTLNPPGD--N 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 330 KAGSIGRcAIPGVELEVrrqdgslcssGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDR 409
Cdd:cd05907 260 RIGTVGK-PLPGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGR 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 410 LKDMIVT-GGENVYSKEVEDVLCTHSDVQDVAVIG--RPHpewgetVVAVLTLKPGKT-----------------LVHED 469
Cdd:cd05907 329 KKDLIITsGGKNISPEPIENALKASPLISQAVVIGdgRPF------LVALIVPDPEALeawaeehgiaytdvaelAANPA 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502603069 470 LRQFME-------TRLARYKIPRIFEVrdtLPR---------TATGKL 501
Cdd:cd05907 403 VRAEIEaaveaanARLSRYEQIKKFLL---LPEpftiengelTPTLKL 447
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
23-507 |
1.73e-68 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 229.10 E-value: 1.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 23 ADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARL 102
Cdd:PLN02246 46 ATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 103 CLVDGARASLITAIQAEPqplaDIQWLSTASATEGLDCFDELLAqaapcGDEHGRPA----PHALAEILYTSGTTGQPKG 178
Cdd:PLN02246 126 IITQSCYVDKLKGLAEDD----GVTVVTIDDPPEGCLHFSELTQ-----ADENELPEveisPDDVVALPYSSGTTGLPKG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 179 CLHSHANV----------------FHaalcaaaatslaPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREF 242
Cdd:PLN02246 197 VMLTHKGLvtsvaqqvdgenpnlyFH------------SDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGAL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISftfgapIAFLAPLSVV-----PDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGP 317
Cdd:PLN02246 265 LELIQRHKVT------IAPFVPPIVLaiaksPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 318 -----LGTVLYPEEavVKAGSIG---RCAipgvELEVRRQD-GSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQG 388
Cdd:PLN02246 339 vlamcLAFAKEPFP--VKSGSCGtvvRNA----ELKIVDPEtGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 389 WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHE 468
Cdd:PLN02246 413 WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITED 492
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 502603069 469 DLRQFMETRLARYK-IPRIFEVrDTLPRTATGKLLKHMLR 507
Cdd:PLN02246 493 EIKQFVAKQVVFYKrIHKVFFV-DSIPKAPSGKILRKDLR 531
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
33-507 |
2.02e-68 |
|
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: 227.26 E-value: 2.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 33 LAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRhsgarlCLVDGARASL 112
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWK------CGACPAYKSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 113 ITAIQAEP---QPLADIQWLSTASATEGLDCFDELLAQAApcgdehGRPAPHALAE-----ILYTSGTTGQPKGCLHSH- 183
Cdd:cd05929 75 RAPRAEACaiiEIKAAALVCGLFTGGGALDGLEDYEAAEG------GSPETPIEDEaagwkMLYSGGTTGRPKGIKRGLp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 184 ANVFHAALCAAAATSLAPTE--RTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTFGAPIAF 261
Cdd:cd05929 149 GGPPDNDTLMAAALGFGPGAdsVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 262 --LAPL-SVVPDvaSYDFSAMRLWAYGGGPLGADMARKLAQVYrSDRFMQVYGMTESGPLgTVLYPEEAVVKAGSIGRcA 338
Cdd:cd05929 228 vrLLKLpEAVRN--AYDLSSLKRVIHAAAPCPPWVKEQWIDWG-GPIIWEYYGGTEGQGL-TIINGEEWLTHPGSVGR-A 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 339 IPGvELEVRRQDGSLCSSGEVGEICLRSAAMMQgYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGG 418
Cdd:cd05929 303 VLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 419 ENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPG---KTLVHEDLRQFMETRLARYKIPRIFEVRDTLPR 495
Cdd:cd05929 381 VNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGadaGTALAEELIAFLRDRLSRYKCPRSIEFVAELPR 460
|
490
....*....|..
gi 502603069 496 TATGKLLKHMLR 507
Cdd:cd05929 461 DDTGKLYRRLLR 472
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
18-507 |
3.74e-67 |
|
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: 222.72 E-value: 3.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 18 KLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRH 97
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 98 SGARLCLVDGAraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaphALAEILYTSGTTGQPK 177
Cdd:cd05919 81 CEARLVVTSAD-----------------------------------------------------DIAYLLYSSGTTGPPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 178 GCLHSHAN-VFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREY-APREFLETLAQERISFTF 255
Cdd:cd05919 108 GVMHAHRDpLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFRPTVLY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 256 GAPiAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDrFMQVYGMTESGPLGTVLYPEEavVKAGSIG 335
Cdd:cd05919 188 GVP-TFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGP-ILDGIGATEVGHIFLSNRPGA--WRLGSTG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 336 RcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIV 415
Cdd:cd05919 264 R-PVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNG-GWYRTGDKFCRDADGWYTHAGRADDMLK 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 416 TGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKT---LVHEDLRQFMETRLARYKIPRIFEVRDT 492
Cdd:cd05919 342 VGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAApqeSLARDIHRHLLERLSAHKVPRRIAFVDE 421
|
490
....*....|....*
gi 502603069 493 LPRTATGKLLKHMLR 507
Cdd:cd05919 422 LPRTATGKLQRFKLR 436
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
3-500 |
6.25e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 224.76 E-value: 6.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 3 NFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPI 82
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 83 NHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPLADIQWLSTASATEGLDC---FDELLAQAAPcgdehGRPA 159
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGavdYEDALAAGSP-----ERDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 PHALAE---ILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTE---------------RTLIAMPIWHSSPLNNWF 221
Cdd:PRK07798 159 GERSPDdlyLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEdeeelakraaagpgmRRFPAPPLMHGAGQWAAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 222 lGTLLMGGTAVL--MREYAPREFLETLAQER---ISFT---FGAPI--AFLAPlsvvpdvASYDFSAMRLWAYGGGPLGA 291
Cdd:PRK07798 239 -AALFSGQTVVLlpDVRFDADEVWRTIEREKvnvITIVgdaMARPLldALEAR-------GPYDLSSLFAIASGGALFSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 292 DMARKLAQVYRSDRFMQVYGMTESGPLGTvlypeeAVVKAGSIGRCAI---PGVELEVRRQDGS--LCSSGEVGEIClRS 366
Cdd:PRK07798 311 SVKEALLELLPNVVLTDSIGSSETGFGGS------GTVAKGAVHTGGPrftIGPRTVVLDEDGNpvEPGSGEIGWIA-RR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 367 AAMMQGYLDNREATAA---VLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIG 443
Cdd:PRK07798 384 GHIPLGYYKDPEKTAEtfpTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502603069 444 RPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGK 500
Cdd:PRK07798 464 VPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
5-507 |
3.07e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 223.29 E-value: 3.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 5 ISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINH 84
Cdd:PRK08162 21 LSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 85 KLQAPEVSYILRHSGARLCLVDGARASLITAIQAE---PQPLA---DIQWLSTASATEGLDcFDELLAQaapcGDEHGRP 158
Cdd:PRK08162 101 RLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALlpgPKPLVidvDDPEYPGGRFIGALD-YEAFLAS----GDPDFAW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 159 AP-----HALAeILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSsplNNW-FLGTL-LMGGTA 231
Cdd:PRK08162 176 TLpadewDAIA-LNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHC---NGWcFPWTVaARAGTN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 232 VLMREYAPREFLETLAQERISFTFGAPIAfLAPLSVVPD----VASYDFSAMrlwaYGGGPLGADMARKLAQVyrSDRFM 307
Cdd:PRK08162 252 VCLRKVDPKLIFDLIREHGVTHYCGAPIV-LSALINAPAewraGIDHPVHAM----VAGAAPPAAVIAKMEEI--GFDLT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 308 QVYGMTES-GPlGTV---------LYPEEAVVKAGSIG---------RCAIPGVELEVRRqDGSlcssgEVGEICLRSAA 368
Cdd:PRK08162 325 HVYGLTETyGP-ATVcawqpewdaLPLDERAQLKARQGvryplqegvTVLDPDTMQPVPA-DGE-----TIGEIMFRGNI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 369 MMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPE 448
Cdd:PRK08162 398 VMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPK 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 502603069 449 WGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFeVRDTLPRTATGKLLKHMLR 507
Cdd:PRK08162 477 WGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQKFVLR 534
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
28-507 |
4.99e-66 |
|
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: 220.07 E-value: 4.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 28 WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLclvdg 107
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 108 arasLITAiqaepQPLADiqwlstasategldcfdellaqaapcgdehgRPAPHALAEILYTSGTTGQPKGCLHSHANVF 187
Cdd:cd05969 76 ----LITT-----EELYE-------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 188 HAALCAAAATSLAPTERtliampIWHSS-PlnNWFLGT-------LLMGGTAVLMR-EYAPREFLETLAQERISFTFGAP 258
Cdd:cd05969 116 FYYFTGKYVLDLHPDDI------YWCTAdP--GWVTGTvygiwapWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 259 IAF--LAPLSVVPdVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSdRFMQVYGMTESGPLGTVLYPEEAVvKAGSIGR 336
Cdd:cd05969 188 TAIrmLMKEGDEL-ARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGV-PIHDTWWQTETGSIMIANYPCMPI-KPGSMGK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 337 cAIPGVELEVRRQDGSLCSSGEVGEICLRSA--AMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMI 414
Cdd:cd05969 265 -PLPGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGYFWFVGRADDII 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 415 VTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPG---KTLVHEDLRQFMETRLARYKIPRIFEVRD 491
Cdd:cd05969 343 KTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfepSDELKEEIINFVRQKLGAHVAPREIEFVD 422
|
490
....*....|....*.
gi 502603069 492 TLPRTATGKLLKHMLR 507
Cdd:cd05969 423 NLPKTRSGKIMRRVLK 438
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
2-508 |
4.65e-65 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 220.02 E-value: 4.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 2 MNFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:PRK13382 43 MGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 INHKLQAPEVSYILRHSGARLCLVDGARASLI-TAIQAEPQPLADIQWLSTASATEGLDCFDELLAQAAPCGDEHGRpap 160
Cdd:PRK13382 123 LNTSFAGPALAEVVTREGVDTVIYDEEFSATVdRALADCPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGR--- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 161 halaEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGtLLMGGTAVLMREYAPR 240
Cdd:PRK13382 200 ----VILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLA-ASLACTIVTRRRFDPE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 EFLETLAQERISFTFGAPIAFLAPLSVVPDV-ASYDFSAMRLWAYGGGPLGADMARKLAqvyrsDRFMQV----YGMTES 315
Cdd:PRK13382 275 ATLDLIDRHRATGLAVVPVMFDRIMDLPAEVrNRYSGRSLRFAAASGSRMRPDVVIAFM-----DQFGDViynnYNATEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 316 GPLGTVLyPEEAVVKAGSIGRCAIpGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNreATAAVLDdqGWYRSGDL 395
Cdd:PRK13382 350 GMIATAT-PADLRAAPDTAGRPAE-GTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG--STKDFHD--GFMASGDV 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 396 ARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFME 475
Cdd:PRK13382 424 GYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVR 503
|
490 500 510
....*....|....*....|....*....|...
gi 502603069 476 TRLARYKIPRIFEVRDTLPRTATGKLLKHMLRG 508
Cdd:PRK13382 504 DNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
5-507 |
4.41e-64 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 218.00 E-value: 4.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 5 ISLLDQQARTRPEKLALRADGQDWSYAALAQAGRR-AATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPIN 83
Cdd:PRK08974 26 VDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAfAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 84 hKLQAP-EVSYILRHSGARLCLVDGARASLITAIQAEPQPLADI-----QWLSTASAT------------------EGLD 139
Cdd:PRK08974 106 -PLYTPrELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVIltrmgDQLSTAKGTlvnfvvkyikrlvpkyhlPDAI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 140 CFDELLAQAApcGDEHGRP--APHALAEILYTSGTTGQPKGCLHSH----ANVFHAALCAAAATSLApTERTLIAMPIWH 213
Cdd:PRK08974 185 SFRSALHKGR--RMQYVKPelVPEDLAFLQYTGGTTGVAKGAMLTHrnmlANLEQAKAAYGPLLHPG-KELVVTALPLYH 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 214 SSPLNNWFLGTLLMGGTAVLMREyaPRE---FLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLG 290
Cdd:PRK08974 262 IFALTVNCLLFIELGGQNLLITN--PRDipgFVKELKKYPFTAITGVNTLFNALLNN-EEFQELDFSSLKLSVGGGMAVQ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 291 ADMARKLAQVYRSdRFMQVYGMTESGPLGTVlYPEEAVVKAGSIGrCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMM 370
Cdd:PRK08974 339 QAVAERWVKLTGQ-YLLEGYGLTECSPLVSV-NPYDLDYYSGSIG-LPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVM 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 371 QGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWG 450
Cdd:PRK08974 416 LGYWQRPEATDEVIKD-GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSG 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502603069 451 ETvVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK08974 495 EA-VKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
7-507 |
4.84e-64 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 219.44 E-value: 4.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALR--------ADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAwRLGAV 78
Cdd:PRK07529 30 LLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG-EAAGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 79 VVPINHKLQAPEVSYILRHSGAR----------------LCLVDGARASLITAIQ-----AEPQPLADIQWLSTASATEG 137
Cdd:PRK07529 109 ANPINPLLEPEQIAELLRAAGAKvlvtlgpfpgtdiwqkVAEVLAALPELRTVVEvdlarYLPGPKRLAVPLIRRKAHAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 138 LDCFDELLA-QAAPCGDEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSP 216
Cdd:PRK07529 189 ILDFDAELArQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 217 LNNWFLGTLLMGGTAVLMR------EYAPREFLETLAQERISFTFGAPIAfLAPLSVVPdVASYDFSAMRLWAYGGGPLG 290
Cdd:PRK07529 269 LLVTGLAPLARGAHVVLATpqgyrgPGVIANFWKIVERYRINFLSGVPTV-YAALLQVP-VDGHDISSLRYALCGAAPLP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 291 ADMARklaqvyrsdRFMQ--------VYGMTESGPLGTVLYPEeAVVKAGSIGRCaIPGVELEVRRQDG-----SLCSSG 357
Cdd:PRK07529 347 VEVFR---------RFEAatgvriveGYGLTEATCVSSVNPPD-GERRIGSVGLR-LPYQRVRVVILDDagrylRDCAVD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 358 EVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQ 437
Cdd:PRK07529 416 EVGVLCIAGPNVFSGYLEAAHNKGLWLED-GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVA 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502603069 438 DVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLA-RYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK07529 495 LAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
12-500 |
5.62e-63 |
|
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: 212.11 E-value: 5.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 12 ARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINhklqapev 91
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLD-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 92 syiLRHSGARlclvdgaraslITAIQAEPQPLADIQwlstasategldcfdellaqaapcgdehgrpAPHALAEILYTSG 171
Cdd:cd05945 73 ---ASSPAER-----------IREILDAAKPALLIA-------------------------------DGDDNAYIIFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 172 TTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLiampiwHSSPLN------NWFlGTLLMGGTAVLMREYA---PREF 242
Cdd:cd05945 108 STGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFL------NQAPFSfdlsvmDLY-PALASGATLVPVPRDAtadPKQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISFTFGAPiAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESgpLGTVL 322
Cdd:cd05945 181 FRFLAEHGITVWVSTP-SFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEA--TVAVT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 323 Y---PEEAVVKAGS--IGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVL---DDQGWYRSGD 394
Cdd:cd05945 258 YievTPEVLDGYDRlpIGY-AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpdEGQRAYRTGD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 395 LARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHE-DLRQF 473
Cdd:cd05945 337 LVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTkAIKAE 416
|
490 500
....*....|....*....|....*..
gi 502603069 474 METRLARYKIPRIFEVRDTLPRTATGK 500
Cdd:cd05945 417 LAERLPPYMIPRRFVYLDELPLNANGK 443
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
19-506 |
4.35e-62 |
|
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: 210.83 E-value: 4.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 19 LALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHs 98
Cdd:cd05923 20 IADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIER- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 99 garlclvdGARASLITAIQAEPQPlADIQWLSTASATEGLDCFDELLAQAAPCGDEHGRPAPHALaeILYTSGTTGQPKG 178
Cdd:cd05923 99 --------GEMTAAVIAVDAQVMD-AIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAF--VFYTSGTTGLPKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 179 CL--HSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTFG 256
Cdd:cd05923 168 AVipQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 257 APIAFLApLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQvYRSDRFMQVYGMTESGplgTVLYPEEAvvKAGSIGR 336
Cdd:cd05923 248 TPTHLDA-LAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ-HLPGEKVNIYGTTEAM---NSLYMRDA--RTGTEMR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 337 caiPGVELEVR--RQDGS---LCSSGEVGEICLRSAA--MMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDR 409
Cdd:cd05923 321 ---PGFFSEVRivRIGGSpdeALANGEEGELIVAAAAdaAFTGYLNQPEATAKKLQD-GWYRTGDVGYVDPSGDVRILGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 410 LKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGkTLVHEDLRQF-METRLARYKIPRIFE 488
Cdd:cd05923 397 VDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFcRASELADFKRPRRYF 475
|
490
....*....|....*...
gi 502603069 489 VRDTLPRTATGKLLKHML 506
Cdd:cd05923 476 FLDELPKNAMNKVLRRQL 493
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
166-500 |
6.65e-62 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 205.97 E-value: 6.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREYAPREFLET 245
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQERISF--TFgAPIafLAPLSVVPDVASYDFSAMRLWAYGGGPlgaDMARKLAQVYRSdRFMQVYGMTE-SGPLGTVL 322
Cdd:cd17637 84 IEEEKVTLmgSF-PPI--LSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGA-TFWSLYGQTEtSGLVTLSP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 323 YPEeavvKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDG 402
Cdd:cd17637 157 YRE----RPGSAGR-PGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 403 YLYIVDRL--KDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLAR 480
Cdd:cd17637 231 YLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIAR 310
|
330 340
....*....|....*....|
gi 502603069 481 YKIPRIFEVRDTLPRTATGK 500
Cdd:cd17637 311 YKKPRYVVFVEALPKTADGS 330
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-507 |
1.43e-61 |
|
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: 208.06 E-value: 1.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 28 WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDG 107
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 108 AraslitaiqaepqpladiqwlstasategldcfdellaqaapcgDEhgrpaphaLAEILYTSGTTGQPKGCLHSHANVF 187
Cdd:cd05971 87 S--------------------------------------------DD--------PALIIYTSGTTGPPKGALHAHRVLL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 188 -HAALCAAAATSLAPTERTLIAMPIWhssplnNWFLGTL------LMGGTAVL---MREYAPREFLETLAQERISFTFGA 257
Cdd:cd05971 115 gHLPGVQFPFNLFPRDGDLYWTPADW------AWIGGLLdvllpsLYFGVPVLahrMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 258 PIAfLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMarkLAQVYR--SDRFMQVYGMTESGPLGT---VLYPeeavVKAG 332
Cdd:cd05971 189 PTA-LKMMRQQGEQLKHAQVKLRAIATGGESLGEEL---LGWAREqfGVEVNEFYGQTECNLVIGncsALFP----IKPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 333 SIGRcAIPGVELEVRRQDGSLCSSGEVGEICLR--SAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRL 410
Cdd:cd05971 261 SMGK-PIPGHRVAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAG-DWLLTGDLGRKDSDGYFWYVGRD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 411 KDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKT---LVHEDLRQFMETRLARYKIPRIF 487
Cdd:cd05971 339 DDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETpsdALAREIQELVKTRLAAHEYPREI 418
|
490 500
....*....|....*....|
gi 502603069 488 EVRDTLPRTATGKLLKHMLR 507
Cdd:cd05971 419 EFVNELPRTATGKIRRRELR 438
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
8-507 |
3.66e-61 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 210.52 E-value: 3.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQART-RPEKLALR----ADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPI 82
Cdd:PRK04319 49 IDRHADGgRKDKVALRyldaSRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 83 NHKLQAPEVSYILRHSGARLclvdgarasLIT-AIQAEPQPLADIQWLST-------ASATEGLDCFDELLAQAAPCGD- 153
Cdd:PRK04319 129 FEAFMEEAVRDRLEDSEAKV---------LITtPALLERKPADDLPSLKHvllvgedVEEGPGTLDFNALMEQASDEFDi 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 154 EHGRPAPHALaeILYTSGTTGQPKGCLHSH-ANVFHAAlcaaaatslapTERTLI-----------AMPiwhssplnNWF 221
Cdd:PRK04319 200 EWTDREDGAI--LHYTSGSTGKPKGVLHVHnAMLQHYQ-----------TGKYVLdlheddvywctADP--------GWV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 222 LGT-------LLMGGTAVLMR-EYAPREFLETLAQERISFTFGAPIAFLAPLSVVPDVAS-YDFSAMRLWAYGGGPLGAD 292
Cdd:PRK04319 259 TGTsygifapWLNGATNVIDGgRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKkYDLSSLRHILSVGEPLNPE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 293 MARKLAQVYrSDRFMQVYGMTESGPLGTVLYPEEAVvKAGSIGRcAIPGVELE-VRRQDGSLcSSGEVGEICLRSA--AM 369
Cdd:PRK04319 339 VVRWGMKVF-GLPIHDNWWMTETGGIMIANYPAMDI-KPGSMGK-PLPGIEAAiVDDQGNEL-PPNRMGNLAIKKGwpSM 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 370 MQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEW 449
Cdd:PRK04319 415 MRGIWNNPEKYESYFAG-DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVR 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502603069 450 GETVVAVLTLKPGKTL---VHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK04319 494 GEIIKAFVALRPGYEPseeLKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
40-509 |
1.30e-60 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 208.58 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 40 AATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGAR-LCLVDGARASLITAIQA 118
Cdd:PRK08751 64 AAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASvLVVIDNFGTTVQQVIAD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 119 EP------QPLADIQWLSTASAT----------------EGLDCFDELLAQaapcGDEHGRP----APHALAEILYTSGT 172
Cdd:PRK08751 144 TPvkqvitTGLGDMLGFPKAALVnfvvkyvkklvpeyriNGAIRFREALAL----GRKHSMPtlqiEPDDIAFLQYTGGT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 173 TGQPKGCLHSH----ANVFHAALCAAAATSLAPTERTLI-AMPIWHSSPLNNWFLGTLLMGGTAVLMREyaPRE---FLE 244
Cdd:PRK08751 220 TGVAKGAMLTHrnlvANMQQAHQWLAGTGKLEEGCEVVItALPLYHIFALTANGLVFMKIGGCNHLISN--PRDmpgFVK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 245 TLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLGADMARKLAQVyRSDRFMQVYGMTESGPlGTVLYP 324
Cdd:PRK08751 298 ELKKTRFTAFTGVNTLFNGLLNT-PGFDQIDFSSLKMTLGGGMAVQRSVAERWKQV-TGLTLVEAYGLTETSP-AACINP 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 325 EEAVVKAGSIGrCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYL 404
Cdd:PRK08751 375 LTLKEYNGSIG-LPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFV 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 405 YIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGEtVVAVLTLKPGKTLVHEDLRQFMETRLARYKIP 484
Cdd:PRK08751 454 YIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE-IVKVVIVKKDPALTAEDVKAHARANLTGYKQP 532
|
490 500
....*....|....*....|....*
gi 502603069 485 RIFEVRDTLPRTATGKLLKHMLRGS 509
Cdd:PRK08751 533 RIIEFRKELPKTNVGKILRRELRDA 557
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
25-507 |
1.34e-60 |
|
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: 208.15 E-value: 1.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 25 GQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCL 104
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 105 VDGARASLITAIQAEPQPLADIQWLSTASATEGLDCFDELLAQAAPCGDEHGRPAPHA------LAEILYTSGTTGQPKG 178
Cdd:cd17642 122 CSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSfdrdeqVALIMNSSGSTGLPKG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 179 CLHSHANV---FHAALCAAAATSLAPTERTLIAMPIWHSSPLNNwFLGTLLMGGTAVLMREYAPREFLETLAQERISFTF 255
Cdd:cd17642 202 VQLTHKNIvarFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 256 GAP--IAFLAPLSVVPdvaSYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESgpLGTVLYPEEAVVKAGS 333
Cdd:cd17642 281 LVPtlFAFFAKSTLVD---KYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTET--TSAILITPEGDDKPGA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 334 IGRcAIPGVELEVRRQD-GSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKD 412
Cdd:cd17642 356 VGK-VVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 413 MIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPR---IFev 489
Cdd:cd17642 435 LIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRggvKF-- 512
|
490
....*....|....*...
gi 502603069 490 RDTLPRTATGKLLKHMLR 507
Cdd:cd17642 513 VDEVPKGLTGKIDRRKIR 530
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
7-501 |
1.46e-60 |
|
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: 206.67 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGAraslitaiqaepqpladiqwlSTASATEGLDCFDELLAQ-AAPCGDEHGRPAPHALAE 165
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRS---------------------LAGRAGGLEVAVVIDEALdAGPAGNPAVPVSPDDLAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSHANVFhAALCAAAATSLAPTERTLIAMPI-WHSSPLNNWflGTLLMGGTAVLMREYA---PRE 241
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGVV-RLVKNTNYVTLGPDDRVLQTSPLaFDASTFEIW--GALLNGARLVLAPKGTlldPDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 242 FLETLAQERISftfgapIAFL-APL-SVVPDVASYDFSAMR-LWAyGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPL 318
Cdd:cd12117 218 LGALIAEEGVT------VLWLtAALfNQLADEDPECFAGLReLLT-GGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 319 GTVLYPEEAVVKAGS--IGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAV------LDDQGWY 390
Cdd:cd12117 291 TTSHVVTELDEVAGSipIGR-PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERfvadpfGPGERLY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 391 RSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTlvHEDL 470
Cdd:cd12117 370 RTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALD--AAEL 447
|
490 500 510
....*....|....*....|....*....|.
gi 502603069 471 RQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd12117 448 RAFLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
3-507 |
1.55e-59 |
|
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: 205.42 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 3 NF-ISLLDQQARTRPEKLAL-----RADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLG 76
Cdd:cd05970 17 NFaYDVVDAMAKEYPDKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 77 AVVVPINHKLQAPEVSYILRHSGARLCLVDGARASL--ITAIQAEPQPLADIQWLStASATEGLDCFDELLAQAAPcgde 154
Cdd:cd05970 97 AIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPeeIEKAAPECPSKPKLVWVG-DPVPEGWIDFRKLIKNASP---- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 155 hGRPAPHALAE--------ILYTSGTTGQPKGCLHSHanvfhaalcaaaatsLAPTERTLIAMpIWHSSPLNNWFL---- 222
Cdd:cd05970 172 -DFERPTANSYpcgedillVYFSSGTTGMPKMVEHDF---------------TYPLGHIVTAK-YWQNVREGGLHLtvad 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 223 --------GTLL---MGGTAVL---MREYAPREFLETLAQERISfTFGAPIAFLAPLsVVPDVASYDFSAMRLWAYGGGP 288
Cdd:cd05970 235 tgwgkavwGKIYgqwIAGAAVFvydYDKFDPKALLEKLSKYGVT-TFCAPPTIYRFL-IREDLSRYDLSSLRYCTTAGEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 289 LGADMARKLAQvYRSDRFMQVYGMTESG-PLGTVLYPEeavVKAGSIGRCAiPGVELEVRRQDGSLCSSGEVGEICLRSA 367
Cdd:cd05970 313 LNPEVFNTFKE-KTGIKLMEGFGQTETTlTIATFPWME---PKPGSMGKPA-PGYEIDLIDREGRSCEAGEEGEIVIRTS 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 368 -----AMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVI 442
Cdd:cd05970 388 kgkpvGLFGGYYKDAEKTAEVWHD-GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502603069 443 GRPHPEWGETVVAVLTL----KPGKTLVHEdLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05970 467 GVPDPIRGQVVKATIVLakgyEPSEELKKE-LQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
10-501 |
4.71e-59 |
|
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: 202.96 E-value: 4.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 10 QQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAP 89
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 90 EVSYILRHSGARLCLVDGARASLitaiqAEPQPLADIQWlstasategldcfDELLAQAAPCGDEHGRPAPHALAEILYT 169
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAGE-----LAVELVAVTLL-------------DQPGAAAGADAEPDPALDADDLAYVIYT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 170 SGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTL-IAMPIWHSSPLNNWflGTLLMGGTAVLMREYA---PREFLET 245
Cdd:cd17651 145 SGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLqFAGLGFDVSVQEIF--STLCAGATLVLPPEEVrtdPPALAAW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQERISFTFgAPIAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMA-RKLAQVYRSDRFMQVYGMTESG-------P 317
Cdd:cd17651 223 LDEQRISRVF-LPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHvvtalslP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 318 LGTVLYPEEAvvkagSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG----WYR 391
Cdd:cd17651 302 GDPAAWPAPP-----PIGR-PIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAErfVPDPFVpgarMYR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 392 SGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLR 471
Cdd:cd17651 376 TGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELR 455
|
490 500 510
....*....|....*....|....*....|
gi 502603069 472 QFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17651 456 AALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
18-507 |
1.16e-58 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 200.40 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 18 KLALRADGQDWSYAALAQAGRRAATVL-YEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILR 96
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 97 HSGARLCLVDGAraslitaiqaepqpladiqwlSTASATEGLdcfdellaqaapcgdehgrpaphalaeILYTSGTTGQP 176
Cdd:cd05958 81 KARITVALCAHA---------------------LTASDDICI---------------------------LAFTSGTTGAP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 177 KGCLHSHANVFHAALC-AAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQERISFTF 255
Cdd:cd05958 113 KATMHFHRDPLASADRyAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 256 GAPIAFLAPLSVvPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDrFMQVYGMTESGPLGTVLYPEEAvvKAGSIG 335
Cdd:cd05958 193 TAPTAYRAMLAH-PDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIP-IIDGIGSTEMFHIFISARPGDA--RPGATG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 336 RcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAvldDQGWYRSGDLARVDEDGYLYIVDRLKDMIV 415
Cdd:cd05958 269 K-PVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRTYV---QGGWNITGDTYSRDPDGYFRHQGRSDDMIV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 416 TGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKT----LVHEdLRQFMETRLARYKIPRIFEVRD 491
Cdd:cd05958 345 SGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpgpvLARE-LQDHAKAHIAPYKYPRAIEFVT 423
|
490
....*....|....*.
gi 502603069 492 TLPRTATGKLLKHMLR 507
Cdd:cd05958 424 ELPRTATGKLQRFALR 439
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
5-509 |
1.38e-58 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 203.33 E-value: 1.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 5 ISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINh 84
Cdd:PRK07059 26 ADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVN- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 85 KLQAP-EVSYILRHSGARLCLVDGARASLITAIQAEPQ-------PLAD---------------IQWLSTASATEGLDCF 141
Cdd:PRK07059 105 PLYTPrELEHQLKDSGAEAIVVLENFATTVQQVLAKTAvkhvvvaSMGDllgfkghivnfvvrrVKKMVPAWSLPGHVRF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 142 DELLAQAAPCGDEHGRPAPHALAEILYTSGTTGQPKGC--LHSH--ANVFHAALCAAAATSLAPTERTLI---AMPIWHS 214
Cdd:PRK07059 185 NDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGAtlLHRNivANVLQMEAWLQPAFEKKPRPDQLNfvcALPLYHI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 215 SPLNNWFLGTLLMGGTAVLMREyaPRE---FLETLAQERISfTFGAPIAFLAPLSVVPDVASYDFSAMRLwAYGGGplga 291
Cdd:PRK07059 265 FALTVCGLLGMRTGGRNILIPN--PRDipgFIKELKKYQVH-IFPAVNTLYNALLNNPDFDKLDFSKLIV-ANGGG---- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 292 dMArklAQVYRSDRFMQV--------YGMTESGPLGTVlYPEEAVVKAGSIGrCAIPGVELEVRRQDGSLCSSGEVGEIC 363
Cdd:PRK07059 337 -MA---VQRPVAERWLEMtgcpitegYGLSETSPVATC-NPVDATEFSGTIG-LPLPSTEVSIRDDDGNDLPLGEPGEIC 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 364 LRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIG 443
Cdd:PRK07059 411 IRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVG 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502603069 444 RPHPEWGEtVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLRGS 509
Cdd:PRK07059 491 VPDEHSGE-AVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDG 555
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
39-507 |
1.92e-58 |
|
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: 200.36 E-value: 1.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 39 RAATVLYEQGVRQGDKLGLLCFNTPGFVFALLG----AWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGARASLIT 114
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAvayaGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 115 AiqAEPQPLADIQWLSTasatEGLDcfdellaqaapcGDEHGRPA----PHALAEILYTSGTTGQPKGCLHSHANVFHAA 190
Cdd:cd05922 85 D--ALPASPDPGTVLDA----DGIR------------AARASAPAhevsHEDLALLLYTSGSTGSPKLVRLSHQNLLANA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 191 LCAAAATSLAPTERTLIAMPIWHSSPLNNwFLGTLLMGGTAVLMREYA-PREFLETLAQERISFTFGAPIAFLAPLSVVP 269
Cdd:cd05922 147 RSIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVlDDAFWEDLREHGATGLAGVPSTYAMLTRLGF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 270 DVASYdfSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPLGTVLYPEEAVVKAGSIGrCAIPGVELEVRRQ 349
Cdd:cd05922 226 DPAKL--PSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIG-LAIPGGEFEILDD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 350 DGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDV 429
Cdd:cd05922 303 DGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502603069 430 LCTHSDVQDVAVIGRPHPEwGETVVAVLTLKPGKTLvhEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05922 383 ARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDP--KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
168-501 |
2.95e-57 |
|
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: 193.39 E-value: 2.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 168 YTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNwFLGTLLMGGTAVLMREYAPREFLETLA 247
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYG-AISALYLGGTFIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 248 QERISFTFGAPIAFLAPLSV-VPDvasydfSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPLgTVLYPEE 326
Cdd:cd17633 86 QYNATVIYLVPTMLQALARTlEPE------SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI-TYNFNQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 327 AVvKAGSIGRcAIPGVELEVRRQDGslcssGEVGEICLRSAAMMQGYLDNREATAavlddQGWYRSGDLARVDEDGYLYI 406
Cdd:cd17633 159 SR-PPNSVGR-PFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 407 VDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTlkpGKTLVHEDLRQFMETRLARYKIPRI 486
Cdd:cd17633 227 VGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPKK 303
|
330
....*....|....*
gi 502603069 487 FEVRDTLPRTATGKL 501
Cdd:cd17633 304 IIFVDSLPYTSSGKI 318
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
2-507 |
5.56e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 198.43 E-value: 5.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 2 MNFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 INHKLQAPEVSYILRHSGARLCLVDGARASL-ITAIQAEPQP--LADIQWL----STASATEGLDCFDELLAQAAPCGDE 154
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWPGFKGIdFAAILAAVPPdaLPPLRAIavvdDAADATPAPAPGARVQLFALPDPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 155 H----GRPAPHALAEILYT-SGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNwFLGTLLMGG 229
Cdd:PRK06164 170 PaaagERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFST-LLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 230 TAVLMREYAPREFLETLAQERISFTFGAPIAFLAPLSVVPdvASYDFSAMRLWAYGGGPLGADMARKLAQvyrsDRFMQV 309
Cdd:PRK06164 249 PLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG--ERADFPSARLFGFASFAPALGELAALAR----ARGVPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 310 YGMTESGPL------GTVLYPEEAVVKAGsiGRCAIPGVELEVRR-QDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA 382
Cdd:PRK06164 323 TGLYGSSEVqalvalQPATDPVSVRIEGG--GRPASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 383 VLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPewGETV-VAVLTLKP 461
Cdd:PRK06164 401 ALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTVpVAFVIPTD 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502603069 462 GKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATG---KLLKHMLR 507
Cdd:PRK06164 479 GASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
25-507 |
2.43e-56 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 197.35 E-value: 2.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 25 GQDWSYAALA-QAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARL- 102
Cdd:PRK12492 47 GVTLSYAELErHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 103 ------------CLVDGARASLITAIQAEPQPLADIQWLSTASATEGLDCFDELLAQAAP------CGDEHG-RPAPHAL 163
Cdd:PRK12492 127 vylnmfgklvqeVLPDTGIEYLIEAKMGDLLPAAKGWLVNTVVDKVKKMVPAYHLPQAVPfkqalrQGRGLSlKPVPVGL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 AEIL---YTSGTTGQPKGCLHSHAN-VFHAALCAAAATSLAPTERTLI---------AMPIWHSSPLNNWFLGTLLMGGT 230
Cdd:PRK12492 207 DDIAvlqYTGGTTGLAKGAMLTHGNlVANMLQVRACLSQLGPDGQPLMkegqevmiaPLPLYHIYAFTANCMCMMVSGNH 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 231 AVLMREyaPRE---FLETLAQERISFTFGAPIAFLApLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSdRFM 307
Cdd:PRK12492 287 NVLITN--PRDipgFIKELGKWRFSALLGLNTLFVA-LMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGC-TIV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 308 QVYGMTESGPLGTVlYPEEAVVKAGSIGrCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQ 387
Cdd:PRK12492 363 EGYGLTETSPVAST-NPYGELARLGTVG-IPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 388 GWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETV-VAVLTLKPGKTLv 466
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVkLFVVARDPGLSV- 519
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502603069 467 hEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK12492 520 -EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
6-501 |
7.93e-56 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 195.11 E-value: 7.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLDQQARTRPEKLAL--RADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPIN 83
Cdd:PRK05852 20 DLVEVAATRLPEAPALvvTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 84 HKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPLAdIQWLSTASATEGLDCFDeLLAQAAPcgdEHGRPAPHAL 163
Cdd:PRK05852 100 PALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLT-VNVGGDSGPSGGTLSVH-LDAATEP---TPATSTPEGL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 ----AEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVL--MREY 237
Cdd:PRK05852 175 rpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpaRGRF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 238 APREFLETLAQERISFTFGAPIAFLAPLSVV-PDVASYDFSAMRLWAYGGGPLGADMARKLaqvyrSDRF----MQVYGM 312
Cdd:PRK05852 255 SAHTFWDDIKAVGATWYTAVPTIHQILLERAaTEPSGRKPAALRFIRSCSAPLTAETAQAL-----QTEFaapvVCAFGM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 313 TE------SGPLGTVLYPEEAVVKAGSIGRCAipGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDD 386
Cdd:PRK05852 330 TEathqvtTTQIEGIGQTENPVVSTGLVGRST--GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 387 qGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLV 466
Cdd:PRK05852 408 -GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPT 486
|
490 500 510
....*....|....*....|....*....|....*
gi 502603069 467 HEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK05852 487 AEELVQFCRERLAAFEIPASFQEASGLPHTAKGSL 521
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
10-507 |
1.43e-55 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 194.81 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 10 QQARTRPEKLAL--RADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQ 87
Cdd:PLN02330 36 QDAELYADKVAFveAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 88 APEVSYILRHSGARLCLVDGARASLITAIQAepqPLADIQWLSTASATEgldcFDELLAQAAPCGDEHGRPAPHA--LAE 165
Cdd:PLN02330 116 ESEIKKQAEAAGAKLIVTNDTNYGKVKGLGL---PVIVLGEEKIEGAVN----WKELLEAADRAGDTSDNEEILQtdLCA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTER--TLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFL 243
Cdd:PLN02330 189 LPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQvvTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 244 ETLAQERISFtfgAPIAFLAPLSVV--PDVASYDFSAMRLWAY--GGGPLGADMARKLAQVYRSDRFMQVYGMTESGPLg 319
Cdd:PLN02330 269 NALITQEVSF---APIVPPIILNLVknPIVEEFDLSKLKLQAImtAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCI- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 320 TVLY--PEEA--VVKAGSIGrCAIPGVELE-VRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGD 394
Cdd:PLN02330 345 TLTHgdPEKGhgIAKKNSVG-FILPNLEVKfIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 395 LARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFM 474
Cdd:PLN02330 424 IGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFV 503
|
490 500 510
....*....|....*....|....*....|...
gi 502603069 475 ETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PLN02330 504 AANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-507 |
6.07e-55 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 193.04 E-value: 6.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGA 108
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 109 RASLITAIqAEPQPLADIQWLSTASAT------EGLDCFDELLAQAApcGD-EHGRPAPHALAEILYTSGTTGQPKGCLH 181
Cdd:PRK06018 121 FVPILEKI-ADKLPSVERYVVLTDAAHmpqttlKNAVAYEEWIAEAD--GDfAWKTFDENTAAGMCYTSGTTGDPKGVLY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 182 SH-ANVFHAALCAAAATSLAPTERTLI-AMPIWHSsplNNWFLG-TLLMGGTAVLMreyaPREFL------ETLAQERIS 252
Cdd:PRK06018 198 SHrSNVLHALMANNGDALGTSAADTMLpVVPLFHA---NSWGIAfSAPSMGTKLVM----PGAKLdgasvyELLDTEKVT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 253 FTFGAPIAFLAPLSVVpDVASYDFSAMRLWAYGggplGADMARKLAQVYrSDRFMQVY---GMTESGPLGTV-------- 321
Cdd:PRK06018 271 FTAGVPTVWLMLLQYM-EKEGLKLPHLKMVVCG----GSAMPRSMIKAF-EDMGVEVRhawGMTEMSPLGTLaalkppfs 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 322 -LYPEEAVVKAGSIGRcAIPGVELEVRRQDG-SLCSSGEV-GEICLRSAAMMQGYLdnrEATAAVLDDQGWYRSGDLARV 398
Cdd:PRK06018 345 kLPGDARLDVLQKQGY-PPFGVEMKITDDAGkELPWDGKTfGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVATI 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 399 DEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRL 478
Cdd:PRK06018 421 DAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKI 500
|
490 500
....*....|....*....|....*....
gi 502603069 479 ARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK06018 501 AKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
23-511 |
4.00e-54 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 191.21 E-value: 4.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 23 ADGQDWSYAALAQAGRRAATVLYEQ-GVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYilRHSGAR 101
Cdd:PLN02574 62 STGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKK--RVVDCS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 102 LCLVdgaraslitaiQAEPQPLADIQWL--STASATEGLDcFDELLAQAAPC-----GDEHGRPAP----HALAEILYTS 170
Cdd:PLN02574 140 VGLA-----------FTSPENVEKLSPLgvPVIGVPENYD-FDSKRIEFPKFyelikEDFDFVPKPvikqDDVAAIMYSS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 171 GTTGQPKGCLHSHANVFHAALC-----AAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLET 245
Cdd:PLN02574 208 GTTGASKGVVLTHRNLIAMVELfvrfeASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQERISFTFGAPIAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPLGTVLYPE 325
Cdd:PLN02574 288 IDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 326 EAVVKAGSIGRCAiPGVELE-VRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYL 404
Cdd:PLN02574 368 EKLSKYSSVGLLA-PNMQAKvVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 405 YIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIP 484
Cdd:PLN02574 447 YIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKV 526
|
490 500
....*....|....*....|....*..
gi 502603069 485 RIFEVRDTLPRTATGKLLKHMLRGSTT 511
Cdd:PLN02574 527 RKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
29-441 |
5.41e-54 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 187.09 E-value: 5.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAAL-AQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDG 107
Cdd:TIGR01733 1 TYRELdERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 108 ARASLITAIQAEPQPLADIQWLSTAsateglDCFDELLAQAAPCGDEhgrpaphaLAEILYTSGTTGQPKGCLHSHANVF 187
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALD------DAPAPPPPDAPSGPDD--------LAYVIYTSGSTGRPKGVVVTHRSLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 188 HAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFlGTLLMGGTAVLMRE---YAPREFLETLAQER-ISFTFGAPiaflA 263
Cdd:TIGR01733 147 NLLAWLARRYGLDPDDRVLQFASLSFDASVEEIF-GALLAGATLVVPPEdeeRDDAALLAALIAEHpVTVLNLTP----S 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 264 PLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTEsgplGTV-------LYPEEAVVKAGSIGR 336
Cdd:TIGR01733 222 LLALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTE----TTVwstatlvDPDDAPRESPVPIGR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 337 CaIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVL--------DDQGWYRSGDLARVDEDGYLYIVD 408
Cdd:TIGR01733 298 P-LANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLG 376
|
410 420 430
....*....|....*....|....*....|...
gi 502603069 409 RLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAV 441
Cdd:TIGR01733 377 RIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
12-508 |
6.03e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 188.66 E-value: 6.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 12 ARTRPEKLALRADGQDWSYAALAqagrRAATVLYEQgVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEV 91
Cdd:PRK07787 10 AAAADIADAVRIGGRVLSRSDLA----GAATAVAER-VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 92 SYILRHSGARLCLVDGARASLitAIQAEPQPLADIQWLSTASategldcfdellaqaapcgdehgrPAPHALAEILYTSG 171
Cdd:PRK07787 85 RHILADSGAQAWLGPAPDDPA--GLPHVPVRLHARSWHRYPE------------------------PDPDAPALIVYTSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 172 TTGQPKGCLHSHANVFHAALCAAAATSLAPtERTLI-AMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAqER 250
Cdd:PRK07787 139 TTGPPKGVVLSRRAIAADLDALAEAWQWTA-DDVLVhGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQALS-EG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 251 ISFTFGAPIAFLaplSVVPDVASYD-FSAMRLWAYGGGPLGADMARKLAQVyRSDRFMQVYGMTESgpLGTVLYPEEAVV 329
Cdd:PRK07787 217 GTLYFGVPTVWS---RIAADPEAARaLRGARLLVSGSAALPVPVFDRLAAL-TGHRPVERYGMTET--LITLSTRADGER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 330 KAGSIGRcAIPGVELEVRRQDGS-LCSSGE-VGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIV 407
Cdd:PRK07787 291 RPGWVGL-PLAGVETRLVDEDGGpVPHDGEtVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 408 DRLK-DMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTlkPGKTLVHEDLRQFMETRLARYKIPRI 486
Cdd:PRK07787 370 GREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSVHKRPRE 447
|
490 500
....*....|....*....|..
gi 502603069 487 FEVRDTLPRTATGKLLKHMLRG 508
Cdd:PRK07787 448 VRFVDALPRNAMGKVLKKQLLS 469
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
6-503 |
7.08e-54 |
|
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: 196.23 E-value: 7.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINhk 85
Cdd:COG1020 480 ELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD-- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 86 LQAPE--VSYILRHSGARLCLVDGARASLItaiqaepqPLADIQWLstasategldCFDELLAQAAPCGDEHGRPAPHAL 163
Cdd:COG1020 558 PAYPAerLAYMLEDAGARLVLTQSALAARL--------PELGVPVL----------ALDALALAAEPATNPPVPVTPDDL 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 AEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLiampiwHSSPLN----NW-FLGTLLMGGTAVLMREYA 238
Cdd:COG1020 620 AYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVL------QFASLSfdasVWeIFGALLSGATLVLAPPEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 239 ---PREFLETLAQERISftfgapIAFLAP--LSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMT 313
Cdd:COG1020 694 rrdPAALAELLARHRVT------VLNLTPslLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPT 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 314 ES--GPLGTVLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG- 388
Cdd:COG1020 768 ETtvDSTYYEVTPPDADGGSVPIGR-PIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfVADPFGf 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 389 ----WYRSGDLARVDEDGYLYIVDRLKDMIvtggenvysK---------EVEDVLCTHSDVQDVAVIGRPHPEWGETVVA 455
Cdd:COG1020 847 pgarLYRTGDLARWLPDGNLEFLGRADDQV---------KirgfrielgEIEAALLQHPGVREAVVVAREDAPGDKRLVA 917
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502603069 456 VLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLK 503
Cdd:COG1020 918 YVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDR 965
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
12-507 |
1.21e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 188.45 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 12 ARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQgDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEV 91
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 92 SYILRHSGARLCLVDgarASLITAIQAEPQPLADI-QWLSTASAtegldcfdELLAQAAPCGDEHgrpAPHALAeilYTS 170
Cdd:PRK07638 90 KERLAISNADMIVTE---RYKLNDLPDEEGRVIEIdEWKRMIEK--------YLPTYAPIENVQN---APFYMG---FTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 171 GTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSplnnwFL----GTLLMGGTAVLMREYAPREFLETL 246
Cdd:PRK07638 153 GSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSL-----FLygaiSTLYVGQTVHLMRKFIPNQVLDKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 247 AQERISFTFGAPIAFLAPLSV--VPDVASYDFSAMRLWaygggplGADMARKLAQVYRSDRFMQVYGMTESGPLgTVLYP 324
Cdd:PRK07638 228 ETENISVMYTVPTMLESLYKEnrVIENKMKIISSGAKW-------EAEAKEKIKNIFPYAKLYEFYGASELSFV-TALVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 325 EEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLdNREATAAVLDDQGWYRSGDLARVDEDGYL 404
Cdd:PRK07638 300 EESERRPNSVGR-PFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYI-IGGVLARELNADGWMTVRDVGYEDEEGFI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 405 YIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTlkpGKTLVHEdLRQFMETRLARYKIP 484
Cdd:PRK07638 378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIK---GSATKQQ-LKSFCLQRLSSFKIP 453
|
490 500
....*....|....*....|...
gi 502603069 485 RIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK07638 454 KEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
166-499 |
1.62e-52 |
|
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: 180.96 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREYAPREFLET 245
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLM-FTLATFHAGGTNVFVRRVDAEEVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQERIS--FTFGAPIAFLAPLSV--VPDVAS-YDFSAMRLWAYGGGPLGADMARKLAQvyrsdrfmqvYGMTESGplGT 320
Cdd:cd17636 84 IEAERCThaFLLPPTIDQIVELNAdgLYDLSSlRSSPAAPEWNDMATVDTSPWGRKPGG----------YGQTEVM--GL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 321 VLYPEEAVVKAGSIGRCAiPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDE 400
Cdd:cd17636 152 ATFAALGGGAIGGAGRPS-PLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 401 DGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLAR 480
Cdd:cd17636 230 DGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIAS 309
|
330
....*....|....*....
gi 502603069 481 YKIPRIFEVRDTLPRTATG 499
Cdd:cd17636 310 YKKPKSVEFADALPRTAGG 328
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
10-501 |
7.89e-52 |
|
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: 184.75 E-value: 7.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 10 QQARTRPEKLALR------ADGQDWSYAALAQAGRRAATVLYEQGvRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPI- 82
Cdd:cd05931 1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 83 --NHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPLADIQWLSTasategldcfdELLAQAAPCGDEHGRPAP 160
Cdd:cd05931 80 ppTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVV-----------DLLPDTSAADWPPPSPDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 161 HALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMreyAPR 240
Cdd:cd05931 149 DDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM---SPA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 EF-------LETLAQERISFTFGAPIAF-LAPLSVVP-DVASYDFSAMRlWAYGGG-PLGADMARKLAQV-----YRSDR 305
Cdd:cd05931 226 AFlrrplrwLRLISRYRATISAAPNFAYdLCVRRVRDeDLEGLDLSSWR-VALNGAePVRPATLRRFAEAfapfgFRPEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 306 FMQVYGMTES------GPLGTVL-----------YPEEAVVKAGSIGR----CAIPGVELEVR---RQDGSLCSSGEVGE 361
Cdd:cd05931 305 FRPSYGLAEAtlfvsgGPPGTGPvvlrvdrdalaGRAVAVAADDPAARelvsCGRPLPDQEVRivdPETGRELPDGEVGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 362 ICLRSAAMMQGYLDNREATAAV------LDDQGWYRSGDLARVDeDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSD 435
Cdd:cd05931 385 IWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502603069 436 VQD---VAVIGRPHPEwGETVVAVLTLKPGKT-LVHEDLRQFMETRLAR---YKIPRIFEVR-DTLPRTATGKL 501
Cdd:cd05931 464 ALRpgcVAAFSVPDDG-EERLVVVAEVERGADpADLAAIAAAIRAAVARehgVAPADVVLVRpGSIPRTSSGKI 536
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
28-507 |
1.02e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 184.14 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 28 WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDG 107
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 108 ARASLITAIQAE-PQ-----PLADIQWLSTASATegLDCFDELL-AQAA----PCGDEHgrpaphALAEILYTSGTTGQP 176
Cdd:PRK07008 120 TFLPLVDALAPQcPNvkgwvAMTDAAHLPAGSTP--LLCYETLVgAQDGdydwPRFDEN------QASSLCYTSGTTGNP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 177 KGCLHSH-ANVFHAALCAAaatslaPTERTLIAM-------PIWHsspLNNWFL--GTLLMGGTAVLmreyaP------R 240
Cdd:PRK07008 192 KGALYSHrSTVLHAYGAAL------PDAMGLSARdavlpvvPMFH---VNAWGLpySAPLTGAKLVL-----PgpdldgK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 EFLETLAQERISFTFGAPIAFLAPLSVVPDvASYDFSAMRLWAYGGGPLGADMARKLAQVYrSDRFMQVYGMTESGPLGT 320
Cdd:PRK07008 258 SLYELIEAERVTFSAGVPTVWLGLLNHMRE-AGLRFSTLRRTVIGGSACPPAMIRTFEDEY-GVEVIHAWGMTEMSPLGT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 321 VL--------YPEEAVVKA-GSIGRcAIPGVELEVRRQDGS-LCSSGEV-GEICLRSAAMMQGYLDNreaTAAVLDDqGW 389
Cdd:PRK07008 336 LCklkwkhsqLPLDEQRKLlEKQGR-VIYGVDMKIVGDDGReLPWDGKAfGDLQVRGPWVIDRYFRG---DASPLVD-GW 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 390 YRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHED 469
Cdd:PRK07008 411 FPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREE 490
|
490 500 510
....*....|....*....|....*....|....*...
gi 502603069 470 LRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK07008 491 LLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
163-507 |
6.10e-51 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 177.67 E-value: 6.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 LAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPR-- 240
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRnp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 ----EFLETLAQERISFTFGAPIAfLAPLSVVPDVAsyDFSAMRLWAYGGGPLGADMARKLaQVYRSDRFMQVYGMTESG 316
Cdd:cd05944 84 glfdNFWKLVERYRITSLSTVPTV-YAALLQVPVNA--DISSLRFAMSGAAPLPVELRARF-EDATGLPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 317 PLGTVLYPEEAVvKAGSIGRcAIPGVELEVRRQDGSL-----CSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYR 391
Cdd:cd05944 160 CLVAVNPPDGPK-RPGSVGL-RLPYARVRIKVLDGVGrllrdCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVAD-GWLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 392 SGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLR 471
Cdd:cd05944 237 TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELL 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 502603069 472 QFMETRLA-RYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05944 317 AWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
162-501 |
7.15e-51 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 176.37 E-value: 7.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 162 ALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGtlLMGGTAVLMREYApRE 241
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS--LLAGAELVLLERN-QA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 242 FLETLAQERISFTfgapiaflaplSVVP---------DVASYDFSAMRLWAYGGGPLGADMARKLAQvyRSDRFMQVYGM 312
Cdd:cd17630 78 LAEDLAPPGVTHV-----------SLVPtqlqrlldsGQGPAALKSLRAVLLGGAPIPPELLERAAD--RGIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 313 TESGplGTVLYPEEAVVKAGSIGRcAIPGVELevRRQDGslcssgevGEICLRSAAMMQGYLDNREATAavLDDQGWYRS 392
Cdd:cd17630 145 TETA--SQVATKRPDGFGRGGVGV-LLPGREL--RIVED--------GEIWVGGASLAMGYLRGQLVPE--FNEDGWFTT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 393 GDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTlvHEDLRQ 472
Cdd:cd17630 210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD--PAELRA 287
|
330 340
....*....|....*....|....*....
gi 502603069 473 FMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17630 288 WLKDKLARFKLPKRIYPVPELPRTGGGKV 316
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
25-506 |
9.39e-51 |
|
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: 179.95 E-value: 9.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 25 GQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCL 104
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 105 vdgaraslitaiqaepqpladiqwlstasategldcfdellaqaapCGDEHgrpaphALAEILYTSGTTGQPKGCLHSHA 184
Cdd:cd05914 85 ----------------------------------------------VSDED------DVALINYTSGTTGNSKGVMLTYR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 185 NVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREyAPREFLETLAQERISFTFGAPIAF--- 261
Cdd:cd05914 113 NIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDK-IPSAKIIALAFAQVTPTLGVPVPLvie 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 262 -LAPLSVVPDVASYDF--------------------------SAMRLWAYGGGPLGADMARKLAQVyrSDRFMQVYGMTE 314
Cdd:cd05914 192 kIFKMDIIPKLTLKKFkfklakkinnrkirklafkkvheafgGNIKEFVIGGAKINPDVEEFLRTI--GFPYTIGYGMTE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 315 SGPLGTVLYPEEavVKAGSIGRcAIPGVELEVRRQDgslcSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGD 394
Cdd:cd05914 270 TAPIISYSPPNR--IRLGSAGK-VIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 395 LARVDEDGYLYIVDRLKDMIVTG-GENVYSKEVE-------DVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLV 466
Cdd:cd05914 343 LGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEakinnmpFVLESLVVVQEKKLVALAYIDPDFLDVKALKQRNIIDAI 422
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502603069 467 HEDLRQFMETRLARY-KIPRIFEVRDTLPRTATGKLLKHML 506
Cdd:cd05914 423 KWEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
3-508 |
2.26e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 180.19 E-value: 2.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 3 NFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPI 82
Cdd:PRK13383 36 NPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 83 NHKLQAPEVSYILRHSGARLCLVDGARASLItaiqaepqpladiqwlstASATEGLDCFDELLAQAAPCGdehGRPAPHA 162
Cdd:PRK13383 116 STEFRSDALAAALRAHHISTVVADNEFAERI------------------AGADDAVAVIDPATAGAEESG---GRPAVAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 LAEI-LYTSGTTGQPKGC-----LHSHANVFhaaLCAAAATSLAPTERTLIAMPIWHSSPLNNWFLgTLLMGGTAVLMRE 236
Cdd:PRK13383 175 PGRIvLLTSGTTGKPKGVprapqLRSAVGVW---VTILDRTRLRTGSRISVAMPMFHGLGLGMLML-TIALGGTVLTHRH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 237 YAPREFLETLAQERISFTFGAPIAFLAPLSVVPDV-ASYDFSAMRLWAYGGGPLGADMARKLAQVYrSDRFMQVYGMTES 315
Cdd:PRK13383 251 FDAEAALAQASLHRADAFTAVPVVLARILELPPRVrARNPLPQLRVVMSSGDRLDPTLGQRFMDTY-GDILYNGYGSTEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 316 GpLGTVLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNreATAAVLDdqGWYRSGDL 395
Cdd:PRK13383 330 G-IGALATPADLRDAPETVGK-PVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG--GGKAVVD--GMTSTGDM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 396 ARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFME 475
Cdd:PRK13383 404 GYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLK 483
|
490 500 510
....*....|....*....|....*....|...
gi 502603069 476 TRLARYKIPRIFEVRDTLPRTATGKLLKHMLRG 508
Cdd:PRK13383 484 DRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
7-501 |
7.14e-50 |
|
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: 178.24 E-value: 7.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGARASLITAiqaepqpladiqwlstasATEGLDCFDELLAqAAPCGDEHGRPAPHALAEI 166
Cdd:cd17646 83 PADRLAYMLADAGPAVVLTTADLAARLPA------------------GGDVALLGDEALA-APPATPPLVPPRPDNLAYV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIwhSSPLNNW-FLGTLLMGGTAVLMR---EYAPREF 242
Cdd:cd17646 144 IYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL--SFDVSVWeLFWPLVAGARLVVARpggHRDPAYL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISFTFGAPiAFLAPLSVVPDVASYDfsAMRLWAYGGGPLGADMARKLAQVYrSDRFMQVYGMTESGpLGTVL 322
Cdd:cd17646 222 AALIREHGVTTCHFVP-SMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALP-GAELHNLYGPTEAA-IDVTH 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 323 YPEEAVVKAGS--IGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVL----DDQG--WYRSGD 394
Cdd:cd17646 297 WPVRGPAETPSvpIGR-PVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvpdpFGPGsrMYRTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 395 LARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHED-LRQF 473
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAaLRAH 455
|
490 500
....*....|....*....|....*...
gi 502603069 474 METRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17646 456 LAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
166-500 |
2.68e-49 |
|
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: 173.34 E-value: 2.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTE--------------RTLIAMPIWHSSPLNNWFlGTLLMGGTA 231
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPsedahkaaaaaagtVMFPAPPLMHGTGSWTAF-GGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 232 VLMR-EYAPREFLETLAQERISFTFGAPIAFLAPL-SVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQV 309
Cdd:cd05924 87 VLPDdRFDPEEVWRTIEKHKVTSMTIVGDAMARPLiDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLVDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 310 YGMTESGPLGTVlYPEEAVVKAGSIGRcaiPGVELEVRRQDGSLC--SSGEVGEIClRSAAMMQGYLDNREATAA---VL 384
Cdd:cd05924 167 FGSSETGFTGSG-HSAGSGPETGPFTR---ANPDTVVLDDDGRVVppGSGGVGWIA-RRGHIPLGYYGDEAKTAEtfpEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 385 DDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKT 464
Cdd:cd05924 242 DGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAG 321
|
330 340 350
....*....|....*....|....*....|....*.
gi 502603069 465 LVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGK 500
Cdd:cd05924 322 VDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
39-507 |
7.09e-49 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 177.13 E-value: 7.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 39 RAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGARASLITAI-- 116
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVlh 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 117 -----QAEPQP----LADIQWLSTASATEgLDcFDELLaqaapcgdEHGRPAPHALAEIL------------YTSGTTGQ 175
Cdd:PLN03102 131 llsseDSNLNLpvifIHEIDFPKRPSSEE-LD-YECLI--------QRGEPTPSLVARMFriqdehdpislnYTSGTTAD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 176 PKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSsplNNWFL--GTLLMGGTAVLMREYAPREFLETLAQERISF 253
Cdd:PLN03102 201 PKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHC---NGWTFtwGTAARGGTSVCMRHVTAPEIYKNIEMHNVTH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 254 TFGAPIAFLAPLSVVPDVASYDFSAMRLWAyGGGPLGADMARKLAQVyrSDRFMQVYGMTESgpLGTVLY---------- 323
Cdd:PLN03102 278 MCCVPTVFNILLKGNSLDLSPRSGPVHVLT-GGSPPPAALVKKVQRL--GFQVMHAYGLTEA--TGPVLFcewqdewnrl 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 324 PEEAVVKAGS---IGRCAIPGVELEVRRQDGSLCSSGE-VGEICLRSAAMMQGYLDNREATAAVLDdQGWYRSGDLARVD 399
Cdd:PLN03102 353 PENQQMELKArqgVSILGLADVDVKNKETQESVPRDGKtMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIH 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 400 EDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHE----------D 469
Cdd:PLN03102 432 PDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDrvdklvtrerD 511
|
490 500 510
....*....|....*....|....*....|....*...
gi 502603069 470 LRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PLN03102 512 LIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
7-507 |
8.84e-49 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 176.96 E-value: 8.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PLN02479 25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDG-----ARASL-ITAIQAE---PQPL--------ADIQWLSTASATEGLDcFDELLAQA- 148
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQefftlAEEALkILAEKKKssfKPPLlivigdptCDPKSLQYALGKGAIE-YEKFLETGd 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 149 -----APCGDEHGRPAphalaeILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSsplNNW-FL 222
Cdd:PLN02479 184 pefawKPPADEWQSIA------LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHC---NGWcFT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 223 GTL-LMGGTAVLMREYAPREFLETLAQERISFTFGAPIAF-----------LAPLSVVPDVASYdfsamrlwayGGGPLG 290
Cdd:PLN02479 255 WTLaALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLntivnapksetILPLPRVVHVMTA----------GAAPPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 291 ADMArklAQVYRSDRFMQVYGMTES-GPlGTV---------LYPEEavvKAGSIGRCAIPGVELE----VRRQDGS-LCS 355
Cdd:PLN02479 325 SVLF---AMSEKGFRVTHTYGLSETyGP-STVcawkpewdsLPPEE---QARLNARQGVRYIGLEgldvVDTKTMKpVPA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 356 SGE-VGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHS 434
Cdd:PLN02479 398 DGKtMGEIVMRGNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHP 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502603069 435 DVQDVAVIGRPHPEWGETVVAVLTLKPG-----KTLVHEDLRQFMETRLARYKIPRIFeVRDTLPRTATGKLLKHMLR 507
Cdd:PLN02479 477 AVLEASVVARPDERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR 553
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
22-507 |
4.81e-48 |
|
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: 174.39 E-value: 4.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 22 RADG--QDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP----INHKLQAPEVSYiL 95
Cdd:cd05906 32 DADGseEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPltvpPTYDEPNARLRK-L 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RHS----GARLCLVDGARASLITAiQAEPQPLADIQWLSTasategldcfDELLAQAApcgDEHGRPA-PHALAEILYTS 170
Cdd:cd05906 111 RHIwqllGSPVVLTDAELVAEFAG-LETLSGLPGIRVLSI----------EELLDTAA---DHDLPQSrPDDLALLMLTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 171 GTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGG-------TAVLMReyaPREFL 243
Cdd:cd05906 177 GSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqqvhvptEEILAD---PLRWL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 244 ETLAQERISFTFgAPIAFLAPL----SVVPDvASYDFSAMRLWAYGGGPLGADMARKLAQVY-----RSDRFMQVYGMTE 314
Cdd:cd05906 254 DLIDRYRVTITW-APNFAFALLndllEEIED-GTWDLSSLRYLVNAGEAVVAKTIRRLLRLLepyglPPDAIRPAFGMTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 315 --SGPLGTVLYPEEAVVKAG---SIGRCaIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGW 389
Cdd:cd05906 332 tcSGVIYSRSFPTYDHSQALefvSLGRP-IPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 390 YRSGDLARVDeDGYLYIVDRLKDMIVTGGENVYSKEVEDVL-----CTHSDVQDVAVigrpHPEWGETVVAVLTLKPGKT 464
Cdd:cd05906 411 FRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpgVEPSFTAAFAV----RDPGAETEELAIFFVPEYD 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502603069 465 L------VHEDLRQF---METRLARYKIPRifeVRDTLPRTATGKLLKHMLR 507
Cdd:cd05906 486 LqdalseTLRAIRSVvsrEVGVSPAYLIPL---PKEEIPKTSLGKIQRSKLK 534
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
16-501 |
1.16e-47 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 171.71 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYIL 95
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RHSGARLCLVDgaraslitaiQAEPQPLAdiqWLSTASAtegldcfDELLAQAAPCGDEHGRPAPHALAEILYTSGTTGQ 175
Cdd:cd12116 81 EDAEPALVLTD----------DALPDRLP---AGLPVLL-------LALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 176 PKGCLHSHANVFHAALCAAAATSLAPTER----TLIAMPIwhsSPLNnwFLGTLLMGGTAVLMRE---YAPREFLETLAQ 248
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMRERLGLGPGDRllavTTYAFDI---SLLE--LLLPLLAGARVVIAPRetqRDPEALARLIEA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 249 ERISFTFGAPiaflAPLSVVPDVASYDFSAMRLWAyGGGPLGADMARKLAQvyRSDRFMQVYGMTESGPLGTVLYPEEAv 328
Cdd:cd12116 216 HSITVMQATP----ATWRMLLDAGWQGRAGLTALC-GGEALPPDLAARLLS--RVGSLWNLYGPTETTIWSTAARVTAA- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 329 VKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVL-------DDQGWYRSGDLARVDED 401
Cdd:cd12116 288 AGPIPIGR-PLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfagPGSRLYRTGDLVRRRAD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 402 GYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPhPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARY 481
Cdd:cd12116 367 GRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRE-DGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAY 445
|
490 500
....*....|....*....|
gi 502603069 482 KIPRIFEVRDTLPRTATGKL 501
Cdd:cd12116 446 MVPSAFVRLDALPLTANGKL 465
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
26-447 |
3.68e-47 |
|
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: 171.11 E-value: 3.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 26 QDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLV 105
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 106 ----------DGARASLITAIQAEPQPL-ADIQWlstasategldcfDELLAQAAPCGDEHgRPAPHALAEILYTSGTTG 174
Cdd:cd05932 85 gklddwkamaPGVPEGLISISLPPPSAAnCQYQW-------------DDLIAQHPPLEERP-TRFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 175 QPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLmGGTAVLMREyAPREFLETLAQERISFT 254
Cdd:cd05932 151 QPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLY-GGVLVAFAE-SLDTFVEDVQRARPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 255 FGAP------------------------IAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADmarkLAQVYRSD--RFMQ 308
Cdd:cd05932 229 FSVPrlwtkfqqgvqdkipqqklnlllkIPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPA----LLEWYRSLglNILE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 309 VYGMTESGPLGTVLYPEEAvvKAGSIGRcAIPGVELEVrrqdgslcssGEVGEICLRSAAMMQGYLDNREATAAVLDDQG 388
Cdd:cd05932 305 AYGMTENFAYSHLNYPGRD--KIGTVGN-AGPGVEVRI----------SEDGEILVRSPALMMGYYKDPEATAEAFTADG 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502603069 389 WYRSGDLARVDEDGYLYIVDRLKDMIVTG-GENVYSKEVEDVLCTHSDVQDVAVIGR--PHP 447
Cdd:cd05932 372 FLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAP 433
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
3-507 |
7.53e-47 |
|
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: 170.72 E-value: 7.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 3 NFIS-LLDQQART-----RPEKLAL-----RADGQDWSYAALAQAGRRAATVLYEQ-GVRQGDKLGLLCFNTPGFVFALL 70
Cdd:cd05928 6 NFASdVLDQWADKekagkRPPNPALwwvngKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 71 GAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEpQPLADIQWLSTASATEGLDCFDELLAQAAp 150
Cdd:cd05928 86 ACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASE-CPSLKTKLLVSEKSRDGWLNFKELLNEAS- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 151 cgDEH-----GRPAPHAlaeILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAP-------TERTLIAMPIWhSSPLN 218
Cdd:cd05928 164 --TEHhcvetGSQEPMA---IYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTasdimwnTSDTGWIKSAW-SSLFE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 219 NWFLGTLLMggtAVLMREYAPREFLETLAQERISFTFGAPIAFlaPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLA 298
Cdd:cd05928 238 PWIQGACVF---VHHLPRFDPLVILKTLSSYPITTFCGAPTVY--RMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 299 QVYRSDRFmQVYGMTESGPLGTVLYPEEavVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSA-----AMMQGY 373
Cdd:cd05928 313 AQTGLDIY-EGYGQTETGLICANFKGMK--IKPGSMGK-ASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 374 LDNREATAAVLddQG-WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGET 452
Cdd:cd05928 389 VDNPEKTAATI--RGdFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502603069 453 VVAVLTLKPG------KTLVHEdLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05928 467 VKAFVVLAPQflshdpEQLTKE-LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
11-507 |
2.96e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 169.09 E-value: 2.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 11 QARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDK-LGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAP 89
Cdd:PRK07867 12 LPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 90 EVSYILRHSGARLCLVDGARASLITAIqaepqpLADIQWLSTASATegldcFDELLAQAAPCGDEHGRPAPHALAEILYT 169
Cdd:PRK07867 92 ALARDIAHADCQLVLTESAHAELLDGL------DPGVRVINVDSPA-----WADELAAHRDAEPPFRVADPDDLFMLIFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 170 SGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLaqE 249
Cdd:PRK07867 161 SGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDV--R 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 250 RISFTF----GAPIAFLAPLSVVPDVASydfSAMRLwAYGGGPLGADMARklaqvyRSDRF----MQVYGMTE------- 314
Cdd:PRK07867 239 RYGATYanyvGKPLSYVLATPERPDDAD---NPLRI-VYGNEGAPGDIAR------FARRFgcvvVDGFGSTEggvaitr 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 315 -----SGPLGtVLYPEEAVVKAGSIGRCAiPGVelevRRQDGSLCSSGEVGEIC-LRSAAMMQGYLDNREATAAVLDDqG 388
Cdd:PRK07867 309 tpdtpPGALG-PLPPGVAIVDPDTGTECP-PAE----DADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRG-G 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 389 WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHE 468
Cdd:PRK07867 382 VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPD 461
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502603069 469 DLRQFMETR--LARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK07867 462 AFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
8-502 |
7.14e-46 |
|
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: 169.29 E-value: 7.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALRADGQD------WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:cd17634 59 LDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 INHKLQAPEVSYILRHSGARLCLV-DGA---------RASLITAIQAEPQPL----------ADIQWlstasaTEGLDC- 140
Cdd:cd17634 139 IFGGFAPEAVAGRIIDSSSRLLITaDGGvragrsvplKKNVDDALNPNVTSVehvivlkrtgSDIDW------QEGRDLw 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 141 FDELLAQAAPcgdEHgRPAPHALAE---ILYTSGTTGQPKGCLHSH-----------ANVFHAALCAAAATSlapterTL 206
Cdd:cd17634 213 WRDLIAKASP---EH-QPEAMNAEDplfILYTSGTTGKPKGVLHTTggylvyaattmKYVFDYGPGDIYWCT------AD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 207 IAMPIWHSsplnnWFL-GTLLMGGTAVLMREY----APREFLETLAQERISFTFGAPIAFLAPLSVVPD-VASYDFSAMR 280
Cdd:cd17634 283 VGWVTGHS-----YLLyGPLACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDaIEGTDRSSLR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 281 LWAYGGGPLGADMARKLAQVYRSDR--FMQVYGMTESGPLGTVLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGE 358
Cdd:cd17634 358 ILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETGGFMITPLPGAIELKAGSATR-PVFGVQPAVVDNEGHPQPGGT 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 359 VGEICLRSA--AMMQGYL--DNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHS 434
Cdd:cd17634 437 EGNLVITDPwpGQTRTLFgdHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502603069 435 DVQDVAVIGRPHPEWGETVVAVLTLKPGKT---LVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLL 502
Cdd:cd17634 517 KVAEAAVVGIPHAIKGQAPYAYVVLNHGVEpspELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
8-507 |
1.95e-45 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 168.13 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQ 87
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 88 APEVSYILRHSGARLCLVDGARASLITAIQAEPQPlADIQWLSTASATEGLDCFDEL--LAQAAPCGDEHGRPAPHA--L 163
Cdd:PRK08279 123 GAVLAHSLNLVDAKHLIVGEELVEAFEEARADLAR-PPRLWVAGGDTLDDPEGYEDLaaAAAGAPTTNPASRSGVTAkdT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 AEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFL 243
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFW 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 244 ETLAQERISfTFGApIAFL------APLSvvPDVASYdfsAMRLwAYGGGpLGADMARKLAQVYRSDRFMQVYGMTESgp 317
Cdd:PRK08279 282 DDVRRYRAT-AFQY-IGELcryllnQPPK--PTDRDH---RLRL-MIGNG-LRPDIWDEFQQRFGIPRILEFYAASEG-- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 318 lGTVLYPEEAVVkaGSIGRCAIPG------VELE------VRRQDGSL--CSSGEVGEICLR--SAAMMQGYLDNREATA 381
Cdd:PRK08279 351 -NVGFINVFNFD--GTVGRVPLWLahpyaiVKYDvdtgepVRDADGRCikVKPGEVGLLIGRitDRGPFDGYTDPEASEK 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 382 AVLDD---QG--WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEW-GETVVA 455
Cdd:PRK08279 428 KILRDvfkKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTdGRAGMA 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502603069 456 VLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK08279 508 AIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLR 559
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
16-501 |
4.97e-45 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 164.02 E-value: 4.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINhkLQAPE--VSY 93
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPID--PAYPVerIAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 94 ILRHSGARLCLVDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaPHALAEILYTSGTT 173
Cdd:cd17643 79 ILADSGPSLLLTD-----------------------------------------------------PDDLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 174 GQPKGCLHSHANVFHAALCAAAATSLAPTERTLIampiWHSSPLN--NWFL-GTLLMGGTAVLMREY---APREFLETLA 247
Cdd:cd17643 106 GRPKGVVVSHANVLALFAATQRWFGFNEDDVWTL----FHSYAFDfsVWEIwGALLHGGRLVVVPYEvarSPEDFARLLR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 248 QERISFTFGAPIAFLAPLSVVpDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQV--YGMTESGPLGTV--LY 323
Cdd:cd17643 182 DEGVTVLNQTPSAFYQLVEAA-DRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVnmYGITETTVHVTFrpLD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 324 PEEAVVKAGSIGRCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG-----WYRSGDLA 396
Cdd:cd17643 261 AADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfVANPFGgpgsrMYRTGDLA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 397 RVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMET 476
Cdd:cd17643 341 RRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKE 420
|
490 500
....*....|....*....|....*
gi 502603069 477 RLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17643 421 LLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-507 |
1.70e-44 |
|
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: 162.30 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGA 108
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 109 RASLITAiqaepqpladiqwlstasategldcfDELLaqaapcgdehgrpaphalaeILYTSGTTGQPKGCLHSHANVFH 188
Cdd:cd05973 82 NRHKLDS--------------------------DPFV--------------------MMFTSGTTGLPKGVPVPLRALAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 189 AALCAAAATSLAPTERTL-IAMPIWhSSPLNNWFLGTLLMGGTAVLMR-EYAPREFLETLAQERISFTFGAPIAFLAPLS 266
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWnAADPGW-AYGLYYAITGPLALGHPTILLEgGFSVESTWRVIERLGVTNLAGSPTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 267 VVPDVASYDFSAMRLWAYGGGPLGADMAR----KLAQVYRSDrfmqvYGMTEsgpLGTVL---YPEEAVVKAGSIGRcAI 339
Cdd:cd05973 195 AGAEVPARPKGRLRRVSSAGEPLTPEVIRwfdaALGVPIHDH-----YGQTE---LGMVLanhHALEHPVHAGSAGR-AM 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 340 PGVELEVRRQDGSLCSSGEVGEICL---RSAAM-MQGYLDNREATAavldDQGWYRSGDLARVDEDGYLYIVDRLKDMIV 415
Cdd:cd05973 266 PGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVIT 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 416 TGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPG---KTLVHEDLRQFMETRLARYKIPRIFEVRDT 492
Cdd:cd05973 342 MSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGhegTPALADELQLHVKKRLSAHAYPRTIHFVDE 421
|
490
....*....|....*
gi 502603069 493 LPRTATGKLLKHMLR 507
Cdd:cd05973 422 LPKTPSGKIQRFLLR 436
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
44-513 |
2.72e-44 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 164.20 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 44 LYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEPQPL 123
Cdd:PLN02860 49 LLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELQNDRLPS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 124 ADIQWLSTASATEGLDCF------DELLAQAAPCGDEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAAT 197
Cdd:PLN02860 129 LMWQVFLESPSSSVFIFLnsflttEMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 198 SLAPTERTLIAMPIWH----SSPLNNwflgtLLMGGTAVLMREYAPREFLETLAQERISFTFGAPiAFLAPL-SVVPDVA 272
Cdd:PLN02860 209 GYGEDDVYLHTAPLCHigglSSALAM-----LMVGACHVLLPKFDAKAALQAIKQHNVTSMITVP-AMMADLiSLTRKSM 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 273 SYD-FSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTES-------------GPLGTVLYPEEAVVKAGSI---- 334
Cdd:PLN02860 283 TWKvFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhdptLESPKQTLQTVNQTKSSSVhqpq 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 335 GRC---AIPGVELEVrrqdgSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLK 411
Cdd:PLN02860 363 GVCvgkPAPHVELKI-----GLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSN 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 412 DMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPG--------------KTLVHEDLRQFMETR 477
Cdd:PLN02860 438 DRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakknLTLSSETLRHHCREK 517
|
490 500 510
....*....|....*....|....*....|....*...
gi 502603069 478 -LARYKIPRIFEV-RDTLPRTATGKLLKHMLRGSTTSH 513
Cdd:PLN02860 518 nLSRFKIPKLFVQwRKPFPLTTTGKIRRDEVRREVLSH 555
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
11-507 |
8.86e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 159.81 E-value: 8.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 11 QARTRPEKLALRADGQDWSYAA-LAQAGRRAATVLyeqGVRQGDK---LGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK13388 10 RDRAGDDTIAVRYGDRTWTWREvLAEAAARAAALI---ALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGARASLITAIQaepqpLADIQWLSTASATegldcFDELLAQAAPCgDEHGRPAPHALAEI 166
Cdd:PRK13388 87 RGAALAADIRRADCQLLVTDAEHRPLLDGLD-----LPGVRVLDVDTPA-----YAELVAAAGAL-TPHREVDAMDPFML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETL 246
Cdd:PRK13388 156 IFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 247 aqERISFTF----GAPIAFLAPLSVVPDVASydfSAMRLwAYGGGPLGADMA----RKLAQVYRSdrfmqvYGMTESGpl 318
Cdd:PRK13388 236 --RRYGATYfnyvGKPLAYILATPERPDDAD---NPLRV-AFGNEASPRDIAefsrRFGCQVEDG------YGSSEGA-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 319 GTVLYPEEAvvKAGSIGRCAiPGV---------ELEVRR--QDGSLCSSGE-VGEICLRS-AAMMQGYLDNREATAAVLD 385
Cdd:PRK13388 302 VIVVREPGT--PPGSIGRGA-PGVaiynpetltECAVARfdAHGALLNADEaIGELVNTAgAGFFEGYYNNPEATAERMR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 386 DqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL 465
Cdd:PRK13388 379 H-GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATF 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 502603069 466 VHEDLRQFMETR--LARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK13388 458 DPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
25-507 |
5.49e-42 |
|
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: 155.59 E-value: 5.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 25 GQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCL 104
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 105 VDgaRASLItaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaphalaeilYTSGTTGQPKGCLHSHA 184
Cdd:cd05940 81 VD--AALYI------------------------------------------------------YTSGTTGLPKAAIISHR 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 185 NVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQERIS-FTF-GAPIAFL 262
Cdd:cd05940 105 RAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATiFQYiGELCRYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 263 APLSVVPDVASYDFSAMrlwaYGGGpLGADMARKLAQVYRSDRFMQVYGMTEsGPLGTVLYPEeavvKAGSIGRC----- 337
Cdd:cd05940 185 LNQPPKPTERKHKVRMI----FGNG-LRPDIWEEFKERFGVPRIAEFYAATE-GNSGFINFFG----KPGAIGRNpsllr 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 338 -----AIPGVELE----VRRQDGSL--CSSGEVGEICLRSAAM--MQGYLDNREATAAVLDD---QG--WYRSGDLARVD 399
Cdd:cd05940 255 kvaplALVKYDLEsgepIRDAEGRCikVPRGEPGLLISRINPLepFDGYTDPAATEKKILRDvfkKGdaWFNTGDLMRLD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 400 EDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEW-GETVVAVLTLKPGKTLVHEDLRQFMETRL 478
Cdd:cd05940 335 GEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTdGRAGMAAIVLQPNEEFDLSALAAHLEKNL 414
|
490 500
....*....|....*....|....*....
gi 502603069 479 ARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05940 415 PGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
25-507 |
6.85e-42 |
|
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: 156.05 E-value: 6.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 25 GQDWSYAALAQAGRRAATVLY-EQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLC 103
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 104 LVDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaPHALAEILYTSGTTGQPKGCLHSH 183
Cdd:cd05937 83 IVD-----------------------------------------------------PDDPAILIYTSGTTGLPKAAAISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 184 ANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFL-ETLAQERISFTF-GAPIAF 261
Cdd:cd05937 110 RRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWkDVRDSGATIIQYvGELCRY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 262 LapLSVVPdvASYDFSAMRLWAYGGGpLGADMARKLAQVYRSDRFMQVYGMTE---------SGPLGTvlypeEAVVKAG 332
Cdd:cd05937 190 L--LSTPP--SPYDRDHKVRVAWGNG-LRPDIWERFRERFNVPEIGEFYAATEgvfaltnhnVGDFGA-----GAIGHHG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 333 SIGRCAIPGVELEVR--RQDGSL-----------CSSGEVGEICLR----SAAMMQGYLDNREATAA-VLDD---QG--W 389
Cdd:cd05937 260 LIRRWKFENQVVLVKmdPETDDPirdpktgfcvrAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESkLVRDvfrKGdiY 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 390 YRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIG--RPHPEwGETVVAVLTLKPGKTLVH 467
Cdd:cd05937 340 FRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkVPGHD-GRAGCAAITLEESSAVPT 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 502603069 468 E----DLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05937 419 EftksLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
29-443 |
7.13e-42 |
|
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: 155.98 E-value: 7.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGA 108
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEND 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 109 raslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaPHALAEILYTSGTTGQPKGCLHSHANVFH 188
Cdd:cd17640 87 ---------------------------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 189 AALCAAAATSLAPTERTLIAMPIWHSsplnnwflgtllmggtavlmreyAPREFletlaqERISFTFGAPIAFLAPLSVV 268
Cdd:cd17640 116 QIRSLSDIVPPQPGDRFLSILPIWHS-----------------------YERSA------EYFIFACGCSQAYTSIRTLK 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 269 PDVASYDFSAM----RLWA--YGG-------GPLGAdmaRKLAQVYRS------------------DRFMQV-------- 309
Cdd:cd17640 167 DDLKRVKPHYIvsvpRLWEslYSGiqkqvskSSPIK---QFLFLFFLSggifkfgisgggalpphvDTFFEAigievlng 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 310 YGMTESGPLGTVLYPEEAVVkaGSIGRCaIPGVELEVRRQDGS-LCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQG 388
Cdd:cd17640 244 YGLTETSPVVSARRLKCNVR--GSVGRP-LPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDG 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 502603069 389 WYRSGDLARVDEDGYLYIVDRLKDMIV-TGGENVYSKEVEDVLCTHSDVQDVAVIG 443
Cdd:cd17640 321 WFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
7-501 |
7.73e-42 |
|
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: 155.17 E-value: 7.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaPHALAEI 166
Cdd:cd12115 84 PPERLRFILEDAQARLVLTD-----------------------------------------------------PDDLAYV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFlGTLLMGGTAVLMREYAPREFLETL 246
Cdd:cd12115 111 IYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELF-GPLATGGKVVLADNVLALPDLPAA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 247 AQERISFTFGAPIAFLAPLSVVPdvasydfSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPLGTVLYPEE 326
Cdd:cd12115 190 AEVTLINTVPSAAAELLRHDALP-------ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 327 AVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA------VLDDQGWYRSGDLARVDE 400
Cdd:cd12115 263 GASGEVSIGR-PLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAErflpdpFGPGARLYRTGDLVRWRP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 401 DGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLAR 480
Cdd:cd12115 342 DGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPA 421
|
490 500
....*....|....*....|.
gi 502603069 481 YKIPRIFEVRDTLPRTATGKL 501
Cdd:cd12115 422 YMVPSRFVRLDALPLTPNGKI 442
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
6-506 |
3.26e-41 |
|
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: 154.24 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLlCFN-TPGFVFALLGAWRLGAVVVPINH 84
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPL-CFEkSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 85 KLQAPEVSYILRHSGARLCLVDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpAPHALA 164
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVLTS----------------------------------------------------SPSDAA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 165 EILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLiampiwHSSplNNWF-------LGTLLMGGTAVLMREY 237
Cdd:cd05918 110 YVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVL------QFA--SYTFdvsileiFTTLAAGGCLCIPSEE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 238 APREFLETLAQErisftFGAPIAFLAPlSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQ-VyrsdRFMQVYGMTESG 316
Cdd:cd05918 182 DRLNDLAGFINR-----LRVTWAFLTP-SVARLLDPEDVPSLRTLVLGGEALTQSDVDTWADrV----RLINAYGPAECT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 317 pLGTVLYPEEAVVKAGSIGRcAIPGVELEVRRQD-GSLCSSGEVGEICLRSAAMMQGYLDNREATAAV-LDDQGW----- 389
Cdd:cd05918 252 -IAATVSPVVPSTDPRNIGR-PLGATCWVVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAWlkqeg 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 390 -------YRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVL--CTHSDVQDVAVIGRPHP-EWGETVVAVLTL 459
Cdd:cd05918 330 sgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLrqSLPGAKEVVVEVVKPKDgSSSPQLVAFVVL 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502603069 460 KPGKTLVHE-----------------DLRQFMETRLARYKIPRIFEVRDTLPRTATGKL----LKHML 506
Cdd:cd05918 410 DGSSSGSGDgdslflepsdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIdrraLRELA 477
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
16-501 |
8.91e-41 |
|
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: 152.52 E-value: 8.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYIL 95
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RHSGARLclvdgaraslitaiqaepqpladiqwlstasategldcfdeLLAQaapcgdeHGRpaphALAEILYTSGTTGQ 175
Cdd:cd17649 81 EDSGAGL-----------------------------------------LLTH-------HPR----QLAYVIYTSGSTGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 176 PKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGtlLMGGTAVLMRE----YAPREFLETLAQERI 251
Cdd:cd17649 109 PKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPP--LICGACVVLRPdelwASADELAEMVRELGV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 252 SfTFGAPIAFLAPLS-VVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVyrSDRFMQVYGMTESGPLGTVLYPEEAVVK 330
Cdd:cd17649 187 T-VLDLPPAYLQQLAeEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEATVTPLVWKCEAGAAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 331 AGS---IGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG-----WYRSGDLARVDE 400
Cdd:cd17649 264 AGAsmpIGR-PLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 401 DGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEwGETVVAVLTLKPGKTL--VHEDLRQFMETRL 478
Cdd:cd17649 343 DGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAAQpeLRAQLRTALRASL 421
|
490 500
....*....|....*....|...
gi 502603069 479 ARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17649 422 PDYMVPAHLVFLARLPLTPNGKL 444
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
7-507 |
9.61e-41 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 153.99 E-value: 9.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARtrPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGD----KLGllcfNTPGF---VFALLgawRLGavV 79
Cdd:PRK10946 30 ILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDtalvQLG----NVAEFyitFFALL---KLG--V 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 80 VPIN----HklQAPEVSYILRHSGARLCLVDGARA-----SLITAIQAEPQPLADIQWLSTASATEgldcFDELLAQAAp 150
Cdd:PRK10946 99 APVNalfsH--QRSELNAYASQIEPALLIADRQHAlfsddDFLNTLVAEHSSLRVVLLLNDDGEHS----LDDAINHPA- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 151 cgdEHGRPAPHALAEILY---TSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNN-WFLGTLL 226
Cdd:PRK10946 172 ---EDFTATPSPADEVAFfqlSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSpGALGVFL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 227 MGGTAVLMREYAPREFLETLAQERISFTFGAPIAFLAPLSVVPDVAS-YDFSAMRLWAYGGGPLGADMARKLAQVYrSDR 305
Cdd:PRK10946 249 AGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSrAQLASLKLLQVGGARLSETLARRIPAEL-GCQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 306 FMQVYGMTEsgplGTVLY-----PEEAVVkaGSIGRCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREAT 380
Cdd:PRK10946 328 LQQVFGMAE----GLVNYtrlddSDERIF--TTQGRPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 381 AAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVA-VLTL 459
Cdd:PRK10946 402 ASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAfLVVK 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502603069 460 KPGKTLVhedLRQF-METRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK10946 482 EPLKAVQ---LRRFlREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
2-507 |
1.06e-40 |
|
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: 154.96 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 2 MNFI-SLLDQQARTRPEKLALRADGQD-----WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRL 75
Cdd:cd05968 60 MNIVeQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 76 GAVVVPINHKLQAPEVSYILRHSGARLCLV-DG--ARASLItaiqaEPQPLADIQWLSTAS---------------ATEG 137
Cdd:cd05968 140 GGIVVPIFSGFGKEAAATRLQDAEAKALITaDGftRRGREV-----NLKEEADKACAQCPTvekvvvvrhlgndftPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 138 LDCFDELLAQAAPCGDEhgRPAPHALAEILYTSGTTGQPKGCLHSHANV-FHAALCAAAATSLAPTERTLIAMPI-WHSS 215
Cdd:cd05968 215 RDLSYDEEKETAGDGAE--RTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLgWMMG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 216 PlnnWFL-GTLLMGGTAVLMREY----APREFLETLAQERISFTFGAP--IAFLAPLSVVPdVASYDFSAMRLWAYGGGP 288
Cdd:cd05968 293 P---WLIfGGLILGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPtlIRALKPRGDAP-VNAHDLSSLRVLGSTGEP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 289 LGADMARKLAQVYRSDR--FMQVYGMTE--SGPLGTVLYPEeavVKAGSIGrCAIPGVELEVRRQDGSLcSSGEVGEICL 364
Cdd:cd05968 369 WNPEPWNWLFETVGKGRnpIINYSGGTEisGGILGNVLIKP---IKPSSFN-GPVPGMKADVLDESGKP-ARPEVGELVL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 365 RSA--AMMQGYL--DNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVA 440
Cdd:cd05968 444 LAPwpGMTRGFWrdEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESA 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 441 VIGRPHPEWGETVVAVLTLKPGKT---LVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05968 524 AIGVPHPVKGEAIVCFVVLKPGVTpteALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
16-503 |
2.15e-40 |
|
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: 152.04 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYIL 95
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RHSGARLCLVDGARASLITAIQAEPQPLADiqwlstasategldcFDELLAQAAPcgdehGRPAPHALAEILYTSGTTGQ 175
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLD---------------ALAAPAPPPP-----VDVAPDDLAYVIFTSGSTGT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 176 PKGCLHSHANVFHAALCAAAATSLAPTERTLIAmpiwhsSPLNnwF-------LGTLLMGGTAVLMREYAPRE---FLET 245
Cdd:cd12114 141 PKGVMISHRAALNTILDINRRFAVGPDDRVLAL------SSLS--FdlsvydiFGALSAGATLVLPDEARRRDpahWAEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQERISFTFGAPIAFLAPLSVVPDvASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTEsGPLGTVLYPE 325
Cdd:cd12114 213 IERHGVTLWNSVPALLEMLLDVLEA-AQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATE-ASIWSIYHPI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 326 EAVVKA-GSI--GRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA----VLDDQGWYRSGDLARV 398
Cdd:cd12114 291 DEVPPDwRSIpyGR-PLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAArfvtHPDGERLYRTGDLGRY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 399 DEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEwGETVVAVLTLKPGKTLVHED-LRQFMETR 477
Cdd:cd12114 370 RPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPDNDGTPIAPDaLRAFLAQT 448
|
490 500
....*....|....*....|....*.
gi 502603069 478 LARYKIPRIFEVRDTLPRTATGKLLK 503
Cdd:cd12114 449 LPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
6-507 |
1.66e-39 |
|
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: 148.61 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHK 85
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 86 LQAPEVSYILRHSGARLCLVDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrPAPHALAE 165
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTT---------------------------------------------------DSPDDLAY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFlGTLLMGGTAVLmREyaPREFLET 245
Cdd:cd17653 110 IIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIF-STLCNGGTLVL-AD--PSDPFAH 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQErISFTFGAPiAFLAPLSvvPDvasyDFSAMRLWAYGGGPLGADMARKLAQvyrSDRFMQVYGMTES--GPLGTVLY 323
Cdd:cd17653 186 VART-VDALMSTP-SILSTLS--PQ----DFPNLKTIFLGGEAVPPSLLDRWSP---GRRLYNAYGPTECtiSSTMTELL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 324 PEEAVVkagsIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATA-AVLDDQGW-----YRSGDLAR 397
Cdd:cd17653 255 PGQPVT----IGK-PIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTAsKFVPDPFWpgsrmYRTGDYGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 398 VDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCT-HSDVQDVAVIGRphpewGETVVAVLTlkPgKTLVHEDLRQFMET 476
Cdd:cd17653 330 WTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIVV-----NGRLVAFVT--P-ETVDVDGLRSELAK 401
|
490 500 510
....*....|....*....|....*....|.
gi 502603069 477 RLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd17653 402 HLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
160-501 |
2.71e-39 |
|
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: 149.02 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 PHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVlmreYAP 239
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV----FHP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 240 -----REFLETLAQERISFTFGAPIaFLAplSVVPDVASYDFSAMRLwAYGGgplGADMARKLAQVYRsDRF----MQVY 310
Cdd:cd05909 222 npldyKKIPELIYDKKATILLGTPT-FLR--GYARAAHPEDFSSLRL-VVAG---AEKLKDTLRQEFQ-EKFgiriLEGY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 311 GMTESGPLGTVLYPEEAvVKAGSIGRcAIPGVELE-VRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGW 389
Cdd:cd05909 294 GTTECSPVISVNTPQSP-NKEGTVGR-PLPGMEVKiVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD-GW 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 390 YRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQ-DVAVIGRPHPEWGETVVAVLTlkpGKTLVHE 468
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLTT---TTDTDPS 447
|
330 340 350
....*....|....*....|....*....|....*
gi 502603069 469 DLRQFMETRLAR--YKIPRIFEVrDTLPRTATGKL 501
Cdd:cd05909 448 SLNDILKNAGISnlAKPSYIHQV-EEIPLLGTGKP 481
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
7-501 |
3.15e-39 |
|
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: 149.02 E-value: 3.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGAraslitaiqaEPQPLADIQwlsTASATEGLDCFDELLAQAAPCGDehgrpaPHALAEI 166
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSH----------LQPPIAFIG---LIDLLDEDTIYHEESENLEPVSK------SDDLAYV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLgTLLMGGTAVLMREYA---PREFL 243
Cdd:cd17655 143 IYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFA-SLLSGNTLYIVRKETvldGQALT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 244 ETLAQERISFTFGAPiaflAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDR-FMQVYGMTESgPLGTVL 322
Cdd:cd17655 222 QYIRQNRITIIDLTP----AHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTET-TVDASI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 323 YP-EEAVVKAGS--IGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATA-AVLDD-----QGWYRSG 393
Cdd:cd17655 297 YQyEPETDQQVSvpIGK-PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAeKFVDDpfvpgERMYRTG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 394 DLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKpgKTLVHEDLRQF 473
Cdd:cd17655 376 DLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSE--KELPVAQLREF 453
|
490 500
....*....|....*....|....*...
gi 502603069 474 METRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17655 454 LARELPDYMIPSYFIKLDEIPLTPNGKV 481
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
10-509 |
1.71e-38 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 147.85 E-value: 1.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 10 QQARTRPEKLALR-ADG-QDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQ 87
Cdd:PRK05857 22 EQARQQPEAIALRrCDGtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 88 APEVSyilrhsgaRLCLVDGARASLIT---AIQAE--PQPLADIQWLsTASATEGLDCFDELLAQAAPCGdEHGRPAPHA 162
Cdd:PRK05857 102 IAAIE--------RFCQITDPAAALVApgsKMASSavPEALHSIPVI-AVDIAAVTRESEHSLDAASLAG-NADQGSEDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 LAEIlYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPT----ERTLIAMPIWHSSPLNnWFLGTLLMGGTAVLMREYA 238
Cdd:PRK05857 172 LAMI-FTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVTwvvgETTYSPLPATHIGGLW-WILTCLMHGGLCVTGGENT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 239 PrEFLETLAQERISFTFGAPiAFLAPLSVVPDVASYDFSAMRLWAYGGG-PLGADMARKLAQVYRSdrfMQVYGMTESGP 317
Cdd:PRK05857 250 T-SLLEILTTNAVATTCLVP-TLLSKLVSELKSANATVPSLRLVGYGGSrAIAADVRFIEATGVRT---AQVYGLSETGC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 318 LGTVLYPEE---AVVKAGSIGRcAIPGVELEVRRQDGS------LCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqG 388
Cdd:PRK05857 325 TALCLPTDDgsiVKIEAGAVGR-PYPGVDVYLAATDGIgptapgAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID-G 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 389 WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETV-VAVLtlkPGKTLVH 467
Cdd:PRK05857 403 WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVgLAVV---ASAELDE 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502603069 468 EDLRQFMETRLARYK-------IPRIFEVRDTLPRTATGKLLKHMLRGS 509
Cdd:PRK05857 480 SAARALKHTIAARFRresepmaRPSTIVIVTDIPRTQSGKVMRASLAAA 528
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-506 |
2.04e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 150.88 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDgarasliTAIQAEPQPLADIQWLStasategLDCFDELlaQAAPCGDEHGRPAPHALAEI 166
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLTQ-------RHLLERLPLPAGVARLP-------LDRDAEW--ADYPDTAPAVQLAGENLAYV 2151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFlgTLLMGGTAVLMREYAPREFLETL 246
Cdd:PRK12316 2152 IYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWF--HPLLNGARVLIRDDELWDPEQLY 2229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 247 AQ-ERISFTFGA-PIAFLAPLSVVPDVASYDfSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTES--GPLGTVL 322
Cdd:PRK12316 2230 DEmERHGVTILDfPPVYLQQLAEHAERDGRP-PAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAvvTPLLWKC 2308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 323 YPEEAVVKAGS-IGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG-----WYRSGD 394
Cdd:PRK12316 2309 RPQDPCGAAYVpIGR-ALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAErfVPDPFSasgerLYRTGD 2387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 395 LARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEwGETVVAVLTLKPGKTLVHEDLRQFM 474
Cdd:PRK12316 2388 LARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVVPDDAAEDLLAELRAWL 2466
|
490 500 510
....*....|....*....|....*....|..
gi 502603069 475 ETRLARYKIPRIFEVRDTLPRTATGKLLKHML 506
Cdd:PRK12316 2467 AARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
39-510 |
3.17e-38 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 148.64 E-value: 3.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 39 RAATVLYEQGVRQGDKLgLLCF-NTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGaraslitaiq 117
Cdd:PRK06060 42 RLGEVLRNRGLSSGDRV-LLCLpDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD---------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 118 aepqPLADiqWLSTASATEGLDCFDELlAQAAPCGDEHGRPAPHALAEilYTSGTTGQPKGCLHSHANVF-HAALCAAAA 196
Cdd:PRK06060 111 ----ALRD--RFQPSRVAEAAELMSEA-ARVAPGGYEPMGGDALAYAT--YTSGTTGPPKAAIHRHADPLtFVDAMCRKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 197 TSLAPTERTLIAMPIWHSSPLNN--WFlgTLLMGGTAVLMREYAPREFLETL-AQERISFTFGAPiAFLAplSVVPDVAS 273
Cdd:PRK06060 182 LRLTPEDTGLCSARMYFAYGLGNsvWF--PLATGGSAVINSAPVTPEAAAILsARFGPSVLYGVP-NFFA--RVIDSCSP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 274 YDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPlgTVLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSL 353
Cdd:PRK06060 257 DSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQ--TFVSNRVDEWRLGTLGR-VLPPYEIRVVAPDGTT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 354 CSSGEVGEICLRSAAMMQGYLDNREAtaaVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTH 433
Cdd:PRK06060 334 AGPGVEGDLWVRGPAIAKGYWNRPDS---PVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIED 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 434 SDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL---VHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLRGST 510
Cdd:PRK06060 411 EAVAEAAVVAVRESTGASTLQAFLVATSGATIdgsVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQS 490
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
164-501 |
1.46e-37 |
|
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: 141.24 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 AEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERT-LIAMPIWHSSPLNnWFLGTLLMGGTAVLMREYAP-RE 241
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVtYLPLPATHIGGLW-WILTCLIHGGLCVTGGENTTyKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 242 FLETLAQERISFTFGAPIAFLAPLSVVPDVASYdFSAMRLWAYGGG-PLGADMArkLAQVYRSDRFMQVYGMTESGPLgT 320
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANAT-VPSLRLIGYGGSrAIAADVR--FIEATGLTNTAQVYGLSETGTA-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 321 VLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDE 400
Cdd:cd17635 159 CLPTDDDSIEINAVGR-PYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLGERRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 401 DGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL-VHEDLRQFMETRLA 479
Cdd:cd17635 237 DGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDEnAIRALKHTIRRELE 316
|
330 340
....*....|....*....|..
gi 502603069 480 RYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17635 317 PYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
6-501 |
4.70e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 146.46 E-value: 4.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHK 85
Cdd:PRK12467 516 QLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 86 LQAPEVSYILRHSGARLCLVDGARASLItaiqaePQPlADIQWLstasategldCFDELLAQAAPCGDEHGRPA--PHAL 163
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQL------PVP-AGLRSL----------CLDEPADLLCGYSGHNPEVAldPDNL 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 AEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIwhSSPLNNWFLGTLLMGGTAVLMREYA----P 239
Cdd:PRK12467 659 AYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTF--AFDLGVTELFGALASGATLHLLPPDcardA 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 240 REFLETLAQERISFTFGAPIAFLAPLSvvpDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESgPLG 319
Cdd:PRK12467 737 EAFAALMADQGVTVLKIVPSHLQALLQ---ASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTET-TVG 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 320 TVLYP---EEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG-----W 389
Cdd:PRK12467 813 VSTYElsdEERDFGNVPIGQ-PLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAErfVPDPFGadggrL 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 390 YRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVH-- 467
Cdd:PRK12467 892 YRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHqa 971
|
490 500 510
....*....|....*....|....*....|....*.
gi 502603069 468 --EDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK12467 972 trDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
25-506 |
7.85e-37 |
|
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: 142.82 E-value: 7.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 25 GQDWSYAALAQAGRRAATVLYEQ-GVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLC 103
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 104 LVDgarASLITAIQAEPQPLAD----IQWLSTASATEGLDCFDELLAQA---APCGDEHGRPAPHALAEILYTSGTTGQP 176
Cdd:cd05938 83 VVA---PELQEAVEEVLPALRAdgvsVWYLSHTSNTEGVISLLDKVDAAsdePVPASLRAHVTIKSPALYIYTSGTTGLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 177 KGCLHSHANVFHAALCAAAATSLApTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLAQERIS-FTF 255
Cdd:cd05938 160 KAARISHLRVLQCSGFLSLCGVTA-DDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTvIQY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 256 GAPIafLAPLSVVPDVASYDFSAMRLwAYGGGpLGADMARKLAQVYRSDRFMQVYGMTEsGPLGTVLYPEE--AVVKAGS 333
Cdd:cd05938 239 IGEL--LRYLCNQPQSPNDRDHKVRL-AIGNG-LRADVWREFLRRFGPIRIREFYGSTE-GNIGFFNYTGKigAVGRVSY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 334 IGRCAIP------GVELE--VRRQDGsLC---SSGEVGE-IC-LRSAAMMQGYLDNREATA-AVLDD---QG--WYRSGD 394
Cdd:cd05938 314 LYKLLFPfelikfDVEKEepVRDAQG-FCipvAKGEPGLlVAkITQQSPFLGYAGDKEQTEkKLLRDvfkKGdvYFNTGD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 395 LARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEW-GETVVAVLTLKPGKTLVHEDLRQF 473
Cdd:cd05938 393 LLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHeGRIGMAAVKLKPGHEFDGKKLYQH 472
|
490 500 510
....*....|....*....|....*....|...
gi 502603069 474 METRLARYKIPRIFEVRDTLPRTATGKLLKHML 506
Cdd:cd05938 473 VREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
26-428 |
9.20e-37 |
|
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: 143.65 E-value: 9.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 26 QDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLV 105
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 106 DGAR-ASLITAIQAEPQPL-ADIQWLSTASATE-GLDCFDELLAQAAPCGDEH-----GRPAPHALAEILYTSGTTGQPK 177
Cdd:cd05933 87 ENQKqLQKILQIQDKLPHLkAIIQYKEPLKEKEpNLYSWDEFMELGRSIPDEQldaiiSSQKPNQCCTLIYTSGTTGMPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 178 GCLHSHAN-VFHAALCAAAATSLAPTER--TLIA-MPIWH--SSPLNNWFlgTLLMGGTAVLMREYAPREFL-ETLAQER 250
Cdd:cd05933 167 GVMLSHDNiTWTAKAASQHMDLRPATVGqeSVVSyLPLSHiaAQILDIWL--PIKVGGQVYFAQPDALKGTLvKTLREVR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 251 ISFTFGAPIAFLAPLSVVPDVASyDFSAMR----LWAYG--------------GGPLGADMARKLaqVYRSDR------- 305
Cdd:cd05933 245 PTAFMGVPRVWEKIQEKMKAVGA-KSGTLKrkiaSWAKGvgletnlklmggesPSPLFYRLAKKL--VFKKVRkalgldr 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 306 -------------------------FMQVYGMTESGPLGTVLYPEEavVKAGSIGRcAIPGVELEVRRQDgslcSSGeVG 360
Cdd:cd05933 322 cqkfftgaapisretlefflslnipIMELYGMSETSGPHTISNPQA--YRLLSCGK-ALPGCKTKIHNPD----ADG-IG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502603069 361 EICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVT-GGENVYSKEVED 428
Cdd:cd05933 394 EICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENVPPVPIED 462
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
31-507 |
1.36e-35 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 139.92 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 31 AALAQAGRRaatvlyEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGARA 110
Cdd:PRK05620 49 AALAHALHD------ELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 111 SLITAIQAEPQPLADIQWLSTASAT-------EGLDCFD---ELLAQAA----PCGDEHgrpaphALAEILYTSGTTGQP 176
Cdd:PRK05620 123 EQLGEILKECPCVRAVVFIGPSDADsaaahmpEGIKVYSyeaLLDGRSTvydwPELDET------TAAAICYSTGTTGAP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 177 KGCLHSHANVFHAALCAAAATSLAPTERT--LIAMPIWH----SSPLNNWFLGT-LLMGGTAVlmreyAPREFLETLAQE 249
Cdd:PRK05620 197 KGVVYSHRSLYLQSLSLRTTDSLAVTHGEsfLCCVPIYHvlswGVPLAAFMSGTpLVFPGPDL-----SAPTLAKIIATA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 250 RISFTFGAPIAFLAPLSVVPDVASYDFSAMRLWAyGGGPLGADMARKLAQVYRSDrFMQVYGMTESGPLGTVLYPEEAVV 329
Cdd:PRK05620 272 MPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYV-GGSAVPPILIKAWEERYGVD-VVHVWGMTETSPVGTVARPPSGVS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 330 KAG------SIGRcaIPgVELEVR-RQDGSLCSSGE--VGEICLRSAAMMQGYL----DNREATAAVLDDQ--------- 387
Cdd:PRK05620 350 GEArwayrvSQGR--FP-ASLEYRiVNDGQVMESTDrnEGEIQVRGNWVTASYYhsptEEGGGAASTFRGEdvedandrf 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 388 ---GWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKT 464
Cdd:PRK05620 427 tadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 502603069 465 LVHE---DLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK05620 507 PTREtaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
8-507 |
1.58e-35 |
|
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: 140.14 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQART-RPEKLALRADG------QDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVV 80
Cdd:cd05967 56 LDRHVEAgRGDQIALIYDSpvtgteRTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 81 PINHKLQAPEVSYILRHSGARL-----CLVDGARAS-----LITAI-QAEPQPLADIQW----LSTASATEGLDC-FDEL 144
Cdd:cd05967 136 VVFGGFAAKELASRIDDAKPKLivtasCGIEPGKVVpykplLDKALeLSGHKPHHVLVLnrpqVPADLTKPGRDLdWSEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 145 LAQAAPCGdehgrPAPHALAE---ILYTSGTTGQPKGCLHS---HANVFHAalcaaaatslapTERTLIAMP----IWHS 214
Cdd:cd05967 216 LAKAEPVD-----CVPVAATDplyILYTSGTTGKPKGVVRDnggHAVALNW------------SMRNIYGIKpgdvWWAA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 215 SPLnNWFLG-------TLLMGGTAVL-----MREYAPREFLETLAQERISFTFGAPIAFLAPLSVVPD---VASYDFSAM 279
Cdd:cd05967 279 SDV-GWVVGhsyivygPLLHGATTVLyegkpVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDgkyIKKYDLSSL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 280 RLWAYGGGPLGADM---ARKLAQVYRSDRFMQvygmTESG------PLGTVLYPeeavVKAGSIGRcAIPGVELEVRRQD 350
Cdd:cd05967 358 RTLFLAGERLDPPTlewAENTLGVPVIDHWWQ----TETGwpitanPVGLEPLP----IKAGSPGK-PVPGYQVQVLDED 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 351 GSLCSSGEVGEICLR---SAAMMQGYLDNREA--TAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKE 425
Cdd:cd05967 429 GEPVGPNELGNIVIKlplPPGCLLTLWKNDERfkKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGE 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 426 VEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMeTRLARYKI-----PRIFEVRDTLPRTATGK 500
Cdd:cd05967 509 MEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKEL-VALVREQIgpvaaFRLVIFVKRLPKTRSGK 587
|
....*..
gi 502603069 501 LLKHMLR 507
Cdd:cd05967 588 ILRRTLR 594
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
7-506 |
2.22e-35 |
|
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: 137.30 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaPHALAEI 166
Cdd:cd17645 83 PGERIAYMLADSSAKILLTN-----------------------------------------------------PDDLAYV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIwhSSPLNNWFLGTLLMGGTAVLMREYAPREFLETL 246
Cdd:cd17645 110 IYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASF--SFDASAWEIFPHLTAGAALHVVPSERRLDLDAL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 247 aqERISFTFGAPIAFLaPLSVVPDVASYDFSAMRLWAYGGGPLGAdMARKLAQVYRSdrfmqvYGMTESGPLGTV--LYP 324
Cdd:cd17645 188 --NDYFNQEGITISFL-PTGAAEQFMQLDNQSLRVLLTGGDKLKK-IERKGYKLVNN------YGPTENTVVATSfeIDK 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 325 EEAVVkagSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG----WYRSGDLARV 398
Cdd:cd17645 258 PYANI---PIGK-PIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEkfIVHPFVpgerMYRTGDLAKF 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 399 DEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTlkPGKTLVHEDLRQFMETRL 478
Cdd:cd17645 334 LPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEELREWLKNDL 411
|
490 500
....*....|....*....|....*...
gi 502603069 479 ARYKIPRIFEVRDTLPRTATGKLLKHML 506
Cdd:cd17645 412 PDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
39-507 |
3.14e-35 |
|
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: 137.95 E-value: 3.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 39 RAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDgarASLITAIQA 118
Cdd:cd05915 36 RLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD---PNLLPLVEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 119 EPQPLADIqwlsTASATE--GLDCFDELLAQAAPcGDEHGRPA----PHALAeilYTSGTTGQPKGCLHSHANVF--HAA 190
Cdd:cd05915 113 IRGELKTV----QHFVVMdeKAPEGYLAYEEALG-EEADPVRVperaACGMA---YTTGTTGLPKGVVYSHRALVlhSLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 191 LCAAAATSLAPTERTLIAMPIWHSSplnNW-FLGTLL-MGGTAVLMREYAPREFL-ETLAQERISfTFGAPIAFLAPLSV 267
Cdd:cd05915 185 ASLVDGTALSEKDVVLPVVPMFHVN---AWcLPYAATlVGAKQVLPGPRLDPASLvELFDGEGVT-FTAGVPTVWLALAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 268 VPDVASYDFSaMRLWAYGGGPLGADMARKLAQVYRSdRFMQVYGMTESGPLGTV--------LYPEEAVVKAGSigRCAI 339
Cdd:cd05915 261 YLESTGHRLK-TLRRLVVGGSAAPRSLIARFERMGV-EVRQGYGLTETSPVVVQnfvkshleSLSEEEKLTLKA--KTGL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 340 PGVELEVRRQDGSLCSSGEVGE----ICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIV 415
Cdd:cd05915 337 PIPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 416 TGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLvHEDLRQFMETRLARYK-IPRIFEVRDTLP 494
Cdd:cd05915 417 SGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPT-PEELNEHLLKAGFAKWqLPDAYVFAEEIP 495
|
490
....*....|...
gi 502603069 495 RTATGKLLKHMLR 507
Cdd:cd05915 496 RTSAGKFLKRALR 508
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
16-501 |
6.76e-35 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 135.84 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYIL 95
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RHSGARLclvdgaraslitaiqaepqpladiqwlstasategldcfdeLLAQAApcgdehgrpaphALAEILYTSGTTGQ 175
Cdd:cd17652 81 ADARPAL-----------------------------------------LLTTPD------------NLAYVIYTSGSTGR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 176 PKGCLHSHANVFHAALCAAAATSLAPTERTL-IAMPIWHSSPLNnwFLGTLLMGGTAVLMREY---APREFLETLAQERI 251
Cdd:cd17652 108 PKGVVVTHRGLANLAAAQIAAFDVGPGSRVLqFASPSFDASVWE--LLMALLAGATLVLAPAEellPGEPLADLLREHRI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 252 SFTFGAPIAflapLSVVPDVasyDFSAMRLWAYGGGPLGADMARKLAqvyRSDRFMQVYGMTESGPLGTV--LYPEEAVV 329
Cdd:cd17652 186 THVTLPPAA----LAALPPD---DLPDLRTLVVAGEACPAELVDRWA---PGRRMINAYGPTETTVCATMagPLPGGGVP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 330 kagSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG-----WYRSGDLARVDEDG 402
Cdd:cd17652 256 ---PIGR-PVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAErfVADPFGapgsrMYRTGDLARWRADG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 403 YLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYK 482
Cdd:cd17652 332 QLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYM 411
|
490
....*....|....*....
gi 502603069 483 IPRIFEVRDTLPRTATGKL 501
Cdd:cd17652 412 VPAAFVVLDALPLTPNGKL 430
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
8-507 |
1.24e-34 |
|
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: 137.31 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALRADGQD------WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAV--V 79
Cdd:cd05966 59 LDRHLKERGDKVAIIWEGDEpdqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVhsV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 80 V-----------PINHklqapevsyilrhSGARLCL-VDGA--RASLI-------TAIQAEPQPLADIQWLST---ASAT 135
Cdd:cd05966 139 VfagfsaesladRIND-------------AQCKLVItADGGyrGGKVIplkeivdEALEKCPSVEKVLVVKRTggeVPMT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 136 EGLD-CFDELLAQAAP-CgdehgrpAPHAL-AE----ILYTSGTTGQPKGCLHSHA-----------NVF--Haalcaaa 195
Cdd:cd05966 206 EGRDlWWHDLMAKQSPeC-------EPEWMdSEdplfILYTSGSTGKPKGVVHTTGgyllyaattfkYVFdyH------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 196 atslaPTERTLIAMPI-W---HS----SPLNNwflgtllmgGTAVLMREYAPR-----EFLETLAQERISFTFGAPIAFL 262
Cdd:cd05966 272 -----PDDIYWCTADIgWitgHSyivyGPLAN---------GATTVMFEGTPTypdpgRYWDIVEKHKVTIFYTAPTAIR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 263 APLSVVPD-VASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDR--FMQVYGMTESG-----PLgtvlyPEEAVVKAGSI 334
Cdd:cd05966 338 ALMKFGDEwVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERcpIVDTWWQTETGgimitPL-----PGATPLKPGSA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 335 GRcAIPGVELEVRRQDGSLCSSGEVGEICLRSA--AMMQG-YLDN-REATAAVLDDQGWYRSGDLARVDEDGYLYIVDRL 410
Cdd:cd05966 413 TR-PFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTiYGDHeRYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRV 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 411 KDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHE---DLRQFMETRLARYKIPRIF 487
Cdd:cd05966 492 DDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKI 571
|
570 580
....*....|....*....|
gi 502603069 488 EVRDTLPRTATGKLLKHMLR 507
Cdd:cd05966 572 QFVPGLPKTRSGKIMRRILR 591
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
310-501 |
1.09e-33 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 132.81 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 310 YGMTESGPLGTVLYPEEAVVKAGSIGRcAIPGVELEVRRQDgslcssgeVGEICLRSAAMMQGYLDNreataaVLDDQGW 389
Cdd:PRK07445 261 YGMTETASQIATLKPDDFLAGNNSSGQ-VLPHAQITIPANQ--------TGNITIQAQSLALGYYPQ------ILDSQGI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 390 YRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVhED 469
Cdd:PRK07445 326 FETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISL-EE 404
|
170 180 190
....*....|....*....|....*....|..
gi 502603069 470 LRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK07445 405 LKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKI 436
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
12-484 |
1.19e-33 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 132.69 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 12 ARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEV 91
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 92 SYILRHSGARLCLVDGAraslitaiQAEPQPLADIQWLSTASATEglDCFDellaqaapcgdehgrpaPHALAEILYTSG 171
Cdd:PRK09029 93 EELLPSLTLDFALVLEG--------ENTFSALTSLHLQLVEGAHA--VAWQ-----------------PQRLATMTLTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 172 TTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLN---NWflgtLLMGGTAVLmREYAPreFLETLAq 248
Cdd:PRK09029 146 STGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGivwRW----LYAGATLVV-RDKQP--LEQALA- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 249 erisftfGAPIAflaplSVVPDvasydfSAMRLWAYGGGPL--------GADMARKLAQVYRSdrfMQV-----YGMTES 315
Cdd:PRK09029 218 -------GCTHA-----SLVPT------QLWRLLDNRSEPLslkavllgGAAIPVELTEQAEQ---QGIrcwcgYGLTEM 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 316 GplGTVlypeeavvkagsigrCA-----IPGVEL-----EVRRQDGslcssgevgEICLRSAAMMQGYLDNREATAAVlD 385
Cdd:PRK09029 277 A--STV---------------CAkradgLAGVGSplpgrEVKLVDG---------EIWLRGASLALGYWRQGQLVPLV-N 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 386 DQGWYRSGDLARVDeDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL 465
Cdd:PRK09029 330 DEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAV 408
|
490
....*....|....*....
gi 502603069 466 vhEDLRQFMETRLARYKIP 484
Cdd:PRK09029 409 --VNLAEWLQDKLARFQQP 425
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-507 |
1.75e-33 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 131.92 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGA 108
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDEN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 109 RAslitaiqaepqplADiqwlstasategldcfDELLaqaapcgdehgrpaphalaeILYTSGTTGQPKGCLHSHANVFH 188
Cdd:cd05974 82 TH-------------AD----------------DPML--------------------LYFTSGTTSKPKLVEHTHRSYPV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 189 AALCAAAATSLAPTERTL-IAMPIWHSSPLNNWFlGTLLMGGTAVLMRE--YAPREFLETLAQERISfTFGAPIAFLAPL 265
Cdd:cd05974 113 GHLSTMYWIGLKPGDVHWnISSPGWAKHAWSCFF-APWNAGATVFLFNYarFDAKRVLAALVRYGVT-TLCAPPTVWRML 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 266 sVVPDVASYDfSAMRLWAYGGGPLGADMARKLAQVY-RSDRfmQVYGMTESGPLgtVLYPEEAVVKAGSIGRcAIPGVEL 344
Cdd:cd05974 191 -IQQDLASFD-VKLREVVGAGEPLNPEVIEQVRRAWgLTIR--DGYGQTETTAL--VGNSPGQPVKAGSMGR-PLPGYRV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 345 EVRRQDGSLCSSGEVgeiCL-----RSAAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGE 419
Cdd:cd05974 264 ALLDPDGAPATEGEV---ALdlgdtRPVGLMKGYAGDPDKTAHAMRG-GYYRTGDIAMRDEDGYLTYVGRADDVFKSSDY 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 420 NVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHE---DLRQFMETRLARYKIPRIFEVRDtLPRT 496
Cdd:cd05974 340 RISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEFAE-LPKT 418
|
490
....*....|.
gi 502603069 497 ATGKLLKHMLR 507
Cdd:cd05974 419 ISGKIRRVELR 429
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
26-447 |
1.55e-32 |
|
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: 131.01 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 26 QDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLV 105
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 106 -DGARASLITAIQAEPQPLADIQWLSTASATEGLDCFDELLAQAAPCGDEHGRPAPHAL------------AEILYTSGT 172
Cdd:cd17641 90 eDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGLYerevaagkgedvAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 173 TGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPI-WHSSPLnnWFLGTLLMGGTAVL-----------MREYAPR 240
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpWIGEQM--YSVGQALVCGFIVNfpeepetmmedLREIGPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 EFL-------ETLAQERISFTFGAPI-AFL------------------APLSVVPDVASY--------------DFSAMR 280
Cdd:cd17641 248 FVLlpprvweGIAADVRARMMDATPFkRFMfelgmklglraldrgkrgRPVSLWLRLASWladallfrplrdrlGFSRLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 281 LWAYGGGPLGADmarklaqVYRSDRFM-----QVYGMTESGPLGTVlyPEEAVVKAGSIGrCAIPGVELEVrrqdgslcs 355
Cdd:cd17641 328 SAATGGAALGPD-------TFRFFHAIgvplkQLYGQTELAGAYTV--HRDGDVDPDTVG-VPFPGTEVRI--------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 356 sGEVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKE-VEDVLCTHS 434
Cdd:cd17641 389 -DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQfIENKLKFSP 467
|
490
....*....|...
gi 502603069 435 DVQDVAVIGRPHP 447
Cdd:cd17641 468 YIAEAVVLGAGRP 480
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
8-507 |
1.06e-31 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 128.90 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALRADGQD------WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAV--V 79
Cdd:TIGR02188 63 VDRHLEARPDKVAIIWEGDEpgevrkITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIhsV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 80 V-------PINHKLQAPEVSYIL-----RHSGARLCL---VDGARASLITAIQ--------AEPqplaDIQWlstasaTE 136
Cdd:TIGR02188 143 VfggfsaeALADRINDAGAKLVItadegLRGGKVIPLkaiVDEALEKCPVSVEhvlvvrrtGNP----VVPW------VE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 137 GLDC-FDELLAQAAP-CgdehgRPAPHAlAE----ILYTSGTTGQPKGCLHS-----------HANVFhaalcaaaatSL 199
Cdd:TIGR02188 213 GRDVwWHDLMAKASAyC-----EPEPMD-SEdplfILYTSGSTGKPKGVLHTtggyllyaamtMKYVF----------DI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 200 APTERTLIAMPI-W---HSSPLnnwfLGTLLMGGTaVLMREYAPR-----EFLETLAQERISFTFGAPIAFLAPLSVVPD 270
Cdd:TIGR02188 277 KDGDIFWCTADVgWitgHSYIV----YGPLANGAT-TVMFEGVPTypdpgRFWEIIEKHKVTIFYTAPTAIRALMRLGDE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 271 -VASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDR--FMQVYGMTESGplGTVLYPEEAVV--KAGSIGRcAIPGVELE 345
Cdd:TIGR02188 352 wVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERcpIVDTWWQTETG--GIMITPLPGATptKPGSATL-PFFGIEPA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 346 VRRQDGSLCS-SGEVGEICLRSA--AMMQG-YLDNREATAAVLDD-QGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGEN 420
Cdd:TIGR02188 429 VVDEEGNPVEgPGEGGYLVIKQPwpGMLRTiYGDHERFVDTYFSPfPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 421 VYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL---VHEDLRQFMETRLARYKIPRIFEVRDTLPRTA 497
Cdd:TIGR02188 509 LGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPddeLRKELRKHVRKEIGPIAKPDKIRFVPGLPKTR 588
|
570
....*....|
gi 502603069 498 TGKLLKHMLR 507
Cdd:TIGR02188 589 SGKIMRRLLR 598
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
7-501 |
2.77e-31 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 126.01 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:cd17644 5 LFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLclvdgaraslitaiqaepqpladiqwlstasategldcfdeLLAQaapcgdehgrpaPHALAEI 166
Cdd:cd17644 85 PQERLTYILEDAQISV-----------------------------------------LLTQ------------PENLAYV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLgTLLMGGTAVLMRE---YAPREFL 243
Cdd:cd17644 112 IYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYV-TLLSGATLVLRPEemrSSLEDFV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 244 ETLAQERISfTFGAPIAFLAPL--SVVPDVASYDfSAMRLWAYGGGPLGADMARKLAQVYRSD-RFMQVYGMTESGPLGT 320
Cdd:cd17644 191 QYIQQWQLT-VLSLPPAYWHLLvlELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGNFiQLINVYGPTEATIAAT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 321 V---LYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATA--------AVLDDQGW 389
Cdd:cd17644 269 VcrlTQLTERNITSVPIGR-PIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAekfishpfNSSESERL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 390 YRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHED 469
Cdd:cd17644 348 YKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVE 427
|
490 500 510
....*....|....*....|....*....|..
gi 502603069 470 LRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17644 428 LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-501 |
3.15e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 128.92 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHK 85
Cdd:PRK12316 515 RLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 86 LQAPEVSYILRHSGARLCLVDGARASLItaiqaepqPL-ADIQWLSTASATEGLDCFDELLAQAAPCGDEhgrpaphaLA 164
Cdd:PRK12316 595 YPAERLAYMLEDSGVQLLLSQSHLGRKL--------PLaAGVQVLDLDRPAAWLEGYSEENPGTELNPEN--------LA 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 165 EILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIwhSSPLNNW-FLGTLLMGGTAVLMRE---YAPR 240
Cdd:PRK12316 659 YVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWeFFWPLMSGARLVVAAPgdhRDPA 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 EFLETLAQERISfTFGAPIAFLAPLSVVPDVASYDfsAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESgplgT 320
Cdd:PRK12316 737 KLVELINREGVD-TLHFVPSMLQAFLQDEDVASCT--SLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEA----A 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 321 VLYPEEAVVKAG----SIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATA------AVLDDQGWY 390
Cdd:PRK12316 810 IDVTHWTCVEEGgdsvPIGR-PIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAerfvpsPFVAGERMY 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 391 RSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPhpewGETVVAVLTLKPGKTLVHEDL 470
Cdd:PRK12316 889 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREAL 964
|
490 500 510
....*....|....*....|....*....|.
gi 502603069 471 RQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK12316 965 KAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
2-501 |
3.81e-31 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 127.04 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 2 MNFISLLDQQARTRPEKLaLRADgqdwsyaALAQAGRRAATvlyeqGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:PRK09192 37 MNFYDRRGQLEEALPYQT-LRAR-------AEAGARRLLAL-----GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 inhkLQAP-----EVSYILRHSGarlcLVDGARASLITAiqaePQPLADiqWLstASATEGLD-----CFDELLAQAAPc 151
Cdd:PRK09192 104 ----LPLPmgfggRESYIAQLRG----MLASAQPAAIIT----PDELLP--WV--NEATHGNPllhvlSHAWFKALPEA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 152 GDEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFH-AALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGT 230
Cdd:PRK09192 167 DVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMAnLRAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 231 AVLM--REYA--PREFLETLAQER--ISF--TFGAPIAFLAPLSVvpDVASYDFSAMRLWAYGGGPLGADMARKLAQVYR 302
Cdd:PRK09192 247 VDYLptRDFArrPLQWLDLISRNRgtISYspPFGYELCARRVNSK--DLAELDLSCWRVAGIGADMIRPDVLHQFAEAFA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 303 ----SDR-FMQVYGMTES------GPLGT-----------------VLYPEEAVVKAGSIGRC--AIPGVELEVRRQDGS 352
Cdd:PRK09192 325 pagfDDKaFMPSYGLAEAtlavsfSPLGSgivveevdrdrleyqgkAVAPGAETRRVRTFVNCgkALPGHEIEIRNEAGM 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 353 LCSSGEVGEICLRSAAMMQGYLDNrEATAAVLDDQGWYRSGDLARVdEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCT 432
Cdd:PRK09192 405 PLPERVVGHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQ 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502603069 433 HSDVQ--DVAVIGRPHPEwGETVVAVLTLKPGKTLVHEDLRQfmetRLARyKIPRIFEVR--------DTLPRTATGKL 501
Cdd:PRK09192 483 EPELRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIH----ALAA-LVRSEFGVEaavelvppHSLPRTSSGKL 555
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
16-501 |
3.85e-31 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 125.27 E-value: 3.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYIL 95
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RHSGARLCLVDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaPHALAEILYTSGTTGQ 175
Cdd:cd17650 81 EDSGAKLLLTQ-----------------------------------------------------PEDLAYVIYTSGTTGK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 176 PKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYA---PREFLETLAQERIS 252
Cdd:cd17650 108 PKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVkldPAALYDLILKSRIT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 253 FTFGAPiAFLAPLSVVPDVASYDFSAMRLWAygggpLGADMARKLAQVYRSDRFMQ------VYGMTESGPLGTvlYPEE 326
Cdd:cd17650 188 LMESTP-ALIRPVMAYVYRNGLDLSAMRLLI-----VGSDGCKAQDFKTLAARFGQgmriinSYGVTEATIDST--YYEE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 327 AVVKAGSIGRCAI----PGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVLDDQGW------YRSGDLA 396
Cdd:cd17650 260 GRDPLGDSANVPIgrplPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 397 RVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRpHPEWGETVVAVLTLkPGKTLVHEDLRQFMET 476
Cdd:cd17650 340 RWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVR-EDKGGEARLCAYVV-AAATLNTAELRAFLAK 417
|
490 500
....*....|....*....|....*
gi 502603069 477 RLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17650 418 ELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
25-507 |
7.23e-31 |
|
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: 124.84 E-value: 7.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 25 GQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCL 104
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 105 VDgARASLITAIQAEPQpladiqwlstasategldcfdellaqAAPCGDEHGRpaphaLAEIlYTSGTTGQPKGCLHSHA 184
Cdd:cd05939 81 FN-LLDPLLTQSSTEPP--------------------------SQDDVNFRDK-----LFYI-YTSGTTGLPKAAVIVHS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 185 NVFHAALCAAAATSLAPTERTLIAMPIWHSSPlNNWFLGTLLMGG-TAVLMREYAPREFLETLAQERISFT--FGAPIAF 261
Cdd:cd05939 128 RYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAG-GIMGVGQALLHGsTVVIRKKFSASNFWDDCVKYNCTIVqyIGEICRY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 262 LAPLSVVPDVASYDfsaMRLwAYGGGpLGADMARKLAQVYRSDRFMQVYGMTES-----------GPLGTV------LYP 324
Cdd:cd05939 207 LLAQPPSEEEQKHN---VRL-AVGNG-LRPQIWEQFVRRFGIPQIGEFYGATEGnsslvnidnhvGACGFNsrilpsVYP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 325 EEAVvkagsigRCAIPGVELeVRRQDG--SLCSSGE----VGEICLRSAAM-MQGYLDNREATAAVLDD-----QGWYRS 392
Cdd:cd05939 282 IRLI-------KVDEDTGEL-IRDSDGlcIPCQPGEpgllVGKIIQNDPLRrFDGYVNEGATNKKIARDvfkkgDSAFLS 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 393 GDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGR--PHPEwGETVVAVLTLKPGKTLVHEdL 470
Cdd:cd05939 354 GDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevPGVE-GRAGMAAIVDPERKVDLDR-F 431
|
490 500 510
....*....|....*....|....*....|....*..
gi 502603069 471 RQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:cd05939 432 SAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1-472 |
3.07e-30 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 123.86 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 1 MMNFISLLDQQARTRPEKLALRA-DGQDW---------SYAALAQAGRRAATVLYEQGVRQGDKLglLCFNTPG-----F 65
Cdd:PRK09274 5 MANIARHLPRAAQERPDQLAVAVpGGRGAdgklaydelSFAELDARSDAIAHGLNAAGIGRGMRA--VLMVTPSleffaL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 66 VFALLGAwrlGAVVVPINhklqaPEVSY--ILRhsgarlCLVDGARASLITaiqaepQPLADI---------QWLSTASA 134
Cdd:PRK09274 83 TFALFKA---GAVPVLVD-----PGMGIknLKQ------CLAEAQPDAFIG------IPKAHLarrlfgwgkPSVRRLVT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 135 TEGLDCF-----DELLAQAAPCGDEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAM 209
Cdd:PRK09274 143 VGGRLLWggttlATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 210 PIwhssplnnwF-LGTLLMGGTAVLMREYA-------PREFLETLAQERISFTFGAPiAFLAPLSVVPDVASYDFSAMRL 281
Cdd:PRK09274 223 PL---------FaLFGPALGMTSVIPDMDPtrpatvdPAKLFAAIERYGVTNLFGSP-ALLERLGRYGEANGIKLPSLRR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 282 WAYGGGPLGADMARKLAQVYRSD-RFMQVYGMTESGPLGTV-----LYPEEAVVKAGS---IGRcAIPGVELEVRR---- 348
Cdd:PRK09274 293 VISAGAPVPIAVIERFRAMLPPDaEILTPYGATEALPISSIesreiLFATRAATDNGAgicVGR-PVDGVEVRIIAisda 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 349 -----QDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG--WYRSGDLARVDEDGYLYIVDRLKDMIVTGGE 419
Cdd:PRK09274 372 pipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGG 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502603069 420 NVYSKEVEDVLCTHSDVQDVAVIGrpHPEWGETV-VAVLTLKPG----KTLVHEDLRQ 472
Cdd:PRK09274 452 TLYTIPCERIFNTHPGVKRSALVG--VGVPGAQRpVLCVELEPGvacsKSALYQELRA 507
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
156-501 |
5.83e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 124.65 E-value: 5.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 156 GRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVlmr 235
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVV--- 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 236 eYAP-----REFLETLAQERISFTFGAPIAFLAPLSVvPDVASYDFSAMRLWAYGggplgadmARKLAQVYRSD---RF- 306
Cdd:PRK08633 854 -YHPdptdaLGIAKLVAKHRATILLGTPTFLRLYLRN-KKLHPLMFASLRLVVAG--------AEKLKPEVADAfeeKFg 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 307 ---MQVYGMTESGPLGTVLYPEEAVV--------KAGSIGRcAIPGVELEVRRQD-GSLCSSGEVGEICLRSAAMMQGYL 374
Cdd:PRK08633 924 iriLEGYGATETSPVASVNLPDVLAAdfkrqtgsKEGSVGM-PLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMKGYL 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 375 DNREATAAVL---DDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCT--HSDVQDVAVIGRPHPEW 449
Cdd:PRK08633 1003 GDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKK 1082
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 502603069 450 GETVVAVLTLKPGKTlvhEDLRQFM-ETRLARYKIP-RIFEVrDTLPRTATGKL 501
Cdd:PRK08633 1083 GEKLVVLHTCGAEDV---EELKRAIkESGLPNLWKPsRYFKV-EALPLLGSGKL 1132
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-501 |
7.68e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 124.89 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK12467 1579 LIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEY 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLV-----------DGARASLITAIQAepqpladiqWLSTASATegldcfdellaqaapcgDEH 155
Cdd:PRK12467 1659 PRERLAYMIEDSGIELLLTqshlqarlplpDGLRSLVLDQEDD---------WLEGYSDS-----------------NPA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 156 GRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPiwHSSPLNNW-FLGTLLMGGTAVLM 234
Cdd:PRK12467 1713 VNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS--FAFDVSVWeLFWPLINGARLVIA 1790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 235 REYA---PREFLETLAQERISFTFGAPIAFLAPLSVVPDVASYdfSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYG 311
Cdd:PRK12467 1791 PPGAhrdPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHP--LSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYG 1868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 312 MTESGPlgTVLY-------PEEAVvkAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLdNREATAA-- 382
Cdd:PRK12467 1869 PTETAV--DVTHwtcrrkdLEGRD--SVPIGQ-PIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYL-NRPALTAer 1942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 383 -VLD-----DQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAV 456
Cdd:PRK12467 1943 fVADpfgtvGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYV 2022
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502603069 457 LTLKPGktLVHED---------LRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK12467 2023 VPTDPG--LVDDDeaqvalraiLKNHLKASLPEYMVPAHLVFLARMPLTPNGKL 2074
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
16-501 |
1.64e-29 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 121.04 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYIL 95
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RHSGARLCLVDGARASLITAIQAEPQPLADIQwlsTASATEGLDCFDEllaqaapcgDEHgrpaphaLAEILYTSGTTGQ 175
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSI---SQEDTSNIDYINN---------SDD-------LLYIIYTSGTTGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 176 PKGCLHSHANVFHAALCAAAATSLAPTERTL-IAMPIWHSSplNNWFLGTLLMGGTAVLMREYAPRE---FLETLAQERI 251
Cdd:cd17656 143 PKGVQLEHKNMVNLLHFEREKTNINFSDKVLqFATCSFDVC--YQEIFSTLLSGGTLYIIREETKRDveqLFDLVKRHNI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 252 SFTFgAPIAFLAPLSVVPDVASYDFSAMRLWAYGGGPLgaDMARKLAQVYRSDR--FMQVYGMTESGPLGT-VLYPEEAV 328
Cdd:cd17656 221 EVVF-LPVAFLKFIFSEREFINRFPTCVKHIITAGEQL--VITNEFKEMLHEHNvhLHNHYGPSETHVVTTyTINPEAEI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 329 VKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVL------DDQGWYRSGDLARVDEDG 402
Cdd:cd17656 298 PELPPIGK-PISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFfpdpfdPNERMYRTGDLARYLPDG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 403 YLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTlkPGKTLVHEDLRQFMETRLARYK 482
Cdd:cd17656 377 NIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAKQLPEYM 454
|
490
....*....|....*....
gi 502603069 483 IPRIFEVRDTLPRTATGKL 501
Cdd:cd17656 455 IPSFFVPLDQLPLTPNGKV 473
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-501 |
2.52e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.06 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHK 85
Cdd:PRK12316 4555 QLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 86 LQAPEVSYILRHSGARLclvdgarasLITAIQAEPQ-PLADiqwlstasateGLDCFDellaqAAPCGDEHGRPA----- 159
Cdd:PRK12316 4635 YPRERLAYMMEDSGAAL---------LLTQSHLLQRlPIPD-----------GLASLA-----LDRDEDWEGFPAhdpav 4689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 ---PHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGtlLMGGTAVLMRE 236
Cdd:PRK12316 4690 rlhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHP--LINGASVVIRD 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 237 ---YAPREFLETLAQERISfTFGAPIAFLAPLSVVPDVASyDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMT 313
Cdd:PRK12316 4768 dslWDPERLYAEIHEHRVT-VLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPT 4845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 314 EsgplgTVLYPEEAVVKAGS--------IGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--- 382
Cdd:PRK12316 4846 E-----TTVTVLLWKARDGDacgaaympIGT-PLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAErfv 4919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 383 --VLDDQG--WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLT 458
Cdd:PRK12316 4920 pdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVP 4999
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502603069 459 LKP-------GKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK12316 5000 QDPaladadeAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
3-401 |
3.78e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 115.14 E-value: 3.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 3 NFISLLDQQARTRPEK--LALR-ADGQDWSYAALAQAGRRA---ATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLG 76
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRpwLAQRePGHGQWRKVTYGEAKRAVdalAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 77 AVVVPInhklqAPEVSyILRHSGARL-CLVDGARASLITAIQAEP-------QPLADIQWLSTASATEGLDC--FDELLA 146
Cdd:PRK12582 130 VPAAPV-----SPAYS-LMSHDHAKLkHLFDLVKPRVVFAQSGAPfaralaaLDLLDVTVVHVTGPGEGIASiaFADLAA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 147 qaAPCGDE----HGRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIA---MPIWHSSPLNN 219
Cdd:PRK12582 204 --TPPTAAvaaaIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSldwMPWNHTMGGNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 220 WFLGTLLMGGTAVL-----MreyaPREFLETLAQER-ISFT--FGAPIAF--LAP-LSVVPDVASYDFSAMRLWAYGGGP 288
Cdd:PRK12582 282 NFNGLLWGGGTLYIddgkpL----PGMFEETIRNLReISPTvyGNVPAGYamLAEaMEKDDALRRSFFKNLRLMAYGGAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 289 LGADMARKL-----AQVYRSDRFMQVYGMTESGPLGTVLY-PEEAVvkaGSIGrCAIPGVELEvrrqdgsLCSSGEVGEI 362
Cdd:PRK12582 358 LSDDLYERMqalavRTTGHRIPFYTGYGATETAPTTTGTHwDTERV---GLIG-LPLPGVELK-------LAPVGDKYEV 426
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 502603069 363 CLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLAR-VDED 401
Cdd:PRK12582 427 RVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfVDPD 466
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-506 |
9.23e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.44 E-value: 9.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLvdgARASLITAIQAEPQPLAdiqwlstasategLDCFDELLAQAAPcgdeHGRPAPHALAEI 166
Cdd:PRK12316 3142 PEERLAYMLEDSGAQLLL---SQSHLRLPLAQGVQVLD-------------LDRGDENYAEANP----AIRTMPENLAYV 3201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIwhSSPLNNWFLGTLLMGGTAVLMREY----APREF 242
Cdd:PRK12316 3202 IYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF--SFDVFVEELFWPLMSGARVVLAGPedwrDPALL 3279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 243 LETLAQERISFTFGAPIAFLAPLSvvpDVASYDFSAMRLWAYGGGPLGADMArklAQVYRSDRFMQVYGMTESGPLGTVL 322
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAFLE---EEDAHRCTSLKRIVCGGEALPADLQ---QQVFAGLPLYNLYGPTEATITVTHW 3353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 323 YPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVL------DDQGWYRSGDLA 396
Cdd:PRK12316 3354 QCVEEGKDAVPIGR-PIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYRTGDLA 3432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 397 RVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPhpewGETVVAVLTLKPGKTLVHEDLRQFMET 476
Cdd:PRK12316 3433 RYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKA 3508
|
490 500 510
....*....|....*....|....*....|
gi 502603069 477 RLARYKIPRIFEVRDTLPRTATGKLLKHML 506
Cdd:PRK12316 3509 SLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-501 |
1.30e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 114.87 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK12467 3100 LIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEY 3179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLvdgARASLITAIqaePQPLADIQWLstasategldcfdelLAQAAPCGDEHGRPAPHA---- 162
Cdd:PRK12467 3180 PRERLAYMIEDSGVKLLL---TQAHLLEQL---PAPAGDTALT---------------LDRLDLNGYSENNPSTRVmgen 3238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 LAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFlGTLLMGGTAVLM--REYAPR 240
Cdd:PRK12467 3239 LAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFL-WTLICGGCLVVRdnDLWDPE 3317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 EFLETLAQERISFTFGAPiAFLAPLSVVPDVASYdfSAMRLWAYGGGPLGAD----MARKLAQVYrsdrFMQVYGMTESG 316
Cdd:PRK12467 3318 ELWQAIHAHRISIACFPP-AYLQQFAEDAGGADC--ASLDIYVFGGEAVPPAafeqVKRKLKPRG----LTNGYGPTEAV 3390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 317 PLGTVL-YPEEAVVKAGS--IGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA-----VLDDQG 388
Cdd:PRK12467 3391 VTVTLWkCGGDAVCEAPYapIGR-PVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAErfvadPFSGSG 3469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 389 --WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPhPEWGETVVAVLTLKPGKTLV 466
Cdd:PRK12467 3470 grLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVPADPQGDW 3548
|
490 500 510
....*....|....*....|....*....|....*
gi 502603069 467 HEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK12467 3549 RETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKV 3583
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-501 |
1.15e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 111.80 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKL 86
Cdd:PRK05691 1136 LLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDY 1215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAPEVSYILRHSGARLCLVDGARaslitaiqaepqpladiqwLSTASATEGLD--CFDELLAQA----APCGDEHGrpap 160
Cdd:PRK05691 1216 PAERLAYMLADSGVELLLTQSHL-------------------LERLPQAEGVSaiALDSLHLDSwpsqAPGLHLHG---- 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 161 HALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIwhSSPLNNW--FLgTLLMGGTAVLM---R 235
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI--SFDVSVWecFW-PLITGCRLVLAgpgE 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 236 EYAPREFLETLAQERISftfgaPIAFLAPLSVV----PDVAsyDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYG 311
Cdd:PRK05691 1350 HRDPQRIAELVQQYGVT-----TLHFVPPLLQLfidePLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYG 1422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 312 MTESGPLGTVLYPEEAVVKAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VLDDQG- 388
Cdd:PRK05691 1423 PTETAINVTHWQCQAEDGERSPIGR-PLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfVPDPLGe 1501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 389 ----WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEwGETVVAVLTLKPGKT 464
Cdd:PRK05691 1502 dgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAA-GAQLVGYYTGEAGQE 1580
|
490 500 510
....*....|....*....|....*....|....*..
gi 502603069 465 LVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK05691 1581 AEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKL 1617
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
8-482 |
1.46e-25 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 110.21 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEK--LALRADGQDW---SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPI 82
Cdd:cd05921 1 LAHWARQAPDRtwLAEREGNGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 83 nhklqAPEVSYI------LRHSGARL--CLVDGARASLITAIQAEPQPLaDIQWLSTASATEGLDC--FDELLAQAAPCG 152
Cdd:cd05921 81 -----SPAYSLMsqdlakLKHLFELLkpGLVFAQDAAPFARALAAIFPL-GTPLVVSRNAVAGRGAisFAELAATPPTAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 153 DEHGRPA--PHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIA--MPIWHSSPLNNWFLGTLLMG 228
Cdd:cd05921 155 VDAAFAAvgPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVdwLPWNHTFGGNHNFNLVLYNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 229 GTAVLMR-EYAPREFLETLAQER-ISFT--FGAPIAF---LAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKL---- 297
Cdd:cd05921 235 GTLYIDDgKPMPGGFEETLRNLReISPTvyFNVPAGWemlVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLqala 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 298 -AQVYRSDRFMQVYGMTESGPLGTVLY-PEEavvKAGSIGrCAIPGVELEVRRQDGSLcssgevgEICLRSAAMMQGYLD 375
Cdd:cd05921 315 vATVGERIPMMAGLGATETAPTATFTHwPTE---RSGLIG-LPAPGTELKLVPSGGKY-------EVRVKGPNVTPGYWR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 376 NREATAAVLDDQGWYRSGDLAR-VDED----GyLYIVDRL-KDMIVTGGE--NVYSKEVEDVLCTHSDVQDVAVIGRPHP 447
Cdd:cd05921 384 QPELTAQAFDEEGFYCLGDAAKlADPDdpakG-LVFDGRVaEDFKLASGTwvSVGPLRARAVAACAPLVHDAVVAGEDRA 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502603069 448 EWG----------ETVVAVLTLKPGKTLVHEDLRQFMETRLARYK 482
Cdd:cd05921 463 EVGalvfpdllacRRLVGLQEASDAEVLRHAKVRAAFRDRLAALN 507
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
8-401 |
3.75e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 109.20 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEK--LALRADGQDW---SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPI 82
Cdd:PRK08180 45 LVHWAQEAPDRvfLAERGADGGWrrlTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 83 nhklqAPEVSYI------LRHSgARLC---LV---DGARASliTAIQAEPqpLADIQWLSTASATEGLDC--FDELLAQA 148
Cdd:PRK08180 125 -----SPAYSLVsqdfgkLRHV-LELLtpgLVfadDGAAFA--RALAAVV--PADVEVVAVRGAVPGRAAtpFAALLATP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 149 APCGDE--HGRPAPHALAEILYTSGTTGQPKGCLHSHanvfhaalcaaaatslapteRTLIA--------MPIWHSSP-- 216
Cdd:PRK08180 195 PTAAVDaaHAAVGPDTIAKFLFTSGSTGLPKAVINTH--------------------RMLCAnqqmlaqtFPFLAEEPpv 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 217 LNNW------FLG------TLLMGGTAvlmreY------APREFLETLAQER-ISFT--FGAPIAF--LAP-LSVVPDVA 272
Cdd:PRK08180 255 LVDWlpwnhtFGGnhnlgiVLYNGGTL-----YiddgkpTPGGFDETLRNLReISPTvyFNVPKGWemLVPaLERDAALR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 273 SYDFSAMRLWAYGGGPLGADMARKL---AQVYRSDR--FMQVYGMTESGPLGTvlYPEEAVVKAGSIGRCAiPGVELEVR 347
Cdd:PRK08180 330 RRFFSRLKLLFYAGAALSQDVWDRLdrvAEATCGERirMMTGLGMTETAPSAT--FTTGPLSRAGNIGLPA-PGCEVKLV 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 502603069 348 RQDGSLcssgevgEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLAR-VDED 401
Cdd:PRK08180 407 PVGGKL-------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRfVDPA 454
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
8-430 |
4.51e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 110.26 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALR--ADGQD----WSYAALAQAGRRAATVLYEQGVrQGDKLGLLCFNTPGFVFALLGAWRLGAVVVP 81
Cdd:PRK05691 15 LQRRAAQTPDRLALRflADDPGegvvLSYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 InhklQAPEVSYilRHSGARL-CLVDGARASLITAIQAEPQPLADIQWLSTASATEGLdCFDELLAQAApcgDEHGRPA- 159
Cdd:PRK05691 94 A----YPPESAR--RHHQERLlSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELL-CVDTLDPALA---EAWQEPAl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 -PHALAEILYTSGTTGQPKGCLHSHANVF--HAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMre 236
Cdd:PRK05691 164 qPDDIAFLQYTSGSTALPKGVQVSHGNLVanEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 237 yAPREFL-------ETLAQERISFTFGAPIAFLAPLSVVPDVA--SYDFSAMRLWAYGGGPLGADMARKLAQVY-----R 302
Cdd:PRK05691 242 -SPAYFLerplrwlEAISEYGGTISGGPDFAYRLCSERVSESAleRLDLSRWRVAYSGSEPIRQDSLERFAEKFaacgfD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 303 SDRFMQVYGMTES------GPLGT----------VLYPEEAVVKAGS-IGRCAIPGVELEVR---RQDGSLCSSGEVGEI 362
Cdd:PRK05691 321 PDSFFASYGLAEAtlfvsgGRRGQgipaleldaeALARNRAEPGTGSvLMSCGRSQPGHAVLivdPQSLEVLGDNRVGEI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502603069 363 CLRSAAMMQGYLDNREATAAV---LDDQGWYRSGDLARVdEDGYLYIVDRLKDMIVTGGENVYSKEVEDVL 430
Cdd:PRK05691 401 WASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
29-502 |
7.34e-25 |
|
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: 108.31 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAAL-AQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDG 107
Cdd:cd17632 69 TYAELwERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 108 ARASLITAIQAEPQ-----------PLADIQWLSTASATEGLDCFDEL--LAQAAPCGDEHGRPAP--------HALAEI 166
Cdd:cd17632 149 EHLDLAVEAVLEGGtpprlvvfdhrPEVDAHRAALESARERLAAVGIPvtTLTLIAVRGRDLPPAPlfrpepddDPLALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 167 LYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAP-TERTLIAMPIWHSSPlNNWFLGTLLMGGTAVlmreYAPREFLET 245
Cdd:cd17632 229 IYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPpASITLNFMPMSHIAG-RISLYGTLARGGTAY----FAAASDMST 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQErisFTFGAPIAFLaplsVVPDVASYDF----SAMRLWAYGGGPLGADMAR---KLAQVYRSDRF------------ 306
Cdd:cd17632 304 LFDD---LALVRPTELF----LVPRVCDMLFqryqAELDRRSVAGADAETLAERvkaELRERVLGGRLlaavcgsaplsa 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 307 -MQV-------------YGMTESGplgtvlypeeAVVKAGSIGRcaiPGV---------ELEVRRQDgslcSSGEVGEIC 363
Cdd:cd17632 377 eMKAfmeslldldlhdgYGSTEAG----------AVILDGVIVR---PPVldyklvdvpELGYFRTD----RPHPRGELL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 364 LRSAAMMQGYLDNREATAAVLDDQGWYRSGD-LARVDEDGYLYiVDRLKDMI-VTGGENVYSKEVEDVLCTHSDVQDVAV 441
Cdd:cd17632 440 VKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDvMAELGPDRLVY-VDRRNNVLkLSQGEFVTVARLEAVFAASPLVRQIFV 518
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502603069 442 IGR-----------PHPEwgetVVAVLTLKPGKTLVHEDLRQF-METRLARYKIPRIFEVrDTLPRTATGKLL 502
Cdd:cd17632 519 YGNserayllavvvPTQD----ALAGEDTARLRAALAESLQRIaREAGLQSYEIPRDFLI-ETEPFTIANGLL 586
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1-501 |
1.27e-24 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 106.90 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 1 MMNFISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLyeQGVRQGDKLGLLCF--NTPGFVFALLGAWRLGAV 78
Cdd:PRK04813 1 IMDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFI--DSLKLPDKSPIIVFghMSPEMLATFLGAVKAGHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 79 VVPINHKLQAPEVSYIlrhsgarlclVDGARASLITAIQAEPQPLADIQWLSTASATEGLDCFDELLAQAAPCGDEHgrp 158
Cdd:PRK04813 79 YIPVDVSSPAERIEMI----------IEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDN--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 159 aphalAEILYTSGTTGQPKGCLHSHANvfhaalcaaaatslaptertLIAMPIW----HSSPLNNWFLG----------- 223
Cdd:PRK04813 146 -----YYIIFTSGTTGKPKGVQISHDN--------------------LVSFTNWmledFALPEGPQFLNqapysfdlsvm 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 224 ----TLLMGGTAVLM-REYA--PREFLETLAQERI-------SFtfgAPIAFLAPlsvvpdvasyDFSA-----MRLWAY 284
Cdd:PRK04813 201 dlypTLASGGTLVALpKDMTanFKQLFETLPQLPInvwvstpSF---ADMCLLDP----------SFNEehlpnLTHFLF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 285 GGGPLGADMARKLAQVYRSDRFMQVYGMTE-SGPLGTVLYPEEAVVKAGS--IGRCAiPGVELEVRRQDGSLCSSGEVGE 361
Cdd:PRK04813 268 CGEELPHKTAKKLLERFPSATIYNTYGPTEaTVAVTSIEITDEMLDQYKRlpIGYAK-PDSPLLIIDEEGTKLPDGEQGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 362 ICLRSAAMMQGYLDNREATAAV---LDDQGWYRSGDLARVDeDGYLYIVDRLKDMIVTGGenvYSKEVEDV---LCTHSD 435
Cdd:PRK04813 347 IVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKLNG---YRIELEEIeqnLRQSSY 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502603069 436 VQDVAVIgrPHpEWGETV---VAVLTLKPGK-----TLVHEdLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK04813 423 VESAVVV--PY-NKDHKVqylIAYVVPKEEDferefELTKA-IKKELKERLMEYMIPRKFIYRDSLPLTPNGKI 492
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
6-501 |
1.43e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 108.72 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 6 SLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHK 85
Cdd:PRK05691 2192 GLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPE 2271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 86 LQAPEVSYILRHSGARLCLVDgarASLITAIQAEPQPLAdiQWlstasategldCF-DELLAQAAPCGDEHGRPA-PHAL 163
Cdd:PRK05691 2272 YPLERLHYMIEDSGIGLLLSD---RALFEALGELPAGVA--RW-----------CLeDDAAALAAYSDAPLPFLSlPQHQ 2335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 AEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLiampiwHSSPLN-----NWFLGTLLMGGTAVLMR--E 236
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCEL------HFYSINfdaasERLLVPLLCGARVVLRAqgQ 2409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 237 YAPREFLETLAQERIS---FT--FGAPIA-FLAplsvvpdvASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVY 310
Cdd:PRK05691 2410 WGAEEICQLIREQQVSilgFTpsYGSQLAqWLA--------GQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAY 2481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 311 GMTES--GPLGTvLYPEEAVVKAGS--IGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAA--VL 384
Cdd:PRK05691 2482 GPTETvvMPLAC-LAPEQLEEGAASvpIGR-VVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAErfVA 2559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 385 D----DQG-WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEwGETVVAVLTL 459
Cdd:PRK05691 2560 DpfaaDGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPS-GKQLAGYLVS 2638
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502603069 460 KPGK------TLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK05691 2639 AVAGqddeaqAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKL 2686
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
52-489 |
4.09e-24 |
|
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: 105.76 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 52 GDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDgaraslitaiqaepqplADIQWLSt 131
Cdd:cd05927 32 ASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD-----------------AGVKVYS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 132 asategldcFDELLAQ--AAPCgdEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVfhaalcaaaatslapTERTLIAM 209
Cdd:cd05927 94 ---------LEEFEKLgkKNKV--PPPPPKPEDLATICYTSGTTGNPKGVMLTHGNI---------------VSNVAGVF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 210 PIWHSSPLnnwflgtllMGGTAVLMrEYAPrefletLAQ--ERI----SFTFGAPIAF--------------LAP--LSV 267
Cdd:cd05927 148 KILEILNK---------INPTDVYI-SYLP------LAHifERVvealFLYHGAKIGFysgdirlllddikaLKPtvFPG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 268 VPDVAS--YD-------------------------------------------FSAM--------RLWAYGGGPLGADMA 294
Cdd:cd05927 212 VPRVLNriYDkifnkvqakgplkrklfnfalnyklaelrsgvvraspfwdklvFNKIkqalggnvRLMLTGSAPLSPEVL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 295 RKLaQVYRSDRFMQVYGMTESGPLGTVLYPEEAvvkagSIGRCAIPGVELEVRRQD------GSLCSSGEvGEICLRSAA 368
Cdd:cd05927 292 EFL-RVALGCPVLEGYGQTECTAGATLTLPGDT-----SVGHVGGPLPCAEVKLVDvpemnyDAKDPNPR-GEVCIRGPN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 369 MMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMI-VTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHP 447
Cdd:cd05927 365 VFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLK 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 502603069 448 EWgetVVAVltlkpgktlVHEDLRQFMETRLARYKIPRIFEV 489
Cdd:cd05927 445 SF---LVAI---------VVPDPDVLKEWAASKGGGTGSFEE 474
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
425-500 |
9.55e-24 |
|
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: 94.53 E-value: 9.55e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502603069 425 EVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGK 500
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1-427 |
2.02e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 103.54 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 1 MMNFISLLDQQARTRPEKLALRA----DGQDWsyAALAQAGRRAATVLYEQGVRQGDKLGLLCfNTPGFVF-ALLGAWRL 75
Cdd:PRK07768 1 MSRFTEKMYANARTSPRGMVTGEpdapVRHTW--GEVHERARRIAGGLAAAGVGPGDAVAVLA-GAPVEIApTAQGLWMR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 76 GAVVVpinhKLQAPEVSYILRH----SGARLCLVdGARASLItaiqAEPqpladiqWLSTASATEGL----DCFDELLAQ 147
Cdd:PRK07768 78 GASLT----MLHQPTPRTDLAVwaedTLRVIGMI-GAKAVVV----GEP-------FLAAAPVLEEKgirvLTVADLLAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 148 AAPCGDEHGRPAPhALAEIlyTSGTTGQPKGCLHSHANVFHAALCAAAATSLAP-TERTLIAMPIWHSSPLNNWFLGTLL 226
Cdd:PRK07768 142 DPIDPVETGEDDL-ALMQL--TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVeTDVMVSWLPLFHDMGMVGFLTVPMY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 227 MGGTAVLMReyaPREFL-------ETLAQERISFTFGAPIAF--LAP-LSVVPDVASYDFSAMRLWAYGGGPLGADMARK 296
Cdd:PRK07768 219 FGAELVKVT---PMDFLrdpllwaELISKYRGTMTAAPNFAYalLARrLRRQAKPGAFDLSSLRFALNGAEPIDPADVED 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 297 LAQV-----YRSDRFMQVYGMTES------GPLGTVLYPEE-----------AV-VKAGSIGRCA-----IPGVELEVRR 348
Cdd:PRK07768 296 LLDAgarfgLRPEAILPAYGMAEAtlavsfSPCGAGLVVDEvdadllaalrrAVpATKGNTRRLAtlgppLPGLEVRVVD 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502603069 349 QDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVlDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVE 427
Cdd:PRK07768 376 EDGQVLPPRGVGVIELRGESVTPGYLTMDGFIPAQ-DADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
156-501 |
9.48e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 99.73 E-value: 9.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 156 GRPAPHALAEILYTSGTTGQPKGCLHSHANVfhAALCAAAATSLAPTERTLIAMPIWHssplnnwflgtllMGGTAVLMR 235
Cdd:PRK07824 30 GEPIDDDVALVVATSGTTGTPKGAMLTAAAL--TASADATHDRLGGPGQWLLALPAHH-------------IAGLQVLVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 236 E---------------YAPREF---LETLAQERiSFTFGAPIAFLAPLSVVPDVASY-DFSAMRLwayGGGPLGADMARK 296
Cdd:PRK07824 95 SviagsepveldvsagFDPTALpraVAELGGGR-RYTSLVPMQLAKALDDPAATAALaELDAVLV---GGGPAPAPVLDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 297 LAQ----VYRSdrfmqvYGMTESGplGTVLYPeeavvkagsiGRcAIPGVELEVrrqdgslcssgEVGEICLRSAAMMQG 372
Cdd:PRK07824 171 AAAaginVVRT------YGMSETS--GGCVYD----------GV-PLDGVRVRV-----------EDGRIALGGPTLAKG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 373 YLDNREATAAVldDQGWYRSGDLARVDeDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGET 452
Cdd:PRK07824 221 YRNPVDPDPFA--EPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQR 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502603069 453 VVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK07824 298 VVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKV 346
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
5-501 |
2.48e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 101.27 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 5 ISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINH 84
Cdd:PRK10252 461 SALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDT 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 85 KLQAPEVSYILRHsgarlclvdgARASLITAIQAEPQPLADIQWLStasategLDCFDELLAqaAPCGDEHGRPAPHALA 164
Cdd:PRK10252 541 GYPDDRLKMMLED----------ARPSLLITTADQLPRFADVPDLT-------SLCYNAPLA--PQGAAPLQLSQPHHTA 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 165 EILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIwhSSPLNNW-FLGTLLMGGTAVLMREYA---PR 240
Cdd:PRK10252 602 YIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPC--SFDVSVWeFFWPFIAGAKLVMAEPEAhrdPL 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 EFLETLAQERISFTFGAP---IAFLAPLSvvPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSdRFMQVYGMTESGp 317
Cdd:PRK10252 680 AMQQFFAEYGVTTTHFVPsmlAAFVASLT--PEGARQSCASLRQVFCSGEALPADLCREWQQLTGA-PLHNLYGPTEAA- 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 318 LGTVLYP----EEAVVKAGS--IGRcaiPGVELEVRRQDGSL--CSSGEVGEICLRSAAMMQGYLDNREATAA-VLDD-- 386
Cdd:PRK10252 756 VDVSWYPafgeELAAVRGSSvpIGY---PVWNTGLRILDARMrpVPPGVAGDLYLTGIQLAQGYLGRPDLTASrFIADpf 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 387 -QG--WYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGR------PHPEWGETVVAVL 457
Cdd:PRK10252 833 aPGerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYL 912
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 502603069 458 TLKPGKTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK10252 913 VSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKL 956
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
163-446 |
3.24e-22 |
|
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: 99.60 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 163 LAEILYTSGTTGQPKGCLHSHANVFHAAL--CAAAATSLAPTERTLIAMPIWHssplnnwflgtllmggtavlmreyapr 240
Cdd:cd17639 90 LACIMYTSGSTGNPKGVMLTHGNLVAGIAglGDRVPELLGPDDRYLAYLPLAH--------------------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 241 eFLEtLAQERISFTFGAPIAFLAPLSVVPDV--------------------ASYD--------------------FS--- 277
Cdd:cd17639 143 -IFE-LAAENVCLYRGGTIGYGSPRTLTDKSkrgckgdltefkptlmvgvpAIWDtirkgvlaklnpmgglkrtlFWtay 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 278 AMRLWAY------------------------------GGGPLGADmarklaqvyrSDRFMQV--------YGMTESGPLG 319
Cdd:cd17639 221 QSKLKALkegpgtplldelvfkkvraalggrlrymlsGGAPLSAD----------TQEFLNIvlcpviqgYGLTETCAGG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 320 TVLYPEEavVKAGSIGRcAIPGVELE-VRRQDGSLCSSGEV--GEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLA 396
Cdd:cd17639 291 TVQDPGD--LETGRVGP-PLPCCEIKlVDWEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIG 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502603069 397 RVDEDGYLYIVDRLKDMIVT-GGENVYSKEVEDVLCTHSDVQDVAVIGRPH 446
Cdd:cd17639 368 EFHPDGTLKIIDRKKDLVKLqNGEYIALEKLESIYRSNPLVNNICVYADPD 418
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
168-500 |
5.09e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 98.18 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 168 YTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMREYAPREFLETLA 247
Cdd:PRK08308 108 YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNILR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 248 QERISFTFGAPiAFLAPLSVVPDVASYDFSAMRlwayGGGPLGADMARKLAQvyRSDRFMQVYGMTEsgplgtvlypeea 327
Cdd:PRK08308 188 NTPQHILYAVP-LMLHILGRLLPGTFQFHAVMT----SGTPLPEAWFYKLRE--RTTYMMQQYGCSE------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 328 vvkAGSIGRCAipgvelevrrqdgSLCSSGEVGeICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIV 407
Cdd:PRK08308 248 ---AGCVSICP-------------DMKSHLDLG-NPLPHVSVSAGSDENAPEEIVVKMGDKEIFTKDLGYKSERGTLHFM 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 408 DRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVheDLRQFMETRLARYKIPRIF 487
Cdd:PRK08308 311 GRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPV--QLREWCIQHLAPYQVPHEI 388
|
330
....*....|...
gi 502603069 488 EVRDTLPRTATGK 500
Cdd:PRK08308 389 ESVTEIPKNANGK 401
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
16-501 |
7.45e-22 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 98.24 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 16 PEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKL-GLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYI 94
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLvGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 95 LRHSGARLCLVDgaraslitaiqaepqpladiqwlstasategldcfdellaqaapcgdehgrpaPHALAEILYTSGTTG 174
Cdd:cd17648 81 LEDTGARVVITN-----------------------------------------------------STDLAYAIYTSGTTG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 175 QPKGCLHSHANV--FHAALCAAAATSLAPTERTLIampiwHSSPLNNWFLGTL---LMGGTAVLMRE----YAPREFLET 245
Cdd:cd17648 108 KPKGVLVEHGSVvnLRTSLSERYFGRDNGDEAVLF-----FSNYVFDFFVEQMtlaLLNGQKLVVPPdemrFDPDRFYAY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 246 LAQERISFTFGAP-------IAFLAPLSVVpDVASYDFSAMRLwaygggplgadmaRKLAQVYRSdRFMQVYGMTESGPL 318
Cdd:cd17648 183 INREKVTYLSGTPsvlqqydLARLPHLKRV-DAAGEEFTAPVF-------------EKLRSRFAG-LIINAYGPTETTVT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 319 GTV-LYPEEAVVKAgSIGrCAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATA--------------AV 383
Cdd:cd17648 248 NHKrFFPGDQRFDK-SLG-RPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAerflpnpfqteqerAR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 384 LDDQGWYRSGDLARVDEDGYLYIVDRlKDMIVT-GGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETV-----VAVL 457
Cdd:cd17648 326 GRNARLYKTGDLVRWLPSGELEYLGR-NDFQVKiRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRiqkylVGYY 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 502603069 458 TLKPGkTLVHEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:cd17648 405 LPEPG-HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
8-507 |
1.54e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 95.21 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALRADGQDW------SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVvvp 81
Cdd:PRK00174 73 LDRHLKTRGDKVAIIWEGDDPgdsrkiTYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV--- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 82 inhklqapevsyilrHS-----------GARLclVD-GARAsLITAIQA----EPQPL---------------------- 123
Cdd:PRK00174 150 ---------------HSvvfggfsaealADRI--IDaGAKL-VITADEGvrggKPIPLkanvdealancpsvekvivvrr 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 124 --ADIQWlstasaTEGLDC-FDELLAQAapcGDEHgrPAPHALAE----ILYTSGTTGQPKGCLHS-----------HAN 185
Cdd:PRK00174 212 tgGDVDW------VEGRDLwWHELVAGA---SDEC--EPEPMDAEdplfILYTSGSTGKPKGVLHTtggylvyaamtMKY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 186 VFHAAlcaaaatslaPTErtliampI--------W---HSSPLnnwfLGTLLMGGTaVLMREYAPR-----EFLETLAQE 249
Cdd:PRK00174 281 VFDYK----------DGD-------VywctadvgWvtgHSYIV----YGPLANGAT-TLMFEGVPNypdpgRFWEVIDKH 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 250 RISFTFGAPIAFLAPLSVVPD-VASYDFSAMRL--------------WAY---GGG--PLGadmarklaqvyrsDRFMQv 309
Cdd:PRK00174 339 KVTIFYTAPTAIRALMKEGDEhPKKYDLSSLRLlgsvgepinpeaweWYYkvvGGErcPIV-------------DTWWQ- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 310 ygmTESGplGTVLYPEEAVV--KAGSIGRcAIPGVELEVRRQDGSLCSSGEVGEICLRSA--AMMQG-YLD-NREATAAV 383
Cdd:PRK00174 405 ---TETG--GIMITPLPGATplKPGSATR-PLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTiYGDhERFVKTYF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 384 LDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGK 463
Cdd:PRK00174 479 STFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGE 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 502603069 464 TlVHEDLRQfmETR---------LARykiPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PRK00174 559 E-PSDELRK--ELRnwvrkeigpIAK---PDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-481 |
2.60e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 93.68 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGF---VFALLgawRLGAVVVpinhklqapevsyilrhsgarlcLV 105
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFfalTFALF---KAGAVPV-----------------------LI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 106 DgaraslitaiqaepqPLADIQWLSTasategldCFDELLAQAAPcgdehGRPAPHALAEILYTSGTTGQPKGCLHSHAN 185
Cdd:cd05910 58 D---------------PGMGRKNLKQ--------CLQEAEPDAFI-----GIPKADEPAAILFTSGSTGTPKGVVYRHGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 186 VFHAALCAAAATSLAPTERTLIAMPIWHssplnnwfLGTLLMGGTAVL--MREYAP-----REFLETLAQERISFTFGAP 258
Cdd:cd05910 110 FAAQIDALRQLYGIRPGEVDLATFPLFA--------LFGPALGLTSVIpdMDPTRParadpQKLVGAIRQYGVSIVFGSP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 259 iAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGADMARKLAQVYRSD-RFMQVYGMTESGPLGTV----LYPEEAVVKAGS 333
Cdd:cd05910 182 -ALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDEaEILTPYGATEALPVSSIgsreLLATTTAATSGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 334 IGRC---AIPGVELEV--------RRQDGSLC-SSGEVGEICLRSAAMMQGYLDNREATA-AVLDDQG---WYRSGDLAR 397
Cdd:cd05910 261 AGTCvgrPIPGVRVRIieiddepiAEWDDTLElPRGEIGEITVTGPTVTPTYVNRPVATAlAKIDDNSegfWHRMGDLGY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 398 VDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLkPGKTLVHEDLRQFMETR 477
Cdd:cd05910 341 LDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPL-PGTITPRARLEQELRAL 419
|
....
gi 502603069 478 LARY 481
Cdd:cd05910 420 AKDY 423
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
160-507 |
3.74e-20 |
|
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: 93.32 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 PHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLM--REY 237
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMptRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 238 A--PREFLETLAQERISFT----FGAP--IAFLAPLSvvpdVASYDFSAMRLWAYGGGPLGADMARKLAQ---VYRSDR- 305
Cdd:cd05908 185 IrrPILWLKKASEHKATIVsspnFGYKyfLKTLKPEK----ANDWDLSSIRMILNGAEPIDYELCHEFLDhmsKYGLKRn 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 306 -FMQVYGMTESG----------PLGTVLY---------PEEAVVKAGSigRCAI------PGVELEVR--RQDGSLCSSG 357
Cdd:cd05908 261 aILPVYGLAEASvgaslpkaqsPFKTITLgrrhvthgePEPEVDKKDS--ECLTfvevgkPIDETDIRicDEDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 358 EVGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVdEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQ 437
Cdd:cd05908 339 YIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVE 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502603069 438 --DVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRLARYKIPRIFEVR--DTLPRTATGKLLKHMLR 507
Cdd:cd05908 418 lgRVVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGWQINEVLpiRRIPKTTSGKVKRYELA 491
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
29-506 |
4.26e-18 |
|
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: 86.76 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGa 108
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 109 raslitaiqaepqpLADIQWLSTASATEGLDcfdellaqaapcgdehgRPAPHALAEILYTSGTTGQPKGCLHSHA---- 184
Cdd:cd17654 97 --------------ELDNAPLSFTPEHRHFN-----------------IRTDECLAYVIHTSGTTGTPKIVAVPHKcilp 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 185 NVFHAALCAAAATslaptERTLIAMPIWHSSPLNNWFLGTLLMGGTAVLMR---EYAPREFLETLAQERISFTFGAPIAF 261
Cdd:cd17654 146 NIQHFRSLFNITS-----EDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPtsvKVLPSKLADILFKRHRITVLQATPTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 262 LAPLSVVpDVASYDFSA---MRLWAYGGGPLGADMARK-LAQVYRSDRFMQVYGMTESGPLGTV--LYPEEAVVKAGSig 335
Cdd:cd17654 221 FRRFGSQ-SIKSTVLSAtssLRVLALGGEPFPSLVILSsWRGKGNRTRIFNIYGITEVSCWALAykVPEEDSPVQLGS-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 336 rcAIPGVELEVRRQDGSlCSSGEVGEICLRSAAMMQGYLDNREATaavlddqgWYRSGDLARVdEDGYLYIVDRLKDMIV 415
Cdd:cd17654 298 --PLLGTVIEVRDQNGS-EGTGQVFLGGLNRVCILDDEVTVPKGT--------MRATGDFVTV-KDGELFFLGRKDSQIK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 416 TGGENVYSKEVEDVLCTHSDVQDVAVIgrphpeW--GETVVAVLTLKPGKTLVHEDLRQFMetrLARYKIPRIFEVRDTL 493
Cdd:cd17654 366 RRGKRINLDLIQQVIESCLGVESCAVT------LsdQQRLIAFIVGESSSSRIHKELQLTL---LSSHAIPDTFVQIDKL 436
|
490
....*....|...
gi 502603069 494 PRTATGKLLKHML 506
Cdd:cd17654 437 PLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-501 |
4.63e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 88.30 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 4 FISLLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPIN 83
Cdd:PRK05691 3722 YVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLD 3801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 84 HKLQAPEVSYILRHSGARLCLVDGARASLITAIQAEpqpladiqwlSTASATEGLDCFDELLAQAAPCGDEHGRPAPHAL 163
Cdd:PRK05691 3802 PGLPAQRLQRIIELSRTPVLVCSAACREQARALLDE----------LGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNL 3871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 164 AEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLapTERTLIAMPIWHSSPLNNW-FLGTLLMGGTAVLMRE---YAP 239
Cdd:PRK05691 3872 AYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLAL--SEADVIAQTASQSFDISVWqFLAAPLFGARVEIVPNaiaHDP 3949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 240 REFLETLAQERISFTFGAPIAFLAPLSvvPDVASYDfsAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPlG 319
Cdd:PRK05691 3950 QGLLAHVQAQGITVLESVPSLIQGMLA--EDRQALD--GLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSD-D 4024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 320 TVLYPEEAVVKAGSIGRCAIP--GVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVL-------DDQGWY 390
Cdd:PRK05691 4025 VAFFRVDLASTRGSYLPIGSPtdNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLY 4104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 391 RSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEwGETVVAVLT-----LKPGKTL 465
Cdd:PRK05691 4105 RTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVN-GKHLVGYLVphqtvLAQGALL 4183
|
490 500 510
....*....|....*....|....*....|....*.
gi 502603069 466 vhEDLRQFMETRLARYKIPRIFEVRDTLPRTATGKL 501
Cdd:PRK05691 4184 --ERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKL 4217
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
158-510 |
8.03e-18 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 86.36 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 158 PAPHALAEILY-TSGTTGQPKGCLHSHANVFH-AALCAAAATSLAPTERTLIAMPIWHSSPLNnwFLGTLLMGGTAVLMR 235
Cdd:PRK05851 148 PPDSGGPAVLQgTAGSTGTPRTAILSPGAVLSnLRGLNARVGLDAATDVGCSWLPLYHDMGLA--FLLTAALAGAPLWLA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 236 -----EYAPREFLETLAQERISFTFGAPIAFlaplSV-------VPDVasyDFSAMRLWAYGGGPLGAD----MARKLAQ 299
Cdd:PRK05851 226 pttafSASPFRWLSWLSDSRATLTAAPNFAY----NLigkyarrVSDV---DLGALRVALNGGEPVDCDgferFATAMAP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 300 V-YRSDRFMQVYGMTES-------GPlGTVLYPEEAVVKAGSIGR------CAIPGVELEVRRQDGSLCSSG-EVGEICL 364
Cdd:PRK05851 299 FgFDAGAAAPSYGLAEStcavtvpVP-GIGLRVDEVTTDDGSGARrhavlgNPIPGMEVRISPGDGAAGVAGrEIGEIEI 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 365 RSAAMMQGYLDnreatAAVLDDQGWYRSGDLARVDEDGyLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAvigr 444
Cdd:PRK05851 378 RGASMMSGYLG-----QAPIDPDDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGA---- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 445 phpewgetVVAVLT----LKPGKTLVHE----DL---RQFMETRLARY--KIPR--IFEVRDTLPRTATGKL----LKHM 505
Cdd:PRK05851 448 --------VVAVGTgegsARPGLVIAAEfrgpDEagaRSEVVQRVASEcgVVPSdvVFVAPGSLPRTSSGKLrrlaVKRS 519
|
....*
gi 502603069 506 LRGST 510
Cdd:PRK05851 520 LEAAD 524
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
4-500 |
8.74e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 86.94 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 4 FISLLDQQARTRPEKLALR-ADGQDWSYAALAQAgrraATVL---YEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVV 79
Cdd:PRK06814 634 FEALIEAAKIHGFKKLAVEdPVNGPLTYRKLLTG----AFVLgrkLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVP 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 80 VPINHKLQAPEVSYILRHSGARLCL-----VDGARAS-LITAIQAEpqplADIQWLSTASATEGL-DCFDELLAQAAPcG 152
Cdd:PRK06814 710 AMINFSAGIANILSACKAAQVKTVLtsrafIEKARLGpLIEALEFG----IRIIYLEDVRAQIGLaDKIKGLLAGRFP-L 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 153 DEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAV 232
Cdd:PRK06814 785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVF 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 233 LmreY-APREFleTLAQERISFTfGAPI-----AFLAPLSVVPDvaSYDFSAMRLWAYGGGPLGADMARKLAQVYRSdRF 306
Cdd:PRK06814 865 L---YpSPLHY--RIIPELIYDT-NATIlfgtdTFLNGYARYAH--PYDFRSLRYVFAGAEKVKEETRQTWMEKFGI-RI 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 307 MQVYGMTESGPLGTVLYPeeAVVKAGSIGRcAIPGVELEVRRQDGslCSSGevGEICLRSAAMMQGYLdnREATAAVLD- 385
Cdd:PRK06814 936 LEGYGVTETAPVIALNTP--MHNKAGTVGR-LLPGIEYRLEPVPG--IDEG--GRLFVRGPNVMLGYL--RAENPGVLEp 1006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 386 -DQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTlkpGKT 464
Cdd:PRK06814 1007 pADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILLTT---ASD 1083
|
490 500 510
....*....|....*....|....*....|....*..
gi 502603069 465 LVHEDLRQFMETR-LARYKIPRIFEVRDTLPRTATGK 500
Cdd:PRK06814 1084 ATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGK 1120
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
42-474 |
2.06e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 85.25 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 42 TVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLV-----------DGARA 110
Cdd:PLN02430 91 SALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqdkkikellepDCKSA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 111 SLITAIQAEPQPLADiqwLSTASATEGLDCF--DELLAQAAPCGDEHGRPAPHALAEILYTSGTTGQPKGCLHSHANVFH 188
Cdd:PLN02430 171 KRLKAIVSFTSVTEE---ESDKASQIGVKTYswIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVAT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 189 AALCAAAATSLAPTERT-----LIAMPIWH--SSPLNNWFL------------------------GTLLMGGTAVLMREY 237
Cdd:PLN02430 248 FVRGVDLFMEQFEDKMThddvyLSFLPLAHilDRMIEEYFFrkgasvgyyhgdlnalrddlmelkPTLLAGVPRVFERIH 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 238 aprEFLETLAQE---RISFTFGA-------------------PIA-FLAPLSVVPDVASydfsAMRLWAYGGGPLGADMA 294
Cdd:PLN02430 328 ---EGIQKALQElnpRRRLIFNAlykyklawmnrgyshkkasPMAdFLAFRKVKAKLGG----RLRLLISGGAPLSTEIE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 295 RKLaQVYRSDRFMQVYGMTESGPLGTVLYPEEAVVkagsIGRCAIPGVELEVRRQDGSLCSS---GE--VGEICLRSAAM 369
Cdd:PLN02430 401 EFL-RVTSCAFVVQGYGLTETLGPTTLGFPDEMCM----LGTVGAPAVYNELRLEEVPEMGYdplGEppRGEICVRGKCL 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 370 MQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMI-VTGGENVYSKEVEDVLCTHSDVQDVAVIGRphpE 448
Cdd:PLN02430 476 FSGYYKNPELTEEVMKD-GWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPIVEDIWVYGD---S 551
|
490 500
....*....|....*....|....*.
gi 502603069 449 WGETVVAVLTLKPGKTLVHEDLRQFM 474
Cdd:PLN02430 552 FKSMLVAVVVPNEENTNKWAKDNGFT 577
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
160-505 |
2.30e-17 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 85.15 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 PHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLgTLLMGGTAVLMreY-A 238
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLF-TPLLTGAEVFL--YpS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 239 P---REFLETLAQERISFTFGAPiAFLAPLSVVPDvaSYDFSAMRLWAYGGGPLgADMARKLAQVYRSDRFMQVYGMTES 315
Cdd:PRK08043 441 PlhyRIVPELVYDRNCTVLFGTS-TFLGNYARFAN--PYDFARLRYVVAGAEKL-QESTKQLWQDKFGLRILEGYGVTEC 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 316 GPLGTVLYPEEAvvKAGSIGR---------CAIPGVElevrrqDGslcssgevGEICLRSAAMMQGYLdnREATAAVLD- 385
Cdd:PRK08043 517 APVVSINVPMAA--KPGTVGRilpgmdarlLSVPGIE------QG--------GRLQLKGPNIMNGYL--RVEKPGVLEv 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 386 ----------DQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDV-LCTHSDVQDVAVIgRPHPEWGETVV 454
Cdd:PRK08043 579 ptaenargemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAI-KSDASKGEALV 657
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 502603069 455 AVLTlkpGKTLVHEDLRQFM-ETRLARYKIPRIFEVRDTLPRTATGK----LLKHM 505
Cdd:PRK08043 658 LFTT---DSELTREKLQQYArEHGVPELAVPRDIRYLKQLPLLGSGKpdfvTLKSM 710
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
160-500 |
2.23e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 81.79 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 PHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLGTLLMGGTAVL-MREYA 238
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFaYNPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 239 PREFLETLAQERISFTFGAPIAFLAPLSVVPDVASyDFSAMRLWAYGGGPLGADMARKLAQVYRSDRFMQVYGMTESGPL 318
Cdd:PRK06334 262 PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQES-CLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 319 GTVlypeeAVVKAGSIGRCA---IPGVE-LEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAV-LDDQGWYRSG 393
Cdd:PRK06334 341 ITI-----NTVNSPKHESCVgmpIRGMDvLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYVTG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 394 DLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVL---CTHSDVQD---VAVIGRPhpewGETV-VAVLTLKPgkTLV 466
Cdd:PRK06334 416 DLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILmegFGQNAADHagpLVVCGLP----GEKVrLCLFTTFP--TSI 489
|
330 340 350
....*....|....*....|....*....|....*.
gi 502603069 467 HE--DLRQFMETRlARYKIPRIFEVrDTLPRTATGK 500
Cdd:PRK06334 490 SEvnDILKNSKTS-SILKISYHHQV-ESIPMLGTGK 523
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
21-424 |
2.63e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 81.68 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 21 LRADGQ--DWSYAALAQAG-RRAA--TVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYIL 95
Cdd:PLN02736 67 IRVDGTvgEYKWMTYGEAGtARTAigSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 96 RH--------SGARL-----CLVDGARASLITAIQAEPQPLAdiqwlSTASATE-GLDCFDELLAQAAPCGDEHGRPAPH 161
Cdd:PLN02736 147 NHaevaaifcVPQTLntllsCLSEIPSVRLIVVVGGADEPLP-----SLPSGTGvEIVTYSKLLAQGRSSPQPFRPPKPE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 162 ALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLNNWFLgtLLMGGTAV--------- 232
Cdd:PLN02736 222 DVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIV--MLHYGVAVgfyqgdnlk 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 233 LMREYA----------PRefLETLAQERISFTFGAP---------IAFLAP----LSVVPDVASYD---FSA-------- 278
Cdd:PLN02736 300 LMDDLAalrptifcsvPR--LYNRIYDGITNAVKESgglkerlfnAAYNAKkqalENGKNPSPMWDrlvFNKikaklggr 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 279 MRLWAYGGGPLGADMARKLaQVYRSDRFMQVYGMTESGPLGTVLYPEEAvvkagSIGRCAIPGVELEVRrqdgsLCSSGE 358
Cdd:PLN02736 378 VRFMSSGASPLSPDVMEFL-RICFGGRVLEGYGMTETSCVISGMDEGDN-----LSGHVGSPNPACEVK-----LVDVPE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 359 V-----------GEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMI-VTGG-------- 418
Cdd:PLN02736 447 MnytsedqpyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGeyiapeki 526
|
....*.
gi 502603069 419 ENVYSK 424
Cdd:PLN02736 527 ENVYAK 532
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
166-506 |
3.41e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 78.24 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAmpiwHSS----PLNNWFLGTLLMGGTAVLMR------ 235
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFS----HSSigwvSFHGFLYGSLSLGNTFVMFEggiikn 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 236 EYAPREFLETLAQERISFTFGAPIAFLAPLSVVPDV----ASYDFSAMRLWAYGGGPLGADMARKLAQVYRSdRFMQVYG 311
Cdd:PTZ00237 335 KHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEAtiirSKYDLSNLKEIWCGGEVIEESIPEYIENKLKI-KSSRGYG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 312 MTESGPlgTVLYPEEAVVKagSIGRCAIPGVELE--VRRQDGSLCSSGEVGEICLR---SAAMMQGYLDNREATAAVLDD 386
Cdd:PTZ00237 414 QTEIGI--TYLYCYGHINI--PYNATGVPSIFIKpsILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSK 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 387 -QGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTL 465
Cdd:PTZ00237 490 fPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSN 569
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502603069 466 VHEDLRQF-------METRLARYKIPRIFEVRDTLPRTATGKLLKHML 506
Cdd:PTZ00237 570 QSIDLNKLkneinniITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
13-500 |
6.20e-15 |
|
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: 77.31 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 13 RTRPEKLALRADG----QDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAV---------- 78
Cdd:cd05943 80 ADADDPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIwsscspdfgv 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 79 ------VVPINHKL--QAPEVSYilrhSGARLClvdgaRASLITAIQAEPQPLADIQWLSTASATEGLDC--------FD 142
Cdd:cd05943 160 pgvldrFGQIEPKVlfAVDAYTY----NGKRHD-----VREKVAELVKGLPSLLAVVVVPYTVAAGQPDLskiakaltLE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 143 ELLAQAAPCGDEHGR-PAPHALAeILYTSGTTGQPKGCLHSHANVF--HaALCAAAATSLAPTERTLiampiWHSSP--- 216
Cdd:cd05943 231 DFLATGAAGELEFEPlPFDHPLY-ILYSSGTTGLPKCIVHGAGGTLlqH-LKEHILHCDLRPGDRLF-----YYTTCgwm 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 217 LNNWFLGTLLMGGTAVLMREYAPREFLETL----AQERISFtFGAPIAFLAPLS---VVPdVASYDFSAMRLWAYGGGPL 289
Cdd:cd05943 304 MWNWLVSGLAVGATIVLYDGSPFYPDTNALwdlaDEEGITV-FGTSAKYLDALEkagLKP-AETHDLSSLRTILSTGSPL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 290 GADMARKLAQVYRSDRFMQVY-GMTESGP---LGTVLYPeeavVKAGSIgRCAIPGVELEVRRQDG-SLcsSGEVGE-IC 363
Cdd:cd05943 382 KPESFDYVYDHIKPDVLLASIsGGTDIIScfvGGNPLLP----VYRGEI-QCRGLGMAVEAFDEEGkPV--WGEKGElVC 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 364 LRSAAMMQGYLDN-------REATAAVLDdqGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDV 436
Cdd:cd05943 455 TKPFPSMPVGFWNdpdgsryRAAYFAKYP--GVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEV 532
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502603069 437 QDVAVIGRPHPEWGETVVAVLTLKPGKTLVHE---DLRQFMETRLARYKIP-RIFEVRDtLPRTATGK 500
Cdd:cd05943 533 EDSLVVGQEWKDGDERVILFVKLREGVELDDElrkRIRSTIRSALSPRHVPaKIIAVPD-IPRTLSGK 599
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
44-411 |
8.64e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 77.32 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 44 LYEQGVRQGDKLGL--------LCfntpgfvfALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGAR-ASLIT 114
Cdd:PTZ00216 138 LAELGLTKGSNVAIyeetrwewLA--------SIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNvPNLLR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 115 AIQAEPQPLADIQWLSTASA---TEGLD--CFDELLAQAAPCGDEHGRPAP---HALAEILYTSGTTGQPKGCLHSHANV 186
Cdd:PTZ00216 210 LMKSGGMPNTTIIYLDSLPAsvdTEGCRlvAWTDVVAKGHSAGSHHPLNIPennDDLALIMYTSGTTGDPKGVMHTHGSL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 187 FHAALCAAAATS-----LAPTERTLIAMPIWHSSPLN--NWFL--GTLLMGGTavlmreyaPREFLET-------LAQER 250
Cdd:PTZ00216 290 TAGILALEDRLNdligpPEEDETYCSYLPLAHIMEFGvtNIFLarGALIGFGS--------PRTLTDTfarphgdLTEFR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 251 ISFTFGAPIAF-----------------------------LAPLSVVPDVASYD---FSA--------MRLWAYGGGPLG 290
Cdd:PTZ00216 362 PVFLIGVPRIFdtikkaveaklppvgslkrrvfdhayqsrLRALKEGKDTPYWNekvFSApravlggrVRAMLSGGGPLS 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 291 ADMARKLAQVYrsDRFMQVYGMTESGPLGTVLYPEEavVKAGSIGRcAIPGVELEvrrqdgsLCSSGEV---------GE 361
Cdd:PTZ00216 442 AATQEFVNVVF--GMVIQGWGLTETVCCGGIQRTGD--LEPNAVGQ-LLKGVEMK-------LLDTEEYkhtdtpeprGE 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 502603069 362 ICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLK 411
Cdd:PTZ00216 510 ILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
8-503 |
1.32e-14 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 76.53 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 8 LDQQARTRPEKLALRA----DGQD--WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAV--V 79
Cdd:PRK10524 59 VDRHLAKRPEQLALIAvsteTDEErtYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 80 VP---INHKL-----QAPEVSYILRHSGARLCLVDGARASLITAI-QAEPQP----LADIQwLSTASATEGLDC-FDELL 145
Cdd:PRK10524 139 VFggfASHSLaaridDAKPVLIVSADAGSRGGKVVPYKPLLDEAIaLAQHKPrhvlLVDRG-LAPMARVAGRDVdYATLR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 146 AQ----AAPCG-DEHGRPAphalaEILYTSGTTGQPKGCLH-----------SHANVFhaalcaaaatSLAPTERTLIAM 209
Cdd:PRK10524 218 AQhlgaRVPVEwLESNEPS-----YILYTSGTTGKPKGVQRdtggyavalatSMDTIF----------GGKAGETFFCAS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 210 PI-W---HS----SPLnnwflgtllMGGTAVLMREYAPRE-----FLETLAQERISFTFGAPIAFLAPLSVVPD-VASYD 275
Cdd:PRK10524 283 DIgWvvgHSyivyAPL---------LAGMATIMYEGLPTRpdagiWWRIVEKYKVNRMFSAPTAIRVLKKQDPAlLRKHD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 276 FSAMRLWAYGGGPLGADMARKLAQVYRS---DRFMQvygmTESG-PLGTVLYPEEAV-VKAGSIGRcAIPGVELEVRRQ- 349
Cdd:PRK10524 354 LSSLRALFLAGEPLDEPTASWISEALGVpviDNYWQ----TETGwPILAIARGVEDRpTRLGSPGV-PMYGYNVKLLNEv 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 350 DGSLCSSGEVGEICLRS----AAMMQGYLDNRE--ATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYS 423
Cdd:PRK10524 429 TGEPCGPNEKGVLVIEGplppGCMQTVWGDDDRfvKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGT 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 424 KEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLVHEDLRQFMETRL-----------ARykiP-RIFEVrD 491
Cdd:PRK10524 509 REIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLALEKEImalvdsqlgavAR---PaRVWFV-S 584
|
570
....*....|..
gi 502603069 492 TLPRTATGKLLK 503
Cdd:PRK10524 585 ALPKTRSGKLLR 596
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
15-508 |
1.89e-14 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 75.99 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 15 RPEKLALRADGQD-----WSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAV---------VV 80
Cdd:PRK03584 97 RDDRPAIIFRGEDgprreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIwsscspdfgVQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 81 PINHKLQ--APEVsyilrhsgarLCLVDG--------ARASLITAIQAEPQPLADIQWLS------TASATEGLDCFDEL 144
Cdd:PRK03584 177 GVLDRFGqiEPKV----------LIAVDGyryggkafDRRAKVAELRAALPSLEHVVVVPylgpaaAAAALPGALLWEDF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 145 LAQAAPCGDEHGR-PAPHALAeILYTSGTTGQPKGCLHSHANV---------FHaalcaaaaTSLAPTERTLiampiWHS 214
Cdd:PRK03584 247 LAPAEAAELEFEPvPFDHPLW-ILYSSGTTGLPKCIVHGHGGIllehlkelgLH--------CDLGPGDRFF-----WYT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 215 SP---LNNWFLGTLLMGGTAVLmreY-------APREFLETLAQERISFtFGAPIAFLAPLS---VVPdVASYDFSAMRL 281
Cdd:PRK03584 313 TCgwmMWNWLVSGLLVGATLVL---YdgspfypDPNVLWDLAAEEGVTV-FGTSAKYLDACEkagLVP-GETHDLSALRT 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 282 WAYGGGPLGADMARKLAQVYRSDrfMQVYGMteSG--------PLGTVLYPeeavVKAGSIgRCAIPGVELEVRRQDG-S 352
Cdd:PRK03584 388 IGSTGSPLPPEGFDWVYEHVKAD--VWLASI--SGgtdicscfVGGNPLLP----VYRGEI-QCRGLGMAVEAWDEDGrP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 353 LcsSGEVGE-ICLRSAAMMQGYLDNreataavlDDQG-WYRS------------GDLARVDEDGYLYIVDRLKDMIVTGG 418
Cdd:PRK03584 459 V--VGEVGElVCTKPFPSMPLGFWN--------DPDGsRYRDayfdtfpgvwrhGDWIEITEHGGVVIYGRSDATLNRGG 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 419 ------EnVYSkEVEDVlcthSDVQDVAVIGRPHPEWGETVVAVLTLKPGKTLvHEDLRQFMETRLARYKIPR-----IF 487
Cdd:PRK03584 529 vrigtaE-IYR-QVEAL----PEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTL-DDALRARIRTTIRTNLSPRhvpdkII 601
|
570 580
....*....|....*....|....*
gi 502603069 488 EVRDtLPRTATGKLL----KHMLRG 508
Cdd:PRK03584 602 AVPD-IPRTLSGKKVelpvKKLLHG 625
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
48-443 |
1.87e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 72.75 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 48 GVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGARASLItaIQAEPQplaDIQ 127
Cdd:PLN02614 100 GVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISEL--FKTCPN---STE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 128 WLSTASATEGLD---------------CFDELLAQAApcGDEHGRP--APHALAEILYTSGTTGQPKGCLHSH------- 183
Cdd:PLN02614 175 YMKTVVSFGGVSreqkeeaetfglviyAWDEFLKLGE--GKQYDLPikKKSDICTIMYTSGTTGDPKGVMISNesivtli 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 184 ANVFHAALCAAAATSLAPT-----------ERTLIAMPIWHSSPLNNW-------------FLGTLLMGGTAVLMREYAP 239
Cdd:PLN02614 253 AGVIRLLKSANAALTVKDVylsylplahifDRVIEECFIQHGAAIGFWrgdvklliedlgeLKPTIFCAVPRVLDRVYSG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 240 RE--------FLETLAQERISFTFGAPIAFLAPLSVVPDVASYDFSAM--------RLWAYGGGPLGADMARKLaQVYRS 303
Cdd:PLN02614 333 LQkklsdggfLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVkqglggnvRIILSGAAPLASHVESFL-RVVAC 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 304 DRFMQVYGMTESGPLGTVLYPEEaVVKAGSIGRcAIPGVELE---VRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREAT 380
Cdd:PLN02614 412 CHVLQGYGLTESCAGTFVSLPDE-LDMLGTVGP-PVPNVDIRlesVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLT 489
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502603069 381 AAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMI-VTGGENVYSKEVEDVLCTHSDVQDVAVIG 443
Cdd:PLN02614 490 KEVLID-GWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVYG 552
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
166-507 |
3.95e-13 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 71.85 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 166 ILYTSGTTGQPKGCLHSHAN-VFHAALCAAAATSLAPTErtliampIWHSSPLNNWFLGTL------LMGGTAVLMREYA 238
Cdd:PLN02654 280 LLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTD-------VYWCTADCGWITGHSyvtygpMLNGATVLVFEGA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 239 PR-----EFLETLAQERISFTFGAPIAFLAPLSVVPD-VASYDFSAMRLWAYGGGPLGADMARKLAQVYRSDR--FMQVY 310
Cdd:PLN02654 353 PNypdsgRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEyVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRcpISDTW 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 311 GMTESGPLGTVLYPEEAVVKAGSigrCAIP--GVELEVRRQDGSLCSSGEVGEICLRSA---AMMQGYLDN-REATAAVL 384
Cdd:PLN02654 433 WQTETGGFMITPLPGAWPQKPGS---ATFPffGVQPVIVDEKGKEIEGECSGYLCVKKSwpgAFRTLYGDHeRYETTYFK 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 385 DDQGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEWGETVVAVLTLKPGKT 464
Cdd:PLN02654 510 PFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVP 589
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 502603069 465 LvHEDLRQFM----ETRLARYKIPRIFEVRDTLPRTATGKLLKHMLR 507
Cdd:PLN02654 590 Y-SEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
33-462 |
1.69e-12 |
|
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: 69.68 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 33 LAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARL------CLVD 106
Cdd:cd05905 21 LSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRValtveaCLKG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 107 GARASLITAIQAE-PQPLA--DIQWLSTASATEGldcFDELLAQAapcgdeHGRPAPHALAEILYTSGTTGQPKGCLHSH 183
Cdd:cd05905 101 LPKKLLKSKTAAEiAKKKGwpKILDFVKIPKSKR---SKLKKWGP------HPPTRDGDTAYIEYSFSSDGSLSGVAVSH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 184 ANVFHAALCAAAATSLAPTERTLIAMPiwHSSPLNNWfLGTLL--MGGTAVLMREYA-----PREFLETLAQERISFTFG 256
Cdd:cd05905 172 SSLLAHCRALKEACELYESRPLVTVLD--FKSGLGLW-HGCLLsvYSGHHTILIPPElmktnPLLWLQTLSQYKVRDAYV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 257 A----PIAFLAPLSVVP--DVASYDFSAMR--LWAYGGGPlgadmarklaQVYRSDRFMQVYG----------------- 311
Cdd:cd05905 249 KlrtlHWCLKDLSSTLAslKNRDVNLSSLRmcMVPCENRP----------RISSCDSFLKLFQtlglspravstefgtrv 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 312 ------MTESGPLGTVLYPEEAVVKAGSIgRCA----------------IPGVELEVRRQDGS-LCSSGEVGEICLRSAA 368
Cdd:cd05905 319 npficwQGTSGPEPSRVYLDMRALRHGVV-RLDerdkpnslplqdsgkvLPGAQVAIVNPETKgLCKDGEIGEIWVNSPA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 369 MMQGY----------LDNREAT--AAVLDDQGWYRSGDL----------ARVDEDGYLYIVDRLKDMIVTGGENVYSKEV 426
Cdd:cd05905 398 NASGYflldgetndtFKVFPSTrlSTGITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRHHPSDI 477
|
490 500 510
....*....|....*....|....*....|....*..
gi 502603069 427 ED-VLCTHSDVQDVAVIgrphpEWGETVVAVLTLKPG 462
Cdd:cd05905 478 EAtVMRVHPYRGRCAVF-----SITGLVVVVAEQPPG 509
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
29-443 |
1.58e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 63.71 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 29 SYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVPINHKLQAPEVSYILRHSGARLCLVDGA 108
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 109 RASLITAIQAEPQP-LADIQWLSTASATE-------GLDCFD-ELLAQAAPCGDEHGRPAPHALAEILYTSGTTGQPKGC 179
Cdd:PLN02861 159 KISSILSCLPKCSSnLKTIVSFGDVSSEQkeeaeelGVSCFSwEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 180 LHSH----ANVFHAALCAAAATSLAPTERTLIA-MPIWH--SSPLNNWFLGT-----LLMGGTAVLMREY---------- 237
Cdd:PLN02861 239 ILTNraiiAEVLSTDHLLKVTDRVATEEDSYFSyLPLAHvyDQVIETYCISKgasigFWQGDIRYLMEDVqalkptifcg 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 238 APREF--LETLAQERIS---------FTF-----------GAPIAFLAPL--SVVPDVASYDFSA-MRLWAYGGGPLGAD 292
Cdd:PLN02861 319 VPRVYdrIYTGIMQKISsggmlrkklFDFaynyklgnlrkGLKQEEASPRldRLVFDKIKEGLGGrVRLLLSGAAPLPRH 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 293 MARKLaQVYRSDRFMQVYGMTES-GPLGTVLYPEEAVVkaGSIGrcaIPGVELEVRRQD-----GSLCSSGEVGEICLRS 366
Cdd:PLN02861 399 VEEFL-RVTSCSVLSQGYGLTEScGGCFTSIANVFSMV--GTVG---VPMTTIEARLESvpemgYDALSDVPRGEICLRG 472
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502603069 367 AAMMQGYLDNREATAAVLDDqGWYRSGDLARVDEDGYLYIVDRLKDMI-VTGGENVYSKEVEDVLCTHSDVQDVAVIG 443
Cdd:PLN02861 473 NTLFSGYHKRQDLTEEVLID-GWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIASIWVYG 549
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
3-427 |
1.27e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.51 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 3 NFISLLDQQARTRPEKLALR-------ADG--QDWSYAALAQAGRRAATVLyEQGVRQGDKLGLLCFNTPGFVFALLGAW 73
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAYRfldfsteRDGvaRDLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 74 RLGAVVVPinhkLQAPEVSyilRHSGaRLCLV-DGARASLItaiqaepqpladiqwLSTASATEGL-DCFDELLAQAAP- 150
Cdd:PRK07769 101 YAGRIAVP----LFDPAEP---GHVG-RLHAVlDDCTPSAI---------------LTTTDSAEGVrKFFRARPAKERPr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 151 ----------CGDEHGRPAPH--ALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIAMPIWHSSPLN 218
Cdd:PRK07769 158 viavdavpdeVGATWVPPEANedTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 219 NWFLGTLLmGGTAVLMREYA----PREFLETLAQER--ISFTFG-AP-IAF-LAPLSVVP--DVASYDFSAMRLWAYGGG 287
Cdd:PRK07769 238 TVLLPALL-GHYITFMSPAAfvrrPGRWIRELARKPggTGGTFSaAPnFAFeHAAARGLPkdGEPPLDLSNVKGLLNGSE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 288 PLGADMARKLAQVYRSDRFMQV-----YGMTE------SGPL---GTVLY-----------------PEEAVVKAgSIGR 336
Cdd:PRK07769 317 PVSPASMRKFNEAFAPYGLPPTaikpsYGMAEatlfvsTTPMdeePTVIYvdrdelnagrfvevpadAPNAVAQV-SAGK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 337 CAIPGVELEVRRQDGSLCSSGEVGEICLRSAAMMQGYLDNREATAAVL-----------------DDQGWYRSGDLArVD 399
Cdd:PRK07769 396 VGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRTGDYG-VY 474
|
490 500
....*....|....*....|....*...
gi 502603069 400 EDGYLYIVDRLKDMIVTGGENVYSKEVE 427
Cdd:PRK07769 475 FDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
158-445 |
1.89e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 60.13 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 158 PAPHALAEILYTSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLIA-MPIWHssplnnwflgtllmggtavlmre 236
Cdd:PLN02387 247 PSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAyLPLAH----------------------- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 237 yapreFLEtLAQERISFTFGAPIAFLAPLSV-------------------------VPDVAS------------------ 273
Cdd:PLN02387 304 -----ILE-LAAESVMAAVGAAIGYGSPLTLtdtsnkikkgtkgdasalkptlmtaVPAILDrvrdgvrkkvdakgglak 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 274 --YDFS-AMRLWAYGGGPLGADMARKL---AQVYR-----------------------SDRFM---------QVYGMTES 315
Cdd:PLN02387 378 klFDIAyKRRLAAIEGSWFGAWGLEKLlwdALVFKkiravlggrirfmlsggaplsgdTQRFIniclgapigQGYGLTET 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 316 GPLGTVLYPEEAvvkagSIGRCAIP----GVELEVRRQDGSLCSSGEV--GEICLRSAAMMQGYLDNREATAAV--LDDQ 387
Cdd:PLN02387 458 CAGATFSEWDDT-----SVGRVGPPlpccYVKLVSWEEGGYLISDKPMprGEIVIGGPSVTLGYFKNQEKTDEVykVDER 532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502603069 388 G--WYRSGDLARVDEDGYLYIVDRLKDMI-VTGGENVYSKEVEDVLCTHSDVQDVAVIGRP 445
Cdd:PLN02387 533 GmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAALSVSPYVDNIMVHADP 593
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
2-461 |
3.21e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 59.19 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 2 MNFISLLDQQARTRPEKLALR-AD-GQDWSYAA----LAQAGRRAATVLYEqgVRQ----GDKLGLLCFNTPGFVFALLG 71
Cdd:PRK05850 1 SSVPSLLRERASLQPDDAAFTfIDyEQDPAGVAetltWSQLYRRTLNVAEE--LRRhgstGDRAVILAPQGLEYIVAFLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 72 AWRLGAVVVPinhkLQAPE-------VSYILRHSGARLCLVDGARASLITAiQAEPQPLAdiqwlSTASATEgLDCFDeL 144
Cdd:PRK05850 79 ALQAGLIAVP----LSVPQggahderVSAVLRDTSPSVVLTTSAVVDDVTE-YVAPQPGQ-----SAPPVIE-VDLLD-L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 145 LAQAAPCGDEHGRPAPhalAEILYTSGTTGQPKGCLHSHANVFH-----AALCAAAATSLAPTERTLIA-MPIWHSSPLn 218
Cdd:PRK05850 147 DSPRGSDARPRDLPST---AYLQYTSGSTRTPAGVMVSHRNVIAnfeqlMSDYFGDTGGVPPPDTTVVSwLPFYHDMGL- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 219 nwFLG---TLLMGGTAVLMreyAPREFLE-------TLAQERISFTFGAPIAFlaPLSVV----PDVASYDFSAMRLWAY 284
Cdd:PRK05850 223 --VLGvcaPILGGCPAVLT---SPVAFLQrparwmqLLASNPHAFSAAPNFAF--ELAVRktsdDDMAGLDLGGVLGIIS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 285 GGGPLGADMARKLAqvyrsDRFMQV----------YGMTE------SGPLGTvlyPEEAV------VKAGSIGRCAI-PG 341
Cdd:PRK05850 296 GSERVHPATLKRFA-----DRFAPFnlretairpsYGLAEatvyvaTREPGQ---PPESVrfdyekLSAGHAKRCETgGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 342 VEL---------EVRRQDGSL---CSSGEVGEICLRSAAMMQGYLDNREAT----AAVLDD------QG-WYRSGDLARV 398
Cdd:PRK05850 368 TPLvsygsprspTVRIVDPDTcieCPAGTVGEIWVHGDNVAAGYWQKPEETertfGATLVDpspgtpEGpWLRTGDLGFI 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502603069 399 DeDGYLYIVDRLKDMIVTGGENVYSKEVEdvlcthSDVQD-----VAVIGRPHpEWGETVVAVLTLKP 461
Cdd:PRK05850 448 S-EGELFIVGRIKDLLIVDGRNHYPDDIE------ATIQEitggrVAAISVPD-DGTEKLVAIIELKK 507
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
344-512 |
1.10e-08 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 58.15 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 344 LEVRRQDGS-LCSSGEVGEICLRSAAMMQGYLDNREATAA------VLDDQGW----------------------YRSGD 394
Cdd:TIGR03443 605 LVVNRNDRTqTCGVGEVGEIYVRAGGLAEGYLGLPELNAEkfvnnwFVDPSHWidldkennkperefwlgprdrlYRTGD 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 395 LARVDEDGYLYIVDRLKDMIVTGG-------------------ENVY----SKEVEDVLCTH------SDVQDVAVIGRP 445
Cdd:TIGR03443 685 LGRYLPDGNVECCGRADDQVKIRGfrielgeidthlsqhplvrENVTlvrrDKDEEPTLVSYivpqdkSDELEEFKSEVD 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502603069 446 HPEWGETVVAvlTLKPGKTLVHeDLRQFMETRLARYKIPRIFEVRDTLPRTATGKLLKHMLRGSTTS 512
Cdd:TIGR03443 765 DEESSDPVVK--GLIKYRKLIK-DIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTA 828
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
7-498 |
2.85e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 56.65 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 7 LLDQQARTRPEKLALRADGQDWSYAALAQAGRRAATVLYEQGVRQGDKLGLLCFNTPGFVFALLGAWRLGAVVVpinhkL 86
Cdd:PRK07868 452 IIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAV-----L 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 87 QAP--EVSYILRHSGARLCLVDgaRASLITAIQAEPQPL----ADIQWLSTASATEGLDcfdelLAQAAPCGDEHG---R 157
Cdd:PRK07868 527 MPPdtDLAAAVRLGGVTEIITD--PTNLEAARQLPGRVLvlggGESRDLDLPDDADVID-----MEKIDPDAVELPgwyR 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 158 PAP---HALAEILY-TSGTTGQPKGCLHSHANVFHAALCAAAATSLAPTERTLiaMPIWHSSPLNNwFLGTLLMGGTAV- 232
Cdd:PRK07868 600 PNPglaRDLAFIAFsTAGGELVAKQITNYRWALSAFGTASAAALDRRDTVYCL--TPLHHESGLLV-SLGGAVVGGSRIa 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 233 LMREYAPREFLETLAQ---ERISFTFgapiAFLAPLSVVPDVASYDFSAMRLWAYGGGPLGadMARKLAQVYRSDRFMQV 309
Cdd:PRK07868 677 LSRGLDPDRFVQEVRQygvTVVSYTW----AMLREVVDDPAFVLHGNHPVRLFIGSGMPTG--LWERVVEAFAPAHVVEF 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 310 YGMTEsgplGTVLYPEEAVVKAGSIGRcAIPG---VELEVRRQDGSL-----------CSSGEVGEICLRSAAmmqgyld 375
Cdd:PRK07868 751 FATTD----GQAVLANVSGAKIGSKGR-PLPGagrVELAAYDPEHDLileddrgfvrrAEVNEVGVLLARARG------- 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 376 NREATAAVLDD-----QGWYRSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVLCTHSDVQDVAVIGRPHPEwG 450
Cdd:PRK07868 819 PIDPTASVKRGvfapaDTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGG-R 897
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502603069 451 ETVVAVLTLKPGKTLVHEDLRQFMEtRLARYKIPRIFEVRDTLPRTAT 498
Cdd:PRK07868 898 QLAVAAVTLRPGAAITAADLTEALA-SLPVGLGPDIVHVVPEIPLSAT 944
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
391-507 |
3.29e-08 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 56.24 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 391 RSGDLARVDEDGYLYIVDRLKDMIVTGGENVYSKEVEDVlC--THSDVQDVAVIGRPHPEWGE---TVVAVLTLKPGKTL 465
Cdd:PLN03052 592 RHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERV-CnaADESVLETAAIGVPPPGGGPeqlVIAAVLKDPPGSNP 670
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 502603069 466 VHEDLRQFMETRLARyKIPRIFEVRDT-----LPRTATGKLLKHMLR 507
Cdd:PLN03052 671 DLNELKKIFNSAIQK-KLNPLFKVSAVvivpsFPRTASNKVMRRVLR 716
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
160-423 |
4.16e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 55.88 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 160 PHALAEILYTSGTTGQPKGCLHSHANVFHAALCA---AAATSLAPT------------ERTLIAMPIWHSSPLNNW---- 220
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLckhSIFKKYNPKthlsylpishiyERVIAYLSFMLGGTINIWskdi 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 221 -FL--------GTLLMGGTAVLMREYA------------PREFLETLAQERISFTFGAPIAFLAPLS---------VVPD 270
Cdd:PTZ00342 383 nYFskdiynskGNILAGVPKVFNRIYTnimteinnlpplKRFLVKKILSLRKSNNNGGFSKFLEGIThisskikdkVNPN 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 271 vasydfsaMRLWAYGGGPLGADMARKLAqVYRSDRFMQVYGMTESGplGTVLYPEEAVVKAGSIGRCAIPGVELEVR--- 347
Cdd:PTZ00342 463 --------LEVILNGGGKLSPKIAEELS-VLLNVNYYQGYGLTETT--GPIFVQHADDNNTESIGGPISPNTKYKVRtwe 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 348 --RQDGSLCSsgevGEICLRSAAMMQGYLDNREATAAVLDDQGWYRSGDLARVDEDGYLYIVDRLKDMI-VTGGE----- 419
Cdd:PTZ00342 532 tyKATDTLPK----GELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEyietd 607
|
....*..
gi 502603069 420 ---NVYS 423
Cdd:PTZ00342 608 mlnNLYS 614
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
357-427 |
8.63e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.58 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 357 GEVGEICLRSAAMMQGYLDNREAT------------------AAVLDDQGWYRSGDLArVDEDGYLYIVDRLKDMIVTGG 418
Cdd:PRK12476 427 GEVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegshaDGAADDGTWLRTGDLG-VYLDGELYITGRIADLIVIDG 505
|
....*....
gi 502603069 419 ENVYSKEVE 427
Cdd:PRK12476 506 RNHYPQDIE 514
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
285-500 |
5.74e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 38.98 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 285 GGGPLGADMARKLAQVYRSDRFmQVYGMTESGPL---------GTVLyPEEAVVkagsigrcaipgVELeVRRQDGSLCS 355
Cdd:COG1541 211 GGEPWSEEMRKEIEERWGIKAY-DIYGLTEVGPGvayeceaqdGLHI-WEDHFL------------VEI-IDPETGEPVP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 356 SGEVGEICLrsaammqgyldnreaTAavLDDQGW----YRSGDLARVDEDG---------YLYIVDRLKDMIVTGGENVY 422
Cdd:COG1541 276 EGEEGELVV---------------TT--LTKEAMplirYRTGDLTRLLPEPcpcgrthprIGRILGRADDMLIIRGVNVF 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502603069 423 SKEVEDVLCTHSDVQD--VAVIGRPHpewGETVVAV-LTLKPGKTLvhEDLRQFMETRL-ARYKIPRIFEV--RDTLPRT 496
Cdd:COG1541 339 PSQIEEVLLRIPEVGPeyQIVVDREG---GLDELTVrVELAPGASL--EALAEAIAAALkAVLGLRAEVELvePGSLPRS 413
|
....
gi 502603069 497 aTGK 500
Cdd:COG1541 414 -EGK 416
|
|
| |
