|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-523 |
3.63e-172 |
|
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: 493.56 E-value: 3.63e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 4 LVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLN 83
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 84 PMYRKAELRHLVDDAGAVGIIcadtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverf 163
Cdd:COG0318 81 PRLTAEELAYILEDSGARALV----------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 164 rgatpeaaevsptdTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKD 243
Cdd:COG0318 102 --------------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 244 CTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAY 323
Cdd:COG0318 168 ATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 324 GMTETSsGVIAVPPDRRAPVDPASgalsIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPD 403
Cdd:COG0318 248 GLTETS-PVVTVNPEDPGERRPGS----VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 404 GRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE 483
Cdd:COG0318 323 GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDA 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2089408387 484 QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:COG0318 403 EELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALR 442
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
4-523 |
4.81e-160 |
|
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: 463.57 E-value: 4.81e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 4 LVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLN 83
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 84 PMYRKAELRHLVDDAGAVGIICADTavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddLVELVERF 163
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAVS-----------------------------------------------FTDLLAAG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 164 RGaTPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELA--RVDDGDVVLAVAPLFHITGAVINATIALM 241
Cdd:cd05936 114 AP-LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 242 KDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHN 321
Cdd:cd05936 193 LGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 322 AYGMTETSSGVIAVPPDRRapvdPASGalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF 401
Cdd:cd05936 273 GYGLTETSPVVAVNPLDGP----RKPG--SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEV 481
Cdd:cd05936 347 VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASL 426
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2089408387 482 TEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05936 427 TEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-523 |
8.94e-131 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 390.70 E-value: 8.94e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 1 MATLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAaal 80
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 81 VLNPM---YRKAELRHLVDDAGAVGIIcADTAVAENAETMQDS--TVRWIVGTSDLDfqtRNDPRVFGDRIRERHDGADD 155
Cdd:PRK06187 82 VLHPInirLKPEEIAYILNDAEDRVVL-VDSEFVPLLAAILPQlpTVRTVIVEGDGP---AAPLAPEVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 156 lvelverfrgaTPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHItGAVIN 235
Cdd:PRK06187 158 -----------TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHV-HAWGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 236 ATIALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKF 315
Cdd:PRK06187 226 PYLALMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 316 GHYIHNAYGMTETSSGVIAVPPDRRAPvDPASGALSIGMALPQVEIRVVDFDGTPLP--DGTQGELEIAGPQVVSGYWQK 393
Cdd:PRK06187 306 GIDLVQGYGMTETSPVVSVLPPEDQLP-GQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 394 PEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFV 473
Cdd:PRK06187 385 PEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2089408387 474 SLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK06187 465 VLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-525 |
2.25e-128 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 384.26 E-value: 2.25e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 1 MATLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAAL 80
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 81 VLNPMYRKAELRHLVDDAGAVGIICADTAVAENAETMQdstvrwivGTSDLDFQTRNDPRVFGDRIRERHDGADDLVELV 160
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATT--------RLPALEHVVICETEEDDPHTEKMKTFTDFLAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 161 ERFRgatpeAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITG--AVINAti 238
Cdd:PRK07656 156 PAER-----APEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGykAGVNA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 239 ALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFG-H 317
Cdd:PRK07656 229 PLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGvD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 318 YIHNAYGMTETSSGVIAVPPDRrapvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEAT 397
Cdd:PRK07656 309 IVLTGYGLSEASGVTTFNRLDD----DRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEAT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 398 AKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLV 476
Cdd:PRK07656 385 AAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLK 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2089408387 477 RDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNT 525
Cdd:PRK07656 465 PGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
11-519 |
8.51e-128 |
|
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: 380.03 E-value: 8.51e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 11 RVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAE 90
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 91 LRHLVDDAGAvgiicadtavaenaetmqdstvrwivgtsdldfqtrndpRVFGDrirerhdgaddlvelverfrgatpea 170
Cdd:cd17631 84 VAYILADSGA---------------------------------------KVLFD-------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 171 aevsptDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFAN 250
Cdd:cd17631 99 ------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFEnKFGHYIHNAYGMTETSS 330
Cdd:cd17631 173 KFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 331 GVIAVPPDrrapvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGD 410
Cdd:cd17631 252 GVTFLSPE-----DHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 411 VAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFV 490
Cdd:cd17631 327 LGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHC 406
|
490 500
....*....|....*....|....*....
gi 2089408387 491 GDRLAAYKRPKHIHIVDELPKTQTGKIRR 519
Cdd:cd17631 407 RERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
10-527 |
2.80e-123 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 372.37 E-value: 2.80e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 10 ARVAAN--PEHPAIAYFDGILSAREVDEMSDAFAVALVEK-GVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMY 86
Cdd:PRK08314 16 LEVSARryPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 87 RKAELRHLVDDAGAVGIICADTAVAENAETMQDSTVRWIVGTSDLDFQTRNDPRVFGDRIRERHDGADDLVELVERF--- 163
Cdd:PRK08314 96 REEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEIAVPAWLRAEPPLQALAPGGVVAWkea 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 164 --RGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAV--INATIA 239
Cdd:PRK08314 176 laAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVhsMNAPIY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 240 LmkDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYI 319
Cdd:PRK08314 256 A--GATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 320 HNAYGMTETSSGVIAVPPDRrapvdPASGALsiGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATA 398
Cdd:PRK08314 334 VEGYGLTETMAQTHSNPPDR-----PKLQCL--GIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPEATA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 399 KTFP--DGR--LRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVS 474
Cdd:PRK08314 407 EAFIeiDGKrfFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 475 LVRDAE--VTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEA 527
Cdd:PRK08314 487 LRPEARgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEK 541
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
4-527 |
1.22e-121 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 368.67 E-value: 1.22e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 4 LVDVWkarVAANPEHPAIaYFDG------ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGA 77
Cdd:COG0365 14 CLDRH---AEGRGDKVAL-IWEGedgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 78 AALVLNPMYRKAELRHLVDDAGAVGIICADTAVAENAETMQDSTVRWIVGtsdldfQTRNDPRVF---GDRIRERHDGAD 154
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALE------ELPSLEHVIvvgRTGADVPMEGDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 155 DLVELVERfRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELA-RVDDGDVVLAVAPLFHITGA- 232
Cdd:COG0365 164 DWDELLAA-ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVlDLKPGDVFWCTADIGWATGHs 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 233 -------VINATIaLMKDCTLVFANrfaADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHF--ASIKTLYSGGAPI 303
Cdd:COG0365 243 yivygplLNGATV-VLYEGRPDFPD---PGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYdlSSLRLLGSAGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 304 PPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDRraPVDPASgalsIGMALPQVEIRVVDFDGTPLPDGTQGELEIAG 383
Cdd:COG0365 319 NPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGL--PVKPGS----MGKPVPGYDVAVVDEDGNPVPPGEEGELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 384 PQVV--SGYWQKPEATAKTF---PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVV 458
Cdd:COG0365 393 PWPGmfRGYWNDPERYRETYfgrFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2089408387 459 GQPDDYQGESVVAFVSL---VRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEA 527
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLkpgVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
177-518 |
7.32e-121 |
|
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: 358.52 E-value: 7.32e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGaVINATIALMKDCTLVFANRFAADV 256
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 257 TLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVP 336
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 337 PDrrapvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDA 416
Cdd:cd04433 160 PD-----DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 417 DGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAA 496
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 2089408387 497 YKRPKHIHIVDELPKTQTGKIR 518
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3-523 |
1.30e-118 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 361.24 E-value: 1.30e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL 82
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAVGIICADTAVAENAETMQDSTVRWIVG---TSDLDFQTRNDPRVFGDRIRERHD----GADD 155
Cdd:PRK05605 113 NPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSvnmIAAMPLLQRLALRLPIPALRKARAaltgPAPG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 156 LV---ELVERFRGA---TPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILA-VATTFAELARVDDGD-VVLAVAPLF 227
Cdd:PRK05605 193 TVpweTLVDAAIGGdgsDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKAWVPGLGDGPeRVLAALPMF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 228 HITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAA 307
Cdd:PRK05605 273 HAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVST 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 308 VEKFENKFGHYIHNAYGMTETSSGVIAVP--PDRRAPvdpasgalSIGMALPQVEIRVVDFD--GTPLPDGTQGELEIAG 383
Cdd:PRK05605 353 VELWEKLTGGLLVEGYGLTETSPIIVGNPmsDDRRPG--------YVGVPFPDTEVRIVDPEdpDETMPDGEEGELLVRG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 384 PQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDD 463
Cdd:PRK05605 425 PQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPRE 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 464 YQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK05605 505 DGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
28-517 |
4.38e-117 |
|
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: 354.21 E-value: 4.38e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICAd 107
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 tavAENAETMQDSTVRWIvgtsdldfqtrNDPRVFGdrIRERHDGADDLVELVERFRGAT----PEAAEVSPTDTAILAY 183
Cdd:cd05911 90 ---PDGLEKVKEAAKELG-----------PKDKIIV--LDDKPDGVLSIEDLLSPTLGEEdedlPPPLKDGKDDTAAILY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 184 TSGTTGPPKGALNSHANILA----VATTFAELARVDDgdVVLAVAPLFHITGavINATIALM-KDCTLVFANRFAADVTL 258
Cdd:cd05911 154 SSGTTGLPKGVCLSHRNLIAnlsqVQTFLYGNDGSND--VILGFLPLYHIYG--LFTTLASLlNGATVIIMPKFDSELFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 259 DAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGH-YIHNAYGMTETSsGVIAVPP 337
Cdd:cd05911 230 DLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETG-GILTVNP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 338 DRrapvDPASGalSIGMALPQVEIRVVDFDG-TPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRD 415
Cdd:cd05911 309 DG----DDKPG--SVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 416 ADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLA 495
Cdd:cd05911 383 EDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVA 462
|
490 500
....*....|....*....|...
gi 2089408387 496 AYKR-PKHIHIVDELPKTQTGKI 517
Cdd:cd05911 463 SYKQlRGGVVFVDEIPKSASGKI 485
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
8-433 |
3.84e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 341.98 E-value: 3.84e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 8 WKARVAANPEHPAIAYFDGI-LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMY 86
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 87 RKAELRHLVDDAGAVGIICADTAVAEN-AETMQDSTVRWIVGTSDLDFQTRNDPrvfgdrirerhdgaddLVELVERFRG 165
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEElLEALGKLEVVKLVLVLDRDPVLKEEP----------------LPEEAKPADV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 166 ATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELA----RVDDGDVVLAVAPLFHITGAVINATIALM 241
Cdd:pfam00501 145 PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 242 KDCTLVFA---NRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHY 318
Cdd:pfam00501 225 AGATVVLPpgfPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 319 IHNAYGMTETSSGVIAVPPdrraPVDPASGALSIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEAT 397
Cdd:pfam00501 305 LVNGYGLTETTGVVTTPLP----LDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELT 380
|
410 420 430
....*....|....*....|....*....|....*..
gi 2089408387 398 AKTFPDGR-LRTGDVAIRDADGWIYLVDRLKDQINVS 433
Cdd:pfam00501 381 AEAFDEDGwYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
28-522 |
6.36e-108 |
|
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: 329.05 E-value: 6.36e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVgiicad 107
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 TAVAenaetmqdstvrwivgTSDLDfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsptDTAILAYTSGT 187
Cdd:cd05935 76 VAVV----------------GSELD--------------------------------------------DLALIPYTSGT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVT 267
Cdd:cd05935 96 TGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 268 YTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDRrapvdPAS 347
Cdd:cd05935 176 FWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLR-----PKL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 348 GALsiGMALPQVEIRVVDF-DGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF--PDGR--LRTGDVAIRDADGWIYL 422
Cdd:cd05935 251 QCL--GIP*FGVDARVIDIeTGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFieIKGRrfFRTGDLGYMDEEGYFFF 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 423 VDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRD--AEVTEQELRAFVGDRLAAYKRP 500
Cdd:cd05935 329 VDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYP 408
|
490 500
....*....|....*....|..
gi 2089408387 501 KHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd05935 409 REVEFVDELPRSASGKILWRLL 430
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
2-522 |
1.76e-103 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 321.99 E-value: 1.76e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALV 81
Cdd:PRK06178 33 RPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNPMYRKAELRHLVDDAGAVGIICADTAVAENAETMQDSTVRWIVGTSDLDFQTRNDPRVFGDRIRERHDGADDLVELVE 161
Cdd:PRK06178 113 VSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAEPTLPLPDSLRAPRLAAAGAIDLLP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 162 RFRGATPEAAEVSPT--DTAILAYTSGTTGPPKGALNSHANILAVATTFAELARV-DDGDVVLAVAPLFHITGAVINATI 238
Cdd:PRK06178 193 ALRACTAPVPLPPPAldALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVgGEDSVFLSFLPEFWIAGENFGLLF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 239 ALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTL--YSGGAPIPPAAVEKFENKFG 316
Cdd:PRK06178 273 PLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVrvVSFVKKLNPDYRQRWRALTG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 317 HYI-HNAYGMTET------SSGVIAVPPD-RRAPVdpasgalSIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVV 387
Cdd:PRK06178 353 SVLaEAAWGMTEThtcdtfTAGFQDDDFDlLSQPV-------FVGLPVPGTEFKICDFEtGELLPLGAEGEIVVRTPSLL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 388 SGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGE 467
Cdd:PRK06178 426 KGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQ 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 468 SVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKhIHIVDELPKTQTGKIRRTEL 522
Cdd:PRK06178 506 VPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-523 |
2.25e-103 |
|
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: 316.93 E-value: 2.25e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 29 SAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICadt 108
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 109 avaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsptDTAILAYTSGTT 188
Cdd:cd05934 82 --------------------------------------------------------------------DPASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 189 GPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVTY 268
Cdd:cd05934 94 GPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 269 T--IGSitVFNALYNSPAAT--AAHfasiKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAvppdrraPVD 344
Cdd:cd05934 174 TnyLGA--MLSYLLAQPPSPddRAH----RLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIG-------PRD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 345 PASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEI---AGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIY 421
Cdd:cd05934 241 EPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFY 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 422 LVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPK 501
Cdd:cd05934 321 FVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPR 400
|
490 500
....*....|....*....|..
gi 2089408387 502 HIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05934 401 YIRFVDDLPKTPTEKVAKAQLR 422
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
32-522 |
3.43e-102 |
|
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: 316.48 E-value: 3.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 32 EVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIIcadtAVA 111
Cdd:cd05904 37 ELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAF----TTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 112 ENAETMQDSTVRWIVGTSDLDfqtrnDPRVFGDRIRERHDGAddlvelverfrgatPEAAEVSPTDTAILAYTSGTTGPP 191
Cdd:cd05904 113 ELAEKLASLALPVVLLDSAEF-----DSLSFSDLLFEADEAE--------------PPVVVIKQDDVAALLYSSGTTGRS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 192 KGALNSHANILAVATTF--AELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVTYT 269
Cdd:cd05904 174 KGVMLTHRNLIAMVAQFvaGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 270 IGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHY-IHNAYGMTETSSGVIAVPPDRRAPVDPASg 348
Cdd:cd05904 254 PVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVdLGQGYGMTESTGVVAMCFAPEKDRAKYGS- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 349 alsIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRL 426
Cdd:cd05904 333 ---VGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 427 KDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIV 506
Cdd:cd05904 410 KELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFV 489
|
490
....*....|....*.
gi 2089408387 507 DELPKTQTGKIRRTEL 522
Cdd:cd05904 490 DAIPKSPSGKILRKEL 505
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
2-528 |
1.11e-101 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 317.00 E-value: 1.11e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALV-EKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAAL 80
Cdd:PRK08974 23 QSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 81 VLNPMYRKAELRHLVDDAGAVGIIcadtAVAENAETMQ----DSTVRWIVGTSdldfqtrndprvFGDRI-RERHDGADD 155
Cdd:PRK08974 103 NVNPLYTPRELEHQLNDSGAKAIV----IVSNFAHTLEkvvfKTPVKHVILTR------------MGDQLsTAKGTLVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 156 LVELVER------------FRGATPEA-------AEVSPTDTAILAYTSGTTGPPKGALNSHANILA----VATTFAELA 212
Cdd:PRK08974 167 VVKYIKRlvpkyhlpdaisFRSALHKGrrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqAKAAYGPLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 213 RVDDGDVVLAVaPLFHITGAVINATIAL-MKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFA 291
Cdd:PRK08974 247 HPGKELVVTAL-PLYHIFALTVNCLLFIeLGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 292 SIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDrrapVDPASGalSIGMALPQVEIRVVDFDGTPL 371
Cdd:PRK08974 326 SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYD----LDYYSG--SIGLPVPSTEIKLVDDDGNEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 372 PDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPA 451
Cdd:PRK08974 400 PPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPK 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2089408387 452 VGEAGVVGQPDDYQGESVVAFVsLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEAK 528
Cdd:PRK08974 480 VLEVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 555
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
2-527 |
1.36e-100 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 314.27 E-value: 1.36e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALV 81
Cdd:PRK07059 23 PSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNPMYRKAELRHLVDDAGAVGIIcadtaVAEN-AETMQ----DSTVRWIVGTS--DL--------DFQTRNDPRV----- 141
Cdd:PRK07059 103 VNPLYTPRELEHQLKDSGAEAIV-----VLENfATTVQqvlaKTAVKHVVVASmgDLlgfkghivNFVVRRVKKMvpaws 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 142 ------FGDRIRERhdgaddlvelverfRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILA--------VATT 207
Cdd:PRK07059 178 lpghvrFNDALAEG--------------ARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVAnvlqmeawLQPA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 208 FAELARVDDGDVVLAVaPLFHITGAVINATIALMKD-CTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAAT 286
Cdd:PRK07059 244 FEKKPRPDQLNFVCAL-PLYHIFALTVCGLLGMRTGgRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 287 AAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDrrapVDPASGalSIGMALPQVEIRVVDF 366
Cdd:PRK07059 323 KLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVD----ATEFSG--TIGLPLPSTEVSIRDD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 367 DGTPLPDGTQGELEIAGPQVVSGYWQKPEATAK-TFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDA 445
Cdd:PRK07059 397 DGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKvMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 446 LVAHPAVGEAGVVGQPDDYQGESVVAFVslVR-DAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK07059 477 VASHPGVLEVAAVGVPDEHSGEAVKLFV--VKkDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
...
gi 2089408387 525 TEA 527
Cdd:PRK07059 555 GKA 557
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
28-524 |
4.72e-99 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 308.09 E-value: 4.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGII--- 104
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLtpk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 105 CADTAVAENAETMQDSTVR--WIVGTSDLDFQtrndprvfgdrirerhdgADDLVELVERFRGATPEAaEVSPTDTAILA 182
Cdd:cd05926 95 GELGPASRAASKLGLAILElaLDVGVLIRAPS------------------AESLSNLLADKKNAKSEG-VPLPDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 183 YTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFA 262
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 263 EHEVTY-----TIGSItvfnaLYNSPAATAAH-FASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIA-- 334
Cdd:cd05926 236 DYNATWytavpTIHQI-----LLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSnp 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 335 VPPDRRAP--VDPASGalsigmalpqVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAK-TFPDGRLRTGDV 411
Cdd:cd05926 311 LPPGPRKPgsVGKPVG----------VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 412 AIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVG 491
Cdd:cd05926 381 GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCR 460
|
490 500 510
....*....|....*....|....*....|...
gi 2089408387 492 DRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:cd05926 461 KHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
3-523 |
1.22e-95 |
|
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: 300.52 E-value: 1.22e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL 82
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAVGIICADTAvaenaetmqdstvrwivgtsdLDFqtrnDPRVFGDRIRERHDG---------A 153
Cdd:COG1021 106 LPAHRRAEISHFAEQSEAVAYIIPDRH---------------------RGF----DYRALARELQAEVPSlrhvlvvgdA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 154 DDLVELVERFRG-ATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHitga 232
Cdd:COG1021 161 GEFTSLDALLAApADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAH---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 233 viNATI-------ALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPP 305
Cdd:COG1021 237 --NFPLsspgvlgVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 306 AAVEKFENKFGHYIHNAYGMTEtssGVIAV-----PPDRRA-----PVDPASgalsigmalpqvEIRVVDFDGTPLPDGT 375
Cdd:COG1021 315 ELARRVRPALGCTLQQVFGMAE---GLVNYtrlddPEEVILttqgrPISPDD------------EVRIVDEDGNPVPPGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 376 QGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGE 454
Cdd:COG1021 380 VGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHD 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 455 AGVVGQPDDYQGESVVAFVsLVRDAEVTEQELRAFVGDR-LAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:COG1021 460 AAVVAMPDEYLGERSCAFV-VPRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
28-523 |
2.24e-95 |
|
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: 296.98 E-value: 2.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAgavgiicad 107
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 tavaenaetmqdstvrwivgtsdldfqtrnDPRVFgdrirerhdgaddlvELVERFRGATPEAaevSPTDTAILAYTSGT 187
Cdd:cd05903 73 ------------------------------KAKVF---------------VVPERFRQFDPAA---MPDAVALLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVT 267
Cdd:cd05903 105 TGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 268 YTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDrraPVDPAS 347
Cdd:cd05903 185 FMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPA---PEDRRL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 348 GalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLK 427
Cdd:cd05903 262 Y--TDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 428 DQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFV-GDRLAAYKRPKHIHIV 506
Cdd:cd05903 340 DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHV 419
|
490
....*....|....*..
gi 2089408387 507 DELPKTQTGKIRRTELR 523
Cdd:cd05903 420 DDLPRTPSGKVQKFRLR 436
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
12-523 |
6.08e-95 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 298.44 E-value: 6.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 12 VAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAEL 91
Cdd:PRK06188 22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 92 RHLVDDAGAVGIICADTAVAENAETMQDS--TVRWIVGTSDLDfqtrndprvfgdrirerhdGADDLVELVERFRGATPE 169
Cdd:PRK06188 102 AYVLEDAGISTLIVDPAPFVERALALLARvpSLKHVLTLGPVP-------------------DGVDLLAAAAKFGPAPLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 170 AAEVsPTDTAILAYTSGTTGPPKGALNSHANILAVATtfAELARVD--DGDVVLAVAPLFHITGAVINATiaLMKDCTLV 247
Cdd:PRK06188 163 AAAL-PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQ--IQLAEWEwpADPRFLMCTPLSHAGGAFFLPT--LLRGGTVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 248 FANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPA----AVEKFENKFGHYihnaY 323
Cdd:PRK06188 238 VLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVrlaeAIERFGPIFAQY----Y 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 324 GMTETSSGVIAVPPDRRAPVDPASgALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPD 403
Cdd:PRK06188 314 GQTEAPMVITYLRKRDHDPDDPKR-LTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 404 GRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE 483
Cdd:PRK06188 393 GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2089408387 484 QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK06188 473 AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
16-528 |
7.95e-95 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 299.64 E-value: 7.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:PRK06710 38 PEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIICADTAVAENAETMQDSTVRWIVGTSDLDFQTRNDPRVFGDRIRERHD-----GADDLVEL---VERFRGAT 167
Cdd:PRK06710 118 HDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNlvvkvSESETIHLwnsVEKEVNTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 168 PEAAEVSPTDTAILAYTSGTTGPPKGALNSHANIlaVATTFAELAR----VDDGDVVLAVAPLFHITGAVINATIALMKD 243
Cdd:PRK06710 198 VEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNL--VSNTLMGVQWlyncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 244 CTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAY 323
Cdd:PRK06710 276 YKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 324 GMTETS----SGVIAvppDRRAPVdpasgalSIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATA 398
Cdd:PRK06710 356 GLTESSpvthSNFLW---EKRVPG-------SIGVPWPDTEAMIMSLEtGEALPPGEIGEIVVKGPQIMKGYWNKPEETA 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 399 KTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRD 478
Cdd:PRK06710 426 AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEG 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2089408387 479 AEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEAK 528
Cdd:PRK06710 506 TECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKR 555
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
8-524 |
3.62e-94 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 295.33 E-value: 3.62e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 8 W-KARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMY 86
Cdd:PRK03640 7 WlKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 87 RKAELRHLVDDAGAVGIICADTAVAENAEtmqDSTVRWivgtSDLDFQTRNDPrvfgdrirerhdgaddlvELVErfrga 166
Cdd:PRK03640 87 SREELLWQLDDAEVKCLITDDDFEAKLIP---GISVKF----AELMNGPKEEA------------------EIQE----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 167 tpeaaEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVInatiaLMKD--- 243
Cdd:PRK03640 137 -----EFDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSI-----LMRSviy 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 244 -CTLVFANRFAADVTLDAFAEHEVTyTIGSITVF---------NALYNSpaataahfaSIKTLYSGGAPIPPAAVEKFEN 313
Cdd:PRK03640 207 gMRVVLVEKFDAEKINKLLQTGGVT-IISVVSTMlqrllerlgEGTYPS---------SFRCMLLGGGPAPKPLLEQCKE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 314 KfGHYIHNAYGMTETSSGVIAVPPDrrapvDPASGALSIGMALPQVEIRVVDfDGTPLPDGTQGELEIAGPQVVSGYWQK 393
Cdd:PRK03640 277 K-GIPVYQSYGMTETASQIVTLSPE-----DALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 394 PEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFV 473
Cdd:PRK03640 350 EDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFV 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 474 slVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK03640 430 --VKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
3-524 |
8.51e-94 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 295.30 E-value: 8.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL 82
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAVGIiCADTAVAENAET----MQDSTVRWIVGTSDldfqtrndprvfgdriRERHDGADDLVE 158
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAF-LVDPALAPTAEAalalLPVDTLILSLVLGG----------------REAPGGWLDFAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 159 LVERFRGATPEAaEVSPTDTAILAYTSGTTGPPKGALNSHANILA--VATTFAelARVDDGDVVLAVAPLFHITGAVINA 236
Cdd:PRK08316 155 WAEAGSVAEPDV-ELADDDLAQILYTSGTESLPKGAMLTHRALIAeyVSCIVA--GDMSADDIPLHALPLYHCAQLDVFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 237 TIALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKF- 315
Cdd:PRK08316 232 GPYLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLp 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 316 GHYIHNAYGMTETSSGVIAVPPDrrapvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPE 395
Cdd:PRK08316 312 GLRFYNCYGQTEIAPLATVLGPE-----EHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 396 ATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL 475
Cdd:PRK08316 387 KTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVP 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2089408387 476 VRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK08316 467 KAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
19-524 |
2.61e-93 |
|
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: 291.50 E-value: 2.61e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 19 PAIAYFDGILSAREVDEMSDAFAVALVEKG-VGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDD 97
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 98 AgavgiicadtavaenaetmqdstvrwivgtsdldfqtrnDPRVFGDRirerhdgaddlvelverfrgatpeaaevsptd 177
Cdd:cd05941 83 S---------------------------------------EPSLVLDP-------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 178 tAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFaaDVT 257
Cdd:cd05941 92 -ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKF--DPK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 258 LDAFAEHEvtytiGSITVFNA---LY------------NSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNA 322
Cdd:cd05941 169 EVAISRLM-----PSITVFMGvptIYtrllqyyeahftDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLER 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 323 YGMTETssGVIAVPP---DRRApvdpasGalSIGMALPQVEIRVVDFDGT-PLPDGTQGELEIAGPQVVSGYWQKPEATA 398
Cdd:cd05941 244 YGMTEI--GMALSNPldgERRP------G--TVGMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATK 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 399 KTF-PDGRLRTGDVAIRDADGWIYLVDRLK-DQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLV 476
Cdd:cd05941 314 EEFtDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLR 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2089408387 477 RDAE-VTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:cd05941 394 AGAAaLSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
4-528 |
2.48e-92 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 292.82 E-value: 2.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 4 LVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALV-EKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL 82
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAVGIICAdTAVAENAETMQDST-VRWIVGTSDLDFQTRNDPRVFGDRIRERHD--------GA 153
Cdd:PRK05677 106 NPLYTAREMEHQFNDSGAKALVCL-ANMAHLAEKVLPKTgVKHVIVTEVADMLPPLKRLLINAVVKHVKKmvpayhlpQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 154 DDLVELVERFRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAEL--ARVDDG-DVVLAVAPLFHIT 230
Cdd:PRK05677 185 VKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALmgSNLNEGcEILIAPLPLYHIY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 231 GAVINA-TIALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVE 309
Cdd:PRK05677 265 AFTFHCmAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 310 KFENKFGHYIHNAYGMTETSSGVIAVPPDrrapvdpASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSG 389
Cdd:PRK05677 345 RWKEVTGCAICEGYGMTETSPVVSVNPSQ-------AIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 390 YWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGES 468
Cdd:PRK05677 418 YWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 469 VVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEAK 528
Cdd:PRK05677 498 IKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELK 557
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
3-525 |
1.43e-90 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 288.21 E-value: 1.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGIL--SAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAAL 80
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 81 VLNPMYRKAELRHLVDDAGAVGIICADTAVAENAETMQDSTVRWIVGTSDLDFQTRNDPRVFGDRIRERHDGADDLV--E 158
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALACERLPELRGVVSLAPAPPPGFLAwhE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 159 LVERFRGATPEA-----AEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAV 233
Cdd:PRK12583 179 LQARGETVSREAlaerqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 234 INATIALMKDCTLVFANR-FAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFE 312
Cdd:PRK12583 259 LANLGCMTVGACLVYPNEaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVM 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 313 NKFgHY--IHNAYGMTETS-----SGViAVPPDRRAPvdpasgalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQ 385
Cdd:PRK12583 339 DEM-HMaeVQIAYGMTETSpvslqTTA-ADDLERRVE--------TVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 386 VVSGYWQKPEATAKTFP-DGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDY 464
Cdd:PRK12583 409 VMKGYWNNPEATAESIDeDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEK 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 465 QGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNT 525
Cdd:PRK12583 489 YGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-523 |
2.98e-87 |
|
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: 275.37 E-value: 2.98e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICAD 107
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 TavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsptDTAILAYTSGT 187
Cdd:cd05972 81 E--------------------------------------------------------------------DPALIYFTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVIN-ATIALMKDCTLVF-ANRFAADVTLDAFAEHE 265
Cdd:cd05972 93 TGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSfFGPWLLGATVFVYeGPRFDAERILELLERYG 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 266 VTYTIGSITVFNALYnSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSgVIAVPPDrrAPVDP 345
Cdd:cd05972 173 VTSFCGPPTAYRMLI-KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGL-TVGNFPD--MPVKP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 346 ASgalsIGMALPQVEIRVVDFDGTPLPDGTQGELEI--AGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLV 423
Cdd:cd05972 249 GS----MGRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFV 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 424 DRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE---QELRAFVGDRLAAYKRP 500
Cdd:cd05972 325 GRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYP 404
|
490 500
....*....|....*....|...
gi 2089408387 501 KHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05972 405 REIEFVEELPKTISGKIRRVELR 427
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
12-523 |
3.07e-87 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 279.39 E-value: 3.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 12 VAANPEHPAIAYFD-GI-LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKA 89
Cdd:PRK08315 26 AARYPDREALVYRDqGLrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 90 ELRHLVDDAGAVGIICAD-------------------TAVAENAETMQDSTVRWIVgtsdldfqtrndprVFGDrirERH 150
Cdd:PRK08315 106 ELEYALNQSGCKALIAADgfkdsdyvamlyelapelaTCEPGQLQSARLPELRRVI--------------FLGD---EKH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 151 DGADDLVELVERFRGATPE-----AAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGD-VVLAVa 224
Cdd:PRK08315 169 PGMLNFDELLALGRAVDDAelaarQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrLCIPV- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 225 PLFHITGAVINATIALMKDCTLVFAN-RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPI 303
Cdd:PRK08315 248 PLYHCFGMVLGNLACVTHGATMVYPGeGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPC 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 304 PPAAVEKFENKFG-HYIHNAYGMTETSSGV----IAVPPDRRApvdpasgaLSIGMALPQVEIRVVD-FDGTPLPDGTQG 377
Cdd:PRK08315 328 PIEVMKRVIDKMHmSEVTIAYGMTETSPVStqtrTDDPLEKRV--------TTVGRALPHLEVKIVDpETGETVPRGEQG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 378 ELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAG 456
Cdd:PRK08315 400 ELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQ 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2089408387 457 VVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK08315 480 VVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
175-523 |
2.25e-86 |
|
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: 270.69 E-value: 2.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 175 PTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVF-ANRFA 253
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 254 ADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFG-HYIHNAYGMTETSSGV 332
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTETSPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 333 ----IAVPPDRRApvdpasgaLSIGMALPQVEIRVVDFDGTPLPD-GTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRL 406
Cdd:cd05917 161 tqtrTDDSIEKRV--------NTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 407 RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQEL 486
Cdd:cd05917 233 HTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDI 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 2089408387 487 RAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05917 313 KAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
32-523 |
4.09e-86 |
|
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: 271.91 E-value: 4.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 32 EVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNpmyrkaelRHLVddagavgiicadtava 111
Cdd:cd05912 6 ELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN--------TRLT---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 112 enaetmqdstvrwivgTSDLDFQTRNdprvfgdrirerhdgaddlvelverfrgatpeaAEVSPTDTAILAYTSGTTGPP 191
Cdd:cd05912 62 ----------------PNELAFQLKD---------------------------------SDVKLDDIATIMYTSGTTGKP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 192 KGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVInatiaLMKD----CTLVFANRFAADVTLDAFAEHEVT 267
Cdd:cd05912 93 KGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSI-----LMRSviygMTVYLVDKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 268 YtigsITVFNALYNSPAATAAHF--ASIKTLYSGGAPIPPAAVEKFENKfGHYIHNAYGMTETSSGVIAVPPDrrapvDP 345
Cdd:cd05912 168 I----ISVVPTMLQRLLEILGEGypNNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCSQIVTLSPE-----DA 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 346 ASGALSIGMALPQVEIRVVDFDGTPlpdGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDR 425
Cdd:cd05912 238 LNKIGSAGKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDR 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 426 LKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVslVRDAEVTEQELRAFVGDRLAAYKRPKHIHI 505
Cdd:cd05912 315 RSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFV--VSERPISEEELIAYCSEKLAKYKVPKKIYF 392
|
490
....*....|....*...
gi 2089408387 506 VDELPKTQTGKIRRTELR 523
Cdd:cd05912 393 VDELPRTASGKLLRHELK 410
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
3-527 |
6.67e-86 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 275.99 E-value: 6.67e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALV-EKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALV 81
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNPMYRKAELRHLVDDAGAVGIICADTAVAENAETMQDSTVRWIVGT-----------SDLDFQTRNDPRVFGDRireRH 150
Cdd:PRK08751 106 VNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTglgdmlgfpkaALVNFVVKYVKKLVPEY---RI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 151 DGADDLVELVERFRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSH----ANILAVATTFAELARVDDG-DVVLAVAP 225
Cdd:PRK08751 183 NGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHrnlvANMQQAHQWLAGTGKLEEGcEVVITALP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 226 LFHITGAVINATIaLMK--DCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPI 303
Cdd:PRK08751 263 LYHIFALTANGLV-FMKigGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 304 PPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDrrapVDPASGalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAG 383
Cdd:PRK08751 342 QRSVAERWKQVTGLTLVEAYGLTETSPAACINPLT----LKEYNG--SIGLPIPSTDACIKDDAGTVLAIGEIGELCIKG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 384 PQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPD 462
Cdd:PRK08751 416 PQVMKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPD 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 463 DYQGEsVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEA 527
Cdd:PRK08751 496 EKSGE-IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
3-524 |
2.99e-85 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 274.39 E-value: 2.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEK-GVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALV 81
Cdd:PRK12492 25 SVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNPMYRKAELRHLVDDAGAVGIICADTAVAENAETMQDSTVRWIVGTSDLDFQtrndPRVFGDRIRERHDGADDLV---- 157
Cdd:PRK12492 105 TNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLL----PAAKGWLVNTVVDKVKKMVpayh 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 158 --------ELVERFRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSH----ANILAVATTFAELArvDDG-------- 217
Cdd:PRK12492 181 lpqavpfkQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHgnlvANMLQVRACLSQLG--PDGqplmkegq 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 218 DVVLAVAPLFHITGAVINATialmkdCTLVFANRFA-----ADVT--LDAFAEHEVTYTIGSITVFNALYNSPAATAAHF 290
Cdd:PRK12492 259 EVMIAPLPLYHIYAFTANCM------CMMVSGNHNVlitnpRDIPgfIKELGKWRFSALLGLNTLFVALMDHPGFKDLDF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 291 ASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDRRAPVDpasgalSIGMALPQVEIRVVDFDGTP 370
Cdd:PRK12492 333 SALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLG------TVGIPVPGTALKVIDDDGNE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 371 LPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAH 449
Cdd:PRK12492 407 LPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAH 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 450 PAVGEAGVVGQPDDYQGESVVAFVsLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK12492 487 PKVANCAAIGVPDERSGEAVKLFV-VARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
14-525 |
1.68e-84 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 270.59 E-value: 1.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 14 ANPEHPAIAYFDG-ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELR 92
Cdd:PRK07514 14 ADRDAPFIETPDGlRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 93 HLVDDAGAVGIICADTAVAENAETMQDSTVRWiVGTSDldfqtrndprvfgdrirerhdgADDLVELVERFRGATPEAAE 172
Cdd:PRK07514 94 YFIGDAEPALVVCDPANFAWLSKIAAAAGAPH-VETLD----------------------ADGTGSLLEAAAAAPDDFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 173 V--SPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFAN 250
Cdd:PRK07514 151 VprGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 RFAADVTLDAFAehEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETss 330
Cdd:PRK07514 231 KFDPDAVLALMP--RATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTET-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 331 GVIAVPP---DRRAPvdpasgalSIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGR 405
Cdd:PRK07514 307 NMNTSNPydgERRAG--------TVGFPLPGVSLRVTDPEtGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFrADGF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 406 LRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQE 485
Cdd:PRK07514 379 FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAA 458
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2089408387 486 LRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNT 525
Cdd:PRK07514 459 ILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
16-522 |
7.96e-84 |
|
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: 267.09 E-value: 7.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIIcadtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaeVSP 175
Cdd:cd05930 81 EDSGAKLVL--------------------------------------------------------------------TDP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 TDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL-FHITGAVINAtiALMKDCTLVFA---NR 251
Cdd:cd05930 93 DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFsFDVSVWEIFG--ALLAGATLVVLpeeVR 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 252 FAADVTLDAFAEHEVTYTIGSITVFNALynSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKF-GHYIHNAYGMTETSS 330
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLRLL--LQELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 331 GVIA--VPPDrrapvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF------P 402
Cdd:cd05930 249 DATYyrVPPD-----DEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfgP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 403 DGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEV 481
Cdd:cd05930 324 GERMyRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGEL 403
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2089408387 482 TEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd05930 404 DEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
9-524 |
5.16e-83 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 266.73 E-value: 5.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 9 KARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALV-EKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYR 87
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 88 KAELRHLVDDAGaVGIICADTAVAENAETMQDST----VRWIVGTSDLDFQTRNDprvfgdrirerhdgaddlvelverf 163
Cdd:PRK06839 89 ENELIFQLKDSG-TTVLFVEKTFQNMALSMQKVSyvqrVISITSLKEIEDRKIDN------------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 164 rgatpeAAEVSPTDTAILAYTSGTTGPPKGALNSHANIL--AVATTFAELARVDDGDVVLAvaPLFHITGAVINATIALM 241
Cdd:PRK06839 143 ------FVEKNESASFIICYTSGTTGKPKGAVLTQENMFwnALNNTFAIDLTMHDRSIVLL--PLFHIGGIGLFAFPTLF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 242 KDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKfGHYIHN 321
Cdd:PRK06839 215 AGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 322 AYGMTETSSGVIAVPPDrrapvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF 401
Cdd:PRK06839 294 GFGMTETSPTVFMLSEE-----DARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEV 481
Cdd:PRK06839 369 QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2089408387 482 TEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK06839 449 IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
31-524 |
6.70e-83 |
|
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: 266.80 E-value: 6.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMY---------RKAELRHLVDDAGAV 101
Cdd:cd12119 29 AEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLfpeqiayiiNHAEDRVVFVDRDFL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 102 GIIcadTAVAENAETMQdstvRWIVGTSDLDFQTRNDPRVFG-DRIRERHDGADDLVELVERfrgatpeaaevsptDTAI 180
Cdd:cd12119 109 PLL---EAIAPRLPTVE----HVVVMTDDAAMPEPAGVGVLAyEELLAAESPEYDWPDFDEN--------------TAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 181 LAYTSGTTGPPKGALNSH-ANIL-AVATTFAELARVDDGDVVLAVAPLFHIT--GAVINATIALMKdctLVFANRFAADV 256
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHrSLVLhAMAALLTDGLGLSESDVVLPVVPMFHVNawGLPYAAAMVGAK---LVLPGPYLDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 257 TLDAFAEHE-VTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHnAYGMTETSS-GVIA 334
Cdd:cd12119 245 SLAELIEREgVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIH-AWGMTETSPlGTVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 335 VPPDRRAPVDPASGA---LSIGMALPQVEIRVVDFDGTPLP-DG-TQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTG 409
Cdd:cd12119 324 RPPSEHSNLSEDEQLalrAKQGRPVPGVELRIVDDDGRELPwDGkAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 410 DVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAF 489
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEF 483
|
490 500 510
....*....|....*....|....*....|....*
gi 2089408387 490 VGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:cd12119 484 LADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
21-523 |
7.40e-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: 261.15 E-value: 7.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 21 IAYFDGI--LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDA 98
Cdd:cd05959 21 TAFIDDAgsLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 99 GAVgIICADTAVAENAETM---QDSTVRWIVGTSDldfqtrndprvfgdriRERHDGADDLVELVERFRGATPEAAeVSP 175
Cdd:cd05959 101 RAR-VVVVSGELAPVLAAAltkSEHTLVVLIVSGG----------------AGPEAGALLLAELVAAEAEQLKPAA-THA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 TDTAILAYTSGTTGPPKGALNSHANILAVATTFAE-LARVDDGDVVLAVAPLFHITG--------AVINATIALMkdctl 246
Cdd:cd05959 163 DDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARnVLGIREDDVCFSAAKLFFAYGlgnsltfpLSVGATTVLM----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 247 vfANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMT 326
Cdd:cd05959 238 --PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGST 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 327 ETSSGVIAVPPDRrapVDPASGalsiGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRL 406
Cdd:cd05959 316 EMLHIFLSNRPGR---VRYGTT----GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 407 RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVR---DAEVTE 483
Cdd:cd05959 389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyeDSEALE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2089408387 484 QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05959 469 EELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
28-526 |
1.79e-80 |
|
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: 258.20 E-value: 1.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAaalVLNPMYRKaelrhlvddagavgiicad 107
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGA---VICPLFSA------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 tavaenaetmqdstvrwivgtsdldfqtrndprvFG-DRIRERHDGADDLVELVerfrgaTPEAAE-VSPTDTAILAYTS 185
Cdd:cd05969 59 ----------------------------------FGpEAIRDRLENSEAKVLIT------TEELYErTDPEDPTLLHYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 186 GTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLV-FANRFAADVTLDAFAEH 264
Cdd:cd05969 99 GTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVvYEGRFDAESWYGIIERV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 265 EVTYTIGSITVFNALYNSPAATAAHF--ASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDRraP 342
Cdd:cd05969 179 KVTVWYTAPTAIRMLMKEGDELARKYdlSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCM--P 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 343 VDPASgalsIGMALPQVEIRVVDFDGTPLPDGTQGELEIAG--PQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWI 420
Cdd:cd05969 257 IKPGS----MGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 421 YLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQ---ELRAFVGDRLAAY 497
Cdd:cd05969 333 WFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAH 412
|
490 500
....*....|....*....|....*....
gi 2089408387 498 KRPKHIHIVDELPKTQTGKIRRTELRNTE 526
Cdd:cd05969 413 VAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-519 |
4.73e-79 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 259.26 E-value: 4.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAIAYFDG----ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGA 77
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 78 aalVLNPMYRKA---ELRHLVDDAGAVGIICADTAVAENAETMQDS--TVRWIVGTSDLDfqTRNDPRVFG-DRIRERHD 151
Cdd:COG1022 91 ---VTVPIYPTSsaeEVAYILNDSGAKVLFVEDQEQLDKLLEVRDElpSLRHIVVLDPRG--LRDDPRLLSlDELLALGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 152 GADDLVELVERfrgatpeAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITG 231
Cdd:COG1022 166 EVADPAELEAR-------RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 232 AVInATIALMKDCTLVFANRFAadvTL-DAFAEHEVTYTIGSITVFNALYNSPAATAA----------HFA--------- 291
Cdd:COG1022 239 RTV-SYYALAAGATVAFAESPD---TLaEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeagglkrklfRWAlavgrryar 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 292 ---------------------------------SIKTLYSGGAPIPPAAVEKFENkFGHYIHNAYGMTETsSGVIAV-PP 337
Cdd:COG1022 315 arlagkspslllrlkhaladklvfsklrealggRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTET-SPVITVnRP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 338 DRRAPvdpasGalSIGMALPQVEIRVvdfdgtplpdGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDA 416
Cdd:COG1022 393 GDNRI-----G--TVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 417 DGWIYLVDRLKDQINVSGYK-VWPREVEDALVAHPAVGEAGVVGQ----------PD--------DYQGESVVAFVSLVR 477
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKnVAPQPIENALKASPLIEQAVVVGDgrpflaalivPDfealgewaEENGLPYTSYAELAQ 535
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 478 DAEVTE---QELRAfVGDRLAAYKRPKHIHIVD--------ELpkTQTGKIRR 519
Cdd:COG1022 536 DPEVRAliqEEVDR-ANAGLSRAEQIKRFRLLPkeftiengEL--TPTLKLKR 585
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
6-522 |
1.04e-78 |
|
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: 254.82 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 6 DVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPM 85
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 86 YRKAELRHLVDDAGAVGIICADTAVAenaetmqdstvrwivgtsdldfqtrndpRVFGDRIRERHDGADDlvelverFRG 165
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAG----------------------------RAGGLEVAVVIDEALD-------AGP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 166 ATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTfAELARVDDGDVVLAVAPL------FHITGAVIN-ATI 238
Cdd:cd12117 126 AGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN-TNYVTLGPDDRVLQTSPLafdastFEIWGALLNgARL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 239 ALMKDCTLVFANRFAadvtlDAFAEHEVTYTIGSITVFNALYNS-PAAtaahFASIKTLYSGGAPIPPAAVEKFENKFGH 317
Cdd:cd12117 205 VLAPKGTLLDPDALG-----ALIAEEGVTVLWLTAALFNQLADEdPEC----FAGLRELLTGGEVVSPPHVRRVLAACPG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 318 -YIHNAYGMTETSSGVIAVPPDRRAPVDpasGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEA 396
Cdd:cd12117 276 lRLVNGYGPTENTTFTTSHVVTELDEVA---GSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 397 TAKTF------PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESV 469
Cdd:cd12117 353 TAERFvadpfgPGERLyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRL 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 470 VAFVslVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd12117 433 VAYV--VAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
3-523 |
1.79e-78 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 256.13 E-value: 1.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPA-IAYFDGI-----LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLG 76
Cdd:PRK13295 25 TINDDLDACVASCPDKTAvTAVRLGTgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 77 AAALVLNPMYRKAELRHLVDDAGAVGIICADT----AVAENAETMQDS-----TVRWIVGTSDLDFQtrndpRVFGDRIR 147
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfDHAAMARRLRPElpalrHVVVVGGDGADSFE-----ALLITPAW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 148 ERhdgADDLVELVERFRGatpeaaevSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLF 227
Cdd:PRK13295 180 EQ---EPDAPAILARLRP--------GPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 228 HITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAA 307
Cdd:PRK13295 249 HQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 308 VEKFENKFGHYIHNAYGMTETSSGVIAVPPDrraPVDPASGalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVV 387
Cdd:PRK13295 329 VERARAALGAKIVSAWGMTENGAVTLTKLDD---PDERAST--TDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 388 SGYWQKPEATAkTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGE 467
Cdd:PRK13295 404 GGYLKRPQLNG-TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGE 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2089408387 468 SVVAFVSLVRDAEVTEQELRAFVGD-RLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK13295 483 RACAFVVPRPGQSLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
13-523 |
4.43e-78 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 257.58 E-value: 4.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 13 AANPEHPAIAYFDGILSAREVDEMSDA--------FAVALVEKGVGHGDRVGIHLQNIPQyaiAFLALWKLGAAALV--L 82
Cdd:PRK07529 36 ARHPDAPALSFLLDADPLDRPETWTYAelladvtrTANLLHSLGVGPGDVVAFLLPNLPE---THFALWGGEAAGIAnpI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAVGIICA----DTAVAENAETMQDS--TVRWIVGTSDLDFQTRNDPRVFGDRIRERHDGADDL 156
Cdd:PRK07529 113 NPLLEPEQIAELLRAAGAKVLVTLgpfpGTDIWQKVAEVLAAlpELRTVVEVDLARYLPGPKRLAVPLIRRKAHARILDF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 157 VELVERFRGATPEAAE-VSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVIN 235
Cdd:PRK07529 193 DAELARQPGDRLFSGRpIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 236 ATIALMKDCTLVFANR--FAADVTLDAFAE----HEVTYTIGSITVFNALYNSPAAtAAHFASIKTLYSGGAPIPPAAVE 309
Cdd:PRK07529 273 GLAPLARGAHVVLATPqgYRGPGVIANFWKiverYRINFLSGVPTVYAALLQVPVD-GHDISSLRYALCGAAPLPVEVFR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 310 KFENKFGHYIHNAYGMTETSSGVIAVPPDRraPVDPASgalsIGMALP--QVEIRVVDFDGTPLPD---GTQGELEIAGP 384
Cdd:PRK07529 352 RFEAATGVRIVEGYGLTEATCVSSVNPPDG--ERRIGS----VGLRLPyqRVRVVILDDAGRYLRDcavDEVGVLCIAGP 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 385 QVVSGYWQkPEATAKTFPDGR-LRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDD 463
Cdd:PRK07529 426 NVFSGYLE-AAHNKGLWLEDGwLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDA 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 464 YQGESVVAFVSLVRDAEVTEQELRAFVGDRL---AAYkrPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK07529 505 HAGELPVAYVQLKPGASATEAELLAFARDHIaerAAV--PKHVRILDALPKTAVGKIFKPALR 565
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
5-522 |
3.12e-76 |
|
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: 248.73 E-value: 3.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 5 VDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNP 84
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 85 MYRKAELRHLVDDAGAVGIIC-ADTAVAENAETMQDSTVRWIVGTsdldfqtrndprvfgdrirerhdgaddlvelverf 163
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTtADLAARLPAGGDVALLGDEALAA----------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 164 RGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL-FHITGAVInaTIALMK 242
Cdd:cd17646 126 PPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLsFDVSVWEL--FWPLVA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 243 DCTLVFA---NRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAhfASIKTLYSGGAPIPPAAVEKFENKFGHYI 319
Cdd:cd17646 204 GARLVVArpgGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSC--ASLRRVFCSGEALPPELAARFLALPGAEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 320 HNAYGMTETSSGVIAVPPDRRAPVDPasgaLSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAK 399
Cdd:cd17646 282 HNLYGPTEAAIDVTHWPVRGPAETPS----VPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 400 TF------PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAF 472
Cdd:cd17646 358 RFvpdpfgPGSRMyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGY 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 473 VSLVRDAE-VTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17646 438 VVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
15-523 |
4.59e-76 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 249.19 E-value: 4.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 15 NPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHL 94
Cdd:PRK07470 20 FPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 95 VDDAGAVGIICaDTAVAENAETMQDS--TVRWIVGTSDLDFqtrndprvfgdrirerhdgADDLVELVERFRGATPEAAE 172
Cdd:PRK07470 100 AEASGARAMIC-HADFPEHAAAVRAAspDLTHVVAIGGARA-------------------GLDYEALVARHLGARVANAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 173 VSPTDTAILAYTSGTTGPPKGALNSHANILAVATTfaELARVDDG----DVVLAVAPLFHitGAVINATIALMKDCTLVF 248
Cdd:PRK07470 160 VDHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITN--HLADLMPGtteqDASLVVAPLSH--GAGIHQLCQVARGAATVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 249 --ANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMT 326
Cdd:PRK07470 236 lpSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 327 ETSSGVIAVPPDRRAPVD-PASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGR 405
Cdd:PRK07470 316 EVTGNITVLPPALHDAEDgPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGW 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 406 LRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQE 485
Cdd:PRK07470 396 FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAE 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 2089408387 486 LRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK07470 476 LLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
10-524 |
6.94e-76 |
|
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: 247.60 E-value: 6.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 10 ARVAAN-PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAaalVLNPM-YR 87
Cdd:cd12118 11 ERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGA---VLNALnTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 88 -KAELRHLVDDAGAVGIICADTAVA-ENAETMQDSTVRWIVGTSDldfqtrndprvfgdrirerhdgaddlvelverfrg 165
Cdd:cd12118 88 lDAEEIAFILRHSEAKVLFVDREFEyEDLLAEGDPDFEWIPPADE----------------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 166 atpeaaevspTDTAILAYTSGTTGPPKGALNSH--ANILAVATTFAelARVDDGDVVLAVAPLFHITGAVINATIAlMKD 243
Cdd:cd12118 133 ----------WDPIALNYTSGTTGRPKGVVYHHrgAYLNALANILE--WEMKQHPVYLWTLPMFHCNGWCFPWTVA-AVG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 244 CTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHnAY 323
Cdd:cd12118 200 GTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTH-VY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 324 GMTETSsGVIAV----------PPDRRAPVDPASGALSIGMAlpqvEIRVVDFDGT-PLP-DG-TQGELEIAGPQVVSGY 390
Cdd:cd12118 279 GLTETY-GPATVcawkpewdelPTEERARLKARQGVRYVGLE----EVDVLDPETMkPVPrDGkTIGEIVFRGNIVMKGY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 391 WQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVV 470
Cdd:cd12118 354 LKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPC 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2089408387 471 AFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIhIVDELPKTQTGKIRRTELRN 524
Cdd:cd12118 434 AFVELKEGAKVTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
3-522 |
1.69e-75 |
|
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: 246.47 E-value: 1.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL 82
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAVGIICADTAvaenaetmqdstvrwivgtsdldfqtrndprvfgdrirERHDGADDLVELVEr 162
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAVAYIVPDRH--------------------------------------AGFDHRALARELAE- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 163 frgatpeaaevSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHitgaviNATIA--- 239
Cdd:cd05920 137 -----------SIPEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH------NFPLAcpg 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 240 ----LMKDCTLVFANRFAADVTLDAFAEHEVTYTigsiTVFNAL----YNSPAATAAHFASIKTLYSGGAPIPPAAVEKF 311
Cdd:cd05920 200 vlgtLLAGGRVVLAPDPSPDAAFPLIEREGVTVT----ALVPALvslwLDAAASRRADLSSLRLLQVGGARLSPALARRV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 312 ENKFGHYIHNAYGMTEtssGVIAV-----PPDRRAPVD--PASgalsigmalPQVEIRVVDFDGTPLPDGTQGELEIAGP 384
Cdd:cd05920 276 PPVLGCTLQQVFGMAE---GLLNYtrlddPDEVIIHTQgrPMS---------PDDEIRVVDEEGNPVPPGEEGELLTRGP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 385 QVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDD 463
Cdd:cd05920 344 YTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDE 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 464 YQGESVVAFVsLVRDAEVTEQELRAFVGDR-LAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd05920 424 LLGERSCAFV-VLRDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
8-523 |
5.47e-75 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 247.00 E-value: 5.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 8 WKARVA-ANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMY 86
Cdd:PRK07786 22 QLARHAlMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 87 RKAELRHLVDDAGAVGIIcADTAVAENAetmqdSTVRWIVGTSDLDFqtrndprVFGDRIRERHDGADDLVelveRFRGA 166
Cdd:PRK07786 102 TPPEIAFLVSDCGAHVVV-TEAALAPVA-----TAVRDIVPLLSTVV-------VAGGSSDDSVLGYEDLL----AEAGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 167 TPEAAEVsPTDT-AILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDG-DVVLAVAPLFHITGAVINATIALMKDC 244
Cdd:PRK07786 165 AHAPVDI-PNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINsDVGFVGVPLFHIAGIGSMLPGLLLGAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 245 TLVFA-NRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFAsIKTLYSGGAPIPPAAVEKFENKF-GHYIHNA 322
Cdd:PRK07786 244 TVIYPlGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFpEAQILAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 323 YGMTETSSGVIAVPPDrrapvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFP 402
Cdd:PRK07786 323 FGQTEMSPVTCMLLGE-----DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 403 DGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRD-AEV 481
Cdd:PRK07786 398 GGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAAL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2089408387 482 TEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK07786 478 TLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
3-530 |
7.14e-75 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 246.59 E-value: 7.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL 82
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAvGIICADTAVAENAETMQDS----TVRWIVgtsDLDFQTRNDPRVfgdrirerhdGADDLVE 158
Cdd:PRK06155 102 NTALRGPQLEHILRNSGA-RLLVVEAALLAALEAADPGdlplPAVWLL---DAPASVSVPAGW----------STAPLPP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 159 LverfrGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGavINATI 238
Cdd:PRK06155 168 L-----DAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNA--LNAFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 239 -ALMKDCTLVFANRFAADVTLDAFAEHE--VTYTIGSITvfNALYNSPAATAAHFASIKTLYSGGapIPPAAVEKFENKF 315
Cdd:PRK06155 241 qALLAGATYVLEPRFSASGFWPAVRRHGatVTYLLGAMV--SILLSQPARESDRAHRVRVALGPG--VPAALHAAFRERF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 316 GHYIHNAYGMTETSSgVIAVPPDRRAPVdpasgalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQ---VVSGYWQ 392
Cdd:PRK06155 317 GVDLLDGYGSTETNF-VIAVTHGSQRPG-------SMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 393 KPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYqGESVVAF 472
Cdd:PRK06155 389 MPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSEL-GEDEVMA 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2089408387 473 VSLVRDAEVTE-QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRntEAKVT 530
Cdd:PRK06155 468 AVVLRDGTALEpVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR--EQGVT 524
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
19-523 |
9.65e-75 |
|
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: 243.14 E-value: 9.65e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 19 PAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELrhlvdda 98
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDY------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 99 gavgiicadtavaenAETMQDSTVRWIVGTSDldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsptDT 178
Cdd:cd05919 75 ---------------AYIARDCEARLVVTSAD----------------------------------------------DI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 179 AILAYTSGTTGPPKGALNSHANILAVATTFA-ELARVDDGDVVLAVAPLFHITGAVINATIALMKDCT-LVFANRFAADV 256
Cdd:cd05919 94 AYLLYSSGTTGPPKGVMHAHRDPLLFADAMArEALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASaVLNPGWPTAER 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 257 TLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVP 336
Cdd:cd05919 174 VLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 337 PDrrapvdpASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDA 416
Cdd:cd05919 254 PG-------AWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDA 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 417 DGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE---QELRAFVGDR 493
Cdd:cd05919 327 DGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLER 406
|
490 500 510
....*....|....*....|....*....|
gi 2089408387 494 LAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05919 407 LSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
32-522 |
1.86e-74 |
|
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: 242.35 E-value: 1.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 32 EVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICADTAVA 111
Cdd:TIGR01923 4 DLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 112 EnaetmqdstvrwivgtsdlDFQtrndprvfgdrirerhdgADDLVELVERFRGATPEAAEVSPTDTAILAYTSGTTGPP 191
Cdd:TIGR01923 84 K-------------------DFQ------------------ADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 192 KGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITG------AVINATialmkdcTLVFANRFAAdvTLDAFAEHE 265
Cdd:TIGR01923 127 KAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGlsilfrWLIEGA-------TLRIVDKFNQ--LLEMIANER 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 266 VTYtigsITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKfGHYIHNAYGMTETSSGVIAVPPdrraPVDP 345
Cdd:TIGR01923 198 VTH----ISLVPTQLNRLLDEGGHNENLRKILLGGSAIPAPLIEEAQQY-GLPIYLSYGMTETCSQVTTATP----EMLH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 346 ASGalSIGMALPQVEIRV-VDfdgtplPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVD 424
Cdd:TIGR01923 269 ARP--DVGRPLAGREIKIkVD------NKEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 425 RLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLvrDAEVTEQELRAFVGDRLAAYKRPKHIH 504
Cdd:TIGR01923 341 RRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVS--ESDISQAKLIAYLTEKLAKYKVPIAFE 418
|
490
....*....|....*...
gi 2089408387 505 IVDELPKTQTGKIRRTEL 522
Cdd:TIGR01923 419 KLDELPYNASGKILRNQL 436
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
31-523 |
9.18e-74 |
|
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: 240.80 E-value: 9.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICadtav 110
Cdd:cd05971 10 KELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 111 aenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhDGADDLvelverfrgatpeaaevsptdtAILAYTSGTTGP 190
Cdd:cd05971 85 ----------------------------------------DGSDDP----------------------ALIIYTSGTTGP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 191 PKGALNSH----ANILAVATTFAELARvdDGDVVLAVAPLFHItGAVINATIALMKDCTLVFANR---FAADVTLDAFAE 263
Cdd:cd05971 103 PKGALHAHrvllGHLPGVQFPFNLFPR--DGDLYWTPADWAWI-GGLLDVLLPSLYFGVPVLAHRmtkFDPKAALDLMSR 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 264 HEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSgVIAVPPDRrAPV 343
Cdd:cd05971 180 YGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNL-VIGNCSAL-FPI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 344 DPASgalsIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVS--GYWQKPEATAKTFPDGRLRTGDVAIRDADGWIY 421
Cdd:cd05971 258 KPGS----MGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAflGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFW 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 422 LVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL---VRDAEVTEQELRAFVGDRLAAYK 498
Cdd:cd05971 334 YVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLnpgETPSDALAREIQELVKTRLAAHE 413
|
490 500
....*....|....*....|....*
gi 2089408387 499 RPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05971 414 YPREIEFVNELPRTATGKIRRRELR 438
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
27-524 |
1.47e-73 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 242.96 E-value: 1.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 27 ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICA 106
Cdd:PLN02246 50 VYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 107 DTAVAENAETMQDSTVRWIVgtsdldfqtrndprvfgdrIRERHDGADDLVELVERFRGATPEAaEVSPTDTAILAYTSG 186
Cdd:PLN02246 130 SCYVDKLKGLAEDDGVTVVT-------------------IDDPPEGCLHFSELTQADENELPEV-EISPDDVVALPYSSG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 187 TTGPPKGALNSHANILavaTTFAELarVD---------DGDVVLAVAPLFHI--------TGAVINATIALMKdctlvfa 249
Cdd:PLN02246 190 TTGLPKGVMLTHKGLV---TSVAQQ--VDgenpnlyfhSDDVILCVLPMFHIyslnsvllCGLRVGAAILIMP------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 nRFAADVTLDAFAEHEVTytIGSIT--VFNALYNSPAATAAHFASIKTLYSGGAPIPpaavEKFENKFGHYIHNA----- 322
Cdd:PLN02246 258 -KFEIGALLELIQRHKVT--IAPFVppIVLAIAKSPVVEKYDLSSIRMVLSGAAPLG----KELEDAFRAKLPNAvlgqg 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 323 YGMTEtSSGVIAVPPD-RRAPVDPASGalSIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKT 400
Cdd:PLN02246 331 YGMTE-AGPVLAMCLAfAKEPFPVKSG--SCGTVVRNAELKIVDPEtGASLPRNQPGEICIRGPQIMKGYLNDPEATANT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 401 F-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDA 479
Cdd:PLN02246 408 IdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGS 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2089408387 480 EVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PLN02246 488 EITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
32-530 |
5.38e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 240.09 E-value: 5.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 32 EVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAgAVGIICADTAVA 111
Cdd:PRK09088 27 ELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDA-EPRLLLGDDAVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 112 ENaetmqdstvrwivGTSDLDFqtrndprvfgdrirerhdgaDDLVELVErfrGATPEAAEVSPTD-TAILAYTSGTTGP 190
Cdd:PRK09088 106 AG-------------RTDVEDL--------------------AAFIASAD---ALEPADTPSIPPErVSLILFTSGTSGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 191 PKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHE--VTY 268
Cdd:PRK09088 150 PKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPAlgITH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 269 TIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKfGHYIHNAYGMTETSSgVIAVPPDrraPVDPASG 348
Cdd:PRK09088 230 YFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGT-VFGMSVD---CDVIRAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 349 ALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLK 427
Cdd:PRK09088 305 AGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDADGFFWVVDRKK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 428 DQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVD 507
Cdd:PRK09088 385 DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVD 464
|
490 500
....*....|....*....|...
gi 2089408387 508 ELPKTQTGKIRRTELRNTEAKVT 530
Cdd:PRK09088 465 ALPRTASGKLQKARLRDALAAGR 487
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
10-526 |
1.10e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 238.29 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 10 ARVAanPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKA 89
Cdd:PRK07788 59 ARRA--PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 90 ELRHLVDDAGAVGIIcADTAVAENAETMQDSTVRWIVGtsdldfqtrndpRVFGDRIRERHDGADDLVELVERfrgATPE 169
Cdd:PRK07788 137 QLAEVAAREGVKALV-YDDEFTDLLSALPPDLGRLRAW------------GGNPDDDEPSGSTDETLDDLIAG---SSTA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 170 AAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFaeLARV--DDGDVVLAVAPLFHITGaVINATIALMKDCTLV 247
Cdd:PRK07788 201 PLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGL--LSRVpfRAGETTLLPAPMFHATG-WAHLTLAMALGSTVV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 248 FANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHF--ASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGM 325
Cdd:PRK07788 278 LRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYdtSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 326 TETSSGVIAVPPD-RRAPVdpasgalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYwqkpeaTA---KTF 401
Cdd:PRK07788 358 TEVAFATIATPEDlAEAPG-------TVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDgrdKQI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEV 481
Cdd:PRK07788 425 IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAAL 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2089408387 482 TEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTE 526
Cdd:PRK07788 505 DEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2-524 |
5.67e-71 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 236.57 E-value: 5.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAI------AYFDGilsarEVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKL 75
Cdd:PRK06087 23 ASLADYWQQTARAMPDKIAVvdnhgaSYTYS-----ALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 76 GAAALVLNPMYRKAELRHLVDDAGAVGIICADTAVAENAETM------QDSTVRWIVGTsdldfqtrndprvfgDRIRER 149
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLilplqnQLPQLQQIVGV---------------DKLAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 150 HDgADDLVELVERFrgaTPEAAEVSPT--DTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLF 227
Cdd:PRK06087 163 TS-SLSLSQIIADY---EPLTTAITTHgdELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 228 HITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAA 307
Cdd:PRK06087 239 HATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 308 VEKfenKFGHYIH--NAYGMTEtSSGVIAVPPDrrapvDPAS--GALSiGMALPQVEIRVVDFDGTPLPDGTQGELEIAG 383
Cdd:PRK06087 319 ARE---CQQRGIKllSVYGSTE-SSPHAVVNLD-----DPLSrfMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 384 PQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPD 462
Cdd:PRK06087 389 PNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPD 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089408387 463 DYQGESVVAFVSLVRD-AEVTEQELRAFVGD-RLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK06087 469 ERLGERSCAYVVLKAPhHSLTLEEVVAFFSRkRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
8-524 |
7.62e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 234.11 E-value: 7.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 8 WKARVAANPEHPAIAYFDG-ILSAREVdemsdAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMY 86
Cdd:PRK07787 5 NPAAVAAAADIADAVRIGGrVLSRSDL-----AGAATAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 87 RKAELRHLVDDAGAVGiicadtavaenaetmqdstvrWIVGTSDldfqtrndprvfGDRIRERHDgaddlVELVERFRGA 166
Cdd:PRK07787 80 GVAERRHILADSGAQA---------------------WLGPAPD------------DPAGLPHVP-----VRLHARSWHR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 167 TPEAaevSPTDTAILAYTSGTTGPPKGALNSHAnilAVATTFAELARVDD---GDVVLAVAPLFHITGAVINATIALMKD 243
Cdd:PRK07787 122 YPEP---DPDAPALIVYTSGTTGPPKGVVLSRR---AIAADLDALAEAWQwtaDDVLVHGLPLFHVHGLVLGVLGPLRIG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 244 CTLVFANRFAADVTLDAFAEHEVTYtIGSITVFNALYNSPAATAAhFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAY 323
Cdd:PRK07787 196 NRFVHTGRPTPEAYAQALSEGGTLY-FGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGHRPVERY 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 324 GMTETSSGVIAvppdrRAPVDPASGalSIGMALPQVEIRVVDFDGTPLP-DG-TQGELEIAGPQVVSGYWQKPEATAKTF 401
Cdd:PRK07787 274 GMTETLITLST-----RADGERRPG--WVGLPLAGVETRLVDEDGGPVPhDGeTVGELQVRGPTLFDGYLNRPDATAAAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 -PDGRLRTGDVAIRDADGWIYLVDRLK-DQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVslVRDA 479
Cdd:PRK07787 347 tADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV--VGAD 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2089408387 480 EVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK07787 425 DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
16-524 |
2.51e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 234.84 E-value: 2.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAaalVLNPMYRKAE----- 90
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGA---VLNTLNTRLDaasia 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 91 --LRHlvddaGAVGIICADT---AVAENAETMQDSTVRWIVGTSDLDFQTrndprvfGDRIrerhdGADDLVELVErfrG 165
Cdd:PRK08162 109 fmLRH-----GEAKVLIVDTefaEVAREALALLPGPKPLVIDVDDPEYPG-------GRFI-----GALDYEAFLA---S 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 166 ATPEAAEVSPTDT--AI-LAYTSGTTGPPKG--------ALNSHANILAvattfAELARvddGDVVLAVAPLFHITGAVI 234
Cdd:PRK08162 169 GDPDFAWTLPADEwdAIaLNYTSGTTGNPKGvvyhhrgaYLNALSNILA-----WGMPK---HPVYLWTLPMFHCNGWCF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 235 NATIALMKDcTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENk 314
Cdd:PRK08162 241 PWTVAARAG-TNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEE- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 315 FGHYIHNAYGMTET---------SSGVIAVPPDRRApvdpasgALSI--GMALPQVE-IRVVDFD-GTPLP-DG-TQGEL 379
Cdd:PRK08162 319 IGFDLTHVYGLTETygpatvcawQPEWDALPLDERA-------QLKArqGVRYPLQEgVTVLDPDtMQPVPaDGeTIGEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 380 EIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVG 459
Cdd:PRK08162 392 MFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 460 QPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIhIVDELPKTQTGKIRRTELRN 524
Cdd:PRK08162 472 KPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQKFVLRE 535
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
16-523 |
1.23e-69 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 232.73 E-value: 1.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:PRK13382 57 PDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIICADtavaENAETMqdstvrwivgtsDLDFQTRNDPRvfgdRIRERHDGADD-LVE-LVERFRGATPEAAEv 173
Cdd:PRK13382 137 TREGVDTVIYDE----EFSATV------------DRALADCPQAT----RIVAWTDEDHDlTVEvLIAAHAGQRPEPTG- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 174 SPTDTAILayTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGaVINATIALMKDCTLVFANRFA 253
Cdd:PRK13382 196 RKGRVILL--TSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWG-FSQLVLAASLACTIVTRRRFD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 254 ADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFA--SIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSG 331
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSgrSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 332 VIAVPPDRRAPVDPAsgalsiGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYwqkPEATAKTFPDGRLRTGDV 411
Cdd:PRK13382 353 ATATPADLRAAPDTA------GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFHDGFMASGDV 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 412 AIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVG 491
Cdd:PRK13382 424 GYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVR 503
|
490 500 510
....*....|....*....|....*....|..
gi 2089408387 492 DRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK13382 504 DNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
16-522 |
4.74e-69 |
|
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: 229.10 E-value: 4.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIICADtavaenaetmqdstvrwivgtsdldfqtrndprvfgdRIRERHDGADDLVELVERFRGATPEA--AEV 173
Cdd:cd12116 81 EDAEPALVLTDD-------------------------------------ALPDRLPAGLPVLLLALAAAAAAPAAprTPV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 174 SPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVA-PLFHItgAVINATIALMKDCTLVFANRf 252
Cdd:cd12116 124 SPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTtYAFDI--SLLELLLPLLAGARVVIAPR- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 253 aaDVTLDA------FAEHEVTYTIGSITVFNALYNSPAATAAHFasikTLYSGGAPIPPAAVEKFENKFGHyIHNAYGMT 326
Cdd:cd12116 201 --ETQRDPealarlIEAHSITVMQATPATWRMLLDAGWQGRAGL----TALCGGEALPPDLAARLLSRVGS-LWNLYGPT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 327 ETS--SGViavppdrrAPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF--- 401
Cdd:cd12116 274 ETTiwSTA--------ARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpd 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 ----PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDyQGESVVAFVSLV 476
Cdd:cd12116 346 pfagPGSRLyRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLK 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2089408387 477 RDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd12116 425 AGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
28-519 |
7.33e-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: 225.55 E-value: 7.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAaalVLNPMY---RKAELRHLVDDAGAVGII 104
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGA---VPVPIYptsSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 105 CADtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsPTDTAILAYT 184
Cdd:cd05907 83 VED-------------------------------------------------------------------PDDLATIIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 185 SGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFAnrFAADVTLDAFAEH 264
Cdd:cd05907 96 SGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFA--SSAETLLDDLSEV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 265 EVTYTIGSITVFNALYNSPAATA-----------AHFASIKTLYSGGAPIPPAAVEKFeNKFGHYIHNAYGMTETSSGVI 333
Cdd:cd05907 174 RPTVFLAVPRVWEKVYAAIKVKAvpglkrklfdlAVGGRLRFAASGGAPLPAELLHFF-RALGIPVYEGYGLTETSAVVT 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 334 AVPPDrrapvDPASGalSIGMALPQVEIRVVDfdgtplpdgtQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVA 412
Cdd:cd05907 253 LNPPG-----DNRIG--TVGKPLPGVEVRIAD----------DGEILVRGPNVMLGYYKNPEATAEALdADGWLHTGDLG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 413 IRDADGWIYLVDRLKD-QINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDY------------------QGESVVAFV 473
Cdd:cd05907 316 EIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFlvalivpdpealeawaeeHGIAYTDVA 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 474 SLVRDAEVtEQELRAFVGD---RLAAYKRPKHIHIVDELP------KTQTGKIRR 519
Cdd:cd05907 396 ELAANPAV-RAEIEAAVEAanaRLSRYEQIKKFLLLPEPFtiengeLTPTLKLKR 449
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
3-516 |
8.55e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 227.46 E-value: 8.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL 82
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAVGIIcADTAVAENAETMQDST--VRWIVgtsdldfqtrndpRVFGDRIRERHDGADDLVELV 160
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALV-YEREFAPRVAEVLPRLpkLRTLV-------------VVEDGSGNDLLPGAVDYEDAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 161 ErFRGATPEAAEVSPTDTAILaYTSGTTGPPKGALNSHANI---LAVATTF------------AELARVDDGDVVLAVAP 225
Cdd:PRK07798 150 A-AGSPERDFGERSPDDLYLL-YTGGTTGMPKGVMWRQEDIfrvLLGGRDFatgepiedeeelAKRAAAGPGMRRFPAPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 226 LFHiTGAVINATIALMKDCTLVFA--NRFAADVTLDAFAEHEVTytigSITVFNALYNSPAATAAHFA------SIKTLY 297
Cdd:PRK07798 228 LMH-GAGQWAAFAALFSGQTVVLLpdVRFDADEVWRTIEREKVN----VITIVGDAMARPLLDALEARgpydlsSLFAIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 298 SGGAPIPPAAVEKFENKFGHY-IHNAYGMTETSSGVIAVPpdrrAPVDPASGALSIGMAlpqVEIRVVDFDGTPLPDGTQ 376
Cdd:PRK07798 303 SGGALFSPSVKEALLELLPNVvLTDSIGSSETGFGGSGTV----AKGAVHTGGPRFTIG---PRTVVLDEDGNPVEPGSG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 377 GELEIA-GPQVVSGYWQKPEATAKTFP--DGRlR---TGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHP 450
Cdd:PRK07798 376 EIGWIArRGHIPLGYYKDPEKTAETFPtiDGV-RyaiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHP 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2089408387 451 AVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGK 516
Cdd:PRK07798 455 DVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
12-523 |
2.55e-67 |
|
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: 225.30 E-value: 2.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 12 VAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAEL 91
Cdd:cd17651 5 AARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 92 RHLVDDAGAVgiicadtAVAENAETMQDSTVRWIVGTSDLDFQTRNDPRvfgdrirerhdgaddlvelverfrgaTPEAA 171
Cdd:cd17651 85 AFMLADAGPV-------LVLTHPALAGELAVELVAVTLLDQPGAAAGAD--------------------------AEPDP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 172 EVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL-FHITGAVINATiaLMKDCTLVFAN 250
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLgFDVSVQEIFST--LCAGATLVLPP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 ---RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIP--PAAVEKFENKFGHYIHNAYGM 325
Cdd:cd17651 210 eevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVltEDLREFCAGLPGLRLHNHYGP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 326 TET---SSGVIAVPPDRRapvdPAsgALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF- 401
Cdd:cd17651 290 TEThvvTALSLPGDPAAW----PA--PPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFv 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 -----PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL 475
Cdd:cd17651 364 pdpfvPGARMyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2089408387 476 VRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd17651 444 DPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-519 |
8.88e-67 |
|
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: 234.75 E-value: 8.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALV 81
Cdd:COG1020 476 ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNPMYRKAELRHLVDDAGAVGIICADTAvaenAETMQDSTVRWIvgtsDLDFQTRNDprvfgdrirerhdgaddlvelve 161
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLTQSAL----AARLPELGVPVL----ALDALALAA----------------------- 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 162 rfRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL------FHITGAVIN 235
Cdd:COG1020 605 --EPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLsfdasvWEIFGALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 236 -ATIALMKDctlvfANRFAADVTLDAFAEHEVTYTIGSITVFNALynsPAATAAHFASIKTLYSGGAPIPPAAVEKFENK 314
Cdd:COG1020 683 gATLVLAPP-----EARRDPAALAELLARHRVTVLNLTPSLLRAL---LDAAPEALPSLRLVLVGGEALPPELVRRWRAR 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 315 FGHY-IHNAYGMTETSSGVIAVPPDrraPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQK 393
Cdd:COG1020 755 LPGArLVNLYGPTETTVDSTYYEVT---PPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNR 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 394 PEATAK-------TFPDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQ 465
Cdd:COG1020 832 PELTAErfvadpfGFPGARLyRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPG 911
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2089408387 466 GESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRR 519
Cdd:COG1020 912 DKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDR 965
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
177-519 |
1.01e-66 |
|
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: 219.06 E-value: 1.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGavINATIALMKDCTL-VFANRFAAD 255
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG--LNLALATFHAGGAnVVMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 256 VTLDAFAEHEVTYtIGSITVFnaLYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSsGVIAV 335
Cdd:cd17637 79 EALELIEEEKVTL-MGSFPPI--LSNLLDAAEKSGVDLSSLRHVLGLDAPETIQRFEETTGATFWSLYGQTETS-GLVTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 336 PPDRRAPVdpasgalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRD 415
Cdd:cd17637 155 SPYRERPG-------SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 416 ADGWIYLVDRL--KDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDR 493
Cdd:cd17637 228 EDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSR 307
|
330 340
....*....|....*....|....*.
gi 2089408387 494 LAAYKRPKHIHIVDELPKTQTGKIRR 519
Cdd:cd17637 308 IARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
16-522 |
3.12e-66 |
|
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: 220.97 E-value: 3.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIIcadtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaeVSP 175
Cdd:cd17652 81 ADARPALLL--------------------------------------------------------------------TTP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 TDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVA-PLFhiTGAVINATIALMKDCTLVFANR--- 251
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFAsPSF--DASVWELLMALLAGATLVLAPAeel 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 252 FAADVTLDAFAEHEVTYTIGSITVFNALynspaaTAAHFASIKTLYSGGAPIPPAAVEKFENkfGHYIHNAYGMTETSSG 331
Cdd:cd17652 171 LPGEPLADLLREHRITHVTLPPAALAAL------PPDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPTETTVC 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 332 VIAVPPDrrapvdPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-------PDG 404
Cdd:cd17652 243 ATMAGPL------PGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFvadpfgaPGS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 405 RL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE 483
Cdd:cd17652 317 RMyRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTA 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 2089408387 484 QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17652 397 AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
12-519 |
8.82e-66 |
|
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: 220.20 E-value: 8.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 12 VAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAEL 91
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 92 RHLVDDAGavgiicadtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatPEAA 171
Cdd:cd05945 81 REILDAAK--------------------------------------------------------------------PALL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 172 EVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL------FHITGAVIN--ATIALMKD 243
Cdd:cd05945 93 IADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFsfdlsvMDLYPALASgaTLVPVPRD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 244 CTLVFANRFAAdvtldaFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKF-GHYIHNA 322
Cdd:cd05945 173 ATADPKQLFRF------LAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 323 YGMTETSSGVIAVPPDRraPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF- 401
Cdd:cd05945 247 YGPTEATVAVTYIEVTP--EVLDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFf 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 -PDGRL--RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL-VR 477
Cdd:cd05945 325 pDEGQRayRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPkPG 404
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2089408387 478 DAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRR 519
Cdd:cd05945 405 AEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDR 446
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
11-526 |
1.51e-65 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 222.46 E-value: 1.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 11 RVAANP--EHPAIAYFDG----ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAaalVLNP 84
Cdd:PRK04319 51 RHADGGrkDKVALRYLDAsrkeKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGA---IVGP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 85 MYrkaelrhlvddaGAVGiicaDTAVAENaetMQDSTVRWIVGTSDLDfqtrndPRVFGDRIRE-RH--------DGADD 155
Cdd:PRK04319 128 LF------------EAFM----EEAVRDR---LEDSEAKVLITTPALL------ERKPADDLPSlKHvllvgedvEEGPG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 156 LVELVERFRGATPEAA--EVSPTDTAILAYTSGTTGPPKGALNSH-ANILAVATTFAEL-ARVDD------------GDV 219
Cdd:PRK04319 183 TLDFNALMEQASDEFDieWTDREDGAILHYTSGSTGKPKGVLHVHnAMLQHYQTGKYVLdLHEDDvywctadpgwvtGTS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 220 VLAVAPLFHitGAVinatialmkdcTLVFANRFAADVTLDAFAEHEVT--YTigSITVFNALYNSPAATAA--HFASIKT 295
Cdd:PRK04319 263 YGIFAPWLN--GAT-----------NVIDGGRFSPERWYRILEDYKVTvwYT--APTAIRMLMGAGDDLVKkyDLSSLRH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 296 LYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDrrAPVDPASgalsIGMALPQVEIRVVDFDGTPLPDGT 375
Cdd:PRK04319 328 ILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIANYPA--MDIKPGS----MGKPLPGIEAAIVDDQGNELPPNR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 376 QGELEI-AG-PQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVG 453
Cdd:PRK04319 402 MGNLAIkKGwPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2089408387 454 EAGVVGQPDDYQGESVVAFVSLVRDAEVTEQ---ELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTE 526
Cdd:PRK04319 482 EAGVIGKPDPVRGEIIKAFVALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2-523 |
1.58e-65 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 221.09 E-value: 1.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAIAYFD--GI---LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLG 76
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIFESsgGVvrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 77 AAALVLNPMYRKAELRHLVDDAGAVGIICADTAVAENAETMQ--DSTVRWIVGTsdldfqTRNDPRVfgdrirerhDGAD 154
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQedATPLRHICLT------RVALPAD---------DGVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 155 DLVELVERFRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVI 234
Cdd:PRK08008 152 SFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 235 NATIALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPA-ATAAHFASIKTLYSggAPIPPAAVEKFEN 313
Cdd:PRK08008 232 AAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPsANDRQHCLREVMFY--LNLSDQEKDAFEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 314 KFGHYIHNAYGMTETSSGVIAVPP--DRRAPvdpasgalSIGMALPQVEIRVVDFDGTPLPDGTQGELEI---AGPQVVS 388
Cdd:PRK08008 310 RFGVRLLTSYGMTETIVGIIGDRPgdKRRWP--------SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 389 GYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGE 467
Cdd:PRK08008 382 EYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2089408387 468 SVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK08008 462 AIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
31-457 |
1.88e-65 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 217.90 E-value: 1.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMSDAFAVALV-EKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICadta 109
Cdd:TIGR01733 3 RELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 110 vaenaetmqdstvrwivgtsdldfQTRNDPRVFGDRIRERHDGADDLVELVERFRGATPEAAeVSPTDTAILAYTSGTTG 189
Cdd:TIGR01733 79 ------------------------DSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAP-SGPDDLAYVIYTSGSTG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 190 PPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLfHITGAVINATIALMKDCTLVFAN----RFAADVTLDAFAEHE 265
Cdd:TIGR01733 134 RPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASL-SFDASVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEHP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 266 VTYTIGSITVFNALynsPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGH-YIHNAYGMTETSSGVIAVPPDRraPVD 344
Cdd:TIGR01733 213 VTVLNLTPSLLALL---AAALPPALASLRLVILGGEALTPALVDRWRARGPGaRLINLYGPTETTVWSTATLVDP--DDA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 345 PASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF--------PDGRL-RTGDVAIRD 415
Cdd:TIGR01733 288 PRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLyRTGDLVRYL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2089408387 416 ADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGV 457
Cdd:TIGR01733 368 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
175-523 |
2.05e-65 |
|
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: 216.19 E-value: 2.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 175 PTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFA----- 249
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 -NRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAAtaAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTET 328
Cdd:cd05944 81 rNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVN--ADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 329 SSGVIAVPPDRraPVDPASgalsIGMALP--QVEIRVVDFDGTPLPD---GTQGELEIAGPQVVSGYWQKPEATAKTFPD 403
Cdd:cd05944 159 TCLVAVNPPDG--PKRPGS----VGLRLPyaRVRIKVLDGVGRLLRDcapDEVGEICVAGPGVFGGYLYTEGNKNAFVAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 404 GRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE 483
Cdd:cd05944 233 GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2089408387 484 QELRAFVGDRLAAYKR-PKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05944 313 EELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
12-522 |
5.60e-65 |
|
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: 219.30 E-value: 5.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 12 VAANPEHPAIAYFDG--ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKA 89
Cdd:cd05923 11 ASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 90 ELRHLVDDAGAVGIICADtaVAENAETMQDSTVRwIVGTSDLDfqtrndprvfGDRIRERHdgaddlvelverfrGATPE 169
Cdd:cd05923 91 ELAELIERGEMTAAVIAV--DAQVMDAIFQSGVR-VLALSDLV----------GLGEPESA--------------GPLIE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 170 AAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELA--RVDDGDVVLAVAPLFHITG--AVINATIALmkDCT 245
Cdd:cd05923 144 DPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAglRHGRHNVVLGLMPLYHVIGffAVLVAALAL--DGT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 246 LVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGM 325
Cdd:cd05923 222 YVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 326 TETSSGVIAvpPDRRAPVDPASGALSigmalpqvEIRVVDFDGTP---LPDGTQGELEIA--GPQVVSGYWQKPEATAKT 400
Cdd:cd05923 302 TEAMNSLYM--RDARTGTEMRPGFFS--------EVRIVRIGGSPdeaLANGEEGELIVAaaADAAFTGYLNQPEATAKK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 401 FPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVsLVRDAE 480
Cdd:cd05923 372 LQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACV-VPREGT 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2089408387 481 VTEQELRAFVGD-RLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd05923 451 LSADELDQFCRAsELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
32-524 |
8.77e-65 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 220.24 E-value: 8.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 32 EVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICADTava 111
Cdd:PLN02330 60 EVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT--- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 112 eNAETMQDSTVRWIVgtsdldfqtrndprvFGDRIRERHDGADDLVELVERfRGATPEAAEVSPTDTAILAYTSGTTGPP 191
Cdd:PLN02330 137 -NYGKVKGLGLPVIV---------------LGEEKIEGAVNWKELLEAADR-AGDTSDNEEILQTDLCALPFSSGTTGIS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 192 KGALNSHANILA--VATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVTYT 269
Cdd:PLN02330 200 KGVMLTHRNLVAnlCSSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 270 IGSITVFNALYNSPAATAAHFASIK--TLYSGGAPIPPAAVEKFENKF-GHYIHNAYGMTETSSGVIAVPpdrrapvDPA 346
Cdd:PLN02330 280 PIVPPIILNLVKNPIVEEFDLSKLKlqAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCITLTHG-------DPE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 347 SG-----ALSIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGW 419
Cdd:PLN02330 353 KGhgiakKNSVGFILPNLEVKFIDPDtGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 420 IYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKR 499
Cdd:PLN02330 433 IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKK 512
|
490 500
....*....|....*....|....*
gi 2089408387 500 PKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PLN02330 513 VRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
41-523 |
1.37e-64 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 217.31 E-value: 1.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 41 AVALVEKGVGHGDRVGIHLQN----IPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICADTAVAENAET 116
Cdd:cd05922 7 ASALLEAGGVRGERVVLILPNrftyIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 117 MQDSTvrwivgtsdldfqtrnDPRVF--GDRIRERHDGADdlvelverfrgatpeAAEVSPTDTAILAYTSGTTGPPKGA 194
Cdd:cd05922 87 LPASP----------------DPGTVldADGIRAARASAP---------------AHEVSHEDLALLLYTSGSTGSPKLV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 195 LNSHANILAVATTFAELARVDDGDVVLAVAPLFHITG-AVINatIALMKDCTLVFANRFAADVTL-DAFAEHEVTYTIGS 272
Cdd:cd05922 136 RLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGlSVLN--THLLRGATLVLTNDGVLDDAFwEDLREHGATGLAGV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 273 ITVFNALYNSPAATAAhFASIKTLYSGGAPIPPAAVEKFENKF-GHYIHNAYGMTETSSGVIAVPPDRrapVDPASGalS 351
Cdd:cd05922 214 PSTYAMLTRLGFDPAK-LPSLRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPER---ILEKPG--S 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 352 IGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKP-EATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQI 430
Cdd:cd05922 288 IGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 431 NVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDyQGESVVAFVslVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELP 510
Cdd:cd05922 368 KLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFV--TAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELP 444
|
490
....*....|...
gi 2089408387 511 KTQTGKIRRTELR 523
Cdd:cd05922 445 LTASGKVDYAALR 457
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
29-523 |
5.69e-64 |
|
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: 215.03 E-value: 5.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 29 SAREVDEMSDAFAVALVEKGVGH-GDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICAD 107
Cdd:cd05958 12 TYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALCAH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 tavaenAETMQDstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsptDTAILAYTSGT 187
Cdd:cd05958 92 ------ALTASD---------------------------------------------------------DICILAFTSGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANILAVATTFA-ELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEV 266
Cdd:cd05958 109 TGAPKATMHFHRDPLASADRYAvNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 267 TYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDRRAPvdpa 346
Cdd:cd05958 189 TVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARP---- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 347 sGALsiGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPqvvSGYWQKPEATAKT-FPDGRLRTGDVAIRDADGWIYLVDR 425
Cdd:cd05958 265 -GAT--GKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTyVQGGWNITGDTYSRDPDGYFRHQGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 426 LKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL---VRDAEVTEQELRAFVGDRLAAYKRPKH 502
Cdd:cd05958 339 SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLrpgVIPGPVLARELQDHAKAHIAPYKYPRA 418
|
490 500
....*....|....*....|.
gi 2089408387 503 IHIVDELPKTQTGKIRRTELR 523
Cdd:cd05958 419 IEFVTELPRTATGKLQRFALR 439
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
6-523 |
2.45e-63 |
|
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: 215.82 E-value: 2.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 6 DVWKARVAANPEHPAIAYFDG-----ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAAL 80
Cdd:cd05970 21 DVVDAMAKEYPDKLALVWCDDageerIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 81 VLNPMYRKAELRHLVDDAGAVGIICADTA-----VAENAETMQDSTVRWIVGTSDLDfqtrndprvfgdrirerhdGADD 155
Cdd:cd05970 101 PATHQLTAKDIVYRIESADIKMIVAIAEDnipeeIEKAAPECPSKPKLVWVGDPVPE-------------------GWID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 156 LVELVERFRGA-TPEAAEVSPT--DTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlfhiTG- 231
Cdd:cd05970 162 FRKLIKNASPDfERPTANSYPCgeDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVAD----TGw 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 232 --AVINATIALMKDCTLVFA---NRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAaTAAHFASIKTLYSGGAPIPPA 306
Cdd:cd05970 238 gkAVWGKIYGQWIAGAAVFVydyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLRYCTTAGEALNPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 307 AVEKFENKFGHYIHNAYGMTETSSGVIAVPPdrrapVDPASGalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQ- 385
Cdd:cd05970 317 VFNTFKEKTGIKLMEGFGQTETTLTIATFPW-----MEPKPG--SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKg 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 386 ----VVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQP 461
Cdd:cd05970 390 kpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVP 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 462 DDYQGESVVAFVSLVRD---AEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05970 470 DPIRGQVVKATIVLAKGyepSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
177-519 |
6.31e-63 |
|
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: 208.89 E-value: 6.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADV 256
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 257 TLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFG-HYIHNAYGMTETSSGVIAV 335
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 336 PPDrrapvDPASGALSIGMALPQVEIRVVDfdgtplpdgtQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIR 414
Cdd:cd17638 161 PGD-----DAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 415 DADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRL 494
Cdd:cd17638 226 DERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERL 305
|
330 340
....*....|....*....|....*
gi 2089408387 495 AAYKRPKHIHIVDELPKTQTGKIRR 519
Cdd:cd17638 306 ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
8-524 |
7.28e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 213.59 E-value: 7.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 8 WKARvaANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYR 87
Cdd:PRK06145 10 FHAR--RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 88 KAELRHLVDDAGAvGIICADTAVAENAETMQDSTVrwivgtsdLDFQTRNDPRVFGdrirerHDGAddlvelverfrgAT 167
Cdd:PRK06145 88 ADEVAYILGDAGA-KLLLVDEEFDAIVALETPKIV--------IDAAAQADSRRLA------QGGL------------EI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 168 PEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLV 247
Cdd:PRK06145 141 PPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 248 FANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKF--GHYIhNAYGM 325
Cdd:PRK06145 221 IHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFtrARYI-DAYGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 326 TETSSGVIAVPPDRRapVDPASgalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGR 405
Cdd:PRK06145 300 TETCSGDTLMEAGRE--IEKIG---STGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 406 LRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQE 485
Cdd:PRK06145 375 FRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEA 454
|
490 500 510
....*....|....*....|....*....|....*....
gi 2089408387 486 LRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK06145 455 LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
11-522 |
1.14e-62 |
|
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: 212.96 E-value: 1.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 11 RVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAE 90
Cdd:cd17655 6 QAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 91 LRHLVDDAGAvGIICADTAVAENAETMQDstvrwIVGTSDLDFQtrndprvfgdrirerHDGADDLvelverfrgatpeA 170
Cdd:cd17655 86 IQYILEDSGA-DILLTQSHLQPPIAFIGL-----IDLLDEDTIY---------------HEESENL-------------E 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 171 AEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIALMKDCTLVF-- 248
Cdd:cd17655 132 PVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFAS-ISFDASVTEIFASLLSGNTLYIvr 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 249 -ANRFAADVTLDAFAEHEVTYTIGSITVFNALynsPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGH--YIHNAYGM 325
Cdd:cd17655 211 kETVLDGQALTQYIRQNRITIIDLTPAHLKLL---DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 326 TETSSGVIAVPPDrraPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF---- 401
Cdd:cd17655 288 TETTVDASIYQYE---PETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFvddp 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 --PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDyQGESVV-AFVslVR 477
Cdd:cd17655 365 fvPGERMyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDE-QGQNYLcAYI--VS 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2089408387 478 DAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17655 442 EKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
28-523 |
1.01e-60 |
|
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: 210.42 E-value: 1.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICAD 107
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 TAVAENaetmqdstvRWIVGTSDLDFQTRNDPRVfGDRIRERHDGADDLVELV------ERFRGATPEAAEVSPTDTAIL 181
Cdd:cd05968 172 GFTRRG---------REVNLKEEADKACAQCPTV-EKVVVVRHLGNDFTPAKGrdlsydEEKETAGDGAERTESEDPLMI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 182 AYTSGTTGPPKGALNSHANI-LAVATTFAELARVDDGDVVLAVAPL------FHITGAVINATIALMKDCTLVFAnrfAA 254
Cdd:cd05968 242 IYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLgwmmgpWLIFGGLILGATMVLYDGAPDHP---KA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 255 DVTLDAFAEHEVTYTIGSITVFNALY-NSPAATAAH-FASIKTLYSGGAPIPPAAVEKFENKFGHY---IHNAYGMTETS 329
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRALKpRGDAPVNAHdLSSLRVLGSTGEPWNPEPWNWLFETVGKGrnpIINYSGGTEIS 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 330 SGVIAVPPDRraPVDPASgalsIGMALPQVEIRVVDFDGTPLPDgTQGELEIAGPQV--VSGYWQKPEATAKTF---PDG 404
Cdd:cd05968 399 GGILGNVLIK--PIKPSS----FNGPVPGMKADVLDESGKPARP-EVGELVLLAPWPgmTRGFWRDEDRYLETYwsrFDN 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 405 RLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL---VRDAEV 481
Cdd:cd05968 472 VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLkpgVTPTEA 551
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2089408387 482 TEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05968 552 LAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
20-523 |
1.05e-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: 208.92 E-value: 1.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 20 AIAYFDGI----LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:cd17642 33 TIAFTDAHtgvnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIICADTA------VAENAETMQ-----DSTVRWIVGTSDLDFQTRNDPRVFGdrirerhdgaddlvelVERFr 164
Cdd:cd17642 113 NISKPTIVFCSKKGlqkvlnVQKKLKIIKtiiilDSKEDYKGYQCLYTFITQNLPPGFN----------------EYDF- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 165 gaTPEAAEvSPTDTAILAYTSGTTGPPKGALNSHANILA-----VATTFAElaRVDDGDVVLAVAPLFHITGAVINATIA 239
Cdd:cd17642 176 --KPPSFD-RDEQVALIMNSSGSTGLPKGVQLTHKNIVArfshaRDPIFGN--QIIPDTAILTVIPFHHGFGMFTTLGYL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 240 LmkdC--TLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFG- 316
Cdd:cd17642 251 I---CgfRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKl 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 317 HYIHNAYGMTETSSGVIAVPPDRRAPVdpasgalSIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPE 395
Cdd:cd17642 328 PGIRQGYGLTETTSAILITPEGDDKPG-------AVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 396 AT-AKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVS 474
Cdd:cd17642 401 ATkALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2089408387 475 LVRDAEVTEQELRAFVGDRLAAYKRPK-HIHIVDELPKTQTGKIRRTELR 523
Cdd:cd17642 481 LEAGKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
12-524 |
3.22e-60 |
|
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: 209.34 E-value: 3.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 12 VAANPEHPAIaYFDG-------ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNP 84
Cdd:cd05966 63 LKERGDKVAI-IWEGdepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 85 MYRKAELRHLVDDAGAVGIICAD-----------TAVAENAETMQDSTVRWIVgtsdldFQTRNDPRVFgdrirerHDGA 153
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITADggyrggkviplKEIVDEALEKCPSVEKVLV------VKRTGGEVPM-------TEGR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 154 D-DLVELVERFRGATPeAAEVSPTDTAILAYTSGTTGPPKGALNSHA-NILAVATTFAELARVDDGDVVLAVAPLFHITG 231
Cdd:cd05966 209 DlWWHDLMAKQSPECE-PEWMDSEDPLFILYTSGSTGKPKGVVHTTGgYLLYAATTFKYVFDYHPDDIYWCTADIGWITG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 232 -------AVINATIALMKDCTLVFANrfaADVTLDAFAEHEVTytigsitvfnALYNSPAA-----------TAAH-FAS 292
Cdd:cd05966 288 hsyivygPLANGATTVMFEGTPTYPD---PGRYWDIVEKHKVT----------IFYTAPTAiralmkfgdewVKKHdLSS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 293 IKTLYSGGAPIPPAAVEKFENKFGHY---IHNAYGMTETSSGVIAVPPDRrAPVDPASGalsiGMALPQVEIRVVDFDGT 369
Cdd:cd05966 355 LRVLGSVGEPINPEAWMWYYEVIGKErcpIVDTWWQTETGGIMITPLPGA-TPLKPGSA----TRPFFGIEPAILDEEGN 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 370 PLPDGTQGELEIAGP-------------QVVSGYWQKpeataktFPdGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYK 436
Cdd:cd05966 430 EVEGEVEGYLVIKRPwpgmartiygdheRYEDTYFSK-------FP-GYYFTGDGARRDEDGYYWITGRVDDVINVSGHR 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 437 VWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL---VRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQ 513
Cdd:cd05966 502 LGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLkdgEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTR 581
|
570
....*....|.
gi 2089408387 514 TGKIRRTELRN 524
Cdd:cd05966 582 SGKIMRRILRK 592
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
21-523 |
7.44e-60 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 205.84 E-value: 7.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 21 IAYFDGI--LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDA 98
Cdd:TIGR02262 22 TAFIDDIssLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 99 GAVGIICADTAVAENAETMQDS-TVRWIVGTSDldfqtrndprvfgdrireRHDGADDLVELV----ERFrgatpEAAEV 173
Cdd:TIGR02262 102 RARVVFVSGALLPVIKAALGKSpHLEHRVVVGR------------------PEAGEVQLAELLatesEQF-----KPAAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 174 SPTDTAILAYTSGTTGPPKGALNSHANILAVATTFA-ELARVDDGDVVLAVAPLFHITGaVINATIALMK--DCTLVFAN 250
Cdd:TIGR02262 159 QADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYArNTLGIREDDVCFSAAKLFFAYG-LGNALTFPMSvgATTVLMGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSS 330
Cdd:TIGR02262 238 RPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 331 GVIAVPPDRrapVDPASGalsiGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGD 410
Cdd:TIGR02262 318 IFLSNLPGD---VRYGTS----GKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 411 VAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFV 490
Cdd:TIGR02262 391 KYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHV 470
|
490 500 510
....*....|....*....|....*....|...
gi 2089408387 491 GDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:TIGR02262 471 KDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
2-523 |
1.74e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 205.75 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALV 81
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNPMYRKAELRHLVDDAGAVGIICADT----AVAENAETMQDSTVRWIVGTSDLDFQTRNDP-RVFGDRirerhdgaddl 156
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWPGfkgiDFAAILAAVPPDALPPLRAIAVVDDAADATPaPAPGAR----------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 157 VELVERFRGATPEAAEVSPTDT---AILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL---FHIT 230
Cdd:PRK06164 159 VQLFALPDPAPPAAAGERAADPdagALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFcgvFGFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 231 GAVInatiALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSpAATAAHFASIKTLysGGAPIPPAAVEK 310
Cdd:PRK06164 239 TLLG----ALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDT-AGERADFPSARLF--GFASFAPALGEL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 311 FE--NKFGHYIHNAYGmtetSSGVIAVPPDRRAPVDPASGALSIGM-ALPQVEIRVVD-FDGTPLPDGTQGELEIAGPQV 386
Cdd:PRK06164 312 AAlaRARGVPLTGLYG----SSEVQALVALQPATDPVSVRIEGGGRpASPEARVRARDpQDGALLPDGESGEIEIRAPSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 387 VSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQ 465
Cdd:PRK06164 388 MRGYLDNPDATARALtDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGK 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 466 GEsVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTG---KIRRTELR 523
Cdd:PRK06164 468 TV-PVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
4-526 |
3.83e-59 |
|
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: 204.62 E-value: 3.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 4 LVDVW--KARVAANPEHPAIAYFDG-----ILSAREVDEMSDAFAVALVEK-GVGHGDRVGIHLQNIPQYAIAFLALWKL 75
Cdd:cd05928 11 VLDQWadKEKAGKRPPNPALWWVNGkgdevKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 76 GaaaLVLNP----MYRKaELRHLVDDAGAVGIICADT-AVAENAETMQDSTVRWIVGTSDldfqtrndprvfgdrirERH 150
Cdd:cd05928 91 G---LVFIPgtiqLTAK-DILYRLQASKAKCIVTSDElAPEVDSVASECPSLKTKLLVSE-----------------KSR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 151 DGADDLVELverFRGATPE--AAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELAR-VDDGDVVLAVAPlf 227
Cdd:cd05928 150 DGWLNFKEL---LNEASTEhhCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLdLTASDIMWNTSD-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 228 hiTGAVINATIALMKDCTL---VFAN---RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAaTAAHFASIKTLYSGGA 301
Cdd:cd05928 225 --TGWIKSAWSSLFEPWIQgacVFVHhlpRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDL-SSYKFPSLQHCVTGGE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 302 PIPPAAVEKFENKFGHYIHNAYGMTETssGVIAVPPdRRAPVDPASgalsIGMALPQVEIRVVDFDGTPLPDGTQGELEI 381
Cdd:cd05928 302 PLNPEVLEKWKAQTGLDIYEGYGQTET--GLICANF-KGMKIKPGS----MGKASPPYDVQIIDDNGNVLPPGTEGDIGI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 382 -AGPQ----VVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAG 456
Cdd:cd05928 375 rVKPIrpfgLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESA 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 457 VVGQPDDYQGESVVAFVSLV-----RDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTE 526
Cdd:cd05928 455 VVSSPDPIRGEVVKAFVVLApqflsHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
29-517 |
5.34e-59 |
|
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: 205.50 E-value: 5.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 29 SAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICAD- 107
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 ----------TAVAENAETMQDSTVRWIVgtsdldFQTRNDPRVFGDrirerhDGAD-DLVELVERfRGATPEAAEVSPT 176
Cdd:cd17634 166 gvragrsvplKKNVDDALNPNVTSVEHVI------VLKRTGSDIDWQ------EGRDlWWRDLIAK-ASPEHQPEAMNAE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHAN-ILAVATTFAELARVDDGDVVLAVAPL-------FHITGAVINATIALMKDCTlvf 248
Cdd:cd17634 233 DPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVgwvtghsYLLYGPLACGATTLLYEGV--- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 249 ANRFAADVTLDAFAEHEVTYTIGSITVFNALYNS-PAATAAH-FASIKTLYSGGAPIPPAAVEKFENKFGHY---IHNAY 323
Cdd:cd17634 310 PNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAgDDAIEGTdRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTW 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 324 GMTETSSGVIavpPDRRAPVDPASGalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGP---QVVSGYWQKP---EAT 397
Cdd:cd17634 390 WQTETGGFMI---TPLPGAIELKAG--SATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpgQTRTLFGDHErfeQTY 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 398 AKTFpDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL-- 475
Cdd:cd17634 465 FSTF-KGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLnh 543
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2089408387 476 -VRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKI 517
Cdd:cd17634 544 gVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
5-523 |
5.71e-59 |
|
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: 206.33 E-value: 5.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 5 VDVWkarVAANPEHPAIaYFDG-------ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGA 77
Cdd:TIGR02188 63 VDRH---LEARPDKVAI-IWEGdepgevrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 78 AALVLNPMYRKAELRHLVDDAGAVGIICADT-----------AVAENAETMQDSTVRW-IVgtsdldfqtrndPRVFGDR 145
Cdd:TIGR02188 139 IHSVVFGGFSAEALADRINDAGAKLVITADEglrggkviplkAIVDEALEKCPVSVEHvLV------------VRRTGNP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 146 IRERHDGAD-DLVELVERFRgATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHAN-ILAVATTFAELARVDDGDVVLAV 223
Cdd:TIGR02188 207 VVPWVEGRDvWWHDLMAKAS-AYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGyLLYAAMTMKYVFDIKDGDIFWCT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 224 APLFHITG-------AVINATIALMKDCTLVFAN--RFAADVTldafaEHEVTytigsitvfnALYNSPAATAAHFA--- 291
Cdd:TIGR02188 286 ADVGWITGhsyivygPLANGATTVMFEGVPTYPDpgRFWEIIE-----KHKVT----------IFYTAPTAIRALMRlgd 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 292 ---------SIKTLYSGGAPIPPAAVEKFENKFGH---YIHNAYGMTETSSGVIAvppdrrapvdPASGALSI--GMA-- 355
Cdd:TIGR02188 351 ewvkkhdlsSLRLLGSVGEPINPEAWMWYYKVVGKercPIVDTWWQTETGGIMIT----------PLPGATPTkpGSAtl 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 356 -LPQVEIRVVDFDGTPLPD-GTQGELEIAG--PQVVSGYWQKPEATAKT----FPdGRLRTGDVAIRDADGWIYLVDRLK 427
Cdd:TIGR02188 421 pFFGIEPAVVDEEGNPVEGpGEGGYLVIKQpwPGMLRTIYGDHERFVDTyfspFP-GYYFTGDGARRDKDGYIWITGRVD 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 428 DQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL---VRDAEVTEQELRAFVGDRLAAYKRPKHIH 504
Cdd:TIGR02188 500 DVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLkdgYEPDDELRKELRKHVRKEIGPIAKPDKIR 579
|
570
....*....|....*....
gi 2089408387 505 IVDELPKTQTGKIRRTELR 523
Cdd:TIGR02188 580 FVPGLPKTRSGKIMRRLLR 598
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
4-519 |
2.03e-58 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 202.81 E-value: 2.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 4 LVDVWKARVAANPEHPAIAYFDG--ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALV 81
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNPMYRKAELRHLVDDAGAVGIICADTAVAENAEtmqdSTVRWIVGTSdldfqtrndpRVFGDRirerhdGADDLVELVE 161
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDADGPHDRAE----PTTRWWPLTV----------NVGGDS------GPSGGTLSVH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 162 RFRGATPEAAEVSPT----DTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITG--AVIN 235
Cdd:PRK05852 158 LDAATEPTPATSTPEglrpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGliAALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 236 ATIALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHF--ASIKTLYSGGAPIPPAAVEKFEN 313
Cdd:PRK05852 238 ATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 314 KFGHYIHNAYGMTE-----TSSGVIAVPPDRRAPVDPASGALSIGmalpqVEIRVVDFDGTPLPDGTQGELEIAGPQVVS 388
Cdd:PRK05852 318 EFAAPVVCAFGMTEathqvTTTQIEGIGQTENPVVSTGLVGRSTG-----AQIRIVGSDGLPLPAGAVGEVWLRGTTVVR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 389 GYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGES 468
Cdd:PRK05852 393 GYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 469 VVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRR 519
Cdd:PRK05852 473 VAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
177-524 |
2.75e-58 |
|
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: 196.40 E-value: 2.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITG-AVINATIALmkDCTLVFANRfAAD 255
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGlAILVRSLLA--GAELVLLER-NQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 256 VTLDAfAEHEVTYTIGSITVFNALYNSPAATAAhFASIKTLYSGGAPIPPAAVEKFENKfGHYIHNAYGMTETSSGVIAV 335
Cdd:cd17630 78 LAEDL-APPGVTHVSLVPTQLQRLLDSGQGPAA-LKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 336 PPDRrapvdpaSGALSIGMALPQVEIRVVDfdgtplpdgtQGELEIAGPQVVSGYWqKPEATAKTFPDGRLRTGDVAIRD 415
Cdd:cd17630 155 RPDG-------FGRGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 416 ADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLvrDAEVTEQELRAFVGDRLA 495
Cdd:cd17630 217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG--RGPADPAELRAWLKDKLA 294
|
330 340
....*....|....*....|....*....
gi 2089408387 496 AYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:cd17630 295 RFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
20-523 |
3.05e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 201.29 E-value: 3.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 20 AIAYFDG-ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQY-AIAFLALwklgAAALVLNPMYRK---AELRHL 94
Cdd:PRK08276 3 VIMAPSGeVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFfEVYWAAR----RSGLYYTPINWHltaAEIAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 95 VDDAGAVGII----CADTAVAENAETMQDSTVRWIVGtsdldfqtrndprvfgdrirERHDGADDLVELVERFRgATPEA 170
Cdd:PRK08276 79 VDDSGAKVLIvsaaLADTAAELAAELPAGVPLLLVVA--------------------GPVPGFRSYEEALAAQP-DTPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 171 AEVSPTDtaiLAYTSGTTGPPKGALN--SHANILAVATTFAELA----RVDDGDVVLAVAPLFHitGAVIN-ATIALMKD 243
Cdd:PRK08276 138 DETAGAD---MLYSSGTTGRPKGIKRplPGLDPDEAPGMMLALLgfgmYGGPDSVYLSPAPLYH--TAPLRfGMSALALG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 244 CTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHF--ASIKTLYSGGAPIPPAAVEKFENKFGHYIHN 321
Cdd:PRK08276 213 GTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYdvSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 322 AYGMTETSSGVIAVPPDRRApvDPASgalsIGMALpQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF 401
Cdd:PRK08276 293 YYASSEGGGVTVITSEDWLA--HPGS----VGKAV-LGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAAR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 -PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAE 480
Cdd:PRK08276 366 nPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2089408387 481 VTE---QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK08276 446 AGDalaAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
23-519 |
5.20e-58 |
|
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: 199.98 E-value: 5.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 23 YFDGI-LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAV 101
Cdd:cd05914 2 YYGGEpLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 102 GIICADtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsPTDTAIL 181
Cdd:cd05914 82 AIFVSD-------------------------------------------------------------------EDDVALI 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 182 AYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVtLDAF 261
Cdd:cd05914 95 NYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAK-IIAL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 262 AEHEVTYTIGS----------------------------ITVFNALYNSPAATAAHFA---SIKTLYSGGAPIPPAaVEK 310
Cdd:cd05914 174 AFAQVTPTLGVpvplviekifkmdiipkltlkkfkfklaKKINNRKIRKLAFKKVHEAfggNIKEFVIGGAKINPD-VEE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 311 FENKFGHYIHNAYGMTETSSGVIAVPPDRRApvdpasgALSIGMALPQVEIRVVDfdgtPLPDGTQGELEIAGPQVVSGY 390
Cdd:cd05914 253 FLRTIGFPYTIGYGMTETAPIISYSPPNRIR-------LGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 391 WQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQI-NVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGES 468
Cdd:cd05914 322 YKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALA 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2089408387 469 VVAFVSL-------VRDAEVTEQELRAFVGDRLAAYKRPKHIHIV-DELPKTQTGKIRR 519
Cdd:cd05914 402 YIDPDFLdvkalkqRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
28-523 |
6.59e-58 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 201.99 E-value: 6.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEK-GVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAvgiiCA 106
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSV----GL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 107 DTAVAENAETMQDSTVRWIVGTSDLDFqtrndprvfgdrirerhdgaDDLVELVERFRGATPEAAEVSPT------DTAI 180
Cdd:PLN02574 143 AFTSPENVEKLSPLGVPVIGVPENYDF--------------------DSKRIEFPKFYELIKEDFDFVPKpvikqdDVAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 181 LAYTSGTTGPPKGALNSHANILAVATTF-----AELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAAD 255
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVELFvrfeaSQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDAS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 256 VTLDAFAEHEVTYTIGSITVFNALYNSPAATAAH-FASIKTLYSGGAPIPPAAVEKFENKFGHY-IHNAYGMTETSsgvi 333
Cdd:PLN02574 283 DMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEvLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTEST---- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 334 AVPpDRRAPVDPASGALSIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDV 411
Cdd:PLN02574 359 AVG-TRGFNTEKLSKYSSVGLLAPNMQAKVVDWStGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIdKDGWLRTGDI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 412 AIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVG 491
Cdd:PLN02574 438 AYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVA 517
|
490 500 510
....*....|....*....|....*....|..
gi 2089408387 492 DRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PLN02574 518 KQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
16-522 |
1.18e-56 |
|
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: 195.99 E-value: 1.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIIcadtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaeVSP 175
Cdd:cd17643 81 ADSGPSLLL--------------------------------------------------------------------TDP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 TDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLavapLFHITG---AVINATIALMKDCTLVFANRf 252
Cdd:cd17643 93 DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSYAfdfSVWEIWGALLHGGRLVVVPY- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 253 aaDVTLDAFAEHEVTYTIGsITVFN----ALY-NSPAATAAHFASIKTLYS--GGAPIPPAAVEKFENKFGHY---IHNA 322
Cdd:cd17643 168 --EVARSPEDFARLLRDEG-VTVLNqtpsAFYqLVEAADRDGRDPLALRYVifGGEALEAAMLRPWAGRFGLDrpqLVNM 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 323 YGMTETSSGVIAVPPDrraPVD-PASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF 401
Cdd:cd17643 245 YGITETTVHVTFRPLD---AADlPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 ---PDG----RL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFV 473
Cdd:cd17643 322 vanPFGgpgsRMyRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYV 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2089408387 474 SLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17643 402 VADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-524 |
1.79e-56 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 195.04 E-value: 1.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICad 107
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 tavaenaetmqdstvrwivgtsDLDfqtrndprvfgdrirERHDGADDLveLVERFrgatpeaaevsptdtailayTSGT 187
Cdd:cd05973 79 ----------------------DAA---------------NRHKLDSDP--FVMMF--------------------TSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAP-------LFHITGAVinatiaLMKDCTLVFANRFAADVTLDA 260
Cdd:cd05973 100 TGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADpgwayglYYAITGPL------ALGHPTILLEGGFSVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 261 FAEHEVTYTIGSITVFNALYNSPAATAAHF-ASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSgVIAvppDR 339
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLLMAAGAEVPARPkGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGM-VLA---NH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 340 RAPVDPASgALSIGMALPQVEIRVVDFDGTPLPDGTQGELEI---AGPQV-VSGYWQKPEATaktfPDGR-LRTGDVAIR 414
Cdd:cd05973 250 HALEHPVH-AGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPA----IDGGyYLTGDTVEF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 415 DADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVT---EQELRAFVG 491
Cdd:cd05973 325 DPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVK 404
|
490 500 510
....*....|....*....|....*....|...
gi 2089408387 492 DRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:cd05973 405 KRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
16-523 |
1.92e-56 |
|
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: 195.28 E-value: 1.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIICADtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsP 175
Cdd:cd17649 81 EDSGAGLLLTHH-------------------------------------------------------------------P 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 TDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIALMKDCTLVFAN--RFA 253
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPdeLWA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 254 -ADVTLDAFAEHEVTytIGSITvfNALYNSPAATAAHF-----ASIKTLYSGGAPIPPAAVEKFEnKFGHYIHNAYGMTE 327
Cdd:cd17649 173 sADELAEMVRELGVT--VLDLP--PAYLQQLAEEADRTgdgrpPSLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 328 TSSGVIAVPPDRRAPVDPASgaLSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF------ 401
Cdd:cd17649 248 ATVTPLVWKCEAGAARAGAS--MPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpdpfg 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 -PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDyQGESVVAFVSLVRDA 479
Cdd:cd17649 326 aPGSRLyRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRAAA 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2089408387 480 EVTE--QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd17649 405 AQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-527 |
2.09e-56 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 204.62 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 8 WKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYR 87
Cdd:PRK12467 518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 88 KAELRHLVDDAGavgiicadtavaenaetmqdstVRWIVGTSDldfQTRNDPRVFGDRIRERHDGADdlveLVERFRGAT 167
Cdd:PRK12467 598 QDRLAYMLDDSG----------------------VRLLLTQSH---LLAQLPVPAGLRSLCLDEPAD----LLCGYSGHN 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 168 PEAAeVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIALMKDCTLV 247
Cdd:PRK12467 649 PEVA-LDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVST-FAFDLGVTELFGALASGATLH 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 248 FANR---FAADVTLDAFAEHEVTYTIGSITVFNALYNSPAAtaAHFASIKTLYSGGAPIPPAAVEK-FENKFGHYIHNAY 323
Cdd:PRK12467 727 LLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRV--ALPRPQRALVCGGEALQVDLLARvRALGPGARLINHY 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 324 GMTETSSGViAVPPDRRAPVDpaSGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-P 402
Cdd:PRK12467 805 GPTETTVGV-STYELSDEERD--FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFvP 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 403 D------GRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDyQGESVVAFVSL 475
Cdd:PRK12467 882 DpfgadgGRLyRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AGLQLVAYLVP 960
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2089408387 476 VRDAEVTEQ-----ELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEA 527
Cdd:PRK12467 961 AAVADGAEHqatrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDA 1017
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
16-522 |
1.66e-55 |
|
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: 194.62 E-value: 1.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:TIGR03098 14 PDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIICADTAVAENAETMQdstvrwivGTSDLDFQTRndprvFGDRIRERHDGADDLVELVERFRGATPEAA--EV 173
Cdd:TIGR03098 94 ADCNVRLLVTSSERLDLLHPALP--------GCHDLRTLII-----VGDPAHASEGHPGEEPASWPKLLALGDADPphPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 174 SPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGaVINATIALMKDCTLVFANRFA 253
Cdd:TIGR03098 161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYG-FNQLTTAFYVGATVVLHDYLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 254 ADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAhFASIKTLYSGGAPIPPAAVEKFENKFGHY-IHNAYGMTETSSGV 332
Cdd:TIGR03098 240 PRDVLKALEKHGITGLAAVPPLWAQLAQLDWPESA-APSLRYLTNSGGAMPRATLSRLRSFLPNArLFLMYGLTEAFRST 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 333 IaVPPDRrapVDPASGalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF------PDGRL 406
Cdd:TIGR03098 319 Y-LPPEE---VDRRPD--SIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrplppfPGELH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 407 RT------GDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAE 480
Cdd:TIGR03098 393 LPelavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2089408387 481 VTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:TIGR03098 473 LDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
10-522 |
4.25e-55 |
|
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: 191.76 E-value: 4.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 10 ARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKA 89
Cdd:cd12115 7 AQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 90 ELRHLVDDAGAVGIIcadtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpe 169
Cdd:cd12115 87 RLRFILEDAQARLVL----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 170 aaeVSPTDTAILAYTSGTTGPPKGALNSHANILA----VATTFA--ELARVddgdvvLAVAPL-FHITGAVINATiaLMK 242
Cdd:cd12115 102 ---TDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAflqwAAAAFSaeELAGV------LASTSIcFDLSVFELFGP--LAT 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 243 DCTLVFANrfAADVTLDAFAEHEVTytigsitvfnaLYNS-PAATAAHF------ASIKTLYSGGAPIPPAAVEK-FENK 314
Cdd:cd12115 171 GGKVVLAD--NVLALPDLPAAAEVT-----------LINTvPSAAAELLrhdalpASVRVVNLAGEPLPRDLVQRlYARL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 315 FGHYIHNAYGMTE--TSSGVIAVPPDrrapvdpASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQ 392
Cdd:cd12115 238 QVERVVNLYGPSEdtTYSTVAPVPPG-------ASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 393 KPEATAKTF------PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQ 465
Cdd:cd12115 311 RPGLTAERFlpdpfgPGARLyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2089408387 466 GESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd12115 391 ERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-531 |
7.43e-55 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 200.18 E-value: 7.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 10 ARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKA 89
Cdd:PRK12316 2011 EQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE 2090
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 90 ELRHLVDDAGAVGIICaDTAVAENAETMQdstvrwivGTSDLDFqtrndprvfgdrirerhDGADDLVElverfRGATPE 169
Cdd:PRK12316 2091 RLAYMLEDSGAALLLT-QRHLLERLPLPA--------GVARLPL-----------------DRDAEWAD-----YPDTAP 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 170 AAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAV-------INATIALMK 242
Cdd:PRK12316 2140 AVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMS-FSFDGAHeqwfhplLNGARVLIR 2218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 243 DCTLVFANRfaadvTLDAFAEHEVTytigsITVFNALY----NSPAATAAHFASIKTLYSGGAPIPPAAVEK-FENKFGH 317
Cdd:PRK12316 2219 DDELWDPEQ-----LYDEMERHGVT-----ILDFPPVYlqqlAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPV 2288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 318 YIHNAYGMTETssgVIAVPPDRRAPVDPASGA-LSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEA 396
Cdd:PRK12316 2289 YLFNGYGPTEA---VVTPLLWKCRPQDPCGAAyVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGL 2365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 397 TAKTF-PD------GRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQpDDYQGES 468
Cdd:PRK12316 2366 TAERFvPDpfsasgERLyRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQ 2444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 469 VVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEAKVTR 531
Cdd:PRK12316 2445 LVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLR 2507
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
16-522 |
9.09e-54 |
|
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: 188.63 E-value: 9.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGIIcADTAVAENAEtmqdstvrwivgtsdldfqtrndprvfgDRIRERHDGADDLVelverfRGATPEAAEVSP 175
Cdd:cd12114 81 ADAGARLVL-TDGPDAQLDV----------------------------AVFDVLILDLDALA------APAPPPPVDVAP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 TDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL------FHITGAvinatiaLMKDCTLVFA 249
Cdd:cd12114 126 DDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLsfdlsvYDIFGA-------LSAGATLVLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 N---RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGH-YIHNAYGM 325
Cdd:cd12114 199 DearRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDaRLISLGGA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 326 TETSSGVIAVPPDrraPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF---P 402
Cdd:cd12114 279 TEASIWSIYHPID---EVPPDWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvthP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 403 DGRL--RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQgESVVAFVSLVRDA- 479
Cdd:cd12114 356 DGERlyRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGG-KRLAAFVVPDNDGt 434
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2089408387 480 EVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd12114 435 PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
40-528 |
2.59e-53 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 189.67 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 40 FAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIIcadtaVAENAETMQD 119
Cdd:PLN02479 58 LASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM-----VDQEFFTLAE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 120 STVRWIVGTSDLDFQT---------RNDPRVFGDRIRErhdGAddlVELVERFRGATPEAAEVSPTD---TAILAYTSGT 187
Cdd:PLN02479 133 EALKILAEKKKSSFKPpllivigdpTCDPKSLQYALGK---GA---IEYEKFLETGDPEFAWKPPADewqSIALGYTSGT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMkdC-TLVFANRFAADVTLDAFAEHEV 266
Cdd:PLN02479 207 TASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAAL--CgTNICLRQVTAKAIYSAIANYGV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 267 TYTIGSITVFNALYNSPAATAA----HFASIKTlySGGAPiPPAAVEKFENKfGHYIHNAYGMTET--SSGVIA------ 334
Cdd:PLN02479 285 THFCAAPVVLNTIVNAPKSETIlplpRVVHVMT--AGAAP-PPSVLFAMSEK-GFRVTHTYGLSETygPSTVCAwkpewd 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 335 -VPPDRRAPVDPASGALSIGMAlpqvEIRVVDF-DGTPLP-DG-TQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGD 410
Cdd:PLN02479 361 sLPPEEQARLNARQGVRYIGLE----GLDVVDTkTMKPVPaDGkTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 411 VAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAE-----VTEQE 485
Cdd:PLN02479 437 LGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDksdeaALAED 516
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2089408387 486 LRAFVGDRLAAYKRPKHIhIVDELPKTQTGKIRRTELRnTEAK 528
Cdd:PLN02479 517 IMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR-AKAK 557
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
11-523 |
3.65e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 187.98 E-value: 3.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 11 RVAANPEHPA-IAYFDG-ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRK 88
Cdd:PRK13391 6 HAQTTPDKPAvIMASTGeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 89 AELRHLVDDAGA-VGIICADTAVAENAETMQDSTVRwivgtsdldfqtrndPRVFGDRIRERhDGADDLVELVERFrGAT 167
Cdd:PRK13391 86 AEAAYIVDDSGArALITSAAKLDVARALLKQCPGVR---------------HRLVLDGDGEL-EGFVGYAEAVAGL-PAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 168 PEAAEVSPTDtaiLAYTSGTTGPPKGALN--SHANI---LAVATTFAELARVDDGDVVLAVAPLFHIT-GAVINATIALm 241
Cdd:PRK13391 149 PIADESLGTD---MLYSSGTTGRPKGIKRplPEQPPdtpLPLTAFLQRLWGFRSDMVYLSPAPLYHSApQRAVMLVIRL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 242 kDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHF--ASIKTLYSGGAPIPPAAVEKFENKFGHYI 319
Cdd:PRK13391 225 -GGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYdlSSLEVAIHAAAPCPPQVKEQMIDWWGPII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 320 HNAYGMTEtSSGVIAVPP----DRRAPVdpasGALSIGmalpqvEIRVVDFDGTPLPDGTQGELEIAGPQVVSgYWQKPE 395
Cdd:PRK13391 304 HEYYAATE-GLGFTACDSeewlAHPGTV----GRAMFG------DLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 396 ATAKT-FPDGRLRT-GDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFV 473
Cdd:PRK13391 372 KTAEArHPDGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 474 SLVRDAEVTE---QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK13391 452 QPVDGVDPGPalaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
41-523 |
1.07e-52 |
|
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: 185.66 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 41 AVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAElrhlvddAGAVGIICADTAVaENAETMQDS 120
Cdd:cd05929 31 ARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAE-------ACAIIEIKAAALV-CGLFTGGGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 121 TVRWivgtsdldfqtRNDPRVFGdrirerhdGADDlvelverfrgaTPEAAEVSPTDtaiLAYTSGTTGPPKGALNSHAN 200
Cdd:cd05929 103 LDGL-----------EDYEAAEG--------GSPE-----------TPIEDEAAGWK---MLYSGGTTGRPKGIKRGLPG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 201 ILAVATT---FAELARVDDGDVVLAVAPLFHITGAVINATiALMKDCTLVFANRFAADVTLDAFAEHEVTYTIGSITVFN 277
Cdd:cd05929 150 GPPDNDTlmaAALGFGPGADSVYLSPAPLYHAAPFRWSMT-ALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 278 ALYNSPAAT--AAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTEtSSGVIAVPPDrrapvDPASGALSIGMA 355
Cdd:cd05929 229 RLLKLPEAVrnAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTE-GQGLTIINGE-----EWLTHPGSVGRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 356 LpQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSgYWQKPEATAKTFPDGRLRT-GDVAIRDADGWIYLVDRLKDQINVSG 434
Cdd:cd05929 303 V-LGKVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 435 YKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVS---LVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPK 511
Cdd:cd05929 381 VNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQpapGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPR 460
|
490
....*....|..
gi 2089408387 512 TQTGKIRRTELR 523
Cdd:cd05929 461 DDTGKLYRRLLR 472
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
13-524 |
2.04e-52 |
|
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: 188.29 E-value: 2.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 13 AANPEHPAIAYFDGI------LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMY 86
Cdd:cd05967 62 AGRGDQIALIYDSPVtgtertYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 87 RKAELRHLVDDAGAVGIICADTAVAENA----ETMQDSTVRwIVGTSDLDFQTRNDPRVFGDRIRERHDgaddlVELVER 162
Cdd:cd05967 142 AAKELASRIDDAKPKLIVTASCGIEPGKvvpyKPLLDKALE-LSGHKPHHVLVLNRPQVPADLTKPGRD-----LDWSEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 163 FRGATP-EAAEVSPTDTAILAYTSGTTGPPKGALNS---HAniLAVATTFAELARVDDGDVVLAVAPLFHITGAVINATI 238
Cdd:cd05967 216 LAKAEPvDCVPVAATDPLYILYTSGTTGKPKGVVRDnggHA--VALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 239 ALMKDCTLVFANRfAADVTLDA------FAEHEVTYTIGSITVFNALYNSPAATA----AHFASIKTLYSGGAPIPPAAV 308
Cdd:cd05967 294 PLLHGATTVLYEG-KPVGTPDPgafwrvIEKYQVNALFTAPTAIRAIRKEDPDGKyikkYDLSSLRTLFLAGERLDPPTL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 309 EKFENKFGHYIHNAYGMTETSSGVIAvPPDRRAPVDPASGalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAG---PQ 385
Cdd:cd05967 373 EWAENTLGVPVIDHWWQTETGWPITA-NPVGLEPLPIKAG--SPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLplpPG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 386 VVSGYWQKPEATAKT----FPdGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQP 461
Cdd:cd05967 450 CLLTLWKNDERFKKLylskFP-GYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2089408387 462 DDYQGESVVAFVSLV----RDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:cd05967 529 DELKGQVPLGLVVLKegvkITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
31-523 |
5.72e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 185.30 E-value: 5.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAgAVGIICADTAV 110
Cdd:PRK07008 43 RDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHA-EDRYVLFDLTF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 111 AENAETM--QDSTVR-WIVGTSDLDFQTRNDPRVFGDRIRERHDGADDLVELVERfrgatpeaaevsptDTAILAYTSGT 187
Cdd:PRK07008 122 LPLVDALapQCPNVKgWVAMTDAAHLPAGSTPLLCYETLVGAQDGDYDWPRFDEN--------------QASSLCYTSGT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANIL--AVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMkDCTLVFANRFAADVTL-DAFAEH 264
Cdd:PRK07008 188 TGNPKGALYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLT-GAKLVLPGPDLDGKSLyELIEAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 265 EVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETS---------SGVIAV 335
Cdd:PRK07008 267 RVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgtlcklkWKHSQL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 336 PPDRRAPVdpasgALSIGMALPQVEIRVVDFDGTPLP-DG-TQGELEIAGPQVVSGYWQKpeaTAKTFPDGRLRTGDVAI 413
Cdd:PRK07008 347 PLDEQRKL-----LEKQGRVIYGVDMKIVGDDGRELPwDGkAFGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVAT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 414 RDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDR 493
Cdd:PRK07008 419 IDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGK 498
|
490 500 510
....*....|....*....|....*....|
gi 2089408387 494 LAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK07008 499 VAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
23-523 |
1.40e-51 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 185.00 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 23 YFDGILSarevdemsdaFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVG 102
Cdd:PLN02860 38 FVDGVLS----------LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 103 IICADTAVAENAETMQDS--TVRWivgtsdldfqtrndpRVFGDRIRER--HDGADDL-VELVERFRGATPEAAEVS-PT 176
Cdd:PLN02860 108 LVTDETCSSWYEELQNDRlpSLMW---------------QVFLESPSSSvfIFLNSFLtTEMLKQRALGTTELDYAWaPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHANIlaVATTFAELARV--DDGDVVLAVAPLFHITGavINATIA-LMKDCTLVFANRFA 253
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSAL--IVQSLAKIAIVgyGEDDVYLHTAPLCHIGG--LSSALAmLMVGACHVLLPKFD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 254 ADVTLDAFAEHEVTYTIGSITVFNAL--YNSPAATAAHFASIKTLYSGGAPIP----PAAVEKFENKfghYIHNAYGMTE 327
Cdd:PLN02860 249 AKAALQAIKQHNVTSMITVPAMMADLisLTRKSMTWKVFPSVRKILNGGGSLSsrllPDAKKLFPNA---KLFSAYGMTE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 328 TSSGVIAVP---PDRRAP-------------VDPASGALSIGMALPQVEIRVvdfdGTPLPDgTQGELEIAGPQVVSGYW 391
Cdd:PLN02860 326 ACSSLTFMTlhdPTLESPkqtlqtvnqtkssSVHQPQGVCVGKPAPHVELKI----GLDESS-RVGRILTRGPHVMLGYW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 392 QKPEATAKTFP-DGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVV 470
Cdd:PLN02860 401 GQNSETASVLSnDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 471 AFVSLvRDA---------------EVTEQELRAFVGDR-LAAYKRPKHIHI-VDELPKTQTGKIRRTELR 523
Cdd:PLN02860 481 ACVRL-RDGwiwsdnekenakknlTLSSETLRHHCREKnLSRFKIPKLFVQwRKPFPLTTTGKIRRDEVR 549
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-529 |
3.30e-51 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 189.40 E-value: 3.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 7 VWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMY 86
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 87 RKAELRHLVDDAGaVGIICADTAVAEnaetmqdstvrwivgTSDLDFQTRndpRVFGDRIRERHDGADDlvelverfrgA 166
Cdd:PRK12316 596 PAERLAYMLEDSG-VQLLLSQSHLGR---------------KLPLAAGVQ---VLDLDRPAAWLEGYSE----------E 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 167 TPEAaEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIALMKDCTL 246
Cdd:PRK12316 647 NPGT-ELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 247 VFA---NRFAADVTLDAFAEHEVTYTIGSITVFNALYnsPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGH-YIHNA 322
Cdd:PRK12316 725 VVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQaGLYNL 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 323 YGMTETSSGVIavppdRRAPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF- 401
Cdd:PRK12316 803 YGPTEAAIDVT-----HWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFv 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 ----PDG--RLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQpddyQGESVVAFVSL 475
Cdd:PRK12316 878 pspfVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVVL 953
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2089408387 476 VRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEAKV 529
Cdd:PRK12316 954 ESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
40-523 |
3.70e-51 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 184.96 E-value: 3.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 40 FAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICAD-----------T 108
Cdd:PRK00174 111 FANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADegvrggkpiplK 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 109 AVAENAETMQDSTVRWIVgtsdldFQtrndpRVFGDRirERHDGAD----DLVELVerfrGATPEAAEVSPTDTAILAYT 184
Cdd:PRK00174 191 ANVDEALANCPSVEKVIV------VR-----RTGGDV--DWVEGRDlwwhELVAGA----SDECEPEPMDAEDPLFILYT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 185 SGTTGPPKGALNSHAN-ILAVATTFAELARVDDGDVVLAVAPLFHITG--------AVINATialmkdcTLVF------- 248
Cdd:PRK00174 254 SGSTGKPKGVLHTTGGyLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGhsyivygpLANGAT-------TLMFegvpnyp 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 249 -ANRFAadvtlDAFAEHEVtytigsitvfNALYNSPAA------------TAAHFASIKTLYSGGAPIPPAAVEKFENKF 315
Cdd:PRK00174 327 dPGRFW-----EVIDKHKV----------TIFYTAPTAiralmkegdehpKKYDLSSLRLLGSVGEPINPEAWEWYYKVV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 316 GHY---IHNAYGMTETSSGVIAvppdrrapvdPASGAL-----SIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGP--- 384
Cdd:PRK00174 392 GGErcpIVDTWWQTETGGIMIT----------PLPGATplkpgSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpg 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 385 ----------QVVSGYWqkpeataKTFPDGRLrTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGE 454
Cdd:PRK00174 462 mmrtiygdheRFVKTYF-------STFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAE 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2089408387 455 AGVVGQPDDYQGESVVAFVSLVRDAEVTE---QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK00174 534 AAVVGRPDDIKGQGIYAFVTLKGGEEPSDelrKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
171-517 |
1.22e-50 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 187.05 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 171 AEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVF-A 249
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYhP 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 NRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETs 329
Cdd:PRK08633 857 DPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATET- 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 330 SGVIAVP-PDRRAP---VDPASGALSIGMALPQVEIRVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPD- 403
Cdd:PRK08633 936 SPVASVNlPDVLAAdfkRQTGSKEGSVGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDi 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 404 ---GRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALvaHPAVGEAG----VVGQPDDYQGESVVAfvsLV 476
Cdd:PRK08633 1016 dgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEEvvfaVTAVPDEKKGEKLVV---LH 1090
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2089408387 477 RDAEVTEQELRAFVGD-RLAAYKRPKHIHIVDELPKTQTGKI 517
Cdd:PRK08633 1091 TCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-527 |
1.31e-50 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 187.47 E-value: 1.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 10 ARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKA 89
Cdd:PRK12316 4559 ERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE 4638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 90 ELRHLVDDAGaVGIICADTAVAENAETMQdstvrwivGTSDLDFqtrndprvfgDRIRERHDgaddlvelverfRGATPE 169
Cdd:PRK12316 4639 RLAYMMEDSG-AALLLTQSHLLQRLPIPD--------GLASLAL----------DRDEDWEG------------FPAHDP 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 170 AAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIALMKDCTLVFA 249
Cdd:PRK12316 4688 AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVVIR 4766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 NRFAAD--VTLDAFAEHEVTYTIGSITVFNALYNSPAAtAAHFASIKTLYSGGAPIPPAAVEKFENKFGH-YIHNAYGMT 326
Cdd:PRK12316 4767 DDSLWDpeRLYAEIHEHRVTVLVFPPVYLQQLAEHAER-DGEPPSLRVYCFGGEAVAQASYDLAWRALKPvYLFNGYGPT 4845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 327 ETSSGVIAVppDRRAPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF----- 401
Cdd:PRK12316 4846 ETTVTVLLW--KARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpf 4923
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 --PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYqGESVVAFV----- 473
Cdd:PRK12316 4924 gaPGGRLyRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVvpqdp 5002
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2089408387 474 SLVRDAEVT---EQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEA 527
Cdd:PRK12316 5003 ALADADEAQaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDA 5059
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
3-524 |
2.04e-50 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 182.38 E-value: 2.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL 82
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAVGIIcADTAVAENAETMQDstvrwivgtsdldfQTRNDPRVF--GDRIRERHDGADDLVELV 160
Cdd:PRK08279 118 NTQQRGAVLAHSLNLVDAKHLI-VGEELVEAFEEARA--------------DLARPPRLWvaGGDTLDDPEGYEDLAAAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 161 ERFRGATPEAAE-VSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIA 239
Cdd:PRK08279 183 AGAPTTNPASRSgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 240 LMKDCTLVFANRFAADVTLDAFAEHEVT---YtIGSITVFnaLYNSPAAT--AAHfasiKTLYSGGAPIPPAAVEKFENK 314
Cdd:PRK08279 263 LAAGATLALRRKFSASRFWDDVRRYRATafqY-IGELCRY--LLNQPPKPtdRDH----RLRLMIGNGLRPDIWDEFQQR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 315 FG-HYIHNAYGMTETSSGVIAVppdrrapvDPASGALSIGMALPQVEIRVVDFD---GTPL----------PDGTQGEL- 379
Cdd:PRK08279 336 FGiPRILEFYAASEGNVGFINV--------FNFDGTVGRVPLWLAHPYAIVKYDvdtGEPVrdadgrcikvKPGEVGLLi 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 380 -EIAGPQVVSGYwQKPEATAK-----TFPDGR--LRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPA 451
Cdd:PRK08279 408 gRITDRGPFDGY-TDPEASEKkilrdVFKKGDawFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPG 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089408387 452 VGEAGVVG-QPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK08279 487 VEEAVVYGvEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
28-523 |
8.14e-50 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 178.74 E-value: 8.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQN-IPQYAIAFLALWkLGAAALVLNPMYRKAELRHLVDDAGA-VGIIC 105
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNdFAFFEAAYAAMR-LGAYAVPVNWHFKPEEIAYILEDSGArVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 106 AD------TAVAENAETMQDSTVRWIVGTSDLDFQTRNDPrvfgdrirerhDGADDLVELVERFRgatPEAAEVSPTDTA 179
Cdd:PRK12406 91 ADllhglaSALPAGVTVLSVPTPPEIAAAYRISPALLTPP-----------AGAIDWEGWLAQQE---PYDGPPVPQPQS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 180 ILaYTSGTTGPPKGA--LNSHANILAVATTFAELAR-VDDGDVVLAVAPLFH-------ITGAVINATIALMKdctlvfa 249
Cdd:PRK12406 157 MI-YTSGTTGHPKGVrrAAPTPEQAAAAEQMRALIYgLKPGIRALLTGPLYHsapnaygLRAGRLGGVLVLQP------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 nRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHF--ASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTE 327
Cdd:PRK12406 229 -RFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYdvSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 328 TSSGVIAVPPDrrapvdpasgALS----IGMALPQVEIRVVDFDGTPLPDGTQGEL--EIAGPQVVSgYWQKPEATAKTF 401
Cdd:PRK12406 308 SGAVTFATSED----------ALShpgtVGKAAPGAELRFVDEDGRPLPQGEIGEIysRIAGNPDFT-YHNKPEKRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEV 481
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATL 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2089408387 482 TEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK12406 457 DEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
177-515 |
1.94e-49 |
|
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: 173.26 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHItGAVINATIALMKDCTLVFANRFAADV 256
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 257 TLDAFAEHEVTY------TIGSITVFNA--LYNspaATAAHFASIKTLYSGGAPIPPAAvekFENKFGhyihnAYGMTET 328
Cdd:cd17636 80 VLELIEAERCTHafllppTIDQIVELNAdgLYD---LSSLRSSPAAPEWNDMATVDTSP---WGRKPG-----GYGQTEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 329 SsGVIAVPpdrrAPVDPASGALsiGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRT 408
Cdd:cd17636 149 M-GLATFA----ALGGGAIGGA--GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 409 GDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRA 488
Cdd:cd17636 222 NDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIE 301
|
330 340
....*....|....*....|....*..
gi 2089408387 489 FVGDRLAAYKRPKHIHIVDELPKTQTG 515
Cdd:cd17636 302 HCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
16-522 |
4.19e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 177.11 E-value: 4.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKaelrhlv 95
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRS------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 ddagavgiicadTAVAENAETMQDSTVrwivgtsdldfqtrndprVFGDRIRERHDGADDLVELVE------RFRGATPE 169
Cdd:PRK13383 122 ------------DALAAALRAHHISTV------------------VADNEFAERIAGADDAVAVIDpatagaEESGGRPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 170 aaeVSPTDTAILaYTSGTTGPPKGALNSH--ANILAVATTFAELARVDDGDVVLAVAPLFHITG-AVINATIALmkDCTL 246
Cdd:PRK13383 172 ---VAAPGRIVL-LTSGTTGKPKGVPRAPqlRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGlGMLMLTIAL--GGTV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 247 VFANRFAADVTLDAFAEHEV-TYTIGSITVFNALYNSPAATAAH-FASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYG 324
Cdd:PRK13383 246 LTHRHFDAEAALAQASLHRAdAFTAVPVVLARILELPPRVRARNpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 325 MTETSSGVIAVPPD-RRAPVdpasgalSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYwqkPEATAKTFPD 403
Cdd:PRK13383 326 STEVGIGALATPADlRDAPE-------TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 404 GRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE 483
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDA 475
|
490 500 510
....*....|....*....|....*....|....*....
gi 2089408387 484 QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:PRK13383 476 AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-531 |
4.64e-49 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 183.05 E-value: 4.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 4 LVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLN 83
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLD 3176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 84 PMYRKAELRHLVDDAGaVGIICADTAVAENAEtmqdstvrwivgtsdldfqtrndprvfgdriRERHDGADDLVELVErf 163
Cdd:PRK12467 3177 PEYPRERLAYMIEDSG-VKLLLTQAHLLEQLP-------------------------------APAGDTALTLDRLDL-- 3222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 164 rGATPE---AAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIAL 240
Cdd:PRK12467 3223 -NGYSEnnpSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS-FSFDGAQERFLWTL 3300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 241 MKDCTLVFA--NRFAADVTLDAFAEHEVTYTIGSITVFNALYNSpaATAAHFASIKTLYSGGAPIPPAAVEKFENKFGH- 317
Cdd:PRK12467 3301 ICGGCLVVRdnDLWDPEELWQAIHAHRISIACFPPAYLQQFAED--AGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPr 3378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 318 YIHNAYGMTETSSGVIAvppdRRAPVD--PASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPE 395
Cdd:PRK12467 3379 GLTNGYGPTEAVVTVTL----WKCGGDavCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPS 3454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 396 ATAKTF-PD------GRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQpDDYQGE 467
Cdd:PRK12467 3455 LTAERFvADpfsgsgGRLyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGK 3533
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089408387 468 SVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEAKVTR 531
Cdd:PRK12467 3534 QLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSR 3597
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
11-523 |
1.39e-47 |
|
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: 173.58 E-value: 1.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 11 RVAANPEHPAIAYFDG------ILSAREVDEMSDAFAVALVEKGvGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL-- 82
Cdd:cd05931 2 RAAARPDRPAYTFLDDeggreeTLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 -NPMYRKAELRHLVDDAGAVGIICAD---TAVAENAETMQDSTVRWIVgtsdldfqtrndprvfgdrirerhdgADDLVE 158
Cdd:cd05931 81 pTPGRHAERLAAILADAGPRVVLTTAaalAAVRAFAASRPAAGTPRLL--------------------------VVDLLP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 159 LVErfrGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATI 238
Cdd:cd05931 135 DTS---AADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 239 ALMKDCTLVF--ANRFAADVT--LDAFAEHEVTYTIGSitvfNALYN------SPAATAA-HFASIKTLYSGGAPIPPAA 307
Cdd:cd05931 212 PLYSGGPSVLmsPAAFLRRPLrwLRLISRYRATISAAP----NFAYDlcvrrvRDEDLEGlDLSSWRVALNGAEPVRPAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 308 VEKFENKFGHY------IHNAYGMTET----SSGVIAVPP------------DRRAPVDPASGA---LSIGMALPQVEIR 362
Cdd:cd05931 288 LRRFAEAFAPFgfrpeaFRPSYGLAEAtlfvSGGPPGTGPvvlrvdrdalagRAVAVAADDPAArelVSCGRPLPDQEVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 363 VVDFDG-TPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-------PDGRLRTGDVAIRdADGWIYLVDRLKDQINVSG 434
Cdd:cd05931 368 IVDPETgRELPDGEVGEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 435 YKVWPREVEDALVAHPAVGEAGVV---GQPDDyQGESVVAFVSLVRDAEVTE-----QELRAFVGDR--LAAYK----RP 500
Cdd:cd05931 447 RNHYPQDIEATAEEAHPALRPGCVaafSVPDD-GEERLVVVAEVERGADPADlaaiaAAIRAAVAREhgVAPADvvlvRP 525
|
570 580
....*....|....*....|...
gi 2089408387 501 KHIhivdelPKTQTGKIRRTELR 523
Cdd:cd05931 526 GSI------PRTSSGKIQRRACR 542
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
10-524 |
2.03e-47 |
|
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: 171.57 E-value: 2.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 10 ARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKA 89
Cdd:cd05918 7 ERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 90 ELRHLVDDAGAVGIICADtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpe 169
Cdd:cd05918 87 RLQEILQDTGAKVVLTSS-------------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 170 aaevsPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIALMKDCTLVFA 249
Cdd:cd05918 105 -----PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFAS-YTFDVSILEIFTTLAAGGCLCIP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 ------NRFAadvtlDAFAEHEVTYTIGSITVFNALynSPAAtaahFASIKTLYSGGAPIPPAAVEKFENKFGhyIHNAY 323
Cdd:cd05918 179 seedrlNDLA-----GFINRLRVTWAFLTPSVARLL--DPED----VPSLRTLVLGGEALTQSDVDTWADRVR--LINAY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 324 GMTETSSGVIAvppdrrAPVDPASGALSIGMALPQVeIRVVDFDGT--PLPDGTQGELEIAGPQVVSGYWQKPEATAKTF 401
Cdd:cd05918 246 GPAECTIAATV------SPVVPSTDPRNIGRPLGAT-CWVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 PD-------------GRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVG--QPDDYQ 465
Cdd:cd05918 319 IEdpawlkqegsgrgRRLyRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvKPKDGS 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2089408387 466 GESV-VAFVSLV-----------------RDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:cd05918 399 SSPQlVAFVVLDgsssgsgdgdslflepsDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
182-519 |
9.82e-47 |
|
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: 165.66 E-value: 9.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 182 AYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHiTGAVINATIALMKDCTLVFANRFAADVTLDAF 261
Cdd:cd17633 6 GFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 262 AEHEVTYTIGSITVFNALYNspaaTAAHFASIKTLYSGGAPIPPAAVEKFENKFGHY-IHNAYGMTETSSGVIAVPPDRR 340
Cdd:cd17633 85 NQYNATVIYLVPTMLQALAR----TLEPESKIKSIFSSGQKLFESTKKKLKNIFPKAnLIEFYGTSELSFITYNFNQESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 341 APvdpasgaLSIGMALPQVEIRVVDFDGtplpdGTQGELEIAGPQVVSGYWQKPEATaktfPDGRLRTGDVAIRDADGWI 420
Cdd:cd17633 161 PP-------NSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVDEEGYL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 421 YLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAfvsLVRDAEVTEQELRAFVGDRLAAYKRP 500
Cdd:cd17633 225 YLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA---LYSGDKLTYKQLKRFLKQKLSRYEIP 301
|
330
....*....|....*....
gi 2089408387 501 KHIHIVDELPKTQTGKIRR 519
Cdd:cd17633 302 KKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
10-523 |
1.20e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 167.49 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 10 ARVAanPEHPAI--AYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYR 87
Cdd:PRK13390 7 AQIA--PDRPAVivAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 88 KAELRHLVDDAGAVGIICADTAVAENAETMQDSTVRWivgtsdldfqtrndprVFGDRIrerhdgaDDLVELVERFRGAT 167
Cdd:PRK13390 85 APEADYIVGDSGARVLVASAALDGLAAKVGADLPLRL----------------SFGGEI-------DGFGSFEAALAGAG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 168 PEAAEvSPTDtAILAYTSGTTGPPKG--------ALNSHAN-ILAVATTFAELArvdDGDVVLAVAPLFHITGAVINATI 238
Cdd:PRK13390 142 PRLTE-QPCG-AVMLYSSGTTGFPKGiqpdlpgrDVDAPGDpIVAIARAFYDIS---ESDIYYSSAPIYHAAPLRWCSMV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 239 ALMKDcTLVFANRFAADVTLDAFAEHEVTYTIGSITVFNALY--NSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFG 316
Cdd:PRK13390 217 HALGG-TVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 317 HYIHNAYGMTETSSGVIAVPPDRRApvDPASGALSIGMALpqveiRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEA 396
Cdd:PRK13390 296 PIVYEYYSSTEAHGMTFIDSPDWLA--HPGSVGRSVLGDL-----HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 397 TAKT-FPDGRLRT--GDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFV 473
Cdd:PRK13390 369 TAAAqHPAHPFWTtvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVI 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 474 SL---VRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK13390 449 QLvegIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
3-524 |
2.68e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 166.11 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGvGHGDRVGIHLQNipqyAIAFLALWkLGAA---- 78
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLEN----RIEFLQLF-AGAAmagw 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 79 -ALVLNPMYRKAELRHlvddagAVGIICADTAVAEnaetmqdstvrwivgtsdldfqtrndpRVFGDRIrerhDGADDLV 157
Cdd:PRK07638 76 tCVPLDIKWKQDELKE------RLAISNADMIVTE---------------------------RYKLNDL----PDEEGRV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 158 ELVERFRGATP-EAAEVSPTDTAILA-----YTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFH--- 228
Cdd:PRK07638 119 IEIDEWKRMIEkYLPTYAPIENVQNApfymgFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHslf 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 229 ITGAV----INATIALMKdctlvfanRFAADVTLDAFaehevtyTIGSITVfnaLYNSPAATAAhFASIK-------TLY 297
Cdd:PRK07638 199 LYGAIstlyVGQTVHLMR--------KFIPNQVLDKL-------ETENISV---MYTVPTMLES-LYKENrvienkmKII 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 298 SGGAPIPPAAVEKFENKFGHY-IHNAYGMTETSSGVIAVPPDRRAPVDpasgalSIGMALPQVEIRVVDFDGTPLPDGTQ 376
Cdd:PRK07638 260 SSGAKWEAEAKEKIKNIFPYAkLYEFYGASELSFVTALVDEESERRPN------SVGRPFHNVQVRICNEAGEEVQKGEI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 377 GELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAG 456
Cdd:PRK07638 334 GTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2089408387 457 VVGQPDDYQGESVVAFVslvrDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK07638 414 VIGVPDSYWGEKPVAII----KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
6-524 |
3.09e-45 |
|
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: 164.79 E-value: 3.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 6 DVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPM 85
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 86 YRKAELRHLVDDAGAVGIICADtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrg 165
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTD---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 166 atpeaaevSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVA-PLFHITGAVINATiaLMKDC 244
Cdd:cd17653 103 --------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLsIAFDACIGEIFST--LCNGG 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 245 TLVFANrfaadvTLDAFAEhevtyTIGSITVFNAlynSPAATA----AHFASIKTLYSGGAPIPPAAVEKFenKFGHYIH 320
Cdd:cd17653 173 TLVLAD------PSDPFAH-----VARTVDALMS---TPSILStlspQDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLY 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 321 NAYGMTETSSGVI--AVPPDRRapvdpasgaLSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATA 398
Cdd:cd17653 237 NAYGPTECTISSTmtELLPGQP---------VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 399 KTF------PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKV-WPREVEDALVAHPAVGEAGVVgqpddYQGESVV 470
Cdd:cd17653 308 SKFvpdpfwPGSRMyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRInLEEIEEVVLQSQPEVTQAAAI-----VVNGRLV 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2089408387 471 AFVSlvrDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:cd17653 383 AFVT---PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
40-519 |
4.65e-45 |
|
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: 164.84 E-value: 4.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 40 FAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIicadtaVAENaetmqd 119
Cdd:cd17640 18 FAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL------VVEN------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 120 stvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevSPTDTAILAYTSGTTGPPKGALNSHA 199
Cdd:cd17640 86 ------------------------------------------------------DSDDLATIIYTSGTTGNPKGVMLTHA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 200 NILAVATTFAELARVDDGDVVLAVAPLFHITGAVINaTIALMKDCTLVFANrfaADVTLDAFAEHEVTYTIGSITVFNAL 279
Cdd:cd17640 112 NLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAE-YFIFACGCSQAYTS---IRTLKDDLKRVKPHYIVSVPRLWESL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 280 Y--------NSPAATA--AHFA----SIKTLYSGGAPIPPaAVEKFENKFGHYIHNAYGMTETSSGVIAvppdrRAPVDP 345
Cdd:cd17640 188 YsgiqkqvsKSSPIKQflFLFFlsggIFKFGISGGGALPP-HVDTFFEAIGIEVLNGYGLTETSPVVSA-----RRLKCN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 346 ASGalSIGMALPQVEIRVVDFDG-TPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLV 423
Cdd:cd17640 262 VRG--SVGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLT 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 424 DRLKDQINVS-GYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAF------------VSLVRDAEVT-------- 482
Cdd:cd17640 340 GRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVPNfeelekwakesgVKLANDRSQLlaskkvlk 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2089408387 483 --EQELRAFVGDRLAA--YKRPKHIHIVDElP------KTQTGKIRR 519
Cdd:cd17640 420 lyKNEIKDEISNRPGFksFEQIAPFALLEE-PfiengeMTQTMKIKR 465
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
177-519 |
1.49e-44 |
|
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: 160.50 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHANILAVATTF-AELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAAD 255
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 256 VTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSgVIAV 335
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGT-ALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 336 PPDrrapvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRD 415
Cdd:cd17635 161 PTD-----DDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 416 ADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVslVRDAEVTEQELRAF---VGD 492
Cdd:cd17635 236 EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAV--VASAELDENAIRALkhtIRR 313
|
330 340
....*....|....*....|....*..
gi 2089408387 493 RLAAYKRPKHIHIVDELPKTQTGKIRR 519
Cdd:cd17635 314 ELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
39-524 |
2.15e-44 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 165.34 E-value: 2.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 39 AFAVALVEK-GVGHGDRVGIHLQNIPQYAIAFLALWKLGAaalVLNPMYRK---AELRHLVDDAgAVGIICADTAVAENA 114
Cdd:PRK05620 50 ALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGA---VFNPLNKQlmnDQIVHIINHA-EDEVIVADPRLAEQL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 115 ETM--QDSTVRWIV--GTSDLDFQTRNDPRvfgdrirerHDGADDLVELVERfRGATPEAAEVSPTDTAILAYTSGTTGP 190
Cdd:PRK05620 126 GEIlkECPCVRAVVfiGPSDADSAAAHMPE---------GIKVYSYEALLDG-RSTVYDWPELDETTAAAICYSTGTTGA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 191 PKGALNSHANI------LAVATTFAelarVDDGDVVLAVAPLFHI-TGAVINAtiALMKDCTLVFANRFAADVTLDAFAE 263
Cdd:PRK05620 196 PKGVVYSHRSLylqslsLRTTDSLA----VTHGESFLCCVPIYHVlSWGVPLA--AFMSGTPLVFPGPDLSAPTLAKIIA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 264 HEVTYTI-GSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSS-GVIAVPPDRRA 341
Cdd:PRK05620 270 TAMPRVAhGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPvGTVARPPSGVS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 342 PVDPASGALSIGMALPQVEIRVVDfDGTPLP--DGTQGELEIAGPQVVSGYWQKPEAT----AKTF-------------P 402
Cdd:PRK05620 350 GEARWAYRVSQGRFPASLEYRIVN-DGQVMEstDRNEGEIQVRGNWVTASYYHSPTEEgggaASTFrgedvedandrftA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 403 DGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVT 482
Cdd:PRK05620 429 DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPT 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2089408387 483 E---QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK05620 509 RetaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
39-517 |
2.31e-44 |
|
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: 163.66 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 39 AFAVA-LVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICADTAVAEnaetm 117
Cdd:cd05909 17 AIALArKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEK----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 118 qdstvrwivGTSDLDFQTRNDPR-VFGDRIRERHDGADDL-VELVERFRGATPEA----AEVSPTDTAILAYTSGTTGPP 191
Cdd:cd05909 92 ---------LKLHHLFDVEYDARiVYLEDLRAKISKADKCkAFLAGKFPPKWLLRifgvAPVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 192 KGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFA-NRFAADVTLDAFAEHEVTYTI 270
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpNPLDYKKIPELIYDKKATILL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 271 GSITVFNALYNspAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSgVIAV---PPDRRAPvdpas 347
Cdd:cd05909 243 GTPTFLRGYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSP-VISVntpQSPNKEG----- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 348 galSIGMALPQVEIRVVDFDG-TPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRL 426
Cdd:cd05909 315 ---TVGRPLPGMEVKIVSVEThEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 427 KDQINVSGYKVWPREVEDALVAH-PAVGEAGVVGQPDDYQGESVVAFVSlvrDAEVTEQELRAFVGD-RLAAYKRPKHIH 504
Cdd:cd05909 392 SRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT---TTDTDPSSLNDILKNaGISNLAKPSYIH 468
|
490
....*....|...
gi 2089408387 505 IVDELPKTQTGKI 517
Cdd:cd05909 469 QVEEIPLLGTGKP 481
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
10-531 |
5.92e-44 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 167.65 E-value: 5.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 10 ARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKA 89
Cdd:PRK12467 1582 DQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRE 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 90 ELRHLVDDAGaVGIICADTAVAEnaetmqdstvRWIVGTSDldfqtrndPRVFGDRIRERHDGADDlvelverfrgATPE 169
Cdd:PRK12467 1662 RLAYMIEDSG-IELLLTQSHLQA----------RLPLPDGL--------RSLVLDQEDDWLEGYSD----------SNPA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 170 AAeVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIALMKDCTLVFA 249
Cdd:PRK12467 1713 VN-LAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIA 1790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 ----NRFAADvTLDAFAEHEVTYTIGSITVFNALYNSPAATAaHFASIKTLYSGGAPIPPAAVEKFENKFG-HYIHNAYG 324
Cdd:PRK12467 1791 ppgaHRDPEQ-LIQLIERQQVTTLHFVPSMLQQLLQMDEQVE-HPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYG 1868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 325 MTETSSGVIAVPPDRrapVDPASGALS-IGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-- 401
Cdd:PRK12467 1869 PTETAVDVTHWTCRR---KDLEGRDSVpIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFva 1945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 -----PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQpDDYQGESVVAFV-- 473
Cdd:PRK12467 1946 dpfgtVGSRLyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVvp 2024
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089408387 474 --SLVRDAEVTEQELRAFVGDRLAA----YKRPKHIHIVDELPKTQTGKIRRTELRNTEAKVTR 531
Cdd:PRK12467 2025 tdPGLVDDDEAQVALRAILKNHLKAslpeYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQ 2088
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
19-523 |
6.91e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 162.93 E-value: 6.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 19 PAIAYFDGILSAREVDEMSDAFAVALveKGVGHGDR---VGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:PRK07867 20 RGLYFEDSFTSWREHIRGSAARAAAL--RARLDPTRpphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAvGIICADTAVAENAetmqdstvrwivgtsdldfqtrnDPRVFGDRIRERHdgADDLVELVERFRGATPEAAEVSP 175
Cdd:PRK07867 98 AHADC-QLVLTESAHAELL-----------------------DGLDPGVRVINVD--SPAWADELAAHRDAEPPFRVADP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 TDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHiTGAVINA-TIALMKDCTLVFANRFAA 254
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFH-SNAVMAGwAVALAAGASIALRRKFSA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 255 DVTLDAFAEHEVTYtigsitvFN--------ALYNSPAATAAHfASIKTLYsgGAPIPPAAVEKFENKFGHYIHNAYGMT 326
Cdd:PRK07867 231 SGFLPDVRRYGATY-------ANyvgkplsyVLATPERPDDAD-NPLRIVY--GNEGAPGDIARFARRFGCVVVDGFGST 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 327 E----------TSSGVIAVPPDRRAPVDPASGAlsigmalpQVEIRVVDFDGTPLPDGTQGEL-EIAGPQVVSGYWQKPE 395
Cdd:PRK07867 301 EggvaitrtpdTPPGALGPLPPGVAIVDPDTGT--------ECPPAEDADGRLLNADEAIGELvNTAGPGGFEGYYNDPE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 396 ATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSL 475
Cdd:PRK07867 373 ADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVL 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2089408387 476 VRDAEVTEQELRAFVGDR--LAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK07867 453 APGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
174-516 |
9.43e-43 |
|
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: 156.00 E-value: 9.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 174 SPTDTAILaYTSGTTGPPKGALNSHANILAVATTFAELARVDD--------------GDVVLAVAPLFHITGaVINATIA 239
Cdd:cd05924 2 SADDLYIL-YTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFtpsedahkaaaaaaGTVMFPAPPLMHGTG-SWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 240 LMKDCTLVF-ANRFAADVTLDAFAEHEVTytigSITVFNALYNSP------AATAAHFASIKTLYSGGAPIPPAAVEKFE 312
Cdd:cd05924 80 LLGGQTVVLpDDRFDPEEVWRTIEKHKVT----SMTIVGDAMARPlidalrDAGPYDLSSLFAISSGGALLSPEVKQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 313 NKFGH-YIHNAYGMTETSSGVIAVPpdrrAPVDPASGALsigmALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVS-GY 390
Cdd:cd05924 156 ELVPNiTLVDAFGSSETGFTGSGHS----AGSGPETGPF----TRANPDTVVLDDDGRVVPPGSGGVGWIARRGHIPlGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 391 WQKPEATAKTFPD-GRLR---TGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQG 466
Cdd:cd05924 228 YGDEAKTAETFPEvDGVRyavPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2089408387 467 ESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGK 516
Cdd:cd05924 308 QEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
16-517 |
1.23e-42 |
|
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: 157.95 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVekGVGHG---DRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELR 92
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLL--SVAEIrpdDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 93 HLVDDAGAVGIIcadtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaae 172
Cdd:cd17648 79 FILEDTGARVVI-------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 173 VSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDD-GDVVLAVAPLFHITGAVINATIALMKDCTLVFAN- 250
Cdd:cd17648 91 TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDnGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPd 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 --RFAADVTLDAFAEHEVTYTIGSITVFNaLYNSPAATaahfaSIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTET 328
Cdd:cd17648 171 emRFDPDRFYAYINREKVTYLSGTPSVLQ-QYDLARLP-----HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTET 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 329 S--SGVIAVPPDRRApvdpasgALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFP---- 402
Cdd:cd17648 245 TvtNHKRFFPGDQRF-------DKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLpnpf 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 403 ----------DGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQ--PDDYQGESV 469
Cdd:cd17648 318 qteqerargrNARLyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKedASQAQSRIQ 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2089408387 470 VAFVSL-VRDAE-VTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKI 517
Cdd:cd17648 398 KYLVGYyLPEPGhVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
16-522 |
1.71e-42 |
|
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: 157.63 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAvgiicaDTAVAEnaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsP 175
Cdd:cd17650 81 EDSGA------KLLLTQ--------------------------------------------------------------P 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 TDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFAN---RF 252
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPdevKL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 253 AADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHY--IHNAYGMTETS- 329
Cdd:cd17650 173 DPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGmrIINSYGVTEATi 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 330 -SGVIAVPPDRrapvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF------P 402
Cdd:cd17650 253 dSTYYEEGRDP----LGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFvenpfaP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 403 DGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVslVRDAEV 481
Cdd:cd17650 329 GERMyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYV--VAAATL 406
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2089408387 482 TEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17650 407 NTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-526 |
1.99e-42 |
|
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: 156.96 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAalvlnpmyrkaelrhlvddagavgIICAD 107
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV------------------------VIPAT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 TAVaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdGADDLVELVERFRGATPEAAEVSPTDTAILAY-TSG 186
Cdd:cd05974 57 TLL-----------------------------------------TPDDLRDRVDRGGAVYAAVDENTHADDPMLLYfTSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 187 TTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFAN--RFAADVTLDAFAEH 264
Cdd:cd05974 96 TTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNyaRFDAKRVLAALVRY 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 265 EVTYTIGSITVFNALYNSPAATAAhfASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDrraPVD 344
Cdd:cd05974 176 GVTTLCAPPTVWRMLIQQDLASFD--VKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQ---PVK 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 345 PASgalsIGMALPQVEIRVVDFDGTPLPDGtQGELEIAGPQVV---SGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIY 421
Cdd:cd05974 251 AGS----MGRPLPGYRVALLDPDGAPATEG-EVALDLGDTRPVglmKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLT 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 422 LVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAE---VTEQELRAFVGDRLAAYK 498
Cdd:cd05974 326 YVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEpspETALEIFRFSRERLAPYK 405
|
490 500
....*....|....*....|....*...
gi 2089408387 499 RPKHIHIVdELPKTQTGKIRRTELRNTE 526
Cdd:cd05974 406 RIRRLEFA-ELPKTISGKIRRVELRRRE 432
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-522 |
2.00e-42 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 163.20 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 9 KARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRK 88
Cdd:PRK12316 3064 EEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPE 3143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 89 AELRHLVDDAGAvgiicadtavaenaetmqdstvRWIVGTSDLDFqtrndPRVFGDRIRERHDGADDLVElverfrgATP 168
Cdd:PRK12316 3144 ERLAYMLEDSGA----------------------QLLLSQSHLRL-----PLAQGVQVLDLDRGDENYAE-------ANP 3189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 169 eAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIALMKDCTLVF 248
Cdd:PRK12316 3190 -AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVL 3267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 249 AN-RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYihNAYGMTE 327
Cdd:PRK12316 3268 AGpEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLY--NLYGPTE 3345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 328 TssgviAVPPDRRAPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF------ 401
Cdd:PRK12316 3346 A-----TITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfv 3420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVgqpdDYQGESVVAFVSLVRDAE 480
Cdd:PRK12316 3421 PGERLyRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAG 3496
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2089408387 481 VTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:PRK12316 3497 DLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
25-524 |
4.20e-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: 156.36 E-value: 4.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 25 DGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGII 104
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 105 cadtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevspTDTAILAYT 184
Cdd:cd05940 81 -----------------------------------------------------------------------VDAALYIYT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 185 SGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEH 264
Cdd:cd05940 90 SGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 265 EVT---YtIGSITVFnaLYNSPAATAAHFASIKTLYSGGapIPPAAVEKFENKFG-HYIHNAYGMTETSSGVIAVPPDRR 340
Cdd:cd05940 170 QATifqY-IGELCRY--LLNQPPKPTERKHKVRMIFGNG--LRPDIWEEFKERFGvPRIAEFYAATEGNSGFINFFGKPG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 341 ApVDPASGALSIGMAlpqveIRVVDFD---GTPL----------PDGTQGEL--EIAGPQVVSGYWQKPEATAK----TF 401
Cdd:cd05940 245 A-IGRNPSLLRKVAP-----LALVKYDlesGEPIrdaegrcikvPRGEPGLLisRINPLEPFDGYTDPAATEKKilrdVF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 PDGR--LRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVG-QPDDYQGESVVAFVSLVRD 478
Cdd:cd05940 319 KKGDawFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGvQVPGTDGRAGMAAIVLQPN 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2089408387 479 AEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:cd05940 399 EEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
14-523 |
1.09e-41 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 157.07 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 14 ANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAalVLNPMY--RKAEL 91
Cdd:PRK10946 35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFshQRSEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 92 rhlvddagavgiicadTAVAENAETmqdstvRWIVGTSDLDFQTRNDprvFGDRIRERH-----------DGADDLVELV 160
Cdd:PRK10946 113 ----------------NAYASQIEP------ALLIADRQHALFSDDD---FLNTLVAEHsslrvvlllndDGEHSLDDAI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 161 ERfrGATPEAAEVSPTD-TAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAP-------------- 225
Cdd:PRK10946 168 NH--PAEDFTATPSPADeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPaahnypmsspgalg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 226 LFHITGAVinatialmkdctlVFANRFAADVTLDAFAEHEVTYTigsitvfnALYnSPAATA-----------AHFASIK 294
Cdd:PRK10946 246 VFLAGGTV-------------VLAPDPSATLCFPLIEKHQVNVT--------ALV-PPAVSLwlqaiaeggsrAQLASLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 295 TLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTEtssGVIAV-----PPDRRAPVD--PASgalsigmalPQVEIRVVDFD 367
Cdd:PRK10946 304 LLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GLVNYtrlddSDERIFTTQgrPMS---------PDDEVWVADAD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 368 GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDAL 446
Cdd:PRK10946 372 GNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 447 VAHPAVGEAGVVGQPDDYQGESVVAFVslvrdaeVTEQELRAFVGDR------LAAYKRPKHIHIVDELPKTQTGKIRRT 520
Cdd:PRK10946 452 LRHPAVIHAALVSMEDELMGEKSCAFL-------VVKEPLKAVQLRRflreqgIAEFKLPDRVECVDSLPLTAVGKVDKK 524
|
...
gi 2089408387 521 ELR 523
Cdd:PRK10946 525 QLR 527
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
179-525 |
2.52e-41 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 156.07 E-value: 2.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 179 AILAYTSGTTGPPKGALNSH-ANIL-AVATTFAELARVDDGDVVLAVAPLFHItgaviNATiALMKDCTLVFANRFAADV 256
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVLhALMANNGDALGTSAADTMLPVVPLFHA-----NSW-GIAFSAPSMGTKLVMPGA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 257 TLDAFAEHE------VTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFEnKFGHYIHNAYGMTETSS 330
Cdd:PRK06018 254 KLDGASVYElldtekVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFE-DMGVEVRHAWGMTEMSP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 331 -GVIAV--PPDRRAPVDPASGALSI-GMALPQVEIRVVDFDGTPLP-DG-TQGELEIAGPQVVSGYWQkpeATAKTF-PD 403
Cdd:PRK06018 333 lGTLAAlkPPFSKLPGDARLDVLQKqGYPPFGVEMKITDDAGKELPwDGkTFGRLKVRGPAVAAAYYR---VDGEILdDD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 404 GRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE 483
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2089408387 484 QELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNT 525
Cdd:PRK06018 490 EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
134-523 |
2.16e-40 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 153.21 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 134 QTRNDPRVFGDRirERHDGADDLVEL--VERFRGATPEAAEV----------SPTDTAILAYTSGTTGPPKGALNSHANI 201
Cdd:cd05906 115 QLLGSPVVLTDA--ELVAEFAGLETLsgLPGIRVLSIEELLDtaadhdlpqsRPDDLALLMLTSGSTGFPKAVPLTHRNI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 202 LAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFA--NRFAADVT--LDAFAEHEVTYTIG---SIT 274
Cdd:cd05906 193 LARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVptEEILADPLrwLDLIDRYRVTITWApnfAFA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 275 VFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHY------IHNAYGMTETSSGVIAVPPDRRAPVDPASG 348
Cdd:cd05906 273 LLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYglppdaIRPAFGMTETCSGVIYSRSFPTYDHSQALE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 349 ALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDaDGWIYLVDRLK 427
Cdd:cd05906 353 FVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTK 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 428 DQINVSGYKVWPREVEDAL-----VAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE--QELRAFVGDRLAAykRP 500
Cdd:cd05906 432 DTIIVNGVNYYSHEIEAAVeevpgVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALSEtlRAIRSVVSREVGV--SP 509
|
410 420
....*....|....*....|....*
gi 2089408387 501 KHIHIV--DELPKTQTGKIRRTELR 523
Cdd:cd05906 510 AYLIPLpkEEIPKTSLGKIQRSKLK 534
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
16-522 |
1.43e-39 |
|
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: 149.93 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLV 95
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 96 DDAGAVGII----CADTAVAENAETMQDSTVRWIVGTSDLDFQTRNDprvfgdrirerhdgaddlvelverfrgatpeaa 171
Cdd:cd17656 82 LDSGVRVVLtqrhLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSD--------------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 172 evsptDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVA-PLFHITGAVINATiaLMKDCTLVFAN 250
Cdd:cd17656 129 -----DLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFAtCSFDVCYQEIFST--LLSGGTLYIIR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 ---RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAP--IPPAAVEKFENKFGHyIHNAYGM 325
Cdd:cd17656 202 eetKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQlvITNEFKEMLHEHNVH-LHNHYGP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 326 TETSsgviAVPPDRRAPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF---- 401
Cdd:cd17656 281 SETH----VVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFfpdp 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 --PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVslVRD 478
Cdd:cd17656 357 fdPNERMyRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VME 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2089408387 479 AEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17656 435 QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
11-523 |
2.04e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 150.56 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 11 RVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGD-RVGIHLQNIPQYaIAFLALWKLGAAALV-LNPMYRK 88
Cdd:PRK13388 10 RDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPlHVGVLLGNTPEM-LFWLAAAALGGYVLVgLNTTRRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 89 AEL----RHlVDdagaVGIICADtavAENAETMQDstvrwiVGTSDLDFQTRNDPRvfgdrirerhdgaddLVELVERFR 164
Cdd:PRK13388 89 AALaadiRR-AD----CQLLVTD---AEHRPLLDG------LDLPGVRVLDVDTPA---------------YAELVAAAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 165 GATPeAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDC 244
Cdd:PRK13388 140 ALTP-HREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 245 TLVFANRFAADVTLDAFAEHEVTYtigsitvFNALYNSPA---ATAAHFASI-KTLYSG-GAPIPPAAVEKFENKFGHYI 319
Cdd:PRK13388 219 AVALPAKFSASGFLDDVRRYGATY-------FNYVGKPLAyilATPERPDDAdNPLRVAfGNEASPRDIAEFSRRFGCQV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 320 HNAYGMTETssGVIAVPpdrrapvDPASGALSIGMALPQVEI-----------RVVDFDGTPL-PDGTQGEL-EIAGPQV 386
Cdd:PRK13388 292 EDGYGSSEG--AVIVVR-------EPGTPPGSIGRGAPGVAIynpetltecavARFDAHGALLnADEAIGELvNTAGAGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 387 VSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQG 466
Cdd:PRK13388 363 FEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVG 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2089408387 467 ESVVAFVSLVRDAEVTEQELRAFVGDR--LAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK13388 443 DQVMAALVLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
12-522 |
5.30e-39 |
|
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: 147.70 E-value: 5.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 12 VAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAEL 91
Cdd:cd17645 8 VERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 92 RHLVDDAGAVGIIcadtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaa 171
Cdd:cd17645 88 AYMLADSSAKILL------------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 172 eVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPlFHITGAVINATIALMKDCTLVFAN- 250
Cdd:cd17645 101 -TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYAS-FSFDASAWEIFPHLTAGAALHVVPs 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 --RFAADVTLDAFAEHEVTYTI---GSITVFNALYNSpaataahfaSIKTLYSGGApippaAVEKFENKfGHYIHNAYGM 325
Cdd:cd17645 179 erRLDLDALNDYFNQEGITISFlptGAAEQFMQLDNQ---------SLRVLLTGGD-----KLKKIERK-GYKLVNNYGP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 326 TETSsgVIAVppdrRAPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF---- 401
Cdd:cd17645 244 TENT--VVAT----SFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFivhp 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 --PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVslVRD 478
Cdd:cd17645 318 fvPGERMyRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYV--TAP 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2089408387 479 AEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17645 396 EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-522 |
6.99e-39 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 152.63 E-value: 6.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALV 81
Cdd:PRK05691 2188 QTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVP 2267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNPMYRKAELRHLVDDAGaVGIICADTAVAENAETMQDSTVRWIVgtsdldfqtrndprvfgdrirerhdgADDLVELVE 161
Cdd:PRK05691 2268 LDPEYPLERLHYMIEDSG-IGLLLSDRALFEALGELPAGVARWCL--------------------------EDDAAALAA 2320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 162 RfrGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANIL----AVATTFAelARVDDGDVvlavaplfHITGAVINAT 237
Cdd:PRK05691 2321 Y--SDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAmhcqAVIERFG--MRADDCEL--------HFYSINFDAA 2388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 238 -----IALMKDCTLVF--ANRFAADVTLDAFAEHEVtytigSITVFNALYNSPAA----TAAHFASIKTLYSGGAPIPPA 306
Cdd:PRK05691 2389 serllVPLLCGARVVLraQGQWGAEEICQLIREQQV-----SILGFTPSYGSQLAqwlaGQGEQLPVRMCITGGEALTGE 2463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 307 AVEKFENKFG-HYIHNAYGMTETSSGVIAVPPDRRAPVDPASgaLSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQ 385
Cdd:PRK05691 2464 HLQRIRQAFApQLFFNAYGPTETVVMPLACLAPEQLEEGAAS--VPIGRVVGARVAYILDADLALVPQGATGELYVGGAG 2541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 386 VVSGYWQKPEATAKTF-PD------GRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAgV 457
Cdd:PRK05691 2542 LAQGYHDRPGLTAERFvADpfaadgGRLyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREA-V 2620
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 458 VGQPDDYQGESVVAFVS--LVRDAEVTEQELRAFVGDRLAA----YKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:PRK05691 2621 VLALDTPSGKQLAGYLVsaVAGQDDEAQAALREALKAHLKQqlpdYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-522 |
1.38e-37 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 148.78 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 2 ATLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALV 81
Cdd:PRK05691 1131 AWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNPMYRKAELRHLVDDAGaVGIICADTAVAENAETMqDSTVRWIVGTSDLDFQTRNDPRVfgdrirerHDGADDLvelve 161
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSG-VELLLTQSHLLERLPQA-EGVSAIALDSLHLDSWPSQAPGL--------HLHGDNL----- 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 162 rfrgatpeaaevsptdtAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL-FHITgaVINATIAL 240
Cdd:PRK05691 1276 -----------------AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIsFDVS--VWECFWPL 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 241 MKDCTLVFA--------NRFAADVTldafaEHEVTYTIGSITVFNALYNSPAATAAHfaSIKTLYSGGAPIPPAAVEKFE 312
Cdd:PRK05691 1337 ITGCRLVLAgpgehrdpQRIAELVQ-----QYGVTTLHFVPPLLQLFIDEPLAAACT--SLRRLFSGGEALPAELRNRVL 1409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 313 NKF-GHYIHNAYGMTETSSGVI----AVPPDRRAPvdpasgalsIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVV 387
Cdd:PRK05691 1410 QRLpQVQLHNRYGPTETAINVThwqcQAEDGERSP---------IGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLA 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 388 SGYWQKPEATAKTF---PDG----RL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVG 459
Cdd:PRK05691 1481 RGYLGRPALTAERFvpdPLGedgaRLyRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLV 1560
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 460 QpDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:PRK05691 1561 R-EGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
13-488 |
1.81e-37 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 145.43 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 13 AANPEHPAIAYFDGI----------LSAREVDEMSDAFAVALVEKGVGHGDR-VGIHLQNIPQYAIAFlALWKLGAAALV 81
Cdd:PRK09274 17 QERPDQLAVAVPGGRgadgklaydeLSFAELDARSDAIAHGLNAAGIGRGMRaVLMVTPSLEFFALTF-ALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 82 LNP-MYRKAELRHL--VDDAGAVGIICAdtavaenaetmqdSTVRWIVGTSDLDFQTR--NDPRVFGdrirerhdGADDL 156
Cdd:PRK09274 96 VDPgMGIKNLKQCLaeAQPDAFIGIPKA-------------HLARRLFGWGKPSVRRLvtVGGRLLW--------GGTTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 157 VELVERFRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINA 236
Cdd:PRK09274 155 ATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPALGM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 237 TIAL--MKDCTLVFANrfaADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENK 314
Cdd:PRK09274 235 TSVIpdMDPTRPATVD---PAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 315 FGHY--IHNAYGMTE----TSSGVIAVPPDRRAPVDPASGALsIGMALPQVEIRVVDFDGTP---------LPDGTQGEL 379
Cdd:PRK09274 312 LPPDaeILTPYGATEalpiSSIESREILFATRAATDNGAGIC-VGRPVDGVEVRIIAISDAPipewddalrLATGEIGEI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 380 EIAGPQVVSGYWQKPEATAKT-FPDG----RLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGE 454
Cdd:PRK09274 391 VVAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKR 470
|
490 500 510
....*....|....*....|....*....|....*..
gi 2089408387 455 AGVVGQPDDYQGESVVAF---VSLVRDAEVTEQELRA 488
Cdd:PRK09274 471 SALVGVGVPGAQRPVLCVelePGVACSKSALYQELRA 507
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
177-524 |
2.05e-37 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 145.55 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHANilAVATTFAELARVDDG--DVVLAVAPLFHITGAVINATIAlMKDCTLVFANRFAA 254
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGtcPVYLWTLPMFHCNGWTFTWGTA-ARGGTSVCMRHVTA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 255 DVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPiPPAAVEKFENKFGHYIHNAYGMTETSSGVI- 333
Cdd:PLN03102 264 PEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEATGPVLf 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 334 --------AVPPDRRAPVDPASGALSIGMAlpQVEIRVVDFDGTPLPDG-TQGELEIAGPQVVSGYWQKPEATAKTFPDG 404
Cdd:PLN03102 343 cewqdewnRLPENQQMELKARQGVSILGLA--DVDVKNKETQESVPRDGkTMGEIVIKGSSIMKGYLKNPKATSEAFKHG 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 405 RLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQ 484
Cdd:PLN03102 421 WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKED 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 485 ELRAFV---GDrLAAYKR--------PKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PLN03102 501 RVDKLVtreRD-LIEYCRenlphfmcPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
31-475 |
3.88e-37 |
|
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: 144.49 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALvlnPMYRKA---ELRHLVDDAGAVGIICAD 107
Cdd:cd17641 15 ADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSL---GIYQDSmaeEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 TAVAENAETMQDST--VRWIVGTSDLDFQTRNDPRVF--------GDRIRERHDGaddlveLVERfrgatpEAAEVSPTD 177
Cdd:cd17641 92 EEQVDKLLEIADRIpsVRYVIYCDPRGMRKYDDPRLIsfedvvalGRALDRRDPG------LYER------EVAAGKGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 178 TAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHI------------TGAVIN---ATIALMK 242
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIgeqmysvgqalvCGFIVNfpeEPETMME 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 243 DC-----TLVFA-----NRFAADV---TLDA------FAEH----------------------EVTYTIGSITVFNALYN 281
Cdd:cd17641 240 DLreigpTFVLLpprvwEGIAADVrarMMDAtpfkrfMFELgmklglraldrgkrgrpvslwlRLASWLADALLFRPLRD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 282 SPAataahFASIKTLYSGGAPIPPaAVEKFENKFGHYIHNAYGMTETsSGVIAVPPDRRAPVDpasgalSIGMALPQVEI 361
Cdd:cd17641 320 RLG-----FSRLRSAATGGAALGP-DTFRFFHAIGVPLKQLYGQTEL-AGAYTVHRDGDVDPD------TVGVPFPGTEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 362 RVVDfdgtplpdgtQGELEIAGPQVVSGYWQKPEATAKTFP-DGRLRTGDVAIRDADGWIYLVDRLKDQINVS-GYKVWP 439
Cdd:cd17641 387 RIDE----------VGEILVRSPGVFVGYYKNPEATAEDFDeDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSP 456
|
490 500 510
....*....|....*....|....*....|....*.
gi 2089408387 440 REVEDALVAHPAVGEAGVVGQPDDYqgesVVAFVSL 475
Cdd:cd17641 457 QFIENKLKFSPYIAEAVVLGAGRPY----LTAFICI 488
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
31-521 |
1.41e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 142.83 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMSDAFAVALVEKGVGHGDRVGIhLQNIP-QYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAV-GIICADT 108
Cdd:PRK07768 33 GEVHERARRIAGGLAAAGVGPGDAVAV-LAGAPvEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRViGMIGAKA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 109 AVaenaetmqdstvrwiVGtsdldfqtrnDP-RVFGDRIRERHDGADDLVELVErfrGATPEAAEVSPTDTAILAYTSGT 187
Cdd:PRK07768 112 VV---------------VG----------EPfLAAAPVLEEKGIRVLTVADLLA---ADPIDPVETGEDDLALMQLTSGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANILAVATTFAELARVD-DGDVVLAVAPLFHITGAVINATIALMKDCTLVFAN--RFAADVTLDA--FA 262
Cdd:PRK07768 164 TGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTpmDFLRDPLLWAelIS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 263 EHEVTYTIGSITVFNALYNSPAATAAHFA----SIKTLYSGGAPIPPAAVEKFEN---KFG---HYIHNAYGMTETSSGV 332
Cdd:PRK07768 244 KYRGTMTAAPNFAYALLARRLRRQAKPGAfdlsSLRFALNGAEPIDPADVEDLLDagaRFGlrpEAILPAYGMAEATLAV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 333 IAVPPDRRAPVDPASGAL-------------------SIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQK 393
Cdd:PRK07768 324 SFSPCGAGLVVDEVDADLlaalrravpatkgntrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 394 PEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAV--GEAGVVGQPDDYQGES-VV 470
Cdd:PRK07768 404 DGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrpGNAVAVRLDAGHSREGfAV 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 471 AFVSLVRDAEVTEQELRAFVGDRLAAY--KRPKHIHIVD--ELPKTQTGKIRRTE 521
Cdd:PRK07768 484 AVESNAFEDPAEVRRIRHQVAHEVVAEvgVRPRNVVVLGpgSIPKTPSGKLRRAN 538
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
173-523 |
2.50e-36 |
|
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: 141.41 E-value: 2.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 173 VSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGD--VVLAVAPLFHITGAVINATIALMKDCTLVFAN 250
Cdd:cd05915 150 VPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEkdVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPiPPAAVEKFEnKFGHY-IHNAYGMTET- 328
Cdd:cd05915 230 RLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSA-APRSLIARF-ERMGVeVRQGYGLTETs 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 329 --SSGVIAVPPDRRAPvDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGE----LEIAGPQVVSGYWQKPEAT-AKTF 401
Cdd:cd05915 308 pvVVQNFVKSHLESLS-EEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATrSALT 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 402 PDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLvRDAEV 481
Cdd:cd05915 387 PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVP-RGEKP 465
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2089408387 482 TEQELRAFVGDRLAAYKR-PKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05915 466 TPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3-522 |
7.58e-36 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 142.88 E-value: 7.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL 82
Cdd:PRK10252 459 TLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 NPMYRKAELRHLVDDAGAVGIIcadtAVAENAETMQDstvrwivgTSDLDFQTRNDPRVfgdrirerhdgaddlvelver 162
Cdd:PRK10252 539 DTGYPDDRLKMMLEDARPSLLI----TTADQLPRFAD--------VPDLTSLCYNAPLA--------------------- 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 163 fRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL-FHITgaVINATIALM 241
Cdd:PRK10252 586 -PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCsFDVS--VWEFFWPFI 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 242 KDCTLVFA----NRFAADVtLDAFAEHEVTYTIGSITVFNALYNSPAATAAHF--ASIKTLYSGGAPIPPAAVEKFENKF 315
Cdd:PRK10252 663 AGAKLVMAepeaHRDPLAM-QQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQscASLRQVFCSGEALPADLCREWQQLT 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 316 GHYIHNAYGMTETSSGVIAVPPDRRAPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPE 395
Cdd:PRK10252 742 GAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPD 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 396 ATAKTF------PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAG----VVGQPDDY 464
Cdd:PRK10252 822 LTASRFiadpfaPGERMyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAAT 901
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 465 QGES--VVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:PRK10252 902 GGDArqLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
31-520 |
9.56e-36 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 141.24 E-value: 9.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMsdafAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICADTA- 109
Cdd:PRK10524 92 DEVNRM----AAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAGs 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 110 -----------VAENAETMQDSTVRWIVGTSDLDFQTRNDPR-VFGDRIRERHDGADDLVELVErfrgatpeaaevsPTD 177
Cdd:PRK10524 168 rggkvvpykplLDEAIALAQHKPRHVLLVDRGLAPMARVAGRdVDYATLRAQHLGARVPVEWLE-------------SNE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 178 TAILAYTSGTTGPPKGA---LNSHAniLAVATTFAELARVDDGDVVLA-------VAPLFHITGAVINATIALMKDCTLV 247
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVqrdTGGYA--VALATSMDTIFGGKAGETFFCasdigwvVGHSYIVYAPLLAGMATIMYEGLPT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 248 fanRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAA--TAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGM 325
Cdd:PRK10524 313 ---RPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPAllRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 326 TETSSGVIAVPPDrrapVDPASGAL-SIGMALPQVEIRVVD-FDGTPLPDGTQGELEIAGP--------------QVVSG 389
Cdd:PRK10524 390 TETGWPILAIARG----VEDRPTRLgSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGPlppgcmqtvwgdddRFVKT 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 390 YWqkpeataKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESV 469
Cdd:PRK10524 466 YW-------SLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVA 538
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 470 VAFVsLVRDAEVT---------EQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKI-RRT 520
Cdd:PRK10524 539 VAFV-VPKDSDSLadrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLlRRA 598
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
44-523 |
1.03e-35 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 141.71 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 44 LVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPmyrkaELRHlvddagavgiicADTAVAEnaetmQDSTVR 123
Cdd:PRK06060 47 LRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANP-----ELHR------------DDHALAA-----RNTEPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 124 WIVGTSDLDfqtrndprvfgDRIRerhdgADDLVELVERFRgatpEAAEVSPTDTAILA--------YTSGTTGPPKGAL 195
Cdd:PRK06060 105 LVVTSDALR-----------DRFQ-----PSRVAEAAELMS----EAARVAPGGYEPMGgdalayatYTSGTTGPPKAAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 196 NSHANILAVATTFAELA-RVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFAN-RFAADV--TLDAFAEHEVTYTIG 271
Cdd:PRK06060 165 HRHADPLTFVDAMCRKAlRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSaPVTPEAaaILSARFGPSVLYGVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 272 SItvFNALYNspAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHY-IHNAYGMTETSSGVIAVPPDRRAPVdpasgal 350
Cdd:PRK06060 245 NF--FARVID--SCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIpILDGIGSTEVGQTFVSNRVDEWRLG------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 351 SIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTfpDGRLRTGDVAIRDADGWIYLVDRLKDQI 430
Cdd:PRK06060 314 TLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 431 NVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAF---VGDRLAAYKRPKHIHIVD 507
Cdd:PRK06060 392 VIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLhrgLLNRLSAFKVPHRFAVVD 471
|
490
....*....|....*.
gi 2089408387 508 ELPKTQTGKIRRTELR 523
Cdd:PRK06060 472 RLPRTPNGKLVRGALR 487
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
177-523 |
2.30e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 135.56 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 177 DTAILAYTSGTTGPPKGALNSHANILAVAT-TFAELArvDDGDVVLAVaPLFHITG------AVINATIALMKDCTLVFa 249
Cdd:PRK07824 36 DVALVVATSGTTGTPKGAMLTAAALTASADaTHDRLG--GPGQWLLAL-PAHHIAGlqvlvrSVIAGSEPVELDVSAGF- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 nrfaaDVTLDAFAEHEV----TYT-IGSITVFNALyNSPAATAAhFASIKTLYSGGAPIPPAAVEKFEnKFGHYIHNAYG 324
Cdd:PRK07824 112 -----DPTALPRAVAELgggrRYTsLVPMQLAKAL-DDPAATAA-LAELDAVLVGGGPAPAPVLDAAA-AAGINVVRTYG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 325 MTETSSGVIavppdrrapVDpasgalsiGMALPQVEIRVVDfdgtplpdgtqGELEIAGPQVVSGYWQKPEATAKTFPdG 404
Cdd:PRK07824 184 MSETSGGCV---------YD--------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVDPDPFAEP-G 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 405 RLRTGDVAIRDaDGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQ 484
Cdd:PRK07824 235 WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 2089408387 485 ELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
8-522 |
2.62e-34 |
|
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: 134.87 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 8 WKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYR 87
Cdd:cd17644 6 FEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 88 KAELRHLVDDAGavgiicadtavaenaetmqdstVRWIVgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgat 167
Cdd:cd17644 86 QERLTYILEDAQ----------------------ISVLL----------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 168 peaaeVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL-FHITGAVINATiaLMKDCTL 246
Cdd:cd17644 103 -----TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIaFDVAAEEIYVT--LLSGATL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 247 VF--ANRFAADVTLDAFAEHEvtytigSITVFN---------ALYNSPAaTAAHFASIKTLYSGGAPIPPAAVEKFENKF 315
Cdd:cd17644 176 VLrpEEMRSSLEDFVQYIQQW------QLTVLSlppaywhllVLELLLS-TIDLPSSLRLVIVGGEAVQPELVRQWQKNV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 316 GHYIH--NAYGMTETSsgVIAVPPDRRAPVDPASGALSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQK 393
Cdd:cd17644 249 GNFIQliNVYGPTEAT--IAATVCRLTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 394 PEATAKTF--------PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDY 464
Cdd:cd17644 327 PELTAEKFishpfnssESERLyKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQP 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2089408387 465 QGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17644 407 GNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
29-523 |
5.90e-34 |
|
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: 134.10 E-value: 5.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 29 SAREVDEMSDAFAVALV-EKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHlvddagavgiiCAD 107
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIH-----------CLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 TavaenaetmqdSTVRWIVgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaeVSPTDTAILAYTSGT 187
Cdd:cd05937 76 L-----------SGSRFVI----------------------------------------------VDPDDPAILIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVT 267
Cdd:cd05937 99 TGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGAT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 268 YTIGSITVFNALYNSPAATAAHFASIKTLYSGGapIPPAAVEKFENKFG-HYIHNAYGMTEtssGVIAVPPDRRAPVdpa 346
Cdd:cd05937 179 IIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNG--LRPDIWERFRERFNvPEIGEFYAATE---GVFALTNHNVGDF--- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 347 sGALSIGMALP---------QVEIRVVDFDGTPL-----------PDGTQGELEIAGP----QVVSGYWQKPEATAK--- 399
Cdd:cd05937 251 -GAGAIGHHGLirrwkfenqVVLVKMDPETDDPIrdpktgfcvraPVGEPGEMLGRVPfknrEAFQGYLHNEDATESklv 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 400 --TFPDGRL--RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVG-QPDDYQGESVVAFVS 474
Cdd:cd05937 330 rdVFRKGDIyfRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvKVPGHDGRAGCAAIT 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 475 LVRDA----EVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05937 410 LEESSavptEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
14-519 |
1.42e-33 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 133.48 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 14 ANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALvlnPmyrkaelrh 93
Cdd:PRK04813 14 TQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYI---P--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 94 lVDDAGAVGIIcadTAVAENAETmqdstvRWIVGTSDLDFqTRNDPRVFgdrirerhdgadDLVELVERFRGATPEAAE- 172
Cdd:PRK04813 82 -VDVSSPAERI---EMIIEVAKP------SLIIATEELPL-EILGIPVI------------TLDELKDIFATGNPYDFDh 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 173 -VSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL-FHI----------TGAVINAtiaL 240
Cdd:PRK04813 139 aVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYsFDLsvmdlyptlaSGGTLVA---L 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 241 MKDCTLVFANRFAADVTLD--------AFAEHevtytigsitvfnALYnSPAATAAHFASIKTLYSGGAPIPPAAVEKFE 312
Cdd:PRK04813 216 PKDMTANFKQLFETLPQLPinvwvstpSFADM-------------CLL-DPSFNEEHLPNLTHFLFCGEELPHKTAKKLL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 313 NKFGH-YIHNAYGMTETSSGV--IAVPPDRRAPVDPasgaLSIGMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSG 389
Cdd:PRK04813 282 ERFPSaTIYNTYGPTEATVAVtsIEITDEMLDQYKR----LPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 390 YWQKPEATAKTF--PDGR--LRTGDVAIRDADGWIYLvDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQ 465
Cdd:PRK04813 358 YLNNPEKTAEAFftFDGQpaYHTGDAGYLEDGLLFYQ-GRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHK 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2089408387 466 GESVVAFVSL-----VRDAEVTeQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRR 519
Cdd:PRK04813 437 VQYLIAYVVPkeedfEREFELT-KAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
25-522 |
2.52e-33 |
|
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: 133.19 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 25 DGILSAREVDEMSDAFAVALV-EKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGI 103
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 104 IcADTAVAENAE----TMQDSTVR-WIVGTSDldfqtrndprvfgdrireRHDGADDLVELVErfrGATPEA------AE 172
Cdd:cd05938 83 V-VAPELQEAVEevlpALRADGVSvWYLSHTS------------------NTEGVISLLDKVD---AASDEPvpaslrAH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 173 VSPTDTAILAYTSGTTGPPKGALNSHANILAvATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRF 252
Cdd:cd05938 141 VTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 253 AADVTLDAFAEHEVT---YtIGSITVFnaLYNSP--AATAAHfasiKTLYSGGAPIPPAAVEKFENKFGH-YIHNAYGMT 326
Cdd:cd05938 220 SASQFWDDCRKHNVTviqY-IGELLRY--LCNQPqsPNDRDH----KVRLAIGNGLRADVWREFLRRFGPiRIREFYGST 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 327 ETSSGVIAVpPDRRAPVDPASGALSigMALPQVEIR--------VVDFDG--TPLPDGTQGEL--EIAGPQVVSGYWQKP 394
Cdd:cd05938 293 EGNIGFFNY-TGKIGAVGRVSYLYK--LLFPFELIKfdvekeepVRDAQGfcIPVAKGEPGLLvaKITQQSPFLGYAGDK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 395 EATAK-----TFPDGRL--RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQP-DDYQG 466
Cdd:cd05938 370 EQTEKkllrdVFKKGDVyfNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTvPGHEG 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2089408387 467 ESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd05938 450 RIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
28-523 |
2.53e-33 |
|
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: 133.11 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGV--GHGDRVGIHLQNIPQYAIAFLALWklgAAALVLNPMYrkaelrhlvddagavgiic 105
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACY---AYSLVTVPLY------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 106 adtavaenaETMQDSTVRWIVGTSDLDFqtrndprVFGDrirerhDGA-----DDLVELVERFRGATPEAAevsPTDTAI 180
Cdd:cd05927 64 ---------DTLGPEAIEYILNHAEISI-------VFCD------AGVkvyslEEFEKLGKKNKVPPPPPK---PEDLAT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 181 LAYTSGTTGPPKGALNSHANIL----AVATTFAELARVDDGDVVLAVAPLFHI-TGAVINATIA--------------LM 241
Cdd:cd05927 119 ICYTSGTTGNPKGVMLTHGNIVsnvaGVFKILEILNKINPTDVYISYLPLAHIfERVVEALFLYhgakigfysgdirlLL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 242 KDC-TL---VFA------NRFAADVtldaFAEHEVTYTIGSiTVFNALYNSPAA-------TAAHFA------------- 291
Cdd:cd05927 199 DDIkALkptVFPgvprvlNRIYDKI----FNKVQAKGPLKR-KLFNFALNYKLAelrsgvvRASPFWdklvfnkikqalg 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 292 -SIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDrrapvDPASGalSIGMALPQVEIRVVD----- 365
Cdd:cd05927 274 gNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPG-----DTSVG--HVGGPLPCAEVKLVDvpemn 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 366 FDGTPLPDgtQGELEIAGPQVVSGYWQKPEATAKTFP-DGRLRTGDVAIRDADGWIYLVDRLKDQINVS-GYKVWPREVE 443
Cdd:cd05927 347 YDAKDPNP--RGEVCIRGPNVFSGYYKDPEKTAEALDeDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYVAPEKIE 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 444 DALVAHPAVGEAGVVGqpDDYQgESVVAFVslVRDAEVTE-------------------QELRAFV---------GDRLA 495
Cdd:cd05927 425 NIYARSPFVAQIFVYG--DSLK-SFLVAIV--VPDPDVLKewaaskgggtgsfeelcknPEVKKAIledlvrlgkENGLK 499
|
570 580 590
....*....|....*....|....*....|....
gi 2089408387 496 AYKRPKHIHIVDELPK------TQTGKIRRTELR 523
Cdd:cd05927 500 GFEQVKAIHLEPEPFSvengllTPTFKLKRPQLK 533
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
24-528 |
2.81e-33 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 134.25 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 24 FDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVL--------------------- 82
Cdd:PLN02654 117 FDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVfagfsaeslaqrivdckpkvv 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 83 ---NPMYRKAELRHLVDDAGAVGIICADTAVA-------ENAETMQDSTVRWIVGtSDLDFQtrndprvfgdrirerhdg 152
Cdd:PLN02654 197 itcNAVKRGPKTINLKDIVDAALDESAKNGVSvgicltyENQLAMKREDTKWQEG-RDVWWQ------------------ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 153 addlvELVERFRgATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHAN-ILAVATTFAELARVDDGDVVLAVAPLFHITG 231
Cdd:PLN02654 258 -----DVVPNYP-TKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCGWITG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 232 -AVINATIALMKDCTLVF---ANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFA--SIKTLYSGGAPIPP 305
Cdd:PLN02654 332 hSYVTYGPMLNGATVLVFegaPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSrkSLRVLGSVGEPINP 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 306 AAVEKFENKFGHY---IHNAYGMTETSsGVIAVPPDRRAPVDPASGALSIGMALPQVeirvVDFDGTPLPDGTQGELEIA 382
Cdd:PLN02654 412 SAWRWFFNVVGDSrcpISDTWWQTETG-GFMITPLPGAWPQKPGSATFPFFGVQPVI----VDEKGKEIEGECSGYLCVK 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 383 GP-----QVVSGYWQKPEATA-KTFPdGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAG 456
Cdd:PLN02654 487 KSwpgafRTLYGDHERYETTYfKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAA 565
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2089408387 457 VVGQPDDYQGESVVAFVSLVRDAEVTEqELRA----FVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRNTEAK 528
Cdd:PLN02654 566 VVGIEHEVKGQGIYAFVTLVEGVPYSE-ELRKslilTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASR 640
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
32-459 |
6.80e-33 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 131.44 E-value: 6.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 32 EVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIIcadtava 111
Cdd:cd05932 11 EVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 112 enaetmqdstvrwiVGTsdLDFQTRNDPRVFGDRIR---------ERHDGADDLVELVERFRGATPEAAEvsptDTAILA 182
Cdd:cd05932 84 --------------VGK--LDDWKAMAPGVPEGLISislpppsaaNCQYQWDDLIAQHPPLEERPTRFPE----QLATLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 183 YTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFA---NRFAADVT-- 257
Cdd:cd05932 144 YTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAeslDTFVEDVQra 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 258 ----------LDAFAEHEVTYTIG--------SITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENkFGHYI 319
Cdd:cd05932 224 rptlffsvprLWTKFQQGVQDKIPqqklnlllKIPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYRS-LGLNI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 320 HNAYGMTETSS-GVIAVPPDRRAPvdpasgalSIGMALPQVEIRVVDfdgtplpdgtQGELEIAGPQVVSGYWQKPEATA 398
Cdd:cd05932 303 LEAYGMTENFAySHLNYPGRDKIG--------TVGNAGPGVEVRISE----------DGEILVRSPALMMGYYKDPEATA 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 399 KTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVS-GYKVWPREVEDALVAHPAVGEAGVVG 459
Cdd:cd05932 365 EAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
294-523 |
4.55e-32 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 128.19 E-value: 4.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 294 KTLYSGGAPIPPAAVEKFENkfgHYIHNA--YGMTETSSGVIAVPPDrrapvDPASGALSIGMALPQVEIRvvdfdgtpL 371
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQARQ---LQLRLAptYGMTETASQIATLKPD-----DFLAGNNSSGQVLPHAQIT--------I 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 372 PDGTQGELEIAGPQVVSGYWQKPEATAKTFPdgrlrTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPA 451
Cdd:PRK07445 297 PANQTGNITIQAQSLALGYYPQILDSQGIFE-----TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2089408387 452 VGEAGVVGQPDDYQGESVVAFVSLVrDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK07445 372 VQDVCVLGLPDPHWGEVVTAIYVPK-DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
180-529 |
1.83e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 125.92 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 180 ILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFAN----RFAad 255
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITnknpKFA-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 256 vtLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFAsiktLYSGGAPIPPAAVEKFENKFGHYIHNaYGMTEtsSGVIAV 335
Cdd:PRK08308 183 --LNILRNTPQHILYAVPLMLHILGRLLPGTFQFHA----VMTSGTPLPEAWFYKLRERTTYMMQQ-YGCSE--AGCVSI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 336 PPDRRAPVDpasgalsIGMALPQVEIrvvdfdgtplpdgTQGELEiagpqvvsgywQKPEATAKTFPDGRLRTGDVAIRD 415
Cdd:PRK08308 254 CPDMKSHLD-------LGNPLPHVSV-------------SAGSDE-----------NAPEEIVVKMGDKEIFTKDLGYKS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 416 ADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSlvRDAEVTEQELRAFVGDRLA 495
Cdd:PRK08308 303 ERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI--SHEEIDPVQLREWCIQHLA 380
|
330 340 350
....*....|....*....|....*....|....
gi 2089408387 496 AYKRPKHIHIVDELPKTQTGKIRRTELRNTEAKV 529
Cdd:PRK08308 381 PYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
16-522 |
2.97e-31 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 127.05 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 16 PEHPAIAYFDGI--LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRH 93
Cdd:PRK05857 28 PEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 94 LVDdagavgiICADTAVAENAETMqdstvrwiVGTSDLDFQTRNDPRVfgdrireRHDGADDLVELVERFRGATPEAAEV 173
Cdd:PRK05857 108 FCQ-------ITDPAAALVAPGSK--------MASSAVPEALHSIPVI-------AVDIAAVTRESEHSLDAASLAGNAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 174 SPTDTAI-LAYTSGTTGPPKGALNSHANILAVATTFAE--LARVD--DGDVVLAVAPLFHITGA--VINAtiaLMKDCTL 246
Cdd:PRK05857 166 QGSEDPLaMIFTSGTTGEPKAVLLANRTFFAVPDILQKegLNWVTwvVGETTYSPLPATHIGGLwwILTC---LMHGGLC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 247 VFANRFAADVTlDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVeKFENKFGHYIHNAYGMT 326
Cdd:PRK05857 243 VTGGENTTSLL-EILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADV-RFIEATGVRTAQVYGLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 327 ETSSGVIAVPPDRRAPVDPASGAlsIGMALPQVEIRVVDFDG----TPL--PDGTQGELEIAGPQVVSGYWQKPEATAKT 400
Cdd:PRK05857 321 ETGCTALCLPTDDGSIVKIEAGA--VGRPYPGVDVYLAATDGigptAPGagPSASFGTLWIKSPANMLGYWNNPERTAEV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 401 FPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGesvvAFVSL--VRD 478
Cdd:PRK05857 399 LIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG----ALVGLavVAS 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 479 AEVTEQELRAFVGDRLAAYK-------RPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:PRK05857 475 AELDESAARALKHTIAARFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
174-473 |
8.89e-30 |
|
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: 122.32 E-value: 8.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 174 SPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAElaRVDDG----DVVLAVAPLFHITG-AVINatIALMKDCTLVF 248
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGD--RVPELlgpdDRYLAYLPLAHIFElAAEN--VCLYRGGTIGY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 249 ANrfAADVTLDAFAE-----HEVTYTI----------------------GSI--TVFNALYN-----------SPAATAA 288
Cdd:cd17639 162 GS--PRTLTDKSKRGckgdlTEFKPTLmvgvpaiwdtirkgvlaklnpmGGLkrTLFWTAYQsklkalkegpgTPLLDEL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 289 HFASIKTL--------YSGGAPIPPAAvEKFENKFGHYIHNAYGMTETSS-GVIAVPPDrrapvdPASGalSIGMALPQV 359
Cdd:cd17639 240 VFKKVRAAlggrlrymLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETCAgGTVQDPGD------LETG--RVGPPLPCC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 360 EIRVVDFD------GTPLPdgtQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQI-N 431
Cdd:cd17639 311 EIKLVDWEeggystDKPPP---RGEILIRGPNVFKGYYKNPEKTKEAFdGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkL 387
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2089408387 432 VSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQgesVVAFV 473
Cdd:cd17639 388 QNGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIV 426
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-524 |
1.68e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 117.96 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDG------ILSAREVDEMSDAFAVALVEKGvGHGDRVGIHLQNIPQYAIAFLALWKLG 76
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRFLADdpgegvVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 77 AAALvlnPMY-----RKAELRHLvddagavgiicadtavaenAETMQDSTVRWIVGTSDLdfqtrNDPRVFGDRIRerhd 151
Cdd:PRK05691 89 VIAV---PAYppesaRRHHQERL-------------------LSIIADAEPRLLLTVADL-----RDSLLQMEELA---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 152 gADDLVEL--VERFRGATPE---AAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDG--DVVLAVA 224
Cdd:PRK05691 138 -AANAPELlcVDTLDPALAEawqEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 225 PLFHITGAV--INATIALMKDCTLVFANRFAADVT--LDAFAEHEVTYTIGSITVFNALYNSPAATAAH---FASIKTLY 297
Cdd:PRK05691 217 PLYHDMGLIggLLQPIFSGVPCVLMSPAYFLERPLrwLEAISEYGGTISGGPDFAYRLCSERVSESALErldLSRWRVAY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 298 SGGAPIPPAAVEKFENKFGHYIHNA------YGMTETS---------SGVIAVPPDRRA----PVDPASGA--LSIGMAL 356
Cdd:PRK05691 297 SGSEPIRQDSLERFAEKFAACGFDPdsffasYGLAEATlfvsggrrgQGIPALELDAEAlarnRAEPGTGSvlMSCGRSQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 357 PQVEIRVVD-FDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF--PDGR--LRTGDVAIRdADGWIYLVDRLKDQIN 431
Cdd:PRK05691 377 PGHAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFveHDGRtwLRTGDLGFL-RDGELFVTGRLKDMLI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 432 VSGYKVWPREVEDALVAHPAVGEAG-VVGQPDDYQGES---VVAFVSLVRDAEVTEQEL----RAFVGDrlAAYKRPKHI 503
Cdd:PRK05691 456 VRGHNLYPQDIEKTVEREVEVVRKGrVAAFAVNHQGEEgigIAAEISRSVQKILPPQALiksiRQAVAE--ACQEAPSVV 533
|
570 580
....*....|....*....|...
gi 2089408387 504 HIVD--ELPKTQTGKIRRTELRN 524
Cdd:PRK05691 534 LLLNpgALPKTSSGKLQRSACRL 556
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
15-523 |
2.43e-27 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 114.58 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 15 NPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHL 94
Cdd:PRK09029 16 RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 95 VDDAGAVGIICADTAVAENAETMQdsTVRWIVGTSDLDFQTRndprvfgdrirerhdgaddlvelverfRGATpeaaevs 174
Cdd:PRK09029 96 LPSLTLDFALVLEGENTFSALTSL--HLQLVEGAHAVAWQPQ---------------------------RLAT------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 175 ptdtaiLAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVInatIA--LMKDCTLVF--AN 250
Cdd:PRK09029 140 ------MTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGI---VWrwLYAGATLVVrdKQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 RFAADVtldafaeHEVTYTigSI--TVFNALYNSPAATAahfaSIKTLYSGGAPIPPAAVEKFEnKFGhyIHN--AYGMT 326
Cdd:PRK09029 211 PLEQAL-------AGCTHA--SLvpTQLWRLLDNRSEPL----SLKAVLLGGAAIPVELTEQAE-QQG--IRCwcGYGLT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 327 ETSSGVIAVPPDRRAPVdpasgalsiGMALPQVEIRVVDfdgtplpdgtqGELEIAGPQVVSGYWQkpeataktfpDGRL 406
Cdd:PRK09029 275 EMASTVCAKRADGLAGV---------GSPLPGREVKLVD-----------GEIWLRGASLALGYWR----------QGQL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 407 rtgdVAIRDADGWIYLVD-------------RLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFV 473
Cdd:PRK09029 325 ----VPLVNDEGWFATRDrgewqngeltilgRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 474 SLvrDAEVTEQELRAFVGDRLAAYKRPKHIHIvdeLPKT--QTG-KIRRTELR 523
Cdd:PRK09029 401 ES--DSEAAVVNLAEWLQDKLARFQQPVAYYL---LPPElkNGGiKISRQALK 448
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
166-523 |
4.68e-27 |
|
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: 114.51 E-value: 4.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 166 ATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPL--------FHITGAVINAT 237
Cdd:cd05908 96 TEEEVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLthdmgliaFHLAPLIAGMN 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 238 IALMKdcTLVFANRfaADVTLDAFAEHEVTYT----IGSiTVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFEN 313
Cdd:cd05908 176 QYLMP--TRLFIRR--PILWLKKASEHKATIVsspnFGY-KYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 314 KFGHY------IHNAYGMTETSSGVIAVPPDRR--------------APV------DP-ASGALSIGMALPQVEIRVVDF 366
Cdd:cd05908 251 HMSKYglkrnaILPVYGLAEASVGASLPKAQSPfktitlgrrhvthgEPEpevdkkDSeCLTFVEVGKPIDETDIRICDE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 367 DGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVA-IRdaDGWIYLVDRLKDQINVSGYKVWPREVED 444
Cdd:cd05908 331 DNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGfIR--NGRLVITGREKDIIFVNGQNVYPHDIER 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 445 ALVAHPAV--GEAGVVGQPD-DYQGESVVAFVSLVRDAEvteqELRAFVGD-RLAAYKRPK-HIHIV---DELPKTQTGK 516
Cdd:cd05908 409 IAEELEGVelGRVVACGVNNsNTRNEEIFCFIEHRKSED----DFYPLGKKiKKHLNKRGGwQINEVlpiRRIPKTTSGK 484
|
....*..
gi 2089408387 517 IRRTELR 523
Cdd:cd05908 485 VKRYELA 491
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
441-516 |
1.03e-26 |
|
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: 103.01 E-value: 1.03e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2089408387 441 EVEDALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGK 516
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
28-488 |
4.53e-26 |
|
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: 111.01 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDA---GAVGII 104
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAepdAFIGIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 105 CADtavaenaetmqdstvrwivgtsdldfqtrndprvfgdrirerhdgaddlvelverfrgatpeaaevsptDTAILAYT 184
Cdd:cd05910 83 KAD---------------------------------------------------------------------EPAAILFT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 185 SGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATiALMKDCTLVFANRFAADVTLDAFAEH 264
Cdd:cd05910 94 SGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLT-SVIPDMDPTRPARADPQKLVGAIRQY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 265 EVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKF--GHYIHNAYGMTE----TSSGVIAVPPD 338
Cdd:cd05910 173 GVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEalpvSSIGSRELLAT 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 339 RRAPVDPASGaLSIGMALPQVEIRVVDFDGTP---------LPDGTQGELEIAGPQVVSGYWQKPEATAKT-FPDGR--- 405
Cdd:cd05910 253 TTAATSGGAG-TCVGRPIPGVRVRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAkIDDNSegf 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 406 -LRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVG--QPDDYQGESVV-AFVSLVRDAEV 481
Cdd:cd05910 332 wHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGvgKPGCQLPVLCVePLPGTITPRAR 411
|
....*..
gi 2089408387 482 TEQELRA 488
Cdd:cd05910 412 LEQELRA 418
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
28-523 |
6.75e-25 |
|
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: 107.51 E-value: 6.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIICad 107
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 108 tavaenaeTMQDstvrwivgtsDLDFQTRNDPrvfgdrirerhdgaddlvelverfrgatPEAAEVSPTDTAILAYTSGT 187
Cdd:cd05939 82 --------NLLD----------PLLTQSSTEP----------------------------PSQDDVNFRDKLFYIYTSGT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 188 TGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFANRFAADVTLDAFAEHEVT 267
Cdd:cd05939 116 TGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 268 YT--IGSITVFnaLYNSPAATAAHFASIKTLYSGGapIPPAAVEKFENKFG-HYIHNAYGMTETSSGVI----------- 333
Cdd:cd05939 196 IVqyIGEICRY--LLAQPPSEEEQKHNVRLAVGNG--LRPQIWEQFVRRFGiPQIGEFYGATEGNSSLVnidnhvgacgf 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 334 ------AVPPDRRAPVDPASGALsigmalpqveIRvvDFDGTPLP--DGTQGEL--EIAGPQVVS---GYWQKpEATAK- 399
Cdd:cd05939 272 nsrilpSVYPIRLIKVDEDTGEL----------IR--DSDGLCIPcqPGEPGLLvgKIIQNDPLRrfdGYVNE-GATNKk 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 400 ------TFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALvaHPAVGEA-----GV-VGQPDDYQGE 467
Cdd:cd05939 339 iardvfKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGIL--SNVLGLEdvvvyGVeVPGVEGRAGM 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2089408387 468 SVVAFVSLVRDAEVTEQELRAfvgdRLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:cd05939 417 AAIVDPERKVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
147-524 |
3.20e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 106.24 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 147 RERHDGADDLVELVERFRGATPEaaeVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELA-RVDDGDVVLAVAP 225
Cdd:PRK09192 150 PLLHVLSHAWFKALPEADVALPR---PTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGlKVRPGDRCVSWLP 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 226 LFHITGAV--------INATIALMKdcTLVFANRfaADVTLDAFAEHEvtytiGSITVfnalynSPA---ATAAHFASIK 294
Cdd:PRK09192 227 FYHDMGLVgflltpvaTQLSVDYLP--TRDFARR--PLQWLDLISRNR-----GTISY------SPPfgyELCARRVNSK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 295 TLYS-----------GGAPIPPAAVEKFENKFG--HYIHNA----YGMTETSSGVIAVPPDR------------------ 339
Cdd:PRK09192 292 DLAEldlscwrvagiGADMIRPDVLHQFAEAFApaGFDDKAfmpsYGLAEATLAVSFSPLGSgivveevdrdrleyqgka 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 340 RAPVDPASGALSI---GMALPQVEIRVVDFDGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRdA 416
Cdd:PRK09192 372 VAPGAETRRVRTFvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-L 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 417 DGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAV--GEAGVVGQPDDyQGESVVAFVslvrDAEVTEQELRAFVGDRL 494
Cdd:PRK09192 451 DGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLV----QCRISDEERRGQLIHAL 525
|
410 420 430
....*....|....*....|....*....|....*..
gi 2089408387 495 AAYKRPKH-IHIVDEL------PKTQTGKIRRTELRN 524
Cdd:PRK09192 526 AALVRSEFgVEAAVELvpphslPRTSSGKLSRAKAKK 562
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
43-523 |
1.88e-23 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 105.05 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 43 ALVEKGVGHGDRVGIHLQNIPQYAIAFLAL-----------WKLGAAAlVLNPMyRKAELRHlvddagavgiICADTAVA 111
Cdd:PRK06814 673 RKLKKNTPPGENVGVMLPNANGAAVTFFALqsagrvpaminFSAGIAN-ILSAC-KAAQVKT----------VLTSRAFI 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 112 ENAEtMQDSTvrwivgtSDLDFQTRndpRVFGDRIRERHDGADDLVELVERFRGATPeAAEVSPTDTAILAYTSGTTGPP 191
Cdd:PRK06814 741 EKAR-LGPLI-------EALEFGIR---IIYLEDVRAQIGLADKIKGLLAGRFPLVY-FCNRDPDDPAVILFTSGSEGTP 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 192 KGALNSHANILAVATTFAelARVD--DGDVVLAVAPLFH---ITGAVINATIALMKdcTLVFAN----RFAADVTLDAFA 262
Cdd:PRK06814 809 KGVVLSHRNLLANRAQVA--ARIDfsPEDKVFNALPVFHsfgLTGGLVLPLLSGVK--VFLYPSplhyRIIPELIYDTNA 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 263 ehevTYTIGSITVFNAlYnspaATAAH---FASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSgVIAVppdr 339
Cdd:PRK06814 885 ----TILFGTDTFLNG-Y----ARYAHpydFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAP-VIAL---- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 340 RAPVDPASGalSIGMALPQVEIRVVDFDGtpLPDGtqGELEIAGPQVVSGYWqKPEA--TAKTFPDGRLRTGDVAIRDAD 417
Cdd:PRK06814 951 NTPMHNKAG--TVGRLLPGIEYRLEPVPG--IDEG--GRLFVRGPNVMLGYL-RAENpgVLEPPADGWYDTGDIVTIDEE 1023
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 418 GWIYLVDRLKDQINVSGYKVWPREVEdALVAH--PAVGEAgVVGQPDDYQGESVVAFVSlvrDAEVTEQELRAFVGDR-- 493
Cdd:PRK06814 1024 GFITIKGRAKRFAKIAGEMISLAAVE-ELAAElwPDALHA-AVSIPDARKGERIILLTT---ASDATRAAFLAHAKAAga 1098
|
490 500 510
....*....|....*....|....*....|..
gi 2089408387 494 --LAAykrPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK06814 1099 seLMV---PAEIITIDEIPLLGTGKIDYVAVT 1127
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1-481 |
1.19e-22 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 101.71 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 1 MATLVDVWKARVAANPEHPaiaYF------DGILSAR------EVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIA 68
Cdd:PLN02736 43 IGTLHDNFVYAVETFRDYK---YLgtrirvDGTVGEYkwmtygEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 69 FLALwklGAAALVLNPMYRKA---ELRHLVDDAGAVGIICadtaVAENAETM-----QDSTVRWIVGTSDLDFQTRNDPR 140
Cdd:PLN02736 120 DHAC---SAYSYVSVPLYDTLgpdAVKFIVNHAEVAAIFC----VPQTLNTLlsclsEIPSVRLIVVVGGADEPLPSLPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 141 VFGDRI----RERHDGADDLVElverFRGATPEaaevsptDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDD 216
Cdd:PLN02736 193 GTGVEIvtysKLLAQGRSSPQP----FRPPKPE-------DVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 217 GDVVLAVAPLFHI-----------TGAVIN----ATIALMKDCTL----VFA------NRFAADVTLDAFAEHEVTYTIg 271
Cdd:PLN02736 262 SDVHISYLPLAHIyervnqivmlhYGVAVGfyqgDNLKLMDDLAAlrptIFCsvprlyNRIYDGITNAVKESGGLKERL- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 272 sitvFNALYN------------SPAATAAHFASIKT--------LYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSG 331
Cdd:PLN02736 341 ----FNAAYNakkqalengknpSPMWDRLVFNKIKAklggrvrfMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 332 VIAVPPDrrapvDPASGalSIGMALPQVEIRVVDF-------DGTPLPdgtQGELEIAGPQVVSGYWQKPEATAKTF-PD 403
Cdd:PLN02736 417 ISGMDEG-----DNLSG--HVGSPNPACEVKLVDVpemnytsEDQPYP---RGEICVRGPIIFKGYYKDEVQTREVIdED 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2089408387 404 GRLRTGDVAIRDADGWIYLVDRLKDQINVS-GYKVWPREVEDALVAHPAVGEAGVVGqpdDYQGESVVAFVSLvrDAEV 481
Cdd:PLN02736 487 GWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYAKCKFVAQCFVYG---DSLNSSLVAVVVV--DPEV 560
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
165-521 |
6.99e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 99.25 E-value: 6.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 165 GATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILA-----VATTFAELARVDDGD-VVLAVAPLFHITGAVINATI 238
Cdd:PRK05850 149 PRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIAnfeqlMSDYFGDTGGVPPPDtTVVSWLPFYHDMGLVLGVCA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 239 ALMKDCTLVFANRFAadvtldaFAEHEVTYtigsitvFNALYNSPAA-TAA-HFA-------------------SIKTLY 297
Cdd:PRK05850 229 PILGGCPAVLTSPVA-------FLQRPARW-------MQLLASNPHAfSAApNFAfelavrktsdddmagldlgGVLGII 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 298 SGGAPIPPAAVEKFENKFGHY------IHNAYGMTETSSGVIAVPPDRRAPV---DPASgaLSIGMA------------- 355
Cdd:PRK05850 295 SGSERVHPATLKRFADRFAPFnlretaIRPSYGLAEATVYVATREPGQPPESvrfDYEK--LSAGHAkrcetgggtplvs 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 356 --LPQVEI-RVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF-----------PDGR-LRTGDVAIRDaDGW 419
Cdd:PRK05850 373 ygSPRSPTvRIVDPDtCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtPEGPwLRTGDLGFIS-EGE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 420 IYLVDRLKDQINVSGYKVWPREVEdALVAHPAVGEAGVVGQPDDyQGESVVAFVSLVR----DAEVTEqELRAFVGDRLA 495
Cdd:PRK05850 452 LFIVGRIKDLLIVDGRNHYPDDIE-ATIQEITGGRVAAISVPDD-GTEKLVAIIELKKrgdsDEEAMD-RLRTVKREVTS 528
|
410 420 430
....*....|....*....|....*....|...
gi 2089408387 496 AYKRPKHIHIVD-------ELPKTQTGKIRRTE 521
Cdd:PRK05850 529 AISKSHGLSVADlvlvapgSIPITTSGKIRRAA 561
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
21-427 |
3.52e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 97.35 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 21 IAYFDG--ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDA 98
Cdd:PTZ00216 113 VTHFNEtrYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRET 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 99 GAVGIICADTAVAENAETMQDSTVRwivgtsdldfqtrNDPRVFGDRIRERHDGAD-------DLVELVERFRGATPEAA 171
Cdd:PTZ00216 193 ECKAIVCNGKNVPNLLRLMKSGGMP-------------NTTIIYLDSLPASVDTEGcrlvawtDVVAKGHSAGSHHPLNI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 172 EVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAE-----LARVDDGDVVLAVAPLFHITG-AVINatIALMKDCT 245
Cdd:PTZ00216 260 PENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDrlndlIGPPEEDETYCSYLPLAHIMEfGVTN--IFLARGAL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 246 LVFANRFaadvTL-DAFA-------EHEVTYTIG------SI----------------TVFNALYNSP------------ 283
Cdd:PTZ00216 338 IGFGSPR----TLtDTFArphgdltEFRPVFLIGvprifdTIkkaveaklppvgslkrRVFDHAYQSRlralkegkdtpy 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 284 -------AATAAHFASIKTLYSGGAPIPPAAVEkFENK-FGHYIhNAYGMTET-SSGVIAVPPDrrapVDPASgalsIGM 354
Cdd:PTZ00216 414 wnekvfsAPRAVLGGRVRAMLSGGGPLSAATQE-FVNVvFGMVI-QGWGLTETvCCGGIQRTGD----LEPNA----VGQ 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2089408387 355 ALPQVEIRVVDFDG-----TPLPdgtQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLK 427
Cdd:PTZ00216 484 LLKGVEMKLLDTEEykhtdTPEP---RGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-522 |
6.53e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.55 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 5 VDVWKARVAANPEHPAIAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIhlqnIPQYAIAFLAL----WKLGAAAL 80
Cdd:PRK05691 3723 VRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVAL----LAERGLDLLGMivgsFKAGAGYL 3798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 81 VLNPMYRKAELRHLVDDAGAVGIICAdTAVAENAETMQDstvrwivgtsdlDFQTRNDPRVfgdrirerhdgaddLV-EL 159
Cdd:PRK05691 3799 PLDPGLPAQRLQRIIELSRTPVLVCS-AACREQARALLD------------ELGCANRPRL--------------LVwEE 3851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 160 VERFRGATPEAAEVS-PTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVV---------------LAv 223
Cdd:PRK05691 3852 VQAGEVASHNPGIYSgPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIaqtasqsfdisvwqfLA- 3930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 224 APLFHITGAVINATIAlmKDCTLVFANRFAADVTldafaeheVTYTIGSItvfnaLYNSPAATAAHFASIKTLYSGGAPI 303
Cdd:PRK05691 3931 APLFGARVEIVPNAIA--HDPQGLLAHVQAQGIT--------VLESVPSL-----IQGMLAEDRQALDGLRWMLPTGEAM 3995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 304 PPAAVEKFENKFGHY-IHNAYGMTETSSGVIAVPpdrrapVDPASGA---LSIGMALPQVEIRVVDFDGTPLPDGTQGEL 379
Cdd:PRK05691 3996 PPELARQWLQRYPQIgLVNAYGPAECSDDVAFFR------VDLASTRgsyLPIGSPTDNNRLYLLDEALELVPLGAVGEL 4069
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 380 EIAGPQVVSGYWQKPEATAKTF-------PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPA 451
Cdd:PRK05691 4070 CVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLyRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAE 4149
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 452 VGEAGVVGQpDDYQGESVVAFVsLVRDAEVTEQELRAFVGDRLAA----YKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:PRK05691 4150 VREAAVAVQ-EGVNGKHLVGYL-VPHQTVLAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
9-499 |
1.70e-20 |
|
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: 94.81 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 9 KARVAanPEHPAIAYFDG-----ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLN 83
Cdd:cd05921 4 WARQA--PDRTWLAEREGnggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 84 PMYR-----KAELRHLVD--DAGAVgiicadtaVAENAETMQDStvrwiVGTSDLDfqtrnDPRVFGDRIRERHDGADDL 156
Cdd:cd05921 82 PAYSlmsqdLAKLKHLFEllKPGLV--------FAQDAAPFARA-----LAAIFPL-----GTPLVVSRNAVAGRGAISF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 157 VELVER-FRGATPEA-AEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGD--VVLAVAPLFHITGA 232
Cdd:cd05921 144 AELAATpPTAAVDAAfAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 233 VINATIALMKDCTLVF------ANRFAAdvTLDAFAEHEVTY----TIGSITVFNALYNSPAATAAHFASIKTLYSGGAP 302
Cdd:cd05921 224 NHNFNLVLYNGGTLYIddgkpmPGGFEE--TLRNLREISPTVyfnvPAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 303 IPPAAVEKFEN----KFGHYI--HNAYGMTETSsgviavpPDRRAPVDPASGALSIGMALPQVEIRVVDFDGtplpdgtQ 376
Cdd:cd05921 302 LSQDVWDRLQAlavaTVGERIpmMAGLGATETA-------PTATFTHWPTERSGLIGLPAPGTELKLVPSGG-------K 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 377 GELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDvAIRDAD------GWIY---LVDRLKDQinvSGYKVWPREVEDAL 446
Cdd:cd05921 368 YEVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGD-AAKLADpddpakGLVFdgrVAEDFKLA---SGTWVSVGPLRARA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 447 VAH--PAVGEAGVVGQPDDYQGESVVAFVSLVR---------DAEVTEQE-LRAFVGDRLAAYKR 499
Cdd:cd05921 444 VAAcaPLVHDAVVAGEDRAEVGALVFPDLLACRrlvglqeasDAEVLRHAkVRAAFRDRLAALNG 508
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
31-521 |
1.82e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 94.88 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALwklGAAALVLNPMYRKAelrhlvdDAGAVGIIcadtav 110
Cdd:PLN02430 80 KEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEAC---AAHSLICVPLYDTL-------GPGAVDYI------ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 111 AENAET----MQDSTVRWIvgtsdLDFQTRNDPRV-----FGDRIRERHDGADDL-------VELVERFRGATPEAAEVS 174
Cdd:PLN02430 144 VDHAEIdfvfVQDKKIKEL-----LEPDCKSAKRLkaivsFTSVTEEESDKASQIgvktyswIDFLHMGKENPSETNPPK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 175 PTDTAILAYTSGTTGPPKGALNSHANILAVAT-------TFAELARVDDgdVVLAVAPLFHITGAVINAtialmkdctlV 247
Cdd:PLN02430 219 PLDICTIMYTSGTSGDPKGVVLTHEAVATFVRgvdlfmeQFEDKMTHDD--VYLSFLPLAHILDRMIEE----------Y 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 248 FANRFAA--------DVTLDAFAEHEVTYTIGSITV----------------------FNALYN---------------S 282
Cdd:PLN02430 287 FFRKGASvgyyhgdlNALRDDLMELKPTLLAGVPRVferihegiqkalqelnprrrliFNALYKyklawmnrgyshkkaS 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 283 PAATAAHFASIKT--------LYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAVPPDRRAPVDpASGALSIGM 354
Cdd:PLN02430 367 PMADFLAFRKVKAklggrlrlLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMLG-TVGAPAVYN 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 355 ALPQVEIRVVDFDgtPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVS- 433
Cdd:PLN02430 446 ELRLEEVPEMGYD--PLGEPPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSq 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 434 GYKVWPREVEDALVAHPAVGEAGVVGqpdDYQGESVVAFVSLVRDAEVTEQELRAFVGDRLAAYKRPK-HIHIVDELPKT 512
Cdd:PLN02430 524 GEYVALEYLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPElKEHILSELKST 600
|
570
....*....|
gi 2089408387 513 -QTGKIRRTE 521
Cdd:PLN02430 601 aEKNKLRGFE 610
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
173-460 |
1.90e-20 |
|
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: 94.73 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 173 VSPTDTAILAYTSGTTGPPKGALNSHANIL----AVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVF 248
Cdd:cd05933 147 QKPNQCCTLIYTSGTTGMPKGVMLSHDNITwtakAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 249 ANRFA---------ADVTLDAF------------------------------------AEHEVTYTIGSITVF------N 277
Cdd:cd05933 227 AQPDAlkgtlvktlREVRPTAFmgvprvwekiqekmkavgaksgtlkrkiaswakgvgLETNLKLMGGESPSPlfyrlaK 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 278 ALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFenkFGHYI--HNAYGMTETSsGVIAVPpdrrapVDPASGALSIGMA 355
Cdd:cd05933 307 KLVFKKVRKALGLDRCQKFFTGAAPISRETLEFF---LSLNIpiMELYGMSETS-GPHTIS------NPQAYRLLSCGKA 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 356 LPQVEIRVVDFDGtplpDGtQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQI-NVS 433
Cdd:cd05933 377 LPGCKTKIHNPDA----DG-IGEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIiTAG 451
|
330 340
....*....|....*....|....*...
gi 2089408387 434 GYKVWPREVEDALVAH-PAVGEAGVVGQ 460
Cdd:cd05933 452 GENVPPVPIEDAVKKElPIISNAMLIGD 479
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
52-519 |
1.95e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 91.71 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 52 GDRVGIHL-QNIpQYAIAFLALWKLGAAALvlnPMYRKAELRHlVDDAGAVGIICADTAVAENAETMQdstvrwivGTSD 130
Cdd:PRK07769 79 GDRVAILApQNL-DYLIAFFGALYAGRIAV---PLFDPAEPGH-VGRLHAVLDDCTPSAILTTTDSAE--------GVRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 131 LdFQTR---NDPRVFGdrirerhdgaddlVELVERFRGATPEAAEVSPTDTAILAYTSGTTGPPKGALNSHANILAVATT 207
Cdd:PRK07769 146 F-FRARpakERPRVIA-------------VDAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 208 FAELARVDDGDVVLAVAPLFHITG-------AVINATIALMKdcTLVFANRFAADVTLDAFAEHevtytiGSITVFNALY 280
Cdd:PRK07769 212 VIDALEGQEGDRGVSWLPFFHDMGlitvllpALLGHYITFMS--PAAFVRRPGRWIRELARKPG------GTGGTFSAAP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 281 NSPAATAA------------HFASIKTLYSGGAPIPPAAVEKFENKFGHY------IHNAYGMTETSSGVIAVPPD---- 338
Cdd:PRK07769 284 NFAFEHAAarglpkdgepplDLSNVKGLLNGSEPVSPASMRKFNEAFAPYglpptaIKPSYGMAEATLFVSTTPMDeept 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 339 ------------RRAPVDP-ASGAL---SIG-MALPQVEIrVVDFD-GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKT 400
Cdd:PRK07769 364 viyvdrdelnagRFVEVPAdAPNAVaqvSAGkVGVSEWAV-IVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAAT 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 401 F-----------------PDGR-LRTGDVAIRdADGWIYLVDRLKDQINVSGYKVWPREVE-DALVAHPAV--GEAGVVG 459
Cdd:PRK07769 443 FqnilksrlseshaegapDDALwVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLEyTAQEATKALrtGYVAAFS 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 460 QPDDYQGESVV--AFVSLVRDAEVTEQELrAFVGDRLAAYKRPKHIHIVDE-----------------------LPKTQT 514
Cdd:PRK07769 522 VPANQLPQVVFddSHAGLKFDPEDTSEQL-VIVAERAPGAHKLDPQPIADDiraaiavrhgvtvrdvllvpagsIPRTSS 600
|
....*
gi 2089408387 515 GKIRR 519
Cdd:PRK07769 601 GKIAR 605
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
40-452 |
5.61e-19 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 90.56 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 40 FAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWK-----------LGAAALV--LNP------MYRKAELRHLVDDAGA 100
Cdd:PLN02387 119 FASGLVALGHNKEERVAIFADTRAEWLIALQGCFRqnitvvtiyasLGEEALChsLNEtevttvICDSKQLKKLIDISSQ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 101 VG----IICADTAVAENAETMQDSTvRWIVGTsdldfqtrndprvFGDrirerhdgaddlvelVERF-RGATPEAAEVSP 175
Cdd:PLN02387 199 LEtvkrVIYMDDEGVDSDSSLSGSS-NWTVSS-------------FSE---------------VEKLgKENPVDPDLPSP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 TDTAILAYTSGTTGPPKGALNSHANILA-VATTFAELARVDDGDVVLAVAPLFHI-------TGAVINATIALMKDCTLV 247
Cdd:PLN02387 250 NDIAVIMYTSGSTGLPKGVMMTHGNIVAtVAGVMTVVPKLGKNDVYLAYLPLAHIlelaaesVMAAVGAAIGYGSPLTLT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 248 -FANRFA----ADVT-------------LDAFAEhEVTYTIG-----SITVFNALYNSPAAT------------------ 286
Cdd:PLN02387 330 dTSNKIKkgtkGDASalkptlmtavpaiLDRVRD-GVRKKVDakgglAKKLFDIAYKRRLAAiegswfgawglekllwda 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 287 -------AAHFASIKTLYSGGAPIPPAAvEKFENK-FGHYIHNAYGMTETSSGVIAVPPDrrapvDPASGalSIGMALPQ 358
Cdd:PLN02387 409 lvfkkirAVLGGRIRFMLSGGAPLSGDT-QRFINIcLGAPIGQGYGLTETCAGATFSEWD-----DTSVG--RVGPPLPC 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 359 VEIRVVDFD-------GTPLPdgtQGELEIAGPQVVSGYWQKPEATAKTFP-DGR-LR---TGDVAIRDADGWIYLVDRL 426
Cdd:PLN02387 481 CYVKLVSWEeggylisDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKvDERgMRwfyTGDIGQFHPDGCLEIIDRK 557
|
490 500
....*....|....*....|....*..
gi 2089408387 427 KDQINVS-GYKVWPREVEDALVAHPAV 452
Cdd:PLN02387 558 KDIVKLQhGEYVSLGKVEAALSVSPYV 584
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
183-524 |
8.01e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 86.72 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 183 YTSGTTGPPKGALNSH-ANILAVATTFAELARVDDGDVVLAVAPL----FHitGAVINatiALMKDCTLVFanrFAADVT 257
Cdd:PTZ00237 261 YTSGTTGNSKAVVRSNgPHLVGLKYYWRSIIEKDIPTVVFSHSSIgwvsFH--GFLYG---SLSLGNTFVM---FEGGII 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 258 LDAFAE---------HEVTYTIGSITVFNALY-NSPAATAAH----FASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAY 323
Cdd:PTZ00237 333 KNKHIEddlwntiekHKVTHTLTLPKTIRYLIkTDPEATIIRskydLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 324 GMTET------SSGVIAVPPDrrapvdpASGalsigmaLPQVEIRVVDF--DGTPLPDGTQGELEIA---GPQVVSGYWQ 392
Cdd:PTZ00237 413 GQTEIgitylyCYGHINIPYN-------ATG-------VPSIFIKPSILseDGKELNVNEIGEVAFKlpmPPSFATTFYK 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 393 KPEATAKTFPD--GRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVG--QPDDYQgeS 468
Cdd:PTZ00237 479 NDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGiyDPDCYN--V 556
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2089408387 469 VVAFVSLVRDAEVT-------EQELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PTZ00237 557 PIGLLVLKQDQSNQsidlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
167-524 |
2.81e-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: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 167 TPEAAEVS--PTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKdc 244
Cdd:PRK08043 354 MPRLAQVKqqPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLT-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 245 tlvfanrfAADVTLDAFAEH-----EVTYTIGSITVF-NALYNSPAATAAH---FASIKTLYSGGAPIPPAAVEKFENKF 315
Cdd:PRK08043 432 --------GAEVFLYPSPLHyrivpELVYDRNCTVLFgTSTFLGNYARFANpydFARLRYVVAGAEKLQESTKQLWQDKF 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 316 GHYIHNAYGMTETSSGV-IAVPPdrrapvdpASGALSIGMALPQVEIRVVdfdgtPLPDGTQG-ELEIAGPQVVSGYW-- 391
Cdd:PRK08043 504 GLRILEGYGVTECAPVVsINVPM--------AAKPGTVGRILPGMDARLL-----SVPGIEQGgRLQLKGPNIMNGYLrv 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 392 QKP---EATAKTFPDGRLR-----TGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVED-ALVAHPAVGEAGVVgQPD 462
Cdd:PRK08043 571 EKPgvlEVPTAENARGEMErgwydTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSD 649
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 463 DYQGESVVAFVSlvrDAEVTEqelrafvgDRLAAYKR---------PKHIHIVDELPKTQTGKIRRTELRN 524
Cdd:PRK08043 650 ASKGEALVLFTT---DSELTR--------EKLQQYARehgvpelavPRDIRYLKQLPLLGSGKPDFVTLKS 709
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
3-412 |
4.66e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 81.25 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 3 TLVDVWKARVAANPEHPAIAYFDGI------LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLG 76
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 77 AAALVLNPMYR-----KAELRHLVDDAgAVGIICADTAV--AENAETMQDSTVRWIVGTSDldfqtrndprvfGDRIRER 149
Cdd:PRK12582 130 VPAAPVSPAYSlmshdHAKLKHLFDLV-KPRVVFAQSGApfARALAALDLLDVTVVHVTGP------------GEGIASI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 150 HdgADDLVelverfrgATPEAAEV-------SPTDTAILAYTSGTTGPPKGALNSH----ANILAVATTFAElARVDDGD 218
Cdd:PRK12582 197 A--FADLA--------ATPPTAAVaaaiaaiTPDTVAKYLFTSGSTGMPKAVINTQrmmcANIAMQEQLRPR-EPDPPPP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 219 VVLAVAPLFHITGAVINATIALMKDCTLVfanrfaadvtLDA-------FAE-----HEVTYT------IGSITVFNALY 280
Cdd:PRK12582 266 VSLDWMPWNHTMGGNANFNGLLWGGGTLY----------IDDgkplpgmFEEtirnlREISPTvygnvpAGYAMLAEAME 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 281 NSPAATAAHFASIKTLYSGGAPIPPAAVEKFE----NKFGHYI--HNAYGMTETSSGVIAV--PPDRRApvdpasgalSI 352
Cdd:PRK12582 336 KDDALRRSFFKNLRLMAYGGATLSDDLYERMQalavRTTGHRIpfYTGYGATETAPTTTGThwDTERVG---------LI 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 353 GMALPQVEIRVVdfdgtplPDGTQGELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVA 412
Cdd:PRK12582 407 GLPLPGVELKLA-------PVGDKYEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAA 460
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
31-433 |
4.68e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 81.22 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALwklGAAALVLNPMYRKAelrhlvdDAGAVGIICADTAV 110
Cdd:PLN02614 83 QEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEAC---NAHGLYCVPLYDTL-------GAGAVEFIISHSEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 111 A----------ENAETMQDST--VRWIVGTSDLDFQTRNDPRVFGDRIRerhdGADDLVELVErfrGATPEAAEVSPTDT 178
Cdd:PLN02614 153 SivfveekkisELFKTCPNSTeyMKTVVSFGGVSREQKEEAETFGLVIY----AWDEFLKLGE---GKQYDLPIKKKSDI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 179 AILAYTSGTTGPPKGALNSHANILAVATTFAEL-----ARVDDGDVVLAVAPLFHITGAVINATIA-------------- 239
Cdd:PLN02614 226 CTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLlksanAALTVKDVYLSYLPLAHIFDRVIEECFIqhgaaigfwrgdvk 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 240 -LMKDCTLVFANRF-AADVTLD-------------AFAEHEV-----TYTIGSITVFNA-LYNSPAATAAHFASIKT--- 295
Cdd:PLN02614 306 lLIEDLGELKPTIFcAVPRVLDrvysglqkklsdgGFLKKFVfdsafSYKFGNMKKGQShVEASPLCDKLVFNKVKQglg 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 296 -----LYSGGAPIPpAAVEKFENKFGH-YIHNAYGMTETSSGVIAVPPDRRAPVDpasgalSIGMALPQVEIR---VVDF 366
Cdd:PLN02614 386 gnvriILSGAAPLA-SHVESFLRVVACcHVLQGYGLTESCAGTFVSLPDELDMLG------TVGPPVPNVDIRlesVPEM 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2089408387 367 DGTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVS 433
Cdd:PLN02614 459 EYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLS 525
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
38-517 |
5.57e-16 |
|
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: 80.78 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 38 DAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPmyrkaelrhlvdDAGAVG-----------IICA 106
Cdd:cd05943 109 ARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSP------------DFGVPGvldrfgqiepkVLFA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 107 DTAVAENAETM-QDSTVRWIV-GTSDLDfQTRNDPRVFGDrirERHDGAD-----DLVELVERFRGATPEAAEVSPTDTA 179
Cdd:cd05943 177 VDAYTYNGKRHdVREKVAELVkGLPSLL-AVVVVPYTVAA---GQPDLSKiakalTLEDFLATGAAGELEFEPLPFDHPL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 180 ILAYTSGTTGPPKGALNSHANILAVAttFAELARVDD---GDVVLAVAPL------FHITGAVINATIALMKDCTLvfan 250
Cdd:cd05943 253 YILYSSGTTGLPKCIVHGAGGTLLQH--LKEHILHCDlrpGDRLFYYTTCgwmmwnWLVSGLAVGATIVLYDGSPF---- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 RFAADVTLDAFAEHEVTYTIGSITVFNAL---YNSPAATaaH-FASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAY--G 324
Cdd:cd05943 327 YPDTNALWDLADEEGITVFGTSAKYLDALekaGLKPAET--HdLSSLRTILSTGSPLKPESFDYVYDHIKPDVLLASisG 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 325 MTETSSGVIAVPPDrrAPVDPasGALS---IGMAlpqveIRVVDFDGTPLPdGTQGELEIAG--PQVVSGYWQKPEATA- 398
Cdd:cd05943 405 GTDIISCFVGGNPL--LPVYR--GEIQcrgLGMA-----VEAFDEEGKPVW-GEKGELVCTKpfPSMPVGFWNDPDGSRy 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 399 -----KTFPdGRLRTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDDYQGESVVAFV 473
Cdd:cd05943 475 raayfAKYP-GVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFV 553
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2089408387 474 SLVRDAEVTEqELRAFVGDRLAAYKRPKH----IHIVDELPKTQTGKI 517
Cdd:cd05943 554 KLREGVELDD-ELRKRIRSTIRSALSPRHvpakIIAVPDIPRTLSGKK 600
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
21-499 |
7.42e-16 |
|
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: 80.58 E-value: 7.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 21 IAYFDGILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAG- 99
Cdd:cd17632 62 LPRFETITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEp 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 100 ---AVGIICADTAVAENAETMQDSTVRWIVGTSDLDFQTRNDprvfgDRIRERHDGADDLVELVE----RFRGATPEAAE 172
Cdd:cd17632 142 rllAVSAEHLDLAVEAVLEGGTPPRLVVFDHRPEVDAHRAAL-----ESARERLAAVGIPVTTLTliavRGRDLPPAPLF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 173 VSPTDT---AILAYTSGTTGPPKGALNSHANILAVATTF-AELARVDDGDVVLAVAPLFHITG-AVINATiaLMKDCTLV 247
Cdd:cd17632 217 RPEPDDdplALLIYTSGSTGTPKGAMYTERLVATFWLKVsSIQDIRPPASITLNFMPMSHIAGrISLYGT--LARGGTAY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 248 FANRFAADVTLDAFAEHEVTYTIGSITVFNALYN-------------SPAATAAHFAS-----------IKTLYSGGAPI 303
Cdd:cd17632 295 FAAASDMSTLFDDLALVRPTELFLVPRVCDMLFQryqaeldrrsvagADAETLAERVKaelrervlggrLLAAVCGSAPL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 304 PPAAVEKFENKFGHYIHNAYGMTETSS----GVIAVPP--DRRApVDpasgalsigmaLPQVEIRVVDfdgTPLPdgtQG 377
Cdd:cd17632 375 SAEMKAFMESLLDLDLHDGYGSTEAGAvildGVIVRPPvlDYKL-VD-----------VPELGYFRTD---RPHP---RG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 378 ELEIAGPQVVSGYWQKPEATAKTF-PDGRLRTGDVAIRDADGWIYLVDRLKDQINVS-GYKVWPREVEDALVAHPAVGEA 455
Cdd:cd17632 437 ELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSqGEFVTVARLEAVFAASPLVRQI 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2089408387 456 GVVGQPDDYQGESVVAFVSLVRDAEvTEQELRAFVGDRLAAYKR 499
Cdd:cd17632 517 FVYGNSERAYLLAVVVPTQDALAGE-DTARLRAALAESLQRIAR 559
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
138-417 |
1.18e-14 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 76.84 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 138 DPRVFGDRIRERHDGADDLVELVERFRGATPEAA--EVSPTDTAILAYTSGTTGPPKGALNSH----ANILAVATTFAEL 211
Cdd:PRK08180 169 DVEVVAVRGAVPGRAATPFAALLATPPTAAVDAAhaAVGPDTIAKFLFTSGSTGLPKAVINTHrmlcANQQMLAQTFPFL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 212 ArvDDGDVVLAVAPLFHITGAVINATIALMKDCTLVF------ANRFAAdvTLDAFaeHEVTYTIgsitVFN-------- 277
Cdd:PRK08180 249 A--EEPPVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkptPGGFDE--TLRNL--REISPTV----YFNvpkgweml 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 278 --ALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKF----ENKFGHYIH--NAYGMTETSSGVIAVPPdrrapvdPASGA 349
Cdd:PRK08180 319 vpALERDAALRRRFFSRLKLLFYAGAALSQDVWDRLdrvaEATCGERIRmmTGLGMTETAPSATFTTG-------PLSRA 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2089408387 350 LSIGMALPQVEIRVVdfdgtplPDGTQGELEIAGPQVVSGYWQKPEATAKTFPD-GRLRTGDvAIRDAD 417
Cdd:PRK08180 392 GNIGLPAPGCEVKLV-------PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEeGYYRSGD-AVRFVD 452
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
165-523 |
1.23e-14 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 76.70 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 165 GATPEAAEVSPTDTAILAYTSGTTGPPKGALNSH----ANILAVATTFAELARVDDGDVVLavaPLFHITG-------AV 233
Cdd:PRK12476 182 GESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHravgTNLVQMILSIDLLDRNTHGVSWL---PLYHDMGlsmigfpAV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 234 INATIALMKDCTLVF-ANRFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFE 312
Cdd:PRK12476 259 YGGHSTLMSPTAFVRrPQRWIKALSEGSRTGRVVTAAPNFAYEWAAQRGLPAEGDDIDLSNVVLIIGSEPVSIDAVTTFN 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 313 NKFGHY------IHNAYGMTETSSGVIAVPPD----------------RRAPVDP----ASGALSIGMALPQVEIRVVDF 366
Cdd:PRK12476 339 KAFAPYglprtaFKPSYGIAEATLFVATIAPDaepsvvyldreqlgagRAVRVAAdapnAVAHVSCGQVARSQWAVIVDP 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 367 D-GTPLPDGTQGELEIAGPQVVSGYWQKPEATAKTF------------------PDGR-LRTGDVAIRdADGWIYLVDRL 426
Cdd:PRK12476 419 DtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTwLRTGDLGVY-LDGELYITGRI 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 427 KDQINVSGYKVWPREVE-DALVAHPAV--GEAGVVGQPDDYQGESVV----AFVSLVRDAEVTEQELRAFVGDRLAAykR 499
Cdd:PRK12476 498 ADLIVIDGRNHYPQDIEaTVAEASPMVrrGYVTAFTVPAEDNERLVIvaerAAGTSRADPAPAIDAIRAAVSRRHGL--A 575
|
410 420
....*....|....*....|....*.
gi 2089408387 500 PKHIHIVDE--LPKTQTGKIRRTELR 523
Cdd:PRK12476 576 VADVRLVPAgaIPRTTSGKLARRACR 601
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
158-522 |
3.44e-14 |
|
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: 74.82 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 158 ELVERFRGATPEAAEVSPTDTAILAY---TSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLaVAPLFHITGAVI 234
Cdd:cd17654 97 ELDNAPLSFTPEHRHFNIRTDECLAYvihTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILF-LTSPLTFDPSVV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 235 NATIALMKDCTLVFA-------NRFAADVTldaFAEHEVTYTIGSITVFNALynsPAATAAHF-----ASIKTLYSGGAP 302
Cdd:cd17654 176 EIFLSLSSGATLLIVptsvkvlPSKLADIL---FKRHRITVLQATPTLFRRF---GSQSIKSTvlsatSSLRVLALGGEP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 303 IPPAAVEKFENKFGHYIH--NAYGMTETSSGVIAVP-PDRRAPVdpasgalSIGMALPQVEIRVVDFDGTPlpdgTQGEL 379
Cdd:cd17654 250 FPSLVILSSWRGKGNRTRifNIYGITEVSCWALAYKvPEEDSPV-------QLGSPLLGTVIEVRDQNGSE----GTGQV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 380 EIAGPQVVsGYWQKPEatakTFPDGRLR-TGDVaIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVgEAGVV 458
Cdd:cd17654 319 FLGGLNRV-CILDDEV----TVPKGTMRaTGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAV 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2089408387 459 GQPDDyqgESVVAF-VSLVRDAEVtEQELRAFVgdrLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17654 392 TLSDQ---QRLIAFiVGESSSSRI-HKELQLTL---LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
165-524 |
1.97e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 72.49 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 165 GATPEAAEVSPTDT---AILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDG-DVVLAVAPLFH-------ITGAV 233
Cdd:PRK05851 138 AHTNRSASLTPPDSggpAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHdmglaflLTAAL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 234 INATIALMKdcTLVFAnrfAADVT-LDAFAEHEVTYTIGSitvfNALYN-----SPAATAAHFASIKTLYSGGAPIPPAA 307
Cdd:PRK05851 218 AGAPLWLAP--TTAFS---ASPFRwLSWLSDSRATLTAAP----NFAYNligkyARRVSDVDLGALRVALNGGEPVDCDG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 308 VEKFENKFGHYIHNA------YGMTETSSGVIAVPPDRRAPVD----PASGALS----IGMALPQVEIRVVDFDGTPLPD 373
Cdd:PRK05851 289 FERFATAMAPFGFDAgaaapsYGLAESTCAVTVPVPGIGLRVDevttDDGSGARrhavLGNPIPGMEVRISPGDGAAGVA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 374 GTQ-GELEIAGPQVVSGYW-QKPEAtaktfPDGRLRTGDVAIRDADGWIyLVDRLKDQINVSGYKVWPREVEDALVAHPA 451
Cdd:PRK05851 369 GREiGEIEIRGASMMSGYLgQAPID-----PDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRG 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 452 VGEAGVVGQPDDYQGesvvAFVSLVRDAEVT---EQELRAFVGDRLAA----------YKRPkhihivDELPKTQTGKIR 518
Cdd:PRK05851 443 VREGAVVAVGTGEGS----ARPGLVIAAEFRgpdEAGARSEVVQRVASecgvvpsdvvFVAP------GSLPRTSSGKLR 512
|
....*.
gi 2089408387 519 RTELRN 524
Cdd:PRK05851 513 RLAVKR 518
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
28-459 |
2.31e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 72.57 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 28 LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALwklGAAALVLNPMYRKAelrhlvdDAGAVGIIC-- 105
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC---NSQGITYVPLYDTL-------GANAVEFIInh 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 106 ADTAVAenaeTMQDSTVRWIVG-----TSDLDFQTRndprvFGDRIRERHDGADDL-VELV--ERFRGATPEAAEVSP-- 175
Cdd:PLN02861 148 AEVSIA----FVQESKISSILSclpkcSSNLKTIVS-----FGDVSSEQKEEAEELgVSCFswEEFSLMGSLDCELPPkq 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 176 -TDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDD-----GDVVLAVAPLFHITGAVINaTIALMKDCTLVFa 249
Cdd:PLN02861 219 kTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDrvateEDSYFSYLPLAHVYDQVIE-TYCISKGASIGF- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 250 nrFAADVT--LDAFAEHEVTYTIGSITVFNALYNS-------------------------------PAATAAHF------ 290
Cdd:PLN02861 297 --WQGDIRylMEDVQALKPTIFCGVPRVYDRIYTGimqkissggmlrkklfdfaynyklgnlrkglKQEEASPRldrlvf 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 291 --------ASIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGVIAvppdRRAPVDPASGalSIGMALPQVEIR 362
Cdd:PLN02861 375 dkikeglgGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFT----SIANVFSMVG--TVGVPMTTIEAR 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 363 VVD-----FDGtpLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRLRTGDVAIRDADGWIYLVDRLKDQINVS-GYK 436
Cdd:PLN02861 449 LESvpemgYDA--LSDVPRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEY 526
|
490 500
....*....|....*....|...
gi 2089408387 437 VWPREVEDALVAHPAVGEAGVVG 459
Cdd:PLN02861 527 VAVENLENTYSRCPLIASIWVYG 549
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
172-470 |
1.19e-11 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 67.15 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 172 EVSPTDTAILAYTSGTTGPPKGALNSHANILAVATTFAELARVDDGDVVLAVAPLFHITGAVINATIALMKDCTLVFA-N 250
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAyN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 251 RFAADVTLDAFAEHEVTYTIGSITVFNALYNSPAATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHY-IHNAYGMTETS 329
Cdd:PRK06334 259 PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIqLRQGYGTTECS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 330 SgVIAVpPDRRAPVDPAsgalSIGMALPQVEIRVVDFDG-TPLPDGTQGELEIAGPQVVSGYWQKPEATAKTFPDGRL-- 406
Cdd:PRK06334 339 P-VITI-NTVNSPKHES----CVGMPIRGMDVLIVSEETkVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGETwy 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2089408387 407 RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHpavgeagvVGQPDDYQGESVV 470
Cdd:PRK06334 413 VTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNAADHAGPLV 468
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
24-523 |
6.09e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 65.12 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 24 FDG-ILSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLvddaGAVG 102
Cdd:PRK07868 468 FDGrVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPDTDLAAAVRL----GGVT 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 103 IICADtavAENAETMQDSTVRWIV--GTSDLDFQTRNDPRVFGdriRERHDgaDDLVELVERFRgATPEAAEvsptDTAI 180
Cdd:PRK07868 544 EIITD---PTNLEAARQLPGRVLVlgGGESRDLDLPDDADVID---MEKID--PDAVELPGWYR-PNPGLAR----DLAF 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 181 LAY-TSGTTGPPKGALNSHANILAVATtfAELARVDDGDVVLAVAPLFH-------ITGAVINAT-IALMKDctlVFANR 251
Cdd:PRK07868 611 IAFsTAGGELVAKQITNYRWALSAFGT--ASAAALDRRDTVYCLTPLHHesgllvsLGGAVVGGSrIALSRG---LDPDR 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 252 FAADVTldAFAEHEVTYTIgsiTVFNALYNSPAATAAHFASIKTLYSGGAP----------IPPAAVEKFenkfghyihn 321
Cdd:PRK07868 686 FVQEVR--QYGVTVVSYTW---AMLREVVDDPAFVLHGNHPVRLFIGSGMPtglwervveaFAPAHVVEF---------- 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 322 aYGMTEtSSGVIAvppdrrapvdPASGAL--SIGMALP---QVEIRVVDFDGTPLPDGTQGELEIAGPQVV------SGY 390
Cdd:PRK07868 751 -FATTD-GQAVLA----------NVSGAKigSKGRPLPgagRVELAAYDPEHDLILEDDRGFVRRAEVNEVgvllarARG 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 391 WQKPEATAKTfpdGRLRTGDVAI-------RDADGWIYLVDRLKDQINVSGYKVWPREVEDALVAHPAVGEAGVVGQPDD 463
Cdd:PRK07868 819 PIDPTASVKR---GVFAPADTWIsteylfrRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVG 895
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 464 YQgESVVAFVSLVRDAEVTEQELRAFVGDrLAAYKRPKHIHIVDELPKTQTGKIRRTELR 523
Cdd:PRK07868 896 GR-QLAVAAVTLRPGAAITAADLTEALAS-LPVGLGPDIVHVVPEIPLSATYRPTVSALR 953
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
14-517 |
5.79e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 61.73 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 14 ANPEHPAIAYF--DGI---LSAREVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPmyrk 88
Cdd:PRK03584 96 RRDDRPAIIFRgeDGPrreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSP---- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 89 aelrhlvdDAGAVGI------------ICAD------------TAVAENAETMqdSTVRWIVGTsdldfqtrndPRVFGD 144
Cdd:PRK03584 172 --------DFGVQGVldrfgqiepkvlIAVDgyryggkafdrrAKVAELRAAL--PSLEHVVVV----------PYLGPA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 145 RIRERHDGADDLVELVERFRGATPEAAEVsPTD--TAILaYTSGTTGPPKGALNSHANILAVAttFAELA---RVDDGDV 219
Cdd:PRK03584 232 AAAAALPGALLWEDFLAPAEAAELEFEPV-PFDhpLWIL-YSSGTTGLPKCIVHGHGGILLEH--LKELGlhcDLGPGDR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 220 VLavapLFHITGAVI-NATI-ALMKDCTLVF--ANRFAADV-TLDAFAEHEvtytigSITVFNAlynSPA---------- 284
Cdd:PRK03584 308 FF----WYTTCGWMMwNWLVsGLLVGATLVLydGSPFYPDPnVLWDLAAEE------GVTVFGT---SAKyldacekagl 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 285 --ATAAHFASIKTLYSGGAPIPPAAVEKFENKFGHYIH--NAYGMTETSSG-VIAVP--PDRRapvdpasGALS---IGM 354
Cdd:PRK03584 375 vpGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKADVWlaSISGGTDICSCfVGGNPllPVYR-------GEIQcrgLGM 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 355 AlpqveIRVVDFDGTPLpDGTQGELEI--AGPQVVSGYWQKP------EATAKTFPdGRLRTGDVAIRDADGWIYLVDRL 426
Cdd:PRK03584 448 A-----VEAWDEDGRPV-VGEVGELVCtkPFPSMPLGFWNDPdgsryrDAYFDTFP-GVWRHGDWIEITEHGGVVIYGRS 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 427 KDQINVSG--------YkvwpREVEdalvAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTEqELRAFVGDRLAAYK 498
Cdd:PRK03584 521 DATLNRGGvrigtaeiY----RQVE----ALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDD-ALRARIRTTIRTNL 591
|
570 580
....*....|....*....|...
gi 2089408387 499 RPKH----IHIVDELPKTQTGKI 517
Cdd:PRK03584 592 SPRHvpdkIIAVPDIPRTLSGKK 614
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
31-522 |
1.74e-07 |
|
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: 54.30 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 31 REVDEMSDAFAVALVEKGVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVDDAGAVGIIcadtaV 110
Cdd:TIGR03443 274 KQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALI-----V 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 111 AENAETMQDSTVRWIvgTSDLDFQTR-------NDPRVFGDRIRErhdGADDLVELVERFRGaTPEAAEVSPTDTAILAY 183
Cdd:TIGR03443 349 IEKAGTLDQLVRDYI--DKELELRTEipalalqDDGSLVGGSLEG---GETDVLAPYQALKD-TPTGVVVGPDSNPTLSF 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 184 TSGTTGPPKGALNSHANiLA-----VATTFAeLARVDDGDVVLAVA----------PLF-----HITGAVINATIALMKD 243
Cdd:TIGR03443 423 TSGSEGIPKGVLGRHFS-LAyyfpwMAKRFG-LSENDKFTMLSGIAhdpiqrdmftPLFlgaqlLVPTADDIGTPGRLAE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 244 ctlvFANRFAADVTldafaeHeVTYTIGSITVFNALYNSPAATAAHFA----------SIKTLYsggapippaavekfEN 313
Cdd:TIGR03443 501 ----WMAKYGATVT------H-LTPAMGQLLSAQATTPIPSLHHAFFVgdiltkrdclRLQTLA--------------EN 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 314 KFghyIHNAYGMTETSSGV--IAVPPDRRAP--------VDPAsgalsiGMALPQVEIRVVD-FDGT-PLPDGTQGELEI 381
Cdd:TIGR03443 556 VC---IVNMYGTTETQRAVsyFEIPSRSSDStflknlkdVMPA------GKGMKNVQLLVVNrNDRTqTCGVGEVGEIYV 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 382 AGPQVVSGYWQKPEATAKTF----------------------------PDGRL-RTGDVAIRDADGWIYLVDRLKDQINV 432
Cdd:TIGR03443 627 RAGGLAEGYLGLPELNAEKFvnnwfvdpshwidldkennkperefwlgPRDRLyRTGDLGRYLPDGNVECCGRADDQVKI 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 433 SGYKVWPREVEDALVAHPAVGE----------------AGVVGQPDdyqGESVVAFVSLVRDAEVTEQ------------ 484
Cdd:TIGR03443 707 RGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeeptlvSYIVPQDK---SDELEEFKSEVDDEESSDPvvkglikyrkli 783
|
570 580 590
....*....|....*....|....*....|....*....
gi 2089408387 485 -ELRAFVGDRLAAYKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:TIGR03443 784 kDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
184-521 |
2.07e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 53.23 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 184 TSGTTGPPKGALNSHANILAVATTFA---ELARVDDGDVVLaVAPLFHITGAVINATIALMK-DCTLVFANRFAADVTLD 259
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELFArslRAAGVRPGDRVQ-NAFGYGLFTGGLGLHYGAERlGATVIPAGGGNTERQLR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 260 AFAEHEVTYTIGS-------ITVFNALYNSPAATaahfaSIKTLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSSGV 332
Cdd:COG1541 170 LMQDFGPTVLVGTpsyllylAEVAEEEGIDPRDL-----SLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVGPGV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 333 IAVPPDRRapvdpasgalsiGMALPQ----VEIrvVDFD-GTPLPDGTQGELeiagpqVVSgywqkpeatakTF-PDG-- 404
Cdd:COG1541 245 AYECEAQD------------GLHIWEdhflVEI--IDPEtGEPVPEGEEGEL------VVT-----------TLtKEAmp 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 405 --RLRTGDVA--IRDA----------DGWIylvDRLKDQINVSGYKVWPREVEDALVAHPAVGeagvvgqpDDYQ----- 465
Cdd:COG1541 294 liRYRTGDLTrlLPEPcpcgrthpriGRIL---GRADDMLIIRGVNVFPSQIEEVLLRIPEVG--------PEYQivvdr 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2089408387 466 -GESVVAFVSLVRDAEVTEQELRAFVGDRLAAYK--RPKhIHIV--DELPKTqTGKIRRTE 521
Cdd:COG1541 363 eGGLDELTVRVELAPGASLEALAEAIAAALKAVLglRAE-VELVepGSLPRS-EGKAKRVI 421
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
175-433 |
1.10e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 51.26 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 175 PTDTAILAYTSGTTGPPKGALNSHANIlavattFAELARVDDGDVV--------LAVAPLFHITGAVInATIALMKDCTL 246
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNL------YNTVVPLCKHSIFkkynpkthLSYLPISHIYERVI-AYLSFMLGGTI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 247 VF----ANRFAADVTldafaEHEVTYTIGSITVFNALYNSPAATAAHFASIK---------------------------- 294
Cdd:PTZ00342 376 NIwskdINYFSKDIY-----NSKGNILAGVPKVFNRIYTNIMTEINNLPPLKrflvkkilslrksnnnggfskflegith 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 295 --------------TLYSGGAPIPPAAVEKFENKFGHYIHNAYGMTETSsGVIAVPPDRRAPVDPASGALSigmalPQVE 360
Cdd:PTZ00342 451 isskikdkvnpnleVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETT-GPIFVQHADDNNTESIGGPIS-----PNTK 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 361 IRVVDF------DGTPlpdgtQGELEIAGPQVVSGYWQKPEATAKTFP-DGRLRTGDVAIRDADGWIYLVDRLKDQINVS 433
Cdd:PTZ00342 525 YKVRTWetykatDTLP-----KGELLIKSDSIFSGYFLEKEQTKNAFTeDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
439-523 |
1.55e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 47.07 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 439 PREVEDA------LVAHPAVGEAGVVGQPDDYQGESVVAFVSlvRDAEVTEQELRAfvgdRLAAYKRPK---HIHIVDEL 509
Cdd:PRK09188 236 DRIDNEApaiqaaLKSDPAVSDVAIALFSLPAKGVGLYAFVE--AELPADEKSLRA----RLAGAKPPKppeHIQPVAAL 309
|
90
....*....|....
gi 2089408387 510 PKTQTGKIRRTELR 523
Cdd:PRK09188 310 PRDADGTVRDDILR 323
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
319-522 |
8.55e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 45.20 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 319 IHNAYGMTETSSGV--IAVPPDRRAP--VDPASGALSIGMALPQVEIRVVD-FDGTPLPD-GTQGELEIAGPQVVSGYWQ 392
Cdd:cd17647 252 IVNMYGTTETQRAVsyFEVPSRSSDPtfLKNLKDVMPAGRGMLNVQLLVVNrNDRTQICGiGEVGEIYVRAGGLAEGYRG 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 393 KPEATAKTF----------------------------PDGRL-RTGDVAIRDADGWIYLVDRLKDQINVSGYKVWPREVE 443
Cdd:cd17647 332 LPELNKEKFvnnwfvepdhwnyldkdnnepwrqfwlgPRDRLyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEID 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 444 DALVAHPAVGEAGVVGQPDDYQGESVVAFVSLVRDAEVTE---------------------------QELRAFVGDRLAA 496
Cdd:cd17647 412 THISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDEsfaqedvpkevstdpivkgligyrkliKDIREFLKKRLAS 491
|
250 260
....*....|....*....|....*.
gi 2089408387 497 YKRPKHIHIVDELPKTQTGKIRRTEL 522
Cdd:cd17647 492 YAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
40-523 |
3.14e-04 |
|
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: 43.49 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 40 FAVALVEK-GVGHGDRVGIHLQNIPQYAIAFLALWKLGAAALVLNPMYRKAELRHLVD----------DAGAVGIICADT 108
Cdd:cd05905 27 IAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGtckvrvaltvEACLKGLPKKLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 109 AVAENAETMQDSTVRWIVGTSDLDFQTRNDPRVFGDRIRerhdgaddlvelverfrgatpeaaeVSPTDTAILAYTSGTT 188
Cdd:cd05905 107 KSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPP-------------------------TRDGDTAYIEYSFSSD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 189 GPPKGALNSHANILAVATTFAELARVDDGDVVLAVAP------LFH------ITGA-VINATIALMKDCTLVFanrfaad 255
Cdd:cd05905 162 GSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDfksglgLWHgcllsvYSGHhTILIPPELMKTNPLLW------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 256 vtLDAFAEHEVTYTIGSITVFNALYNSPAATAAH-------FASIKTLY-SGGAPIPPAAVEKFENKFG-HYIHNAYGMT 326
Cdd:cd05905 235 --LQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASlknrdvnLSSLRMCMvPCENRPRISSCDSFLKLFQtLGLSPRAVST 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 327 ETSSGVIAVPPDRRAP--------VDPAS--------------GALSI---GMALPQVEIRVVDFDGTPL-PDGTQGELE 380
Cdd:cd05905 313 EFGTRVNPFICWQGTSgpepsrvyLDMRAlrhgvvrlderdkpNSLPLqdsGKVLPGAQVAIVNPETKGLcKDGEIGEIW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 381 IAGPQVVSGYWQKP---EATAKTFPDGRL----------RTGD----------VAIRDADGWIYLVDRLKDQINVSGYKV 437
Cdd:cd05905 393 VNSPANASGYFLLDgetNDTFKVFPSTRLstgitnnsyaRTGLlgflrptkctDLNVEEHDLLFVVGSIDETLEVRGLRH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 438 WPREVED-ALVAHPAVGEAGVVgqpdDYQGESVVafvsLVRDAEVTEQELRAFVGDRLAAYKRPKHIhIVD--------E 508
Cdd:cd05905 473 HPSDIEAtVMRVHPYRGRCAVF----SITGLVVV----VAEQPPGSEEEALDLVPLVLNAILEEHQV-IVDcvalvppgS 543
|
570
....*....|....*
gi 2089408387 509 LPKTQTGKIRRTELR 523
Cdd:cd05905 544 LPKNPLGEKQRMEIR 558
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
363-530 |
1.26e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 41.60 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 363 VVDFDGTPLPDGTQGELEIA-GPQVVSG------------YWQ-KPEATAKTFpdgRlRTGDVAIRDADGWIYLVDRLKD 428
Cdd:PLN03052 538 ILDDSGNPYPDDAPCTGELAlFPLMFGAsstllnadhykvYFKgMPVFNGKIL---R-RHGDIFERTSGGYYRAHGRADD 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2089408387 429 QINVSGYKVWPREVE---DAlvAHPAVGEAGVVGQPDDYQG-ESVVAFVSL--VRDAEVTEQELRAF----VGDRLAAYK 498
Cdd:PLN03052 614 TMNLGGIKVSSVEIErvcNA--ADESVLETAAIGVPPPGGGpEQLVIAAVLkdPPGSNPDLNELKKIfnsaIQKKLNPLF 691
|
170 180 190
....*....|....*....|....*....|..
gi 2089408387 499 RPKHIHIVDELPKTQTGKIRRTELRNTEAKVT 530
Cdd:PLN03052 692 KVSAVVIVPSFPRTASNKVMRRVLRQQLAQEL 723
|
|
| |
