|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
14-560 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 957.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 14 KLQKSIGQYVARGTAELHYLRKIIESGAIGLEPPLNYAALAADIRKWGEVGMLPSHNARRAPNRAAVIDEEGTLTFSELD 93
Cdd:PRK07788 2 KLMKSVSGYLTRGSAEAHYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFAGLVAHAARRAPDRAALIDERGTLTYAELD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 94 EAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDDEYTKAVS 173
Cdd:PRK07788 82 EQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 174 LAQPPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTAPAPKASRRASIIILTSGTTGTPKGANRNTPPTLAPIGGILS 253
Cdd:PRK07788 162 ALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 254 HVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPD 333
Cdd:PRK07788 242 RVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 334 LSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGA 413
Cdd:PRK07788 322 TSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 414 VGRIFVGNAFPFEGYTGGGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAI 493
Cdd:PRK07788 402 VGRIFVGNGFPFEGYTDGRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVI 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 801237227 494 GVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK07788 482 GVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
39-558 |
0e+00 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 543.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 39 SGAIGLEPPLNYAALAADIRKWGevgMLPSHN----ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGV 114
Cdd:PRK13382 20 AGLIAPMRPDRYLRIVAAMRREG---MGPTSGfaiaAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 115 AILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDDEYTKAVSlaqpplgklRALGVNPD---- 190
Cdd:PRK13382 97 GIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVD---------RALADCPQatri 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 191 DDKPSGSSDETLAELIAHSSTAPAPKASRRASIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMF 270
Cdd:PRK13382 168 VAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 271 HALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAE 350
Cdd:PRK13382 248 HAWGFSQLVLAASLACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 351 LATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG 430
Cdd:PRK13382 328 VVIAFMDQFGDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 431 GGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVK 510
Cdd:PRK13382 408 GSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 801237227 511 KPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK13382 488 KPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
63-560 |
1.26e-148 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 435.01 E-value: 1.26e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 63 VGMLPSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLN 142
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 143 SEFSGPQIKEVSDREGAKVIIyddeytkavslaqpplgklralgvnpdddkpsgssdetlaeliahsstapapkasrrAS 222
Cdd:COG0318 81 PRLTAEELAYILEDSGARALV---------------------------------------------------------TA 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 223 IIILTSGTTGTPKGA---NRNTpptLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAAL-AMFLGSTLVLRRRFKPAL 298
Cdd:COG0318 104 LILYTSGTTGRPKGVmltHRNL---LANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLaPLLAGATLVLLPRFDPER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 299 VLEDIEKHKATSMVVVPVMLSRILDQLEKtePKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIA 378
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 379 GPKDLQFN-PSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG---GGGKQIIDGLLSSGDVGYFDERGL 454
Cdd:COG0318 259 NPEDPGERrPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNdpeATAEAFRDGWLRTGDLGRLDEDGY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 455 LYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKV 534
Cdd:COG0318 339 LYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKV 418
|
490 500
....*....|....*....|....*.
gi 801237227 535 PREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:COG0318 419 PRRVEFVDELPRTASGKIDRRALRER 444
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
34-557 |
1.31e-122 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 370.87 E-value: 1.31e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 34 RKIIESGAigLEPPLNYAALAAdIRKWGEVGMLP----SHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVR 109
Cdd:PRK13383 7 RALVRSGL--LNPPSPRAVLRL-LREASRGGTNPytllAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 110 AGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLralgvnp 189
Cdd:PRK13383 84 PGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVI------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 190 ddDKPSGSSDETLAEliahsstapaPKASRRASIIILTSGTTGTPKGANRnTPPTLAPIG---GILSHVPFKAGEVTLLP 266
Cdd:PRK13383 157 --DPATAGAEESGGR----------PAVAAPGRIVLLTSGTTGKPKGVPR-APQLRSAVGvwvTILDRTRLRTGSRISVA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 267 SPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQ 346
Cdd:PRK13383 224 MPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 347 LGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFE 426
Cdd:PRK13383 304 LDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 427 GYTGGGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRA 506
Cdd:PRK13383 384 RYTDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAA 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 801237227 507 FVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK13383 464 FVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
224-553 |
1.29e-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: 361.60 E-value: 1.29e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 IILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDI 303
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 304 EKHKATSMVVVPVMLSRILDQLEktEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVA-FATIAGPKD 382
Cdd:cd04433 85 EREKVTILLGVPTLLARLLKAPE--SAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgTVATGPPDD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 383 LQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ---IIDGLLSSGDVGYFDERGLLYVSG 459
Cdd:cd04433 163 DARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATaavDEDGWYRTGDLGRLDEDGYLYIVG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 460 RDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVI 539
Cdd:cd04433 243 RLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVV 322
|
330
....*....|....
gi 801237227 540 FLDELPRNPTGKVL 553
Cdd:cd04433 323 FVDALPRTASGKID 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
68-558 |
3.33e-114 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 349.10 E-value: 3.33e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 68 SHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSG 147
Cdd:PRK06187 13 RHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRA-LGVNPDDDKPSGSSDETLAELIA-HSSTAPAPKASRR-ASII 224
Cdd:PRK06187 93 EEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTvIVEGDGPAAPLAPEVGEYEELLAaASDTFDFPDIDENdAAAM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 225 ILTSGTTGTPKGA---NRNTpptLAPIGGILSHVPFKAGEVTLLPSPMFH--ALGYMHaaLAMFLGSTLVLRRRFKPALV 299
Cdd:PRK06187 173 LYTSGTTGHPKGVvlsHRNL---FLHSLAVCAWLKLSRDDVYLVIVPMFHvhAWGLPY--LALMAGAKQVIPRRFDPENL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVMLSRILDqlEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTE----VAFA 375
Cdd:PRK06187 248 LDLIETERVTFFFAVPTIWQMLLK--APRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTEtspvVSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 376 TIAgPKDLQFNP--STVGPVVKGVTVKILDENGNEVP--QGAVGRIFVGNAFPFEGYTGG---GGKQIIDGLLSSGDVGY 448
Cdd:PRK06187 326 PPE-DQLPGQWTkrRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRpeaTAETIDGGWLHTGDVGY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 449 FDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDH 528
Cdd:PRK06187 405 IDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGR 484
|
490 500 510
....*....|....*....|....*....|
gi 801237227 529 LARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK06187 485 LAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
67-554 |
6.67e-112 |
|
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: 340.36 E-value: 6.67e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 67 PSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFS 146
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 147 GPQIKEVSDREGAKVIIyDDEytkavslaqpplgklralgvnpdddkpsgssdetlaeliahsstapapkasrraSIIIL 226
Cdd:cd17631 81 PPEVAYILADSGAKVLF-DDL------------------------------------------------------ALLMY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 TSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGY-MHAALAMFLGSTLVLRRRFKPALVLEDIEK 305
Cdd:cd17631 106 TSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPETVLDLIER 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 306 HKATSMVVVPVMLSRILDQLEKTEPkpDLSSLKIVFVSGSQLGAELAtRALGDLGPVIYNMYGSTEVAF-ATIAGPKDLQ 384
Cdd:cd17631 186 HRVTSFFLVPTMIQALLQHPRFATT--DLSSLRAVIYGGAPMPERLL-RALQARGVKFVQGYGMTETSPgVTFLSPEDHR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 385 FNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY------TGgggKQIIDGLLSSGDVGYFDERGLLYVS 458
Cdd:cd17631 263 RKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYwnrpeaTA---AAFRDGWFHTGDLGRLDEDGYLYIV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 459 GRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREV 538
Cdd:cd17631 340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSV 419
|
490
....*....|....*.
gi 801237227 539 IFLDELPRNPTGKVLK 554
Cdd:cd17631 420 EFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
70-558 |
3.97e-110 |
|
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: 336.84 E-value: 3.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 70 NARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQ 149
Cdd:cd05936 8 AARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 150 IKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLralGVNPDDdkpsgssdetlaelIAHsstapapkasrrasiIILTSG 229
Cdd:cd05936 88 LEHILNDSGAKALIVAVSFTDLLAAGAPLGERV---ALTPED--------------VAV---------------LQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 230 TTGTPKGA---NRNTpptLAPIGGILSHVPF--KAGEVTLLPSPMFHALGYM-HAALAMFLGSTLVLRRRFKPALVLEDI 303
Cdd:cd05936 136 TTGVPKGAmltHRNL---VANALQIKAWLEDllEGDDVVLAALPLFHVFGLTvALLLPLALGATIVLIPRFRPIGVLKEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 304 EKHKATSMVVVPVMLSRILDQLEKTepKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDL 383
Cdd:cd05936 213 RKHRVTIFPGVPTMYIALLNAPEFK--KRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 384 QFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG---GGGKQIIDGLLSSGDVGYFDERGLLYVSGR 460
Cdd:cd05936 291 PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNrpeETAEAFVDGWLRTGDIGYMDEDGYFFIVDR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 461 DDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIF 540
Cdd:cd05936 371 KKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEF 450
|
490
....*....|....*...
gi 801237227 541 LDELPRNPTGKVLKRELR 558
Cdd:cd05936 451 RDELPKSAVGKILRRELR 468
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
71-559 |
2.27e-105 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 326.09 E-value: 2.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPD-DDKPSGSSDETLAELIA-HSSTAPAPK-ASRRASIIILT 227
Cdd:PRK07656 95 AYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETeEDDPHTEKMKTFTDFLAaGDPAERAPEvDPDDVADILFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 228 SGTTGTPKGA---NRNTPPTLAPIGGILShvpFKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVLRRRFKPALVLEDI 303
Cdd:PRK07656 175 SGTTGRPKGAmltHRQLLSNAADWAEYLG---LTEGDRYLAANPFFHVFGYKAGVNAPLMrGATILPLPVFDPDEVFRLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 304 EKHKATSMVVVPVMLSRILDQLEKTEpkPDLSSLKIVFVSGSQLGAELATRALGDLG-PVIYNMYGSTEVA-FATIAGP- 380
Cdd:PRK07656 252 ETERITVLPGPPTMYNSLLQHPDRSA--EDLSSLRLAVTGAASMPVALLERFESELGvDIVLTGYGLSEASgVTTFNRLd 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 381 KDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY------TGGGGKQiiDGLLSSGDVGYFDERGL 454
Cdd:PRK07656 330 DDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYyddpeaTAAAIDA--DGWLHTGDLGRLDEEGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 455 LYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKV 534
Cdd:PRK07656 408 LYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKV 487
|
490 500
....*....|....*....|....*
gi 801237227 535 PREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PRK07656 488 PRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
78-558 |
1.34e-103 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 321.26 E-value: 1.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 78 AAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDRE 157
Cdd:PRK12406 3 ATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 158 GAKVIIYDDEYTKAVSLAQP----------PLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTAPAPKASRRAsiIILT 227
Cdd:PRK12406 83 GARVLIAHADLLHGLASALPagvtvlsvptPPEIAAAYRISPALLTPPAGAIDWEGWLAQQEPYDGPPVPQPQS--MIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 228 SGTTGTPKGANRN--TPPTLAPIGGILSHV-PFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIE 304
Cdd:PRK12406 161 SGTTGHPKGVRRAapTPEQAAAAEQMRALIyGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPEELLQLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 305 KHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELaTRALGDL-GPVIYNMYGSTEVAFATIAGPKDL 383
Cdd:PRK12406 241 RHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADV-KRAMIEWwGPVIYEYYGSTESGAVTFATSEDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 384 QFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFV---GNA-FPFEGYTGGGGKQIIDGLLSSGDVGYFDERGLLYVSG 459
Cdd:PRK12406 320 LSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSriaGNPdFTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 460 RDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVI 539
Cdd:PRK12406 400 RKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIE 479
|
490
....*....|....*....
gi 801237227 540 FLDELPRNPTGKVLKRELR 558
Cdd:PRK12406 480 IMAELPREDSGKIFKRRLR 498
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
77-558 |
1.15e-98 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 308.37 E-value: 1.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 77 RAAVIDEEG-TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSD 155
Cdd:PRK08276 1 PAVIMAPSGeVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 156 REGAKVII----YDDEYTKAVSLAQPPLGKLRALGVNPDDDKPsgssdetLAELIAHSSTAPAPKASRRASIIiLTSGTT 231
Cdd:PRK08276 81 DSGAKVLIvsaaLADTAAELAAELPAGVPLLLVVAGPVPGFRS-------YEEALAAQPDTPIADETAGADML-YSSGTT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 232 GTPKGANRNTP------PTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEK 305
Cdd:PRK08276 153 GRPKGIKRPLPgldpdeAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEALALIER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 306 HKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQF 385
Cdd:PRK08276 233 YRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITSEDWLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 386 NPSTVGPVVKGVtVKILDENGNEVPQGAVGRIFV-GNAFPFEgYTGGGGK----QIIDGLLSSGDVGYFDERGLLYVSGR 460
Cdd:PRK08276 313 HPGSVGKAVLGE-VRILDEDGNELPPGEIGTVYFeMDGYPFE-YHNDPEKtaaaRNPHGWVTVGDVGYLDEDGYLYLTDR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 461 DDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDT---IKQYVRDHLARYKVPRE 537
Cdd:PRK08276 391 KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALaaeLIAWLRGRLAHYKCPRS 470
|
490 500
....*....|....*....|.
gi 801237227 538 VIFLDELPRNPTGKVLKRELR 558
Cdd:PRK08276 471 IDFEDELPRTPTGKLYKRRLR 491
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
48-560 |
3.49e-94 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 298.56 E-value: 3.49e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 48 LNYAALAADirkwgevgmlpsHNARRAPNRAAVI-----DEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHR 122
Cdd:COG0365 8 LNIAYNCLD------------RHAEGRGDKVALIwegedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 123 WFVIANYGAARVGARIILLNSEFSGpqiKEVSDR---EGAKVIIYDDEYT---KAVSL------AQPPLGKLRA-LGVNP 189
Cdd:COG0365 76 EAVIAMLACARIGAVHSPVFPGFGA---EALADRiedAEAKVLITADGGLrggKVIDLkekvdeALEELPSLEHvIVVGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 190 DDDKPSGSSDETLAELIAHSSTAPAPkASRRAS---IIILTSGTTGTPKGANRNTpptlapiGGILSHVP--------FK 258
Cdd:COG0365 153 TGADVPMEGDLDWDELLAAASAEFEP-EPTDADdplFILYTSGTTGKPKGVVHTH-------GGYLVHAAttakyvldLK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 259 AGEVTLLPSP---MFHALGYMHAALAMflGSTLVL---RRRFK-PALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPK 331
Cdd:COG0365 225 PGDVFWCTADigwATGHSYIVYGPLLN--GATVVLyegRPDFPdPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 332 PDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQ 411
Cdd:COG0365 303 YDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 412 GAVGRIFVGNAFP--FEGYTGGGGKQI------IDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISG 483
Cdd:COG0365 383 GEEGELVIKGPWPgmFRGYWNDPERYRetyfgrFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 484 HPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDT---IKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:COG0365 463 HPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELakeLQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
65-558 |
1.87e-93 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 295.06 E-value: 1.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 65 MLPSHNARRAPNRAAVI-DEEGT-LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLN 142
Cdd:PRK13391 1 MYPGIHAQTTPDKPAVImASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 143 SEFSGPQIKEVSDREGAKVIIYDDEYTKAVSLA--QPPLGKLRaLGVNPDDDKPSGssdETLAELIAHSSTAPAPKaSRR 220
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKLDVARALlkQCPGVRHR-LVLDGDGELEGF---VGYAEAVAGLPATPIAD-ESL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 221 ASIIILTSGTTGTPKGANR-------NTPPTLAPIGGILSHvpFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRR 293
Cdd:PRK13391 156 GTDMLYSSGTTGRPKGIKRplpeqppDTPLPLTAFLQRLWG--FRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 294 FKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVA 373
Cdd:PRK13391 234 FDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 374 FATIAGPKDLQFNPSTVGPVVKGVtVKILDENGNEVPQGAVGRIFVGNAFPFEgYTGGGGK----QIIDGLLS-SGDVGY 448
Cdd:PRK13391 314 GFTACDSEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKtaeaRHPDGTWStVGDIGY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 449 FDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQ---YV 525
Cdd:PRK13391 392 VDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAEliaFC 471
|
490 500 510
....*....|....*....|....*....|...
gi 801237227 526 RDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK13391 472 RQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
51-559 |
3.37e-89 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 284.52 E-value: 3.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 51 AALAADIRKWgEVGMLPSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYG 130
Cdd:PRK08316 2 MERSTRARRQ-TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 131 AARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDDEYTKAV--SLAQPPLGKLRALGVNPDDDkPSGSSDETLAELIAH 208
Cdd:PRK08316 81 CARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAeaALALLPVDTLILSLVLGGRE-APGGWLDFADWAEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 209 SSTAPAPKASRRASIIIL-TSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGyMHAAL--AMFLG 285
Cdd:PRK08316 160 SVAEPDVELADDDLAQILyTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQ-LDVFLgpYLYVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 286 STLVLRRRFKPALVLEDIEKHKATSMVVVP---VMLSRILDqLEKTepkpDLSSLKIVFVSGSQLG----AELATRaLGD 358
Cdd:PRK08316 239 ATNVILDAPDPELILRTIEAERITSFFAPPtvwISLLRHPD-FDTR----DLSSLRKGYYGASIMPvevlKELRER-LPG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 359 LGpvIYNMYGSTEVA-FATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ-- 435
Cdd:PRK08316 313 LR--FYNCYGQTEIApLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTae 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 436 -IIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGA 514
Cdd:PRK08316 391 aFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 801237227 515 DLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PRK08316 471 TVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
71-558 |
2.38e-87 |
|
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: 278.11 E-value: 2.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIAnygaarvgARIILLNSEFSGPQI 150
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFA--------AAAAWKCGACPAYKS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIiyddEYTKAVSLAQPPLGKlRALGVNPDDDKPSGSSDETLAEliahsstapapkASRRASIIILTSGT 230
Cdd:cd05929 74 SRAPRAEACAII----EIKAAALVCGLFTGG-GALDGLEDYEAAEGGSPETPIE------------DEAAGWKMLYSGGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKGANRNTP---PTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHK 307
Cdd:cd05929 137 TGRPKGIKRGLPggpPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRLIERYR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 308 ATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNP 387
Cdd:cd05929 217 VTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIINGEEWLTHP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 388 STVGPVVKGVtVKILDENGNEVPQGAVGRIFVGNAFPFE---GYTGGGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEM 464
Cdd:cd05929 297 GSVGRAVLGK-VHILDEDGNEVPPGEIGEVYFANGPGFEytnDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDM 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 465 IVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGAD---LDEDTIKQYVRDHLARYKVPREVIFL 541
Cdd:cd05929 376 IISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADagtALAEELIAFLRDRLSRYKCPRSIEFV 455
|
490
....*....|....*..
gi 801237227 542 DELPRNPTGKVLKRELR 558
Cdd:cd05929 456 AELPRDDTGKLYRRLLR 472
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
82-553 |
1.48e-86 |
|
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: 276.40 E-value: 1.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 82 DEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKV 161
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 162 IIYDDEYTKAVSLAQ---PPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTAPAPKASRRASIIILTSGTTGTPKGA- 237
Cdd:cd05911 86 IFTDPDGLEKVKEAAkelGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVc 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 238 --NRNTpptLAPIGGILSHVP--FKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVV 313
Cdd:cd05911 166 lsHRNL---IANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 314 VP---VMLSR--ILDqlektepKPDLSSLKIVFVSGSQLGAELAtRALGDLGP--VIYNMYGSTEVAFATIAGPkDLQFN 386
Cdd:cd05911 243 VPpiaAALAKspLLD-------KYDLSSLRVILSGGAPLSKELQ-ELLAKRFPnaTIKQGYGMTETGGILTVNP-DGDDK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 387 PSTVGPVVKGVTVKILDENGNE-VPQGAVGRIFVGNAFPFEGYTGG----GGKQIIDGLLSSGDVGYFDERGLLYVSGRD 461
Cdd:cd05911 314 PGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNpeatKETFDEDGWLHTGDIGYFDEDGYLYIVDRK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 462 DEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPR-EVIF 540
Cdd:cd05911 394 KELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRgGVVF 473
|
490
....*....|...
gi 801237227 541 LDELPRNPTGKVL 553
Cdd:cd05911 474 VDEIPKSASGKIL 486
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
69-468 |
1.34e-85 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 271.88 E-value: 1.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAV-IDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSG 147
Cdd:pfam00501 3 RQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTAPAPKASRR-ASIIIL 226
Cdd:pfam00501 83 EELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDdLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 TSGTTGTPKGANRNTPPTLAPIGGILSHVP----FKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVLRRRF---KPAL 298
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLaGATVVLPPGFpalDPAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 299 VLEDIEKHKATSMVVVPVMLSRILDQLEktEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTE--VAFAT 376
Cdd:pfam00501 243 LLELIERYKVTVLYGVPTLLNMLLEAGA--PKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTEttGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 377 IAGPKDLQFNPSTVGPVVKGVTVKILDEN-GNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ----IIDGLLSSGDVGYFDE 451
Cdd:pfam00501 321 PLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTaeafDEDGWYRTGDLGRRDE 400
|
410
....*....|....*..
gi 801237227 452 RGLLYVSGRDDEMIVSG 468
Cdd:pfam00501 401 DGYLEIVGRKKDQIKLG 417
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
71-560 |
1.37e-82 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 266.06 E-value: 1.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK03640 12 AFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYtkavslaqpplgklralgvnpdDDKPSGSSDETLAELIAHSSTAPAPKAS---RRASIIILT 227
Cdd:PRK03640 92 LWQLDDAEVKCLITDDDF----------------------EAKLIPGISVKFAELMNGPKEEAEIQEEfdlDEVATIMYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 228 SGTTGTPKG-----ANRntppTLAPIGGILShVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLED 302
Cdd:PRK03640 150 SGTTGKPKGviqtyGNH----WWSAVGSALN-LGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDAEKINKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 303 IEKHKATSMVVVPVMLSRILDQLEKtEPKPdlSSLKIVFVSGsqlG----AELATRALGDLgPViYNMYGSTEVA--FAT 376
Cdd:PRK03640 225 LQTGGVTIISVVSTMLQRLLERLGE-GTYP--SSFRCMLLGG---GpapkPLLEQCKEKGI-PV-YQSYGMTETAsqIVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 377 IAgPKDLQFNPSTVGPVVKGVTVKILDeNGNEVPQGAVGRIFVGNAFPFEGY---TGGGGKQIIDGLLSSGDVGYFDERG 453
Cdd:PRK03640 297 LS-PEDALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYlnrEDATRETFQDGWFKTGDIGYLDEEG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 454 LLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKkpGADLDEDTIKQYVRDHLARYK 533
Cdd:PRK03640 375 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYK 452
|
490 500
....*....|....*....|....*..
gi 801237227 534 VPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK03640 453 VPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
86-559 |
5.41e-78 |
|
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: 252.69 E-value: 5.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYD 165
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 166 DEYTKAVSLAQPplGKLRALgvnpdddkpsgssdetlaeliahsstapapkasrrasiiILTSGTTGTPKGANRNTPPTL 245
Cdd:cd05903 81 ERFRQFDPAAMP--DAVALL---------------------------------------LFTSGTTGEPKGVMHSHNTLS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 246 APIGGILSHVPFKAGEVTLLPSPMFHALGYMHAA-LAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQ 324
Cdd:cd05903 120 ASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFtLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 325 LEKTEPkpDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPS-TVGPVVKGVTVKILD 403
Cdd:cd05903 200 VEEAGE--PLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLyTDGRPLPGVEIKVVD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 404 ENGNEVPQGAVGRIFVGNAFPFEGYTGG---GGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDL 480
Cdd:cd05903 278 DTGATLAPGVEGELLSRGPSVFLGYLDRpdlTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 481 ISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYV-RDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:cd05903 358 LLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
65-558 |
6.58e-78 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 254.16 E-value: 6.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 65 MLPSHNARRAPNRAAVIDEEG--TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLN 142
Cdd:PRK13390 1 MYPGTHAQIAPDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 143 SEFSGPQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDdkpSGSSDETLAeliahsstAPAPKASRR-- 220
Cdd:PRK13390 81 HHLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIDG---FGSFEAALA--------GAGPRLTEQpc 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 221 ASIIILTSGTTGTPKGANRNTP---------PTLAPIGGILShvpFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLR 291
Cdd:PRK13390 150 GAVMLYSSGTTGFPKGIQPDLPgrdvdapgdPIVAIARAFYD---ISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 292 RRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTE 371
Cdd:PRK13390 227 KRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 372 VAFATIAGPKDLQFNPSTVGPVVKGvTVKILDENGNEVPQGAVGRI-FVGNAFPFEGY-----TGGGGKQIIDGLLSSGD 445
Cdd:PRK13390 307 AHGMTFIDSPDWLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVyFERDRLPFRYLndpekTAAAQHPAHPFWTTVGD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 446 VGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQ-- 523
Cdd:PRK13390 386 LGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELAREli 465
|
490 500 510
....*....|....*....|....*....|....*.
gi 801237227 524 -YVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK13390 466 dYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
71-560 |
9.67e-77 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 250.93 E-value: 9.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAK-GVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQ 149
Cdd:PRK06839 12 AYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 150 IKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVnpdddkpsgssdETLAELIAHSSTAPAPKASRRASIIILTSG 229
Cdd:PRK06839 92 LIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISI------------TSLKEIEDRKIDNFVEKNESASFIICYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 230 TTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGY-MHAALAMFLGSTLVLRRRFKPALVLEDIEKHKA 308
Cdd:PRK06839 160 TTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIgLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 309 TSMVVVPVMLSRILDQLEKTepKPDLSSLKIVFVSGSQLGAELaTRALGDLGPVIYNMYGSTEVAFAT-IAGPKDLQFNP 387
Cdd:PRK06839 240 TVVMGVPTIHQALINCSKFE--TTNLQSVRWFYNGGAPCPEEL-MREFIDRGFLFGQGFGMTETSPTVfMLSEEDARRKV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 388 STVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY---TGGGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEM 464
Cdd:PRK06839 317 GSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYwnrPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 465 IVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDEL 544
Cdd:PRK06839 397 IISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKEL 476
|
490
....*....|....*.
gi 801237227 545 PRNPTGKVLKRELRKL 560
Cdd:PRK06839 477 PKNATGKIQKAQLVNQ 492
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
60-559 |
2.52e-76 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 251.59 E-value: 2.52e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 60 WGEVGMLP--SHNARRAPNRAAVIDEEGT-LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGA 136
Cdd:PRK06087 20 WGDASLADywQQTARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 137 RIILLNSEFSGPQIKEVSDREGAKVIIYDDEY--TKAVSLAQPPLGKLRALG--VNPDDDKPSGSSDeTLAELIAHSS-- 210
Cdd:PRK06087 100 VSVPLLPSWREAELVWVLNKCQAKMFFAPTLFkqTRPVDLILPLQNQLPQLQqiVGVDKLAPATSSL-SLSQIIADYEpl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 211 TAPAPKASRRASIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALA-MFLGSTLV 289
Cdd:PRK06087 179 TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTApFLIGARSV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 290 LRRRFKPALVLEDIEKHKAT-SMVVVPVMLSrILDQLEKTEPkpDLSSLKIVFVSGSQLGAELATRALGDlGPVIYNMYG 368
Cdd:PRK06087 259 LLDIFTPDACLALLEQQRCTcMLGATPFIYD-LLNLLEKQPA--DLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 369 STEVAFATIAGPKD-LQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGggKQII------DGLL 441
Cdd:PRK06087 335 STESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDE--PELTaraldeEGWY 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 442 SSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVV-KKPGADLD-ED 519
Cdd:PRK06087 413 YSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlKAPHHSLTlEE 492
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 801237227 520 TIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PRK06087 493 VVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-558 |
3.10e-74 |
|
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: 242.20 E-value: 3.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 88 TFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDde 167
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 168 ytkavslaqpplgklralgvnpdddkpsgssdetLAEliahsstapapkasrrasiIILTSGTTGTPKG---ANRNtppt 244
Cdd:cd05934 83 ----------------------------------PAS-------------------ILYTSGTTGPPKGvviTHAN---- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 245 lAPIGGILS--HVPFKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRI 321
Cdd:cd05934 106 -LTFAGYYSarRFGLGEDDVYLTVLPLFHINAQAVSVLAALSvGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 322 LdqleKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFAtIAGPKDLQFNPSTVGPVVKGVTVKI 401
Cdd:cd05934 185 L----AQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVG-VIGPRDEPRRPGSIGRPAPGYEVRI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 402 LDENGNEVPQGAVGRIFVGNAFP---FEGYTG---GGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPA 475
Cdd:cd05934 260 VDDDGQELPAGEPGELVIRGLRGwgfFKGYYNmpeATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 476 EVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKR 555
Cdd:cd05934 340 EVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKA 419
|
...
gi 801237227 556 ELR 558
Cdd:cd05934 420 QLR 422
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
86-559 |
2.89e-73 |
|
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: 239.56 E-value: 2.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSgpqIKEVSDregakviiyd 165
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLT---PNELAF---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 166 deytkavslaqpplgKLRALGVNPDDdkpsgssdetlaeliahsstapapkasrrASIIILTSGTTGTPKGAnrntPPTL 245
Cdd:cd05912 68 ---------------QLKDSDVKLDD-----------------------------IATIMYTSGTTGKPKGV----QQTF 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 246 -----APIGGILShVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSR 320
Cdd:cd05912 100 gnhwwSAIGSALN-LGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 321 ILDQLEKTEPkpdlSSLKIVFVSGSQLGAELATRALgDLGPVIYNMYGSTEVA--FATIAgPKDLQFNPSTVGPVVKGVT 398
Cdd:cd05912 179 LLEILGEGYP----NNLRCILLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETCsqIVTLS-PEDALNKIGSAGKPLFPVE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 399 VKILDENGNEvpqGAVGRIFVGNAFPFEGYTG---GGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPA 475
Cdd:cd05912 253 LKIEDDGQPP---YEVGEILLKGPNVTKGYLNrpdATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 476 EVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKpgADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKR 555
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRH 407
|
....
gi 801237227 556 ELRK 559
Cdd:cd05912 408 ELKQ 411
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
88-559 |
7.90e-73 |
|
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: 241.38 E-value: 7.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 88 TFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDDE 167
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 168 YTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLA---ELIA-HSSTAPAPKASRR-ASIIILTSGTTGTPKG---ANR 239
Cdd:cd12119 107 FLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLayeELLAaESPEYDWPDFDENtAAAICYTSGTTGNPKGvvySHR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 240 ----NTPPTLAPIGgilshVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLR-RRFKPALVLEDIEKHKATSMVVV 314
Cdd:cd12119 187 slvlHAMAALLTDG-----LGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPgPYLDPASLAELIEREGVTFAAGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 315 PVMLSRILDQLEKTepKPDLSSLKIVFVSGSQLGAELATRALgDLGPVIYNMYGSTEV-AFATIAGPKDLQFNPS----- 388
Cdd:cd12119 262 PTVWQGLLDHLEAN--GRDLSSLRRVVIGGSAVPRSLIEAFE-ERGVRVIHAWGMTETsPLGTVARPPSEHSNLSedeql 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 389 ----TVGPVVKGVTVKILDENGNEVPQ--GAVGRIFVGNAFPFEGYTGGGGKQII---DGLLSSGDVGYFDERGLLYVSG 459
Cdd:cd12119 339 alraKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEAlteDGWLRTGDVATIDEDGYLTITD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 460 RDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVI 539
Cdd:cd12119 419 RSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVV 498
|
490 500
....*....|....*....|
gi 801237227 540 FLDELPRNPTGKVLKRELRK 559
Cdd:cd12119 499 FVDEIPKTSTGKIDKKALRE 518
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
70-557 |
1.75e-72 |
|
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: 240.21 E-value: 1.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 70 NARRAPNRAAVIDEEG--TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSG 147
Cdd:cd05904 14 FASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQI-KEVSDrEGAKVIIYDDEYTKAVSLAQPPLGKLralgvnpdDDKPSGSSDETLAELIAHSSTAPAPKASRRASIIIL 226
Cdd:cd05904 94 AEIaKQVKD-SGAKLAFTTAELAEKLASLALPVVLL--------DSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 -TSGTTGTPKGA---NRNTpptlapIGGILSHVPFKAGE-----VTLLPSPMFHALGYMHAALA-MFLGSTLVLRRRFKP 296
Cdd:cd05904 165 ySSGTTGRSKGVmltHRNL------IAMVAQFVAGEGSNsdsedVFLCVLPMFHIYGLSSFALGlLRLGATVVVMPRFDL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 297 ALVLEDIEKHKATSMVVVPVMLSRILDQLEktEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNM-YGSTEV--A 373
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVLALVKSPI--VDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQgYGMTEStgV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 374 FATIAGPKDLQFNPSTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGYTG---GGGKQII-DGLLSSGDVGY 448
Cdd:cd05904 317 VAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNnpeATAATIDkEGWLHTGDLCY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 449 FDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDH 528
Cdd:cd05904 397 IDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQ 476
|
490 500
....*....|....*....|....*....
gi 801237227 529 LARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd05904 477 VAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
69-560 |
5.87e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 240.67 E-value: 5.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGP 148
Cdd:PRK05605 40 NAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 149 QIKEVSDREGAKVIIYDDeytKAVSLAQ--------------------P---------PLGKLRALgvnpdDDKPSGSSD 199
Cdd:PRK05605 120 ELEHPFEDHGARVAIVWD---KVAPTVErlrrttpletivsvnmiaamPllqrlalrlPIPALRKA-----RAALTGPAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 200 ETL-------AELIAHSSTAPAPKASRRASIIIL-TSGTTGTPKGAnrntpptlapiggILSH-------------VPF- 257
Cdd:PRK05605 192 GTVpwetlvdAAIGGDGSDVSHPRPTPDDVALILyTSGTTGKPKGA-------------QLTHrnlfanaaqgkawVPGl 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 258 -KAGEVTLLPSPMFHALGY-MHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEktEPKPDLS 335
Cdd:PRK05605 259 gDGPERVLAALPMFHAYGLtLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAE--ERGVDLS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 336 SLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILD-ENGNE-VPQGA 413
Cdd:PRK05605 337 GVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDpEDPDEtMPDGE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 414 VGRIFVGNAFPFEGYTG---GGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEA 490
Cdd:PRK05605 417 EGELLVRGPQVFKGYWNrpeETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDA 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 491 AAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK05605 497 AVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
68-560 |
6.12e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 239.17 E-value: 6.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 68 SHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSG 147
Cdd:PRK07470 14 RQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQIKEVSDREGAKVIIYDD---EYTKAVSLAQPPLGKLRALGvnpddDKPSGSSDETLaeLIAHSSTAPAPKASRR--AS 222
Cdd:PRK07470 94 DEVAYLAEASGARAMICHAdfpEHAAAVRAASPDLTHVVAIG-----GARAGLDYEAL--VARHLGARVANAAVDHddPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 223 IIILTSGTTGTPKGAnrntpptlapiggILSH--------------VPFKAGE-VTLLPSPMFHALGyMHAALAMFLGST 287
Cdd:PRK07470 167 WFFFTSGTTGRPKAA-------------VLTHgqmafvitnhladlMPGTTEQdASLVVAPLSHGAG-IHQLCQVARGAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 288 LVL--RRRFKPALVLEDIEKHKATSMVVVPVMLsRILDQLEKTEpKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYN 365
Cdd:PRK07470 233 TVLlpSERFDPAEVWALVERHRVTNLFTVPTIL-KMLVEHPAVD-RYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 366 MYGSTEVAFATIAGPKDLQFnpSTVGPVVK---------GVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG---GGG 433
Cdd:PRK07470 311 YFGLGEVTGNITVLPPALHD--AEDGPDARigtcgfertGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNnpeANA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 434 KQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPG 513
Cdd:PRK07470 389 KAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDG 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 801237227 514 ADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK07470 469 APVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
76-559 |
8.06e-72 |
|
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: 237.98 E-value: 8.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 76 NRAAVIDEEGT-LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVS 154
Cdd:cd05926 3 APALVVPGSTPaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 DREGAKVIIYD-DEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTAPAPKASRRASIIIL-TSGTTG 232
Cdd:cd05926 83 ADLGSKLVLTPkGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILhTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 233 TPKG---ANRNTpptLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVLRRRFKPALVLEDIEKHKA 308
Cdd:cd05926 163 RPKGvplTHRNL---AASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAaGGSVVLPPRFSASTFWPDVRDYNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 309 TSMVVVPVMLSrILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLG-PVIyNMYGSTEVAFATIAGPKDL-QFN 386
Cdd:cd05926 240 TWYTAVPTIHQ-ILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGaPVL-EAYGMTEAAHQMTSNPLPPgPRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 387 PSTVGPVVkGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG-------GGGKqiiDGLLSSGDVGYFDERGLLYVSG 459
Cdd:cd05926 318 PGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNnpeanaeAAFK---DGWFRTGDLGYLDADGYLFLTG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 460 RDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVI 539
Cdd:cd05926 394 RIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVY 473
|
490 500
....*....|....*....|
gi 801237227 540 FLDELPRNPTGKVLKRELRK 559
Cdd:cd05926 474 FVDELPKTATGKIQRRKVAE 493
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
63-551 |
1.97e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 232.85 E-value: 1.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 63 VGMLPSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLN 142
Cdd:PRK07798 5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 143 SEFSGPQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSD-ETLAELIAHSSTAPAPKA-SRR 220
Cdd:PRK07798 85 YRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGaVDYEDALAAGSPERDFGErSPD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 221 ASIIILTSGTTGTPKG------------ANRNTPPTLAPIGGILSHVPFKA--GEVTLLP-SPMFHALGYMHAALAMFLG 285
Cdd:PRK07798 165 DLYLLYTGGTTGMPKGvmwrqedifrvlLGGRDFATGEPIEDEEELAKRAAagPGMRRFPaPPLMHGAGQWAAFAALFSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 286 STLVL--RRRFKPALVLEDIEKHKATSMVVV-PVMLSRILDQLEKTEPkPDLSSLKIVFVSGSQLGAElATRALGDLGP- 361
Cdd:PRK07798 245 QTVVLlpDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGP-YDLSSLFAIASGGALFSPS-VKEALLELLPn 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 362 -VIYNMYGSTEVAFATIAGPKDLQfnPSTVGPVVK-GVTVKILDENGNEVP--QGAVGRIFVGNAFPFeGYTGGGGK--- 434
Cdd:PRK07798 323 vVLTDSIGSSETGFGGSGTVAKGA--VHTGGPRFTiGPRTVVLDEDGNPVEpgSGEIGWIARRGHIPL-GYYKDPEKtae 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 435 --QIIDG--LLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVK 510
Cdd:PRK07798 400 tfPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQL 479
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 801237227 511 KPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGK 551
Cdd:PRK07798 480 REGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
51-558 |
7.07e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 231.03 E-value: 7.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 51 AALAADIRKWGEVGMLPSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARN--HRWFVIan 128
Cdd:PRK06188 2 ATMADLLHSGATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNrpEVLMAI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 129 yGAARV-GARIILLNSEFSGPQIKEVSDREGAKVIIYDDEY--TKAVSLAQPPLGKLRALGVNPDDDKPSgssdetLAEL 205
Cdd:PRK06188 80 -GAAQLaGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPfvERALALLARVPSLKHVLTLGPVPDGVD------LLAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 206 IAHSSTAPAPKASRRASIIIL--TSGTTGTPKGA---NRNTPpTLAPIggILSHVPFKAGEVTLLPSPMFHALGYMHAAl 280
Cdd:PRK06188 153 AAKFGPAPLVAAALPPDIAGLayTGGTTGKPKGVmgtHRSIA-TMAQI--QLAEWEWPADPRFLMCTPLSHAGGAFFLP- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 281 AMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILD--QLEKTepkpDLSSLKIVFVSGSQLGAELATRALGD 358
Cdd:PRK06188 229 TLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDhpDLRTR----DLSSLETVYYGASPMSPVRLAEAIER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 359 LGPVIYNMYGSTEVAFA-TIAGPKD-LQFNP---STVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY----- 428
Cdd:PRK06188 305 FGPIFAQYYGQTEAPMViTYLRKRDhDPDDPkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYwnrpe 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 429 -TGgggKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAF 507
Cdd:PRK06188 385 eTA---EAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 801237227 508 VVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK06188 462 VVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
68-559 |
1.72e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 229.28 E-value: 1.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 68 SHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAgDGVAILARNHRWFVIANYGAARVGARIILLNSEFSG 147
Cdd:PRK07638 8 KKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQIKEVSDREGAKVIIYDDEYtkavslaqppLGKLralgvnPDDDKPSGSSDEtLAELIAHSSTAPAPKASRRASIIIL- 226
Cdd:PRK07638 87 DELKERLAISNADMIVTERYK----------LNDL------PDEEGRVIEIDE-WKRMIEKYLPTYAPIENVQNAPFYMg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 -TSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEK 305
Cdd:PRK07638 150 fTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRKFIPNQVLDKLET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 306 HKATSMVVVPVMLsrilDQLEKTEPKPDlSSLKIVfVSGSQLGAElATRALGDLGP--VIYNMYGSTEVAFATIAGPKDL 383
Cdd:PRK07638 230 ENISVMYTVPTML----ESLYKENRVIE-NKMKII-SSGAKWEAE-AKEKIKNIFPyaKLYEFYGASELSFVTALVDEES 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 384 QFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGG---GKQIIDGLLSSGDVGYFDERGLLYVSGR 460
Cdd:PRK07638 303 ERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGvlaRELNADGWMTVRDVGYEDEEGFIYIVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 461 DDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVvkKPGAdlDEDTIKQYVRDHLARYKVPREVIF 540
Cdd:PRK07638 383 EKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--KGSA--TKQQLKSFCLQRLSSFKIPKEWHF 458
|
490
....*....|....*....
gi 801237227 541 LDELPRNPTGKVLKRELRK 559
Cdd:PRK07638 459 VDEIPYTNSGKIARMEAKS 477
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
87-559 |
1.40e-67 |
|
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: 224.91 E-value: 1.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 87 LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDD 166
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 167 EytkavslaqpplgklralgvnpdddkpsgssdetlaeliahsstapapkasrRASIIILTSGTTGTPKGAnrntpptLA 246
Cdd:cd05972 81 E----------------------------------------------------DPALIYFTSGTTGLPKGV-------LH 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 247 PIGGILSHVPFKAGEVTLLPSPMFHAL---GYMHAALAMF-----LGSTLVL--RRRFKPALVLEDIEKHKATSMVVVPV 316
Cdd:cd05972 102 THSYPLGHIPTAAYWLGLRPDDIHWNIadpGWAKGAWSSFfgpwlLGATVFVyeGPRFDAERILELLERYGVTSFCGPPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 317 MLSRILDQLEktePKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAfATIAGPKDLQFNPSTVGPVVKG 396
Cdd:cd05972 182 AYRMLIKQDL---SSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG-LTVGNFPDMPVKPGSMGRPTPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 397 VTVKILDENGNEVPQGAVGRIFV--GNAFPFEGYTGGGGK---QIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGEN 471
Cdd:cd05972 258 YDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKteaSIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 472 VFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGA-DLDEDT--IKQYVRDHLARYKVPREVIFLDELPRNP 548
Cdd:cd05972 338 IGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYePSEELAeeLQGHVKKVLAPYKYPREIEFVEELPKTI 417
|
490
....*....|.
gi 801237227 549 TGKVLKRELRK 559
Cdd:cd05972 418 SGKIRRVELRD 428
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
71-560 |
1.11e-66 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 226.19 E-value: 1.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTL--TFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGP 148
Cdd:PRK12583 28 VARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 149 QIKEVSDREGAKVIIYDDEY------------------TKAVSLAQPPLGKLRALgVNPDDDKPSGSSdeTLAELIAHSS 210
Cdd:PRK12583 108 ELEYALGQSGVRWVICADAFktsdyhamlqellpglaeGQPGALACERLPELRGV-VSLAPAPPPGFL--AWHELQARGE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 211 T-APAPKASRRASI-------IILTSGTTGTPKGAnrntppTLAPiGGILSHVPFKAGEVTL-------LPSPMFHALGY 275
Cdd:PRK12583 185 TvSREALAERQASLdrddpinIQYTSGTTGFPKGA------TLSH-HNILNNGYFVAESLGLtehdrlcVPVPLYHCFGM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 276 MHAALA-MFLGSTLVL-RRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPkpDLSSLKIVFVSGSQLGAELAT 353
Cdd:PRK12583 258 VLANLGcMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNF--DLSSLRTGIMAGAPCPIEVMR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 354 RALGDLG-PVIYNMYGSTE---VAFATIAGpKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYT 429
Cdd:PRK12583 336 RVMDEMHmAEVQIAYGMTEtspVSLQTTAA-DDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYW 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 430 GG--GGKQIID--GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLR 505
Cdd:PRK12583 415 NNpeATAESIDedGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIV 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 801237227 506 AFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK12583 495 AWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
71-558 |
1.14e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 224.38 E-value: 1.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAVSLAQPPLGKlralgvnpddDKPSGSSDETLAEliAHSSTAPA-PKASRRASIIILTSG 229
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALETPKIVI----------DAAAQADSRRLAQ--GGLEIPPQaAVAPTDLVRLMYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 230 TTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALA-MFLGSTLVLRRRFKPALVLEDIEKHKA 308
Cdd:PRK06145 160 TTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAvLWVGGTLRIHREFDPEAVLAAIERHRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 309 TSMVVVPVMLSRILdqlekTEPKP---DLSSLKIVfVSGSQLGAELATRALGDL--GPVIYNMYGSTEvafaTIAGP--- 380
Cdd:PRK06145 240 TCAWMAPVMLSRVL-----TVPDRdrfDLDSLAWC-IGGGEKTPESRIRDFTRVftRARYIDAYGLTE----TCSGDtlm 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 381 ---KDLQFNPSTvGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGK---QIIDGLLSSGDVGYFDERGL 454
Cdd:PRK06145 310 eagREIEKIGST-GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKtaeAFYGDWFRSGDVGYLDEEGF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 455 LYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKV 534
Cdd:PRK06145 389 LYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKV 468
|
490 500
....*....|....*....|....
gi 801237227 535 PREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK06145 469 PRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
75-558 |
2.06e-66 |
|
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: 224.17 E-value: 2.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVS 154
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 DREGAKVIIYDDEYtkaVSLAQPPLGKLRALGVNPDDDKPSGSSDET--LAELIAHSSTAPAPKASRRASII--ILTSGT 230
Cdd:cd05959 98 EDSRARVVVVSGEL---APVLAAALTKSEHTLVVLIVSGGAGPEAGAllLAELVAAEAEQLKPAATHADDPAfwLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKGA---NRNTPPTL----APIGGILShvpfkaGEVTLLPSPMFHALGYMHAAL-AMFLGSTLVLR-RRFKPALVLE 301
Cdd:cd05959 175 TGRPKGVvhlHADIYWTAelyaRNVLGIRE------DDVCFSAAKLFFAYGLGNSLTfPLSVGATTVLMpERPTPAAVFK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 302 DIEKHKATSMVVVPVMLSRILDqlEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAG-P 380
Cdd:cd05959 249 RIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNrP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 381 KDLQfnPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ---IIDGLLSSGDVGYFDERGLLYV 457
Cdd:cd05959 327 GRVR--YGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTrdtFQGEWTRTGDKYVRDDDGFYTY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 458 SGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGA---DLDEDTIKQYVRDHLARYKV 534
Cdd:cd05959 405 AGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYedsEALEEELKEFVKDRLAPYKY 484
|
490 500
....*....|....*....|....
gi 801237227 535 PREVIFLDELPRNPTGKVLKRELR 558
Cdd:cd05959 485 PRWIVFVDELPKTATGKIQRFKLR 508
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
71-560 |
3.25e-66 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 224.25 E-value: 3.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILL-----NSEf 145
Cdd:COG1021 35 AERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFAlpahrRAE- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 146 sgpqIKEVSDREGAKVIIYDDEYTK------AVSL-AQPPlgKLRALGVnpdddkpSGSSDET--LAELIAH--SSTAPA 214
Cdd:COG1021 114 ----ISHFAEQSEAVAYIIPDRHRGfdyralARELqAEVP--SLRHVLV-------VGDAGEFtsLDALLAApaDLSEPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 215 PKASRRAsIIILTSGTTGTPKGANRNTPPTL------APIGGilshvpFKAGEVTLLPSPMFH--------ALGYMHAal 280
Cdd:COG1021 181 PDPDDVA-FFQLSGGTTGLPKLIPRTHDDYLysvrasAEICG------LDADTVYLAALPAAHnfplsspgVLGVLYA-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 281 amflGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTepKPDLSSLKIVFVSGSQLGAELATRALGDLG 360
Cdd:COG1021 252 ----GGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERS--RYDLSSLRVLQVGGAKLSPELARRVRPALG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 361 PVIYNMYGSTE--VAFATIAGPKDLQFNpsTVG-PVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY--------- 428
Cdd:COG1021 326 CTLQQVFGMAEglVNYTRLDDPEEVILT--TQGrPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYyrapehnar 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 429 --TGgggkqiiDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRA 506
Cdd:COG1021 404 afTP-------DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 801237227 507 FVVKKpGADLDEDTIKQYVRD-HLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:COG1021 477 FVVPR-GEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
71-558 |
9.83e-65 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 220.70 E-value: 9.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVID------EEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGAriiLLNse 144
Cdd:PRK13295 34 VASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA---VLN-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 145 fsgPQIKEVSDRE--------GAKVII-------YDdeYTKAVSLAQPPLGKLR-ALGVNPDDDkpsGSSDETLAE-LIA 207
Cdd:PRK13295 109 ---PLMPIFRERElsfmlkhaESKVLVvpktfrgFD--HAAMARRLRPELPALRhVVVVGGDGA---DSFEALLITpAWE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 208 HSSTAPAPKASRRAS-----IIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMH-AALA 281
Cdd:PRK13295 181 QEPDAPAILARLRPGpddvtQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYgLMMP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 282 MFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEktEPKPDLSSLKIVFVSGSQLGAELATRALGDLGP 361
Cdd:PRK13295 261 VMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVK--ESGRPVSSLRTFLCAGAPIPGALVERARAALGA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 362 VIYNMYGSTEVAFATIAGPKD-LQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY------TGGGGk 434
Cdd:PRK13295 339 KIVSAWGMTENGAVTLTKLDDpDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYlkrpqlNGTDA- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 435 qiiDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGA 514
Cdd:PRK13295 418 ---DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQ 494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 801237227 515 DLDEDTIKQYVRDH-LARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK13295 495 SLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
75-557 |
8.42e-64 |
|
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: 215.47 E-value: 8.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILA-RNHRWfVIANYGAARVGARIILLNSEFSGPQIKEV 153
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLeRSLEM-VVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 154 SDREGAKVIIyddeytkavslaqpplgklralgVNPDDdkpsgssdetlaeliahsstapapkasrrASIIILTSGTTGT 233
Cdd:cd05930 80 LEDSGAKLVL-----------------------TDPDD-----------------------------LAYVIYTSGSTGK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 234 PKGanrntppTLAPIGGILSHV-------PFKAGEVTL-LPSPMF-HALGYMHAALAmfLGSTLVL---RRRFKPALVLE 301
Cdd:cd05930 108 PKG-------VMVEHRGLVNLLlwmqeayPLTPGDRVLqFTSFSFdVSVWEIFGALL--AGATLVVlpeEVRKDPEALAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 302 DIEKHKATSMVVVPVMLSRILDQLEKTepkpDLSSLKIVFVSGSQLGAELATRALGDLGPV-IYNMYGSTEVAFATIAG- 379
Cdd:cd05930 179 LLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELLPGArLVNLYGPTEATVDATYYr 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 --PKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG---------------GGGKqiidgLLS 442
Cdd:cd05930 255 vpPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNrpeltaerfvpnpfgPGER-----MYR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 443 SGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIK 522
Cdd:cd05930 330 TGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELR 409
|
490 500 510
....*....|....*....|....*....|....*
gi 801237227 523 QYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd05930 410 AHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
71-557 |
1.44e-63 |
|
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: 216.22 E-value: 1.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGT--LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGP 148
Cdd:cd05923 11 ASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 149 QIKEVSDR-EGAKVIIYDD-EYTKAVSLAqppLGKLRALGVNPDDDKPSGSSDetlaeliahsSTAPAPKASRRASIIIL 226
Cdd:cd05923 91 ELAELIERgEMTAAVIAVDaQVMDAIFQS---GVRVLALSDLVGLGEPESAGP----------LIEDPPREPEQPAFVFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 TSGTTGTPKGA---NRNTPPTLApiggILSHVP---FKAGEVTLLPSPMFHALGYMHA-ALAMFLGSTLVLRRRFKPALV 299
Cdd:cd05923 158 TSGTTGLPKGAvipQRAAESRVL----FMSTQAglrHGRHNVVLGLMPLYHVIGFFAVlVAALALDGTYVVVEEFDPADA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVMLSRILDQLEKTEPKpdLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIag 379
Cdd:cd05923 234 LKLIEQERVTSLFATPTHLDALAAAAEFAGLK--LSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLY-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 pkDLQFNPSTVGPV-----VKgvTVKILDENGNEVPQGAVGRIFVGNA--FPFEGYTG---GGGKQIIDGLLSSGDVGYF 449
Cdd:cd05923 310 --MRDARTGTEMRPgffseVR--IVRIGGSPDEALANGEEGELIVAAAadAAFTGYLNqpeATAKKLQDGWYRTGDVGYV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 450 DERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGaDLDEDTIKQYVRD-H 528
Cdd:cd05923 386 DPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCRAsE 464
|
490 500
....*....|....*....|....*....
gi 801237227 529 LARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd05923 465 LADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
69-559 |
1.54e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 217.34 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRA---PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEF 145
Cdd:PRK07786 22 QLARHAlmqPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 146 SGPQIKEVSDREGAKVIIYDDEYT---KAVSLAQPPLGKLRALGVNPDDDkpSGSSDETLAEliAHSSTAPAPKASRRAS 222
Cdd:PRK07786 102 TPPEIAFLVSDCGAHVVVTEAALApvaTAVRDIVPLLSTVVVAGGSSDDS--VLGYEDLLAE--AGPAHAPVDIPNDSPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 223 IIILTSGTTGTPKGAN-RNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLR--RRFKPALV 299
Cdd:PRK07786 178 LIMYTSGTTGRPKGAVlTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYplGAFDPGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVMLSRILDqlektEPKPDLSSLKIVFVS-GSQLGAELATRALGDLGP--VIYNMYGSTEVAFAT 376
Cdd:PRK07786 258 LDVLEAEKVTGIFLVPAQWQAVCA-----EQQARPRDLALRVLSwGAAPASDTLLRQMAATFPeaQILAAFGQTEMSPVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 377 -IAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY---TGGGGKQIIDGLLSSGDVGYFDER 452
Cdd:PRK07786 333 cMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYwnnPEATAEAFAGGWFHSGDLVRQDEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 453 GLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFV-VKKPGADLDEDTIKQYVRDHLAR 531
Cdd:PRK07786 413 GYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRLAR 492
|
490 500
....*....|....*....|....*...
gi 801237227 532 YKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PRK07786 493 YKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
87-557 |
1.67e-63 |
|
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: 214.27 E-value: 1.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 87 LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNsefsgPQIKEvsdREGAkVIIYDD 166
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPIN-----PMLKE---RELE-YILNDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 167 EYTKAVSlaqpplgklralgvnpdddkpsGSSDETLAeliahsstapapkasrrasIIILTSGTTGTPKGAnRNTPPTLA 246
Cdd:cd05935 73 GAKVAVV----------------------GSELDDLA-------------------LIPYTSGTTGLPKGC-MHTHFSAA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 247 PIGGILSHVPFKAGEVTLLPS-PMFHALGYMHAA-LAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQ 324
Cdd:cd05935 111 ANALQSAVWTGLTPSDVILAClPLFHVTGFVGSLnTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 325 LEKTEPkpDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKdLQFNPSTVGPVVKGVTVKILD- 403
Cdd:cd05935 191 PEFKTR--DLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPP-LRPKLQCLGIP*FGVDARVIDi 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 404 ENGNEVPQGAVGRIFVGNAFPFEGY-----------TGGGGKQiidgLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENV 472
Cdd:cd05935 268 ETGRELPPNEVGEIVVRGPQIFKGYwnrpeeteesfIEIKGRR----FFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 473 FPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPG--ADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTG 550
Cdd:cd05935 344 WPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASG 423
|
....*..
gi 801237227 551 KVLKREL 557
Cdd:cd05935 424 KILWRLL 430
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
63-560 |
1.73e-63 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 217.76 E-value: 1.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 63 VGMLPSHNARRAPNRAAVIDEEGTL--TFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGAriIL 140
Cdd:PRK08315 18 IGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA--IL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 141 LN-------SEfsgpqIKEVSDREGAKVIIYDDE----------YTKAVSLAQPPLGKLRALGVnP--------DDDKPS 195
Cdd:PRK08315 96 VTinpayrlSE-----LEYALNQSGCKALIAADGfkdsdyvamlYELAPELATCEPGQLQSARL-PelrrviflGDEKHP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 196 GSsdETLAELIAHSSTAPAPK-ASRRASI-------IILTSGTTGTPKGA---NRNtpptlapiggILS-------HVPF 257
Cdd:PRK08315 170 GM--LNFDELLALGRAVDDAElAARQATLdpddpinIQYTSGTTGFPKGAtltHRN----------ILNngyfigeAMKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 258 KAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVL-RRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKtePKPDLS 335
Cdd:PRK08315 238 TEEDRLCIPVPLYHCFGMVLGNLACVThGATMVYpGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDF--ARFDLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 336 SLKIVFVSGSQLGAELATRALGDLgpviyNM------YGSTE---VAFAT-IAGPKDLQFnpSTVGPVVKGVTVKILD-E 404
Cdd:PRK08315 316 SLRTGIMAGSPCPIEVMKRVIDKM-----HMsevtiaYGMTEtspVSTQTrTDDPLEKRV--TTVGRALPHLEVKIVDpE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 405 NGNEVPQGAVGRIFVgnafpfEGY------------TggggKQIID--GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGE 470
Cdd:PRK08315 389 TGETVPRGEQGELCT------RGYsvmkgywndpekT----AEAIDadGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 471 NVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTG 550
Cdd:PRK08315 459 NIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTG 538
|
570
....*....|
gi 801237227 551 KVLKRELRKL 560
Cdd:PRK08315 539 KIQKFKMREM 548
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
70-557 |
1.63e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 214.82 E-value: 1.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 70 NARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAK-GVRAGDGVAILARNHRWFVIANYGAARVGARIILLN-----S 143
Cdd:PRK08314 19 SARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNpmnreE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 144 EF------SG-----------PQIKEVSDREG-AKVII--YDDEYTKAVSLAQPPLgklraLGVNPDDDKPSGSSDETLA 203
Cdd:PRK08314 99 ELahyvtdSGarvaivgselaPKVAPAVGNLRlRHVIVaqYSDYLPAEPEIAVPAW-----LRAEPPLQALAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 204 ELIAHSSTAPAPKASRR-ASIIILTSGTTGTPKG---ANRNTPPTLAPiGGILSHVPFKAgeVTLLPSPMFHALGY---M 276
Cdd:PRK08314 174 EALAAGLAPPPHTAGPDdLAVLPYTSGTTGVPKGcmhTHRTVMANAVG-SVLWSNSTPES--VVLAVLPLFHVTGMvhsM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 277 HAALamFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQ--LEKTepkpDLSSLKIVFVSGSQLGAELATR 354
Cdd:PRK08314 251 NAPI--YAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASpgLAER----DLSSLRYIGGGGAAMPEAVAER 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 355 ALGDLGPVIYNMYGSTEVAFATIAGPKD---LQfnpsTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGYTG 430
Cdd:PRK08314 325 LKELTGLDYVEGYGLTETMAQTHSNPPDrpkLQ----CLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 431 gggKQ--------IIDGL--LSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEF 500
Cdd:PRK08314 401 ---RPeataeafiEIDGKrfFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRR 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 801237227 501 GARLRAFVVKKPGAD--LDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK08314 478 GETVKAVVVLRPEARgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
28-560 |
2.12e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 214.90 E-value: 2.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 28 AELHYLRKIIESGAIGLEP--PLNYAALAADIRKWgevgmlpshnARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLA 105
Cdd:PRK06178 8 AELRALQQAAWPAGIPREPeyPHGERPLTEYLRAW----------ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 106 KGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGkLRAL 185
Cdd:PRK06178 78 RGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETS-LRHV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 186 GVN---------PDDDKPSGSSDETLA-----ELIAHSSTAPAPKASRRASI-----IILTSGTTGTPKG---ANRNTPP 243
Cdd:PRK06178 157 IVTsladvlpaePTLPLPDSLRAPRLAaagaiDLLPALRACTAPVPLPPPALdalaaLNYTGGTTGMPKGcehTQRDMVY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 244 TLAPIGGIlsHVPFKAGEVTLLPSPMFHALGYMHAAL-AMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRIL 322
Cdd:PRK06178 237 TAAAAYAV--AVVGGEDSVFLSFLPEFWIAGENFGLLfPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 323 DQLEKTEPkpDLSSLKIVFVSG--SQLGAELATRALGDLGPVIYNM-YGSTEVAFA-TI-----AGPKDLQFNPSTVGPV 393
Cdd:PRK06178 315 DHPRFAEY--DLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCdTFtagfqDDDFDLLSQPVFVGLP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 394 VKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGYTG---GGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGG 469
Cdd:PRK06178 393 VPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNkpeATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 470 ENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPrEVIFLDELPRNPT 549
Cdd:PRK06178 473 MSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTAT 551
|
570
....*....|.
gi 801237227 550 GKVLKRELRKL 560
Cdd:PRK06178 552 GKVRKQDLQAL 562
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
223-552 |
4.78e-62 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 207.51 E-value: 4.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 223 IIILTSGTTGTPKGAnrntpptlapiggILSHVPFKA-------------GEVTLLPSPMFHALGyMHAALAMF-LGSTL 288
Cdd:cd17637 4 VIIHTAAVAGRPRGA-------------VLSHGNLIAanlqlihamglteADVYLNMLPLFHIAG-LNLALATFhAGGAN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 289 VLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPkpDLSSLKIVfvSGSQlGAELATRALGDLGPVIYNMYG 368
Cdd:cd17637 70 VVMEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGV--DLSSLRHV--LGLD-APETIQRFEETTGATFWSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 369 STEVA-FATIAGPKDlqfNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGG---GKQIIDGLLSSG 444
Cdd:cd17637 145 QTETSgLVTLSPYRE---RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPeltAYTFRNGWHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 445 DVGYFDERGLLYVSGR--DDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIK 522
Cdd:cd17637 222 DLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELI 301
|
330 340 350
....*....|....*....|....*....|
gi 801237227 523 QYVRDHLARYKVPREVIFLDELPRNPTGKV 552
Cdd:cd17637 302 EFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
75-558 |
1.76e-61 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 210.89 E-value: 1.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEG-TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNhRWFVIANYGAA-RVGARIILLNSEFSGPQIKE 152
Cdd:PRK07514 16 RDAPFIETPDGlRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEK-SPEALALYLATlRAGAVFLPLNTAYTLAELDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 153 -VSDREgAKVIIYDDEYTKAVSLAQPPLGklrALGVNPDDDKPSGSsdetLAELIAHSST--APAPKASRRASIIILTSG 229
Cdd:PRK07514 95 fIGDAE-PALVVCDPANFAWLSKIAAAAG---APHVETLDADGTGS----LLEAAAAAPDdfETVPRGADDLAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 230 TTGTPKGAnrntpptlapiggILSHV-------------PFKAGEVTLLPSPMFHALGYMHAA-LAMFLGSTLVLRRRFK 295
Cdd:PRK07514 167 TTGRSKGA-------------MLSHGnllsnaltlvdywRFTPDDVLIHALPIFHTHGLFVATnVALLAGASMIFLPKFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 296 PALVLEDIEKhkATSMVVVPVMLSRILDQLEKTepkPDLSSLKIVFVSGSQ-LGAE----LATRAlgdlGPVIYNMYGST 370
Cdd:PRK07514 234 PDAVLALMPR--ATVMMGVPTFYTRLLQEPRLT---REAAAHMRLFISGSApLLAEthreFQERT----GHAILERYGMT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 371 EVAFATiAGPKDLQFNPSTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGY-----------TGgggkqiiD 438
Cdd:PRK07514 305 ETNMNT-SNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYwrmpektaeefRA-------D 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 439 GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDE 518
Cdd:PRK07514 377 GFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDE 456
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 801237227 519 DTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK07514 457 AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
222-554 |
1.46e-60 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 203.50 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 222 SIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVLRRRFKPALVL 300
Cdd:cd17638 3 SDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLtGATVVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 301 EDIEKHKATSMVVVPVMLSRILDqlEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLG-PVIYNMYGSTEVAFATIAG 379
Cdd:cd17638 83 EAIERERITVLPGPPTLFQSLLD--HPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 PKD-LQFNPSTVGPVVKGVTVKILDEngnevpqgavGRIFVGNAFPFEGY---TGGGGKQI-IDGLLSSGDVGYFDERGL 454
Cdd:cd17638 161 PGDdAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYlddPEATAEAIdADGWLHTGDVGELDERGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 455 LYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKV 534
Cdd:cd17638 231 LRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANYKV 310
|
330 340
....*....|....*....|
gi 801237227 535 PREVIFLDELPRNPTGKVLK 554
Cdd:cd17638 311 PRFVRFLDELPRNASGKVMK 330
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
227-558 |
9.68e-60 |
|
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: 201.74 E-value: 9.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 TSGTTGTPKGA---NRNTPPTLAPIGgilSHVPFKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVL-RRRFKPALVLE 301
Cdd:cd05917 10 TSGTTGSPKGAtltHHNIVNNGYFIG---ERLGLTEQDRLCIPVPLFHCFGSVLGVLACLThGATMVFpSPSFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 302 DIEKHKATSMVVVPVMLSRILDQLEKtePKPDLSSLKIVFVSGSQLGAELATRALGDLG-PVIYNMYGSTE---VAFATI 377
Cdd:cd05917 87 AIEKEKCTALHGVPTMFIAELEHPDF--DKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTEtspVSTQTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 378 AG-PKDLQFNpsTVGPVVKGVTVKILDENGNEVPQ-GAVGRIFVGNAFPFEGYTGGGGK--QII--DGLLSSGDVGYFDE 451
Cdd:cd05917 165 TDdSIEKRVN--TVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKtaEAIdgDGWLHTGDLAVMDE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 452 RGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLAR 531
Cdd:cd05917 243 DGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAH 322
|
330 340
....*....|....*....|....*..
gi 801237227 532 YKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:cd05917 323 YKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
226-552 |
2.23e-59 |
|
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: 199.94 E-value: 2.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 226 LTSGTTGTPKGANRNTPPTLA--PIGGILSHVpfKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDI 303
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIEsfVCNEDLFNI--SGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 304 EKHKATSMVVVPVMLsrilDQLEKTEpKPDlSSLKIVFvSGSQLGAELATRALGDLGP--VIYNMYGSTEVAFATIAGPK 381
Cdd:cd17633 85 NQYNATVIYLVPTML----QALARTL-EPE-SKIKSIF-SSGQKLFESTKKKLKNIFPkaNLIEFYGTSELSFITYNFNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 382 DLQfNPSTVGPVVKGVTVKILDENGNEVpqgavGRIFVGNAFPFEGYTGGGGKQIiDGLLSSGDVGYFDERGLLYVSGRD 461
Cdd:cd17633 158 ESR-PPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYVRGGFSNP-DGWMSVGDIGYVDEEGYLYLVGRE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 462 DEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVkkpGADLDEDTIKQYVRDHLARYKVPREVIFL 541
Cdd:cd17633 231 SDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPKKIIFV 307
|
330
....*....|.
gi 801237227 542 DELPRNPTGKV 552
Cdd:cd17633 308 DSLPYTSSGKI 318
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
76-559 |
5.01e-59 |
|
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: 202.52 E-value: 5.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 76 NRAAVIDEEGTLTFSELDEAAHAVANGLLAKG-VRAGDGVAILARNHRWFVIANYGAARVGAriillnsefsgpqikevs 154
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 dregakviiyddeytKAVSLAQpplgklralgvnpdddkpsgssDETLAELiAHSSTAPAPKASRRASIIILTSGTTGTP 234
Cdd:cd05941 63 ---------------VAVPLNP----------------------SYPLAEL-EYVITDSEPSLVLDPALILYTSGTTGRP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 235 KGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALA-MFLGSTLVLRRRFKPALVLEDIEKHKATSMVV 313
Cdd:cd05941 105 KGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCpLFAGASVEFLPKFDPKEVAISRLMPSITVFMG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 314 VPVMLSRILDQLEKTEPKPDLSSLKI-----VFVSGSqlgAELATRALGDL----GPVIYNMYGSTEVAFATiAGPKDLQ 384
Cdd:cd05941 185 VPTIYTRLLQYYEAHFTDPQFARAAAaerlrLMVSGS---AALPVPTLEEWeaitGHTLLERYGMTEIGMAL-SNPLDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 385 FNPSTVGPVVKGVTVKILDENGNE-VPQGAVGRIFVGNAFPFEGY-----------TGgggkqiiDGLLSSGDVGYFDER 452
Cdd:cd05941 261 RRPGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVRGPSVFKEYwnkpeatkeefTD-------DGWFKTGDLGVVDED 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 453 GLLYVSGR-DDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGAD-LDEDTIKQYVRDHLA 530
Cdd:cd05941 334 GYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAaLSLEELKEWAKQRLA 413
|
490 500
....*....|....*....|....*....
gi 801237227 531 RYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:cd05941 414 PYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
77-558 |
6.75e-59 |
|
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: 202.31 E-value: 6.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 77 RAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDR 156
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 157 EGAKVIIYDDEytkAVSLAQpplgklralgvnpdddkpsgssdetlaeliahsstapapkasrrasiiiLTSGTTGTPKG 236
Cdd:cd05919 81 CEARLVVTSAD---DIAYLL-------------------------------------------------YSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 237 ---ANRNTPPTL----APIGGIlshvpfKAGEVTLLPSPMFHALGYMHAAL-AMFLGSTLVLR-RRFKPALVLEDIEKHK 307
Cdd:cd05919 109 vmhAHRDPLLFAdamaREALGL------TPGDRVFSSAKMFFGYGLGNSLWfPLAVGASAVLNpGWPTAERVLATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 308 ATSMVVVPVMLSRILDQleKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDlQFNP 387
Cdd:cd05919 183 PTVLYGVPTFYANLLDS--CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPG-AWRL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 388 STVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ---IIDGLLSSGDVGYFDERGLLYVSGRDDEM 464
Cdd:cd05919 260 GSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSratFNGGWYRTGDKFCRDADGWYTHAGRADDM 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 465 IVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDE---DTIKQYVRDHLARYKVPREVIFL 541
Cdd:cd05919 340 LKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIAFV 419
|
490
....*....|....*..
gi 801237227 542 DELPRNPTGKVLKRELR 558
Cdd:cd05919 420 DELPRTATGKLQRFKLR 436
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
220-560 |
2.71e-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: 197.17 E-value: 2.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 220 RASIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRfkPALV 299
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLER--NQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVMLSRILDQLEktePKPDLSSLKIVFVSGSQLGAELATRALgDLGPVIYNMYGSTEVAfATIAG 379
Cdd:cd17630 79 AEDLAPPGVTHVSLVPTQLQRLLDSGQ---GPAALKSLRAVLLGGAPIPPELLERAA-DRGIPLYTTYGMTETA-SQVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 PKDLQFNPSTVGPVVKGVTVKILDEngnevpqgavGRIFVGNAFPFEGYTGGGGKQII--DGLLSSGDVGYFDERGLLYV 457
Cdd:cd17630 154 KRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPEFneDGWFTTKDLGELHADGRLTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 458 SGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEdtIKQYVRDHLARYKVPRE 537
Cdd:cd17630 224 LGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAE--LRAWLKDKLARFKLPKR 301
|
330 340
....*....|....*....|...
gi 801237227 538 VIFLDELPRNPTGKVLKRELRKL 560
Cdd:cd17630 302 IYPVPELPRTGGGKVDRRALRAW 324
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
77-558 |
1.29e-57 |
|
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: 198.86 E-value: 1.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 77 RAAVIDEEGTLTFSELDEAAHAVANGLLAKGV-RAGDGVAILARNHRWFVIANYGAARVGAriillnsefsgpqikevsd 155
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGA------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 156 regakviiyddeytkaVSLAQPPLgkLRAlgvnPDDDKPSGSSDETLAeLIAHSSTApapkaSRRASIIILTSGTTGTPK 235
Cdd:cd05958 62 ----------------IAVATMPL--LRP----KELAYILDKARITVA-LCAHALTA-----SDDICILAFTSGTTGAPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 236 GANRNTPPTLAPIGGILSHV-PFKAGEVTLLPSPMFHALGYMHAALAMF-LGSTLVLRRRFKPALVLEDIEKHKATSMVV 313
Cdd:cd05958 114 ATMHFHRDPLASADRYAVNVlRLREDDRFVGSPPLAFTFGLGGVLLFPFgVGASGVLLEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 314 VPVMLSRILDQLEKTEPkpDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATI-AGPKDLQfnPSTVGP 392
Cdd:cd05958 194 APTAYRAMLAHPDAAGP--DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFIsARPGDAR--PGATGK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 393 VVKGVTVKILDENGNEVPQGAVGRIFVGNAfpfEGYTGGGGKQ----IIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSG 468
Cdd:cd05958 270 PVPGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRqrtyVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 469 GENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQ---YVRDHLARYKVPREVIFLDELP 545
Cdd:cd05958 347 GYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARElqdHAKAHIAPYKYPRAIEFVTELP 426
|
490
....*....|...
gi 801237227 546 RNPTGKVLKRELR 558
Cdd:cd05958 427 RTATGKLQRFALR 439
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
71-558 |
1.04e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 197.72 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTL--TFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGP 148
Cdd:PRK09088 5 ARLQPQRLAAVDLALGRrwTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 149 QIKEVSDREGAKVIIYDDEytkavslaqpplgkLRALGVNPDDdkpsgssdetLAELIAHSSTA-PAPKAS---RRASII 224
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDA--------------VAAGRTDVED----------LAAFIASADALePADTPSippERVSLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 225 ILTSGTTGTPKGA---NRNTPPTlAPIGGILSHVpfKAGEVTLLPSPMFHALGY---MHAALAMflGSTLVLRRRFKPAL 298
Cdd:PRK09088 141 LFTSGTSGQPKGVmlsERNLQQT-AHNFGVLGRV--DAHSSFLCDAPMFHIIGLitsVRPVLAV--GGSILVSNGFEPKR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 299 VLEDIEKHK--ATSMVVVPVMLSRILDQlektePKPDLSSLK--IVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVA- 373
Cdd:PRK09088 216 TLGRLGDPAlgITHYFCVPQMAQAFRAQ-----PGFDAAALRhlTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGt 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 374 -FATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY-----------TGgggkqiiDGLL 441
Cdd:PRK09088 291 vFGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYwrrpqatarafTG-------DGWF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 442 SSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTI 521
Cdd:PRK09088 364 RTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERI 443
|
490 500 510
....*....|....*....|....*....|....*..
gi 801237227 522 KQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK09088 444 RSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
71-558 |
2.16e-56 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 198.06 E-value: 2.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK06155 31 AERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNpdDDKPSGSSDETLAELIAHSSTAPAPKASRR---ASIIILT 227
Cdd:PRK06155 111 EHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLL--DAPASVSVPAGWSTAPLPPLDAPAPAAAVQpgdTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 228 SGTTGTPKGANrnTPPTLAPIGGILS--HVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEK 305
Cdd:PRK06155 189 SGTTGPSKGVC--CPHAQFYWWGRNSaeDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 306 HKATSMVVVPVMLSrILDQLEKTEPKPDlSSLKIVFVSG--SQLGAELATRalgdLGPVIYNMYGSTEVAFAtIAGPKDL 383
Cdd:PRK06155 267 HGATVTYLLGAMVS-ILLSQPARESDRA-HRVRVALGPGvpAALHAAFRER----FGVDLLDGYGSTETNFV-IAVTHGS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 384 QfNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPF---EGYTGGGGKQII---DGLLSSGDVGYFDERGLLYV 457
Cdd:PRK06155 340 Q-RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFafaTGYFGMPEKTVEawrNLWFHTGDRVVRDADGWFRF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 458 SGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPRE 537
Cdd:PRK06155 419 VDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRY 498
|
490 500
....*....|....*....|.
gi 801237227 538 VIFLDELPRNPTGKVLKRELR 558
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLR 519
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
66-559 |
5.97e-55 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 194.04 E-value: 5.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 66 LPSH-----NARRAPNRAAVIDEE--GTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARI 138
Cdd:PLN02246 23 LPLHdycfeRLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 139 ILLNSEFSGPQIKEVSDREGAKVIIYDDEYtkavslaqppLGKLRALGVNPD------DDKPSGSSDetLAELIAHSSTA 212
Cdd:PLN02246 103 TTANPFYTPAEIAKQAKASGAKLIITQSCY----------VDKLKGLAEDDGvtvvtiDDPPEGCLH--FSELTQADENE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 213 PAPKASRRASIIIL--TSGTTGTPKG---ANRNTPPTLAP-IGGILSHVPFKAGEVTLLPSPMFHALGyMHAAL--AMFL 284
Cdd:PLN02246 171 LPEVEISPDDVVALpySSGTTGLPKGvmlTHKGLVTSVAQqVDGENPNLYFHSDDVILCVLPMFHIYS-LNSVLlcGLRV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 285 GSTLVLRRRFKPALVLEDIEKHKAT-SMVVVPVML----SRILDqlektepKPDLSSLKIVFVSGSQLGAELaTRALGDL 359
Cdd:PLN02246 250 GAAILIMPKFEIGALLELIQRHKVTiAPFVPPIVLaiakSPVVE-------KYDLSSIRMVLSGAAPLGKEL-EDAFRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 360 GP--VIYNMYGSTEvafatiAGP---KDLQF-------NPSTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFE 426
Cdd:PLN02246 322 LPnaVLGQGYGMTE------AGPvlaMCLAFakepfpvKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 427 GYTGG--GGKQIID--GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGA 502
Cdd:PLN02246 396 GYLNDpeATANTIDkdGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGE 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 801237227 503 RLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PLN02246 476 VPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
71-557 |
3.18e-54 |
|
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: 191.00 E-value: 3.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:cd05920 25 AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAVSLAqpplgklralgvnpdddkpsgssdetLAELIAHSSTAPApkasrrasIIILTSGT 230
Cdd:cd05920 105 SAFCAHAEAVAYIVPDRHAGFDHRA--------------------------LARELAESIPEVA--------LFLLSGGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKGANRN------TPPTLAPIGGILSHVpfkageVTLLPSPMFH--------ALGYMHAalamflGSTLVLRRRFKP 296
Cdd:cd05920 151 TGTPKLIPRThndyayNVRASAEVCGLDQDT------VYLAVLPAAHnfplacpgVLGTLLA------GGRVVLAPDPSP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 297 ALVLEDIEKHKATSMVVVPVMLSRILDQLEKtePKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTE--VAF 374
Cdd:cd05920 219 DAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEglLNY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 375 ATIAGPKDLQFNpsTVG-PVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY-----------TGgggkqiiDGLLS 442
Cdd:cd05920 297 TRLDDPDEVIIH--TQGrPMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYyrapehnarafTP-------DGFYR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 443 SGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGAdLDEDTIK 522
Cdd:cd05920 368 TGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPP-PSAAQLR 446
|
490 500 510
....*....|....*....|....*....|....*.
gi 801237227 523 QYVRDH-LARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd05920 447 RFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
88-558 |
8.17e-54 |
|
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: 188.80 E-value: 8.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 88 TFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDde 167
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 168 ytkavslaqpplgklralgvnpdddkpsGSSDetlaeliahsstaPApkasrrasIIILTSGTTGTPKGA---------- 237
Cdd:cd05971 86 ----------------------------GSDD-------------PA--------LIIYTSGTTGPPKGAlhahrvllgh 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 238 -----------NRN-----TPPTLAPIGGILshvpfkageVTLLPSPMFhalgymhaalamflGSTLVLRR--RFKPALV 299
Cdd:cd05971 117 lpgvqfpfnlfPRDgdlywTPADWAWIGGLL---------DVLLPSLYF--------------GVPVLAHRmtKFDPKAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPdlSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAG 379
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQ--VKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNC 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 PKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFV--GNAFPFEGY---TGGGGKQIIDGLLSSGDVGYFDERGL 454
Cdd:cd05971 252 SALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVelPDPVAFLGYwnnPSATEKKMAGDWLLTGDLGRKDSDGY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 455 LYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDED---TIKQYVRDHLAR 531
Cdd:cd05971 332 FWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAA 411
|
490 500
....*....|....*....|....*..
gi 801237227 532 YKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:cd05971 412 HEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
69-558 |
2.02e-53 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 190.26 E-value: 2.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVIDEEGTLTFSELDEAAHAVA----NGLlakGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSE 144
Cdd:PRK08974 31 QAVARYADQPAFINMGEVMTFRKLEERSRAFAaylqNGL---GLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 145 FSGPQIKEVSDREGAKVI------------IYDDEYTKAVSLA----QPPLGKlRALgVN----------PDDDKPSGSS 198
Cdd:PRK08974 108 YTPRELEHQLNDSGAKAIvivsnfahtlekVVFKTPVKHVILTrmgdQLSTAK-GTL-VNfvvkyikrlvPKYHLPDAIS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 199 -DETLAelIAHSSTAPAPKASRRA-SIIILTSGTTGTPKGA---NRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFH-- 271
Cdd:PRK08974 186 fRSALH--KGRRMQYVKPELVPEDlAFLQYTGGTTGVAKGAmltHRNMLANLEQAKAAYGPLLHPGKELVVTALPLYHif 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 272 ALGyMHAALAMFLGST--LVLRRRFKPALVLEdIEKHKATSMVVVPVMLSRILDQLEKTEPkpDLSSLKIVFVSGSQLGA 349
Cdd:PRK08974 264 ALT-VNCLLFIELGGQnlLITNPRDIPGFVKE-LKKYPFTAITGVNTLFNALLNNEEFQEL--DFSSLKLSVGGGMAVQQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 350 ELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY- 428
Cdd:PRK08974 340 AVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYw 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 429 --TGGGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRA 506
Cdd:PRK08974 420 qrPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKI 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 801237227 507 FVVKKpGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK08974 500 FVVKK-DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
71-558 |
6.56e-53 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 187.97 E-value: 6.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVI--DEEG---TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEF 145
Cdd:PRK08008 17 ADVYGHKTALIfeSSGGvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 146 SGPQIKEVSDREGAKVIIYDDE----YTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTAPaPKASRRA 221
Cdd:PRK08008 97 LREESAWILQNSQASLLVTSAQfypmYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPATLCYAP-PLSTDDT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 222 SIIILTSGTTGTPKGAnrntpptlapiggILSH-------------VPFKAGEVTLLPSPMFHALGYMHAALAMF-LGST 287
Cdd:PRK08008 176 AEILFTSGTTSRPKGV-------------VITHynlrfagyysawqCALRDDDVYLTVMPAFHIDCQCTAAMAAFsAGAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 288 LVLRRRFKPALVLEDIEKHKATSMVVVPVMLsRILdQLEKTEPKPDLSSLKIVF----VSGSQLGAeLATRalgdLGPVI 363
Cdd:PRK08008 243 FVLLEKYSARAFWGQVCKYRATITECIPMMI-RTL-MVQPPSANDRQHCLREVMfylnLSDQEKDA-FEER----FGVRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 364 YNMYGSTEvafaTIAG-----PKDLQFNPStVGPVVKGVTVKILDENGNEVPQGAVGRIFVgnafpfegyTGGGGKQII- 437
Cdd:PRK08008 316 LTSYGMTE----TIVGiigdrPGDKRRWPS-IGRPGFCYEAEIRDDHNRPLPAGEIGEICI---------KGVPGKTIFk 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 438 ---------------DGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGA 502
Cdd:PRK08008 382 eyyldpkatakvleaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 801237227 503 RLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK08008 462 AIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
71-557 |
1.41e-51 |
|
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: 183.63 E-value: 1.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:cd17646 8 AARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIyddeyTKAVSLAQPPLGKLRALGVNPDDDkpsgssdetlaeliAHSSTAPAPKASR-RASIIILTSG 229
Cdd:cd17646 88 AYMLADAGPAVVL-----TTADLAARLPAGGDVALLGDEALA--------------APPATPPLVPPRPdNLAYVIYTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 230 TTGTPKG--------ANRntpptlapIGGILSHVPFKAGEVTLLPSPmfhaLGYMHAALAMFL----GSTLVLRR---RF 294
Cdd:cd17646 149 STGRPKGvmvthagiVNR--------LLWMQDEYPLGPGDRVLQKTP----LSFDVSVWELFWplvaGARLVVARpggHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 295 KPALVLEDIEKHKATSMVVVPVMLSRILDqlektEPKPD-LSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVA 373
Cdd:cd17646 217 DPAYLAALIREHGVTTCHFVPSMLRVFLA-----EPAAGsCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 374 FATIAGPKDLQFNPSTV--GPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG--------------GGGKQii 437
Cdd:cd17646 292 IDVTHWPVRGPAETPSVpiGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGrpaltaerfvpdpfGPGSR-- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 438 dgLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPG-ADL 516
Cdd:cd17646 370 --MYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGaAGP 447
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 801237227 517 DEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17646 448 DTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
52-560 |
4.38e-51 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 185.54 E-value: 4.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 52 ALAADIRKWGEVGM----LP-------SHNARRAPNRAAVI--------DEEGTLTFSELDEAAHAVANGLLAKGVRAGD 112
Cdd:PRK07529 5 ATLADIEAIEAVPLaardLPastyellSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 113 GVAILARNHRWFVIANYGAARVGariIL--LNSEFSGPQIKEVSDREGAKVIIYDDEYTKA-----VSLAQPPLGKLRA- 184
Cdd:PRK07529 85 VVAFLLPNLPETHFALWGGEAAG---IAnpINPLLEPEQIAELLRAAGAKVLVTLGPFPGTdiwqkVAEVLAALPELRTv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 185 LGVNPDDDKPSGSS-----------------DETLAELIAHSSTAPAPKASRRASIIILTSGTTGTPKGANRNTPPTLAP 247
Cdd:PRK07529 162 VEVDLARYLPGPKRlavplirrkaharildfDAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 248 IGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVL------RrrfKPALV---LEDIEKHKATSMVVVPVM 317
Cdd:PRK07529 242 AWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLArGAHVVLatpqgyR---GPGVIanfWKIVERYRINFLSGVPTV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 318 LSRILDQlekteP--KPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVK 395
Cdd:PRK07529 319 YAALLQV-----PvdGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 396 GVTVKI--LDENGN---EVPQGAVGRIFVGNAFPFEGYTGG---GGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVS 467
Cdd:PRK07529 394 YQRVRVviLDDAGRylrDCAVDEVGVLCIAGPNVFSGYLEAahnKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 468 GGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLA-RYKVPREVIFLDELPR 546
Cdd:PRK07529 474 GGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPK 553
|
570
....*....|....
gi 801237227 547 NPTGKVLKRELRKL 560
Cdd:PRK07529 554 TAVGKIFKPALRRD 567
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
87-558 |
3.96e-50 |
|
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: 178.85 E-value: 3.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 87 LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDD 166
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 167 EYTKAVSLAQPplgklralgvnpdddkpsgssdetlaeliahsstapapkasrraSIIILTSGTTGTPKGAnrntpptla 246
Cdd:cd05969 81 ELYERTDPEDP--------------------------------------------TLLHYTSGTTGTPKGV--------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 247 piggILSHVPFKAGEVT------LLPSPMFH-------ALGYMHAALAMFL-GSTLVLRR-RFKPALVLEDIEKHKATSM 311
Cdd:cd05969 108 ----LHVHDAMIFYYFTgkyvldLHPDDIYWctadpgwVTGTVYGIWAPWLnGVTNVVYEgRFDAESWYGIIERVKVTVW 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 312 VVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVG 391
Cdd:cd05969 184 YTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 392 PVVKGVTVKILDENGNEVPQGAVGRIFVGNAFP--FEGYTGGGGK---QIIDGLLSSGDVGYFDERGLLYVSGRDDEMIV 466
Cdd:cd05969 264 KPLPGVKAAVVDENGNELPPGTKGILALKPGWPsmFRGIWNDEERyknSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 467 SGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDE---DTIKQYVRDHLARYKVPREVIFLDE 543
Cdd:cd05969 344 TSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKLGAHVAPREIEFVDN 423
|
490
....*....|....*
gi 801237227 544 LPRNPTGKVLKRELR 558
Cdd:cd05969 424 LPKTRSGKIMRRVLK 438
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
72-558 |
1.41e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 179.96 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 72 RRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAK-GVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK05677 35 QRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVI------------IYDDEYTKAVSLAQPP--LGKLRALGVN----------PDDDKPSGSS-DETLAEL 205
Cdd:PRK05677 115 EHQFNDSGAKALvclanmahlaekVLPKTGVKHVIVTEVAdmLPPLKRLLINavvkhvkkmvPAYHLPQAVKfNDALAKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 206 IAHSSTAPAPKASRRAsIIILTSGTTGTPKGA---NRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGY-MHAALA 281
Cdd:PRK05677 195 AGQPVTEANPQADDVA-VLQYTGGTTGVAKGAmltHRNLVANMLQCRALMGSNLNEGCEILIAPLPLYHIYAFtFHCMAM 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 282 MFLG--STLVLRRRFKPALVlEDIEKHKATSMVvvpvMLSRILDQLEKTEP--KPDLSSLKIVFVSGSQLGAELATRALG 357
Cdd:PRK05677 274 MLIGnhNILISNPRDLPAMV-KELGKWKFSGFV----GLNTLFVALCNNEAfrKLDFSALKLTLSGGMALQLATAERWKE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 358 DLGPVIYNMYGSTEVA-FATIAGPKDLQfnPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY--TGGGGK 434
Cdd:PRK05677 349 VTGCAICEGYGMTETSpVVSVNPSQAIQ--VGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYwqRPEATD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 435 QIID--GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKP 512
Cdd:PRK05677 427 EILDsdGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKP 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 801237227 513 GADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK05677 507 GETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
87-559 |
2.83e-49 |
|
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: 176.17 E-value: 2.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 87 LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDd 166
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 167 eytkavsLAQppLGKLralgvnpDDDkpsgssdeTLAELiahsstapapkasrrasiiiLTSGTTGTPKGanrntppTLA 246
Cdd:cd05973 80 -------AAN--RHKL-------DSD--------PFVMM--------------------FTSGTTGLPKG-------VPV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 247 PIGGILSHVPFKAGEVTLLPSPMFH-------ALGYMHAALA-MFLG-STLVLRRRFKPALVLEDIEKHKATSMVVVPVM 317
Cdd:cd05973 109 PLRALAAFGAYLRDAVDLRPEDSFWnaadpgwAYGLYYAITGpLALGhPTILLEGGFSVESTWRVIERLGVTNLAGSPTA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 318 LSRILDQLEKTEPKPDLSsLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAF--ATIAGPKDlQFNPSTVGPVVK 395
Cdd:cd05973 189 YRLLMAAGAEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMvlANHHALEH-PVHAGSAGRAMP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 396 GVTVKILDENGNEVPQGAVGRIFVGNA----FPFEGYTGGGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGEN 471
Cdd:cd05973 267 GWRVAVLDDDGDELGPGEPGRLAIDIAnsplMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 472 VFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLD---EDTIKQYVRDHLARYKVPREVIFLDELPRNP 548
Cdd:cd05973 347 IGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
490
....*....|.
gi 801237227 549 TGKVLKRELRK 559
Cdd:cd05973 427 SGKIQRFLLRR 437
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
75-559 |
1.57e-48 |
|
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: 175.57 E-value: 1.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVS 154
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 DREGAKVIIYDDEYTKAVSLAqpplgklralgvnpdddkpSGSSDETlaeliahsstaPAPKASRRASIII-LTSGTTGT 233
Cdd:cd12118 98 RHSEAKVLFVDREFEYEDLLA-------------------EGDPDFE-----------WIPPADEWDPIALnYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 234 PKGA---NRNTppTLAPIGGILSHvPFKAGEVTLLPSPMFHALGYMHA-ALAMFlGSTLVLRRRFKPALVLEDIEKHKAT 309
Cdd:cd12118 148 PKGVvyhHRGA--YLNALANILEW-EMKQHPVYLWTLPMFHCNGWCFPwTVAAV-GGTNVCLRKVDAKAIYDLIEKHKVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 310 SMVVVPVMLSRILDqlektEPKPDLSSLK---IVFVSGSQLGAELaTRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFN 386
Cdd:cd12118 224 HFCGAPTVLNMLAN-----APPSDARPLPhrvHVMTAGAPPPAAV-LAKMEELGFDVTHVYGLTETYGPATVCAWKPEWD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 387 --PSTVGPVVK---GVTVKILDE-------NGNEVPQGA--VGRI-FVGNAFpFEGY---TGGGGKQIIDGLLSSGDVGY 448
Cdd:cd12118 298 elPTEERARLKarqGVRYVGLEEvdvldpeTMKPVPRDGktIGEIvFRGNIV-MKGYlknPEATAEAFRGGWFHSGDLAV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 449 FDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDH 528
Cdd:cd12118 377 IHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREH 456
|
490 500 510
....*....|....*....|....*....|.
gi 801237227 529 LARYKVPREVIFlDELPRNPTGKVLKRELRK 559
Cdd:cd12118 457 LAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
71-559 |
5.26e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 174.87 E-value: 5.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDG-VAILARNHRWFVIANYGAARVGARIILLNSEFSGPQ 149
Cdd:PRK07867 13 PLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 150 IKEVSDREGAKVIIYDDEYtkaVSLAQPPLGKLRALGVnpdddkpsgSSDETLAELIAHSSTAPAPKASRRAS--IIILT 227
Cdd:PRK07867 93 LARDIAHADCQLVLTESAH---AELLDGLDPGVRVINV---------DSPAWADELAAHRDAEPPFRVADPDDlfMLIFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 228 SGTTGTPKgANRNTPPTLAPIGGILS-HVPFKAGEVTLLPSPMFHALGYMHA-ALAMFLGSTLVLRRRFKPALVLEDIEK 305
Cdd:PRK07867 161 SGTSGDPK-AVRCTHRKVASAGVMLAqRFGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIALRRKFSASGFLPDVRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 306 HKATSMVVVPVMLSRILdqleKTEPKPD--LSSLKIVFvsgsqlGAELATRALGDL----GPVIYNMYGSTE--VAFA-T 376
Cdd:PRK07867 240 YGATYANYVGKPLSYVL----ATPERPDdaDNPLRIVY------GNEGAPGDIARFarrfGCVVVDGFGSTEggVAITrT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 377 IAGPkdlqfnPSTVGPVVKGVtvKILD-ENGNEVPQGAVGRIFVGNAF-------------PFEGYTG---GGGKQIIDG 439
Cdd:PRK07867 310 PDTP------PGALGPLPPGV--AIVDpDTGTECPPAEDADGRLLNADeaigelvntagpgGFEGYYNdpeADAERMRGG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 440 LLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDED 519
Cdd:PRK07867 382 VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPD 461
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 801237227 520 TIKQYV--RDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PRK07867 462 AFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
71-558 |
1.44e-47 |
|
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: 172.91 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:cd17651 5 AARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIiyddeytkavsLAQPPLgklraLGVNPDDDKPSGSSDETLAELIAHSSTAPAPKASRRAsIIILTSGT 230
Cdd:cd17651 85 AFMLADAGPVLV-----------LTHPAL-----AGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLA-YVIYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLpspmFHALGYMHAALAMFL----GSTLVLRR---RFKPALVLEDI 303
Cdd:cd17651 148 TGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQ----FAGLGFDVSVQEIFStlcaGATLVLPPeevRTDPPALAAWL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 304 EKHKATSMVVVPVMLSRILDQLekTEPKPDLSSLKIVFVSGSQLGAELATRAL--GDLGPVIYNMYGSTEVAFAT---IA 378
Cdd:cd17651 224 DEQRISRVFLPTVALRALAEHG--RPLGVRLAALRYLLTGGEQLVLTEDLREFcaGLPGLRLHNHYGPTETHVVTalsLP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 379 GPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGK---------QIIDGLL-SSGDVGY 448
Cdd:cd17651 302 GDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELtaerfvpdpFVPGARMyRTGDLAR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 449 FDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDH 528
Cdd:cd17651 382 WLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATH 461
|
490 500 510
....*....|....*....|....*....|
gi 801237227 529 LARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:cd17651 462 LPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
75-560 |
1.53e-47 |
|
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: 175.20 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVI------DEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLnseFSGP 148
Cdd:cd05967 65 GDQIALIydspvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVV---FGGF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 149 QIKEVSDR----------------EGAKVIIYDDEYTKAVSLAQPPLGK---LRALGVNPDDDKPSGSSDetLAELIA-H 208
Cdd:cd05967 142 AAKELASRiddakpklivtascgiEPGKVVPYKPLLDKALELSGHKPHHvlvLNRPQVPADLTKPGRDLD--WSELLAkA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 209 SSTAPAPKASRRASIIILTSGTTGTPKGANRNTPPTLAPIGGILSHV-PFKAGEVTLLPSPMFHALGYMHAALAMFL-GS 286
Cdd:cd05967 220 EPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIyGIKPGDVWWAASDVGWVVGHSYIVYGPLLhGA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 287 TLVLRRRfKPALVLED------IEKHKATSMVVVPVMLSRI--LDQLEKTEPKPDLSSLKIVFVSGSQLGA---ELATRA 355
Cdd:cd05967 300 TTVLYEG-KPVGTPDPgafwrvIEKYQVNALFTAPTAIRAIrkEDPDGKYIKKYDLSSLRTLFLAGERLDPptlEWAENT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 356 LGDlgPVIYNmYGSTEVAFATIAGPKDLQFNP----STVGPVvKGVTVKILDENGNEVPQGAVGRIFVGNAFP------- 424
Cdd:cd05967 379 LGV--PVIDH-WWQTETGWPITANPVGLEPLPikagSPGKPV-PGYQVQVLDEDGEPVGPNELGNIVIKLPLPpgclltl 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 425 -------FEGYTGgggkqIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDD 497
Cdd:cd05967 455 wknderfKKLYLS-----KFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRD 529
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 801237227 498 KEFGARLRAFVVKKPGADLDEDT----IKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:cd05967 530 ELKGQVPLGLVVLKEGVKITAEElekeLVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI 596
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
45-553 |
6.42e-47 |
|
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: 173.15 E-value: 6.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 45 EPPLNYAAL--AADIRKWGEVGMLP-SHNA-----RRAPNRAAVI--DEEG----TLTFSELDEAAHAVANGLLAKGVRA 110
Cdd:cd17634 29 YQKVKNTSFapGAPSIKWFEDATLNlAANAldrhlRENGDRTAIIyeGDDTsqsrTISYRELHREVCRFAGTLLDLGVKK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 111 GDGVAILARNHRWFVIANYGAARVGAriiLLNSEFSGPQIKEVSDR---EGAKVIIYDDEYTKAvslaqpplGKLRALGV 187
Cdd:cd17634 109 GDRVAIYMPMIPEAAVAMLACARIGA---VHSVIFGGFAPEAVAGRiidSSSRLLITADGGVRA--------GRSVPLKK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 188 NPDDD-KPSGSSDETLA--------------------ELIAHSSTA--PAPKASRRASIIILTSGTTGTPKGANRNTPPT 244
Cdd:cd17634 178 NVDDAlNPNVTSVEHVIvlkrtgsdidwqegrdlwwrDLIAKASPEhqPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 245 LAPIGGILSHV-PFKAGEVTLlpspMFHALGYM--HAAL---AMFLGSTLVLRRRF----KPALVLEDIEKHKATSMVVV 314
Cdd:cd17634 258 LVYAATTMKYVfDYGPGDIYW----CTADVGWVtgHSYLlygPLACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 315 PVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAE---LATRALGDLGPVIYNMYGSTEVAFATIA---GPKDLQFNPS 388
Cdd:cd17634 334 PTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEayeWYWKKIGKEKCPVVDTWWQTETGGFMITplpGAIELKAGSA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 389 TVgPVVkGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ--------IIDGLLSSGDVGYFDERGLLYVSGR 460
Cdd:cd17634 414 TR-PVF-GVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHErfeqtyfsTFKGMYFSGDGARRDEDGYYWITGR 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 461 DDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGA-DLDE--DTIKQYVRDHLARYKVPRE 537
Cdd:cd17634 492 SDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVePSPElyAELRNWVRKEIGPLATPDV 571
|
570
....*....|....*.
gi 801237227 538 VIFLDELPRNPTGKVL 553
Cdd:cd17634 572 VHWVDSLPKTRSGKIM 587
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
71-557 |
1.31e-46 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 169.35 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDdeytkavslaqpplgklralgvnPDDdkpsgssdetLAeliahsstapapkasrrasIIILTSGT 230
Cdd:cd05945 81 REILDAAKPALLIAD-----------------------GDD----------NA-------------------YIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKG---ANRNTpptLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRR---FKPALVLEDIE 304
Cdd:cd05945 109 TGRPKGvqiSHDNL---VSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRdatADPKQLFRFLA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 305 KHKATSMVVVPVMLSRILdqLEKTEPKPDLSSLKIVFVSGSQLGAELAtRALGDLGP--VIYNMYGSTE--VAFATIAGP 380
Cdd:cd05945 186 EHGITVWVSTPSFAAMCL--LSPTFTPESLPSLRHFLFCGEVLPHKTA-RALQQRFPdaRIYNTYGPTEatVAVTYIEVT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 381 KDL--QFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ-----IIDGLLS--SGDVGYFDE 451
Cdd:cd05945 263 PEVldGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTaaaffPDEGQRAyrTGDLVRLEA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 452 RGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGAD-LDEDTIKQYVRDHLA 530
Cdd:cd05945 343 DGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEaGLTKAIKAELAERLP 422
|
490 500
....*....|....*....|....*..
gi 801237227 531 RYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd05945 423 PYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-551 |
1.44e-46 |
|
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: 167.17 E-value: 1.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 IILTSGTTGTPKG---------------ANRNTPPTLAPigGILSHVPFKAGEVTLLP-SPMFHALGYMHAALAMFLGST 287
Cdd:cd05924 8 ILYTGGTTGMPKGvmwrqedifrmlmggADFGTGEFTPS--EDAHKAAAAAAGTVMFPaPPLMHGTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 288 LVL-RRRFKPALVLEDIEKHKATSMVVV-PVMLSRILDQLEKTEPKpDLSSLKIVFVSGSQLGAELATRALgDLGP--VI 363
Cdd:cd05924 86 VVLpDDRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPY-DLSSLFAISSGGALLSPEVKQGLL-ELVPniTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 364 YNMYGSTEVAFATI---------AGPKDLqFNPSTVgpvvkgvtvkILDENGNEVPQG--AVGRIFVGNAFPfEGYTGGG 432
Cdd:cd05924 164 VDAFGSSETGFTGSghsagsgpeTGPFTR-ANPDTV----------VLDDDGRVVPPGsgGVGWIARRGHIP-LGYYGDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 433 GK-----QIIDGL--LSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLR 505
Cdd:cd05924 232 AKtaetfPEVDGVryAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 801237227 506 AFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGK 551
Cdd:cd05924 312 AVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
94-558 |
3.10e-46 |
|
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: 168.39 E-value: 3.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 94 EAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIIL----LNSEFSGPQIKEVSDREGAKVIIYDdeyT 169
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLvfvpLNPTLKESVLRYLVADAGGRIVLAD---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 170 KAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTApapkasrrasIIILTSGTTGTPKG---ANRNTPPTLA 246
Cdd:cd05922 78 GAADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLA----------LLLYTSGSTGSPKLvrlSHQNLLANAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 247 PIGGILSHVPFKAGEvTLLPSPMFHALGYMHAALAMflGSTLVLRRRFK-PALVLEDIEKHKATSMVVVPVMLSrILDQL 325
Cdd:cd05922 148 SIAEYLGITADDRAL-TVLPLSYDYGLSVLNTHLLR--GATLVLTNDGVlDDAFWEDLREHGATGLAGVPSTYA-MLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 326 ekTEPKPDLSSLKIVFVSGSQLGAELaTRALGDLGPV--IYNMYGSTEvAFA--TIAGPKDLQFNPSTVGPVVKGVTVKI 401
Cdd:cd05922 224 --GFDPAKLPSLRYLTQAGGRLPQET-IARLRELLPGaqVYVMYGQTE-ATRrmTYLPPERILEKPGSIGLAIPGGEFEI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 402 LDENGNEVPQGAVGRIFV---------GNAFPFEGYTGGGGkqiidGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENV 472
Cdd:cd05922 300 LDDDGTPTPPGEPGEIVHrgpnvmkgyWNDPPYRRKEGRGG-----GVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 473 FPAEVEDLISGHPDVVEAAAIGVDDkEFGARLRAFVVKKPGADLDEdtIKQYVRDHLARYKVPREVIFLDELPRNPTGKV 552
Cdd:cd05922 375 SPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDKIDPKD--VLRSLAERLPPYKVPATVRVVDELPLTASGKV 451
|
....*.
gi 801237227 553 LKRELR 558
Cdd:cd05922 452 DYAALR 457
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
72-558 |
6.98e-46 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 169.62 E-value: 6.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 72 RRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAK-GVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK12492 35 KKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAVS----------LAQPPLGKL----RALGVN----------PDDDKPSGSSDETLAELI 206
Cdd:PRK12492 115 RHQFKDSGARALVYLNMFGKLVQevlpdtgieyLIEAKMGDLlpaaKGWLVNtvvdkvkkmvPAYHLPQAVPFKQALRQG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 207 AHSSTAPAPKASRRASIIILTSGTTGTPKGAN-------RNTPPTLAPIG--GILSHVPFKAG-EVTLLPSPMFHALGYM 276
Cdd:PRK12492 195 RGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMlthgnlvANMLQVRACLSqlGPDGQPLMKEGqEVMIAPLPLYHIYAFT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 277 HAALAMFLG---STLVLRRRFKPALVLEdIEKHKATSMVVVPVMLSRILDQLEKTepKPDLSSLKIVFVSGSQLGAELAT 353
Cdd:PRK12492 275 ANCMCMMVSgnhNVLITNPRDIPGFIKE-LGKWRFSALLGLNTLFVALMDHPGFK--DLDFSALKLTNSGGTALVKATAE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 354 RALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY--TGG 431
Cdd:PRK12492 352 RWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYwqQPE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 432 GGKQIID--GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVV 509
Cdd:PRK12492 432 ATAEALDaeGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVV 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 801237227 510 -KKPGADLDEdtIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK12492 512 aRDPGLSVEE--LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
65-558 |
9.82e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 167.47 E-value: 9.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 65 MLPSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVAngllaKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSE 144
Cdd:PRK07787 4 LNPAAVAAAADIADAVRIGGRVLSRSDLAGAATAVA-----ERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 145 fSGPqikevsdREGAKviIYDDEYTKAVsLAQPPLGkLRALGVNPDDdkPSGSSDETLAEliahsstaPAPKAsrrASII 224
Cdd:PRK07787 79 -SGV-------AERRH--ILADSGAQAW-LGPAPDD-PAGLPHVPVR--LHARSWHRYPE--------PDPDA---PALI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 225 ILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAAL-AMFLGSTLVLRRRFKPALVLEDI 303
Cdd:PRK07787 134 VYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLgPLRIGNRFVHTGRPTPEAYAQAL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 304 EKhKATSMVVVPVMLSRILDQLEKTEPkpdLSSLKIVfVSGSQ-LGAELATRALGDLGPVIYNMYGSTEvAFATIAGPKD 382
Cdd:PRK07787 214 SE-GGTLYFGVPTVWSRIAADPEAARA---LRGARLL-VSGSAaLPVPVFDRLAALTGHRPVERYGMTE-TLITLSTRAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 383 LQFNPSTVGPVVKGVTVKILDENGNEVPQG--AVGRIFVGNAFPFEGYTG----GGGKQIIDGLLSSGDVGYFDERGLLY 456
Cdd:PRK07787 288 GERRPGWVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNrpdaTAAAFTADGWFRTGDVAVVDPDGMHR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 457 VSGRDD-EMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVkkPGADLDEDTIKQYVRDHLARYKVP 535
Cdd:PRK07787 368 IVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSVHKRP 445
|
490 500
....*....|....*....|...
gi 801237227 536 REVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK07787 446 REVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
66-555 |
2.54e-45 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 167.76 E-value: 2.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 66 LPSHNARRAPNRAAVI--DEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNS 143
Cdd:PRK05852 21 LVEVAATRLPEAPALVvtADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 144 EFSGPQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLrALGVNPDDDKPSGSSDETLAELIAHSSTAPAPKASRRA-S 222
Cdd:PRK05852 101 ALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPL-TVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDdA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 223 IIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVL---RRRFKPALV 299
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLlpaRGRFSAHTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVmLSRILDQLEKTEPKPDL-SSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTE----VAF 374
Cdd:PRK05852 260 WDDIKAVGATWYTAVPT-IHQILLERAATEPSGRKpAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEathqVTT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 375 ATIAGPKDLQFNPSTVGPVVK--GVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGG---GGKQIIDGLLSSGDVGYF 449
Cdd:PRK05852 339 TQIEGIGQTENPVVSTGLVGRstGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDptiTAANFTDGWLRTGDLGSL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 450 DERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHL 529
Cdd:PRK05852 419 SAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERL 498
|
490 500
....*....|....*....|....*.
gi 801237227 530 ARYKVPREVIFLDELPRNPTGKVLKR 555
Cdd:PRK05852 499 AAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
87-559 |
3.94e-45 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 167.67 E-value: 3.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 87 LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDD 166
Cdd:PLN02860 33 RTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 167 E----YTKAVSLAQPPLgKLRALGVNPDDDKPSGSSD----ETLAELIAHSSTAPAPKASRRASIIILTSGTTGTPKGA- 237
Cdd:PLN02860 113 TcsswYEELQNDRLPSL-MWQVFLESPSSSVFIFLNSflttEMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVt 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 238 ---NRNTPPTLAPIggilSHVPFKAGEVTLLPSPMFHaLGYMHAALAMFL-GSTLVLRRRFKPALVLEDIEKHKATSMVV 313
Cdd:PLN02860 192 ishSALIVQSLAKI----AIVGYGEDDVYLHTAPLCH-IGGLSSALAMLMvGACHVLLPKFDAKAALQAIKQHNVTSMIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 314 VPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALgDLGP--VIYNMYGSTE-------------------V 372
Cdd:PLN02860 267 VPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAK-KLFPnaKLFSAYGMTEacssltfmtlhdptlespkQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 373 AFATIAGPKDLQFNP---STVGPVVKGVTVKI-LDENGNevpqgaVGRIFVGNAFPFEGYTGgggkQII--------DGL 440
Cdd:PLN02860 346 TLQTVNQTKSSSVHQpqgVCVGKPAPHVELKIgLDESSR------VGRILTRGPHVMLGYWG----QNSetasvlsnDGW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 441 LSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFV----------VK 510
Cdd:PLN02860 416 LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwsdNE 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 801237227 511 KPGAD----LDEDTIKQYVRD-HLARYKVPRE-VIFLDELPRNPTGKVLKRELRK 559
Cdd:PLN02860 496 KENAKknltLSSETLRHHCREkNLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
71-557 |
4.04e-45 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 165.84 E-value: 4.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:cd12117 7 AARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAeliahsstapapkasrrasIIILTSGT 230
Cdd:cd12117 87 AFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLA-------------------YVMYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKGanrntppTLAPIGGIL------SHVPFKAGEVTLLPSPM-FHALGY-MHAALamFLGSTLVL--RRRFKPALVL 300
Cdd:cd12117 148 TGRPKG-------VAVTHRGVVrlvkntNYVTLGPDDRVLQTSPLaFDASTFeIWGAL--LNGARLVLapKGTLLDPDAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 301 ED-IEKHKATSMVVVPVMLSRILDQlektepKPD-LSSLKIVFVSGSQLGAELATRALGDLGPV-IYNMYGSTE-VAFAT 376
Cdd:cd12117 219 GAlIAEEGVTVLWLTAALFNQLADE------DPEcFAGLRELLTGGEVVSPPHVRRVLAACPGLrLVNGYGPTEnTTFTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 377 IAGPKDLQFNPSTV--GPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG--------------GGGKQiidgL 440
Cdd:cd12117 293 SHVVTELDEVAGSIpiGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNrpaltaerfvadpfGPGER----L 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 441 LSSGD-VGYFDERGLLYVSGRDDEMIVSgGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVkkPGADLDED 519
Cdd:cd12117 369 YRTGDlARWLPDGRLEFLGRIDDQVKIR-GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALDAA 445
|
490 500 510
....*....|....*....|....*....|....*...
gi 801237227 520 TIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd12117 446 ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
71-557 |
4.16e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 167.52 E-value: 4.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK06710 34 ASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTEREL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSdeTLAELIAHSSTAPAPKASRRASI------- 223
Cdd:PRK06710 114 EYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKN--LLYPFVQKKQSNLVVKVSESETIhlwnsve 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 -------------------IILTSGTTGTPKG---ANRN-TPPTLAPIGGILSHVpfKAGEVTLLPSPMFHALGyMHAA- 279
Cdd:PRK06710 192 kevntgvevpcdpendlalLQYTGGTTGFPKGvmlTHKNlVSNTLMGVQWLYNCK--EGEEVVLGVLPFFHVYG-MTAVm 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 280 -LAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPkpDLSSLKIVFVSGSQLGAELATRALGD 358
Cdd:PRK06710 269 nLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEY--DISSIRACISGSAPLPVEVQEKFETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 359 LGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ-- 435
Cdd:PRK06710 347 TGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETaa 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 436 -IIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGA 514
Cdd:PRK06710 427 vLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGT 506
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 801237227 515 DLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK06710 507 ECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
71-560 |
6.37e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 166.46 E-value: 6.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTK----AVSLAQPPLGKLRALGVNPDDDKPSGSSDETLA---ELIAHSSTAPAPKASRRAS- 222
Cdd:PRK06164 100 AHILGRGRARWLVVWPGFKGidfaAILAAVPPDALPPLRAIAVVDDAADATPAPAPGarvQLFALPDPAPPAAAGERAAd 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 223 -----IIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPA 297
Cdd:PRK06164 180 pdagaLLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 298 LVLEDIEKHKATSMVVVPVMLSRILDQlekTEPKPDLSSLKIV-FVSGSQLGAELATRALgDLGPVIYNMYGSTEVAFAT 376
Cdd:PRK06164 260 RTARALRRHRVTHTFGNDEMLRRILDT---AGERADFPSARLFgFASFAPALGELAALAR-ARGVPLTGLYGSSEVQALV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 377 IAGPKDLQFNPSTVG---PVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGYTG---GGGKQII-DGLLSSGDVGY 448
Cdd:PRK06164 336 ALQPATDPVSVRIEGggrPASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDnpdATARALTdDGYFRTGDLGY 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 449 FDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFgARLRAFVVKKPGADLDEDTIKQYVRDH 528
Cdd:PRK06164 416 TRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGK-TVPVAFVIPTDGASPDEAGLMAACREA 494
|
490 500 510
....*....|....*....|....*....|....*
gi 801237227 529 LARYKVPREVIFLDELPRNPTG---KVLKRELRKL 560
Cdd:PRK06164 495 LAGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
63-560 |
1.34e-44 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 166.17 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 63 VGMLPSHNARraPNRAAVIDEEG--TLTFSELDEAAHAVANGLLAK-GVRAGDGVAILARNHRWFVIANYGAARVGARII 139
Cdd:PLN02574 43 VSFIFSHHNH--NGDTALIDSSTgfSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 140 LLNSEFSGPQIK-EVSDREGAKVIIYDDEYTKAvslaqPPLGkLRALGVNPDDDKPSGSSDETLAELIAHSSTAPAPKAS 218
Cdd:PLN02574 121 TMNPSSSLGEIKkRVVDCSVGLAFTSPENVEKL-----SPLG-VPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 219 RR---ASIIILTSGTTGTPKG---ANRNTpptlapIGGILSHVPFKAGE--------VTLLPSPMFHALGymhaaLAMF- 283
Cdd:PLN02574 195 IKqddVAAIMYSSGTTGASKGvvlTHRNL------IAMVELFVRFEASQyeypgsdnVYLAALPMFHIYG-----LSLFv 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 284 -----LGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPdLSSLKIVfvsgSQLGAELATRALGD 358
Cdd:PLN02574 264 vgllsLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEV-LKSLKQV----SCGAAPLSGKFIQD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 359 LGPVIYNM-----YGSTEVAFATIAGPKDLQF-NPSTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGYTGG 431
Cdd:PLN02574 339 FVQTLPHVdfiqgYGMTESTAVGTRGFNTEKLsKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNN 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 432 GGKQII----DGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAF 507
Cdd:PLN02574 419 PKATQStidkDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAF 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 801237227 508 VVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PLN02574 499 VVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
69-559 |
1.97e-44 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 165.31 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVIDE-EGTL---TFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSE 144
Cdd:PRK06018 18 HAARIHGNREVVTRSvEGPIvrtTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 145 FSGPQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDD-------KPSGSSDETLAEliAHSSTAPAPKA 217
Cdd:PRK06018 98 LFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPSVERYVVLTDAAhmpqttlKNAVAYEEWIAE--ADGDFAWKTFD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 218 SRRASIIILTSGTTGTPKG---ANR-NTPPTLAPIGGilSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLR-R 292
Cdd:PRK06018 176 ENTAAGMCYTSGTTGDPKGvlySHRsNVLHALMANNG--DALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPgA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 293 RFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKpdLSSLKIVFVSGSQLgAELATRALGDLGPVIYNMYGSTEV 372
Cdd:PRK06018 254 KLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLK--LPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 373 A-----------FATIAGPKDLQFNpSTVGPVVKGVTVKILDENGNEVPQG--AVGRIFVGNAFPFEGYTGGGGKQI-ID 438
Cdd:PRK06018 331 SplgtlaalkppFSKLPGDARLDVL-QKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYRVDGEILdDD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 439 GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDE 518
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 801237227 519 DTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PRK06018 490 EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
268-552 |
2.48e-44 |
|
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: 160.16 E-value: 2.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 268 PMFHaLGYMHAALAMFL-GSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILdQLEKTEpKPDLSSLKivFVSGSQ 346
Cdd:cd17636 49 PLFH-IGTLMFTLATFHaGGTNVFVRRVDAEEVLELIEAERCTHAFLLPPTIDQIV-ELNADG-LYDLSSLR--SSPAAP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 347 LGAELATralGDLGPVIYNM--YGSTEV----AFATIAGPkdlqfNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVG 420
Cdd:cd17636 124 EWNDMAT---VDTSPWGRKPggYGQTEVmglaTFAALGGG-----AIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVAR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 421 NAFPFEGYTGG---GGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDD 497
Cdd:cd17636 196 GPTVMAGYWNRpevNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPD 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 801237227 498 KEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKV 552
Cdd:cd17636 276 PRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
75-559 |
2.92e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 164.73 E-value: 2.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVS 154
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 DREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGS---SDETLAELIAHSS---TAPAPKASRRASIIILTS 228
Cdd:PRK08162 112 RHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGrfiGALDYEAFLASGDpdfAWTLPADEWDAIALNYTS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 229 GTTGTPKGA---NRNTppTLAPIGGILS-HVPFKAgeVTLLPSPMFHALGYMHA-ALAMfLGSTLVLRRRFKPALVLEDI 303
Cdd:PRK08162 192 GTTGNPKGVvyhHRGA--YLNALSNILAwGMPKHP--VYLWTLPMFHCNGWCFPwTVAA-RAGTNVCLRKVDPKLIFDLI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 304 EKHKATSMVVVPVMLSRILDQLEktEPKPDLSSLKIVFVSGSQLGAEL--ATRALG-DLGPViynmYGSTEVafatiagp 380
Cdd:PRK08162 267 REHGVTHYCGAPIVLSALINAPA--EWRAGIDHPVHAMVAGAAPPAAViaKMEEIGfDLTHV----YGLTET-------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 381 kdlqFNPSTVG-------------------------PVVKGVTVkiLD-ENGNEVPQGA--VGRIFV-GNAFpFEGY--- 428
Cdd:PRK08162 333 ----YGPATVCawqpewdalplderaqlkarqgvryPLQEGVTV--LDpDTMQPVPADGetIGEIMFrGNIV-MKGYlkn 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 429 ---TGgggKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLR 505
Cdd:PRK08162 406 pkaTE---EAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPC 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 801237227 506 AFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFlDELPRNPTGKVLKRELRK 559
Cdd:PRK08162 483 AFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLRE 535
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
69-528 |
8.37e-44 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 164.50 E-value: 8.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVIDEEG----TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSE 144
Cdd:COG1022 19 RRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 145 FSGPQIKEVSDREGAKVIIYDDE--YTKAVSlAQPPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTAPAPKA--SRR 220
Cdd:COG1022 99 SSAEEVAYILNDSGAKVLFVEDQeqLDKLLE-VRDELPSLRHIVVLDPRGLRDDPRLLSLDELLALGREVADPAEleARR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 221 ASI-------IILTSGTTGTPKGA---NRNtppTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVL 290
Cdd:COG1022 178 AAVkpddlatIIYTSGTTGRPKGVmltHRN---LLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYALAAGATVAF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 291 RRRfkPALVLEDIEKHKATSMVVVP----VMLSRILDQLEKTEP----------------------KPDLSSL------- 337
Cdd:COG1022 255 AES--PDTLAEDLREVKPTFMLAVPrvweKVYAGIQAKAEEAGGlkrklfrwalavgrryararlaGKSPSLLlrlkhal 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 338 --KIVF--------------VSGSQ-LGAELAT--RALGdlgpV-IYNMYGSTEVAfATIAGPKDLQFNPSTVGPVVKGV 397
Cdd:COG1022 333 adKLVFsklrealggrlrfaVSGGAaLGPELARffRALG----IpVLEGYGLTETS-PVITVNRPGDNRIGTVGPPLPGV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 398 TVKIlDENGnEV----PQgaVgrifvgnafpFEGY------TggggKQII--DGLLSSGDVGYFDERGLLYVSGRDDEMI 465
Cdd:COG1022 408 EVKI-AEDG-EIlvrgPN--V----------MKGYyknpeaT----AEAFdaDGWLHTGDIGELDEDGFLRITGRKKDLI 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 801237227 466 V-SGGENVFPAEVEDLISGHPDVVEAAAIGvDDKEFgarLRAFVVkkpgadLDEDTIKQYVRDH 528
Cdd:COG1022 470 VtSGGKNVAPQPIENALKASPLIEQAVVVG-DGRPF---LAALIV------PDFEALGEWAEEN 523
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
46-558 |
1.19e-43 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 163.27 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 46 PPLNYAALAAdirkwgevgmLPSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFV 125
Cdd:PRK07059 18 DASQYPSLAD----------LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 126 IANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDDEYTKAVS--LAQPP------------LGkLRALGVN--- 188
Cdd:PRK07059 88 VAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQqvLAKTAvkhvvvasmgdlLG-FKGHIVNfvv 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 189 -------PDDDKPSGSS-DETLAELiAHSSTAPAPKASRRASIIILTSGTTGTPKGA---NRNTPPTLAPIGGILSHVPF 257
Cdd:PRK07059 167 rrvkkmvPAWSLPGHVRfNDALAEG-ARQTFKPVKLGPDDVAFLQYTGGTTGVSKGAtllHRNIVANVLQMEAWLQPAFE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 258 KAGEV----TLLPSPMFH--ALGyMHAALAMFLGSTLVL--RRRFKPALVLEdIEKHKATSMVVVPVMLSRILDQLEKte 329
Cdd:PRK07059 246 KKPRPdqlnFVCALPLYHifALT-VCGLLGMRTGGRNILipNPRDIPGFIKE-LKKYQVHIFPAVNTLYNALLNNPDF-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 330 PKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEV 409
Cdd:PRK07059 322 DKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 410 PQGAVGRIFVGNAFPFEGY------TGgggKQII-DGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLIS 482
Cdd:PRK07059 402 PLGEPGEICIRGPQVMAGYwnrpdeTA---KVMTaDGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 801237227 483 GHPDVVEAAAIGVDDKEFGARLRAFVVKKpGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK07059 479 SHPGVLEVAAVGVPDEHSGEAVKLFVVKK-DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
86-539 |
1.26e-43 |
|
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: 161.22 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYD 165
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 166 DeytkavslaqpplgklralgvnPDDdkpsgssdetLAeliahsstapapkasrrasIIILTSGTTGTPKGA---NRNTp 242
Cdd:cd05907 85 D----------------------PDD----------LA-------------------TIIYTSGTTGRPKGVmlsHRNI- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 243 ptLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVLRRRFKpaLVLEDIEKHKATSMVVVPVMLSRI 321
Cdd:cd05907 113 --LSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLaGARIYFASSAE--TLLDDLSEVRPTVFLAVPRVWEKV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 322 LDQLEKTEPKPD---------LSSLKIVFVSGSQLGAELATRALGdLGPVIYNMYGSTEV-AFATIAGPKDLQFNpsTVG 391
Cdd:cd05907 189 YAAIKVKAVPGLkrklfdlavGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETsAVVTLNPPGDNRIG--TVG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 392 PVVKGVTVKILDEngnevpqgavGRIFVGNAFPFEGYTG--GGGKQII--DGLLSSGDVGYFDERGLLYVSGRDDEMIV- 466
Cdd:cd05907 266 KPLPGVEVRIADD----------GEILVRGPNVMLGYYKnpEATAEALdaDGWLHTGDLGEIDEDGFLHITGRKKDLIIt 335
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 801237227 467 SGGENVFPAEVEDLISGHPDVVEAAAIGvDDKEFgarLRAFVVkkpgadLDEDTIKQYVRDHLARYKVPREVI 539
Cdd:cd05907 336 SGGKNISPEPIENALKASPLISQAVVIG-DGRPF---LVALIV------PDPEALEAWAEEHGIAYTDVAELA 398
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
75-557 |
5.87e-43 |
|
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: 159.76 E-value: 5.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAI-LARNHRWfVIANYGAARVGARIILLNSEFSGPQIKEV 153
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVyLPRSARL-VAAMLAVLKAGAAYVPLDPDYPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 154 SDREGAKVIIYDDEytkavsLAQPPLGKLRALGVNPDDDKPSGSSdetlaeliahsstAPAPKASRRASIIILTSGTTGT 233
Cdd:cd12116 80 LEDAEPALVLTDDA------LPDRLPAGLPVLLLALAAAAAAPAA-------------PRTPVSPDDLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 234 PKG---ANRNTPPTLAPIGGILShvpFKAGEVTL-LPSPMFHAlgymhAALAMFL----GSTLVLRRR---FKPALVLED 302
Cdd:cd12116 141 PKGvvvSHRNLVNFLHSMRERLG---LGPGDRLLaVTTYAFDI-----SLLELLLpllaGARVVIAPRetqRDPEALARL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 303 IEKHKATSMVVVPVMLSRILDqlekTEPKPdLSSLKIVfVSGSQLGAELAtRALGDLGPVIYNMYGSTEvafATI---AG 379
Cdd:cd12116 213 IEAHSITVMQATPATWRMLLD----AGWQG-RAGLTAL-CGGEALPPDLA-ARLLSRVGSLWNLYGPTE---TTIwstAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 PKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNA----------------FPFEGYTGGGGKqiidgLLSS 443
Cdd:cd12116 283 RVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDgvaqgylgrpaltaerFVPDPFAGPGSR-----LYRT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 444 GDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIgVDDKEFGARLRAFVVKKPGADLDEDTIKQ 523
Cdd:cd12116 358 GDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDAAALRA 436
|
490 500 510
....*....|....*....|....*....|....
gi 801237227 524 YVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd12116 437 HLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
227-560 |
6.57e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 156.87 E-value: 6.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 TSGTTGTPKGAnRNTPPTLAPIGGILSHVP-FKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVLRRRF---KPALVLE 301
Cdd:cd05944 10 TGGTTGTPKLA-QHTHSNEVYNAWMLALNSlFDPDDVLLCGLPLFHVNGSVVTLLTPLAsGAHVVLAGPAgyrNPGLFDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 302 D---IEKHKATSMVVVPVMLSRILdqleKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIA 378
Cdd:cd05944 89 FwklVERYRITSLSTVPTVYAALL----QVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 379 GPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQ-----GAVGRIFVGNAFPFEGYTGGGGKQII---DGLLSSGDVGYFD 450
Cdd:cd05944 165 NPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLrdcapDEVGEICVAGPGVFGGYLYTEGNKNAfvaDGWLNTGDLGRLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 451 ERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLA 530
Cdd:cd05944 245 ADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARDHVP 324
|
330 340 350
....*....|....*....|....*....|.
gi 801237227 531 -RYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:cd05944 325 eRAAVPKHIEVLEELPVTAVGKVFKPALRAD 355
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
71-558 |
6.86e-43 |
|
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: 165.03 E-value: 6.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGA------------RI 138
Cdd:COG1020 486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAayvpldpaypaeRL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 139 --ILLNSefsgpqikevsdreGAKVIIYDDEYTKAVSLAQPPLgklralgVNPDDdkpsgssdetlAELIAHSSTAPAPK 216
Cdd:COG1020 566 ayMLEDA--------------GARLVLTQSALAARLPELGVPV-------LALDA-----------LALAAEPATNPPVP 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 217 ASRRASI-IILTSGTTGTPKG--------ANRntpptlapIGGILSHVPFKAGEVTLlpspMFHALGYMHAALAMFL--- 284
Cdd:COG1020 614 VTPDDLAyVIYTSGSTGRPKGvmvehralVNL--------LAWMQRRYGLGPGDRVL----QFASLSFDASVWEIFGall 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 285 -GSTLVLRR---RFKPALVLEDIEKHKATSMVVVPVMLSRILDqlektEPKPDLSSLKIVFVSGSQLGAELATRALGDL- 359
Cdd:COG1020 682 sGATLVLAPpeaRRDPAALAELLARHRVTVLNLTPSLLRALLD-----AAPEALPSLRLVLVGGEALPPELVRRWRARLp 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 360 GPVIYNMYGSTEVA-FATIA--GPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVG---------------- 420
Cdd:COG1020 757 GARLVNLYGPTETTvDSTYYevTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGgaglargylnrpelta 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 421 -----NAFPFEG---Y-TggggkqiidgllssGDVGYFDERGLLYVSGRDDEMI-VSGgenvF---PAEVEDLISGHPDV 487
Cdd:COG1020 837 erfvaDPFGFPGarlYrT--------------GDLARWLPDGNLEFLGRADDQVkIRG----FrieLGEIEAALLQHPGV 898
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801237227 488 VEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:COG1020 899 REAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
84-560 |
3.00e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 159.10 E-value: 3.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 84 EGTL---TFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAK 160
Cdd:PRK07008 34 EGDIhryTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 161 VIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDK-PSGS----SDETLAEliAHSSTAPAPK-ASRRASIIILTSGTTGTP 234
Cdd:PRK07008 114 YVLFDLTFLPLVDALAPQCPNVKGWVAMTDAAHlPAGStpllCYETLVG--AQDGDYDWPRfDENQASSLCYTSGTTGNP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 235 KGA---NRNTppTLAPIGGILSHVPFKAGEVTLLP-SPMFH--ALGYMHAAlAMfLGSTLVLRrrfKPAL----VLEDIE 304
Cdd:PRK07008 192 KGAlysHRST--VLHAYGAALPDAMGLSARDAVLPvVPMFHvnAWGLPYSA-PL-TGAKLVLP---GPDLdgksLYELIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 305 KHKATSMVVVPVMLSRILDQLEKTEPKpdLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVA-FATIAGP--K 381
Cdd:PRK07008 265 AERVTFSAGVPTVWLGLLNHMREAGLR--FSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSpLGTLCKLkwK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 382 DLQFNPSTV-------GPVVKGVTVKILDENGNEVPQGAV--GRIFVGNAFPFEGYTGGGGKQIIDGLLSSGDVGYFDER 452
Cdd:PRK07008 343 HSQLPLDEQrkllekqGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYFRGDASPLVDGWFPTGDVATIDAD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 453 GLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARY 532
Cdd:PRK07008 423 GFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKW 502
|
490 500
....*....|....*....|....*...
gi 801237227 533 KVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK07008 503 WIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
79-560 |
4.91e-42 |
|
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: 158.46 E-value: 4.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 79 AVIDEEgtLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEF-----------SG 147
Cdd:cd17642 39 AHTGVN--YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYnereldhslniSK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQIKEVSDREGAKVIiyddeytkAVSLAQPPLGKLRALGVNPD------DDKPSGSSDEtlAELIAHSSTAPAPKASRRA 221
Cdd:cd17642 117 PTIVFCSKKGLQKVL--------NVQKKLKIIKTIIILDSKEDykgyqcLYTFITQNLP--PGFNEYDFKPPSFDRDEQV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 222 SIIILTSGTTGTPKG---ANRNTPPTLA----PIGG--------ILSHVPFKAGevtllpSPMFHALGYMhaalamFLGS 286
Cdd:cd17642 187 ALIMNSSGSTGLPKGvqlTHKNIVARFShardPIFGnqiipdtaILTVIPFHHG------FGMFTTLGYL------ICGF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 287 TLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSrILDQLEKTEpKPDLSSLKIVFVSGSQLGAELATRALGDLG-PVIYN 365
Cdd:cd17642 255 RVVLMYKFEEELFLRSLQDYKVQSALLVPTLFA-FFAKSTLVD-KYDLSNLHEIASGGAPLSKEVGEAVAKRFKlPGIRQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 366 MYGSTEVAFATIAGPkDLQFNPSTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGYTGG--GGKQII--DGL 440
Cdd:cd17642 333 GYGLTETTSAILITP-EGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNpeATKALIdkDGW 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 441 LSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDT 520
Cdd:cd17642 412 LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKE 491
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 801237227 521 IKQYVRDHLARYKVPR-EVIFLDELPRNPTGKVLKRELRKL 560
Cdd:cd17642 492 VMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
68-558 |
6.30e-42 |
|
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: 159.19 E-value: 6.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 68 SHNARRAPNRAAVI--DEEG---TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLN 142
Cdd:cd05968 68 DKWLADTRTRPALRweGEDGtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 143 SEF-SGPQIKEVSDREgAKVIIYDDEYT---KAVSL---------AQPPLGKL---RALGvnpDDDKPSGSSDETLAELI 206
Cdd:cd05968 148 SGFgKEAAATRLQDAE-AKALITADGFTrrgREVNLkeeadkacaQCPTVEKVvvvRHLG---NDFTPAKGRDLSYDEEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 207 AhsstAPAPKASRRAS----IIILTSGTTGTPKGAnrntpptlapiggilSHV----PFKAGEVTLLPSPM--------F 270
Cdd:cd05968 224 E----TAGDGAERTESedplMIIYTSGTTGKPKGT---------------VHVhagfPLKAAQDMYFQFDLkpgdlltwF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 271 HALGYMHAALAMF----LGSTLVLRRRF----KPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFV 342
Cdd:cd05968 285 TDLGWMMGPWLIFggliLGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 343 SGSQLGAE----LATRALGDLGPVIyNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPqGAVGRIF 418
Cdd:cd05968 365 TGEPWNPEpwnwLFETVGKGRNPII-NYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPAR-PEVGELV 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 419 VGNAFPfeGYTGGGGK----------QIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVV 488
Cdd:cd05968 443 LLAPWP--GMTRGFWRdedryletywSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVL 520
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 801237227 489 EAAAIGVDDKEFGARLRAFVVKKPGADLDE---DTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:cd05968 521 ESAAIGVPHPVKGEAIVCFVVLKPGVTPTEalaEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
86-558 |
1.19e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 157.73 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAK-GVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIY 164
Cdd:PRK08751 50 TITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 165 DDEYTKAVS--LAQPPLGKLRALGVNPDDDKPSGS-------------SDETLA------ELIAHSSTAPAPK---ASRR 220
Cdd:PRK08751 130 IDNFGTTVQqvIADTPVKQVITTGLGDMLGFPKAAlvnfvvkyvkklvPEYRINgairfrEALALGRKHSMPTlqiEPDD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 221 ASIIILTSGTTGTPKGA---NRNTPPTLAPIGGILSHV-PFKAG-EVTLLPSPMFHALGYMHAALA-MFLG--STLVLRR 292
Cdd:PRK08751 210 IAFLQYTGGTTGVAKGAmltHRNLVANMQQAHQWLAGTgKLEEGcEVVITALPLYHIFALTANGLVfMKIGgcNHLISNP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 293 RFKPALVLEdIEKHKATSMVVVPVMLSRIL-----DQLektepkpDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMY 367
Cdd:PRK08751 290 RDMPGFVKE-LKKTRFTAFTGVNTLFNGLLntpgfDQI-------DFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 368 GSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY--TGGGGKQIID--GLLSS 443
Cdd:PRK08751 362 GLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYwkRPEETAKVMDadGWLHT 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 444 GDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGAdLDEDTIKQ 523
Cdd:PRK08751 442 GDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA-LTAEDVKA 520
|
490 500 510
....*....|....*....|....*....|....*
gi 801237227 524 YVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK08751 521 HARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
69-535 |
1.44e-41 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 155.80 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIAnYGAA-RVGARIILLNSEFSG 147
Cdd:PRK09029 11 HWAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLA-YLALlQCGARVLPLNPQLPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQIKEVSDREGAKVIIYDDEytkavSLAQPPLGKLRALGVNpdddkpsgssdetlaeliahsSTAPAPKASRRASIIILT 227
Cdd:PRK09029 90 PLLEELLPSLTLDFALVLEG-----ENTFSALTSLHLQLVE---------------------GAHAVAWQPQRLATMTLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 228 SGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFH--ALGYMHAALAMflGSTLVLRrrfKPALVLEDIEk 305
Cdd:PRK09029 144 SGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHvsGQGIVWRWLYA--GATLVVR---DKQPLEQALA- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 306 hKATSMVVVPVMLSRILDQLEKTepkpdlSSLKIVFVSGSQLGAELaTRALGDLGPVIYNMYGSTEVAFATIAGPKDlqf 385
Cdd:PRK09029 218 -GCTHASLVPTQLWRLLDNRSEP------LSLKAVLLGGAAIPVEL-TEQAEQQGIRCWCGYGLTEMASTVCAKRAD--- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 386 NPSTVGPVVKGVTVKILDengnevpqgavGRIFVGNAFPFEGYTGGGgkQII-----DGLLSSGDVGYFDErGLLYVSGR 460
Cdd:PRK09029 287 GLAGVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQG--QLVplvndEGWFATRDRGEWQN-GELTILGR 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 801237227 461 DDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEdtIKQYVRDHLARYKVP 535
Cdd:PRK09029 353 LDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVN--LAEWLQDKLARFQQP 425
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
71-558 |
2.16e-41 |
|
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: 156.89 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVI-----DEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEF 145
Cdd:cd05970 27 AKEYPDKLALVwcddaGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 146 SGPQIKEVSDREGAKVIIYDDE--YTKAVSLAQPPLGKLRALgVNPDDDKPSGSSDetLAELIAHSS------TAPAPKA 217
Cdd:cd05970 107 TAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKL-VWVGDPVPEGWID--FRKLIKNASpdferpTANSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 218 SRRASIIILTSGTTGTPKGANRNTpptLAPIGGILS-----HVPFKAGEVTLLPSPMFHAL-----GYMHAALAMFLGSt 287
Cdd:cd05970 184 GEDILLVYFSSGTTGMPKMVEHDF---TYPLGHIVTakywqNVREGGLHLTVADTGWGKAVwgkiyGQWIAGAAVFVYD- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 288 lvlRRRFKPALVLEDIEKHKATSMVVVPVMLsRILDQlEKTEpKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMY 367
Cdd:cd05970 260 ---YDKFDPKALLEKLSKYGVTTFCAPPTIY-RFLIR-EDLS-RYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 368 GSTEVAFaTIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFV--GNAFP---FEGYTGGGGKQ---IIDG 439
Cdd:cd05970 334 GQTETTL-TIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtSKGKPvglFGGYYKDAEKTaevWHDG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 440 LLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVV----KKPGAD 515
Cdd:cd05970 413 YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakgYEPSEE 492
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 801237227 516 LdEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:cd05970 493 L-KKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
71-559 |
2.55e-41 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 157.34 E-value: 2.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK08279 47 AARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTapAPKASRRASII------ 224
Cdd:PRK08279 127 AHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPT--TNPASRSGVTAkdtafy 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 225 ILTSGTTGTPKGAN---RNTPPTLAPIGGILShvpFKAGEVTLLPSPMFHALGYMHA---ALAMflGSTLVLRRRFKPAL 298
Cdd:PRK08279 205 IYTSGTTGLPKAAVmshMRWLKAMGGFGGLLR---LTPDDVLYCCLPLYHNTGGTVAwssVLAA--GATLALRRKFSASR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 299 VLEDIEKHKATSMVVVPVMLSRILDQlektEPKPDLSSLKIVFVSGSQLGAEL----ATRalgdLG-PVIYNMYGSTE-- 371
Cdd:PRK08279 280 FWDDVRRYRATAFQYIGELCRYLLNQ----PPKPTDRDHRLRLMIGNGLRPDIwdefQQR----FGiPRILEFYAASEgn 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 372 VAFATIagpkdlqFN-PSTVG--PVVKGVTVKIL-----------DENGN--EVPQG----AVGRIfvGNAFPFEGYTGG 431
Cdd:PRK08279 352 VGFINV-------FNfDGTVGrvPLWLAHPYAIVkydvdtgepvrDADGRciKVKPGevglLIGRI--TDRGPFDGYTDP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 432 GG--KQIIDGLLSSGDVgYFDERGLLyvsgRDDEMivsG---------------GENVFPAEVEDLISGHPDVVEAAAIG 494
Cdd:PRK08279 423 EAseKKILRDVFKKGDA-WFNTGDLM----RDDGF---GhaqfvdrlgdtfrwkGENVATTEVENALSGFPGVEEAVVYG 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 801237227 495 VDDKEFGARL-RAFVVKKPGADLDEDTIKQYVRDHLARYKVPrevIFL---DELPRNPTGKVLKRELRK 559
Cdd:PRK08279 495 VEVPGTDGRAgMAAIVLADGAEFDLAALAAHLYERLPAYAVP---LFVrlvPELETTGTFKYRKVDLRK 560
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
69-559 |
3.59e-41 |
|
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: 154.00 E-value: 3.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILA-RNHRWfVIANYGAARVGARIILLNSEFSG 147
Cdd:cd17653 5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSdRSLEM-LVAILAILKAGAAYVPLDAKLPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQIKEVSDREGAKVIIYDDeytkavslaqpplgklralgvNPDDDkpsgssdetlaeliahsstapapkasrraSIIILT 227
Cdd:cd17653 84 ARIQAILRTSGATLLLTTD---------------------SPDDL-----------------------------AYIIFT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 228 SGTTGTPKGanrntppTLAPIGGILSHVPFKAGEVTLLP--------SPMFHA-LGYMHAALAMflGSTLVLRrrfKPAL 298
Cdd:cd17653 114 SGSTGIPKG-------VMVPHRGVLNYVSQPPARLDVGPgsrvaqvlSIAFDAcIGEIFSTLCN--GGTLVLA---DPSD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 299 VLEDIEKHKATSMVVvPVMLSrildqlekTEPKPDLSSLKIVFVSGSQLGAELATRALGdlGPVIYNMYGSTEVAFaTIA 378
Cdd:cd17653 182 PFAHVARTVDALMST-PSILS--------TLSPQDFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTI-SST 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 379 GPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG--------------GGGKQIidglLSSG 444
Cdd:cd17653 250 MTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGnpaltaskfvpdpfWPGSRM----YRTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 445 DVGYFDERGLLYVSGRDDEMIVSGGENV-FPAEVEDLISGHPDVVEAAAIGVDDkefgaRLRAFVVkkPgADLDEDTIKQ 523
Cdd:cd17653 326 DYGRWTEDGGLEFLGREDNQVKVRGFRInLEEIEEVVLQSQPEVTQAAAIVVNG-----RLVAFVT--P-ETVDVDGLRS 397
|
490 500 510
....*....|....*....|....*....|....*.
gi 801237227 524 YVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:cd17653 398 ELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
224-552 |
3.89e-41 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 151.64 E-value: 3.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 IILTSGTTGTPKGANRNTPPTLAPIGGILSHV-PFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKP-ALVLE 301
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTyKSLFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 302 DIEKHKATSMVVVPVMLSRILdqLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPK 381
Cdd:cd17635 86 ILTTNAVTTTCLVPTLLSKLV--SELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 382 DLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ---IIDGLLSSGDVGYFDERGLLYVS 458
Cdd:cd17635 164 DDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTaevLIDGWVNTGDLGERREDGFLFIT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 459 GRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKpgADLDEDTI---KQYVRDHLARYKVP 535
Cdd:cd17635 244 GRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS--AELDENAIralKHTIRRELEPYARP 321
|
330
....*....|....*..
gi 801237227 536 REVIFLDELPRNPTGKV 552
Cdd:cd17635 322 STIVIVTDIPRTQSGKV 338
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
75-557 |
7.61e-41 |
|
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: 153.97 E-value: 7.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAI-LARNHRWfVIANYGAARVGARIILLNSEFSGPQIKEV 153
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVtLPKGPEQ-VVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 154 SDREGAKVIIYDDEYTKAVSLAQPplgklralgVNPDDDKPSGSSDETLAELIAHSSTApapkasrrasIIILTSGTTGT 233
Cdd:cd12114 80 LADAGARLVLTDGPDAQLDVAVFD---------VLILDLDALAAPAPPPPVDVAPDDLA----------YVIFTSGSTGT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 234 PKG------ANRNTpptlapIGGILSHVPFKAGEVTLLPSPMFHALG-Y-MHAALAmfLGSTLVL---RRRFKPALVLED 302
Cdd:cd12114 141 PKGvmishrAALNT------ILDINRRFAVGPDDRVLALSSLSFDLSvYdIFGALS--AGATLVLpdeARRRDPAHWAEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 303 IEKHKATSMVVVPVMLSRILDQLEktEPKPDLSSLKIVFVSGSQLGAELATRaLGDLGP--VIYNMYGSTEVAFATIAGP 380
Cdd:cd12114 213 IERHGVTLWNSVPALLEMLLDVLE--AAQALLPSLRLVLLSGDWIPLDLPAR-LRALAPdaRLISLGGATEASIWSIYHP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 381 KDLQfnPSTVGPVVKGV-----TVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGK------QIIDG--LLSSGDVG 447
Cdd:cd12114 290 IDEV--PPDWRSIPYGRplanqRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELtaarfvTHPDGerLYRTGDLG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 448 YFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEfGARLRAFVVKKPGAD-LDEDTIKQYVR 526
Cdd:cd12114 368 RYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPDNDGTpIAPDALRAFLA 446
|
490 500 510
....*....|....*....|....*....|.
gi 801237227 527 DHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd12114 447 QTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
73-560 |
7.73e-40 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 152.45 E-value: 7.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 73 RAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGarIILLNSEFS------ 146
Cdd:PRK10946 35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFShqrsel 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 147 ---GPQIKE---VSDREGAkvIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDkpsgssdetLAELIAHSSTA--PAPKAS 218
Cdd:PRK10946 113 nayASQIEPallIADRQHA--LFSDDDFLNTLVAEHSSLRVVLLLNDDGEHS---------LDDAINHPAEDftATPSPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 219 RRASIIILTSGTTGTPKganrNTPPT----------LAPIGGILSHVPF----KAGEVTLLPSPmfHALGYMHAalamfl 284
Cdd:PRK10946 182 DEVAFFQLSGGSTGTPK----LIPRThndyyysvrrSVEICGFTPQTRYlcalPAAHNYPMSSP--GALGVFLA------ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 285 GSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIY 364
Cdd:PRK10946 250 GGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 365 NMYGSTE--VAFATIAGPKDLQFNpsTVG-PVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY--TGGGGKQIID- 438
Cdd:PRK10946 330 QVFGMAEglVNYTRLDDSDERIFT--TQGrPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYykSPQHNASAFDa 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 439 -GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAF-VVKKPgadL 516
Cdd:PRK10946 408 nGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFlVVKEP---L 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 801237227 517 DEDTIKQYVRDH-LARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK10946 485 KAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQW 529
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
88-492 |
1.46e-39 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 148.95 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 88 TFSELDEAAHAVANGLLA-KGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDD 166
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 167 EYTKAVSLAQPPLGKLRALGVNPDDDkpsGSSDETLAELIAHSSTApapkasrrasIIILTSGTTGTPKGA---NRNtpp 243
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDD---APAPPPPDAPSGPDDLA----------YVIYTSGSTGRPKGVvvtHRS--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 244 TLAPIGGILSHVPFKAGEVTLlpspMFHALGYMHAALAMFL----GSTLVL----RRRFKPALVLEDIEKHKATSMVVVP 315
Cdd:TIGR01733 145 LVNLLAWLARRYGLDPDDRVL----QFASLSFDASVEEIFGallaGATLVVppedEERDDAALLAALIAEHPVTVLNLTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 316 VMLSRILDQLEktepkPDLSSLKIVFVSGSQLGAELATRALGDLGPV-IYNMYGSTE----VAFATIAGPKDLQFNPSTV 390
Cdd:TIGR01733 221 SLLALLAAALP-----PALASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTEttvwSTATLVDPDDAPRESPVPI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 391 GPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGK---QIIDGLLS---------SGDVGYFDERGLLYVS 458
Cdd:TIGR01733 296 GRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELtaeRFVPDPFAggdgarlyrTGDLVRYLPDGNLEFL 375
|
410 420 430
....*....|....*....|....*....|....
gi 801237227 459 GRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAA 492
Cdd:TIGR01733 376 GRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
71-558 |
1.29e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 149.02 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELdeAAHAVANGLLAKGVRAGDG---VAILARNHRWFVIANYGAARVGARIILLNSEFSG 147
Cdd:PRK13388 11 DRAGDDTIAVRYGDRTWTWREV--LAEAAARAAALIALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQIKEVSDREGAKVIIYDDEYtkavslaqppLGKLRALGVnPDDDKPSGSSDETLAELIAHSSTAPAPKASRRAS-IIIL 226
Cdd:PRK13388 89 AALAADIRRADCQLLVTDAEH----------RPLLDGLDL-PGVRVLDVDTPAYAELVAAAGALTPHREVDAMDPfMLIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 TSGTTGTPKgANRNTPPTLAPIGGIL----SHVpfkAGEVTLLPSPMFHALGYMHA-ALAMFLGSTLVLRRRFKPALVLE 301
Cdd:PRK13388 158 TSGTTGAPK-AVRCSHGRLAFAGRALterfGLT---RDDVCYVSMPLFHSNAVMAGwAPAVASGAAVALPAKFSASGFLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 302 DIEKHKATSMVVVPVMLSRILDQLEKtePKPDLSSLKIVFvsGSQLG----AELATRalgdLGPVIYNMYGSTEVAFATI 377
Cdd:PRK13388 234 DVRRYGATYFNYVGKPLAYILATPER--PDDADNPLRVAF--GNEASprdiAEFSRR----FGCQVEDGYGSSEGAVIVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 378 AGPkdlQFNPSTVGPVVKGVT-----------VKILDENGNEV-PQGAVGRIF-VGNAFPFEGY---TGGGGKQIIDGLL 441
Cdd:PRK13388 306 REP---GTPPGSIGRGAPGVAiynpetltecaVARFDAHGALLnADEAIGELVnTAGAGFFEGYynnPEATAERMRHGMY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 442 SSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTI 521
Cdd:PRK13388 383 WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAF 462
|
490 500 510
....*....|....*....|....*....|....*....
gi 801237227 522 KQYV--RDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK13388 463 AAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
83-559 |
1.50e-38 |
|
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: 148.38 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 83 EEGTLTFSELDEAAHAVANGLL-AKGVRAGDGVA-ILARNHRWFVIaNYGAARVGARIILLNSEFSGPQIKEVSDREGAK 160
Cdd:cd05928 38 DEVKWSFRELGSLSRKAANVLSgACGLQRGDRVAvILPRVPEWWLV-NVACIRTGLVFIPGTIQLTAKDILYRLQASKAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 161 VIIYDDEYTKAVS--LAQPPLGKLRALgVNPDDDKPSGSsdetLAELIAHSSTAP--APKASRRASIIILTSGTTGTPKG 236
Cdd:cd05928 117 CIVTSDELAPEVDsvASECPSLKTKLL-VSEKSRDGWLN----FKELLNEASTEHhcVETGSQEPMAIYFTSGTTGSPKM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 237 ANRntpptlapiggilSH----VPFKAGE---VTLLPSPMFHAL---GYMHAAL-----AMFLGSTLVLRR--RFKPALV 299
Cdd:cd05928 192 AEH-------------SHsslgLGLKVNGrywLDLTASDIMWNTsdtGWIKSAWsslfePWIQGACVFVHHlpRFDPLVI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVMLsRILDQLEKTEPKpdLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFaTIAG 379
Cdd:cd05928 259 LKTLSSYPITTFCGAPTVY-RMLVQQDLSSYK--FPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGL-ICAN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 PKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIF--VGNAFP---FEGYTGGGGK--QIIDG-LLSSGDVGYFDE 451
Cdd:cd05928 335 FKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGirVKPIRPfglFSGYVDNPEKtaATIRGdFYLTGDRGIMDE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 452 RGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKP---GADLDEDT--IKQYVR 526
Cdd:cd05928 415 DGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPqflSHDPEQLTkeLQQHVK 494
|
490 500 510
....*....|....*....|....*....|...
gi 801237227 527 DHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:cd05928 495 SVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
82-560 |
4.08e-38 |
|
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: 146.71 E-value: 4.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 82 DEEGT-LTFSELDEAAHAVANgLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAK 160
Cdd:cd05909 2 DTLGTsLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 161 VIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTAP--------APKASRRASIIILTSGTTG 232
Cdd:cd05909 81 TVLTSKQFIEKLKLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKFPPKwllrifgvAPVQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 233 TPKG---ANRNtppTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVLrrRFKP---ALVLEDIEK 305
Cdd:cd05909 161 LPKGvvlSHKN---LLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLsGIKVVF--HPNPldyKKIPELIYD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 306 HKATSMVVVPVMLSRILdqleKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQF 385
Cdd:cd05909 236 KKATILLGTPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQSPN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 386 NPSTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFV-GNAFpFEGYTG---GGGKQIIDGLLSSGDVGYFDERGLLYVSGR 460
Cdd:cd05909 312 KEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVrGPNV-MLGYLNepeLTSFAFGDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 461 DDEMIVSGGENVFPAEVEDLISGH-PDVVEAAAIGVDDKEFGARLRAFVVKKpgaDLDEDTIKQYVRDH-LARYKVPREV 538
Cdd:cd05909 391 LSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTT---DTDPSSLNDILKNAgISNLAKPSYI 467
|
490 500
....*....|....*....|..
gi 801237227 539 IFLDELPRNPTGKVLKRELRKL 560
Cdd:cd05909 468 HQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
86-559 |
1.82e-36 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 142.81 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNhrwfvIANYGAARVGarIILLNSEFSGP-------QIKEVSDREG 158
Cdd:PLN02330 55 AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPN-----VAEYGIVALG--IMAAGGVFSGAnptalesEIKKQAEAAG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 159 AKVIIYDD-EYTKAVSLAQPP--LGKLR-ALGVNPDD--DKPSGSSDETLAELIAHSSTAPAPkasrrasiiiLTSGTTG 232
Cdd:PLN02330 128 AKLIVTNDtNYGKVKGLGLPVivLGEEKiEGAVNWKEllEAADRAGDTSDNEEILQTDLCALP----------FSSGTTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 233 TPKG---ANRNTPPTLApiGGILSHVPFKAGEVTLLP-SPMFHALGYMHAALAMFLGS-TLVLRRRFKPALVLEDIEKHK 307
Cdd:PLN02330 198 ISKGvmlTHRNLVANLC--SSLFSVGPEMIGQVVTLGlIPFFHIYGITGICCATLRNKgKVVVMSRFELRTFLNALITQE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 308 AT-SMVVVPVMLSRILDQLEKtepKPDLSSLKI--VFVSGSQLGAELATRALGDLGPV-IYNMYGSTEVAFATI--AGPK 381
Cdd:PLN02330 276 VSfAPIVPPIILNLVKNPIVE---EFDLSKLKLqaIMTAAAPLAPELLTAFEAKFPGVqVQEAYGLTEHSCITLthGDPE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 382 DLQ--FNPSTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGYTGGG---GKQI-IDGLLSSGDVGYFDERGL 454
Cdd:PLN02330 353 KGHgiAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKeetDRTIdEDGWLHTGDIGYIDDDGD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 455 LYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKV 534
Cdd:PLN02330 433 IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKK 512
|
490 500
....*....|....*....|....*
gi 801237227 535 PREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PLN02330 513 VRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
66-559 |
3.63e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 144.92 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 66 LPSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEF 145
Cdd:PRK12467 517 LIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 146 SGPQIKEVSDREGAKVIIYDDEytkavSLAQPPL-GKLRALGVNPDDDKPSGSSDEtlaeliaHSSTAPAPkasRRASII 224
Cdd:PRK12467 597 PQDRLAYMLDDSGVRLLLTQSH-----LLAQLPVpAGLRSLCLDEPADLLCGYSGH-------NPEVALDP---DNLAYV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 225 ILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRR---FKPALVLE 301
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAA 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 302 DIEKHKATSMVVVPVMLSRILDQLEKTEPKPdlssLKIVFVSGSQLGAELAT--RALGDlGPVIYNMYGSTEVAFATIAG 379
Cdd:PRK12467 742 LMADQGVTVLKIVPSHLQALLQASRVALPRP----QRALVCGGEALQVDLLArvRALGP-GARLINHYGPTETTVGVSTY 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 P---KDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQI---------IDG--LLSSGD 445
Cdd:PRK12467 817 ElsdEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAerfvpdpfgADGgrLYRTGD 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 446 VGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDkEFGARLRAFVVKKPGADLDE-----DT 520
Cdd:PRK12467 897 LARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPG-DAGLQLVAYLVPAAVADGAEhqatrDE 975
|
490 500 510
....*....|....*....|....*....|....*....
gi 801237227 521 IKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PRK12467 976 LKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
75-557 |
5.96e-36 |
|
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: 139.75 E-value: 5.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAI-LARnhrwfvianygaarvGARII--LLNSEFSGpqik 151
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALaLPR---------------SAELIvaLLAILKAG---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 152 evsdreGAKVIIyDDEYTKA-----VSLAQPplgklRALGVNPDDdkpsgssdetlaeliahsstapapkasrrASIIIL 226
Cdd:cd17643 62 ------GAYVPI-DPAYPVEriafiLADSGP-----SLLLTDPDD-----------------------------LAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 TSGTTGTPKGA---NRNTPPTLAPIGGILshvPFKAGEVTLlpspMFHALGY------MHAALAMflGSTLVL-----RR 292
Cdd:cd17643 101 TSGSTGRPKGVvvsHANVLALFAATQRWF---GFNEDDVWT----LFHSYAFdfsvweIWGALLH--GGRLVVvpyevAR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 293 rfKPALVLEDIEKHKATSMVVVPVMLSRILDQLEktEPKPDLSSLKIVFVSGSQLGAELATR---ALGDLGPVIYNMYGS 369
Cdd:cd17643 172 --SPEDFARLLRDEGVTVLNQTPSAFYQLVEAAD--RDGRDPLALRYVIFGGEALEAAMLRPwagRFGLDRPQLVNMYGI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 370 TEVA-FAT--IAGPKDLQ-FNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYT---------------G 430
Cdd:cd17643 248 TETTvHVTfrPLDAADLPaAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLgrpeltaerfvanpfG 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 431 GGGKQiidgLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVK 510
Cdd:cd17643 328 GPGSR----MYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVA 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 801237227 511 KPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17643 404 DDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
82-558 |
2.68e-35 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 139.65 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 82 DEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFsGPqiKEVSDR---EG 158
Cdd:PRK04319 69 SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAF-ME--EAVRDRledSE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 159 AKVIIYDDEYTKAVSLAQPPlgKLRA-LGVNPDDDKPSGSSDetLAELIAHSSTAPAPKASRRASIIIL--TSGTTGTPK 235
Cdd:PRK04319 146 AKVLITTPALLERKPADDLP--SLKHvLLVGEDVEEGPGTLD--FNALMEQASDEFDIEWTDREDGAILhyTSGSTGKPK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 236 GAnrntpptLAPIGGILSH-------VPFKAGEV---TLLP-----------SPMFHalgymhaalamflGSTLVLRR-R 293
Cdd:PRK04319 222 GV-------LHVHNAMLQHyqtgkyvLDLHEDDVywcTADPgwvtgtsygifAPWLN-------------GATNVIDGgR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 294 FKPALVLEDIEKHKATSMVVVPV---MLSRILDQLEKtepKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGST 370
Cdd:PRK04319 282 FSPERWYRILEDYKVTVWYTAPTairMLMGAGDDLVK---KYDLSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 371 EVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFP--FEGYTGGGGKQ---IIDGLLSSGD 445
Cdd:PRK04319 359 ETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPsmMRGIWNNPEKYesyFAGDWYVSGD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 446 VGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDED---TIK 522
Cdd:PRK04319 439 SAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElkeEIR 518
|
490 500 510
....*....|....*....|....*....|....*.
gi 801237227 523 QYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK04319 519 GFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
221-560 |
2.13e-34 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 135.51 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 221 ASIIILTSGTTGTPKGAnRNTPPTL-APIGGILSHvpFKAGEVT---LLPspMFHALGYMHAALAMFLGSTLVL--RRRF 294
Cdd:PRK07445 122 GWIMIPTGGSSGQIRFA-IHTWETLtASVQGFQRY--FQLQQVNsfcVLP--LYHVSGLMQFMRSFLTGGKLVIlpYKRL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 295 KPALVLEDiekhKATSMVV--VPVMLSRILdqlekTEPKPDLSSLKIVFVSGS----QLgAELATRALGDLGPViynmYG 368
Cdd:PRK07445 197 KSGQELPP----NPSDFFLslVPTQLQRLL-----QLRPQWLAQFRTILLGGApawpSL-LEQARQLQLRLAPT----YG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 369 STEVAfATIAG--PKD-LQFNPStVGPVVKGVTVKIldengnevPQGAVGRIFVGNAFPFEGYTggggKQIID--GLLSS 443
Cdd:PRK07445 263 MTETA-SQIATlkPDDfLAGNNS-SGQVLPHAQITI--------PANQTGNITIQAQSLALGYY----PQILDsqGIFET 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 444 GDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGaDLDEDTIKQ 523
Cdd:PRK07445 329 DDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKT 407
|
330 340 350
....*....|....*....|....*....|....*..
gi 801237227 524 YVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK07445 408 AIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
68-559 |
2.54e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.32 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 68 SHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSG 147
Cdd:PRK12316 2010 AEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPA 2089
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQIKEVSDREGAKVIIYDdeytKAVSLAQPPLGKLRALGVNPDddkpsgssdetlAELIAHSSTAPAPK-ASRRASIIIL 226
Cdd:PRK12316 2090 ERLAYMLEDSGAALLLTQ----RHLLERLPLPAGVARLPLDRD------------AEWADYPDTAPAVQlAGENLAYVIY 2153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 227 TSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPM----FHAlGYMHAALAmflGSTLVLR--RRFKPALVL 300
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFsfdgAHE-QWFHPLLN---GARVLIRddELWDPEQLY 2229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 301 EDIEKHKATSMVVVPVMLSRILDQLEKTEPKPdlsSLKIVFVSGSQLGAELATRALGDLGPV-IYNMYGSTEVAF----- 374
Cdd:PRK12316 2230 DEMERHGVTILDFPPVYLQQLAEHAERDGRPP---AVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVtpllw 2306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 375 -ATIAGPKDLQFNPstVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY----------------TGGGGKqii 437
Cdd:PRK12316 2307 kCRPQDPCGAAYVP--IGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYlnrpgltaerfvpdpfSASGER--- 2381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 438 dgLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEfGARLRAFVVKKPGADLD 517
Cdd:PRK12316 2382 --LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVVPDDAAEDL 2458
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 801237227 518 EDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PRK12316 2459 LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
83-557 |
2.19e-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: 133.57 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 83 EEGTLTFSELDEAAHAVANGLLAK-GVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKV 161
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 162 IIYDDEYTKAVslaQPPLGKLRALGVN----PDDDKPSGSsdETLAELIAHSSTAPAPKASRRAS------IIILTSGTT 231
Cdd:cd05938 82 LVVAPELQEAV---EEVLPALRADGVSvwylSHTSNTEGV--ISLLDKVDAASDEPVPASLRAHVtikspaLYIYTSGTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 232 GTPKGANRNTPPTLApIGGILSHVPFKAGEVTLLPSPMFHALGYMHAAL-AMFLGSTLVLRRRFKPALVLEDIEKHKATs 310
Cdd:cd05938 157 GLPKAARISHLRVLQ-CSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGgCIELGATCVLKPKFSASQFWDDCRKHNVT- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 311 mvvVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPV-IYNMYGSTE--VAFATIAG-------- 379
Cdd:cd05938 235 ---VIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIrIREFYGSTEgnIGFFNYTGkigavgrv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 --------PKDL-QFNPSTVGPVvkgvtvkiLDENGN--EVPQGAVGRIF--VGNAFPFEGYTGG---GGKQIIDGLLSS 443
Cdd:cd05938 312 sylykllfPFELiKFDVEKEEPV--------RDAQGFciPVAKGEPGLLVakITQQSPFLGYAGDkeqTEKKLLRDVFKK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 444 GDVgYF--------DERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARL-RAFVVKKPGA 514
Cdd:cd05938 384 GDV-YFntgdllvqDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIgMAAVKLKPGH 462
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 801237227 515 DLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd05938 463 EFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
71-557 |
1.46e-32 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 131.28 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGT--LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGP 148
Cdd:PRK05857 24 ARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 149 QIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGV-----------NPDDDKPSGSSDETLAELIAhsstapapka 217
Cdd:PRK05857 104 AIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVdiaavtresehSLDAASLAGNADQGSEDPLA---------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 218 srrasiIILTSGTTGTPKG---ANRN---TPPTLAPIGgiLSHVPFKAGEVTLLPSPMFHALGY-------MHAALAMFL 284
Cdd:PRK05857 174 ------MIFTSGTTGEPKAvllANRTffaVPDILQKEG--LNWVTWVVGETTYSPLPATHIGGLwwiltclMHGGLCVTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 285 G-STLVLRrrfkpalvlEDIEKHKATSMVVVPVMLSRILDQLEKTEPkpDLSSLKIVFVSGSQLGAElATRALGDLGPVI 363
Cdd:PRK05857 246 GeNTTSLL---------EILTTNAVATTCLVPTLLSKLVSELKSANA--TVPSLRLVGYGGSRAIAA-DVRFIEATGVRT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 364 YNMYGSTEVAFATIAGPKD----LQFNPSTVGPVVKGVTVKILDENG------NEVPQGAVGRIFVGNAFPFEGYTGG-- 431
Cdd:PRK05857 314 AQVYGLSETGCTALCLPTDdgsiVKIEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNpe 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 432 -GGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVk 510
Cdd:PRK05857 394 rTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV- 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 801237227 511 kPGADLDEDTIKQYVRDHLARYK-------VPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK05857 473 -ASAELDESAARALKHTIAARFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
75-557 |
2.08e-32 |
|
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: 129.29 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVS 154
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 DREGAKVIIyddeyTKAVSLAqpplgklralgvnpdddkpsgssdetlaeliahsstapapkasrrasIIILTSGTTGTP 234
Cdd:cd17652 81 ADARPALLL-----TTPDNLA-----------------------------------------------YVIYTSGSTGRP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 235 KGA---NRNTPPTLAPIGGILSHVPfkAGEVTLLPSPMFHAlGYMHAALAMFLGSTLVL----RRRFKPALvLEDIEKHK 307
Cdd:cd17652 109 KGVvvtHRGLANLAAAQIAAFDVGP--GSRVLQFASPSFDA-SVWELLMALLAGATLVLapaeELLPGEPL-ADLLREHR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 308 ATSMVVVPVMLSRIldqlektePKPDLSSLKIVFVSGSQLGAELATRALGdlGPVIYNMYGSTEV-AFATIAGPkDLQFN 386
Cdd:cd17652 185 ITHVTLPPAALAAL--------PPDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPTETtVCATMAGP-LPGGG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 387 PSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYT---------------GGGGKQiidgLLSSGDVGYFDE 451
Cdd:cd17652 254 VPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLnrpgltaerfvadpfGAPGSR----MYRTGDLARWRA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 452 RGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLAR 531
Cdd:cd17652 330 DGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPG 409
|
490 500
....*....|....*....|....*.
gi 801237227 532 YKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17652 410 YMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
66-557 |
2.40e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.16 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 66 LPSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEF 145
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 146 SGPQIKEVSDREGAKVIIYDDEYTKAVSLAQpplgklralGV-NPDDDKPSgssdetlAELIAHSSTAPAPKAS-RRASI 223
Cdd:PRK12316 596 PAERLAYMLEDSGVQLLLSQSHLGRKLPLAA---------GVqVLDLDRPA-------AWLEGYSEENPGTELNpENLAY 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 IILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVL---RRRFKPALVL 300
Cdd:PRK12316 660 VIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaapGDHRDPAKLV 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 301 EDIEKHKATSMVVVPVMLSRILdqleKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLgPV--IYNMYGSTEVAF-ATI 377
Cdd:PRK12316 740 ELINREGVDTLHFVPSMLQAFL----QDEDVASCTSLRRIVCSGEALPADAQEQVFAKL-PQagLYNLYGPTEAAIdVTH 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 378 AGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGG--------KQIIDG--LLSSGDVG 447
Cdd:PRK12316 815 WTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGltaerfvpSPFVAGerMYRTGDLA 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 448 YFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDdkefGARLRAFVV-KKPGADLDEDtIKQYVR 526
Cdd:PRK12316 895 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVlESEGGDWREA-LKAHLA 969
|
490 500 510
....*....|....*....|....*....|.
gi 801237227 527 DHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK12316 970 ASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
86-560 |
5.40e-32 |
|
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: 128.24 E-value: 5.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYD 165
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 166 deytkavslaqpplgklralgvnpdddkpsgssdetlaeliahsstapapkasrrASIIILTSGTTGTPKGAnRNTPPTL 245
Cdd:cd05940 83 -------------------------------------------------------AALYIYTSGTTGLPKAA-IISHRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 246 APIGGILSHVPFKAGEVTLLPS-PMFHALGYMHAALAMFL-GSTLVLRRRFKPALVLEDIEKHKATSMVVVpvmlSRILD 323
Cdd:cd05940 107 WRGGAFFAGSGGALPSDVLYTClPLYHSTALIVGWSACLAsGATLVIRKKFSASNFWDDIRKYQATIFQYI----GELCR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 324 QLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLG-PVIYNMYGSTE--VAFATIAG-PKDLQFNPSTVGPVVKGVTV 399
Cdd:cd05940 183 YLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGvPRIAEFYAATEgnSGFINFFGkPGAIGRNPSLLRKVAPLALV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 400 K--------ILDENG--NEVPQGAVGRIF--VGNAFPFEGYTGGGG--KQII-------DGLLSSGDVGYFDERGLLYVS 458
Cdd:cd05940 263 KydlesgepIRDAEGrcIKVPRGEPGLLIsrINPLEPFDGYTDPAAteKKILrdvfkkgDAWFNTGDLMRLDGEGFWYFV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 459 GRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARL-RAFVVKKPGADLDEDTIKQYVRDHLARYKVPRE 537
Cdd:cd05940 343 DRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAgMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLF 422
|
490 500
....*....|....*....|...
gi 801237227 538 VIFLDELPRNPTGKVLKRELRKL 560
Cdd:cd05940 423 LRLQPEMEITGTFKQQKVDLRNE 445
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
75-558 |
8.68e-32 |
|
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: 127.87 E-value: 8.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLnsefsgpqikevs 154
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPL------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 dregakviiyDDEYtkavslaqpPLGKLRALGVnpdddkpsgssDETLAELIAHsstapapkASRRASIIILTSGTTGTP 234
Cdd:cd17649 68 ----------DPEY---------PAERLRYMLE-----------DSGAGLLLTH--------HPRQLAYVIYTSGSTGTP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 235 KGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPM-FHAL--GYMHAALAmflGSTLVLR---RRFKPALVLEDIEKHKA 308
Cdd:cd17649 110 KGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFnFDGAheQLLPPLIC---GACVVLRpdeLWASADELAEMVRELGV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 309 TSMVVVPVMLSRILDQLEKTEPKPDLSsLKIVFVSGSQLGAELATRALGdlGPV-IYNMYGSTEvafATIA-----GPKD 382
Cdd:cd17649 187 TVLDLPPAYLQQLAEEADRTGDGRPPS-LRLYIFGGEALSPELLRRWLK--APVrLFNAYGPTE---ATVTplvwkCEAG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 383 LQFNPSTV--GPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY----------------TGGGGKqiidgLLSSG 444
Cdd:cd17649 261 AARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYlgrpeltaerfvpdpfGAPGSR-----LYRTG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 445 DVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDkEFGARLRAFVVKKPGADLDED--TIK 522
Cdd:cd17649 336 DLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDG-AGGKQLVAYVVLRAAAAQPELraQLR 414
|
490 500 510
....*....|....*....|....*....|....*.
gi 801237227 523 QYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:cd17649 415 TALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
75-560 |
1.73e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 128.60 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVS 154
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 DREGAKVIIYDDEYTkavSLAQPPLG---------KLRALGVNPDDDKPSGSSDETLAE-LIAHSSTAPAPKAS-----R 219
Cdd:PLN03102 108 RHAKPKILFVDRSFE---PLAREVLHllssedsnlNLPVIFIHEIDFPKRPSSEELDYEcLIQRGEPTPSLVARmfriqD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 220 RASIIIL--TSGTTGTPKGAnrntppTLAPIGGILSHVPFKAG------EVTLLPSPMFHALGYMHAALAMFLGSTLVLR 291
Cdd:PLN03102 185 EHDPISLnyTSGTTADPKGV------VISHRGAYLSTLSAIIGwemgtcPVYLWTLPMFHCNGWTFTWGTAARGGTSVCM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 292 RRFKPALVLEDIEKHKATSMVVVPVMLsRILDQLEKTEPKPDLSSLKiVFVSGSQLGAELaTRALGDLGPVIYNMYGSTE 371
Cdd:PLN03102 259 RHVTAPEIYKNIEMHNVTHMCCVPTVF-NILLKGNSLDLSPRSGPVH-VLTGGSPPPAAL-VKKVQRLGFQVMHAYGLTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 372 vafATiaGP----------KDLQFNPSTVGPVVKGVTVKIL-------DENGNEVPQGA--VGRIFVGNAFPFEGY---T 429
Cdd:PLN03102 336 ---AT--GPvlfcewqdewNRLPENQQMELKARQGVSILGLadvdvknKETQESVPRDGktMGEIVIKGSSIMKGYlknP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 430 GGGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVV 509
Cdd:PLN03102 411 KATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801237227 510 KKPGADLDEDTIK----------QYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PLN03102 491 LEKGETTKEDRVDklvtrerdliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
71-559 |
2.16e-31 |
|
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: 127.78 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAV-IDEEGT---LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSefs 146
Cdd:cd05906 20 AERGPTKGITyIDADGSeefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTV--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 147 GPQIKEVSDRE----------GAKVIIYDDEytkavslAQPPLGKLRALGVNPDDdkpsgsSDETLAELIAHSSTAPAPK 216
Cdd:cd05906 97 PPTYDEPNARLrklrhiwqllGSPVVLTDAE-------LVAEFAGLETLSGLPGI------RVLSIEELLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 217 AS-RRASIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFH--ALGYMHAAlAMFLGS------- 286
Cdd:cd05906 164 SRpDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHvgGLVELHLR-AVYLGCqqvhvpt 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 287 TLVLRRrfkPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKP-DLSSLKIVFVSGSQLGAELATRALGDLGP---- 361
Cdd:cd05906 243 EEILAD---PLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTwDLSSLRYLVNAGEAVVAKTIRRLLRLLEPyglp 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 362 --VIYNMYGSTE--------VAFATIAGPKDLQFnpSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY--- 428
Cdd:cd05906 320 pdAIRPAFGMTEtcsgviysRSFPTYDHSQALEF--VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYynn 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 429 --------TGgggkqiiDGLLSSGDVGYFDErGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVE--AAAIGVDDK 498
Cdd:cd05906 398 peanaeafTE-------DGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDP 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 801237227 499 EFGARLRAfVVKKPGADLDEDTIKQY--VRDHLARYK--VPREVIFL--DELPRNPTGKVLKRELRK 559
Cdd:cd05906 470 GAETEELA-IFFVPEYDLQDALSETLraIRSVVSREVgvSPAYLIPLpkEEIPKTSLGKIQRSKLKA 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
71-560 |
5.13e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.31 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK12316 4561 ARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERL 4640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIyddeyTKAVSLAQPPLGK-LRALGVNPDDDkpsgssdetlaeLIAHSSTAPA-PKASRRASIIILTS 228
Cdd:PRK12316 4641 AYMMEDSGAALLL-----TQSHLLQRLPIPDgLASLALDRDED------------WEGFPAHDPAvRLHPDNLAYVIYTS 4703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 229 GTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPM----FHaLGYMHAALAmflGSTLVLR--RRFKPALVLED 302
Cdd:PRK12316 4704 GSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFsfdgSH-EGLYHPLIN---GASVVIRddSLWDPERLYAE 4779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 303 IEKHKATSMVVVPVMLSRIldqLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPV-IYNMYGSTEVAFATI--AG 379
Cdd:PRK12316 4780 IHEHRVTVLVFPPVYLQQL---AEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVyLFNGYGPTETTVTVLlwKA 4856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 380 PKDLQFNPSTV--GPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY----------------TGGGGKqiidgLL 441
Cdd:PRK12316 4857 RDGDACGAAYMpiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYlerpaltaerfvpdpfGAPGGR-----LY 4931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 442 SSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKeFGARLRAFVVKKPG--ADLDE- 518
Cdd:PRK12316 4932 RTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVVPQDPalADADEa 5010
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 801237227 519 -----DTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK12316 5011 qaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQP 5057
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
71-557 |
1.56e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 124.35 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGAriillnsefsgpqi 150
Cdd:cd12115 9 AARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGA-------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 kevsdregakviiyddeytkavslAQPPLgklralgvnpDDDKPSGSSDETLAE-LIAHSSTAPAPKAsrrasIIILTSG 229
Cdd:cd12115 75 ------------------------AYVPL----------DPAYPPERLRFILEDaQARLVLTDPDDLA-----YVIYTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 230 TTGTPKGA---NRNTpptLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLrrrFKPALVLEDIEKH 306
Cdd:cd12115 116 STGRPKGVaieHRNA---AAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVL---ADNVLALPDLPAA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 307 KATSMV-VVPVMLSRILDQlektEPKPdlSSLKIVFVSGSQLGAELATRaLGDLGPV--IYNMYGSTE-VAFATIAG-PK 381
Cdd:cd12115 190 AEVTLInTVPSAAAELLRH----DALP--ASVRVVNLAGEPLPRDLVQR-LYARLQVerVVNLYGPSEdTTYSTVAPvPP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 382 DLQFNPStVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGG----KQIIDGLLSS------GDVGYFDE 451
Cdd:cd12115 263 GASGEVS-IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGltaeRFLPDPFGPGarlyrtGDLVRWRP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 452 RGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLAR 531
Cdd:cd12115 342 DGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPA 421
|
490 500
....*....|....*....|....*.
gi 801237227 532 YKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd12115 422 YMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
83-557 |
1.75e-30 |
|
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: 124.48 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 83 EEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVI 162
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 163 IYDDEytkavslaqpplgklralgvnpdddkpsgssdETLAeliahsstapapkasrrasIIILTSGTTGTPKGANRNTP 242
Cdd:cd05914 84 FVSDE--------------------------------DDVA-------------------LINYTSGTTGNSKGVMLTYR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 243 PTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHA-ALAMFLGSTLVLRRRFKPALvLEDIEKHKATSMVVVPVMLsrI 321
Cdd:cd05914 113 NIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTlLLPLLNGAHVVFLDKIPSAK-IIALAFAQVTPTLGVPVPL--V 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 322 LDQLEKTE--PKPDLSSLKI----------------------------VFVSGsqlGAELA---TRALGDLGPVIYNMYG 368
Cdd:cd05914 190 IEKIFKMDiiPKLTLKKFKFklakkinnrkirklafkkvheafggnikEFVIG---GAKINpdvEEFLRTIGFPYTIGYG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 369 STEVA-FATIAGPKDLQFnpSTVGPVVKGVTVKILDENgnevPQGAVGRIFVGNAFPFEGYTGG--GGKQII--DGLLSS 443
Cdd:cd05914 267 MTETApIISYSPPNRIRL--GSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNpeATAEAFdkDGWFHT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 444 GDVGYFDERGLLYVSGRDDEMIVSG-GENVFPAEVEDLISGHPDVVEAAAIGVDDKEfgaRLRAFV------VKKPGADL 516
Cdd:cd05914 341 GDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVVQEKKL---VALAYIdpdfldVKALKQRN 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 801237227 517 DEDTIKQYVRDHLARY-----KVPREVIFLDELPRNPTGKvLKREL 557
Cdd:cd05914 418 IIDAIKWEVRDKVNQKvpnykKISKVKIVKEEFEKTPKGK-IKRFL 462
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
77-559 |
1.75e-30 |
|
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: 124.85 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 77 RAAVIdeEGTLTFSELDEAAHA-------VANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQ 149
Cdd:cd05915 10 RKEVV--SRLHTGEVHRTTYAEvyqrarrLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 150 IKEVSDREGAKVIIYDDEYtkaVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAelIAHSSTAPAPKASRRASIII-LTS 228
Cdd:cd05915 88 IAYILNHAEDKVLLFDPNL---LPLVEAIRGELKTVQHFVVMDEKAPEGYLAYE--EALGEEADPVRVPERAACGMaYTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 229 GTTGTPK-------GANRNtpptlAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHA-ALAMFLGSTLVLRRRFKPALVL 300
Cdd:cd05915 163 GTTGLPKgvvyshrALVLH-----SLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPyAATLVGAKQVLPGPRLDPASLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 301 EDIEKHKATSMVVVPVMLSRIL---DQLEKTEPkpdlssLKIVFVSGSQLGAELATRaLGDLGPVIYNM-YGSTEV---- 372
Cdd:cd05915 238 ELFDGEGVTFTAGVPTVWLALAdylESTGHRLK------TLRRLVVGGSAAPRSLIA-RFERMGVEVRQgYGLTETspvv 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 373 -------AFATIAGPKDLQF----------------NPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGyt 429
Cdd:cd05915 311 vqnfvksHLESLSEEEKLTLkaktglpiplvrlrvaDEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSALTPD-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 430 ggggkqiidGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFvV 509
Cdd:cd05915 389 ---------GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV-V 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 801237227 510 KKPGADLDEDTIKQYVRDHLARYK-VPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:cd05915 459 VPRGEKPTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
71-551 |
2.01e-30 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 127.08 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK10252 468 AAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KevsdregakvIIYDDEYTKAVSLAQPPLGKLralgvnpdDDKPSGSSDETLAELIAHSSTAPAPKASRRASIIILTSGT 230
Cdd:PRK10252 548 K----------MMLEDARPSLLITTADQLPRF--------ADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGS 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKGA--------NRntpptlapiggIL---SHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVL-----RRrf 294
Cdd:PRK10252 610 TGRPKGVmvgqtaivNR-----------LLwmqNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMaepeaHR-- 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 295 KPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAF 374
Cdd:PRK10252 677 DPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAV 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 375 ATI---AGPKDLQFNPSTVGPV---VKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG--------------GGGK 434
Cdd:PRK10252 757 DVSwypAFGEELAAVRGSSVPIgypVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGrpdltasrfiadpfAPGE 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 435 QIidglLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGV----DDKEFG--ARLRAFV 508
Cdd:PRK10252 837 RM----YRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqAAATGGdaRQLVGYL 912
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 801237227 509 VKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGK 551
Cdd:PRK10252 913 VSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGK 955
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
71-557 |
2.03e-30 |
|
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: 124.36 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:cd17655 7 AEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIiyddeytkavsLAQPPLGKLRA-LGVNPDDDKPSGSSDETlaeliahSSTAPAPKASRRAsIIILTSG 229
Cdd:cd17655 87 QYILEDSGADIL-----------LTQSHLQPPIAfIGLIDLLDEDTIYHEES-------ENLEPVSKSDDLA-YVIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 230 TTGTPKGA---NRNtpptlapiggiLSHVPFKAGE---------VTLLPSPMFHA-LGYMHAALAmfLGSTLVLRRR--- 293
Cdd:cd17655 148 STGKPKGVmieHRG-----------VVNLVEWANKviyqgehlrVALFASISFDAsVTEIFASLL--SGNTLYIVRKetv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 294 FKPALVLEDIEKHKATSMVVVPVMLSrILDQLEKTEPkpdlSSLKIVFVSGSQLGAELATR--ALGDLGPVIYNMYGSTE 371
Cdd:cd17655 215 LDGQALTQYIRQNRITIIDLTPAHLK-LLDAADDSEG----LSLKHLIVGGEALSTELAKKiiELFGTNPTITNAYGPTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 372 -VAFATI--AGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY----TGGGGKQIIDGLLSS- 443
Cdd:cd17655 290 tTVDASIyqYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYlnrpELTAEKFVDDPFVPGe 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 444 -----GDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPgaDLDE 518
Cdd:cd17655 370 rmyrtGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--ELPV 447
|
490 500 510
....*....|....*....|....*....|....*....
gi 801237227 519 DTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17655 448 AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
71-557 |
2.30e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 127.20 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK12467 1584 AAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERL 1663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIyddeyTKAVSLAQPPLG-KLRALGVNPDDDKPSGSSDETLAELIAHSSTApapkasrrasIIILTSG 229
Cdd:PRK12467 1664 AYMIEDSGIELLL-----TQSHLQARLPLPdGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLA----------YVIYTSG 1728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 230 TTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPM---FHALGYMHAALAmflGSTLVLRR---RFKPALVLEDI 303
Cdd:PRK12467 1729 STGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFafdVSVWELFWPLIN---GARLVIAPpgaHRDPEQLIQLI 1805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 304 EKHKATSMVVVPVMLSRILDQLEKTEPKPdlsSLKIVFVSGSQLGAELATRALGDLGPV-IYNMYGSTE----VAFATIA 378
Cdd:PRK12467 1806 ERQQVTTLHFVPSMLQQLLQMDEQVEHPL---SLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTEtavdVTHWTCR 1882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 379 GPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY-----------------TGGGgkqiidGLL 441
Cdd:PRK12467 1883 RKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYlnrpaltaerfvadpfgTVGS------RLY 1956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 442 SSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEfGARLRAFVVKKPGADLDED-- 519
Cdd:PRK12467 1957 RTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAN-GKQLVAYVVPTDPGLVDDDea 2035
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 801237227 520 ------TIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK12467 2036 qvalraILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
86-560 |
1.19e-29 |
|
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: 122.15 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYd 165
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 166 deytkavslaqpplgklralgvnpdddkpsgssdETLAELIAHSSTAPA---PKASRRASIIILTSGTTGTPKGANRNTP 242
Cdd:cd05939 82 ----------------------------------NLLDPLLTQSSTEPPsqdDVNFRDKLFYIYTSGTTGLPKAAVIVHS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 243 PTLAPIGGILSHVPFKAGEVTLLPSPMFH-ALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRI 321
Cdd:cd05939 128 RYYRIAAGAYYAFGMRPEDVVYDCLPLYHsAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 322 LDQlektEPKPDLSSLKIVFVSGSQLGAELATRALGDLG-PVIYNMYGSTE-----VAFATIAGPkdLQFNP---STVGP 392
Cdd:cd05939 208 LAQ----PPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGiPQIGEFYGATEgnsslVNIDNHVGA--CGFNSrilPSVYP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 393 V----VKGVTVK-ILDENGNEVPQGA------VGRIFVGNAF-PFEGYT--GGGGKQIIDGLLSSGDVGY-------FDE 451
Cdd:cd05939 282 IrlikVDEDTGElIRDSDGLCIPCQPgepgllVGKIIQNDPLrRFDGYVneGATNKKIARDVFKKGDSAFlsgdvlvMDE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 452 RGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVD--DKEFGARLRAFVVKKPGADLDEdtIKQYVRDHL 529
Cdd:cd05939 362 LGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvpGVEGRAGMAAIVDPERKVDLDR--FSAVLAKSL 439
|
490 500 510
....*....|....*....|....*....|.
gi 801237227 530 ARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:cd05939 440 PPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
75-558 |
3.46e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 121.88 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVS 154
Cdd:PLN02479 34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 DREGAKVIIYDDEYtkaVSLAQPPLGKLralgvnpdDDKPSGSSDETLAELIAHSSTAPAP--KASRRASI--------- 223
Cdd:PLN02479 114 EHSKSEVVMVDQEF---FTLAEEALKIL--------AEKKKSSFKPPLLIVIGDPTCDPKSlqYALGKGAIeyekfletg 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 ---------------IIL--TSGTTGTPKGA--NRNTPPTLAPIGGILSHVPfkAGEVTLLPSPMFHALGYMHA-ALAMF 283
Cdd:PLN02479 183 dpefawkppadewqsIALgyTSGTTASPKGVvlHHRGAYLMALSNALIWGMN--EGAVYLWTLPMFHCNGWCFTwTLAAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 284 LGSTLVLRRRFKPAlVLEDIEKHKATSMVVVPVMLSRILDQlEKTEPKPDLSSLKIVFVSGSQLGAELATrALGDLGPVI 363
Cdd:PLN02479 261 CGTNICLRQVTAKA-IYSAIANYGVTHFCAAPVVLNTIVNA-PKSETILPLPRVVHVMTAGAAPPPSVLF-AMSEKGFRV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 364 YNMYGSTEV-AFATIAG--------PKDLQ-------------------FNPSTVGPV-VKGVTVKILDENGNEVPQGAV 414
Cdd:PLN02479 338 THTYGLSETyGPSTVCAwkpewdslPPEEQarlnarqgvryiglegldvVDTKTMKPVpADGKTMGEIVMRGNMVMKGYL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 415 GRIfVGNAFPFEGytggggkqiidGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIG 494
Cdd:PLN02479 418 KNP-KANEEAFAN-----------GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 495 VDDKEFGARLRAFVVKKPGAD------LDEDTIKqYVRDHLARYKVPREVIFlDELPRNPTGKVLKRELR 558
Cdd:PLN02479 486 RPDERWGESPCAFVTLKPGVDksdeaaLAEDIMK-FCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLR 553
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
69-560 |
8.06e-29 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 120.82 E-value: 8.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAV-----IDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGA------- 136
Cdd:PRK10524 62 HLAKRPEQLALIavsteTDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAihsvvfg 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 137 ---------RIillnsEFSGPQIKEVSD--REGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAEL 205
Cdd:PRK10524 142 gfashslaaRI-----DDAKPVLIVSADagSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDRGLAPMARVAGRDVDYATL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 206 IAHSSTAPAPKA---SRRASIIILTSGTTGTPKGANRNTpptlapiGGI-------LSHVpF--KAGEVTLLPSPMFHAL 273
Cdd:PRK10524 217 RAQHLGARVPVEwleSNEPSYILYTSGTTGKPKGVQRDT-------GGYavalatsMDTI-FggKAGETFFCASDIGWVV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 274 GYMHAALAMFLG--STLV---LRRRFKPALVLEDIEKHKATSMVVVPVMLsRILdqlEKTEP----KPDLSSLKIVFVSG 344
Cdd:PRK10524 289 GHSYIVYAPLLAgmATIMyegLPTRPDAGIWWRIVEKYKVNRMFSAPTAI-RVL---KKQDPallrKHDLSSLRALFLAG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 345 SQLGAELATRALGDLG-PVIYNmYGSTEVAFATIAGPKDLQFNPSTVG----PVVkGVTVKILDEN-GNEVPQGAVGRIF 418
Cdd:PRK10524 365 EPLDEPTASWISEALGvPVIDN-YWQTETGWPILAIARGVEDRPTRLGspgvPMY-GYNVKLLNEVtGEPCGPNEKGVLV 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 419 VGNAFP--------------FEGYTGGGGKQIidglLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGH 484
Cdd:PRK10524 443 IEGPLPpgcmqtvwgdddrfVKTYWSLFGRQV----YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 485 PDVVEAAAIGVDDKEFGARLRAFVVKKPGADLD--------EDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRE 556
Cdd:PRK10524 519 PAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRA 598
|
....
gi 801237227 557 LRKL 560
Cdd:PRK10524 599 IQAI 602
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
71-560 |
1.02e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 122.19 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK12467 3105 VARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERL 3184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIyddeyTKAVSLAQ-PPLGKLRALGVnpDDDKPSGSSDETLAELIAHSSTApapkasrrasIIILTSG 229
Cdd:PRK12467 3185 AYMIEDSGVKLLL-----TQAHLLEQlPAPAGDTALTL--DRLDLNGYSENNPSTRVMGENLA----------YVIYTSG 3247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 230 TTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLR--RRFKPALVLEDIEKHK 307
Cdd:PRK12467 3248 STGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRdnDLWDPEELWQAIHAHR 3327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 308 ATSMVVVPVMLSrildQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPV-IYNMYGSTEVAFATI--AGPKDLQ 384
Cdd:PRK12467 3328 ISIACFPPAYLQ----QFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTEAVVTVTlwKCGGDAV 3403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 385 FNPSTV--GPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY----------------TGGGGKqiidgLLSSGDV 446
Cdd:PRK12467 3404 CEAPYApiGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYhqrpsltaerfvadpfSGSGGR-----LYRTGDL 3478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 447 GYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVdDKEFGARLRAFVV-KKPGADLdedtiKQYV 525
Cdd:PRK12467 3479 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVpADPQGDW-----RETL 3552
|
490 500 510
....*....|....*....|....*....|....*....
gi 801237227 526 RDHLAR----YKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK12467 3553 RDHLAAslpdYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
30-559 |
2.75e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.83 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 30 LHYLRKIIE--SGAIGLEPPLNYAALAADIRKWGE----------VGMLPSHNARRAPNRAAVIDEEGTLTFSELDEAAH 97
Cdd:PRK12316 3014 QNLLRGMVEnpQRSVDELAMLDAEERGQLLEAWNAtaaeyplergVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRAN 3093
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 98 AVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIiyddeytkavsLAQP 177
Cdd:PRK12316 3094 RLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL-----------LSQS 3162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 178 PLGKLRALGVNPDDDKPSgssDETLAELIAHSSTAPAPKASrrasiIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPF 257
Cdd:PRK12316 3163 HLRLPLAQGVQVLDLDRG---DENYAEANPAIRTMPENLAY-----VIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGL 3234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 258 KAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKpDLSSL 337
Cdd:PRK12316 3235 GVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH-RCTSL 3313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 338 KIVFVSGSQLGAELATRALgdLGPVIYNMYGSTEVAF-ATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGR 416
Cdd:PRK12316 3314 KRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATItVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGE 3391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 417 IFVGNAFPFEGYTGGGGK----------QIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPD 486
Cdd:PRK12316 3392 LYLGGEGLARGYHNRPGLtaerfvpdpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPW 3471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 801237227 487 VVEAAAIGVDdkefGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:PRK12316 3472 VREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
69-560 |
4.39e-28 |
|
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: 118.11 E-value: 4.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVI------DEEGTLTFSELDEAAHAVANGLLAKGvRAGDGVAILARNHRWFVIANYG---AARVGARII 139
Cdd:cd05931 1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGclyAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 140 LLNSEFSGPQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDetlaeliahSSTAPAPKASR 219
Cdd:cd05931 80 PPTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAA---------DWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 220 RAsIIILTSGTTGTPKGA---NRNTpptLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALA-MFLGSTLVL----- 290
Cdd:cd05931 151 IA-YLQYTSGSTGTPKGVvvtHRNL---LANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTpLYSGGPSVLmspaa 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 291 --RRrfkPALVLEDIEKHKATSMVVvPVM-----LSRILDqlEKTEPKpDLSSLKI------------------------ 339
Cdd:cd05931 227 flRR---PLRWLRLISRYRATISAA-PNFaydlcVRRVRD--EDLEGL-DLSSWRValngaepvrpatlrrfaeafapfg 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 340 ----------------VFVSGSQLGAELATRALGDLgpviynmygstevAFATIAGPKDLQFNPST----VGPVVKGVTV 399
Cdd:cd05931 300 frpeafrpsyglaeatLFVSGGPPGTGPVVLRVDRD-------------ALAGRAVAVAADDPAARelvsCGRPLPDQEV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 400 KILDENGN-EVPQGAVGRIFV--------------GNAFPFEGYTGGGGkqiiDGLLSSGDVGYFDErGLLYVSGRDDEM 464
Cdd:cd05931 367 RIVDPETGrELPDGEVGEIWVrgpsvasgywgrpeATAETFGALAATDE----GGWLRTGDLGFLHD-GELYITGRLKDL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 465 IVSGGENVFPAEVEDLISGHPDVVE---AAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLAR-YKV-PREVI 539
Cdd:cd05931 442 IIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAReHGVaPADVV 521
|
570 580
....*....|....*....|...
gi 801237227 540 FL--DELPRNPTGKVLKRELRKL 560
Cdd:cd05931 522 LVrpGSIPRTSSGKIQRRACRAA 544
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
41-557 |
7.21e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 119.50 E-value: 7.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 41 AIGlEPPLNYAALAADIRKWGEVGMLPS---------HNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAG 111
Cdd:PRK05691 1103 ALG-DVQLLDAAERAQLAQWGQAPCAPAqawlpellnEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPD 1181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 112 DGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIiyddeytkavslaqppLGKLRALGVNPDD 191
Cdd:PRK05691 1182 VCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELL----------------LTQSHLLERLPQA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 192 DKPSGSSDETLaELIAHSSTAPAPKAS-RRASIIILTSGTTGTPKGANrNTPPTLAP-IGGILSHVPFKAGEVTLLPSPM 269
Cdd:PRK05691 1246 EGVSAIALDSL-HLDSWPSQAPGLHLHgDNLAYVIYTSGSTGQPKGVG-NTHAALAErLQWMQATYALDDSDVLMQKAPI 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 270 FHALGYMHAALAMFLGSTLVLR---RRFKPALVLEDIEKHKATSMVVVPVMLSRILDqlektEPK-PDLSSLKIVFVSGS 345
Cdd:PRK05691 1324 SFDVSVWECFWPLITGCRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFID-----EPLaAACTSLRRLFSGGE 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 346 QLGAELATRALGDLGPV-IYNMYGSTEVAFATI---AGPKDLQFNPstVGPVVKGVTVKILDENGNEVPQGAVGRIFVGN 421
Cdd:PRK05691 1399 ALPAELRNRVLQRLPQVqLHNRYGPTETAINVThwqCQAEDGERSP--IGRPLGNVLCRVLDAELNLLPPGVAGELCIGG 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 422 AFPFEGYTGGGG----KQIIDG-------LLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVvEA 490
Cdd:PRK05691 1477 AGLARGYLGRPAltaeRFVPDPlgedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGV-AQ 1555
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 801237227 491 AAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK05691 1556 AAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
82-556 |
1.67e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 116.25 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 82 DEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSefsgP-----------QI 150
Cdd:PRK07768 25 DAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQ----PtprtdlavwaeDT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAVSLaqpplgkLRALGVNPDddkpsgssdeTLAELIAHSSTAPAPKASRRASIIILTSGT 230
Cdd:PRK07768 101 LRVIGMIGAKAVVVGEPFLAAAPV-------LEEKGIRVL----------TVADLLAADPIDPVETGEDDLALMQLTSGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKgANRNTPPTL-APIGGILSHVPFKAG-EVTLLPSPMFHALGyMHAALA--MFLGSTLV-------LRRrfkPALV 299
Cdd:PRK07768 164 TGSPK-AVQITHGNLyANAEAMFVAAEFDVEtDVMVSWLPLFHDMG-MVGFLTvpMYFGAELVkvtpmdfLRD---PLLW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATsMVVVP----VMLSRILDQLEKtEPKPDLSSLKIVfVSGSQLGAELATRALGDLGP-------VIYNMYG 368
Cdd:PRK07768 239 AELISKYRGT-MTAAPnfayALLARRLRRQAK-PGAFDLSSLRFA-LNGAEPIDPADVEDLLDAGArfglrpeAILPAYG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 369 STE----VAFATIAGP-------KDL-----QFNPST---------VGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAF 423
Cdd:PRK07768 316 MAEatlaVSFSPCGAGlvvdevdADLlaalrRAVPATkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 424 PFEGYTGGGG---KQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVE--AAAIGVDDK 498
Cdd:PRK07768 396 VTPGYLTMDGfipAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgnAVAVRLDAG 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 801237227 499 EFGARLrAFVVKKPGADlDEDTIKQYVRD--HLARYKV---PREVIFLD--ELPRNPTGKvLKRE 556
Cdd:PRK07768 476 HSREGF-AVAVESNAFE-DPAEVRRIRHQvaHEVVAEVgvrPRNVVVLGpgSIPKTPSGK-LRRA 537
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
59-560 |
2.75e-27 |
|
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: 116.12 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 59 KWGEVGML-PSHNA-----RRAPNRAAVI------DEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVI 126
Cdd:cd05966 45 KWFEGGKLnISYNCldrhlKERGDKVAIIwegdepDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 127 ANYGAARVGA--RIIllnseFSGPQIKEVSDR---EGAKVIIYDDEY---TKAVSLAQ---------PPLGKLRALGVNP 189
Cdd:cd05966 125 AMLACARIGAvhSVV-----FAGFSAESLADRindAQCKLVITADGGyrgGKVIPLKEivdealekcPSVEKVLVVKRTG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 190 DDDKPSGSSDETLAELIAHSST--APAPKASRRASIIILTSGTTGTPKGANRNTpptlapiGGILSHV--PFK------- 258
Cdd:cd05966 200 GEVPMTEGRDLWWHDLMAKQSPecEPEWMDSEDPLFILYTSGSTGKPKGVVHTT-------GGYLLYAatTFKyvfdyhp 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 259 ---------AGEVT----LLPSPMfhALGymhAALAMFLGS-TLVLRRRFkpalvLEDIEKHKATSMVVVPVMLSRILDQ 324
Cdd:cd05966 273 ddiywctadIGWITghsyIVYGPL--ANG---ATTVMFEGTpTYPDPGRY-----WDIVEKHKVTIFYTAPTAIRALMKF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 325 LEKTEPKPDLSSLKIvfvsgsqlgaelatraLGDLGPVI--------YNMYGSTEVAF--------------ATIAGPKD 382
Cdd:cd05966 343 GDEWVKKHDLSSLRV----------------LGSVGEPInpeawmwyYEVIGKERCPIvdtwwqtetggimiTPLPGATP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 383 LQfnPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFP------------FE-GYTggggkQIIDGLLSSGDVGYF 449
Cdd:cd05966 407 LK--PGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPgmartiygdherYEdTYF-----SKFPGYYFTGDGARR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 450 DERGLLYVSGR-DDEMIVSGgENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDT---IKQYV 525
Cdd:cd05966 480 DEDGYYWITGRvDDVINVSG-HRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELrkeLRKHV 558
|
570 580 590
....*....|....*....|....*....|....*
gi 801237227 526 RDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:cd05966 559 RKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKI 593
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
68-560 |
5.28e-27 |
|
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: 114.18 E-value: 5.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 68 SHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLnsEFSG 147
Cdd:cd05918 6 EERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL--DPSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQ--IKEVSDREGAKVIIyddeytkavslaqpplgklralgvnpdddkpsgssdetlaeliAHSSTAPApkasrrasIII 225
Cdd:cd05918 84 PLqrLQEILQDTGAKVVL-------------------------------------------TSSPSDAA--------YVI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 226 LTSGTTGTPKGAnrntpptlapiggILSHVPFKAGEVTLLP--------------SPMFHA-LGYMHAALAmfLGSTLVL 290
Cdd:cd05918 113 FTSGSTGKPKGV-------------VIEHRALSTSALAHGRalgltsesrvlqfaSYTFDVsILEIFTTLA--AGGCLCI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 291 ----RRRFKPALVledIEKHKATSMVVVPVmLSRILDqlektePKpDLSSLKIVFVSGSQLGAELATRALGdlGPVIYNM 366
Cdd:cd05918 178 pseeDRLNDLAGF---INRLRVTWAFLTPS-VARLLD------PE-DVPSLRTLVLGGEALTQSDVDTWAD--RVRLINA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 367 YGSTEVAFATIAGPKDLQFNPSTVGPVVkGVTVKILDENGNE--VPQGAVGRIFVG----------------NAFPF--- 425
Cdd:cd05918 245 YGPAECTIAATVSPVVPSTDPRNIGRPL-GATCWVVDPDNHDrlVPIGAVGELLIEgpilargylndpektaAAFIEdpa 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 426 ---EGYTGGGGKqiidgLLSSGDVGYFDERG-LLYVsGRDDEMIVSGGENVFPAEVEDLISGHPDV---VEAAAIGVDDK 498
Cdd:cd05918 324 wlkQEGSGRGRR-----LYRTGDLVRYNPDGsLEYV-GRKDTQVKIRGQRVELGEIEHHLRQSLPGakeVVVEVVKPKDG 397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 801237227 499 EFGARLRAFVVKKPGADLDEDT-----------------IKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:cd05918 398 SSSPQLVAFVVLDGSSSGSGDGdslflepsdefralvaeLRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
75-560 |
1.15e-26 |
|
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: 112.88 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKG-VRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEV 153
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 154 SDREGAKVIIyddeytkavslaqpplgklralgvnpdddkpSGSSDetLAeliahsstapapkasrrasIIILTSGTTGT 233
Cdd:cd17648 81 LEDTGARVVI-------------------------------TNSTD--LA-------------------YAIYTSGTTGK 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 234 PKGanrntppTLAPIGGI------LSHVPFKAGE----VTLLPSPMF-HALGYMhaALAMFLGSTLVL---RRRFKPALV 299
Cdd:cd17648 109 PKG-------VLVEHGSVvnlrtsLSERYFGRDNgdeaVLFFSNYVFdFFVEQM--TLALLNGQKLVVppdEMRFDPDRF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVMLSRI-LDQLektepkpdlSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIA 378
Cdd:cd17648 180 YAYINREKVTYLSGTPSVLQQYdLARL---------PHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHK 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 379 G--PKDLQFNPStVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGY------TG--------GGGKQIIDG--- 439
Cdd:cd17648 251 RffPGDQRFDKS-LGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYlnrpelTAerflpnpfQTEQERARGrna 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 440 -LLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGA-----RLRAFVVKKPG 513
Cdd:cd17648 330 rLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkYLVGYYLPEPG 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 801237227 514 AdLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVlkrELRKL 560
Cdd:cd17648 410 H-VPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL---DVRAL 452
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
72-560 |
3.48e-25 |
|
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: 110.05 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 72 RRAPNRAAVI-DEEGT---LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFsG 147
Cdd:cd05943 80 ADADDPAAIYaAEDGErteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDF-G 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQikEVSDREG---AKVIIYDDEYTKA---------VSLAQPPLGKLRALGVNPDD------DKPSGSSDETLAELIAHS 209
Cdd:cd05943 159 VP--GVLDRFGqiePKVLFAVDAYTYNgkrhdvrekVAELVKGLPSLLAVVVVPYTvaagqpDLSKIAKALTLEDFLATG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 210 STAPAPKASRRAS---IIILTSGTTGTPKganrntpptlaPI----GGILS--------HVPFKAGEVTLLpspmFHALG 274
Cdd:cd05943 237 AAGELEFEPLPFDhplYILYSSGTTGLPK-----------CIvhgaGGTLLqhlkehilHCDLRPGDRLFY----YTTCG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 275 YMH-----AALAmfLGSTLVLR--RRFKPAL-VLEDI-EKHKATSMVVVPvmlsRILDQLEKTEPKP----DLSSLKIVF 341
Cdd:cd05943 302 WMMwnwlvSGLA--VGATIVLYdgSPFYPDTnALWDLaDEEGITVFGTSA----KYLDALEKAGLKPaethDLSSLRTIL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 342 VSGSQLGAELATRALGDLGP-VIYNMY-GSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPqGAVGRIFV 419
Cdd:cd05943 376 STGSPLKPESFDYVYDHIKPdVLLASIsGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVW-GEKGELVC 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 420 GNAFP-----FEGYTGGGGKQ-----IIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVE 489
Cdd:cd05943 455 TKPFPsmpvgFWNDPDGSRYRaayfaKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVED 534
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 801237227 490 AAAIGVDDKEFGARLRAFVVKKPGADLDED---TIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:cd05943 535 SLVVGQEWKDGDERVILFVKLREGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKI 608
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
75-557 |
5.17e-25 |
|
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: 107.94 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVS 154
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 DREGAKVIIYDdeytkavslaqpplgklralgvnPDDdkpsgssdetlaeliahsstapapkasrrASIIILTSGTTGTP 234
Cdd:cd17650 81 EDSGAKLLLTQ-----------------------PED-----------------------------LAYVIYTSGTTGKP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 235 KGA---NRNTPPTLApigGILSHVPFKAGEVTLLP-SPMFHALGYMHAALAMFLGSTLVL---RRRFKPALVLEDIEKHK 307
Cdd:cd17650 109 KGVmveHRNVAHAAH---AWRREYELDSFPVRLLQmASFSFDVFAGDFARSLLNGGTLVIcpdEVKLDPAALYDLILKSR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 308 ATSMVVVPVMLSRILDQLEktEPKPDLSSLKIVFVSGSQLGAELATRALGDLGP--VIYNMYGSTEvafATI-------- 377
Cdd:cd17650 186 ITLMESTPALIRPVMAYVY--RNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQgmRIINSYGVTE---ATIdstyyeeg 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 378 -AGPKDLQFNPstVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG--------------GGGKQiidgLLS 442
Cdd:cd17650 261 rDPLGDSANVP--IGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNrpeltaerfvenpfAPGER----MYR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 443 SGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVkkPGADLDEDTIK 522
Cdd:cd17650 335 TGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAELR 412
|
490 500 510
....*....|....*....|....*....|....*
gi 801237227 523 QYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17650 413 AFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
75-557 |
1.40e-24 |
|
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: 107.17 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 75 PNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVS 154
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 155 DREGAKVIIYDDEYTkaVSLAQpplgklRALGVNPDDDKPSGSSDETLAELIAHSSTApapkasrrasIIILTSGTTGTP 234
Cdd:cd17656 82 LDSGVRVVLTQRHLK--SKLSF------NKSTILLEDPSISQEDTSNIDYINNSDDLL----------YIIYTSGTTGKP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 235 KGA---NRNtpptlapIGGILSH-----VPFKAGEVTLLPSPMFHaLGYMHAALAMFLGSTLVL----RRRFKPALVlED 302
Cdd:cd17656 144 KGVqleHKN-------MVNLLHFerektNINFSDKVLQFATCSFD-VCYQEIFSTLLSGGTLYIireeTKRDVEQLF-DL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 303 IEKHKaTSMVVVPV-MLSRILDQLEKTEPKPDlsSLKIVFVSGSQLG-AELATRALGDLGPVIYNMYGSTE---VAFATI 377
Cdd:cd17656 215 VKRHN-IEVVFLPVaFLKFIFSEREFINRFPT--CVKHIITAGEQLViTNEFKEMLHEHNVHLHNHYGPSEthvVTTYTI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 378 AGPKDLQFNPSTVGPVVKgVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG----GGGKQIIDG------LLSSGDVG 447
Cdd:cd17656 292 NPEAEIPELPPIGKPISN-TWIYILDQEQQLQPQGIVGELYISGASVARGYLNrqelTAEKFFPDPfdpnerMYRTGDLA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 448 YFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVkkPGADLDEDTIKQYVRD 527
Cdd:cd17656 371 RYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAK 448
|
490 500 510
....*....|....*....|....*....|
gi 801237227 528 HLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17656 449 QLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
83-559 |
2.42e-24 |
|
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: 105.98 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 83 EEGTLTFSELDEAAHAVANGLL-AKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKV 161
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 162 IIYDDEYTkavslaqpplgklralgvnpdddkpsgssdetlaeliahsstapapkasrraSIIILTSGTTGTPKGA---N 238
Cdd:cd05937 82 VIVDPDDP----------------------------------------------------AILIYTSGTTGLPKAAaisW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 239 RNTPPTLAPIGGILShvpFKAGEVTLLPSPMFHALGYMHAALAMFL-GSTLVLRRRFKPALVLEDIEKHKATSMVVVPVM 317
Cdd:cd05937 110 RRTLVTSNLLSHDLN---LKNGDRTYTCMPLYHGTAAFLGACNCLMsGGTLALSRKFSASQFWKDVRDSGATIIQYVGEL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 318 LSRILDqlekTEPKPDLSSLKIVFVSGSQLGAELATRALGDLG-PVIYNMYGSTEVAFATIagpkDLQFNPSTVGPVVKG 396
Cdd:cd05937 187 CRYLLS----TPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNvPEIGEFYAATEGVFALT----NHNVGDFGAGAIGHH 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 397 ------------VTVKILDENGN-----------EVPQG----AVGRIFVGNAFPFEGYTGGGG---KQIIDGLLSSGDV 446
Cdd:cd05937 259 glirrwkfenqvVLVKMDPETDDpirdpktgfcvRAPVGepgeMLGRVPFKNREAFQGYLHNEDateSKLVRDVFRKGDI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 447 gYF--------DERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDE 518
Cdd:cd05937 339 -YFrtgdllrqDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAVP 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 801237227 519 DTI-----KQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRK 559
Cdd:cd05937 418 TEFtksllASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
476-551 |
2.62e-24 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 96.46 E-value: 2.62e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 801237227 476 EVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGK 551
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
222-557 |
3.48e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 105.12 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 222 SIIILTSGTTGTPKGANRntppTLAPIGG-ILSHVPFKAGEVTLLP---SPMFHALGYMHAALAmflgstlVLRRRFKPA 297
Cdd:PRK08308 104 SLLQYSSGTTGEPKLIRR----SWTEIDReIEAYNEALNCEQDETPivaCPVTHSYGLICGVLA-------ALTRGSKPV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 298 LV-----------LEDIEKHKATSmvvVPVMLSRILDQLEKTEpkpdlsSLKIVFVSGSQLGAELATRaLGDLGPVIYNM 366
Cdd:PRK08308 173 IItnknpkfalniLRNTPQHILYA---VPLMLHILGRLLPGTF------QFHAVMTSGTPLPEAWFYK-LRERTTYMMQQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 367 YGSTEVAFATIAgpKDLQFnPSTVGPVVKGVTVKIldeNGNEvpqGAVGRIFVGNafpfegytggGGKQIidgllSSGDV 446
Cdd:PRK08308 243 YGCSEAGCVSIC--PDMKS-HLDLGNPLPHVSVSA---GSDE---NAPEEIVVKM----------GDKEI-----FTKDL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 447 GYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEdtIKQYVR 526
Cdd:PRK08308 299 GYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQ--LREWCI 376
|
330 340 350
....*....|....*....|....*....|.
gi 801237227 527 DHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK08308 377 QHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
69-557 |
6.09e-24 |
|
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: 104.82 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFsgP 148
Cdd:cd17644 8 EQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNY--P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 149 QIKEVSDREGAKViiyddeytkAVSLAQPplgklralgvnpdddkpsgssdETLAeliahsstapapkasrrasIIILTS 228
Cdd:cd17644 86 QERLTYILEDAQI---------SVLLTQP----------------------ENLA-------------------YVIYTS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 229 GTTGTPKGAnrntpptlapiggILSH---VPFKAG--EVTLLPSPM----FHALGYMHAALAMFL----GSTLVLR---R 292
Cdd:cd17644 116 GSTGKPKGV-------------MIEHqslVNLSHGliKEYGITSSDrvlqFASIAFDVAAEEIYVtllsGATLVLRpeeM 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 293 RFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPkPDLSSLKIVFVSGSQLGAELATRALGDLGPVI--YNMYGST 370
Cdd:cd17644 183 RSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTI-DLPSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINVYGPT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 371 EVAF-ATIAGPKDLQFNPST---VGPVVKGVTVKILDENGNEVPQGAVGRIFVGNA----------------F---PFEG 427
Cdd:cd17644 262 EATIaATVCRLTQLTERNITsvpIGRPIANTQVYILDENLQPVPVGVPGELHIGGVglargylnrpeltaekFishPFNS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 428 YTGgggkqiiDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAF 507
Cdd:cd17644 342 SES-------ERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAY 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 801237227 508 VVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17644 415 IVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
194-560 |
1.22e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 102.43 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 194 PSGSSDETLAELIAHSSTAPAPKASRRAsIIILTSGTTGTPKGANRnTPPTLAPiGGILSHvPFKAGEVT-LLPSPMFHA 272
Cdd:PRK07824 11 PVPAQDERRAALLRDALRVGEPIDDDVA-LVVATSGTTGTPKGAML-TAAALTA-SADATH-DRLGGPGQwLLALPAHHI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 273 LGY---MHAALAMFLGSTLVLRRRFKPALVLEDIEKHKA----TSMVvvPVMLSRILDQLEKTEPkpdLSSLKIVFVSGS 345
Cdd:PRK07824 87 AGLqvlVRSVIAGSEPVELDVSAGFDPTALPRAVAELGGgrryTSLV--PMQLAKALDDPAATAA---LAELDAVLVGGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 346 QLGAELATRAlGDLGPVIYNMYGSTEVAFATIAGpkdlqfnpstvGPVVKGVTVKILDengnevpqgavGRIFVGNAFPF 425
Cdd:PRK07824 162 PAPAPVLDAA-AAAGINVVRTYGMSETSGGCVYD-----------GVPLDGVRVRVED-----------GRIALGGPTLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 426 EGYTGgggkqIID-------GLLSSGDVGYFDErGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDK 498
Cdd:PRK07824 219 KGYRN-----PVDpdpfaepGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDD 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 801237227 499 EFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK07824 293 RLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
87-560 |
1.82e-23 |
|
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: 103.03 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 87 LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDD 166
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 167 eytkaVSLAQPPLgklralgvnpdddkpsgssdetlaeliahsstapapkasrrasIIILTSGTTGTPK---GANRNTP- 242
Cdd:cd05974 81 -----NTHADDPM-------------------------------------------LLYFTSGTTSKPKlveHTHRSYPv 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 243 ---PTLAPIGgilshvpFKAGEVTL-LPSPMF--HALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPV 316
Cdd:cd05974 113 ghlSTMYWIG-------LKPGDVHWnISSPGWakHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPT 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 317 MLSRILDQlektepkpDLSSLKI----VFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAfATIAGPKDLQFNPSTVGP 392
Cdd:cd05974 186 VWRMLIQQ--------DLASFDVklreVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETT-ALVGNSPGQPVKAGSMGR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 393 VVKGVTVKILDENGNEVPQGAVGrIFVGNAFP---FEGYTGGGGKQ---IIDGLLSSGDVGYFDERGLLYVSGRDDEMIV 466
Cdd:cd05974 257 PLPGYRVALLDPDGAPATEGEVA-LDLGDTRPvglMKGYAGDPDKTahaMRGGYYRTGDIAMRDEDGYLTYVGRADDVFK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 467 SGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDT---IKQYVRDHLARYKVPREVIFLdE 543
Cdd:cd05974 336 SSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETaleIFRFSRERLAPYKRIRRLEFA-E 414
|
490
....*....|....*..
gi 801237227 544 LPRNPTGKVLKRELRKL 560
Cdd:cd05974 415 LPKTISGKIRRVELRRR 431
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
71-532 |
2.52e-23 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 103.83 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEG----------TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIIL 140
Cdd:PRK09274 16 AQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 141 LNSEFSGPQIKEVSDREGAKVIIyddeytkAVSLAQ--------PPLGKLRALGVnpddDKPSGSSDETLAELIAHSSTA 212
Cdd:PRK09274 96 VDPGMGIKNLKQCLAEAQPDAFI-------GIPKAHlarrlfgwGKPSVRRLVTV----GGRLLWGGTTLATLLRDGAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 213 PAPKASRRA---SIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLlpsPMFHALGYMHAALAMflgSTLV 289
Cdd:PRK09274 165 PFPMADLAPddmAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDL---PTFPLFALFGPALGM---TSVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 290 LRRRF-KPALV-----LEDIEKHKATSMVVVPVMLSRILDQLEKTEPKpdLSSLKIVFVSGSQLGAELATRALGDLGPV- 362
Cdd:PRK09274 239 PDMDPtRPATVdpaklFAAIERYGVTNLFGSPALLERLGRYGEANGIK--LPSLRRVISAGAPVPIAVIERFRAMLPPDa 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 363 -IYNMYGSTEV-AFATIAGPKDLQfnpST-----------VGPVVKGVTVKILD---------ENGNEVPQGAVGRIFVG 420
Cdd:PRK09274 317 eILTPYGATEAlPISSIESREILF---ATraatdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 421 NAFPFEGYTG-----GGGKqIIDGLLS----SGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAA 491
Cdd:PRK09274 394 GPMVTRSYYNrpeatRLAK-IPDGQGDvwhrMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 801237227 492 AIGVddKEFGARLRAFVV-KKPGADLDEDTIKQYVRDHLARY 532
Cdd:PRK09274 473 LVGV--GVPGAQRPVLCVeLEPGVACSKSALYQELRALAAAH 512
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
86-502 |
4.51e-23 |
|
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: 102.44 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARN-HRWFvIANYGAARVGAriillnsefsgpqikevsdregakviiy 164
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNsPRWL-IADQGIMALGA---------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 165 ddeytkavslAQPPLGklralgvnpdddkpSGSSDETLAELIAHS--STAPAPKASRRASIIILTSGTTGTPKGANRNTP 242
Cdd:cd17640 56 ----------VDVVRG--------------SDSSVEELLYILNHSesVALVVENDSDDLATIIYTSGTTGNPKGVMLTHA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 243 PTLAPIGGILSHVPFKAGEVTLLPSPMFHAlgYMHAAlAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVP----VML 318
Cdd:cd17640 112 NLLHQIRSLSDIVPPQPGDRFLSILPIWHS--YERSA-EYFIFACGCSQAYTSIRTLKDDLKRVKPHYIVSVPrlweSLY 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 319 SRILDQLEKTEP------KPDLSSLKIVF-VSGSQLGAELATRALGDLGPVIYNMYGSTE----VAFATIAGPKDlqfnp 387
Cdd:cd17640 189 SGIQKQVSKSSPikqflfLFFLSGGIFKFgISGGGALPPHVDTFFEAIGIEVLNGYGLTEtspvVSARRLKCNVR----- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 388 STVGPVVKGVTVKILDENGNEV-PQGAVGRIFVGNAFPFEGY------TggggKQII--DGLLSSGDVGYFDERGLLYVS 458
Cdd:cd17640 264 GSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYyknpeaT----SKVLdsDGWFNTGDLGWLTCGGELVLT 339
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 801237227 459 GRDDEMIV-SGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGA 502
Cdd:cd17640 340 GRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGA 384
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
82-560 |
2.28e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 101.01 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 82 DEEGTLTFSELDEAAHAVANGLLAK-GVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAK 160
Cdd:PRK05620 34 AEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 161 VIIYDDEYTKAVSLAQPPLGKLRAL---GVNPDDD----KPSGSSDETLAELIAHSSTA-PAPKASRR-ASIIILTSGTT 231
Cdd:PRK05620 114 VIVADPRLAEQLGEILKECPCVRAVvfiGPSDADSaaahMPEGIKVYSYEALLDGRSTVyDWPELDETtAAAICYSTGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 232 GTPKGA------------NRNTPPTLApiggiLSHvpfkaGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRrrfKPALV 299
Cdd:PRK05620 194 GAPKGVvyshrslylqslSLRTTDSLA-----VTH-----GESFLCCVPIYHVLSWGVPLAAFMSGTPLVFP---GPDLS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVV----VPVMLSRILDQLEKTEPKPdlSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTE-VAF 374
Cdd:PRK05620 261 APTLAKIIATAMPRvahgVPTLWIQLMVHYLKNPPER--MSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTEtSPV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 375 ATIAGPkdlqfnPSTV------------GPVVKGVTVKILDE----NGNEVPQGAV---GRIFVGNAFPFEGYTGGG--- 432
Cdd:PRK05620 339 GTVARP------PSGVsgearwayrvsqGRFPASLEYRIVNDgqvmESTDRNEGEIqvrGNWVTASYYHSPTEEGGGaas 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 433 ---GKQI--------IDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFG 501
Cdd:PRK05620 413 tfrGEDVedandrftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 801237227 502 ARLRAFVVKKPGADLDEDT---IKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK05620 493 ERPLAVTVLAPGIEPTRETaerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQH 554
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
203-558 |
6.81e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 99.72 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 203 AELIAHSSTA-PA---PKASRRASIIILTSGTTGTPKGA-NRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMH 277
Cdd:PRK06060 125 AELMSEAARVaPGgyePMGGDALAYATYTSGTTGPPKAAiHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 278 AA-LAMFLGSTLV-------------LRRRFKPALvlediekhkatsMVVVPVMLSRILDQLEktepkPD-LSSLKIVFV 342
Cdd:PRK06060 205 SVwFPLATGGSAVinsapvtpeaaaiLSARFGPSV------------LYGVPNFFARVIDSCS-----PDsFRSLRCVVS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 343 SGSQLGAELATRALGDLGPV-IYNMYGSTEVAFATIAGPKDlQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGN 421
Cdd:PRK06060 268 AGEALELGLAERLMEFFGGIpILDGIGSTEVGQTFVSNRVD-EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRG 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 422 AFPFEGYTGGGGKQIID-GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEF 500
Cdd:PRK06060 347 PAIAKGYWNRPDSPVANeGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTG 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801237227 501 GARLRAFVVKKPGADLDEDTIKQYVRDHLAR---YKVPREVIFLDELPRNPTGKVLKRELR 558
Cdd:PRK06060 427 ASTLQAFLVATSGATIDGSVMRDLHRGLLNRlsaFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
224-560 |
7.95e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 99.43 E-value: 7.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 IILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSP-----MFHalGYMHAALAmfLGSTLVLRRR--FKP 296
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSsigwvSFH--GFLYGSLS--LGNTFVMFEGgiIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 297 ALVLED----IEKHKATSMVVVPvmlsRILDQLEKTEP-------KPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYN 365
Cdd:PTZ00237 335 KHIEDDlwntIEKHKVTHTLTLP----KTIRYLIKTDPeatiirsKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 366 MYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRI-------------FVGNAFPFegytggg 432
Cdd:PTZ00237 411 GYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVafklpmppsfattFYKNDEKF------- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 433 gKQIID---GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVV 509
Cdd:PTZ00237 484 -KQLFSkfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLV 562
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 801237227 510 KKPGAD---LD----EDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PTZ00237 563 LKQDQSnqsIDlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKF 620
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
73-560 |
9.48e-22 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 99.10 E-value: 9.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 73 RAPNRAAVI--DEEG---TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFsG 147
Cdd:PRK03584 96 RRDDRPAIIfrGEDGprrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDF-G 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 148 PQikEVSDREGA---KVIIYDDEYT---KAVSLaqppLGKLRAL--------------GVNPDDDKPSGSSDETLAELIA 207
Cdd:PRK03584 175 VQ--GVLDRFGQiepKVLIAVDGYRyggKAFDR----RAKVAELraalpslehvvvvpYLGPAAAAAALPGALLWEDFLA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 208 HSSTAPaPKASRRAS----IIILTSGTTGTPKganrntpptlaPI----GGILS--------HVPFKAGEVTLlpspMFH 271
Cdd:PRK03584 249 PAEAAE-LEFEPVPFdhplWILYSSGTTGLPK-----------CIvhghGGILLehlkelglHCDLGPGDRFF----WYT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 272 ALGYM----HAAlAMFLGSTLVLR--RRFKPAL-VLED-IEKHKATSMVVVPvmlsRILDQLEKTEPKP----DLSSLKI 339
Cdd:PRK03584 313 TCGWMmwnwLVS-GLLVGATLVLYdgSPFYPDPnVLWDlAAEEGVTVFGTSA----KYLDACEKAGLVPgethDLSALRT 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 340 VFVSGSQLGAELATRALGDLGPVIY--NMYGSTEVAFATIAGpkdlqfNPSTvgPVVKG--------VTVKILDENGNEV 409
Cdd:PRK03584 388 IGSTGSPLPPEGFDWVYEHVKADVWlaSISGGTDICSCFVGG------NPLL--PVYRGeiqcrglgMAVEAWDEDGRPV 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 410 pQGAVGRIFVGNAFP-------------------FEGYtggggkqiiDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGE 470
Cdd:PRK03584 460 -VGEVGELVCTKPFPsmplgfwndpdgsryrdayFDTF---------PGVWRHGDWIEITEHGGVVIYGRSDATLNRGGV 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 471 NVFPAE----VEDLisghPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDED---TIKQYVRDHLARYKVPREVIFLDE 543
Cdd:PRK03584 530 RIGTAEiyrqVEAL----PEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDAlraRIRTTIRTNLSPRHVPDKIIAVPD 605
|
570
....*....|....*..
gi 801237227 544 LPRNPTGKVLKRELRKL 560
Cdd:PRK03584 606 IPRTLSGKKVELPVKKL 622
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
71-557 |
4.46e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 98.32 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:PRK05691 2198 AARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERL 2277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTKAvslaqppLGKLRAlGVNP---DDDKPSgssdetlaelIAHSSTAPAPKAS--RRASIII 225
Cdd:PRK05691 2278 HYMIEDSGIGLLLSDRALFEA-------LGELPA-GVARwclEDDAAA----------LAAYSDAPLPFLSlpQHQAYLI 2339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 226 LTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLlpspMFHALGYMHAA----LAMFLGSTLVLRRR--FKPALV 299
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCEL----HFYSINFDAASerllVPLLCGARVVLRAQgqWGAEEI 2415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVMLSRILDQLEKtepKPDLSSLKIVFVSGSQLGAELATRALGDLGP-VIYNMYGSTEVAFATIA 378
Cdd:PRK05691 2416 CQLIREQQVSILGFTPSYGSQLAQWLAG---QGEQLPVRMCITGGEALTGEHLQRIRQAFAPqLFFNAYGPTETVVMPLA 2492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 379 --GPKDLQFNPSTV--GPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQI---------IDG--LLSS 443
Cdd:PRK05691 2493 clAPEQLEEGAASVpiGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAerfvadpfaADGgrLYRT 2572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 444 GDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVdDKEFGARLRAFVVKKPGADLDE----- 518
Cdd:PRK05691 2573 GDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAVAGQDDEaqaal 2651
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 801237227 519 -DTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK05691 2652 rEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
71-557 |
1.54e-20 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 94.54 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI 150
Cdd:cd17645 8 VERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIyddeytkavslaqpplgklralgVNPDDdkpsgssdetlaeliahsstapapkasrrASIIILTSGT 230
Cdd:cd17645 88 AYMLADSSAKILL-----------------------TNPDD-----------------------------LAYVIYTSGS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKGAnrnTPPTLAPIGGILSHVP-FKAGEVTllPSPMFHALGYMHAALAMF----LGSTL-VLRRRFKPALV-LEDI 303
Cdd:cd17645 116 TGLPKGV---MIEHHNLVNLCEWHRPyFGVTPAD--KSLVYASFSFDASAWEIFphltAGAALhVVPSERRLDLDaLNDY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 304 EKHKATSMVVVPVMLSRILDQLEKTepkpdlsSLKIVFVSGSQLgaelatRALGDLGPVIYNMYGSTEVAFATIAGPKDL 383
Cdd:cd17645 191 FNQEGITISFLPTGAAEQFMQLDNQ-------SLRVLLTGGDKL------KKIERKGYKLVNNYGPTENTVVATSFEIDK 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 384 QFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTG----GGGKQIIDGLLS------SGDVGYFDERG 453
Cdd:cd17645 258 PYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNrpelTAEKFIVHPFVPgermyrTGDLAKFLPDG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 454 LLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEdtIKQYVRDHLARYK 533
Cdd:cd17645 338 NIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEE--LREWLKNDLPDYM 415
|
490 500
....*....|....*....|....
gi 801237227 534 VPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17645 416 IPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
71-560 |
3.34e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 91.91 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 71 ARRAPNRAAVIDEEGT-LTFSELDEAAHAVANgLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQ 149
Cdd:PRK08633 625 AKRNWSRLAVADSTGGeLSYGKALTGALALAR-LLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAA 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 150 IKEVSDREGAKVIIYDDEY-----TKAVSLAQPPLGKLRALgvnpDDDKPSGSSDETLAELIAhSSTAPA---------- 214
Cdd:PRK08633 704 LKSAIEQAQIKTVITSRKFleklkNKGFDLELPENVKVIYL----EDLKAKISKVDKLTALLA-ARLLPArllkrlygpt 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 215 PKASRRASIIiLTSGTTGTPKG---ANRNTpptLAPIGGILSHVPFKAGEVTLLPSPMFHALGymhaalamFLGST-LVL 290
Cdd:PRK08633 779 FKPDDTATII-FSSGSEGEPKGvmlSHHNI---LSNIEQISDVFNLRNDDVILSSLPFFHSFG--------LTVTLwLPL 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 291 RRRFK------P---ALVLEDIEKHKATSMVVVPVMLsRILDQLEKTEPKpDLSSLKIVFVSGSQLGAELATRALGDLGP 361
Cdd:PRK08633 847 LEGIKvvyhpdPtdaLGIAKLVAKHRATILLGTPTFL-RLYLRNKKLHPL-MFASLRLVVAGAEKLKPEVADAFEEKFGI 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 362 VIYNMYGSTE---VAFATIAGPKDLQFN------PSTVGPVVKGVTVKILD-ENGNEVPQGAVGRIFVGNAFPFEGYTGG 431
Cdd:PRK08633 925 RILEGYGATEtspVASVNLPDVLAADFKrqtgskEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGD 1004
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 432 GGK-----QIIDGL--LSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISG--HPDVVEAAAIGVDDKEFGA 502
Cdd:PRK08633 1005 PEKtaeviKDIDGIgwYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGE 1084
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 801237227 503 RLraFVVKKPGAdLDEDTIKQYVRD-HLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK08633 1085 KL--VVLHTCGA-EDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
86-500 |
4.35e-18 |
|
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: 87.80 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNH-RWFvIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIY 164
Cdd:cd05933 8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSpEWF-IAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 165 DDEYTKAVSLA-QPPLGKLRA---LGVNPDDDKPS------------GSSDETLAELIahSSTAPapkasRRASIIILTS 228
Cdd:cd05933 87 ENQKQLQKILQiQDKLPHLKAiiqYKEPLKEKEPNlyswdefmelgrSIPDEQLDAII--SSQKP-----NQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 229 GTTGTPKG---ANRNTPPTLAPIGGILSHVPFKAGE---VTLLPSPMFHA------LGYMHAALAMF-----LGSTLV-L 290
Cdd:cd05933 160 GTTGMPKGvmlSHDNITWTAKAASQHMDLRPATVGQesvVSYLPLSHIAAqildiwLPIKVGGQVYFaqpdaLKGTLVkT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 291 RRRFKPAL------VLEDI-EKHKA----------------------TSMVVV-----PVMLSRILDQL--EKTEPKPDL 334
Cdd:cd05933 240 LREVRPTAfmgvprVWEKIqEKMKAvgaksgtlkrkiaswakgvgleTNLKLMggespSPLFYRLAKKLvfKKVRKALGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 335 SSLKIVFVSGSQLGAELATRALGdLGPVIYNMYGSTEVAFA-TIAGPKDLQFNpsTVGPVVKGVTVKILDENGNevpqgA 413
Cdd:cd05933 320 DRCQKFFTGAAPISRETLEFFLS-LNIPIMELYGMSETSGPhTISNPQAYRLL--SCGKALPGCKTKIHNPDAD-----G 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 414 VGRIFVGNAFPFEGYTGGGGK--QIID--GLLSSGDVGYFDERGLLYVSGRDDEMIV-SGGENVFPAEVEDLISGHPDVV 488
Cdd:cd05933 392 IGEICFWGRHVFMGYLNMEDKteEAIDedGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVPPVPIEDAVKKELPII 471
|
490
....*....|..
gi 801237227 489 EAAAIGVDDKEF 500
Cdd:cd05933 472 SNAMLIGDKRKF 483
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
86-532 |
5.90e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 86.75 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNsefsgpqikevsdregakviiyd 165
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLID----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 166 deytkavslaqPPLGKlRALGVNPDDDKPSGSSDETLAELIAhsstapapkasrrasIIILTSGTTGTPKGANRNTPPTL 245
Cdd:cd05910 59 -----------PGMGR-KNLKQCLQEAEPDAFIGIPKADEPA---------------AILFTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 246 APIGGILSHVPFKAGEVTLLPSPMFhalgymhAALAMFLGSTLVL-----RR--RFKPALVLEDIEKHKATSMVVVPVML 318
Cdd:cd05910 112 AQIDALRQLYGIRPGEVDLATFPLF-------ALFGPALGLTSVIpdmdpTRpaRADPQKLVGAIRQYGVSIVFGSPALL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 319 SRILDQLEKTEPKpdLSSLKIVFVSGSQLGAELATR---ALGDLGPvIYNMYGSTEVAFATIAGPKDL----QFNPST-- 389
Cdd:cd05910 185 ERVARYCAQHGIT--LPSLRRVLSAGAPVPIALAARlrkMLSDEAE-ILTPYGATEALPVSSIGSRELlattTAATSGga 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 390 ---VGPVVKGVTVKILD---------ENGNEVPQGAVGRIFVGNAFPFEGYTG-----------GGGKQIidgLLSSGDV 446
Cdd:cd05910 262 gtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNrpvatalakidDNSEGF---WHRMGDL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 447 GYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKefGARLRAFVVKK-PGADLDEDTIKQYV 525
Cdd:cd05910 339 GYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKP--GCQLPVLCVEPlPGTITPRARLEQEL 416
|
....*..
gi 801237227 526 RDHLARY 532
Cdd:cd05910 417 RALAKDY 423
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
224-552 |
5.96e-18 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 86.87 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 IILTSGTTGTPKG-----ANrntppTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRR---FK 295
Cdd:PRK04813 148 IIFTSGTTGKPKGvqishDN-----LVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKdmtAN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 296 PALVLEDIEKHKATSMVVVP-----VMLSRILDQlEKtepkpdLSSLKIVFVSGSQLGAELAtRALGDLGP--VIYNMYG 368
Cdd:PRK04813 223 FKQLFETLPQLPINVWVSTPsfadmCLLDPSFNE-EH------LPNLTHFLFCGEELPHKTA-KKLLERFPsaTIYNTYG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 369 STE--VAFATIAGPKDL--QFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFV-GNAFPfEGYTGGGGKQ-----IID 438
Cdd:PRK04813 295 PTEatVAVTSIEITDEMldQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVIsGPSVS-KGYLNNPEKTaeaffTFD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 439 GLLS--SGDVGYFDErGLLYVSGRDDEMIVSGGenvFPAEVEDlISGH----PDVVEAAAIGVDDKEFGARLRAFVVKKP 512
Cdd:PRK04813 374 GQPAyhTGDAGYLED-GLLFYQGRIDFQIKLNG---YRIELEE-IEQNlrqsSYVESAVVVPYNKDHKVQYLIAYVVPKE 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 801237227 513 GaDLDED-----TIKQYVRDHLARYKVPREVIFLDELPRNPTGKV 552
Cdd:PRK04813 449 E-DFEREfeltkAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKI 492
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
224-557 |
5.23e-17 |
|
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: 83.68 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 IILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTL--------VLRRRFK 295
Cdd:cd17654 123 VIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLlivptsvkVLPSKLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 296 PALvledIEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQL--GAELATRALGDLGPVIYNMYGSTEV- 372
Cdd:cd17654 203 DIL----FKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFpsLVILSSWRGKGNRTRIFNIYGITEVs 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 373 AFATIAGPKDLQfNPSTVGPVVKGVTVKILDENGNEVPqgavGRIFVGnafpfeGYTGGGgkqIIDGLL--------SSG 444
Cdd:cd17654 279 CWALAYKVPEED-SPVQLGSPLLGTVIEVRDQNGSEGT----GQVFLG------GLNRVC---ILDDEVtvpkgtmrATG 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 445 DVGYFdERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHpDVVEAAAIGVDDKEfgaRLRAFVVKKPGADLDEDTIkqy 524
Cdd:cd17654 345 DFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESC-LGVESCAVTLSDQQ---RLIAFIVGESSSSRIHKEL--- 416
|
330 340 350
....*....|....*....|....*....|...
gi 801237227 525 VRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17654 417 QLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
220-559 |
9.73e-17 |
|
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: 82.92 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 220 RASIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALA--------MFLGSTLVLR 291
Cdd:cd05908 107 ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLApliagmnqYLMPTRLFIR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 292 RrfkPALVLEDIEKHKATsMVVVPVMLSR-ILDQLEKTEPKP-DLSSLKIVFVSGSQLGAELATRALGDLGP------VI 363
Cdd:cd05908 187 R---PILWLKKASEHKAT-IVSSPNFGYKyFLKTLKPEKANDwDLSSIRMILNGAEPIDYELCHEFLDHMSKyglkrnAI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 364 YNMYGSTEVAFATIAGPKDLQFNPST---------------------------VGPVVKGVTVKILDENGNEVPQGAVGR 416
Cdd:cd05908 263 LPVYGLAEASVGASLPKAQSPFKTITlgrrhvthgepepevdkkdsecltfveVGKPIDETDIRICDEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 417 IFVGNAFPFEGYTGG--GGKQII--DGLLSSGDVGY-FDERglLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVV--E 489
Cdd:cd05908 343 IQIRGKNVTPGYYNNpeATAKVFtdDGWLKTGDLGFiRNGR--LVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgR 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 801237227 490 AAAIGVDDKEFGA-RLRAFVVKKPGADlDEDTIKQYVRDHLARYKVPR--EVIFLDELPRNPTGKVLKRELRK 559
Cdd:cd05908 421 VVACGVNNSNTRNeEIFCFIEHRKSED-DFYPLGKKIKKHLNKRGGWQinEVLPIRRIPKTTSGKVKRYELAQ 492
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
222-484 |
7.95e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 80.25 E-value: 7.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 222 SIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAAL-AMFLGSTLVLRRR-FKPALV 299
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLfPLLSGVPVVFAYNpLYPKKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LEDIEKHKATSMVVVPVMLSRILDQLEKTEPKpdLSSLKIVFVSGSQLGAELATRALGDLGPV-IYNMYGSTE----VAF 374
Cdd:PRK06334 266 VEMIDEAKVTFLGSTPVFFDYILKTAKKQESC--LPSLRFVVIGGDAFKDSLYQEALKTFPHIqLRQGYGTTEcspvITI 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 375 ATIAGPKdlqfNPSTVGPVVKGVTVKILDENGN-EVPQGAVGRIFVGNAFPFEGYTG---GGGKQIIDGLL--SSGDVGY 448
Cdd:PRK06334 344 NTVNSPK----HESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGedfGQGFVELGGETwyVTGDLGY 419
|
250 260 270
....*....|....*....|....*....|....*.
gi 801237227 449 FDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGH 484
Cdd:PRK06334 420 VDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
86-557 |
2.38e-15 |
|
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: 78.71 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSgPqikevsdregAKVIIYd 165
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYP-P----------ARQNIY- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 166 deytkaVSLAQPP-LGKLRALGV--NPDddkpsgsSDETLAeliahsstapapkasrrasiiiLTSGTTGTPKGAnRNTP 242
Cdd:cd17647 88 ------LGVAKPRgLIVIRAAGVvvGPD-------SNPTLS----------------------FTSGSEGIPKGV-LGRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 243 PTLApiggilSHVPFKAGEVTLLPSPMFHAL-GYMHAALA------MFLGSTLVLRRR---FKPALVLEDIEKHKATSMV 312
Cdd:cd17647 132 FSLA------YYFPWMAKRFNLSENDKFTMLsGIAHDPIQrdmftpLFLGAQLLVPTQddiGTPGRLAEWMAKYGATVTH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 313 VVPVMLSRILDQleKTEPKPdlsSLKIVFVSGSQLGAELATRaLGDLGPV--IYNMYGSTEVA-----FATIAGPKDLQF 385
Cdd:cd17647 206 LTPAMGQLLTAQ--ATTPFP---KLHHAFFVGDILTKRDCLR-LQTLAENvrIVNMYGTTETQravsyFEVPSRSSDPTF 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 386 --NPSTVGPVVKGV-TVKILDENGNEVPQ----GAVGRIFVGNAFPFEGYTGG---GGKQII------------------ 437
Cdd:cd17647 280 lkNLKDVMPAGRGMlNVQLLVVNRNDRTQicgiGEVGEIYVRAGGLAEGYRGLpelNKEKFVnnwfvepdhwnyldkdnn 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 438 -----------DGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRA 506
Cdd:cd17647 360 epwrqfwlgprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVS 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 801237227 507 FVVKKPGADLDEDT---------------------------IKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:cd17647 440 YIVPRFDKPDDESFaqedvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
87-494 |
7.05e-15 |
|
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: 77.12 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 87 LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIY-- 164
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 165 --DDEYTKAVSLAQPPLGKLRALGVNPDDDKPsgssdETLAELIAHSSTAPAPKASRRASIIiLTSGTTGTPKGANRNTP 242
Cdd:cd05932 87 ldDWKAMAPGVPEGLISISLPPPSAANCQYQW-----DDLIAQHPPLEERPTRFPEQLATLI-YTSGTTGQPKGVMLTFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 243 PTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLrrrFKPAL--VLEDIEKHKATSMVVVPVMLS- 319
Cdd:cd05932 161 SFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVA---FAESLdtFVEDVQRARPTLFFSVPRLWTk 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 320 ---RILDQLektePKPDLSS-LKIVFVSG-------SQLGAELATRALGDLGPV--------------IYNMYGSTE-VA 373
Cdd:cd05932 238 fqqGVQDKI----PQQKLNLlLKIPVVNSlvkrkvlKGLGLDQCRLAGCGSAPVppallewyrslglnILEAYGMTEnFA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 374 FATIAGPKDLQFnpSTVGPVVKGVTVKILDEngnevpqgavGRIFVGNAFPFEGY----TGGGGKQIIDGLLSSGDVGYF 449
Cdd:cd05932 314 YSHLNYPGRDKI--GTVGNAGPGVEVRISED----------GEILVRSPALMMGYykdpEATAEAFTADGFLRTGDKGEL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 801237227 450 DERGLLYVSGRDDEMI-VSGGENVFPAEVEDLISGHPDVVEAAAIG 494
Cdd:cd05932 382 DADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
84-560 |
9.88e-15 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 77.25 E-value: 9.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 84 EGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQI-KEVSD------- 155
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLaQRIVDckpkvvi 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 156 -----REGAKVI----IYD---DEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAELIA-HSSTAPAPKASRRAS 222
Cdd:PLN02654 198 tcnavKRGPKTInlkdIVDaalDESAKNGVSVGICLTYENQLAMKREDTKWQEGRDVWWQDVVPnYPTKCEVEWVDAEDP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 223 IIIL-TSGTTGTPKGANRNTPPTLAPIGGILSHV-PFKAGEVTLLPSPMFHALGYMHAALA-MFLGSTLVLrrrFKPALV 299
Cdd:PLN02654 278 LFLLyTSGSTGKPKGVLHTTGGYMVYTATTFKYAfDYKPTDVYWCTADCGWITGHSYVTYGpMLNGATVLV---FEGAPN 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 300 LED-------IEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAElATR----ALGDLGPVIYNMYG 368
Cdd:PLN02654 355 YPDsgrcwdiVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPS-AWRwffnVVGDSRCPISDTWW 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 369 STEVA-FATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQIID--------G 439
Cdd:PLN02654 434 QTETGgFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYEttyfkpfaG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 440 LLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDED 519
Cdd:PLN02654 514 YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE 593
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 801237227 520 TIKQY---VRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PLN02654 594 LRKSLiltVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
86-508 |
2.71e-14 |
|
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: 75.54 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYD 165
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 166 DE--YTKAVSLAqPPLGKLRAL------GVNPDDDKPSGSSDETLAELIAHSstAPAPKASRRA---------SIIILTS 228
Cdd:cd17641 91 DEeqVDKLLEIA-DRIPSVRYViycdprGMRKYDDPRLISFEDVVALGRALD--RRDPGLYEREvaagkgedvAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 229 GTTGTPKGANRNTPPTLAPIGGILSHVPFKAGE--VTLLPSPMFHALGYMhAALAMFLGSTLvlrrRF--KPALVLEDIE 304
Cdd:cd17641 168 GTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDeyVSVLPLPWIGEQMYS-VGQALVCGFIV----NFpeEPETMMEDLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 305 KHKATSMVVVP----VMLS-------------------------RILDQLEKTEPKPD---------------------- 333
Cdd:cd17641 243 EIGPTFVLLPPrvweGIAAdvrarmmdatpfkrfmfelgmklglRALDRGKRGRPVSLwlrlaswladallfrplrdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 334 LSSLKIVFVSGSQLGAELAT--RALG-DLGPViynmYGSTEVAFATIAGPkDLQFNPSTVGPVVKGVTVKIlDEngnevp 410
Cdd:cd17641 323 FSRLRSAATGGAALGPDTFRffHAIGvPLKQL----YGQTELAGAYTVHR-DGDVDPDTVGVPFPGTEVRI-DE------ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 411 qgaVGRIFVGNAFPFEGYTGGGGKQII----DGLLSSGDVGYFDERGLLYVSGR-DDEMIVSGGENVFPAEVEDLISGHP 485
Cdd:cd17641 391 ---VGEILVRSPGVFVGYYKNPEATAEdfdeDGWLHTGDAGYFKENGHLVVIDRaKDVGTTSDGTRFSPQFIENKLKFSP 467
|
490 500
....*....|....*....|...
gi 801237227 486 DVVEAAAIGvDDKEFgarLRAFV 508
Cdd:cd17641 468 YIAEAVVLG-AGRPY---LTAFI 486
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
179-559 |
6.43e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 74.42 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 179 LGKLRALgvnpdddkPSGSSDETLAElIAHS--STAPAPKASRRASIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVP 256
Cdd:PRK05851 119 LERLRAV--------DSSVTVHDLAT-AAHTnrSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 257 FKAGE-VTLLPSPMFHALGYMHAALAMFLGSTLVL--RRRFK--PALVLEDIEKHKATsMVVVPVMLSRILDQLEKTEPK 331
Cdd:PRK05851 190 LDAATdVGCSWLPLYHDMGLAFLLTAALAGAPLWLapTTAFSasPFRWLSWLSDSRAT-LTAAPNFAYNLIGKYARRVSD 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 332 PDLSSLKIVFVSGSQLGAELATRALGDLGPVIYN------MYGSTEVAFA-TIAGPKD-LQFNPST------------VG 391
Cdd:PRK05851 269 VDLGALRVALNGGEPVDCDGFERFATAMAPFGFDagaaapSYGLAESTCAvTVPVPGIgLRVDEVTtddgsgarrhavLG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 392 PVVKGVTVKILDENGN-EVPQGAVGRIFVGNAFPFEGYTGGggkQIID--GLLSSGDVGYFDERGLLyVSGRDDEMIVSG 468
Cdd:PRK05851 349 NPIPGMEVRISPGDGAaGVAGREIGEIEIRGASMMSGYLGQ---APIDpdDWFPTGDLGYLVDGGLV-VCGRAKELITVA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 469 GENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRaFVVKKPGADLDEDTIKQYVRDHLARY--KVPREVIFLD--EL 544
Cdd:PRK05851 425 GRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPG-LVIAAEFRGPDEAGARSEVVQRVASEcgVVPSDVVFVApgSL 503
|
410
....*....|....*
gi 801237227 545 PRNPTGKVLKRELRK 559
Cdd:PRK05851 504 PRTSSGKLRRLAVKR 518
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
181-551 |
2.93e-13 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 71.72 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 181 KLRALGVNPDDDKpsgsSDETLA--------ELIAH----SSTAPAPKASRrasiIILTSGTTGTPKGANRnTPPTLAPI 248
Cdd:COG1541 41 KFDEAGVDPDDIK----SLEDLAklpfttkeDLRDNypfgLFAVPLEEIVR----IHASSGTTGKPTVVGY-TRKDLDRW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 249 GGILSHVPFKAGeVTllPSPMFH-ALGY--------MHAALAMfLGSTLVlrrrfkPA------LVLEDIEKHKATSMVV 313
Cdd:COG1541 112 AELFARSLRAAG-VR--PGDRVQnAFGYglftgglgLHYGAER-LGATVI------PAgggnteRQLRLMQDFGPTVLVG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 314 VPVMLSRILDQLEKTEPKPDLSSLKIVFVSG----SQLGAELATRalgdLGPVIYNMYGSTEVafatiagpkdlqfnpst 389
Cdd:COG1541 182 TPSYLLYLAEVAEEEGIDPRDLSLKKGIFGGepwsEEMRKEIEER----WGIKAYDIYGLTEV----------------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 390 vGPVV-------KG-------VTVKILD-ENGNEVPQGAVGRI----FVGNAFPfegytggggkqiidgLL--SSGDVGY 448
Cdd:COG1541 241 -GPGVayeceaqDGlhiwedhFLVEIIDpETGEPVPEGEEGELvvttLTKEAMP---------------LIryRTGDLTR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 449 FDE---------RGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLD-- 517
Cdd:COG1541 305 LLPepcpcgrthPRIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEal 384
|
410 420 430
....*....|....*....|....*....|....*.
gi 801237227 518 EDTIKQYVRDHLaryKVPREVIFL--DELPRnPTGK 551
Cdd:COG1541 385 AEAIAAALKAVL---GLRAEVELVepGSLPR-SEGK 416
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
86-559 |
5.80e-13 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 71.65 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIK---EVSDREG---A 159
Cdd:PLN03052 208 RMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIAtrlKISKAKAiftQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 160 KVIIYDDE----YTKAVSlAQPPlgklRALgVNPDDDKPSG----SSDETLAELIAHSSTAPAPKASRRA-------SII 224
Cdd:PLN03052 288 DVIVRGGKsiplYSRVVE-AKAP----KAI-VLPADGKSVRvklrEGDMSWDDFLARANGLRRPDEYKAVeqpveafTNI 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 225 ILTSGTTGTPKGanrnTPPT-LAPI---GGILSHVPFKAGEVTLLPSpmfhALGYMH------------AALAMFLGSTL 288
Cdd:PLN03052 362 LFSSGTTGEPKA----IPWTqLTPLraaADAWAHLDIRKGDIVCWPT----NLGWMMgpwlvyasllngATLALYNGSPL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 289 vlRRRFkpALVLEDIekhKATSMVVVPVML-----SRILDQLektepkpDLSSLKIVFVSG--SQLGAELATRALGDLGP 361
Cdd:PLN03052 434 --GRGF--AKFVQDA---KVTMLGTVPSIVktwknTNCMAGL-------DWSSIRCFGSTGeaSSVDDYLWLMSRAGYKP 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 362 VIyNMYGSTEVAFATIAG----PKDL-QFnpSTVGpvvKGVTVKILDENGNEVPQGAVGRIFVG-------------NAF 423
Cdd:PLN03052 500 II-EYCGGTELGGGFVTGsllqPQAFaAF--STPA---MGCKLFILDDSGNPYPDDAPCTGELAlfplmfgasstllNAD 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 424 PFEGYTGG----GGKQiidgLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLI-SGHPDVVEAAAIGVDDK 498
Cdd:PLN03052 574 HYKVYFKGmpvfNGKI----LRRHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPP 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 801237227 499 EFGA-RLRAFVVKK--PGADLDEDTIKQYVRDHLAR-----YKVPREVIFlDELPRNPTGKVLKRELRK 559
Cdd:PLN03052 650 GGGPeQLVIAAVLKdpPGSNPDLNELKKIFNSAIQKklnplFKVSAVVIV-PSFPRTASNKVMRRVLRQ 717
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
70-557 |
6.92e-13 |
|
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: 71.63 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 70 NARRAPNRAAVI---------DEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGA---- 136
Cdd:TIGR03443 245 NAEKHPDRTCVVetpsfldpsSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGAtfsv 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 137 ---------RII---------LLNSEFSGPQIKEVSDregakviiYDDEYTKAVSLaqpplgkLRALGVNPDDD----KP 194
Cdd:TIGR03443 325 idpaypparQTIylsvakpraLIVIEKAGTLDQLVRD--------YIDKELELRTE-------IPALALQDDGSlvggSL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 195 SGSSDETLAELIAhsstapapKASRRASIII---------LTSGTTGTPKGAnRNTPPTLApiggilSHVPFKAGEVTLL 265
Cdd:TIGR03443 390 EGGETDVLAPYQA--------LKDTPTGVVVgpdsnptlsFTSGSEGIPKGV-LGRHFSLA------YYFPWMAKRFGLS 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 266 PSPMFHAL-GYMHAALA------MFLGSTLVLRRR---FKPALVLEDIEKHKATSMVVVPVMlsrilDQL---EKTEPKP 332
Cdd:TIGR03443 455 ENDKFTMLsGIAHDPIQrdmftpLFLGAQLLVPTAddiGTPGRLAEWMAKYGATVTHLTPAM-----GQLlsaQATTPIP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 333 dlsSLKIVFVSGSQLGAELATRaLGDLGP--VIYNMYGSTE----VAFATIAGPK-DLQF--NPSTVGPVVKG-VTVKIL 402
Cdd:TIGR03443 530 ---SLHHAFFVGDILTKRDCLR-LQTLAEnvCIVNMYGTTEtqraVSYFEIPSRSsDSTFlkNLKDVMPAGKGmKNVQLL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 403 DENGNEVPQ----GAVGRIFVGNAFPFEGYTGG----------------------------GGKQ----IIDGLLSSGDV 446
Cdd:TIGR03443 606 VVNRNDRTQtcgvGEVGEIYVRAGGLAEGYLGLpelnaekfvnnwfvdpshwidldkennkPEREfwlgPRDRLYRTGDL 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 447 GYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGA----------DL 516
Cdd:TIGR03443 686 GRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKSdeleefksevDD 765
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 801237227 517 DEDT----------------IKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:TIGR03443 766 EESSdpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
224-557 |
7.17e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.12 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 224 IILTSGTTGTPKGANRNTPPTLapiGGILSHVPF----KAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRF--KPA 297
Cdd:PRK05691 3874 VIYTSGSTGLPKGVMVEQRGML---NNQLSKVPYlalsEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIahDPQ 3950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 298 LVLEDIEKHKATSMVVVPVMLSRILdqlekTEPKPDLSSLKIVFVSGSQLGAELATRAL---GDLGPViyNMYG----ST 370
Cdd:PRK05691 3951 GLLAHVQAQGITVLESVPSLIQGML-----AEDRQALDGLRWMLPTGEAMPPELARQWLqryPQIGLV--NAYGpaecSD 4023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 371 EVAFATIagpkDLQFNPSTVGPV---VKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYT---------------GGG 432
Cdd:PRK05691 4024 DVAFFRV----DLASTRGSYLPIgspTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVgdplrtalafvphpfGAP 4099
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 433 GKQiidgLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAaIGVDDKEFGARLRAFVVKKP 512
Cdd:PRK05691 4100 GER----LYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQ 4174
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 801237227 513 GADLDE---DTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKREL 557
Cdd:PRK05691 4175 TVLAQGallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
396-560 |
5.06e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 68.63 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 396 GVTVKILDENGNEVPQGAVGRIFVGNAFP-----------------FEGYTGGggkqiidglLSSGDVGYFDERGLLYVS 458
Cdd:PRK00174 432 GIQPAVVDEEGNPLEGGEGGNLVIKDPWPgmmrtiygdherfvktyFSTFKGM---------YFTGDGARRDEDGYYWIT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 459 GR-DDEMIVSG---GEnvfpAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQyVRDHLAR--- 531
Cdd:PRK00174 503 GRvDDVLNVSGhrlGT----AEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKE-LRNWVRKeig 577
|
170 180 190
....*....|....*....|....*....|
gi 801237227 532 -YKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK00174 578 pIAKPDVIQFAPGLPKTRSGKIMRRILRKI 607
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
391-560 |
2.34e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 66.18 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 391 GPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQ---IIDGLLSSGDVGYFDErGLLYVSGRDDEMIVS 467
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQdvlAADGWLDTGDLGYLLD-GYLYITGRAKDLIII 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 468 GGENVFPAEVEDLISGHPDVV--EAAAIGVDDkEFGARLrAFVVKKPGADLDE-----DTIKQYVRdhlARYKVPREVIF 540
Cdd:PRK09192 467 NGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQ-ENGEKI-VLLVQCRISDEERrgqliHALAALVR---SEFGVEAAVEL 541
|
170 180
....*....|....*....|..
gi 801237227 541 L--DELPRNPTGKVLKRELRKL 560
Cdd:PRK09192 542 VppHSLPRTSSGKLSRAKAKKR 563
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
72-560 |
6.01e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 62.29 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 72 RRAPNRAAVID-EEGTLTFSELDEAAhAVANGLLAKGVRAGDGVAILARN-----------HRW-FVIA--NY--GAARV 134
Cdd:PRK06814 643 IHGFKKLAVEDpVNGPLTYRKLLTGA-FVLGRKLKKNTPPGENVGVMLPNangaavtffalQSAgRVPAmiNFsaGIANI 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 135 -------GARIILLNSEFS-----GPQIKEVSdrEGAKvIIYDDEYTKAVSLAQPPLGKL-----RALGVNPDDDKPSgs 197
Cdd:PRK06814 722 lsackaaQVKTVLTSRAFIekarlGPLIEALE--FGIR-IIYLEDVRAQIGLADKIKGLLagrfpLVYFCNRDPDDPA-- 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 198 sdetlaeliahsstapapkasrrasIIILTSGTTGTPKG---ANRNTpptLAPIGGILSHVPFKAGEVTLLPSPMFHALG 274
Cdd:PRK06814 797 -------------------------VILFTSGSEGTPKGvvlSHRNL---LANRAQVAARIDFSPEDKVFNALPVFHSFG 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 275 YMHAALAMFLGSTLV------LRRRFKPALVLEDiekhKATSMVVVPVMLSrildQLEKTEPKPDLSSLKIVFVSGSQLG 348
Cdd:PRK06814 849 LTGGLVLPLLSGVKVflypspLHYRIIPELIYDT----NATILFGTDTFLN----GYARYAHPYDFRSLRYVFAGAEKVK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 349 AElaTRAL--GDLGPVIYNMYGSTEVAfATIAGPKDLQFNPSTVGPVVKGVTVKILDENGneVPQGavGRIFVGNAFPFE 426
Cdd:PRK06814 921 EE--TRQTwmEKFGIRILEGYGVTETA-PVIALNTPMHNKAGTVGRLLPGIEYRLEPVPG--IDEG--GRLFVRGPNVML 993
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 427 GYTGGGGKQII----DGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISG-HPDVvEAAAIGVDDKEFG 501
Cdd:PRK06814 994 GYLRAENPGVLeppaDGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDA-LHAAVSIPDARKG 1072
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 502 ARLrafVVKKPGADLDEDTIKQYVRDH-LARYKVPREVIFLDELPRNPTGKVLKRELRKL 560
Cdd:PRK06814 1073 ERI---ILLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
87-528 |
8.11e-10 |
|
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: 61.46 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 87 LTFSELDEAAHAVANGLLAKGVRAGDG--VAILARNHRWFVIANYGAARVG--------------ARIILLNSEfsgpqI 150
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSlvtvplydtlgpeaIEYILNHAE-----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 151 KEVSDREGAKVIIYDDEYTkavslaqppLGKLRALGVNPDddKPsgssdETLAeliahsstapapkasrrasIIILTSGT 230
Cdd:cd05927 81 SIVFCDAGVKVYSLEEFEK---------LGKKNKVPPPPP--KP-----EDLA-------------------TICYTSGT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 231 TGTPKGA---NRNTPPTLAPIGGIL-SHVPFKAGEVTL--LPSP-----MFHALGYMH-AALAMFLGSTLVLrrrfkpal 298
Cdd:cd05927 126 TGNPKGVmltHGNIVSNVAGVFKILeILNKINPTDVYIsyLPLAhiferVVEALFLYHgAKIGFYSGDIRLL-------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 299 vLEDIEKHKATSMVVVPVMLSRILD--------------------------QLEKTEPKPDLSSLKIVF----------- 341
Cdd:cd05927 198 -LDDIKALKPTVFPGVPRVLNRIYDkifnkvqakgplkrklfnfalnyklaELRSGVVRASPFWDKLVFnkikqalggnv 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 342 ---VSGSQ-LGAELATRALGDLGPVIYNMYGSTE-VAFATIAGPKDlqFNPSTVGPVVKGVTVKILD--ENG----NEVP 410
Cdd:cd05927 277 rlmLTGSApLSPEVLEFLRVALGCPVLEGYGQTEcTAGATLTLPGD--TSVGHVGGPLPCAEVKLVDvpEMNydakDPNP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 411 QGAVgrIFVGNAFpFEGY------TggggKQII--DGLLSSGDVGYFDERGLLYVSGRDDEMI-VSGGENVFPAEVEDLI 481
Cdd:cd05927 355 RGEV--CIRGPNV-FSGYykdpekT----AEALdeDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIY 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 801237227 482 SGHPDVveaAAIGVDDKEFGARLRAFVVkkpgadLDEDTIKQYVRDH 528
Cdd:cd05927 428 ARSPFV---AQIFVYGDSLKSFLVAIVV------PDPDVLKEWAASK 465
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
86-539 |
1.57e-09 |
|
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: 60.55 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 86 TLTFSELDEAAHAVANGLLAKG-VRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIY 164
Cdd:cd17632 67 TITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 165 DDEY---TKAVSLAQPPLGKLRALGVNPDDDK-------------PSGSSDETLAELIAHSSTAPAPKASR------RAS 222
Cdd:cd17632 147 SAEHldlAVEAVLEGGTPPRLVVFDHRPEVDAhraalesarerlaAVGIPVTTLTLIAVRGRDLPPAPLFRpepdddPLA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 223 IIILTSGTTGTPKGA---NRNTPP---TLAPIGGI------------LSHVpfkAGEVTLLPSPMFHALGYMHAALAMfl 284
Cdd:cd17632 227 LLIYTSGSTGTPKGAmytERLVATfwlKVSSIQDIrppasitlnfmpMSHI---AGRISLYGTLARGGTAYFAAASDM-- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 285 gSTLvlrrrfkpalvLEDIEKHKATSMVVVP----VMLSRILDQLE----------------KTEPKPDL--SSLKIVFV 342
Cdd:cd17632 302 -STL-----------FDDLALVRPTELFLVPrvcdMLFQRYQAELDrrsvagadaetlaervKAELRERVlgGRLLAAVC 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 343 SGSQLGAELATRALGDLGPVIYNMYGSTEvafatiAGpkdlqfnpstvGPVVKGVTVK--ILDENGNEVPQGAV------ 414
Cdd:cd17632 370 GSAPLSAEMKAFMESLLDLDLHDGYGSTE------AG-----------AVILDGVIVRppVLDYKLVDVPELGYfrtdrp 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 415 ---GRIFVGNAFPFEGY--TGGGGKQIID--GLLSSGDVgyFDERG---LLYVSGRDDEMIVSGGENVFPAEVEDLISGH 484
Cdd:cd17632 433 hprGELLVKTDTLFPGYykRPEVTAEVFDedGFYRTGDV--MAELGpdrLVYVDRRNNVLKLSQGEFVTVARLEAVFAAS 510
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 801237227 485 PDVVEAAAIGVDDKEFgarLRAFVVKKPGADLDEDT--IKQYVRDHLAR---------YKVPREVI 539
Cdd:cd17632 511 PLVRQIFVYGNSERAY---LLAVVVPTQDALAGEDTarLRAALAESLQRiareaglqsYEIPRDFL 573
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
69-406 |
7.72e-09 |
|
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: 58.21 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVIDEEG-----TLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNS 143
Cdd:cd05921 3 HWARQAPDRTWLAEREGnggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 144 EFSgpqikeVSDREGAKVIIYDDEYTKAVSLAQ--PPLGklRALGVNPDDDKP--------SGSSDETLAELIAHSSTAP 213
Cdd:cd05921 83 AYS------LMSQDLAKLKHLFELLKPGLVFAQdaAPFA--RALAAIFPLGTPlvvsrnavAGRGAISFAELAATPPTAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 214 APKASRRA-----SIIILTSGTTGTPKgANRNTPPTL-APIGGILSHVPFKAGEVTLLPS--PMFHALGYMHA-ALAMFL 284
Cdd:cd05921 155 VDAAFAAVgpdtvAKFLFTSGSTGLPK-AVINTQRMLcANQAMLEQTYPFFGEEPPVLVDwlPWNHTFGGNHNfNLVLYN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 285 GSTLVLRR-RFKPALVLEDIEKHKATSMVV---VPVMLSRILDQLEKTEP--KPDLSSLKIVFVSGSQLG-------AEL 351
Cdd:cd05921 234 GGTLYIDDgKPMPGGFEETLRNLREISPTVyfnVPAGWEMLVAALEKDEAlrRRFFKRLKLMFYAGAGLSqdvwdrlQAL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 801237227 352 ATRALGDLGPvIYNMYGSTEVAfATIAGPKDLQFNPSTVGPVVKGVTVKILDENG 406
Cdd:cd05921 314 AVATVGERIP-MMAGLGATETA-PTATFTHWPTERSGLIGLPAPGTELKLVPSGG 366
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
125-558 |
1.00e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 57.90 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 125 VIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDD----------------EYTKAVSLAQPPLGKLRALGVN 188
Cdd:PLN03051 8 VIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDvvlrggralplyskvvEAAPAKAIVLPAAGEPVAVPLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 189 PDD---------DKPSGSSDETLAELIAHSSTAPapkasrraSIIILTSGTTGTPKGanrnTPPT-LAPIGGIL---SHV 255
Cdd:PLN03051 88 EQDlswcdflgvAAAQGSVGGNEYSPVYAPVESV--------TNILFSSGTTGEPKA----IPWThLSPLRCASdgwAHM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 256 PFKAGEVTLLPSpmfhALGYMH------------AALAMFLGSTLvlRRRFkpalvLEDIEKHKATSMVVVPVMLSRILD 323
Cdd:PLN03051 156 DIQPGDVVCWPT----NLGWMMgpwllysaflngATLALYGGAPL--GRGF-----GKFVQDAGVTVLGLVPSIVKAWRH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 324 QLEKTEPKPDLSSLKIVFVSGSQLGAE----LATrALGDLGPVIyNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTV 399
Cdd:PLN03051 225 TGAFAMEGLDWSKLRVFASTGEASAVDdvlwLSS-VRGYYKPVI-EYCGGTELASGYISSTLLQPQAPGAFSTASLGTRF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 400 KILDENGNEVPQGAVGRIFVGNAFPFEGYT-----GGGGKQIIDGLLSSGDVGYFDER----------GLLYVSGRDDEM 464
Cdd:PLN03051 303 VLLNDNGVPYPDDQPCVGEVALAPPMLGASdrllnADHDKVYYKGMPMYGSKGMPLRRhgdimkrtpgGYFCVQGRADDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 465 IVSGGENVFPAEVEDLI-SGHPDVVEAAAIGVDDKEFGARL-----RAFVVKKPGADLDEDTIKQYVRDHLAR-----YK 533
Cdd:PLN03051 383 MNLGGIKTSSVEIERACdRAVAGIAETAAVGVAPPDGGPELlviflVLGEEKKGFDQARPEALQKKFQEAIQTnlnplFK 462
|
490 500
....*....|....*....|....*
gi 801237227 534 VPReVIFLDELPRNPTGKVLKRELR 558
Cdd:PLN03051 463 VSR-VKIVPELPRNASNKLLRRVLR 486
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
303-546 |
1.43e-08 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 57.25 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 303 IEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPkd 382
Cdd:cd05913 166 IKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPGVAFE-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 383 lqfNPSTVGPVV--KGVTVKILD-ENGNEVPQGAVGRIFVGN----AFPFEGYTGGGGKQIIDGLLSSGDVGYFDERgll 455
Cdd:cd05913 244 ---CEEKDGLHIweDHFIPEIIDpETGEPVPPGEVGELVFTTltkeAMPLIRYRTRDITRLLPGPCPCGRTHRRIDR--- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 456 yVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDT--IKQYVRDHL-ARY 532
Cdd:cd05913 318 -ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVRPEADDDEKLeaLKQRLERHIkSVL 396
|
250
....*....|....*.
gi 801237227 533 KVPREVIFL--DELPR 546
Cdd:cd05913 397 GVTVEVELVepGSLPR 412
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
69-402 |
5.21e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 52.36 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 69 HNARRAPNRAAVIDEEGT------LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARII--- 139
Cdd:PRK12582 57 KWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAApvs 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 140 ----LLNSEFSgpQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDddkPSGSSDETLAELIAhssTAPAP 215
Cdd:PRK12582 137 paysLMSHDHA--KLKHLFDLVKPRVVFAQSGAPFARALAALDLLDVTVVHVTGP---GEGIASIAFADLAA---TPPTA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 216 K-ASRRASI-------IILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGE---VTLLPSPMFHALGyMHAALAMFL 284
Cdd:PRK12582 209 AvAAAIAAItpdtvakYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNHTMG-GNANFNGLL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 285 --GSTLVLRR-RFKPALVLEDIEKHKATSMVV---VPVMLSRILDQLEKTEP--KPDLSSLKIVFVSGSQLG-------A 349
Cdd:PRK12582 288 wgGGTLYIDDgKPLPGMFEETIRNLREISPTVygnVPAGYAMLAEAMEKDDAlrRSFFKNLRLMAYGGATLSddlyermQ 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 801237227 350 ELATRALGDLGPvIYNMYGSTEVAfATIAGPKDLQFNPSTVGPVVKGVTVKIL 402
Cdd:PRK12582 368 ALAVRTTGHRIP-FYTGYGATETA-PTTTGTHWDTERVGLIGLPLPGVELKLA 418
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
212-551 |
5.44e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 52.41 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 212 APAPKASRRASIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLV-- 289
Cdd:PRK08043 358 AQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVfl 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 290 ----LRRRFKPALVLEdiekhkatSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVfVSGSQLGAElATRAL--GDLGPVI 363
Cdd:PRK08043 438 ypspLHYRIVPELVYD--------RNCTVLFGTSTFLGNYARFANPYDFARLRYV-VAGAEKLQE-STKQLwqDKFGLRI 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 364 YNMYGSTEVA-FATIAGPkdLQFNPSTVGPVVKGVTVKILD----ENGNEV----PQGAVGRIFVGNAFPFEGYTGGGGK 434
Cdd:PRK08043 508 LEGYGVTECApVVSINVP--MAAKPGTVGRILPGMDARLLSvpgiEQGGRLqlkgPNIMNGYLRVEKPGVLEVPTAENAR 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 435 QIID-GLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISG-HPDVVEAAAIGVDdkefGARLRAFVVKKP 512
Cdd:PRK08043 586 GEMErGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKQHATAIKSD----ASKGEALVLFTT 661
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 801237227 513 GADLDEDTIKQYVRDH-LARYKVPREVIFLDELPRNPTGK 551
Cdd:PRK08043 662 DSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
40-236 |
2.77e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 50.26 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 40 GAIGLEPPLNYAALAADIRKWGEvgmlpsHNARRAPNRAAV---IDEEG--TLTFSELDEAAHAVANGLLAKGVRAGDGV 114
Cdd:PRK08180 24 GTIYLRSAEPLGDYPRRLTDRLV------HWAQEAPDRVFLaerGADGGwrRLTYAEALERVRAIAQALLDRGLSAERPL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 115 AILARN---HrwFVIAnYGAARVGARII-------LLNSEFSgpQIKEVSDREGAKVIIYDD--EYTKAVSlAQPPLGKL 182
Cdd:PRK08180 98 MILSGNsieH--ALLA-LAAMYAGVPYApvspaysLVSQDFG--KLRHVLELLTPGLVFADDgaAFARALA-AVVPADVE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 801237227 183 RALGVNPDDdkpsGSSDETLAELIAHSSTAPAPKASRRA---SI--IILTSGTTGTPKG 236
Cdd:PRK08180 172 VVAVRGAVP----GRAATPFAALLATPPTAAVDAAHAAVgpdTIakFLFTSGSTGLPKA 226
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
81-323 |
3.96e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 49.71 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 81 IDEEGT------LTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFsGPQIKE-- 152
Cdd:PLN02736 67 IRVDGTvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTL-GPDAVKfi 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 153 VSDREGAKVIIYDDEYTKAVS-LAQPPlgKLRALGVNPDDDK-----PSGSSDE--TLAELIAH---SSTAPAPKASRRA 221
Cdd:PLN02736 146 VNHAEVAAIFCVPQTLNTLLScLSEIP--SVRLIVVVGGADEplpslPSGTGVEivTYSKLLAQgrsSPQPFRPPKPEDV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 222 SIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFH--------ALGYMHAALAMFLGSTLVLrrr 293
Cdd:PLN02736 224 ATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyervnqiVMLHYGVAVGFYQGDNLKL--- 300
|
250 260 270
....*....|....*....|....*....|
gi 801237227 294 fkpalvLEDIEKHKATSMVVVPVMLSRILD 323
Cdd:PLN02736 301 ------MDDLAALRPTIFCSVPRLYNRIYD 324
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
441-552 |
1.50e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801237227 441 LSSGDVGyFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVV---EAAAIGVDDK-EFG----ARLRAFVVKKP 512
Cdd:PRK05691 431 LRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkgRVAAFAVNHQgEEGigiaAEISRSVQKIL 509
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 801237227 513 GADLDEDTIKQYVRDhlARYKVPREVIFLD--ELPRNPTGKV 552
Cdd:PRK05691 510 PPQALIKSIRQAVAE--ACQEAPSVVLLLNpgALPKTSSGKL 549
|
|
| |
