|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
7-538 |
0e+00 |
|
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: 1060.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 7 IKKGPAPFYPLEDGTAGEQLHKAMKRYALVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSL 86
Cdd:cd17642 1 IIVGPGPFYPLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 87 QFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYT 166
Cdd:cd17642 81 QFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 167 FVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHG 246
Cdd:cd17642 161 FITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 247 FGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEA 326
Cdd:cd17642 241 FGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 327 VAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPE 406
Cdd:cd17642 321 VAKRFKLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 407 ATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 486
Cdd:cd17642 401 ATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 110555473 487 LEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 538
Cdd:cd17642 481 LEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
41-530 |
0e+00 |
|
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: 641.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 41 AFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGI 120
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 121 SQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTShlppGFNEYDFVPESFDRDKTIALIMNSSG 200
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTL----GEEDEDLPPPLKDGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 201 STGLPKGVALPHRTACVRFSHARDPIFGNqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDY 280
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLSQVQTFLYGN-DGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 281 KIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPG 360
Cdd:cd05911 236 KITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 361 AVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKS 440
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 441 LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVD 520
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVFVD 475
|
490
....*....|
gi 110555473 521 EVPKGLTGKL 530
Cdd:cd05911 476 EIPKSASGKI 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
37-529 |
1.67e-154 |
|
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: 451.30 E-value: 1.67e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 116
Cdd:cd05904 19 PSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 117 SMGISQPTVVFVSKKGLQKILnvqkklPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPgfneydfvPESFDRDKTIALIM 196
Cdd:cd05904 99 QVKDSGAKLAFTTAELAEKLA------SLALPVVLLDSAEFDSLSFSDLLFEADEAEP--------PVVVIKQDDVAALL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 197 NSSGSTGLPKGVALPHR--TACVRFSHARdpiFGNQIIPDTAILSVVPFHH--GFGMFTtLGYLICGFRVVLMYRFEEEL 272
Cdd:cd05904 165 YSSGTTGRSKGVMLTHRnlIAMVAQFVAG---EGSNSDSEDVFLCVLPMFHiyGLSSFA-LGLLRLGATVVVMPRFDLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 273 FLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILIT 352
Cdd:cd05904 241 LLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 353 P---EGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDED 429
Cdd:cd05904 321 FapeKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 430 EHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTA 509
Cdd:cd05904 401 GYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPY 480
|
490 500
....*....|....*....|
gi 110555473 510 KKLRgGVVFVDEVPKGLTGK 529
Cdd:cd05904 481 KKVR-KVAFVDAIPKSPSGK 499
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
23-542 |
2.30e-127 |
|
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: 380.31 E-value: 2.30e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 23 GEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAV 102
Cdd:COG0318 2 ADLLRRAAARH---PDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 103 APANDIYNERELLNSMGISQPTVVFVskkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfv 182
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVT------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 183 pesfdrdktiALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGM-FTTLGYLICGFR 261
Cdd:COG0318 103 ----------ALILYTSGTTGRPKGVMLTHRNLL---ANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGAT 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 262 VVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYG 341
Cdd:COG0318 170 LVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVR-IVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 342 LTETTSAILITPE--GDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLH 419
Cdd:COG0318 249 LTETSPVVTVNPEdpGERRPGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 420 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 499
Cdd:COG0318 327 TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELR 406
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 110555473 500 DYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKA 542
Cdd:COG0318 407 AFLRERLARYKVPR-RVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
52-539 |
1.89e-119 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 362.76 E-value: 1.89e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 131
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 GLQKILNVQKKLPIiqKIIIMDSKTDyqGFQSMYTFVTShlppgfNEYDFVPESFDRDKTIALIMnSSGSTGLPKGVALP 211
Cdd:PLN02246 132 YVDKLKGLAEDDGV--TVVTIDDPPE--GCLHFSELTQA------DENELPEVEISPDDVVALPY-SSGTTGLPKGVMLT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 212 HRTACVRFSHARD---PIFGnqIIPDTAILSVVPFHHGFGMFTTLgylICGFRV----VLMYRFEEELFLRSLQDYKIQS 284
Cdd:PLN02246 201 HKGLVTSVAQQVDgenPNLY--FHSDDVILCVLPMFHIYSLNSVL---LCGLRVgaaiLIMPKFEIGALLELIQRHKVTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 285 ALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILI------TPEgDDK 358
Cdd:PLN02246 276 APFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMclafakEPF-PVK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 359 PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRL 438
Cdd:PLN02246 355 SGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 439 KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVF 518
Cdd:PLN02246 435 KELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIH-KVFF 513
|
490 500
....*....|....*....|.
gi 110555473 519 VDEVPKGLTGKLDARKIREIL 539
Cdd:PLN02246 514 VDSIPKAPSGKILRKDLRAKL 534
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
191-531 |
1.40e-115 |
|
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: 345.81 E-value: 1.40e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 191 TIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNqiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEE 270
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT---EGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 271 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAIL 350
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 351 ITP--EGDDKPGAVGKVVPFFEAKVVDLDTGkTLGVNQRGELCVRGPMIMSGYVNNPEATnALIDKDGWLHSGDIAYWDE 428
Cdd:cd04433 157 TGPpdDDARKPGSVGRPVPGVEVRIVDPDGG-ELPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 429 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTT 508
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|...
gi 110555473 509 AKKLRgGVVFVDEVPKGLTGKLD 531
Cdd:cd04433 315 YKVPR-RVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
51-536 |
1.33e-99 |
|
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: 309.49 E-value: 1.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVsk 130
Cdd:cd05936 25 LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 kglqkilnvqkklpiiqkiiimdsktdyqgfqsMYTFVTSHLPPGFNEYDFVPESFDrdktIALIMNSSGSTGLPKGVAL 210
Cdd:cd05936 103 ---------------------------------AVSFTDLLAAGAPLGERVALTPED----VAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 211 PHR------TACVRfshardpIFGNQIIPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELFLRSLQDYKIQ 283
Cdd:cd05936 146 THRnlvanaLQIKA-------WLEDLLEGDDVVLAALPLFHVFGLTVALLLpLALGATIVLIPRFRPIGVLKEIRKHRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 284 SALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITP-EGDDKPGAV 362
Cdd:cd05936 219 IFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVP-IVEGYGLTETSPVVAVNPlDGPRKPGSI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 363 GKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLI 442
Cdd:cd05936 298 GIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 443 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEV 522
Cdd:cd05936 376 IVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPR-QVEFRDEL 454
|
490
....*....|....
gi 110555473 523 PKGLTGKLDARKIR 536
Cdd:cd05936 455 PKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
51-537 |
1.36e-96 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 303.26 E-value: 1.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 130
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVT--SHLPPgfnEYDFVPesFDRDkTIALIMNSSGSTGLPKGV 208
Cdd:PRK06187 112 EFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEEllAAASD---TFDFPD--IDEN-DAAAMLYTSGTTGHPKGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 209 ALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVP-FH-HGFGmfttLGY--LICGFRVVLMYRFEEELFLRSLQDYKIQS 284
Cdd:PRK06187 186 VLSHRNL---FLHSLAVCAWLKLSRDDVYLVIVPmFHvHAWG----LPYlaLMAGAKQVIPRRFDPENLLDLIETERVTF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 285 ALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLpGIRQGYGLTETTSAILITPEGDD------K 358
Cdd:PRK06187 259 FFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGI-DLVQGYGMTETSPVVSVLPPEDQlpgqwtK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 359 PGAVGKVVPFFEAKVVDLDtGKTLGVNQR--GELCVRGPMIMSGYVNNPEATNALIDkDGWLHSGDIAYWDEDEHFFIVD 436
Cdd:PRK06187 338 RRSAGRPLPGVEARIVDDD-GDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 437 RLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVttAK-KLRGG 515
Cdd:PRK06187 416 RIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRL--AKfKLPKR 493
|
490 500
....*....|....*....|..
gi 110555473 516 VVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK06187 494 IAFVDELPRTSVGKILKRVLRE 515
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
2-544 |
4.64e-95 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 299.97 E-value: 4.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 2 EDAKNIKKGPAPFYPL-EDGTAGEQLHKAMKRYAlvpGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVV 80
Cdd:PLN02330 9 EDNEHIFRSRYPSVPVpDKLTLPDFVLQDAELYA---DKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 81 CSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQkkLPIIqkiiimdsktdYQG 160
Cdd:PLN02330 86 VLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLG--LPVI-----------VLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 161 FQSMYTFV--TSHLPPGFNEYD-FVPESFDRDKTIALIMnSSGSTGLPKGVALPHRTACVRFSHARDPIfGNQIIPDTAI 237
Cdd:PLN02330 153 EEKIEGAVnwKELLEAADRAGDtSDNEEILQTDLCALPF-SSGTTGISKGVMLTHRNLVANLCSSLFSV-GPEMIGQVVT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 238 LSVVPFHHGFGM----FTTL---GylicgfRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNL- 309
Cdd:PLN02330 231 LGLIPFFHIYGItgicCATLrnkG------KVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLk 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 310 -HEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETtSAILIT---PE---GDDKPGAVGKVVPFFEAKVVDLDTGKTL 382
Cdd:PLN02330 305 lQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEH-SCITLThgdPEkghGIAKKNSVGFILPNLEVKFIDPDTGRSL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 383 GVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHP 462
Cdd:PLN02330 384 PKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 463 NIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKA 542
Cdd:PLN02330 464 SVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVR-VVQFVDSIPKSLSGKIMRRLLKEKMLSI 542
|
..
gi 110555473 543 KK 544
Cdd:PLN02330 543 NK 544
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
26-531 |
9.93e-94 |
|
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: 292.98 E-value: 9.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 26 LHKAMKRYalvPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPA 105
Cdd:cd17631 1 LRRRARRH---PDRTALVFGGRS--LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 106 NDIYNERELLNSMGISQPTVVFvskkglqkilnvqkklpiiqkiiiMDsktdyqgfqsmytfvtshlppgfneydfvpes 185
Cdd:cd17631 76 NFRLTPPEVAYILADSGAKVLF------------------------DD-------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 186 fdrdktIALIMNSSGSTGLPKGVALPHRTacvRFSHARDPIFGNQIIPDTAILSVVPFHHGFGM-FTTLGYLICGFRVVL 264
Cdd:cd17631 100 ------LALLMYTSGTTGRPKGAMLTHRN---LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 265 MYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlPGIRQGYGLTE 344
Cdd:cd17631 171 LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARG--VKFVQGYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 345 TTSAILITPEGD--DKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGD 422
Cdd:cd17631 249 TSPGVTFLSPEDhrRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 423 IAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYV 502
Cdd:cd17631 327 LGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHC 406
|
490 500
....*....|....*....|....*....
gi 110555473 503 ASQVTTAKKLRgGVVFVDEVPKGLTGKLD 531
Cdd:cd17631 407 RERLARYKIPK-SVEFVDALPRNATGKIL 434
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
37-445 |
1.08e-93 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 292.29 E-value: 1.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAHIEvDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 116
Cdd:pfam00501 9 PDKTALEVGEGR-RLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 117 SMGISQPTVVFV-SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPgfneydFVPESFDRDkTIALI 195
Cdd:pfam00501 88 ILEDSGAKVLITdDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPP------PPPPPPDPD-DLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 196 MNSSGSTGLPKGVALPHR------TACVRFSHARDPIFgnqiiPDTAILSVVPFHHGFGM-FTTLGYLICGFRVVLM--- 265
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRnlvanvLSIKRVRPRGFGLG-----PDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPpgf 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTET 345
Cdd:pfam00501 236 PALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 TSAILITPEGDDK---PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGD 422
Cdd:pfam00501 315 TGVVTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGD 394
|
410 420
....*....|....*....|...
gi 110555473 423 IAYWDEDEHFFIVDRLKSLIKYK 445
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
37-539 |
2.52e-86 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 277.88 E-value: 2.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELL 115
Cdd:PLN02574 53 NGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 116 NSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKT-DYQGFQSMYTFvtshlppgfnEYDFVPESFDRDKTIAL 194
Cdd:PLN02574 133 KRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRiEFPKFYELIKE----------DFDFVPKPVIKQDDVAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 195 IMNSSGSTGLPKGVALPHRTAC------VRFSHARDPIFGNqiipDTAILSVVPFHH--GFGMFTTlGYLICGFRVVLMY 266
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIamvelfVRFEASQYEYPGS----DNVYLAALPMFHiyGLSLFVV-GLLSLGSTIVVMR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 267 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTL-IDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTET 345
Cdd:PLN02574 278 RFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 TSAIL--ITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDI 423
Cdd:PLN02574 358 TAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 424 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVA 503
Cdd:PLN02574 438 AYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVA 517
|
490 500 510
....*....|....*....|....*....|....*.
gi 110555473 504 SQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:PLN02574 518 KQVAPYKKVR-KVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
49-537 |
5.66e-82 |
|
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: 264.56 E-value: 5.66e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 49 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFV 128
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 129 SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtSHLPPGFNEYDFV-PESFDRDKTIALIMNSSGSTGLPKG 207
Cdd:cd05926 93 PKGELGPASRAASKLGLAILELALDVGVLIRAPSA------ESLSNLLADKKNAkSEGVPLPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 208 VALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTT-LGYLICGFRVVLMYRFEEELFLRSLQDYKIQ--S 284
Cdd:cd05926 167 VPLTHRNLA---ASATNITNTYKLTPDDRTLVVMPLFHVHGLVASlLSTLAAGGSVVLPPRFSASTFWPDVRDYNATwyT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 285 AllVPTLFSFFAKSTLIDKYD-LSNLHEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTSAILITP--EGDDKPGA 361
Cdd:cd05926 244 A--VPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEAAHQMTSNPlpPGPRKPGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 362 VGKvvPF-FEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKS 440
Cdd:cd05926 321 VGK--PVgVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 441 LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVtTAKKLRGGVVFVD 520
Cdd:cd05926 398 LINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHL-AAFKVPKKVYFVD 476
|
490
....*....|....*..
gi 110555473 521 EVPKGLTGKLDARKIRE 537
Cdd:cd05926 477 ELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
24-537 |
3.87e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 262.92 E-value: 3.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 24 EQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVA 103
Cdd:PRK07656 9 ELLARAARRF---GDKEAYVFG--DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 104 PANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFvTSHLPPGFNEYDFVP 183
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTF-TDFLAAGDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 184 ESFDrdkTIALIMNSSGSTGLPKGVALPHRTAcvrFSHARDpiFGN--QIIPDTAILSVVPFHHGFGMftTLGYLIC--- 258
Cdd:PRK07656 163 VDPD---DVADILFTSGTTGRPKGAMLTHRQL---LSNAAD--WAEylGLTEGDRYLAANPFFHVFGY--KAGVNAPlmr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 259 GFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQ 338
Cdd:PRK07656 233 GATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 339 GYGLTETTSAILITPEGDDK---PGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 415
Cdd:PRK07656 313 GYGLSEASGVTTFNRLDDDRktvAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 416 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 495
Cdd:PRK07656 392 GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 110555473 496 KEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK07656 472 EELIAYCREHL--AKyKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
51-537 |
4.02e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 263.74 E-value: 4.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKR-YGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVS 129
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 130 KKGLQKILNVQKKLPIiqKIIIMDSKTDYQGFQSMYTF----VTSHLPPGFNEYDFV-------------PESFDRDkTI 192
Cdd:PRK08314 116 SELAPKVAPAVGNLRL--RHVIVAQYSDYLPAEPEIAVpawlRAEPPLQALAPGGVVawkealaaglappPHTAGPD-DL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHRTacVRFShardpIFGNQI----IPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVLMYR 267
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRT--VMAN-----AVGSVLwsnsTPESVVLAVLPLFHVTGMVHSMnAPIYAGATVVLMPR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 268 FEEELFLRSLQDYKIQSALLVPT-LFSFFAkSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRFH-LPGIR--QGYGLT 343
Cdd:PRK08314 266 WDREAAARLIERYRVTHWTNIPTmVVDFLA-SPGLAERDLSSLRYIGGGGAAMP----EAVAERLKeLTGLDyvEGYGLT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 344 ETTSAILITPEGDDKPGAVGkvVPFF--EAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT-NALIDKDG--WL 418
Cdd:PRK08314 341 ETMAQTHSNPPDRPKLQCLG--IPTFgvDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATaEAFIEIDGkrFF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 419 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL--EHGKTMTEK 496
Cdd:PRK08314 419 RTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLrpEARGKTTEE 498
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 110555473 497 EIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK08314 499 EIIAWAREHMAAYKYPR-IVEFVDSLPKSGSGKILWRQLQE 538
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
51-533 |
1.19e-80 |
|
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: 258.95 E-value: 1.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNEREL---LNSMGIsqptvvf 127
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELeyiLNDSGA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 128 vskkglqkilnvqkklpiiqKIIIMDSKTDyqgfqsmytfvtshlppgfneydfvpesfdrdkTIALIMNSSGSTGLPKG 207
Cdd:cd05935 75 --------------------KVAVVGSELD---------------------------------DLALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 208 VALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLI-CGFRVVLMYRFEEELFLRSLQDYKIQSAL 286
Cdd:cd05935 102 CMHTHFSA---AANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVyVGGTYVLMARWDRETALELIEKYKVTFWT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 287 LVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlpGIR--QGYGLTETTSAILITPEGDDKPGAVGk 364
Cdd:cd05935 179 NIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT---GLRfvEGYGLTETMSQTHTNPPLRPKLQCLG- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 365 vVPFF--EAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT-NALIDKDG--WLHSGDIAYWDEDEHFFIVDRLK 439
Cdd:cd05935 255 -IP*FgvDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETeESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 440 SLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL--EHGKTMTEKEIVDYVASQVTTAKKLRgGVV 517
Cdd:cd05935 334 RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLrpEYRGKVTEEDIIEWAREQMAAYKYPR-EVE 412
|
490
....*....|....*.
gi 110555473 518 FVDEVPKGLTGKLDAR 533
Cdd:cd05935 413 FVDELPRSASGKILWR 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
48-539 |
6.04e-76 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 250.41 E-value: 6.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 48 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVF 127
Cdd:COG0365 37 ERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 128 VSKKGL---------QKILNVQKKLPIIQKIII---MDSKTDYQGFQSMYTFVTSHLPpgfneyDFVPESFDRDkTIALI 195
Cdd:COG0365 117 TADGGLrggkvidlkEKVDEALEELPSLEHVIVvgrTGADVPMEGDLDWDELLAAASA------EFEPEPTDAD-DPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 196 MNSSGSTGLPKGVALPHR--TACVRFSHARdpIFGnqIIPDTAILSVVP----FHHGFGMFttlGYLICGFRVVLmyrFE 269
Cdd:COG0365 190 LYTSGTTGKPKGVVHTHGgyLVHAATTAKY--VLD--LKPGDVFWCTADigwaTGHSYIVY---GPLLNGATVVL---YE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 270 E-------ELFLRSLQDYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGY 340
Cdd:COG0365 260 GrpdfpdpGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVP-IVDGW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 341 GLTETTSAILITPEGDD-KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM--IMSGYVNNPEAT-NALIDK-D 415
Cdd:COG0365 339 GQTETGGIFISNLPGLPvKPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYrETYFGRfP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 416 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 495
Cdd:COG0365 418 GWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 110555473 496 ---KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:COG0365 498 elaKELQAHVREELGPYAYPR-EIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
10-540 |
2.44e-73 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 243.53 E-value: 2.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 10 GPAPFY-------PLEDGTAGEQLHKAMKRYalvPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCS 82
Cdd:PRK12583 1 MPQPSYyqgggdkPLLTQTIGDAFDATVARF---PDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 83 ENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK--KG------LQKILN----------VQKKLP 144
Cdd:PRK12583 78 PNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafKTsdyhamLQELLPglaegqpgalACERLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 145 IIQKIIIMDSK-----TDYQGFQSMYTFVTSHlppgfnEYDFVPESFDRDKTIAlIMNSSGSTGLPKGVALPHRTacvrf 219
Cdd:PRK12583 158 ELRGVVSLAPApppgfLAWHELQARGETVSRE------ALAERQASLDRDDPIN-IQYTSGTTGFPKGATLSHHN----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 220 shardpIFGNQII-------PDTAILSV-VPFHHGFGM-FTTLGYLICGFRVVL-MYRFEEELFLRSLQDYKIQSALLVP 289
Cdd:PRK12583 226 ------ILNNGYFvaeslglTEHDRLCVpVPLYHCFGMvLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 290 TLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKP---GAVGKVV 366
Cdd:PRK12583 300 TMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLErrvETVGRTQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 367 PFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKG 446
Cdd:PRK12583 380 PHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 447 YQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGL 526
Cdd:PRK12583 459 ENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPR-YFRFVDEFPMTV 537
|
570
....*....|....
gi 110555473 527 TGKLDARKIREILI 540
Cdd:PRK12583 538 TGKVQKFRMREISI 551
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-536 |
8.18e-70 |
|
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: 227.93 E-value: 8.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 SGSTGLPKGVALPHRTacvrfshardpIFGNQII--------PDTAILSVVPFHHGFGMftTLGYLIC---GFRVVlmyr 267
Cdd:cd05917 11 SGTTGSPKGATLTHHN-----------IVNNGYFigerlgltEQDRLCIPVPLFHCFGS--VLGVLAClthGATMV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 268 FEEELF-----LRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGL 342
Cdd:cd05917 74 FPSPSFdplavLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 343 TETTSAILITPEGDD---KPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLH 419
Cdd:cd05917 154 TETSPVSTQTRTDDSiekRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 420 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 499
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIK 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 110555473 500 DYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 536
Cdd:cd05917 314 AYCKGKIAHYKVPR-YVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
16-541 |
5.67e-68 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 229.31 E-value: 5.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 16 PLEDGTAGEQLHKAMKRYalvPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENS-----LQFFM 90
Cdd:PRK08315 12 PLLEQTIGQLLDRTAARY---PDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVpewvlTQFAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 91 PVLGAlfIGVAVAPAndiYNEREL---LNSMGISqpTVVFVSK-----------------KGLQKILNVQKKLPIIQKII 150
Cdd:PRK08315 89 AKIGA--ILVTINPA---YRLSELeyaLNQSGCK--ALIAADGfkdsdyvamlyelapelATCEPGQLQSARLPELRRVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 151 IMDSKTdyqgFQSMYTF-----VTSHLPPGfnEYDFVPESFDRDKTIAlIMNSSGSTGLPKGVALPHR---------TAC 216
Cdd:PRK08315 162 FLGDEK----HPGMLNFdellaLGRAVDDA--ELAARQATLDPDDPIN-IQYTSGTTGFPKGATLTHRnilnngyfiGEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 217 VRFSHArDPIfgnqIIPdtailsvVPFHHGFGMftTLGYLIC---GFRVVLMY-RFEEELFLRSLQDYKIQSALLVPTLF 292
Cdd:PRK08315 235 MKLTEE-DRL----CIP-------VPLYHCFGM--VLGNLACvthGATMVYPGeGFDPLATLAAVEEERCTALYGVPTMF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 293 -------SFfakstliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDD---KPGAV 362
Cdd:PRK08315 301 iaeldhpDF-------ARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPlekRVTTV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 363 GKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLI 442
Cdd:PRK08315 374 GRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 443 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEV 522
Cdd:PRK08315 454 IRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPR-YIRFVDEF 532
|
570
....*....|....*....
gi 110555473 523 PKGLTGKLDARKIREILIK 541
Cdd:PRK08315 533 PMTVTGKIQKFKMREMMIE 551
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
31-539 |
7.44e-68 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 227.44 E-value: 7.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 31 KRYALVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMK-RYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY 109
Cdd:PRK06839 10 KRAYLHPDRIAIITE--EEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 110 NERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtshlppgfneyDFVPESFDRD 189
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKID----------------NFVEKNESAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 190 ktiALIMNSSGSTGLPKGVALphrTACVRFSHARDPIFGNQIIPDTAILSVVPFHH--GFGMFTtLGYLICGFRVVLMYR 267
Cdd:PRK06839 152 ---FIICYTSGTTGKPKGAVL---TQENMFWNALNNTFAIDLTMHDRSIVLLPLFHigGIGLFA-FPTLFAGGVIIVPRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 268 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGirQGYGLTETTS 347
Cdd:PRK06839 225 FEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 348 AILITPEGD--DKPGAVGKVVPFFEAKVVDLDTGKtLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAY 425
Cdd:PRK06839 303 TVFMLSEEDarRKVGSIGKPVLFCDYELIDENKNK-VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLAR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 426 WDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQ 505
Cdd:PRK06839 381 VDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLF 460
|
490 500 510
....*....|....*....|....*....|....
gi 110555473 506 VTTAKKLRgGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:PRK06839 461 LAKYKIPK-EIVFLKELPKNATGKIQKAQLVNQL 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
50-537 |
1.20e-67 |
|
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: 224.53 E-value: 1.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 50 DITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPtvvfvs 129
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 130 kkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpeSFDRdktIALIMNSSGSTGLPKGVA 209
Cdd:cd05912 75 -------------------------------------------------------KLDD---IATIMYTSGTTGKPKGVQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 210 LphrTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVP 289
Cdd:cd05912 97 Q---TFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 290 TLFSffaksTLIDKYDL---SNLHEIASGGAPLSKEVGEaVAKRFHLPgIRQGYGLTETTSAIL-ITPE-GDDKPGAVGK 364
Cdd:cd05912 174 TMLQ-----RLLEILGEgypNNLRCILLGGGPAPKPLLE-QCKEKGIP-VYQSYGMTETCSQIVtLSPEdALNKIGSAGK 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 365 VVPFFEAKVVDLDTGKtlgvNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY 444
Cdd:cd05912 247 PLFPVELKIEDDGQPP----YEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIIS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 445 KGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEhgKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVP 523
Cdd:cd05912 322 GGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKL--AKyKVPKKIYFVDELP 397
|
490
....*....|....
gi 110555473 524 KGLTGKLDARKIRE 537
Cdd:cd05912 398 RTASGKLLRHELKQ 411
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
52-537 |
1.77e-67 |
|
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: 227.13 E-value: 1.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 131
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 GLQKILNVQKKLPIIQKIIIMDSKTDYQ-----GFQSMYTFVTSHlPPGFNEYDFvpesfDrDKTIALIMNSSGSTGLPK 206
Cdd:cd12119 107 FLPLLEAIAPRLPTVEHVVVMTDDAAMPepagvGVLAYEELLAAE-SPEYDWPDF-----D-ENTAAAICYTSGTTGNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 207 GVALPHRTAcvrFSHA---RDPIFGNQIIPDTaILSVVP-FH-HGFGM-FTTLgylICGFRVVLMYRFEE-ELFLRSLQD 279
Cdd:cd12119 180 GVVYSHRSL---VLHAmaaLLTDGLGLSESDV-VLPVVPmFHvNAWGLpYAAA---MVGAKLVLPGPYLDpASLAELIER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 280 YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRFHLPGIR--QGYGLTET----TSAILITP 353
Cdd:cd12119 253 EGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVP----RSLIEAFEERGVRviHAWGMTETsplgTVARPPSE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 354 EGDDKPGAV-------GKVVPFFEAKVVDLDT------GKTlgvnqRGELCVRGPMIMSGYVNNPEATNALiDKDGWLHS 420
Cdd:cd12119 329 HSNLSEDEQlalrakqGRPVPGVELRIVDDDGrelpwdGKA-----VGELQVRGPWVTKSYYKNDEESEAL-TEDGWLRT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 421 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVD 500
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLE 482
|
490 500 510
....*....|....*....|....*....|....*...
gi 110555473 501 YVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:cd12119 483 FLADKV--AKwWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
18-464 |
5.66e-67 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 227.68 E-value: 5.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 18 EDGTAGEQLHKAMKRYalvPGTIAFT--DAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGA 95
Cdd:COG1022 9 PADTLPDLLRRRAARF---PDRVALRekEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 96 LFIGVAVAPandIY---NERELLNSMGISQPTVVFVSKKG-LQKILNVQKKLPIIQKIIIMDSKTDYQG-----FQSMYT 166
Cdd:COG1022 86 LAAGAVTVP---IYptsSAEEVAYILNDSGAKVLFVEDQEqLDKLLEVRDELPSLRHIVVLDPRGLRDDprllsLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 167 FVTSHLPPGfnEYDFVPESFDRDkTIALIMNSSGSTGLPKGVALPHR--TACVRFSHARDPIFgnqiiPDTAILSVVPFH 244
Cdd:COG1022 163 LGREVADPA--ELEARRAAVKPD-DLATIIYTSGTTGRPKGVMLTHRnlLSNARALLERLPLG-----PGDRTLSFLPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 245 HGFGMFTTLGYLICGFRVVlmyrFEE--ELFLRSLQDYKIQSALLVP----------------------TLFSFF----- 295
Cdd:COG1022 235 HVFERTVSYYALAAGATVA----FAEspDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrKLFRWAlavgr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 296 -----------------AKSTLIDKYDLSNLHE--------IASGGAPLSKEVGEAvakrFH---LPgIRQGYGLTETTS 347
Cdd:COG1022 311 ryararlagkspslllrLKHALADKLVFSKLREalggrlrfAVSGGAALGPELARF----FRalgIP-VLEGYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 348 AILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWD 427
Cdd:COG1022 386 VITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELD 454
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 110555473 428 EDEHFFIVDRLKSLI-----KYkgyqVAPAELESILLQHPNI 464
Cdd:COG1022 455 EDGFLRITGRKKDLIvtsggKN----VAPQPIENALKASPLI 492
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
50-544 |
8.30e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 226.45 E-value: 8.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 50 DITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVS 129
Cdd:PRK06710 49 DITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 130 KKGLQKILNVQKKLPIiqKIIIMDSKTDYQGFQS--MYTFVT------------SHLPPGFNEYD-----FVPESFDRDK 190
Cdd:PRK06710 129 DLVFPRVTNVQSATKI--EHVIVTRIADFLPFPKnlLYPFVQkkqsnlvvkvseSETIHLWNSVEkevntGVEVPCDPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 191 TIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFgNQIIPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLMYRFE 269
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLY-NCKEGEEVVLGVLPFFHVYGMTAVMNLSIMqGYKMVLIPKFD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 270 EELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVaKRFHLPGIRQGYGLTETTSAI 349
Cdd:PRK06710 286 MKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKF-ETVTGGKLVEGYGLTESSPVT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 350 LITPEGDDK-PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDE 428
Cdd:PRK06710 365 HSNFLWEKRvPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 429 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIvDYVASQVTT 508
Cdd:PRK06710 444 DGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEEL-NQFARKYLA 522
|
490 500 510
....*....|....*....|....*....|....*.
gi 110555473 509 AKKLRGGVVFVDEVPKGLTGKLdarkIREILIKAKK 544
Cdd:PRK06710 523 AYKVPKVYEFRDELPKTTVGKI----LRRVLIEEEK 554
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
51-544 |
5.35e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 224.49 E-value: 5.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 130
Cdd:PRK05605 58 TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 K------------GLQKIL--NVQKKLPIIQKI-------IIMDSKTDYQG-------FQSMytfvTSHLPPGFNEYDFV 182
Cdd:PRK05605 138 KvaptverlrrttPLETIVsvNMIAAMPLLQRLalrlpipALRKARAALTGpapgtvpWETL----VDAAIGGDGSDVSH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 183 PESfdRDKTIALIMNSSGSTGLPKGVALPHRT--ACVRFSHARDPIFGNQiipDTAILSVVPFHHGFG--MFTTLGYLIc 258
Cdd:PRK05605 214 PRP--TPDDVALILYTSGTTGKPKGAQLTHRNlfANAAQGKAWVPGLGDG---PERVLAALPMFHAYGltLCLTLAVSI- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 259 GFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVgeaVAKRFHLPG--I 336
Cdd:PRK05605 288 GGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVST---VELWEKLTGglL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 337 RQGYGLTETTSAILITPEGDD-KPGAVGkvVPF--FEAKVVDLDT-GKTLGVNQRGELCVRGPMIMSGYVNNPEATNALI 412
Cdd:PRK05605 365 VEGYGLTETSPIIVGNPMSDDrRPGYVG--VPFpdTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 413 dKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKT 492
Cdd:PRK05605 443 -LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAA 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 110555473 493 MTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKAKK 544
Cdd:PRK05605 522 LDPEGLRAYCREHLTRYKVPR-RFYHVDELPRDQLGKVRRREVREELLEKLG 572
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
51-536 |
1.05e-65 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 219.47 E-value: 1.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSk 130
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 kgLQKILnvqkklpiiqkiiimdsktdyqgfqsmYTfvtshlppgfneydfvpesfdrdktialimnsSGSTGLPKGVAL 210
Cdd:cd05934 83 --PASIL---------------------------YT--------------------------------SGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 211 PHR---TACVRFSHARDpifgnqIIPDTAILSVVPFHHGFGMFTT-LGYLICGFRVVLMYRFEEELFLRSLQDYKIQSAL 286
Cdd:cd05934 102 THAnltFAGYYSARRFG------LGEDDVYLTVLPLFHINAQAVSvLAALSVGATLVLLPRFSASRFWSDVRRYGATVTN 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 287 LVPTLFSFFAKsTLIDKYDLSN-LHEIASGGAPlsKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPGAVGKV 365
Cdd:cd05934 176 YLGAMLSYLLA-QPPSPDDRAHrLRAAYGAPNP--PELHEEFEERFGVR-LLEGYGMTETIVGVIGPRDEPRRPGSIGRP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 366 VPFFEAKVVDlDTGKTLGVNQRGELCVR---GPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLI 442
Cdd:cd05934 252 APGYEVRIVD-DDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 443 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTaKKLRGGVVFVDEV 522
Cdd:cd05934 330 RRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY-FKVPRYIRFVDDL 408
|
490
....*....|....
gi 110555473 523 PKGLTGKLDARKIR 536
Cdd:cd05934 409 PKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
21-542 |
5.90e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 217.88 E-value: 5.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 21 TAGEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGV 100
Cdd:PRK08316 12 TIGDILRRSARRY---PDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 101 AVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKI-IIMDSKTDYQG----FQSMYTfvtshlppg 175
Cdd:PRK08316 87 VHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLIlSLVLGGREAPGgwldFADWAE--------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 176 fNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHR------TACvrfshardpIFGNQIIPDTAILSVVPFHHGFGM 249
Cdd:PRK08316 158 -AGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRaliaeyVSC---------IVAGDMSADDIPLHALPLYHCAQL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 250 FTTLG-YLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVA 328
Cdd:PRK08316 228 DVFLGpYLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 329 KRfhLPGIR--QGYGLTET--TSAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNN 404
Cdd:PRK08316 308 ER--LPGLRfyNCYGQTEIapLATVLGPEEHLRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 405 PEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAV 484
Cdd:PRK08316 385 PEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 485 VVLEHGKTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARKIREILIKA 542
Cdd:PRK08316 464 VVPKAGATVTEDELIAHCRARL-AGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
52-536 |
2.12e-63 |
|
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: 213.74 E-value: 2.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPtvvfvskk 131
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 glqkilnvqkklpiiqKIIIMDSKTdyqgfqsmytfvtshlppgfneydfvpesfdrdktIALIMNSSGSTGLPKGVALP 211
Cdd:cd05972 74 ----------------KAIVTDAED-----------------------------------PALIYFTSGTTGLPKGVLHT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 212 HRTACVRFSHARDPIfgnQIIPDTAILSVV-PFHHGFGMFTTLGYLICGFRVVL--MYRFEEELFLRSLQDYKIQSALLV 288
Cdd:cd05972 103 HSYPLGHIPTAAYWL---GLRPDDIHWNIAdPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 289 PTLFSFFAKStLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPF 368
Cdd:cd05972 180 PTAYRMLIKQ-DLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 369 FEAKVVDlDTGKTLGVNQRGELCVR--GPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKG 446
Cdd:cd05972 258 YDVAIID-DDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 447 YQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVASQVTTAKKLRgGVVFVDEVP 523
Cdd:cd05972 336 YRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPR-EIEFVEELP 414
|
490
....*....|...
gi 110555473 524 KGLTGKLDARKIR 536
Cdd:cd05972 415 KTISGKIRRVELR 427
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
30-539 |
1.10e-62 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 213.29 E-value: 1.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 30 MKRYALVPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY 109
Cdd:PRK03640 9 KQRAFLTPDRTAIEFEEKK--VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 110 NERELLNSMGISQPTVVFVSKkglqkilNVQKKLPIIQKIIImdsktdyqgfqsmytfvtSHLPPGFNEYDFVPESFDRD 189
Cdd:PRK03640 87 SREELLWQLDDAEVKCLITDD-------DFEAKLIPGISVKF------------------AELMNGPKEEAEIQEEFDLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 190 KTiALIMNSSGSTGLPKGVALphrTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFE 269
Cdd:PRK03640 142 EV-ATIMYTSGTTGKPKGVIQ---TYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 270 EELFLRSLQDYKIQSALLVPTLFSffaksTLIDKYDLSNLHE----IASGGAPLSKEVGEaVAKRFHLPGIrQGYGLTET 345
Cdd:PRK03640 218 AEKINKLLQTGGVTIISVVSTMLQ-----RLLERLGEGTYPSsfrcMLLGGGPAPKPLLE-QCKEKGIPVY-QSYGMTET 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 TSAILITPEGD--DKPGAVGKvvPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDI 423
Cdd:PRK03640 291 ASQIVTLSPEDalTKLGSAGK--PLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 424 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVleHGKTMTEKEIVDYVA 503
Cdd:PRK03640 368 GYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV--KSGEVTEEELRHFCE 445
|
490 500 510
....*....|....*....|....*....|....*..
gi 110555473 504 SQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:PRK03640 446 EKL--AKyKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
37-536 |
6.30e-62 |
|
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: 211.84 E-value: 6.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 116
Cdd:cd05959 18 GDKTAFIDDAGS--LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 117 SMGISQPTVVFVSKKGLQKILN-VQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPpgfneyDFVPESFDRDKtIALI 195
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLAAaLTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAE------QLKPAATHADD-PAFW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 196 MNSSGSTGLPKGVALPHRTACVRFSHARDPIFGnqIIPDTAILSVVP--FHHGFG--MFTTLGYlicGFRVVLM-YRFEE 270
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYWTAELYARNVLG--IREDDVCFSAAKlfFAYGLGnsLTFPLSV---GATTVLMpERPTP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 271 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAIL 350
Cdd:cd05959 244 AAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD-ILDGIGSTEMLHIFL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 351 ITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDE 430
Cdd:cd05959 323 SNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 431 HFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVASQVT 507
Cdd:cd05959 401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAleeELKEFVKDRLA 480
|
490 500
....*....|....*....|....*....
gi 110555473 508 TAKKLRgGVVFVDEVPKGLTGKLDARKIR 536
Cdd:cd05959 481 PYKYPR-WIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
18-537 |
3.08e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 207.92 E-value: 3.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 18 EDGTAGEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALF 97
Cdd:PRK06188 10 SGATYGHLLVSALKRY---PDRPALVLG--DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 98 IG---VAVAPANDIYNERELLNSMGISqpTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtshlpp 174
Cdd:PRK06188 85 AGlrrTALHPLGSLDDHAYVLEDAGIS--TLIVDPAPFVERALALLARVPSLKHVLTLGPVPDGVDLLA----------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 175 GFNEYDFVP-ESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRfshardpifgNQII-------PDTAILSVVPFHHG 246
Cdd:PRK06188 152 AAAKFGPAPlVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATM----------AQIQlaewewpADPRFLMCTPLSHA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 247 FGMFTTLGyLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSffaksTLID-----KYDLSNLHEIASGGAPLSK 321
Cdd:PRK06188 222 GGAFFLPT-LLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIY-----ALLDhpdlrTRDLSSLETVYYGASPMSP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 322 -EVGEAVaKRFHlPGIRQGYGLTETTSAILITPEGDDKP------GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG 394
Cdd:PRK06188 296 vRLAEAI-ERFG-PIFAQYYGQTEAPMVITYLRKRDHDPddpkrlTSCGRPTPGLRVALLD-EDGREVAQGEVGEICVRG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 395 PMIMSGYVNNPEATnALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPD 474
Cdd:PRK06188 373 PLVMDGYWNRPEET-AEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPD 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110555473 475 DDAGELPAAVVVLEHGKTMTEKEIVDYVASQ---VTTAKKlrggVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK06188 452 EKWGEAVTAVVVLRPGAAVDAAELQAHVKERkgsVHAPKQ----VDFVDSLPLTALGKPDKKALRA 513
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
47-488 |
3.95e-60 |
|
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: 205.52 E-value: 3.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 47 IEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandIY------NERELLNSmgi 120
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP---IYptssaeQIAYILND--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 121 SQPTVVFVSKK-GLQKIlnvqkklpiiqkiiimdsktdyqgfqsMYTfvtshlppgfneydfvpesfdrdktialimnsS 199
Cdd:cd05907 76 SEAKALFVEDPdDLATI---------------------------IYT--------------------------------S 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 200 GSTGLPKGVALPHRTACvrfSHARDpifGNQIIPDTA---ILSVVPFHHGFGMFTTLgYLICGFRVVLMYRFEEELFLRS 276
Cdd:cd05907 97 GTTGRPKGVMLSHRNIL---SNALA---LAERLPATEgdrHLSFLPLAHVFERRAGL-YVPLLAGARIYFASSAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 277 LQDYKIQSALLVPTLF-SFFA----------KSTLIDKYDLSNLHEIASGGAPLSKEVGEavakRFHLPGI--RQGYGLT 343
Cdd:cd05907 170 LSEVRPTVFLAVPRVWeKVYAaikvkavpglKRKLFDLAVGGRLRFAASGGAPLPAELLH----FFRALGIpvYEGYGLT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 344 ETTSAILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDI 423
Cdd:cd05907 246 ETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDL 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110555473 424 AYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNIFDAGVAGlpddDAGELPAAVVVLE 488
Cdd:cd05907 315 GEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG----DGRPFLVALIVPD 376
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
44-537 |
4.78e-59 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 205.04 E-value: 4.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 44 DAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNEREL---LNSMGI 120
Cdd:cd05970 41 DAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIvyrIESADI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 121 SQptVVFVSKKGL-QKILNVQKKLPIIQKIIIMdSKTDYQGFQSMYTFVtSHLPPgfneyDFVP---ESFDRDKTIALIM 196
Cdd:cd05970 121 KM--IVAIAEDNIpEEIEKAAPECPSKPKLVWV-GDPVPEGWIDFRKLI-KNASP-----DFERptaNSYPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 197 NSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVL--MYRFEEELF 273
Cdd:cd05970 192 FSSGTTGMPKMVEHDFTYP---LGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIyGQWIAGAAVFVydYDKFDPKAL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 274 LRSLQDYKIQSALLVPTLFSFFAKSTLiDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITP 353
Cdd:cd05970 269 LEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK-LMEGFGQTETTLTIATFP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 354 EGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVR----GPM-IMSGYVNNPEATnALIDKDGWLHSGDIAYWDE 428
Cdd:cd05970 347 WMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRtskgKPVgLFGGYYKDAEKT-AEVWHDGYYHTGDAAWMDE 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 429 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVaSQ 505
Cdd:cd05970 425 DGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEelkKELQDHV-KK 503
|
490 500 510
....*....|....*....|....*....|..
gi 110555473 506 VTTAKKLRGGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:cd05970 504 VTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
51-537 |
4.92e-58 |
|
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: 199.82 E-value: 4.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAM-KRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTvvfvs 129
Cdd:cd05941 12 ITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 130 kkglqkilnvqkklpiiqkiIIMDsktdyqgfqsmytfvtshlppgfneydfvpesfdrdktIALIMNSSGSTGLPKGVA 209
Cdd:cd05941 87 --------------------LVLD--------------------------------------PALILYTSGTTGRPKGVV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 210 LPHR--TACVR-FSHARdpifgnQIIPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVLMYRFEEELFLRSLQDYKIQSA 285
Cdd:cd05941 109 LTHAnlAANVRaLVDAW------RWTEDDVLLHVLPLHHVHGLVNALlCPLFAGASVEFLPKFDPKEVAISRLMPSITVF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 286 LLVPTLFS--------FFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAiLITP-EGD 356
Cdd:cd05941 183 MGVPTIYTrllqyyeaHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHT-LLERYGMTEIGMA-LSNPlDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 357 DKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVD 436
Cdd:cd05941 261 RRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 437 RLKS-LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGK-TMTEKEIVDyVASQVTTAKKLRG 514
Cdd:cd05941 341 RSSVdIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKE-WAKQRLAPYKRPR 419
|
490 500
....*....|....*....|...
gi 110555473 515 GVVFVDEVPKGLTGKLDARKIRE 537
Cdd:cd05941 420 RLILVDELPRNAMGKVNKKELRK 442
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
52-535 |
7.99e-58 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 199.21 E-value: 7.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVskk 131
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 glqkilnvqkklpiiqkiiimDSKTDYQGFQSmytfVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALP 211
Cdd:TIGR01923 78 ---------------------DSLLEEKDFQA----DSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 212 HRTacvRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEelFLRSLQDYKIQSALLVPTL 291
Cdd:TIGR01923 133 FRN---HYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 292 FSFFAKSTLIDkydlSNLHEIASGGAPLSKEVGEAVAKRfHLPgIRQGYGLTETTSAIL-ITPEGDDKPGAVGKVVPFFE 370
Cdd:TIGR01923 208 LNRLLDEGGHN----ENLRKILLGGSAIPAPLIEEAQQY-GLP-IYLSYGMTETCSQVTtATPEMLHARPDVGRPLAGRE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 371 AKV-VDLDTGktlgvnqRGELCVRGPMIMSGYVNNPEATNAlIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQV 449
Cdd:TIGR01923 282 IKIkVDNKEG-------HGEIMVKGANLMKGYLYQGELTPA-FEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 450 APAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEhgKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTG 528
Cdd:TIGR01923 354 YPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKL--AKyKVPIAFEKLDELPYNASG 429
|
....*..
gi 110555473 529 KLDARKI 535
Cdd:TIGR01923 430 KILRNQL 436
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
26-547 |
1.56e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 198.83 E-value: 1.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 26 LHKAMKRYALVPgtiAFTDahIEVDITYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAP 104
Cdd:PRK05677 30 LKQSCQRFADKP---AFSN--LGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 105 ANDIYNERELLNSMGISQPTVVF------------VSKKGLQKIL--NVQKKLPIIQKIIIMDSKTDYQGFQSMYtfvts 170
Cdd:PRK05677 105 TNPLYTAREMEHQFNDSGAKALVclanmahlaekvLPKTGVKHVIvtEVADMLPPLKRLLINAVVKHVKKMVPAY----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 171 HLPP--GFNE-------YDFVPESFDRDKtIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPDTAILSVV 241
Cdd:PRK05677 180 HLPQavKFNDalakgagQPVTEANPQADD-VAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIAPL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 242 PFHHGFGM-FTTLGYLICGFRVVLMYRFEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPL 319
Cdd:PRK05677 259 PLYHIYAFtFHCMAMMLIGNHNILISNPRDlPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMAL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 320 SKevgeAVAKRF-HLPG--IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM 396
Cdd:PRK05677 339 QL----ATAERWkEVTGcaICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 397 IMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDD 476
Cdd:PRK05677 414 VMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEK 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110555473 477 AGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKaKKGGK 547
Cdd:PRK05677 494 SGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPK-AVEFRDELPTTNVGKILRRELRDEELK-KAGLK 562
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
20-538 |
1.65e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 198.23 E-value: 1.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 20 GTAGEQLHKAMKRYalvPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG 99
Cdd:PRK07788 49 GPFAGLVAHAARRA---PDRAALIDERGT--LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 100 VAVApandiynereLLNSmGISQPTVVFVSKKglQKIlnvqkklpiiqKIIIMDSKtdyqgfqsmYTFVTSHLPPGFNEY 179
Cdd:PRK07788 124 ARII----------LLNT-GFSGPQLAEVAAR--EGV-----------KALVYDDE---------FTDLLSALPPDLGRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 180 -------DFVPESFDRDKTIA-------------------LIMNSSGSTGLPKGVALPHRTACVrfshardpifgnqiiP 233
Cdd:PRK07788 171 rawggnpDDDEPSGSTDETLDdliagsstaplpkppkpggIVILTSGTTGTPKGAPRPEPSPLA---------------P 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 234 DTAILSVVPFHHGF------GMFTTLGY----LICGFR--VVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFF--AKST 299
Cdd:PRK07788 236 LAGLLSRVPFRAGEttllpaPMFHATGWahltLAMALGstVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRIldLGPE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 300 LIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETTSAILITPEGDDK-PGAVGKVVPFFEAKVVDlDT 378
Cdd:PRK07788 316 VLAKYDTSSLKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAFATIATPEDLAEaPGTVGRPPKGVTVKILD-EN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 379 GKTLGVNQRGELCVRGPMIMSGYVN--NPEAtnalidKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELES 456
Cdd:PRK07788 394 GNEVPRGVVGRIFVGNGFPFEGYTDgrDKQI------IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 457 ILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 536
Cdd:PRK07788 468 LLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPR-DVVFLDELPRNPTGKVLKRELR 546
|
..
gi 110555473 537 EI 538
Cdd:PRK07788 547 EM 548
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
12-531 |
3.90e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 197.57 E-value: 3.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 12 APFYPLEDGTAGEQLHKAMKRYALVPGTIAFtdAHievDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMP 91
Cdd:PRK06178 25 EPEYPHGERPLTEYLRAWARERPQRPAIIFY--GH---VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 92 VLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIiqKIIIMDSKTDyqgfqsmytFVTSH 171
Cdd:PRK06178 100 FFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSL--RHVIVTSLAD---------VLPAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 172 ----LPPGFNE--------YDFVP-----------ESFDRDKTIALimN-SSGSTGLPKGVALPHR-------TAC-VRF 219
Cdd:PRK06178 169 ptlpLPDSLRAprlaaagaIDLLPalractapvplPPPALDALAAL--NyTGGTTGMPKGCEHTQRdmvytaaAAYaVAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 220 SHARDPIFgnqiipdtaiLSVVPFH----HGFGMfttLGYLICGFRVVLMYRFEEELFLRSLQDYKIQS-ALLVPTLFSF 294
Cdd:PRK06178 247 VGGEDSVF----------LSFLPEFwiagENFGL---LFPLFSGATLVLLARWDAVAFMAAVERYRVTRtVMLVDNAVEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 295 FAKSTLIDkYDLSNLHEIasGGAPLSKEVGEAVAKRFH-LPG--IRQG-YGLTETTSAILITP--EGDD-----KPGAVG 363
Cdd:PRK06178 314 MDHPRFAE-YDLSSLRQV--RVVSFVKKLNPDYRQRWRaLTGsvLAEAaWGMTETHTCDTFTAgfQDDDfdllsQPVFVG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 364 KVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK 443
Cdd:PRK06178 391 LPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 444 YKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAK--KLRggvvFVDE 521
Cdd:PRK06178 470 VNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKvpEIR----IVDA 545
|
570
....*....|
gi 110555473 522 VPKGLTGKLD 531
Cdd:PRK06178 546 LPMTATGKVR 555
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-536 |
3.22e-54 |
|
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: 189.96 E-value: 3.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHRTAcvrfshardpIFGNQII-------PDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM 265
Cdd:cd05922 120 ALLLYTSGSTGSPKLVRLSHQNL----------LANARSIaeylgitADDRALTVLPLSYDYGLSVLNTHLLRGATLVLT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 YRFE-EELFLRSLQDYKIQSALLVPTLFSFFAKSTlIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTE 344
Cdd:cd05922 190 NDGVlDDAFWEDLREHGATGLAGVPSTYAMLTRLG-FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 345 TTSAILITP--EGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGD 422
Cdd:cd05922 269 ATRRMTYLPpeRILEKPGSIGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 423 IAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPdDDAGELPAAVVVLEHGktMTEKEIVDYV 502
Cdd:cd05922 348 LARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDK--IDPKDVLRSL 424
|
330 340 350
....*....|....*....|....*....|....
gi 110555473 503 ASQVTTAkKLRGGVVFVDEVPKGLTGKLDARKIR 536
Cdd:cd05922 425 AERLPPY-KVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
192-530 |
1.93e-53 |
|
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: 184.24 E-value: 1.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMftTLGYLIC---GFRVVLMYRF 268
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCA---DLTEDDRYLIINPFFHTFGY--KAGIVAClltGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSA 348
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 349 ILITPEGD--DKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYW 426
Cdd:cd17638 157 TMCRPGDDaeTVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 427 DEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQV 506
Cdd:cd17638 226 DERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERL 305
|
330 340
....*....|....*....|....
gi 110555473 507 TTAKKLRgGVVFVDEVPKGLTGKL 530
Cdd:cd17638 306 ANYKVPR-FVRFLDELPRNASGKV 328
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
21-537 |
4.61e-53 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 189.32 E-value: 4.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 21 TAGEQLHKAMKRYALVPGTIAFTDAhievdITYAEYFEMSVRLAE-AMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG 99
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKT-----ITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 100 VAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQkiIIMDSKTDYQGF--QSMYTFVTSHLPPGFN 177
Cdd:PRK08751 101 LTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQ--VITTGLGDMLGFpkAALVNFVVKYVKKLVP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 178 EYDF-----------------VPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPD--TAIL 238
Cdd:PRK08751 179 EYRIngairfrealalgrkhsMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEgcEVVI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 239 SVVPFHHGFGM------FTTLG---YLICGFRvvlmyrfEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNL 309
Cdd:PRK08751 259 TALPLYHIFALtanglvFMKIGgcnHLISNPR-------DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 310 HEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRG 388
Cdd:PRK08751 332 KMTLGGGMAVQRSVAERWKQVTGLTLV-EAYGLTETSPAACINPlTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 389 ELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAG 468
Cdd:PRK08751 410 ELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVA 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110555473 469 VAGLPDDDAGELpAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK08751 490 AVGVPDEKSGEI-VKVVIVKKDPALTAEDVKAHARANLTGYKQPR-IIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
200-542 |
7.74e-52 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 187.08 E-value: 7.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 200 GSTGLPKGVALPHrtacvrfshardpifGNQII------------PDTAILSVVPFHHGFGMFTT-LGYLICGFRVVLM- 265
Cdd:PRK07529 223 GTTGMPKLAQHTH---------------GNEVAnawlgalllglgPGDTVFCGLPLFHVNALLVTgLAPLARGAHVVLAt 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 ---YRFEEEL--FLRSLQDYKIQSALLVPTLFSFFAKsTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGY 340
Cdd:PRK07529 288 pqgYRGPGVIanFWKIVERYRINFLSGVPTVYAALLQ-VPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVR-IVEGY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 341 GLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDLD-TGKTL---GVNQRGELCVRGPMIMSGYVNnPEATNALIDKD 415
Cdd:PRK07529 366 GLTEATCVSSVNPpDGERRIGSVGLRLPYQRVRVVILDdAGRYLrdcAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLED 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 416 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 495
Cdd:PRK07529 445 GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE 524
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 110555473 496 KEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGK-----LDARKIREILIKA 542
Cdd:PRK07529 525 AELLAFARDHIAERAAVPKHVRILDALPKTAVGKifkpaLRRDAIRRVLRAA 576
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
77-536 |
3.71e-51 |
|
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: 182.53 E-value: 3.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 77 RIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKIlnVQKKLPIIQ---KIIIM- 152
Cdd:cd05909 33 NVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKL--KLHHLFDVEydaRIVYLe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 153 DSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTiALIMNSSGSTGLPKGVALPHR---------TACVRFShar 223
Cdd:cd05909 111 DLRAKISKADKCKAFLAGKFPPKWLLRIFGVAPVQPDDP-AVILFTSGSEGLPKGVVLSHKnllanveqiTAIFDPN--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 224 dpifgnqiiPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYR-FEEELFLRSLQDYKIQSALLVPTLFSFFAKStlI 301
Cdd:cd05909 187 ---------PEDVVFGALPFFHSFGLTGCLWLpLLSGIKVVFHPNpLDYKKIPELIYDKKATILLGTPTFLRGYARA--A 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 302 DKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILI-TPEGDDKPGAVGKVVPFFEAKVVDLDTGK 380
Cdd:cd05909 256 HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECSPVISVnTPQSPNKEGTVGRPLPGMEVKIVSVETHE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 381 TLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ 460
Cdd:cd05909 335 EVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSE 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 461 H-PNIFDAGVAGLPDDDAGElpaAVVVLEHGKTMTEKEIVDYV-ASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 536
Cdd:cd05909 414 IlPEDNEVAVVSVPDGRKGE---KIVLLTTTTDTDPSSLNDILkNAGISNLAKPS-YIHQVEEIPLLGTGKPDYVTLK 487
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
71-544 |
3.95e-51 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 184.10 E-value: 3.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 71 GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNEREL---LNSMGISqpTVVFVSK--KGLQKILNvqkKLPI 145
Cdd:PRK08974 70 GLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELehqLNDSGAK--AIVIVSNfaHTLEKVVF---KTPV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 146 iqKIIIMDSKTDYQGF--QSMYTFVTS---------HLPPG--FNE-------YDFVPESFDRDkTIALIMNSSGSTGLP 205
Cdd:PRK08974 145 --KHVILTRMGDQLSTakGTLVNFVVKyikrlvpkyHLPDAisFRSalhkgrrMQYVKPELVPE-DLAFLQYTGGTTGVA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 206 KGVALPHRTACVRFSHArDPIFGNQIIPDTA-ILSVVPFHHGFGM------FTTLG---YLICGFRVVlmyrfeeELFLR 275
Cdd:PRK08974 222 KGAMLTHRNMLANLEQA-KAAYGPLLHPGKElVVTALPLYHIFALtvncllFIELGgqnLLITNPRDI-------PGFVK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 276 SLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPlskeVGEAVAKRFH-LPGIR--QGYGLTETTSAILIT 352
Cdd:PRK08974 294 ELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMA----VQQAVAERWVkLTGQYllEGYGLTECSPLVSVN 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 353 PEG-DDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEH 431
Cdd:PRK08974 370 PYDlDYYSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 432 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELpAAVVVLEHGKTMTEKEIVDYVASQVTTAK- 510
Cdd:PRK08974 448 LRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLTEEELITHCRRHLTGYKv 526
|
490 500 510
....*....|....*....|....*....|....*.
gi 110555473 511 -KLrggVVFVDEVPKGLTGKLDARKIR-EILIKAKK 544
Cdd:PRK08974 527 pKL---VEFRDELPKSNVGKILRRELRdEARAKVDN 559
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
32-537 |
4.93e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 183.44 E-value: 4.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 32 RYALV-PGTIAFTdaHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYN 110
Cdd:PRK07786 25 RHALMqPDAPALR--FLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 111 ERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQsmYTFVTSHLPPGFNEYDfVPESfdrdk 190
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLG--YEDLLAEAGPAHAPVD-IPND----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 191 TIALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQI-IPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL--MYR 267
Cdd:PRK07786 175 SPALIMYTSGTTGRPKGAVLTHANLT---GQAMTCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIypLGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 268 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETtS 347
Cdd:PRK07786 252 FDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEM-S 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 348 AILITPEGDD---KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDkDGWLHSGDIA 424
Cdd:PRK07786 330 PVTCMLLGEDairKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 425 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG-KTMTEKEIVDYVA 503
Cdd:PRK07786 408 RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLT 487
|
490 500 510
....*....|....*....|....*....|....
gi 110555473 504 SQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK07786 488 DRLARYKHPK-ALEIVDALPRNPAGKVLKTELRE 520
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
46-537 |
6.95e-51 |
|
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: 181.73 E-value: 6.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 46 HIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSlqffmPVLGALFIGVAVAPAndiynereLLNSmgisqptv 125
Cdd:cd12118 25 YGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNT-----PAMYELHFGVPMAGA--------VLNA-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 126 vfvskkglqkiLNVQKKLPIIQ--------KIIIMDSKTDYQGFQSMytfvtshlppGFNEYDFVPESfDRDKTIALimN 197
Cdd:cd12118 84 -----------LNTRLDAEEIAfilrhseaKVLFVDREFEYEDLLAE----------GDPDFEWIPPA-DEWDPIAL--N 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 198 -SSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVP-FH-----HGFGMFTTLGYLICgfrvvlMYRFEE 270
Cdd:cd12118 140 yTSGTTGRPKGVVYHHRGA---YLNALANILEWEMKQHPVYLWTLPmFHcngwcFPWTVAAVGGTNVC------LRKVDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 271 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAV-AKRFHlpgIRQGYGLTETTSAI 349
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMeELGFD---VTHVYGLTETYGPA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 350 LI---TPEGDDKPGA----------VGkVVPFFEAKVVDLDT-------GKTLGvnqrgELCVRGPMIMSGYVNNPEATN 409
Cdd:cd12118 288 TVcawKPEWDELPTEerarlkarqgVR-YVGLEEVDVLDPETmkpvprdGKTIG-----EIVFRGNIVMKGYLKNPEATA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 410 ALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 489
Cdd:cd12118 362 EAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKE 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 110555473 490 GKTMTEKEIVDYVASQVTTAKKLRgGVVFvDEVPKGLTGKLDARKIRE 537
Cdd:cd12118 441 GAKVTEEEIIAFCREHLAGFMVPK-TVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
11-536 |
8.37e-51 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 182.91 E-value: 8.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 11 PAPFYPLEDGTAGEQLHKAMKRYALVPgtiAFTDahIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFM 90
Cdd:PRK07059 14 PAEIDASQYPSLADLLEESFRQYADRP---AFIC--MGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 91 PVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK---GLQKILNvqkKLPIiqKIIIMDSKTDYQGFQS-MYT 166
Cdd:PRK07059 89 AIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENfatTVQQVLA---KTAV--KHVVVASMGDLLGFKGhIVN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 167 FVTSHLP--------PGFNEYD----------FVPESFDRDKtIALIMNSSGSTGLPKGVALPHRT--ACVRFSHA-RDP 225
Cdd:PRK07059 164 FVVRRVKkmvpawslPGHVRFNdalaegarqtFKPVKLGPDD-VAFLQYTGGTTGVSKGATLLHRNivANVLQMEAwLQP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 226 IFGNQIIPDT-AILSVVPFHHGFGMftTLGYLI---CGFRVVLMYRFEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTL 300
Cdd:PRK07059 243 AFEKKPRPDQlNFVCALPLYHIFAL--TVCGLLgmrTGGRNILIPNPRDiPGFIKELKKYQVHIFPAVNTLYNALLNNPD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 301 IDKYDLSNLhEIASGGAplsKEVGEAVAKR-FHLPG--IRQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDl 376
Cdd:PRK07059 321 FDKLDFSKL-IVANGGG---MAVQRPVAERwLEMTGcpITEGYGLSETSPVATCNPvDATEFSGTIGLPLPSTEVSIRD- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 377 DTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELES 456
Cdd:PRK07059 396 DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 457 ILLQHPNIFDAGVAGLPDDDAGELPAAVVVlEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 536
Cdd:PRK07059 476 VVASHPGVLEVAAVGVPDEHSGEAVKLFVV-KKDPALTEEDVKAFCKERLTNYKRPK-FVEFRTELPKTNVGKILRRELR 553
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
24-538 |
1.41e-50 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 182.33 E-value: 1.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 24 EQLHKAMKRYALVPgtiAFTDahIEVDITYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAV 102
Cdd:PRK12492 28 EVFERSCKKFADRP---AFSN--LGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 103 APANDIYNERELLNSMGISQP-TVVFVSKKGLQkilnVQKKLP--IIQKII---IMDSKTDYQGFQsMYTFVTS------ 170
Cdd:PRK12492 103 VNTNPLYTAREMRHQFKDSGArALVYLNMFGKL----VQEVLPdtGIEYLIeakMGDLLPAAKGWL-VNTVVDKvkkmvp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 171 --HLPP--GFNE---------YDFVPESFDrdkTIALIMNSSGSTGLPKGVALPHRT---------ACVRfSHARDpifG 228
Cdd:PRK12492 178 ayHLPQavPFKQalrqgrglsLKPVPVGLD---DIAVLQYTGGTTGLAKGAMLTHGNlvanmlqvrACLS-QLGPD---G 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 229 NQIIPD--TAILSVVPFHHGFGmFTT--LGYLICGFRVVLMYRFEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDK 303
Cdd:PRK12492 251 QPLMKEgqEVMIAPLPLYHIYA-FTAncMCMMVSGNHNVLITNPRDiPGFIKELGKWRFSALLGLNTLFVALMDHPGFKD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 304 YDLSNLHEIASGGAPLSKevgeAVAKRF-HLPGIR--QGYGLTETTSAILITPEGD-DKPGAVGKVVPFFEAKVVDlDTG 379
Cdd:PRK12492 330 LDFSALKLTNSGGTALVK----ATAERWeQLTGCTivEGYGLTETSPVASTNPYGElARLGTVGIPVPGTALKVID-DDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 380 KTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILL 459
Cdd:PRK12492 405 NELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110555473 460 QHPNIFDAGVAGLPDDDAGELPAAVVVLEHGkTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 538
Cdd:PRK12492 485 AHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENF-TGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
51-537 |
1.44e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 181.43 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 130
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmYTFVTSHLPPGfneydfvpeSFDRDKTIALIMNSSGSTGLPKGV-- 208
Cdd:PRK13391 105 AKLDVARALLKQCPGVRHRLVLDGDGELEGFVG-YAEAVAGLPAT---------PIADESLGTDMLYSSGTTGRPKGIkr 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 209 ALPHR--TACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSAL 286
Cdd:PRK13391 175 PLPEQppDTPLPLTAFLQRLWG--FRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 287 LVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETTSAILI-TPEGDDKPGAVG 363
Cdd:PRK13391 253 LVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWG-PIIHEYYAATEGLGFTACdSEEWLAHPGTVG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 364 KVVpFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSgYVNNPEATNALIDKDG-WLHSGDIAYWDEDEHFFIVDRLKSLI 442
Cdd:PRK13391 332 RAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 443 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVASQVTTAKKLRgGVVFV 519
Cdd:PRK13391 409 ISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFCRQRLSRQKCPR-SIDFE 487
|
490
....*....|....*...
gi 110555473 520 DEVPKGLTGKLDARKIRE 537
Cdd:PRK13391 488 DELPRLPTGKLYKRLLRD 505
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
52-537 |
2.53e-50 |
|
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: 179.11 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELlnsmgisqptvVFVSKK 131
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHEL-----------AFILRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 GLQKILnvqkklpiiqkiIIMDSktdyqgfqsmytfvtshlppgFNEYDFVPESFDrdktIALIMNSSGSTGLPKGVALP 211
Cdd:cd05903 72 AKAKVF------------VVPER---------------------FRQFDPAAMPDA----VALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 212 HRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHH--GFGMFTTLGYLIcGFRVVLMYRFEEELFLRSLQDYKIQSALLVP 289
Cdd:cd05903 115 HNTL---SASIRQYAERLGLGPGDVFLVASPMAHqtGFVYGFTLPLLL-GAPVVLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 290 TLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRqGYGLTETTSAILITPEGDDKPGAV--GKVVP 367
Cdd:cd05903 191 PFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS-AYGSTECPGAVTSITPAPEDRRLYtdGRPLP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 368 FFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEaTNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGY 447
Cdd:cd05903 270 GVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPD-LTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 448 QVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLT 527
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPS 427
|
490
....*....|
gi 110555473 528 GKLDARKIRE 537
Cdd:cd05903 428 GKVQKFRLRE 437
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
195-531 |
6.97e-50 |
|
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: 174.77 E-value: 6.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 195 IMNSSGSTGLPKGVALPHR---TACVRFSHARdpifgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEE 271
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGnliAANLQLIHAM------GLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 272 LFLRSLQDYKIqsallvpTLFSFFAK--STLIDK-----YDLSNLHEIASGGAPlskevgeAVAKRFH-LPGIR--QGYG 341
Cdd:cd17637 79 EALELIEEEKV-------TLMGSFPPilSNLLDAaeksgVDLSSLRHVLGLDAP-------ETIQRFEeTTGATfwSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 342 LTETTSAILITPEgDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSG 421
Cdd:cd17637 145 QTETSGLVTLSPY-RERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 422 DIAYWDEDEHFFIVDRL--KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 499
Cdd:cd17637 222 DLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELI 301
|
330 340 350
....*....|....*....|....*....|..
gi 110555473 500 DYVASQVTTAKKLRgGVVFVDEVPKGLTGKLD 531
Cdd:cd17637 302 EFVGSRIARYKKPR-YVVFVEALPKTADGSID 332
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
48-536 |
7.10e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 178.64 E-value: 7.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 48 EVDITYAEYFEMSVRLAEamkryGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVF 127
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 128 VSKKGlqkilnVQKKLPIIQKIIIMDSktdyqgfqsmytfvtSHLPPgfnEYDfvPESfdrdktIALIMNSSGSTGLPKG 207
Cdd:PRK07787 98 GPAPD------DPAGLPHVPVRLHARS---------------WHRYP---EPD--PDA------PALIVYTSGTTGPPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 208 VALPHR--TACVR-FSHARdpifgnQIIPDTAILSVVP-FH-HGFgMFTTLGYLICGFRVVLMYRFEEELFLRSLQDyki 282
Cdd:PRK07787 146 VVLSRRaiAADLDaLAEAW------QWTADDVLVHGLPlFHvHGL-VLGVLGPLRIGNRFVHTGRPTPEAYAQALSE--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 283 QSALL--VPTLFSFFAKSTLIDKyDLSNLHEIASGGAPLSKEVGEAVAkrfHLPGIR--QGYGLTETtsaiLIT----PE 354
Cdd:PRK07787 216 GGTLYfgVPTVWSRIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLA---ALTGHRpvERYGMTET----LITlstrAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 355 GDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQR--GELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHF 432
Cdd:PRK07787 288 GERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 433 FIVDRlKS--LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVleHGKTMTEKEIVDYVASQVTTAK 510
Cdd:PRK07787 367 RIVGR-EStdLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSVHK 443
|
490 500
....*....|....*....|....*.
gi 110555473 511 KLRgGVVFVDEVPKGLTGKLDARKIR 536
Cdd:PRK07787 444 RPR-EVRFVDALPRNAMGKVLKKQLL 468
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
52-543 |
1.41e-49 |
|
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: 176.92 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSkk 131
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 glqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvPESFDRD--KTIALIMNSSGSTGLPKGVA 209
Cdd:cd05969 80 ---------------------------------------------------EELYERTdpEDPTLLHYTSGTTGTPKGVL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 210 LPHR-------TACVRFSHARDPIFGNQIIP----DTAILSVVPFHHGFGMfttlgylicgfrVVLMYRFEEELFLRSLQ 278
Cdd:cd05969 109 HVHDamifyyfTGKYVLDLHPDDIYWCTADPgwvtGTVYGIWAPWLNGVTN------------VVYEGRFDAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 279 DYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETtSAILIT--PE 354
Cdd:cd05969 177 RVKVTVWYTAPTAIRMLMKEgdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWWQTET-GSIMIAnyPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 355 GDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRG--PMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHF 432
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDEN-GNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 433 FIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVasqvttA 509
Cdd:cd05969 333 WFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFV------R 406
|
490 500 510
....*....|....*....|....*....|....*....
gi 110555473 510 KKLRGGVV-----FVDEVPKGLTGKLDARkireiLIKAK 543
Cdd:cd05969 407 QKLGAHVApreieFVDNLPKTRSGKIMRR-----VLKAK 440
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
192-536 |
1.64e-49 |
|
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: 176.90 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRT---ACVRFSHArdpIFGNQiiPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYR 267
Cdd:cd05958 99 ICILAFTSGTTGAPKATMHFHRDplaSADRYAVN---VLRLR--EDDRFVGSPPLAFTFGLGGVLLFpFGVGASGVLLEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 268 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTS 347
Cdd:cd05958 174 ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIP-IIDGIGSTEMFH 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 348 AILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPmimSGYVNNPEATNALIDKDGWLHSGDIAYWD 427
Cdd:cd05958 253 IFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 428 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVAS 504
Cdd:cd05958 329 PDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAKA 408
|
330 340 350
....*....|....*....|....*....|..
gi 110555473 505 QVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 536
Cdd:cd05958 409 HIAPYKYPR-AIEFVTELPRTATGKLQRFALR 439
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-536 |
2.63e-49 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 174.21 E-value: 2.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGValPHRTACVRFSH---ARDPIFGnqiiPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLM-- 265
Cdd:cd05944 4 VAAYFHTGGTTGTPKLA--QHTHSNEVYNAwmlALNSLFD----PDDVLLCGLPLFHVNGSVVTLLTPLAsGAHVVLAgp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 --YR----FEEelFLRSLQDYKIQSALLVPTLFSffAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQG 339
Cdd:cd05944 78 agYRnpglFDN--FWKLVERYRITSLSTVPTVYA--ALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLP-VVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 340 YGLTETTSAILIT-PEGDDKPGAVGKVVPFFEAKVVDLD----TGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDk 414
Cdd:cd05944 153 YGLTEATCLVAVNpPDGPKRPGSVGLRLPYARVRIKVLDgvgrLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVA- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 415 DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT 494
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 110555473 495 EKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIR 536
Cdd:cd05944 312 EEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
19-541 |
4.36e-49 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 178.02 E-value: 4.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 19 DGTAGEQLHKAMKRYalvPGTIAFTDAHiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFI 98
Cdd:PRK06087 22 DASLADYWQQTARAM---PDKIAVVDNH-GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 99 GVAVAPANDIYNERELLNSMGISQPTVVFV-----SKKGLQKILNVQKKLPIIQKIIIMDSKTdyqgfQSMYTFVTSH-L 172
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLA-----PATSSLSLSQiI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 173 PPGFNEYDFVPESFDrdkTIALIMNSSGSTGLPKGVALPHRTacVRFSHaRDPIFGNQIIPDTAILSVVPFHHGFGMF-- 250
Cdd:PRK06087 173 ADYEPLTTAITTHGD---ELAAVLFTSGTEGLPKGVMLTHNN--ILASE-RAYCARLNLTWQDVFMMPAPLGHATGFLhg 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 251 TTLGYLIcGFRVVLMYRFEEELFLRSLQDYKIqSALLVPTLFSFFAKSTL-IDKYDLSNLHEIASGGAPLSKEVgeavAK 329
Cdd:PRK06087 247 VTAPFLI-GARSVLLDIFTPDACLALLEQQRC-TCMLGATPFIYDLLNLLeKQPADLSALRFFLCGGTTIPKKV----AR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 330 RFHLPGIR--QGYGLTETTSAILITPegdDKP-----GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYV 402
Cdd:PRK06087 321 ECQQRGIKllSVYGSTESSPHAVVNL---DDPlsrfmHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 403 NNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPA 482
Cdd:PRK06087 397 DEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSC 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 483 AVVVL-EHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREILIK 541
Cdd:PRK06087 477 AYVVLkAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMR 536
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
50-537 |
1.14e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 175.84 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 50 DITYAEyFEMSVRLAEAM-KRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiynerellnsMGISQPTVVFV 128
Cdd:PRK06145 27 EISYAE-FHQRILQAAGMlHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN-----------YRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 129 SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPpgfneydFVPESFDRDKTIALIMNSSGSTGLPKGV 208
Cdd:PRK06145 95 LGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLE-------IPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 209 AlpHRTACVRFSHArDPIFGNQIIPDTAILSVVPFHH-GFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALL 287
Cdd:PRK06145 168 M--HSYGNLHWKSI-DHVIALGLTASERLLVVGPLYHvGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 288 VPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGD--DKPGAVGKV 365
Cdd:PRK06145 245 APVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGReiEKIGSTGRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 366 VPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYK 445
Cdd:PRK06145 325 LAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 446 GYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVfVDEVPKG 525
Cdd:PRK06145 403 GENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKV-RDELPRN 481
|
490
....*....|..
gi 110555473 526 LTGKLDARKIRE 537
Cdd:PRK06145 482 PSGKVLKRVLRD 493
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
42-537 |
1.21e-48 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 177.39 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 42 FTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGIS 121
Cdd:PRK04319 65 YLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 122 QPTVVFVSKKGLQKIlnVQKKLPIIQKIIIMDSKTDYQGfqsmytfVTSHLPPGFNEY--DFVPESFDRDKTiALIMNSS 199
Cdd:PRK04319 145 EAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEEGP-------GTLDFNALMEQAsdEFDIEWTDREDG-AILHYTS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 200 GSTGLPKGVALPHRTACVRFSHAR---------------DP---------IFGnqiipdtailsvvPFHHGFGMfttlgy 255
Cdd:PRK04319 215 GSTGKPKGVLHVHNAMLQHYQTGKyvldlheddvywctaDPgwvtgtsygIFA-------------PWLNGATN------ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 256 licgfrVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLIDKYDLSNLHEIASGGAPLSKEV---GEAVakr 330
Cdd:PRK04319 276 ------VIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLmgAGDDLVKKYDLSSLRHILSVGEPLNPEVvrwGMKV--- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 331 FHLPgIRQGYGLTETtSAILI--TPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG--PMIMSGYVNNPE 406
Cdd:PRK04319 347 FGLP-IHDNWWMTET-GGIMIanYPAMDIKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKgwPSMMRGIWNNPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 407 ATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 486
Cdd:PRK04319 424 KYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVA 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110555473 487 LEHGKTMTE---KEIVDYVasqvttaKKLRGGVV------FVDEVPKGLTGKLDAR--KIRE 537
Cdd:PRK04319 503 LRPGYEPSEelkEEIRGFV-------KKGLGAHAapreieFKDKLPKTRSGKIMRRvlKAWE 557
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
18-539 |
5.06e-48 |
|
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: 174.95 E-value: 5.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 18 EDGTAGEQLHKAMKRYalvPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALF 97
Cdd:COG1021 23 RGETLGDLLRRRAERH---PDRIAVVDGERR--LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 98 IG---VAVAPAndiYNERELLNSMGISQPTVVFVSKK----GLQKILN-VQKKLPIIQKIIIMDSKTDYQGFQSMYTFVT 169
Cdd:COG1021 98 AGaipVFALPA---HRRAEISHFAEQSEAVAYIIPDRhrgfDYRALAReLQAEVPSLRHVLVVGDAGEFTSLDALLAAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 170 SHLPPGfneydfvPESFDrdktIALIMNSSGSTGLPKGVALPHRT-AC-VRFShARdpIFGnqIIPDTAILSVVPFHHGF 247
Cdd:COG1021 175 DLSEPR-------PDPDD----VAFFQLSGGTTGLPKLIPRTHDDyLYsVRAS-AE--ICG--LDADTVYLAALPAAHNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 248 GM--FTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGE 325
Cdd:COG1021 239 PLssPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 326 AVAKRFHlPGIRQGYGLTEttSAILITPEGDD---------KPgavgkVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM 396
Cdd:COG1021 319 RVRPALG-CTLQQVFGMAE--GLVNYTRLDDPeevilttqgRP-----ISPDDEVRIVD-EDGNPVPPGEVGELLTRGPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 397 IMSGYVNNPEAtNAL-IDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDD 475
Cdd:COG1021 390 TIRGYYRAPEH-NARaFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110555473 476 DAGELPAAVVVLeHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:COG1021 469 YLGERSCAFVVP-RGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
40-537 |
5.13e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 174.32 E-value: 5.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 40 IAFTDAHIevdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMG 119
Cdd:PRK08276 5 MAPSGEVV----TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 120 ISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTdyqgfqsmytfvtshlPPGFNEY----DFVPESFDRDKTIALI 195
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGP----------------VPGFRSYeealAAQPDTPIADETAGAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 196 MN-SSGSTGLPKGV--ALPHRTACVR-FSHARDPIFGNQIIPDTAILSVVPFHHG----FGMFTtlgyLICGFRVVLMYR 267
Cdd:PRK08276 145 MLySSGTTGRPKGIkrPLPGLDPDEApGMMLALLGFGMYGGPDSVYLSPAPLYHTaplrFGMSA----LALGGTVVVMEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 268 FEEELFLRSLQDYKIQSALLVPTLFSFFAKstLID----KYDLSNLHEIASGGAPLSKEVgeavaKRFHL----PGIRQG 339
Cdd:PRK08276 221 FDAEEALALIERYRVTHSQLVPTMFVRMLK--LPEevraRYDVSSLRVAIHAAAPCPVEV-----KRAMIdwwgPIIHEY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 340 YGLTETTSAILITPEgD--DKPGAVGKVVpFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGW 417
Cdd:PRK08276 294 YASSEGGGVTVITSE-DwlAHPGSVGKAV-LGEVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 418 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE-- 495
Cdd:PRK08276 371 VTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDal 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 110555473 496 -KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK08276 451 aAELIAWLRGRLAHYKCPR-SIDFEDELPRTPTGKLYKRRLRD 492
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
193-536 |
9.84e-48 |
|
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: 171.85 E-value: 9.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHRtacVRFSHARDPIFGNQIIPDTAILSVVPFHHGF--GMFTTL-GYLICGFRVVL--MYR 267
Cdd:cd05971 91 ALIIYTSGTTGPPKGALHAHR---VLLGHLPGVQFPFNLFPRDGDLYWTPADWAWigGLLDVLlPSLYFGVPVLAhrMTK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 268 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTE--- 344
Cdd:cd05971 168 FDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVE-VNEFYGQTEcnl 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 345 --TTSAILitpeGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVR--GPMIMSGYVNNPEATNALIdKDGWLHS 420
Cdd:cd05971 247 viGNCSAL----FPIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 421 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KE 497
Cdd:cd05971 321 GDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDalaRE 400
|
330 340 350
....*....|....*....|....*....|....*....
gi 110555473 498 IVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 536
Cdd:cd05971 401 IQELVKTRLAAHEYPR-EIEFVNELPRTATGKIRRRELR 438
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
194-537 |
8.67e-47 |
|
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: 170.25 E-value: 8.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMNSSGSTGLPKGV--ALPHRTACVrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEE 271
Cdd:cd05929 129 KMLYSGGTTGRPKGIkrGLPGGPPDN--DTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 272 LFLRSLQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVakrFHL--PGIRQGYGLTETTS 347
Cdd:cd05929 207 EFLRLIERYRVTFAQFVPTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQW---IDWggPIIWEYYGGTEGQG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 348 AILITpeGDD---KPGAVGKVVpFFEAKVVDLDtGKTLGVNQRGELCVRGPMiMSGYVNNPEATNALIDKDGWLHSGDIA 424
Cdd:cd05929 284 LTIIN--GEEwltHPGSVGRAV-LGKVHILDED-GNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 425 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVV---VLEHGKTMTEKEIVDY 501
Cdd:cd05929 359 YLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpaPGADAGTALAEELIAF 438
|
330 340 350
....*....|....*....|....*....|....*.
gi 110555473 502 VASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:cd05929 439 LRDRLSRYKCPR-SIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
37-539 |
1.94e-46 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 170.62 E-value: 1.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAHIE----VDITYAEYFEMSVRLAEAMKRYGLNTNHriVVCSE--NSLQFFMPVLGALFIGVAVAPANDIYN 110
Cdd:PRK13295 38 PDKTAVTAVRLGtgapRRFTYRELAALVDRVAVGLARLGVGRGD--VVSCQlpNWWEFTVLYLACSRIGAVLNPLMPIFR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 111 ERELLNSMGISQPTVVFVSK--KGL---QKILNVQKKLPIIQKIIIMDSKTDyQGFQSMYTfvtshlPPGFNEYDFVPES 185
Cdd:PRK13295 116 ERELSFMLKHAESKVLVVPKtfRGFdhaAMARRLRPELPALRHVVVVGGDGA-DSFEALLI------TPAWEQEPDAPAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 186 FDRDKT----IALIMNSSGSTGLPKGVAlphrtacvrfsHARDPIFGNqIIP---------DTAILSVVPFHH--GFgMF 250
Cdd:PRK13295 189 LARLRPgpddVTQLIYTSGTTGEPKGVM-----------HTANTLMAN-IVPyaerlglgaDDVILMASPMAHqtGF-MY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 251 TTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKR 330
Cdd:PRK13295 256 GLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 331 FHLPgIRQGYGLTETTSAILITPEGDDKPGAV--GKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEAT 408
Cdd:PRK13295 336 LGAK-IVSAWGMTENGAVTLTKLDDPDERASTtdGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 409 NalIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLE 488
Cdd:PRK13295 414 G--TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 110555473 489 HGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:PRK13295 492 PGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
198-537 |
2.54e-46 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 169.88 E-value: 2.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 198 SSGSTGLPKGV----ALPHRTAcvRFSHARDPIFGnqIIPDTAILSVVPFHH----GFGMFT-TLGYLIcgfrvVLMYRF 268
Cdd:PRK12406 160 TSGTTGHPKGVrraaPTPEQAA--AAEQMRALIYG--LKPGIRALLTGPLYHsapnAYGLRAgRLGGVL-----VLQPRF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEELFLRSLQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETT 346
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWG-PVIYEYYGSTESG 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 347 SAILITPEGD-DKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGP-MIMSGYVNNPEAtNALIDKDGWLHSGDIA 424
Cdd:PRK12406 310 AVTFATSEDAlSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAgNPDFTYHNKPEK-RAEIDRGGFITSGDVG 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 425 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVAS 504
Cdd:PRK12406 388 YLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKA 467
|
330 340 350
....*....|....*....|....*....|...
gi 110555473 505 QVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK12406 468 RLAGYKVPK-HIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
51-529 |
1.75e-45 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 167.36 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSk 130
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 kglqkilnvQKKLPIIQKIiimdskTDYQGFQSMYTF----------VTSHLPPgfneyDFVPESFDRDKtIALIMNSSG 200
Cdd:PRK07514 108 ---------PANFAWLSKI------AAAAGAPHVETLdadgtgslleAAAAAPD-----DFETVPRGADD-LAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 201 STGLPKGVALPHR----TACV-----RFShardpifgnqiiPDTAILSVVPFHHGFGMF-TTLGYLICGFRVVLMYRFEE 270
Cdd:PRK07514 167 TTGRSKGAMLSHGnllsNALTlvdywRFT------------PDDVLIHALPIFHTHGLFvATNVALLAGASMIFLPKFDP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 271 ELFLRSLQdykiQSALL--VPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRF-HlpGIRQGYGLTETts 347
Cdd:PRK07514 235 DAVLALMP----RATVMmgVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTgH--AILERYGMTET-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 348 aILIT--P-EGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIA 424
Cdd:PRK07514 307 -NMNTsnPyDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 425 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVAS 504
Cdd:PRK07514 386 KIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKG 465
|
490 500
....*....|....*....|....*.
gi 110555473 505 QVttAK-KLRGGVVFVDEVPKGLTGK 529
Cdd:PRK07514 466 RL--ARfKQPKRVFFVDELPRNTMGK 489
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
52-542 |
3.22e-45 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 167.24 E-value: 3.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 131
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 GLQKILNVQKKLPIIQKIIIMDSKtdyqgfqsmytfVTSHLPPGFNEYDFVP--ESFD----RDKTIALIMNSSGSTGLP 205
Cdd:PRK06155 128 LLAALEAADPGDLPLPAVWLLDAP------------ASVSVPAGWSTAPLPPldAPAPaaavQPGDTAAILYTSGTTGPS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 206 KGVALPHrtacvrfshARDPIFGN------QIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQD 279
Cdd:PRK06155 196 KGVCCPH---------AQFYWWGRnsaedlEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 280 YKIQSALLVPTLFSFFAKSTlidKYDLSNLHEIASGGAP-LSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPeGDDK 358
Cdd:PRK06155 267 HGATVTYLLGAMVSILLSQP---ARESDRAHRVRVALGPgVPAALHAAFRERFGVD-LLDGYGSTETNFVIAVTH-GSQR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 359 PGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG--PM-IMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIV 435
Cdd:PRK06155 342 PGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 436 DRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgG 515
Cdd:PRK06155 420 DRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPR-Y 498
|
490 500
....*....|....*....|....*..
gi 110555473 516 VVFVDEVPKGLTGKLDARKIREILIKA 542
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLREQGVTA 525
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
21-538 |
2.14e-44 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 168.95 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 21 TAGEQLHKAMKRyalVPGTIAFTDAhIEVDITYAEYFEMSVRLAEAMKRYGLNTNHrIVVCSENSLQFFMPVLGALFIGV 100
Cdd:PRK08633 616 PLAEAWIDTAKR---NWSRLAVADS-TGGELSYGKALTGALALARLLKRELKDEEN-VGILLPPSVAGALANLALLLAGK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 101 AVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKI--LNVQKKLPIIQKIIIM-DSKTDYQGFQSMYTFVTSHLPPGFN 177
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLknKGFDLELPENVKVIYLeDLKAKISKVDKLTALLAARLLPARL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 178 EYDFVPESFDRDKTIALIMnSSGSTGLPKGVALPHRTacvrfshardpIFGN-----QIIP---DTAILSVVPFHHGFGM 249
Cdd:PRK08633 771 LKRLYGPTFKPDDTATIIF-SSGSEGEPKGVMLSHHN-----------ILSNieqisDVFNlrnDDVILSSLPFFHSFGL 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 250 -FTTLGYLICGFRVVLMYRFEEELFLRSLQDyKIQSALLV--PTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEA 326
Cdd:PRK08633 839 tVTLWLPLLEGIKVVYHPDPTDALGIAKLVA-KHRATILLgtPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADA 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 327 VAKRFHLPgIRQGYGLTETTSAILI-TP---EGDD------KPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPM 396
Cdd:PRK08633 918 FEEKFGIR-ILEGYGATETSPVASVnLPdvlAADFkrqtgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQ 996
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 397 IMSGYVNNPEATNALI---DKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQhpnIFDAG----- 468
Cdd:PRK08633 997 VMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK---ALGGEevvfa 1073
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 469 VAGLPDDDAGElpaAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 538
Cdd:PRK08633 1074 VTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
198-539 |
2.35e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 164.44 E-value: 2.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 198 SSGSTGLPKGVALPHRT-ACVRFSHARDpifgnqIIPDT----AILSVVPFHHGFGMfttlgYLIC----GFRVVLMY-- 266
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQmAFVITNHLAD------LMPGTteqdASLVVAPLSHGAGI-----HQLCqvarGAATVLLPse 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 267 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETT 346
Cdd:PRK07470 240 RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLG-KVLVQYFGLGEVT 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 347 SAILITP----EGDDKP----GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAtNALIDKDGWL 418
Cdd:PRK07470 319 GNITVLPpalhDAEDGPdariGTCGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEA-NAKAFRDGWF 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 419 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEI 498
Cdd:PRK07470 397 RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAEL 476
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 110555473 499 VDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:PRK07470 477 LAWLDGKV--ARyKLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
18-531 |
9.78e-44 |
|
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: 162.11 E-value: 9.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 18 EDGTAGEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALF 97
Cdd:cd05920 13 QDEPLGDLLARSAARH---PDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 98 IGVAVAPANDIYNERELLNSMGISQPTVVFVSKKglqkilnvqkklpiiqkiiimdsktdYQGFQSMYTFVTSHlppgfn 177
Cdd:cd05920 88 LGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDR--------------------------HAGFDHRALARELA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 178 eyDFVPEsfdrdktIALIMNSSGSTGLPKGVALPHR------TACVRFSHardpifgnqIIPDTAILSVVPFHHGFGMFT 251
Cdd:cd05920 136 --ESIPE-------VALFLLSGGTTGTPKLIPRTHNdyaynvRASAEVCG---------LDQDTVYLAVLPAAHNFPLAC 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 252 --TLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAK 329
Cdd:cd05920 198 pgVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 330 RFHlPGIRQGYGLTETtsaiLITPEGDDKPGAV-----GK-VVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVN 403
Cdd:cd05920 278 VLG-CTLQQVFGMAEG----LLNYTRLDDPDEViihtqGRpMSPDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 404 NPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAA 483
Cdd:cd05920 352 APEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 110555473 484 VVVLEHGKT--------MTEKEIVDYvasqvttakKLRGGVVFVDEVPKGLTGKLD 531
Cdd:cd05920 432 FVVLRDPPPsaaqlrrfLRERGLAAY---------KLPDRIEFVDSLPLTAVGKID 478
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
46-536 |
1.91e-43 |
|
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: 160.32 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 46 HIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTV 125
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 126 VFVSkkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfdrDKTIALIMNSSGSTGLP 205
Cdd:cd05919 86 VVTS-----------------------------------------------------------ADDIAYLLYSSGTTGPP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 206 KGVALPHR---TACVRFSHardPIFGnqIIPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVLM--YRFEEELFLRSLQd 279
Cdd:cd05919 107 KGVMHAHRdplLFADAMAR---EALG--LTPGDRVFSSAKMFFGYGLGNSLwFPLAVGASAVLNpgWPTAERVLATLAR- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 280 YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKP 359
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGP-ILDGIGATEVGHIFLSNRPGAWRL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 360 GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLK 439
Cdd:cd05919 260 GSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRAD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 440 SLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVASQVtTAKKLRGGV 516
Cdd:cd05919 338 DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERL-SAHKVPRRI 416
|
490 500
....*....|....*....|
gi 110555473 517 VFVDEVPKGLTGKLDARKIR 536
Cdd:cd05919 417 AFVDELPRTATGKLQRFKLR 436
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
194-531 |
9.61e-43 |
|
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: 155.54 E-value: 9.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMNSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVP-FHHGFgMFTTLGYLICGFRVVLMYRFEEEL 272
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQAL---LAQALVLAVLQAIDEGTVFLNSGPlFHIGT-LMFTLATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 273 FLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHeiASGGAPLSKEVGEAVAKRF-HLPGirqGYGLTETTSAILI 351
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLR--SSPAAPEWNDMATVDTSPWgRKPG---GYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 352 TPEGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEaTNALIDKDGWLHSGDIAYWDEDEH 431
Cdd:cd17636 155 AALGGGAIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPE-VNARRTRGGWHHTNDLGRREPDGS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 432 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKK 511
Cdd:cd17636 233 LSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKK 312
|
330 340
....*....|....*....|
gi 110555473 512 LRgGVVFVDEVPKGLTGKLD 531
Cdd:cd17636 313 PK-SVEFADALPRTAGGADD 331
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
46-530 |
1.99e-42 |
|
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: 157.99 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 46 HIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTV 125
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 126 VFVSkkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRDKTiALIMNSSGSTGLP 205
Cdd:cd05914 83 IFVS---------------------------------------------------------DEDDV-ALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 206 KGVALPHRT--ACVRFSHARDPifgnqIIPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELfLRSLQDYKI 282
Cdd:cd05914 105 KGVMLTYRNivSNVDGVKEVVL-----LGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAK-IIALAFAQV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 283 QSALLVPTLFSFF--AKSTLIDKYDLS-----------------------------NLHEIASGGAPLSKEVgEAVAKRF 331
Cdd:cd05914 179 TPTLGVPVPLVIEkiFKMDIIPKLTLKkfkfklakkinnrkirklafkkvheafggNIKEFVIGGAKINPDV-EEFLRTI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 332 HLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGktlgvNQRGELCVRGPMIMSGYVNNPEATNAL 411
Cdd:cd05914 258 GFPYT-IGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPA-----TGEGEIIVRGPNVMKGYYKNPEATAEA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 412 IDKDGWLHSGDIAYWDEDEHFFIVDRLKSLI-KYKGYQVAPAELESILLQHPNIFDAGVaGLPDDDAGEL----PAAVVV 486
Cdd:cd05914 332 FDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLV-VVQEKKLVALayidPDFLDV 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 110555473 487 LEHGKTMTEK----EIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKL 530
Cdd:cd05914 411 KALKQRNIIDaikwEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKI 458
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
52-513 |
3.39e-42 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 159.19 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPtVVFVSKK 131
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRP-VMLVTDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 GLQK--ILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHL------PPGFNeYDFVPESfdrdktIALIMNSSGSTG 203
Cdd:PLN02860 113 TCSSwyEELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLkqralgTTELD-YAWAPDD------AVLICFTSGTTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 204 LPKGVALPHRtACVRFSHARDPIFGNQiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQ 283
Cdd:PLN02860 186 RPKGVTISHS-ALIVQSLAKIAIVGYG--EDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 284 SALLVPTLFS---FFAKSTLIDKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTET--------------- 345
Cdd:PLN02860 263 SMITVPAMMAdliSLTRKSMTWKVFPS-VRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhdptle 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 TSAILITPEGDDKPGA--------VGKVVPFFEAKVVDLDTGKTlgvnqrGELCVRGPMIMSGYVNNPEATNALIDKDGW 417
Cdd:PLN02860 342 SPKQTLQTVNQTKSSSvhqpqgvcVGKPAPHVELKIGLDESSRV------GRILTRGPHVMLGYWGQNSETASVLSNDGW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 418 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKE 497
Cdd:PLN02860 416 LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNE 495
|
490
....*....|....*.
gi 110555473 498 IVDYVASQVTTAKKLR 513
Cdd:PLN02860 496 KENAKKNLTLSSETLR 511
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
21-533 |
3.86e-42 |
|
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: 157.67 E-value: 3.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 21 TAGEQLHKAMKRyalVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGV 100
Cdd:cd05923 2 TVFEMLRRAASR---APDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 101 AVAPANDIYNEREL--LNSMGISQPTVVFVSKKGLQKIlnvqkklpiIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGfne 178
Cdd:cd05923 79 VPALINPRLKAAELaeLIERGEMTAAVIAVDAQVMDAI---------FQSGVRVLALSDLVGLGEPESAGPLIEDPP--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 179 ydfvpesfDRDKTIALIMNSSGSTGLPKGVALPHRTACVR---FSHARDPIFGNQiipdTAILSVVPFHHGFGMFTTL-G 254
Cdd:cd05923 147 --------REPEQPAFVFYTSGTTGLPKGAVIPQRAAESRvlfMSTQAGLRHGRH----NVVLGLMPLYHVIGFFAVLvA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 255 YLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKrfHLP 334
Cdd:cd05923 215 ALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ--HLP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 335 GIRQG-YGLTETTSAiLITPegDDKPGAVGKVVPFFEAKVVDLDTG--KTLGVNQRGELCVR--GPMIMSGYVNNPEATN 409
Cdd:cd05923 293 GEKVNiYGTTEAMNS-LYMR--DARTGTEMRPGFFSEVRIVRIGGSpdEALANGEEGELIVAaaADAAFTGYLNQPEATA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 410 ALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 489
Cdd:cd05923 370 KKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 110555473 490 GkTMTEKEIVDY-VASQVTTAKKLRgGVVFVDEVPKGLTGKLDAR 533
Cdd:cd05923 449 G-TLSADELDQFcRASELADFKRPR-RYFFLDELPKNAMNKVLRR 491
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
52-536 |
4.44e-42 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 157.92 E-value: 4.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 131
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 GLQKILNVQKKLPI-IQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEYdfVPESFDrdkTIALIMNSSGSTGLPKGVAL 210
Cdd:PRK08008 119 FYPMYRQIQQEDATpLRHICLTRVALPADDGVSSFTQLKAQQPATLCYA--PPLSTD---DTAEILFTSGTTSRPKGVVI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 211 PHrtACVRFSHardpIFG---NQIIPDTAILSVVP-FHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYK----- 281
Cdd:PRK08008 194 TH--YNLRFAG----YYSawqCALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRatite 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 282 -----IQSALLVPTL----------FSFFakstlidkydlsnLHeiasggapLSKEVGEAVAKRFhlpGIR--QGYGLTE 344
Cdd:PRK08008 268 cipmmIRTLMVQPPSandrqhclreVMFY-------------LN--------LSDQEKDAFEERF---GVRllTSYGMTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 345 TTSAILITPEGDDK--PgAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG---PMIMSGYVNNPEATNALIDKDGWLH 419
Cdd:PRK08008 324 TIVGIIGDRPGDKRrwP-SIGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 420 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 499
Cdd:PRK08008 402 TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFF 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 110555473 500 DYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIR 536
Cdd:PRK08008 482 AFCEQNM--AKfKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
51-538 |
3.49e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 155.81 E-value: 3.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 130
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYER 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQ---SMYTFVTShlppGFNEYDFVPESFDrDktiALIMNSSGSTGLPKG 207
Cdd:PRK07798 109 EFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPgavDYEDALAA----GSPERDFGERSPD-D---LYLLYTGGTTGMPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 208 VALphRTACVRFSH--ARDPIFGNQI------------IPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL--MYRFEEE 271
Cdd:PRK07798 181 VMW--RQEDIFRVLlgGRDFATGEPIedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLlpDVRFDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 272 LFLRSLQDYKIQSALLVPTLFsffAKStLID------KYDLSNLHEIASGGAPLSKEVGEAVAKrfHLPG--IRQGYGLT 343
Cdd:PRK07798 259 EVWRTIEREKVNVITIVGDAM---ARP-LLDaleargPYDLSSLFAIASGGALFSPSVKEALLE--LLPNvvLTDSIGSS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 344 ETTSAILITPegddKPGAVGKVVPFFEA----KVVDLDTGKTL-GVNQRGELCVRGPmIMSGYVNNPEATNAL---IDKD 415
Cdd:PRK07798 333 ETGFGGSGTV----AKGAVHTGGPRFTIgprtVVLDEDGNPVEpGSGEIGWIARRGH-IPLGYYKDPEKTAETfptIDGV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 416 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 495
Cdd:PRK07798 408 RYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 110555473 496 KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREI 538
Cdd:PRK07798 488 AELRAHCRSSLAGYKVPR-AIWFVDEVQRSPAGKADYRWAKEQ 529
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
193-534 |
1.58e-40 |
|
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: 152.30 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFE 269
Cdd:cd05930 96 AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY---PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLpeeVRKD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 270 EELFLRSLQDYKIQSALLVPTLFSFFAKStlIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTsaI 349
Cdd:cd05930 173 PEALADLLAEEGITVLHLTPSLLRLLLQE--LELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEAT--V 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 350 LIT----PEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD-----GWL 418
Cdd:cd05930 249 DATyyrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNpfgpgERM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 419 H-SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKE 497
Cdd:cd05930 328 YrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEE 407
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 110555473 498 IVDYVASQ-----VTTAkklrggVVFVDEVPKGLTGKLDARK 534
Cdd:cd05930 408 LRAHLAERlpdymVPSA------FVVLDALPLTPNGKVDRKA 443
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
10-537 |
1.85e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 154.13 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 10 GPAPFYPLEDGTAGEQlhkamkryalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVV----CSEN- 84
Cdd:PRK06164 8 RADTLASLLDAHARAR-----------PDAVALIDE--DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVwlpnCIEWv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 85 SLQFFMPVLGALFIGVavapaNDIYNERELLNSMGISQPTVVFV--SKKGLQ--KILN-VQKK-LPIIQKIIIMDSKTDY 158
Cdd:PRK06164 75 VLFLACARLGATVIAV-----NTRYRSHEVAHILGRGRARWLVVwpGFKGIDfaAILAaVPPDaLPPLRAIAVVDDAADA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 159 QgfqSMYTFVTSHLPPGFNEYDFVP---ESFDRDKTIALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGnqIIPDT 235
Cdd:PRK06164 150 T---PAPAPGARVQLFALPDPAPPAaagERAADPDAGALLFTTSGTTSGPKLVLHRQATL-LRHARAIARAYG--YDPGA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 236 AILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKyDLSNLHE--IA 313
Cdd:PRK06164 224 VLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLfgFA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 314 SGGAPLSKEVGEAVAKRFHLPGIrqgYGLTETTSAILITPEGDD-----KPGAVgKVVPFFEAKVVDLDTGKTLGVNQRG 388
Cdd:PRK06164 303 SFAPALGELAALARARGVPLTGL---YGSSEVQALVALQPATDPvsvriEGGGR-PASPEARVRARDPQDGALLPDGESG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 389 ELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAG 468
Cdd:PRK06164 379 EIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQ 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110555473 469 VAGLpDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTG---KLDARKIRE 537
Cdd:PRK06164 459 VVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREAL-AGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
35-539 |
2.59e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 152.65 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 35 LVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENS-----LQFFMPVLGALFIgvavaPANDIY 109
Cdd:PRK09088 7 LQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSvwlvaLHFACARVGAIYV-----PLNWRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 110 NERELLNSMGISQPTVVfVSKKGLQkilnvqkklpiiqkiiimDSKTDYQGFQSMYTFVTSHLPpgfneyDFVPeSFDRD 189
Cdd:PRK09088 82 SASELDALLQDAEPRLL-LGDDAVA------------------AGRTDVEDLAAFIASADALEP------ADTP-SIPPE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 190 KtIALIMNSSGSTGLPKGVALPHRTAcvrfshardpifgNQIIPDTAILSVVPFHHGF----GMFTTLGyLICGFRVVLM 265
Cdd:PRK09088 136 R-VSLILFTSGTSGQPKGVMLSERNL-------------QQTAHNFGVLGRVDAHSSFlcdaPMFHIIG-LITSVRPVLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 YR--------FEEELFLRSLQD--YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAP-LSKEVGEAVAKrfhlp 334
Cdd:PRK09088 201 VGgsilvsngFEPKRTLGRLGDpaLGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPhAAEDILGWLDD----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 335 GIRQ--GYGLTETTSAILITPEG---DDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATN 409
Cdd:PRK09088 276 GIPMvdGFGMSEAGTVFGMSVDCdviRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 410 ALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 489
Cdd:PRK09088 355 RAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 110555473 490 GKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:PRK09088 435 GAPLDLERIRSHLSTRL--AKyKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
192-539 |
5.50e-40 |
|
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: 147.86 E-value: 5.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHR--TACVRFSHARDPIFGnqiiPDTAILSVVPFHHGfGMFTTLGYLICGFRVVLMYRfe 269
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAAnlLASAAGLHSRLGFGG----GDSWLLSLPLYHVG-GLAILVRSLLAGAELVLLER-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 270 EELFLRSLQDYKIQSALLVPT-LFSFFAKSTLIDkyDLSNLHEIASGGAPLSKEVGEAVAKRfHLPGIrQGYGLTETTSA 348
Cdd:cd17630 75 NQALAEDLAPPGVTHVSLVPTqLQRLLDSGQGPA--ALKSLRAVLLGGAPIPPELLERAADR-GIPLY-TTYGMTETASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 349 ILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATnaLIDKDGWLHSGDIAYWDE 428
Cdd:cd17630 151 VATKRPDGFGRGGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLRGQLVP--EFNEDGWFTTKDLGELHA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 429 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKtmTEKEIVDYVASQVTT 508
Cdd:cd17630 218 DGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA--DPAELRAWLKDKLAR 295
|
330 340 350
....*....|....*....|....*....|.
gi 110555473 509 AKKLRgGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:cd17630 296 FKLPK-RIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
195-537 |
1.53e-39 |
|
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: 151.08 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 195 IMNSSGSTGLPKGVALPHR------TACVRFSHARDP--IFGNqiIPDT-----AILSVV-PFHHGFGMFttlgylicgf 260
Cdd:cd05928 179 IYFTSGTTGSPKMAEHSHSslglglKVNGRYWLDLTAsdIMWN--TSDTgwiksAWSSLFePWIQGACVF---------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 261 rVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLiDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGY 340
Cdd:cd05928 247 -VHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDL-SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEGY 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 341 GLTETTsAILITPEGDD-KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVR-GPM----IMSGYVNNPEATNALIDK 414
Cdd:cd05928 324 GQTETG-LICANFKGMKiKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 415 DGWLhSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL-----EH 489
Cdd:cd05928 402 DFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLapqflSH 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 110555473 490 GKTMTEKEIVDYVASqVTTAKKLRGGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:cd05928 481 DPEQLTKELQQHVKS-VTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
198-531 |
2.28e-39 |
|
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: 146.01 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 198 SSGSTGLPKGVALPHRTACVRFSHARDpIFgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSL 277
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIESFVCNED-LF--NISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 278 QDYKIQSALLVPTLFSFFAKSTLIDkydlSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDD 357
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 358 KPGAVGKVVPFFEAKVVDLDTGKTlgvnqrGELCVRGPMIMSGYVNNPEatnalIDKDGWLHSGDIAYWDEDEHFFIVDR 437
Cdd:cd17633 161 PPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVRGGF-----SNPDGWMSVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 438 LKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVlehGKTMTEKEIVDYVASQVTTAKKLRgGVV 517
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPK-KII 305
|
330
....*....|....
gi 110555473 518 FVDEVPKGLTGKLD 531
Cdd:cd17633 306 FVDSLPYTSSGKIA 319
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
51-462 |
4.50e-39 |
|
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: 150.06 E-value: 4.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNT--NHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynereLLNSMGISqpTVVFV 128
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVP---------LYDTLGPE--AIEYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 129 SKKGLQKILNVQKKLPIIQKIIIMDsktdyQGFQsmytfvtshlppgfNEYDFVPESFDrdkTIALIMNSSGSTGLPKGV 208
Cdd:cd05927 75 LNHAEISIVFCDAGVKVYSLEEFEK-----LGKK--------------NKVPPPPPKPE---DLATICYTSGTTGNPKGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 209 ALPHR---TACVRFSHArdPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLmYRFEEELFLRSLQDYKIQSA 285
Cdd:cd05927 133 MLTHGnivSNVAGVFKI--LEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGF-YSGDIRLLLDDIKALKPTVF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 286 LLVPTLF--------------SFFAK---------------------STLIDKYDLS--------NLHEIASGGAPLSKE 322
Cdd:cd05927 210 PGVPRVLnriydkifnkvqakGPLKRklfnfalnyklaelrsgvvraSPFWDKLVFNkikqalggNVRLMLTGSAPLSPE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 323 VGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDL-DTGKT-LGVNQRGELCVRGPMIMSG 400
Cdd:cd05927 290 VLEFLRVALGCP-VLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVpEMNYDaKDPNPRGEVCIRGPNVFSG 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110555473 401 YVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHP 462
Cdd:cd05927 369 YYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSP 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
51-535 |
3.12e-38 |
|
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: 145.85 E-value: 3.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 130
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIADG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfdrdktiALIMNSSGSTGLPKGVAL 210
Cdd:cd05945 97 DDN-----------------------------------------------------------AYIIFTSGSTGRPKGVQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 211 PHRtACVRFSHARDPIFgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL----MYRFEEELFlRSLQDYKIQSAL 286
Cdd:cd05945 118 SHD-NLVSFTNWMLSDF--PLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPvprdATADPKQLF-RFLAEHGITVWV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 287 LVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT---SAILITPE--GDDKPGA 361
Cdd:cd05945 194 STPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATvavTYIEVTPEvlDGYDRLP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 362 VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA---LIDKDGWLHSGDIAYWDEDEHFFIVDRL 438
Cdd:cd05945 274 IGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRTGDLVRLEADGLLFYRGRL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 439 KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG----KTMTEKE-----IVDYVASQvtta 509
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGaeagLTKAIKAelaerLPPYMIPR---- 428
|
490 500
....*....|....*....|....*.
gi 110555473 510 kklrgGVVFVDEVPKGLTGKLDARKI 535
Cdd:cd05945 429 -----RFVYLDELPLNANGKIDRKAL 449
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
192-530 |
6.17e-38 |
|
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: 142.78 E-value: 6.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRTACVRFSHARdpIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLMYRFEE 270
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQ--KEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 271 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGA-PLSKEVgeAVAKRFHLPGIRQGYGLTETTSAI 349
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSrAIAADV--RFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 350 LItPEGDDKP--GAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWD 427
Cdd:cd17635 159 CL-PTDDDSIeiNAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 428 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV----LEHGKTMTEKEIVDYVA 503
Cdd:cd17635 236 EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVasaeLDENAIRALKHTIRREL 315
|
330 340
....*....|....*....|....*..
gi 110555473 504 SQVTTAKKlrggVVFVDEVPKGLTGKL 530
Cdd:cd17635 316 EPYARPST----IVIVTDIPRTQSGKV 338
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
51-464 |
1.14e-37 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 145.44 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMgiSQPTVvfvsk 130
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSL--NETEC----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 kglqkilnvqkklpiiqKIIIMDSKTDyqgfqsmytfvtshlppgfneydfvpesfdrdkTIALIMNSSGSTGLPKGVAL 210
Cdd:cd17639 79 -----------------SAIFTDGKPD---------------------------------DLACIMYTSGSTGNPKGVML 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 211 PHRTaCVRFSHARDPIFGNQIIPDTAILSVVPFHH-----------------GFGMFTTLGYLICG--------FRVVLM 265
Cdd:cd17639 109 THGN-LVAGIAGLGDRVPELLGPDDRYLAYLPLAHifelaaenvclyrggtiGYGSPRTLTDKSKRgckgdlteFKPTLM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 Y---------------------RFEEELFLRSLQdYKiQSALLVPTLFSF-----FAKstlIDKYDLSNLHEIASGGAPL 319
Cdd:cd17639 188 VgvpaiwdtirkgvlaklnpmgGLKRTLFWTAYQ-SK-LKALKEGPGTPLldelvFKK---VRAALGGRLRYMLSGGAPL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 320 SKEvgeavAKRF---HLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGK--TLGVNQRGELCVRG 394
Cdd:cd17639 263 SAD-----TQEFlniVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGysTDKPPPRGEILIRG 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110555473 395 PMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYK-GYQVAPAELESILLQHPNI 464
Cdd:cd17639 338 PNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV 408
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
52-469 |
1.59e-37 |
|
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: 143.17 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerellnsMGISQPTvvfvsk 130
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP-------------LDPAYPA------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLQKILNVqkklpIIQKIIIMDSktDYQGFQSMYTFVTSHLPPGFNEYD------FVPESFDRDKTIALIMNSSGSTGL 204
Cdd:TIGR01733 62 ERLAFILED-----AGARLLLTDS--ALASRLAGLVLPVILLDPLELAALddapapPPPDAPSGPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 205 PKGVALPHRTACVRFSHARDPIFGNqiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMY----RFEEELFLRSLQDY 280
Cdd:TIGR01733 135 PKGVVVTHRSLVNLLAWLARRYGLD---PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 281 KIQSALLVPTLFSFFAKStliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT---SAILITPEGDD 357
Cdd:TIGR01733 212 PVTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTvwsTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 358 KPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATN--------ALIDKDGWLHSGDIAYWD 427
Cdd:TIGR01733 289 RESPVpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 110555473 428 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGV 469
Cdd:TIGR01733 368 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
49-537 |
2.32e-37 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 145.03 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 49 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFV 128
Cdd:PRK05852 42 IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 129 SKKGL-QKILNVQKKLPIiqKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNeydfVPESFDRDKtiALIMNSSGSTGLPKG 207
Cdd:PRK05852 122 DADGPhDRAEPTTRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATS----TPEGLRPDD--AMIMFTGGTTGLPKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 208 VALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFEEELFLRSLQDYKIQS 284
Cdd:PRK05852 194 VPWTHANIA---SSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLparGRFSAHTFWDDIKAVGATW 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 285 ALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTSAILITP-EGDDK--- 358
Cdd:PRK05852 271 YTAVPTIHQILLEraATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVV-CAFGMTEATHQVTTTQiEGIGQten 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 359 ----PGAVGKVVPFfEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFI 434
Cdd:PRK05852 350 pvvsTGLVGRSTGA-QIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 435 VDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVtTAKKLRG 514
Cdd:PRK05852 427 RGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERL-AAFEIPA 505
|
490 500
....*....|....*....|...
gi 110555473 515 GVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK05852 506 SFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
51-536 |
3.04e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 144.38 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 130
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLQKILNVQKKLPIIqkiIIMDSKTDyqGFQSMYTFVTSHLPPgfneydfvpesFDRDKTIALIMNSSGSTGLPKGVA- 209
Cdd:PRK13390 105 ALDGLAAKVGADLPLR---LSFGGEID--GFGSFEAALAGAGPR-----------LTEQPCGAVMLYSSGTTGFPKGIQp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 210 -LPHRTAcvrfSHARDPI-------FGnqIIPDTAILSVVPFHHGF-----GMFTTLGYlicgfRVVLMYRFEEELFLRS 276
Cdd:PRK13390 169 dLPGRDV----DAPGDPIvaiarafYD--ISESDIYYSSAPIYHAAplrwcSMVHALGG-----TVVLAKRFDAQATLGH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 277 LQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETTSAILI-TP 353
Cdd:PRK13390 238 VERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG-PIVYEYYSSTEAHGMTFIdSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 354 EGDDKPGAVGKVVpFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDG--WLHSGDIAYWDEDEH 431
Cdd:PRK13390 317 DWLAHPGSVGRSV-LGDLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 432 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVASQVTT 508
Cdd:PRK13390 395 LYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDelaRELIDYTRSRIAH 474
|
490 500
....*....|....*....|....*...
gi 110555473 509 AKKLRgGVVFVDEVPKGLTGKLDARKIR 536
Cdd:PRK13390 475 YKAPR-SVEFVDELPRTPTGKLVKGLLR 501
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
195-538 |
1.26e-36 |
|
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: 144.00 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 195 IMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGnqIIPDTAILS------VVpfHHGFGMFttlGYLICGFRVVLmyrF 268
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYG--IKPGDVWWAasdvgwVV--GHSYIVY---GPLLHGATTVL---Y 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEE--------LFLRSLQDYKIQSALLVPTLFSFFAK----STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGI 336
Cdd:cd05967 305 EGKpvgtpdpgAFWRVIEKYQVNALFTAPTAIRAIRKedpdGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 337 RQgYGLTETTSAILITPEGDD----KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM---IMSGYVNNPEA-- 407
Cdd:cd05967 385 DH-WWQTETGWPITANPVGLEplpiKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLPLppgCLLTLWKNDERfk 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 408 TNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL 487
Cdd:cd05967 463 KLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVL 542
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 488 EHGKTMT----EKEIVDYVASQ---VTTAKKlrggVVFVDEVPKGLTGKLDARKIREI 538
Cdd:cd05967 543 KEGVKITaeelEKELVALVREQigpVAAFRL----VIFVKRLPKTRSGKILRRTLRKI 596
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
11-539 |
2.38e-36 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 142.04 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 11 PAPFYPLEDGTAGEQLHKAMKRYALVpGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIV-VCSENslQFF 89
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTK-GITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVIlQFDDN--EDF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 90 MPVLGALFIG------VAVAPANDIYNER--------ELLNsmgisQPtVVFVSKKGLQKILNVQKKLPI-IQKIIIMDS 154
Cdd:cd05906 78 IPAFWACVLAgfvpapLTVPPTYDEPNARlrklrhiwQLLG-----SP-VVLTDAELVAEFAGLETLSGLpGIRVLSIEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 155 KTDYQGfqsmytfvtshlppgfnEYDFVPESFDrdkTIALIMNSSGSTGLPKGVALPHRTACVRFSHArdpIFGNQIIPD 234
Cdd:cd05906 152 LLDTAA-----------------DHDLPQSRPD---DLALLMLTSGSTGFPKAVPLTHRNILARSAGK---IQHNGLTPQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 235 TAILSVVPFHH--GFGMFTTLG-YLICG-FRV----VLMyrfEEELFLRSLQDYKIQsallvptlFSF---FAKSTLID- 302
Cdd:cd05906 209 DVFLNWVPLDHvgGLVELHLRAvYLGCQqVHVpteeILA---DPLRWLDLIDRYRVT--------ITWapnFAFALLNDl 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 303 -------KYDLSNLHEIASGGAPLSKEVGEAVA---KRFHLPG--IRQGYGLTETTSAIL--ITPEGDDKPGA-----VG 363
Cdd:cd05906 278 leeiedgTWDLSSLRYLVNAGEAVVAKTIRRLLrllEPYGLPPdaIRPAFGMTETCSGVIysRSFPTYDHSQAlefvsLG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 364 KVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDeDEHFFIVDRLKSLIK 443
Cdd:cd05906 358 RPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTII 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 444 YKGYQVAPAELESILLQHPNI---FDAGVAGLPDDDAGE------LPAAVVVLEHGKTMteKEIVDYVASQVTTAKKLrg 514
Cdd:cd05906 436 VNGVNYYSHEIEAAVEEVPGVepsFTAAFAVRDPGAETEelaiffVPEYDLQDALSETL--RAIRSVVSREVGVSPAY-- 511
|
570 580
....*....|....*....|....*..
gi 110555473 515 gVVFV--DEVPKGLTGKLDARKIREIL 539
Cdd:cd05906 512 -LIPLpkEEIPKTSLGKIQRSKLKAAF 537
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
52-538 |
4.41e-36 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 142.08 E-value: 4.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENS-----LQFFMPVLGALfigvaVAPANDIYNERELLNSMGISQPTVV 126
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTpamyeMHFAVPMAGAV-----LNPINTRLDATSIAAILRHAKPKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 127 FVSKKG---LQKILNV------QKKLPIIQkIIIMDSKT-------DYQGFQSMYTFVTSHLPPGF---NEYDfvPESFD 187
Cdd:PLN03102 116 FVDRSFeplAREVLHLlssedsNLNLPVIF-IHEIDFPKrpsseelDYECLIQRGEPTPSLVARMFriqDEHD--PISLN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 188 RdktialimnSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR 267
Cdd:PLN03102 193 Y---------TSGTTADPKGVVISHRGA---YLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 268 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKR-FHlpgIRQGYGLTETT 346
Cdd:PLN03102 261 VTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLgFQ---VMHAYGLTEAT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 347 SAILIT---------PEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQR-----GELCVRGPMIMSGYVNNPEATNALI 412
Cdd:PLN03102 338 GPVLFCewqdewnrlPENQQMELKARQGVSILGLADVDVKNKETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 413 dKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKT 492
Cdd:PLN03102 418 -KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGET 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 110555473 493 MTEKEIVDYVASQVTTAKKLRGG---------VVFVDEVPKGLTGKLDARKIREI 538
Cdd:PLN03102 497 TKEDRVDKLVTRERDLIEYCRENlphfmcprkVVFLQELPKNGNGKILKPKLRDI 551
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
194-530 |
5.21e-35 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 136.88 E-value: 5.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMF-TTLGYLICGFRVVLMYR-FEEE 271
Cdd:cd05973 92 VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAV---DLRPEDSFWNAADPGWAYGLYyAITGPLALGHPTILLEGgFSVE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 272 LFLRSLQDYKIQSALLVPTLF-SFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETtSAIL 350
Cdd:cd05973 169 STWRVIERLGVTNLAGSPTAYrLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVP-IHDHYGQTEL-GMVL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 351 ITPEGDDKP---GAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCV---RGP-MIMSGYVNNPEATNAlidkDGWLHSGDI 423
Cdd:cd05973 247 ANHHALEHPvhaGSAGRAMPGWRVAVLDDD-GDELGPGEPGRLAIdiaNSPlMWFRGYQLPDTPAID----GGYYLTGDT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 424 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT---EKEIVD 500
Cdd:cd05973 322 VEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQL 401
|
330 340 350
....*....|....*....|....*....|
gi 110555473 501 YVASQVTTAKKLRgGVVFVDEVPKGLTGKL 530
Cdd:cd05973 402 HVKKRLSAHAYPR-TIHFVDELPKTPSGKI 430
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
31-537 |
5.54e-35 |
|
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: 138.53 E-value: 5.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 31 KRYALVPGTIAFT----DAHIEVDITYAEYFEMSVRLAEAMKRYGLnTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAN 106
Cdd:cd05931 1 RRAAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 107 DIYNERE---LLNSMGISQPTVVFVSKK---GLQKILNVQKKLPIIQkIIIMDSKTDyqgfqsmytfvtshLPPGfneyD 180
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLTTAAalaAVRAFAASRPAAGTPR-LLVVDLLPD--------------TSAA----D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 181 FVPESFDRDkTIALIMNSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGY-LICG 259
Cdd:cd05931 141 WPPPSPDPD-DIAYLQYTSGSTGTPKGVVVTHRNL---LANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTpLYSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 260 FRVVLM---------YRFeeelfLRSLQDYKIQ-SAllVPTlfsfFA--------KSTLIDKYDLSNLHEIASGGAPLSK 321
Cdd:cd05931 217 GPSVLMspaaflrrpLRW-----LRLISRYRATiSA--APN----FAydlcvrrvRDEDLEGLDLSSWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 322 EVGEAVAKRF---------HLPGirqgYGLTETTSAILITPEGD---------------------DKPGAV-----GKVV 366
Cdd:cd05931 286 ATLRRFAEAFapfgfrpeaFRPS----YGLAEATLFVSGGPPGTgpvvlrvdrdalagravavaaDDPAARelvscGRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 367 PFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNAL------IDKDGWLHSGDIAYWDEDEhFFIVDRLKS 440
Cdd:cd05931 362 PDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLHDGE-LYITGRLKD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 441 LIKYKGYQVAPAELESILLQHPNIFDAGVA---GLPDDDAGELpaaVVVLEHGKTMTE---KEIVDYVASQVTTAKKLR- 513
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPALRPGCVaafSVPDDGEERL---VVVAEVERGADPadlAAIAAAIRAAVAREHGVAp 517
|
570 580
....*....|....*....|....*.
gi 110555473 514 GGVVFV--DEVPKGLTGKLDARKIRE 537
Cdd:cd05931 518 ADVVLVrpGSIPRTSSGKIQRRACRA 543
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-533 |
1.67e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 130.97 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQII-----------PDTAILSVVPFHHGFGMFTTLGYLICGFRV 262
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPsedahkaaaaaAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 263 VLM-YRFEEELFLRSLQDYKIQSALLVPTLFsffAKStLIDK------YDLSNLHEIASGGAPLSKEVGEAVAKRFHLPG 335
Cdd:cd05924 87 VLPdDRFDPEEVWRTIEKHKVTSMTIVGDAM---ARP-LIDAlrdagpYDLSSLFAISSGGALLSPEVKQGLLELVPNIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 336 IRQGYGLTETTS-AILITPEGDDKPGAVGKVVPffEAKVVDLDTGKTL-GVNQRGELCVRGpMIMSGYVNNPEAT-NALI 412
Cdd:cd05924 163 LVDAFGSSETGFtGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPpGSGGVGWIARRG-HIPLGYYGDEAKTaETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 413 DKDG--WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG 490
Cdd:cd05924 240 EVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 110555473 491 KTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDAR 533
Cdd:cd05924 320 AGVDLEELREHCRTRI-ARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
30-537 |
2.33e-33 |
|
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: 133.33 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 30 MKRYALVPGTIAFTDahieVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENslqffMPVLGALFIGVAVAPA---- 105
Cdd:cd05915 8 FGRKEVVSRLHTGEV----HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFN-----HFRHLEAYFAVPGMGAvlht 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 106 -NDIYNERELLNSMGISQPTVVFVSKKGLQKilnVQKKLPIIQKIiiMDSKTDYQGFQSMYTFVTSHLPpgfneyDFVP- 183
Cdd:cd05915 79 aNPRLSPKEIAYILNHAEDKVLLFDPNLLPL---VEAIRGELKTV--QHFVVMDEKAPEGYLAYEEALG------EEADp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 184 ESFDRDKTIALIMnSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQII--PDTAILSVVPFHHGFG-----MFTTLGYL 256
Cdd:cd05915 148 VRVPERAACGMAY-TTGTTGLPKGVVYSHRAL---VLHSLAASLVDGTAlsEKDVVLPVVPMFHVNAwclpyAATLVGAK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 257 ICGFRVVLmyrfEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPlSKEVGEAVaKRFHLPGI 336
Cdd:cd05915 224 QVLPGPRL----DPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSA-APRSLIAR-FERMGVEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 337 RQGYGLTET---TSAILITPEGDDKP-------GAVGKVVPFFEAkvVDLDTGKTLGVNQRGE----LCVRGPMIMSGYV 402
Cdd:cd05915 298 RQGYGLTETspvVVQNFVKSHLESLSeeekltlKAKTGLPIPLVR--LRVADEEGRPVPKDGKalgeVQLKGPWITGGYY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 403 NNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPA 482
Cdd:cd05915 376 GNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPL 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 110555473 483 AVVVLEHGKTmTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:cd05915 456 AVVVPRGEKP-TPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
28-544 |
4.23e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 132.21 E-value: 4.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 28 KAMKRYA-LVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMkRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAN 106
Cdd:PRK07638 5 KEYKKHAsLQPNKIAIKEN--DRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 107 DIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLpiiqkIIIMDSKTDYQGFQSMYTFVTS--HLP--PGFneydfv 182
Cdd:PRK07638 82 IKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRV-----IEIDEWKRMIEKYLPTYAPIENvqNAPfyMGF------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 183 pesfdrdktialimnSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAIL---SVVPFHHGFGMFTTLgYLicG 259
Cdd:PRK07638 151 ---------------TSGSTGKPKAFLRAQQSWLHSFDCNVHDF---HMKREDSVLiagTLVHSLFLYGAISTL-YV--G 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 260 FRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKstlIDKYdLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQG 339
Cdd:PRK07638 210 QTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYK---ENRV-IENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 340 YGLTETTSAILITPEGDD-KPGAVGKvvPFFEAKV-VDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALiDKDGW 417
Cdd:PRK07638 286 YGASELSFVTALVDEESErRPNSVGR--PFHNVQVrICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAREL-NADGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 418 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVvleHGKTmTEKE 497
Cdd:PRK07638 363 MTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TKQQ 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 110555473 498 IVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLD---ARKIREILIKAKK 544
Cdd:PRK07638 439 LKSFCLQRLSSFKIPK-EWHFVDEIPYTNSGKIArmeAKSWIENQEKIYE 487
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
52-537 |
4.54e-33 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 132.95 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 131
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 GLQKILNVQKKLPIIQKIIIMDSKtdyqgfqsmytfvtSHLP----PGFNEY---------DFVPESFDRDkTIALIMNS 198
Cdd:PRK06018 121 FVPILEKIADKLPSVERYVVLTDA--------------AHMPqttlKNAVAYeewiaeadgDFAWKTFDEN-TAAGMCYT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 SGSTGLPKGVALPHRTacvRFSHArdpIFGNQiiPDT-------AILSVVPFHHGFGMFTTLGYLICGFRVVL------- 264
Cdd:PRK06018 186 SGTTGDPKGVLYSHRS---NVLHA---LMANN--GDAlgtsaadTMLPVVPLFHANSWGIAFSAPSMGTKLVMpgakldg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 265 --MYrfeeELflrsLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRFHLPGI--RQGY 340
Cdd:PRK06018 258 asVY----EL----LDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP----RSMIKAFEDMGVevRHAW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 341 GLTET----TSAILiTPEGDDKPGAVGKVV-------PF-FEAKVVDlDTGKTLGVNQR--GELCVRGPMIMSGYVnnpE 406
Cdd:PRK06018 326 GMTEMsplgTLAAL-KPPFSKLPGDARLDVlqkqgypPFgVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYY---R 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 407 ATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 486
Cdd:PRK06018 401 VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQ 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 110555473 487 LEHGKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK06018 481 LKPGETATREEILKYMDGKI--AKwWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
51-471 |
1.88e-32 |
|
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: 129.79 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSk 130
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 kglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRDKTIALIMNSSGSTGLPKGVAL 210
Cdd:cd17640 85 --------------------------------------------------------NDSDDLATIIYTSGTTGNPKGVML 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 211 PHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGfrVVLMY---RFeeelFLRSLQDYKIQSALL 287
Cdd:cd17640 109 THANLLHQIRSLSDIV---PPQPGDRFLSILPIWHSYERSAEYFIFACG--CSQAYtsiRT----LKDDLKRVKPHYIVS 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 288 VPTLF-------------SFFAKSTLIDKYDLSNLHEIA-SGGAPLSKEVgeavAKRFHLPGIR--QGYGLTETTSAILI 351
Cdd:cd17640 180 VPRLWeslysgiqkqvskSSPIKQFLFLFFLSGGIFKFGiSGGGALPPHV----DTFFEAIGIEvlNGYGLTETSPVVSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 352 TPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEH 431
Cdd:cd17640 256 RRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGE 335
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 110555473 432 FFIVDRLKSLIKYK-GYQVAPAELESILLQHPNIFDAGVAG 471
Cdd:cd17640 336 LVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
49-487 |
4.86e-32 |
|
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: 129.51 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 49 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLG---ALFIGVAVAPANDIYNERELLNSmgiSQPTV 125
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAiwmAGHISVPLYPTLNPDTIRYVLEH---SESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 126 VFVSKkgLQKILNVQKKLP--IIQKII----IMDSKTDYQGFQSMYTFVTSHLPPGfneydfvpesfdrDKTIALIMNSS 199
Cdd:cd05932 82 LFVGK--LDDWKAMAPGVPegLISISLpppsAANCQYQWDDLIAQHPPLEERPTRF-------------PEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 200 GSTGLPKGVAlpHRTACVRFSHARDpIFGNQIIPDTAILSVVPFHHGFG-MFTTLGYLICGFRVVlmyrFEEEL--FLRS 276
Cdd:cd05932 147 GTTGQPKGVM--LTFGSFAWAAQAG-IEHIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVA----FAESLdtFVED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 277 LQDYKIQSALLVPTLFSFFAKStLIDKYDLSNLHEI--------------------------ASGGAPLSkevgEAVAKR 330
Cdd:cd05932 220 VQRARPTLFFSVPRLWTKFQQG-VQDKIPQQKLNLLlkipvvnslvkrkvlkglgldqcrlaGCGSAPVP----PALLEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 331 FHLPG--IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEAT 408
Cdd:cd05932 295 YRSLGlnILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEAT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 409 NALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNIFDAGV--AGLPDddagelPAAVV 485
Cdd:cd05932 364 AEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVigSGLPA------PLALV 437
|
..
gi 110555473 486 VL 487
Cdd:cd05932 438 VL 439
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
51-471 |
1.05e-31 |
|
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: 129.08 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG-VAVAPANDIYNER--ELLNSMGisqPTVVF 127
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGaLSLGIYQDSMAEEvaYLLNYTG---ARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 128 VS-KKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRD------KTIALIMNSSG 200
Cdd:cd17641 89 AEdEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGLYEREvaagkgEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 201 STGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHH-GFGMFTTLGYLICGF------------------- 260
Cdd:cd17641 169 TTGKPKLAMLSHGNF---LGHCAAYLAADPLGPGDEYVSVLPLPWiGEQMYSVGQALVCGFivnfpeepetmmedlreig 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 261 -RVVL--------------------------MYRFEEELFLRSL-QDYKIQSALLVPTLFSFFAKSTLI----DKYDLSN 308
Cdd:cd17641 246 pTFVLlpprvwegiaadvrarmmdatpfkrfMFELGMKLGLRALdRGKRGRPVSLWLRLASWLADALLFrplrDRLGFSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 309 LHEIASGGAPLskevGEAVAKRFHLPGI--RQGYGLTETTSAILITPEGDDKPGAVGkvVPFFEAKVvdldtgktlGVNQ 386
Cdd:cd17641 326 LRSAATGGAAL----GPDTFRFFHAIGVplKQLYGQTELAGAYTVHRDGDVDPDTVG--VPFPGTEV---------RIDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 387 RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK-YKGYQVAPAELESILLQHPNIF 465
Cdd:cd17641 391 VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPYIA 470
|
....*.
gi 110555473 466 DAGVAG 471
Cdd:cd17641 471 EAVVLG 476
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
51-455 |
3.26e-31 |
|
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: 127.86 E-value: 3.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG---VAVAPANDIYNERELLNSmgiSQPTVVF 127
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGgiaVGIYTTNSPEACQYVAET---SEANILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 128 V-SKKGLQKILNVQKKLPIIQKIII--------MDSKTDYQGFQSMYTFVTSHlppgfnEYDFVPESFDRDKTIALIMNS 198
Cdd:cd05933 86 VeNQKQLQKILQIQDKLPHLKAIIQykeplkekEPNLYSWDEFMELGRSIPDE------QLDAIISSQKPNQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 sGSTGLPKGVALPHRT------ACVRFSHARDPIFGNQIIpdtaiLSVVPFHH----GFGMFTTL--------------- 253
Cdd:cd05933 160 -GTTGMPKGVMLSHDNitwtakAASQHMDLRPATVGQESV-----VSYLPLSHiaaqILDIWLPIkvggqvyfaqpdalk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 254 GYLICGFRVV----------LMYRFEEELFLRSLQDYKIQSALLV-------------------PTLFSFFAKSTLIDK- 303
Cdd:cd05933 234 GTLVKTLREVrptafmgvprVWEKIQEKMKAVGAKSGTLKRKIASwakgvgletnlklmggespSPLFYRLAKKLVFKKv 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 304 ---YDLSNLHEIASGGAPLSKEVgeavaKRFHLP---GIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLD 377
Cdd:cd05933 314 rkaLGLDRCQKFFTGAAPISRET-----LEFFLSlniPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPD 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110555473 378 TgktlgvNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQ-VAPAELE 455
Cdd:cd05933 389 A------DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIE 461
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
34-533 |
6.64e-31 |
|
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: 125.92 E-value: 6.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 34 ALVPGTIAFTDAHIEVdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERE 113
Cdd:cd17651 6 ARTPDAPALVAEGRRL--TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 114 LLNSMGISQPTVVfVSKKGLQKILNVQKKLPIIQKIIIMDSKTDyqgfqsmytfvTSHLPPgfneydfvpesFDRDKTiA 193
Cdd:cd17651 84 LAFMLADAGPVLV-LTHPALAGELAVELVAVTLLDQPGAAAGAD-----------AEPDPA-----------LDADDL-A 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGnqIIPDTAILSVVPFhhGFGMFT--TLGYLICGFRVVLM---YRF 268
Cdd:cd17651 140 YVIYTSGSTGRPKGVVMPHRSL-ANLVAWQARASS--LGPGARTLQFAGL--GFDVSVqeIFSTLCAGATLVLPpeeVRT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSkeVGEAVAKRF-HLPGIR--QGYGLTET 345
Cdd:cd17651 215 DPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLV--LTEDLREFCaGLPGLRlhNHYGPTET 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 TSAILITPEGD----DKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWL--- 418
Cdd:cd17651 293 HVVTALSLPGDpaawPAPPPIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpga 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 419 ---HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 495
Cdd:cd17651 372 rmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDA 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 110555473 496 KEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDAR 533
Cdd:cd17651 452 AELRAALATHL-PEYMVPSAFVLLDALPLTPNGKLDRR 488
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
267-537 |
7.28e-31 |
|
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: 124.60 E-value: 7.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 267 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIdKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETT 346
Cdd:cd05974 162 RFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLA-SFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 347 SAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTlgvnQRGELCV-----RGPMIMSGYVNNPEATNALIdKDGWLHSG 421
Cdd:cd05974 239 ALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPA----TEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 422 DIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG---KTMTEKEI 498
Cdd:cd05974 314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyepSPETALEI 393
|
250 260 270
....*....|....*....|....*....|....*....
gi 110555473 499 VDYVASQVTTAKKLRgGVVFVdEVPKGLTGKLDARKIRE 537
Cdd:cd05974 394 FRFSRERLAPYKRIR-RLEFA-ELPKTISGKIRRVELRR 430
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
51-537 |
1.49e-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: 124.75 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 130
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KglqkilnVQKKLPIIQKIIIMDSKTdyqgfqsMYTFVTSHLPPGFNEYDfvpesfdrdktIALIMNSSGSTGLPKGVAL 210
Cdd:cd17655 103 H-------LQPPIAFIGLIDLLDEDT-------IYHEESENLEPVSKSDD-----------LAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 211 PHRtACVRFSHArdpiFGNQIIPDTA--ILSVVPFHHGFGMFTTLGYLICGFRVVLmYRFEE----ELFLRSLQDYKIQS 284
Cdd:cd17655 158 EHR-GVVNLVEW----ANKVIYQGEHlrVALFASISFDASVTEIFASLLSGNTLYI-VRKETvldgQALTQYIRQNRITI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 285 ALLVPTLFSFFAKstlIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHL-PGIRQGYGLTETT---SAILITPEGDDKPG 360
Cdd:cd17655 232 IDLTPAHLKLLDA---ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTvdaSIYQYEPETDQQVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 361 A-VGKvvPFFEAKVVDLDT-GKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWL------HSGDIAYWDEDEHF 432
Cdd:cd17655 309 VpIGK--PLGNTRIYILDQyGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 433 FIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVlehgktmTEKEIvdyVASQVTT--AK 510
Cdd:cd17655 387 EFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-------SEKEL---PVAQLREflAR 456
|
490 500 510
....*....|....*....|....*....|..
gi 110555473 511 KLRGGVV---FV--DEVPKGLTGKLDARKIRE 537
Cdd:cd17655 457 ELPDYMIpsyFIklDEIPLTPNGKVDRKALPE 488
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
51-537 |
3.25e-30 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 124.49 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVApandiynereLLNSMGISQPTVVFVSK 130
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL----------LLNTSFAGPALAEVVTR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLQKILNVQKKLPIIQKII--------IMDSkTDYQGFQSMYTFVTSHLPpgfneyDFVPESFDRDKTIALimnSSGST 202
Cdd:PRK13382 139 EGVDTVIYDEEFSATVDRALadcpqatrIVAW-TDEDHDLTVEVLIAAHAG------QRPEPTGRKGRVILL---TSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 203 GLPKGvalphrtacvrfshARDPIFGNqIIPDTAILSVVPFHHG------FGMFTTLGY--------LICgfRVVLMYRF 268
Cdd:PRK13382 209 GTPKG--------------ARRSGPGG-IGTLKAILDRTPWRAEeptvivAPMFHAWGFsqlvlaasLAC--TIVTRRRF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETT 346
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMFDRImdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG-DVIYNNYNATEAG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 347 SAILITPEGDDK-PGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVnnPEATNALIDkdGWLHSGDIAY 425
Cdd:PRK13382 351 MIATATPADLRAaPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGYT--SGSTKDFHD--GFMASGDVGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 426 WDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQ 505
Cdd:PRK13382 426 LDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDN 505
|
490 500 510
....*....|....*....|....*....|..
gi 110555473 506 VTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK13382 506 LANYKVPR-DIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
34-533 |
1.49e-29 |
|
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: 121.54 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 34 ALVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNE-- 111
Cdd:cd12117 8 ARTPDAVAVVYG--DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAer 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 112 -RELLNSmgiSQPTVVfVSKKGLQKILNVQKKLPIIQkiiimdsktdyqgfQSMYTFVTSHLPPGFNeydfvPESfdrdk 190
Cdd:cd12117 86 lAFMLAD---AGAKVL-LTDRSLAGRAGGLEVAVVID--------------EALDAGPAGNPAVPVS-----PDD----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 191 tIALIMNSSGSTGLPKGVALPHRtACVRFshARDPIFGnQIIPDTAILSVVPfhHGF--GMFTTLGYLICGFRVVLMyrf 268
Cdd:cd12117 138 -LAYVMYTSGSTGRPKGVAVTHR-GVVRL--VKNTNYV-TLGPDDRVLQTSP--LAFdaSTFEIWGALLNGARLVLA--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEELFL--RSLQDY----KIQSALLVPTLFSFFAKStliDKYDLSNLHEIASGGAPLS-KEVGEAVAkrfHLPGIR--QG 339
Cdd:cd12117 208 PKGTLLdpDALGALiaeeGVTVLWLTAALFNQLADE---DPECFAGLRELLTGGEVVSpPHVRRVLA---ACPGLRlvNG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 340 YGLTETT--SAILITPEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 415
Cdd:cd12117 282 YGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVAD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 416 GWL------HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 489
Cdd:cd12117 361 PFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 110555473 490 GktmtekeiVDYVASQVTTAKKLRGG-----VVFVDEVPKGLTGKLDAR 533
Cdd:cd12117 441 A--------LDAAELRAFLRERLPAYmvpaaFVVLDELPLTANGKVDRR 481
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
180-537 |
1.87e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 122.10 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 180 DFVPESFDRDKTIALIMnSSGSTGLPKGVALPHRTACV-------RFSHARDpifgnqiipDTAILSVVPFHHGFGMFTT 252
Cdd:PRK07867 143 EPPFRVADPDDLFMLIF-TSGTSGDPKAVRCTHRKVASagvmlaqRFGLGPD---------DVCYVSMPLFHSNAVMAGW 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 253 LGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSF-FAKSTLIDkyDLSNLHEIASG--GAPLSKevgEAVAK 329
Cdd:PRK07867 213 AVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYvLATPERPD--DADNPLRIVYGneGAPGDI---ARFAR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 330 RFhlpGIR--QGYGLTETtsAILITPEGDDKPGAVGKVVPffEAKVVDLDTGK------------TLGVNQRGELC-VRG 394
Cdd:PRK07867 288 RF---GCVvvDGFGSTEG--GVAITRTPDTPPGALGPLPP--GVAIVDPDTGTecppaedadgrlLNADEAIGELVnTAG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 395 PMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPD 474
Cdd:PRK07867 361 PGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPD 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110555473 475 DDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVV-FVDEVPKGLTGKLDARKIRE 537
Cdd:PRK07867 440 PVVGDQVMAALVLAPGAKFDPDAFAEFLAAQPDLGPKQWPSYVrVCAELPRTATFKVLKRQLSA 503
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
51-540 |
2.36e-29 |
|
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: 122.21 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFV-- 128
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITad 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 129 --SKKGlqKILNVQKKL-------PIIQKIIIM------DSKTDYqGFQSMYTFVTSHlPPGFneydfvpESFDRDKTIA 193
Cdd:cd05968 172 gfTRRG--REVNLKEEAdkacaqcPTVEKVVVVrhlgndFTPAKG-RDLSYDEEKETA-GDGA-------ERTESEDPLM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMnSSGSTGLPKGVAlpHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM-----YRF 268
Cdd:cd05968 241 IIY-TSGTTGKPKGTV--HVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYdgapdHPK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEELFlRSLQDYKIQSALLVPTLF-SFFAKST-LIDKYDLSNLHEIASGGAPLSKE----VGEAVAKRfHLPGIRQGYGl 342
Cdd:cd05968 318 ADRLW-RMVEDHEITHLGLSPTLIrALKPRGDaPVNAHDLSSLRVLGSTGEPWNPEpwnwLFETVGKG-RNPIINYSGG- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 343 TETTSAIL----ITPEgddKPGAVGKVVPFFEAKVVDlDTGKTLgVNQRGELCVRGPMI-MS-GYVNNPEA-TNALIDK- 414
Cdd:cd05968 395 TEISGGILgnvlIKPI---KPSSFNGPVPGMKADVLD-ESGKPA-RPEVGELVLLAPWPgMTrGFWRDEDRyLETYWSRf 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 415 -DGWLHsGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTM 493
Cdd:cd05968 470 dNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTP 548
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 110555473 494 TE---KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILI 540
Cdd:cd05968 549 TEalaEELMERVADELGKPLSPE-RILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
30-548 |
2.54e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 121.88 E-value: 2.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 30 MKRYALVPGTIAfTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY 109
Cdd:PLN02479 26 LERAAVVHPTRK-SVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 110 NERELLNSMGISQPTVVFVSKK------GLQKILNVQK----KLPIIqkIIIMDSKTDYQGFQSM-------YTfvtSHL 172
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEfftlaeEALKILAEKKkssfKPPLL--IVIGDPTCDPKSLQYAlgkgaieYE---KFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 173 PPGFNEYDFVPESfDRDKTIALIMnSSGSTGLPKGVALPHRTACVrFSHARDPIFGnqiIPDTAI-LSVVPFHHGFGM-F 250
Cdd:PLN02479 180 ETGDPEFAWKPPA-DEWQSIALGY-TSGTTASPKGVVLHHRGAYL-MALSNALIWG---MNEGAVyLWTLPMFHCNGWcF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 251 TTLGYLICGFRVVLMYRFEEELFlRSLQDYKIQSALLVPTLFSFFAKSTLIDKY-DLSNLHEIASGGAPLSKEVGEAVAK 329
Cdd:PLN02479 254 TWTLAALCGTNICLRQVTAKAIY-SAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHVMTAGAAPPPSVLFAMSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 330 RfhlpGIR--QGYGLTET---TSAILITPEGDDKPGAVG---------KVVPFFEAKVVDLDTGKTLGVNQR--GELCVR 393
Cdd:PLN02479 333 K----GFRvtHTYGLSETygpSTVCAWKPEWDSLPPEEQarlnarqgvRYIGLEGLDVVDTKTMKPVPADGKtmGEIVMR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 394 GPMIMSGYVNNPEAtNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLP 473
Cdd:PLN02479 409 GNMVMKGYLKNPKA-NEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARP 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 474 DDDAGELPAAVVVLEHG-----KTMTEKEIVDYVASQVtTAKKLRGGVVFvDEVPKGLTGKLDARKIREiliKAKKGGKI 548
Cdd:PLN02479 488 DERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERL-PAYWVPKSVVF-GPLPKTATGKIQKHVLRA---KAKEMGPV 562
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
30-550 |
2.24e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 118.90 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 30 MKRYALV-PGTIAFTdaHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSlqffMPVLGALFiGVAVAPAndi 108
Cdd:PRK08162 24 LERAAEVyPDRPAVI--HGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNI----PAMVEAHF-GVPMAGA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 109 ynereLLNSMGI--SQPTVVFVSKKGLQKILNV--------QKKLPII--QKIIIMD------------SKTDYQGFqsm 164
Cdd:PRK08162 94 -----VLNTLNTrlDAASIAFMLRHGEAKVLIVdtefaevaREALALLpgPKPLVIDvddpeypggrfiGALDYEAF--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 165 ytfvtshLPPGFNEYDFVPESfDRDKTIALimN-SSGSTGLPKGVALPHRTAcvrFSHArdpiFGNQI---IPDTAI-LS 239
Cdd:PRK08162 166 -------LASGDPDFAWTLPA-DEWDAIAL--NyTSGTTGNPKGVVYHHRGA---YLNA----LSNILawgMPKHPVyLW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 240 VVP-FH-----HGFGMFTTLGYLICgfrvvlMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIA 313
Cdd:PRK08162 229 TLPmFHcngwcFPWTVAARAGTNVC------LRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 314 SGGAPLSKEVGEAVAKRfhlpGIR--QGYGLTET---TSAILITPEGDDKPG---AVGKV---VPFF---EAKVVDLDT- 378
Cdd:PRK08162 303 VAGAAPPAAVIAKMEEI----GFDltHVYGLTETygpATVCAWQPEWDALPLderAQLKArqgVRYPlqeGVTVLDPDTm 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 379 ------GKTLGvnqrgELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPA 452
Cdd:PRK08162 379 qpvpadGETIG-----EIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 453 ELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFvDEVPKGLTGKLDA 532
Cdd:PRK08162 453 EVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPK-AVVF-GELPKTSTGKIQK 530
|
570
....*....|....*...
gi 110555473 533 RKIREiliKAKKGGKIAV 550
Cdd:PRK08162 531 FVLRE---QAKSLKAIDL 545
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
199-539 |
5.15e-28 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 117.26 E-value: 5.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 SGSTGLPKGVALPHRTACVRF-SHARdpIFGnqIIPDTAILSvvpF-HHGFG-----MFTTlgyLICGFRVVLMYrfEEE 271
Cdd:cd05918 115 SGSTGKPKGVVIEHRALSTSAlAHGR--ALG--LTSESRVLQ---FaSYTFDvsileIFTT---LAAGGCLCIPS--EED 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 272 L---FLRSLQDYKIQSALLVPTLFSffakstLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLpgiRQGYGLTETT-S 347
Cdd:cd05918 183 RlndLAGFINRLRVTWAFLTPSVAR------LLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRL---INAYGPAECTiA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 348 AILITPEGDDKPGAVGKVVPFFeAKVVDLDT-GKTLGVNQRGELCVRGPMIMSGYVNNPEATN-ALIDKDGWLH------ 419
Cdd:cd05918 254 ATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAaAFIEDPAWLKqegsgr 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 420 ------SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQH-PNIFDAGVAGLPDDDAGELPAAVVVLEHGKT 492
Cdd:cd05918 333 grrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGS 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110555473 493 MTEK--------EIVDYVASQVTTAK-KLRGGV---------VFVDEVPKGLTGKLDARKIREIL 539
Cdd:cd05918 413 SSGSgdgdslflEPSDEFRALVAELRsKLRQRLpsymvpsvfLPLSHLPLTASGKIDRRALRELA 477
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
192-486 |
7.23e-27 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 115.20 E-value: 7.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVvlmyRFEEE 271
Cdd:PLN02736 223 VATICYTSGTTGTPKGVVLTHGNLIANVAGSSLST---KFYPSDVHISYLPLAHIYERVNQIVMLHYGVAV----GFYQG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 272 LFLRSLQDYkiqsALLVPTLFS-------------------------------FFAK----------STLIDKYDLSNLH 310
Cdd:PLN02736 296 DNLKLMDDL----AALRPTIFCsvprlynriydgitnavkesgglkerlfnaaYNAKkqalengknpSPMWDRLVFNKIK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 311 E--------IASGGAPLSKEVGEAVakRFHLPG-IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKT 381
Cdd:PLN02736 372 AklggrvrfMSSGASPLSPDVMEFL--RICFGGrVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNY 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 382 LGVNQ---RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESI 457
Cdd:PLN02736 450 TSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENV 529
|
330 340
....*....|....*....|....*....
gi 110555473 458 LLQHPNIFDAGVAGlpDDDAGELPAAVVV 486
Cdd:PLN02736 530 YAKCKFVAQCFVYG--DSLNSSLVAVVVV 556
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
37-537 |
1.04e-26 |
|
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: 112.79 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerelln 116
Cdd:cd17653 11 PDAVAVESL--GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 117 smgisqptvvfvskkglqkilnVQKKLPIIQKIIIMDsktdyqgfQSMYTFVtshLPPgfneydfvpesfDRDKTIALIM 196
Cdd:cd17653 77 ----------------------LDAKLPSARIQAILR--------TSGATLL---LTT------------DSPDDLAYII 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 197 NSSGSTGLPKGVALPHR--TACVRFSHARdpiFGNQiiPDTAILSV--VPFHHGFG-MFTTLGYlicGFRVVLmyRFEEE 271
Cdd:cd17653 112 FTSGSTGIPKGVMVPHRgvLNYVSQPPAR---LDVG--PGSRVAQVlsIAFDACIGeIFSTLCN---GGTLVL--ADPSD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 272 LFLRSLQdyKIQSALLVPTLFSffakstLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRfhlPGIRQGYGLTETTSAILI 351
Cdd:cd17653 182 PFAHVAR--TVDALMSTPSILS------TLSPQDFPNLKTIFLGGEAVPPSLLDRWSPG---RRLYNAYGPTECTISSTM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 352 TPEGDDKPGAVGKVVPffEAKVVDLDTGKTL-GVNQRGELCVRGPMIMSGYVNNPEATNA----LIDKDGWLH--SGDIA 424
Cdd:cd17653 251 TELLPGQPVTIGKPIP--NSTCYILDADLQPvPEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyrTGDYG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 425 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDdagELPAAVVvlehgktmteKEIVDYVAS 504
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNG---RLVAFVT----------PETVDVDGL 395
|
490 500 510
....*....|....*....|....*....|....*...
gi 110555473 505 QVTTAKKLR-----GGVVFVDEVPKGLTGKLDARKIRE 537
Cdd:cd17653 396 RSELAKHLPsyavpDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
193-538 |
1.74e-26 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 114.68 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHR---------TACVRFsHARDPIFgnqiipdtailSVVPFHHGFGMFT-TLGYLICGFRV 262
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRnllanraqvAARIDF-SPEDKVF-----------NALPVFHSFGLTGgLVLPLLSGVKV 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 263 VLM-----YRFEEELFlrslqdYKIQSALLV--PTLFSFFAKSTliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlpG 335
Cdd:PRK06814 864 FLYpsplhYRIIPELI------YDTNATILFgtDTFLNGYARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEKF---G 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 336 IR--QGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtgktlGVNQRGELCVRGPMIMSGYV--NNPEATNAL 411
Cdd:PRK06814 933 IRilEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVP-----GIDEGGRLFVRGPNVMLGYLraENPGVLEPP 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 412 idKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ-HPNIFDAGVAgLPDDDAGElpaAVVVLEHG 490
Cdd:PRK06814 1008 --ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVS-IPDARKGE---RIILLTTA 1081
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 110555473 491 KTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 538
Cdd:PRK06814 1082 SDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
52-533 |
4.89e-26 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 110.92 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERELLNSMgisqptvvfvskk 131
Cdd:cd17649 14 SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPL-DPEYPAERLRYM------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 glqkilnvqkklpiiqkiiIMDSKTdyqgfqsmyTFVTSHLPpgfneydfvpesfdrdKTIALIMNSSGSTGLPKGVALP 211
Cdd:cd17649 80 -------------------LEDSGA---------GLLLTHHP----------------RQLAYVIYTSGSTGTPKGVAVS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 212 HrTACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL----MYRFEEELfLRSLQDYKIQSALL 287
Cdd:cd17649 116 H-GPLAAHCQATAERYG--LTPGDRELQFASFNFDGAHEQLLPPLICGACVVLrpdeLWASADEL-AEMVRELGVTVLDL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 288 VPTLFSFFAKSTLIDKYDL-SNLHEIASGGAPLSKEVgeavAKRFHLPGIR--QGYGLTETT-SAILITPEGDDKPGA-- 361
Cdd:cd17649 192 PPAYLQQLAEEADRTGDGRpPSLRLYIFGGEALSPEL----LRRWLKAPVRlfNAYGPTEATvTPLVWKCEAGAARAGas 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 362 --VGKVVPFFEAKVVDLDTGkTLGVNQRGELCVRGPMIMSGYVNNPEATNA--LIDKDG-----WLHSGDIAYWDEDEHF 432
Cdd:cd17649 268 mpIGRPLGGRSAYILDADLN-PVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRDDGVI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 433 FIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV---------LEHGKTMTEKEIVDYVa 503
Cdd:cd17649 347 EYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLraaaaqpelRAQLRTALRASLPDYM- 425
|
490 500 510
....*....|....*....|....*....|
gi 110555473 504 sqVTTAkklrggVVFVDEVPKGLTGKLDAR 533
Cdd:cd17649 426 --VPAH------LVFLARLPLTPNGKLDRK 447
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
37-534 |
7.18e-26 |
|
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: 110.84 E-value: 7.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAHIEVdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY-NERell 115
Cdd:cd12116 1 PDATAVRDDDRSL--SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYpADR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 116 nsmgisqptvvfvskkgLQKILNVQKKlpiiqKIIIMDSKTDYQGFQsmYTFVTSHLPPGFNEYDFVPESFDRDKTIALI 195
Cdd:cd12116 76 -----------------LRYILEDAEP-----ALVLTDDALPDRLPA--GLPVLLLALAAAAAAPAAPRTPVSPDDLAYV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 196 MNSSGSTGLPKGVALPHRtACVRFSHA--RDPIFGnqiiPDTAILSVVPFhhGFGMFT--TLGYLICGFRVVLMYR---F 268
Cdd:cd12116 132 IYTSGSTGRPKGVVVSHR-NLVNFLHSmrERLGLG----PGDRLLAVTTY--AFDISLleLLLPLLAGARVVIAPRetqR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLheiaSGGAPLSkevgEAVAKRFHLPGIR--QGYGLTETT 346
Cdd:cd12116 205 DPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTAL----CGGEALP----PDLAARLLSRVGSlwNLYGPTETT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 347 ---SAILITPEgdDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHS--- 420
Cdd:cd12116 277 iwsTAARVTAA--AGPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPgsr 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 421 ----GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELpAAVVVLEHGKTMTEK 496
Cdd:cd12116 354 lyrtGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAA 432
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 110555473 497 EIVDYVASQ-----VTTAkklrggVVFVDEVPKGLTGKLDaRK 534
Cdd:cd12116 433 ALRAHLRATlpaymVPSA------FVRLDALPLTANGKLD-RK 468
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
51-430 |
8.65e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 111.51 E-value: 8.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNER-----ELLNSMGISQPTV 125
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLVsqdfgKLRHVLELLTPGL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 126 VFVS-----KKGLQKILNVQKKLPIIQKIIIMDSKTDYQgfqsmyTFVTSHLPPGfneydfVPESFDR--DKTIALIMNS 198
Cdd:PRK08180 150 VFADdgaafARALAAVVPADVEVVAVRGAVPGRAATPFA------ALLATPPTAA------VDAAHAAvgPDTIAKFLFT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 SGSTGLPKGVALPHRTACV---------RFSHARDPIfgnqiipdtaILSVVPFHHGFGMFTTLGYlicgfrvVL----- 264
Cdd:PRK08180 218 SGSTGLPKAVINTHRMLCAnqqmlaqtfPFLAEEPPV----------LVDWLPWNHTFGGNHNLGI-------VLynggt 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 265 MY---------RFEEELflRSLQDykIQSALL--VPTLF---------------SFFakstlidkydlSNLHEIASGGAP 318
Cdd:PRK08180 281 LYiddgkptpgGFDETL--RNLRE--ISPTVYfnVPKGWemlvpalerdaalrrRFF-----------SRLKLLFYAGAA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 319 LSKEVGE-----AVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtGKTlgvnqrgELCVR 393
Cdd:PRK08180 346 LSQDVWDrldrvAEATCGERIRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVG-GKL-------EVRVK 417
|
410 420 430
....*....|....*....|....*....|....*...
gi 110555473 394 GPMIMSGYVNNPEATNALIDKDGWLHSGDIAYW-DEDE 430
Cdd:PRK08180 418 GPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPAD 455
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
51-530 |
1.02e-25 |
|
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: 111.13 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVcsenslqfFMPV-------------LGALFIGV-------AVAPANDIYN 110
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAI--------YMPMipeaavamlacarIGAVHSVIfggfapeAVAGRIIDSS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 111 ERELLNSMGISQPTVVFVSKKGLQKILNVQkkLPIIQKIIIMD-SKTDYQGFQSM---YTFVTSHLPPGFNeydfvPESF 186
Cdd:cd17634 157 SRLLITADGGVRAGRSVPLKKNVDDALNPN--VTSVEHVIVLKrTGSDIDWQEGRdlwWRDLIAKASPEHQ-----PEAM 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 187 DRDKTIaLIMNSSGSTGLPKGVALPHR----TACVRFSHARDpIFGNQIIPDTAILSVVPFHHgfgmFTTLGYLICGFRV 262
Cdd:cd17634 230 NAEDPL-FILYTSGTTGKPKGVLHTTGgylvYAATTMKYVFD-YGPGDIYWCTADVGWVTGHS----YLLYGPLACGATT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 263 VLmyrFE-------EELFLRSLQDYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKrfHL 333
Cdd:cd17634 304 LL---YEgvpnwptPARMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINPEAYEWYWK--KI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 334 PGIR----QGYGLTETTSAILITPEGDDKPGAVGKVVPFF--EAKVVDlDTGKTLGVNQRGELCVRGP---MIMSGYVNN 404
Cdd:cd17634 379 GKEKcpvvDTWWQTETGGFMITPLPGAIELKAGSATRPVFgvQPAVVD-NEGHPQPGGTEGNLVITDPwpgQTRTLFGDH 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 405 PEATNALIDK-DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAA 483
Cdd:cd17634 458 ERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 110555473 484 VVVLEHGKTMTEK---EIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKL 530
Cdd:cd17634 538 YVVLNHGVEPSPElyaELRNWVRKEIGPLATPD-VVHWVDSLPKTRSGKI 586
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
199-488 |
1.22e-25 |
|
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: 112.26 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 SGSTGLPKGVALPHRTAcVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFEEELFLR 275
Cdd:COG1020 626 SGSTGRPKGVMVEHRAL-VNLLAWMQRRYG--LGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAppeARRDPAALAE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 276 SLQDYKIQSALLVPTLFsffakSTLID--KYDLSNLHEIASGGAPLSKEVGEAVAKRFhlPGIR--QGYGLTETT--SAI 349
Cdd:COG1020 703 LLARHRVTVLNLTPSLL-----RALLDaaPEALPSLRLVLVGGEALPPELVRRWRARL--PGARlvNLYGPTETTvdSTY 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 350 LITPEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA-----LIDKDG--WLHS 420
Cdd:COG1020 776 YEVTPPDADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadPFGFPGarLYRT 854
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 421 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLE 488
Cdd:COG1020 855 GDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPE 922
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
193-531 |
2.51e-25 |
|
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: 108.94 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDpIFG----NQIIPDTAI---LSVvpfhhgFGMFTTLGyliCGFRVVLM 265
Cdd:cd12115 108 AYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAA-AFSaeelAGVLASTSIcfdLSV------FELFGPLA---TGGKVVLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 yrfEEELFLRSLQDYKiQSALL--VPTlfsffAKSTLIDKYDL-SNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGL 342
Cdd:cd12115 178 ---DNVLALPDLPAAA-EVTLIntVPS-----AAAELLRHDALpASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 343 TETT--SAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWL-- 418
Cdd:cd12115 249 SEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpg 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 419 ----HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT 494
Cdd:cd12115 328 arlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGL 407
|
330 340 350
....*....|....*....|....*....|....*..
gi 110555473 495 EKEIVDYVAsQVTTAKKLRGGVVFVDEVPKGLTGKLD 531
Cdd:cd12115 408 VEDLRRHLG-TRLPAYMVPSRFVRLDALPLTPNGKID 443
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
26-550 |
5.23e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 108.94 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 26 LHKAMKRYALVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPA 105
Cdd:PRK05857 17 LDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 106 NDIYNERELLNSMGISQPTVVFV---SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYtfvtshlPPGFNEYDfv 182
Cdd:PRK05857 97 DGNLPIAAIERFCQITDPAAALVapgSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAS-------LAGNADQG-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 183 pesfdRDKTIALIMnSSGSTGLPKGVALPHRT--ACVRFSHARDPIFGNQIIPDTAiLSVVPFHHGFGMFTTLGYLICGf 260
Cdd:PRK05857 168 -----SEDPLAMIF-TSGTTGEPKAVLLANRTffAVPDILQKEGLNWVTWVVGETT-YSPLPATHIGGLWWILTCLMHG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 261 rVVLMYRFEEELFLRS-LQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGaplSKEVGEAVakRF-HLPGIR- 337
Cdd:PRK05857 240 -GLCVTGGENTTSLLEiLTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADV--RFiEATGVRt 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 338 -QGYGLTETTSAILITPEGDD-----KPGAVGKVVPFFEAKVVDLDTG-----KTLGVNQRGELCVRGPMIMSGYVNNPE 406
Cdd:PRK05857 314 aQVYGLSETGCTALCLPTDDGsivkiEAGAVGRPYPGVDVYLAATDGIgptapGAGPSASFGTLWIKSPANMLGYWNNPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 407 ATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 486
Cdd:PRK05857 394 RTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110555473 487 lehgkTMTEKEIVDYVASQVTTAKKLR---------GGVVFVDEVPKGLTGKLdarkIREILIKAKKGGKIAV 550
Cdd:PRK05857 473 -----ASAELDESAARALKHTIAARFRresepmarpSTIVIVTDIPRTQSGKV----MRASLAAAATADKARV 536
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
193-534 |
8.67e-25 |
|
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: 106.95 E-value: 8.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRfeEEL 272
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRGLA---NLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPA--EEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 273 -----FLRSLQDYKIQSALLVPTLFSffakstLIDKYDLSNLHEIASGGAPLSKEvgeaVAKRFHlPGIR--QGYGLTET 345
Cdd:cd17652 171 lpgepLADLLREHRITHVTLPPAALA------ALPPDDLPDLRTLVVAGEACPAE----LVDRWA-PGRRmiNAYGPTET 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 T-SAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWL 418
Cdd:cd17652 240 TvCATMAGPLPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTaerfvaDPFGAPGSRM 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 419 H-SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAgVAGLPDDDAGE--LpAAVVVLEHGKTMTE 495
Cdd:cd17652 319 YrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEA-VVVVRDDRPGDkrL-VAYVVPAPGAAPTA 396
|
330 340 350
....*....|....*....|....*....|....*....
gi 110555473 496 KEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARK 534
Cdd:cd17652 397 AELRAHLAERL-PGYMVPAAFVVLDALPLTPNGKLDRRA 434
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
307-462 |
1.10e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 108.53 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 307 SNLHEIASGGAPLSKEVGEAVAKRFHLpgIRQGYGLTETT--SAILITpeGDDKPGAVGKVVPFFEAKVVDLDTGK-TLG 383
Cdd:PTZ00216 428 GRVRAMLSGGGPLSAATQEFVNVVFGM--VIQGWGLTETVccGGIQRT--GDLEPNAVGQLLKGVEMKLLDTEEYKhTDT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 384 VNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK-YKGYQVAPAELESILLQHP 462
Cdd:PTZ00216 504 PEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNE 583
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
37-539 |
1.38e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 107.38 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAvaPANDIYNEREL-L 115
Cdd:PRK10946 37 SDAIAVICG--ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSeL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 116 NSMGIS-QPTVVFVSKK-----GLQKILNVQKKLPIIQkIIIMDSKTDYQGFQSmytfVTSHLPPGFneyDFVPESFDRd 189
Cdd:PRK10946 113 NAYASQiEPALLIADRQhalfsDDDFLNTLVAEHSSLR-VVLLLNDDGEHSLDD----AINHPAEDF---TATPSPADE- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 190 ktIALIMNSSGSTGLPKgvaLPHRTA-----CVRFShardpifgNQII---PDTAILSVVPFHHGFGMFT--TLGYLICG 259
Cdd:PRK10946 184 --VAFFQLSGGSTGTPK---LIPRTHndyyySVRRS--------VEICgftPQTRYLCALPAAHNYPMSSpgALGVFLAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 260 FRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRfhLPG-- 335
Cdd:PRK10946 251 GTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWlqAIAEGGSRAQLASLKLLQVGGARLS----ETLARR--IPAel 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 336 ---IRQGYGLTE---------TTSAILITPEG-----DDkpgavgkvvpffEAKVVDLDtGKTLGVNQRGELCVRGPMIM 398
Cdd:PRK10946 325 gcqLQQVFGMAEglvnytrldDSDERIFTTQGrpmspDD------------EVWVADAD-GNPLPQGEVGRLMTRGPYTF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 399 SGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAG 478
Cdd:PRK10946 392 RGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 479 ELPAAVVVLEHG-------KTMTEKEIVDYvasqvttakKLRGGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:PRK10946 472 EKSCAFLVVKEPlkavqlrRFLREQGIAEF---------KLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
192-542 |
1.50e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 107.40 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRT--ACVRfSHARDpifGNQIIPDTAILSVVPFHHGFGMfttLGYLI----CGFRVVLM 265
Cdd:PRK09192 178 IAYLQYSSGSTRFPRGVIITHRAlmANLR-AISHD---GLKVRPGDRCVSWLPFYHDMGL---VGFLLtpvaTQLSVDYL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 YrfEEELFLRSLQDYKIQS----ALLVPTLFSF-----FAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGI 336
Cdd:PRK09192 251 P--TRDFARRPLQWLDLISrnrgTISYSPPFGYelcarRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGF 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 337 RQ-----GYGLTETTSAILITPEG----------------------DDKPGAV------GKVVPFFEAKVVDlDTGKTLG 383
Cdd:PRK09192 329 DDkafmpSYGLAEATLAVSFSPLGsgivveevdrdrleyqgkavapGAETRRVrtfvncGKALPGHEIEIRN-EAGMPLP 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 384 VNQRGELCVRGPMIMSGYVNNPEATNALiDKDGWLHSGDIAYWDEDEhFFIVDRLKSLIKYKGYQVAPAELESILLQHPN 463
Cdd:PRK09192 408 ERVVGHICVRGPSLMSGYFRDEESQDVL-AADGWLDTGDLGYLLDGY-LYITGRAKDLIIINGRNIWPQDIEWIAEQEPE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 464 IF--DAGVAGLPDDDaGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFV--DEVPKGLTGKLDARKIREIL 539
Cdd:PRK09192 486 LRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIHALAALVRSEFGVEAAVELVppHSLPRTSSGKLSRAKAKKRY 564
|
...
gi 110555473 540 IKA 542
Cdd:PRK09192 565 LSG 567
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
181-493 |
1.59e-24 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 107.98 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 181 FVPESFDrdktIALIMNSSGSTGLPKGVALPHRT--ACVRFSHARDPIFGNQIIPDTAILSVVPFHHgfgmfttlgylic 258
Cdd:PLN02430 215 NPPKPLD----ICTIMYTSGTSGDPKGVVLTHEAvaTFVRGVDLFMEQFEDKMTHDDVYLSFLPLAH------------- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 259 gfrvvLMYRFEEELFLRS-----------------LQDYK-----------------IQSAL--LVPTLFSFFaksTLID 302
Cdd:PLN02430 278 -----ILDRMIEEYFFRKgasvgyyhgdlnalrddLMELKptllagvprvferihegIQKALqeLNPRRRLIF---NALY 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 303 KYDLSNLHE-----------------------------IASGGAPLSKEVgEAVAKRFHLPGIRQGYGLTETTSAILIT- 352
Cdd:PLN02430 350 KYKLAWMNRgyshkkaspmadflafrkvkaklggrlrlLISGGAPLSTEI-EEFLRVTSCAFVVQGYGLTETLGPTTLGf 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 353 PEGDDKPGAVGKVVPFFEAKVVDL-DTG-KTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDE 430
Cdd:PLN02430 429 PDEMCMLGTVGAPAVYNELRLEEVpEMGyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNG 507
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110555473 431 HFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNIFDAGVAGlpdDDAGELPAAVVVLEHGKTM 493
Cdd:PLN02430 508 VLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNEENTN 568
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
190-537 |
1.74e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 107.03 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 190 KTIALIMNSSGSTGLPKGVALPH-------RTACVRFSHARDpifgnqiipDTAILSVVPFHHGFGMFTTLGYLICGFRV 262
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHgrlafagRALTERFGLTRD---------DVCYVSMPLFHSNAVMAGWAPAVASGAAV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 263 VLMYRFEEELFLRSLQDYKIqsallvpTLFSFFAK------STLIDKYDLSNLHEIASGGAPlSKEVGEAVAKRFhlpGI 336
Cdd:PRK13388 221 ALPAKFSASGFLDDVRRYGA-------TYFNYVGKplayilATPERPDDADNPLRVAFGNEA-SPRDIAEFSRRF---GC 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 337 R--QGYGLTETtsAILITPEGDDKPGAVGKvvPFFEAKVVDLDTGKT-----LGVNQR--------GELCVR-GPMIMSG 400
Cdd:PRK13388 290 QveDGYGSSEG--AVIVVREPGTPPGSIGR--GAPGVAIYNPETLTEcavarFDAHGAllnadeaiGELVNTaGAGFFEG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 401 YVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGEL 480
Cdd:PRK13388 366 YYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQ 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 481 PAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFV-DEVPKGLTGKLDARKIRE 537
Cdd:PRK13388 445 VMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYVRIaADLPSTATNKVLKRELIA 502
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
51-424 |
1.22e-23 |
|
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: 104.82 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY-----NERELLNSMGISQPTV 125
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslmsqDLAKLKHLFELLKPGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 126 VFVS-----KKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFqsmytfvtSHLPPGFNeydfVPESFDR--DKTIALIMNS 198
Cdd:cd05921 106 VFAQdaapfARALAAIFPLGTPLVVSRNAVAGRGAISFAEL--------AATPPTAA----VDAAFAAvgPDTVAKFLFT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 SGSTGLPKGVALPHRTACVRFSHARD--PIFGNqiiPDTAILSVVPFHHGFGMFTtlgylicGFRVVL-----MY----- 266
Cdd:cd05921 174 SGSTGLPKAVINTQRMLCANQAMLEQtyPFFGE---EPPVLVDWLPWNHTFGGNH-------NFNLVLynggtLYiddgk 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 267 ----RFEEELflRSLQDYKIQSALLVPTLFSFFAK-----STLIDKYdLSNLHEIASGGAPLSKEVGE-----AVAKRFH 332
Cdd:cd05921 244 pmpgGFEETL--RNLREISPTVYFNVPAGWEMLVAalekdEALRRRF-FKRLKLMFYAGAGLSQDVWDrlqalAVATVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 333 LPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtGKTlgvnqrgELCVRGPMIMSGYVNNPEATNALI 412
Cdd:cd05921 321 RIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSG-GKY-------EVRVKGPNVTPGYWRQPELTAQAF 392
|
410
....*....|..
gi 110555473 413 DKDGWLHSGDIA 424
Cdd:cd05921 393 DEEGFYCLGDAA 404
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
193-531 |
1.65e-23 |
|
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: 103.54 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDPI-FGNQiipDtailSVVPFHH---GFGMFTTLGYLICGFRVVLM--- 265
Cdd:cd17643 96 AYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFgFNED---D----VWTLFHSyafDFSVWEIWGALLHGGRLVVVpye 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIR--QGYGLT 343
Cdd:cd17643 169 VARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvNMYGIT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 344 ETT---SAILITPegDDKPGA----VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA--LIDK 414
Cdd:cd17643 249 ETTvhvTFRPLDA--ADLPAAaaspIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfVANP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 415 DG-----WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 489
Cdd:cd17643 326 FGgpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADD 405
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 110555473 490 GKTMTEKEIVDYVAsQVTTAKKLRGGVVFVDEVPKGLTGKLD 531
Cdd:cd17643 406 GAAADIAELRALLK-ELLPDYMVPARYVPLDALPLTVNGKLD 446
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
195-541 |
1.70e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 104.44 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 195 IMNSSGSTGLPKGVAL---PHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRV-VLMYRFEE 270
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRsngPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGgIIKNKHIE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 271 ELFLRSLQDYKIQSALLVPTLFSFFAK-----STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRqGYGLTET 345
Cdd:PTZ00237 339 DDLWNTIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR-GYGQTEI 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 TSAILITPEGDDKP-GAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPM---IMSGYVNNPEATNALIDK-DGWLHS 420
Cdd:PTZ00237 418 GITYLYCYGHINIPyNATGVPSIFIKPSILSED-GKELNVNEIGEVAFKLPMppsFATTFYKNDEKFKQLFSKfPGYYNS 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 421 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT------ 494
Cdd:PTZ00237 497 GDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQsidlnk 576
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 110555473 495 -EKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLdarkIREILIK 541
Cdd:PTZ00237 577 lKNEINNIITQDIESLAVLR-KIIIVNQLPKTKTGKI----PRQIISK 619
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
182-539 |
3.22e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 103.15 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 182 VPESFDRDktIALIMNSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDT-AILSVVPFHHGFGMfttLGYLIcgf 260
Cdd:PRK07768 146 PVETGEDD--LALMQLTSGSTGSPKAVQITHGNL---YANAEAMFVAAEFDVETdVMVSWLPLFHDMGM---VGFLT--- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 261 rvVLMYRFEEELFLRSLqDYkIQSALLVPTLFSF----------FAKSTLI---------DKYDLSNLHEIASGGAPLSK 321
Cdd:PRK07768 215 --VPMYFGAELVKVTPM-DF-LRDPLLWAELISKyrgtmtaapnFAYALLArrlrrqakpGAFDLSSLRFALNGAEPIDP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 322 EVGEA---VAKRFHLP--GIRQGYGLTETTSAILITPEGD---------------------DKPGA-----VGKVVPFFE 370
Cdd:PRK07768 291 ADVEDlldAGARFGLRpeAILPAYGMAEATLAVSFSPCGAglvvdevdadllaalrravpaTKGNTrrlatLGPPLPGLE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 371 AKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNnPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVA 450
Cdd:PRK07768 371 VRVVDED-GQVLPPRGVGVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 451 PAELESILLQHPNIFDAGVA--GLPDDDAGELPAavVVLE---HGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDE---V 522
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAVavRLDAGHSREGFA--VAVEsnaFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGpgsI 526
|
410
....*....|....*..
gi 110555473 523 PKGLTGKLDARKIREIL 539
Cdd:PRK07768 527 PKTPSGKLRRANAAELV 543
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
37-530 |
5.18e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 102.38 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 116
Cdd:PRK13383 49 PGRTAIIDD--DGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 117 SMGISQPTVVFVSKKGLQKILNVQkklpiiQKIIIMDSKTdyqgfqsmytfVTSHlppgfneydfvpESFDRDKTIA--- 193
Cdd:PRK13383 127 ALRAHHISTVVADNEFAERIAGAD------DAVAVIDPAT-----------AGAE------------ESGGRPAVAApgr 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMNSSGSTGLPKGVAlphrtacvRFSHARDPIFGNQIIPDTAILSV-------VPFHHGFGMFTTLGYLICGFRVVLMY 266
Cdd:PRK13383 178 IVLLTSGTTGKPKGVP--------RAPQLRSAVGVWVTILDRTRLRTgsrisvaMPMFHGLGLGMLMLTIALGGTVLTHR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 267 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKstLIDKYDLSN----LHEIASGGAPLSKEVGeavaKRF---HLPGIRQG 339
Cdd:PRK13383 250 HFDAEAALAQASLHRADAFTAVPVVLARILE--LPPRVRARNplpqLRVVMSSGDRLDPTLG----QRFmdtYGDILYNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 340 YGLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNpeATNALIDkdGWL 418
Cdd:PRK13383 324 YGSTEVGIGALATPaDLRDAPETVGKPVAGCPVRILDRN-NRPVGPRVTGRIFVGGELAGTRYTDG--GGKAVVD--GMT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 419 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEI 498
Cdd:PRK13383 399 STGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQL 478
|
490 500 510
....*....|....*....|....*....|..
gi 110555473 499 VDYVASQVTTAKKLRgGVVFVDEVPKGLTGKL 530
Cdd:PRK13383 479 RDYLKDRVSRFEQPR-DINIVSSIPRNPTGKV 509
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
192-537 |
9.39e-23 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 101.41 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRTacvrFSHARDPIfGNQIIPDT--AILSVVPFHHGFGMFTtlGYLICGFRVVLMYRFE 269
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHEN----LVHNMFAI-LNSTEWKTkdRILSWMPLTHDMGLIA--FHLAPLIAGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 270 EELFLR--SLQDYKIQ----SALLVPT----LFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQG 339
Cdd:cd05908 181 TRLFIRrpILWLKKASehkaTIVSSPNfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 340 -----YGLTETTSAILITPEG------------------------DDKPGA----VGKVVPFFEAKVVDlDTGKTLGVNQ 386
Cdd:cd05908 261 ailpvYGLAEASVGASLPKAQspfktitlgrrhvthgepepevdkKDSECLtfveVGKPIDETDIRICD-EDNKILPDGY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 387 RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWdEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFD 466
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 467 AGVA--GLPDDDAGElPAAVVVLEHGKtmTEKEIVDYvASQVTTAKKLRGG-----VVFVDEVPKGLTGKLDARKIRE 537
Cdd:cd05908 419 GRVVacGVNNSNTRN-EEIFCFIEHRK--SEDDFYPL-GKKIKKHLNKRGGwqineVLPIRRIPKTTSGKVKRYELAQ 492
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
51-480 |
1.25e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 102.05 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY-----NERELLNSMGISQPTV 125
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmshDHAKLKHLFDLVKPRV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 126 VFVSKKGL-QKILNVQKKLPIiqKIIIMDSKTDYQGFQSMYTFVTShlPPGfneyDFVPESFDR--DKTIALIMNSSGST 202
Cdd:PRK12582 161 VFAQSGAPfARALAALDLLDV--TVVHVTGPGEGIASIAFADLAAT--PPT----AAVAAAIAAitPDTVAKYLFTSGST 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 203 GLPKGVALPHRTAC--------VRfshARDPifgNQIIPDtaILSVVPFHH------GFGMFTTLG---YLICGFRVVLM 265
Cdd:PRK12582 233 GMPKAVINTQRMMCaniamqeqLR---PREP---DPPPPV--SLDWMPWNHtmggnaNFNGLLWGGgtlYIDDGKPLPGM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 yrFEEELflRSLQDYKIQSALLVPTLFSFFAKSTLIDKyDL-----SNLHEIASGGAPLSKEVGE-----AVAKRFHLPG 335
Cdd:PRK12582 305 --FEETI--RNLREISPTVYGNVPAGYAMLAEAMEKDD-ALrrsffKNLRLMAYGGATLSDDLYErmqalAVRTTGHRIP 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 336 IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 415
Cdd:PRK12582 380 FYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAP--------VGDKYEVRVKGPNVTPGYHKDPELTAAAFDEE 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 416 GWLHSGDIA-YWDEDehffivDRLKSLI-------KYK---GYQVAPAELESILLQ--HPNIFDAGVAGLPDDDAGEL 480
Cdd:PRK12582 452 GFYRLGDAArFVDPD------DPEKGLIfdgrvaeDFKlstGTWVSVGTLRPDAVAacSPVIHDAVVAGQDRAFIGLL 523
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
198-539 |
1.83e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 100.94 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 198 SSGSTGLPKGVALPHRTACVrfsHArdpiFGNQIiPDT-------AILSVVP-FH-HGFGmfttLGYL--ICGFRVVL-- 264
Cdd:PRK07008 184 TSGTTGNPKGALYSHRSTVL---HA----YGAAL-PDAmglsardAVLPVVPmFHvNAWG----LPYSapLTGAKLVLpg 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 265 -------MYR-FEEElflrslqdyKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlpGI 336
Cdd:PRK07008 252 pdldgksLYElIEAE---------RVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEY---GV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 337 R--QGYGLTET----TSAILiTPEGDDKPGAV--------GKVVPFFEAKVVDlDTGKTL---GVNQrGELCVRGPMIMS 399
Cdd:PRK07008 320 EviHAWGMTEMsplgTLCKL-KWKHSQLPLDEqrkllekqGRVIYGVDMKIVG-DDGRELpwdGKAF-GDLQVRGPWVID 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 400 GYVNNpeATNALIDkdGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGE 479
Cdd:PRK07008 397 RYFRG--DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDE 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110555473 480 LPAAVVVLEHGKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 539
Cdd:PRK07008 473 RPLLVVVKRPGAEVTREELLAFYEGKV--AKwWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
51-462 |
2.20e-22 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 101.35 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVApanDIY---NERELLNSMGISQPTVVF 127
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVV---TIYaslGEEALCHSLNETEVTTVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 128 VSKKGLQKILNVQKKLPIIQKIIIMD---SKTDYQGFQSMYTFVTShlppgFNEYD------FVPESFDRDKTIALIMNS 198
Cdd:PLN02387 184 CDSKQLKKLIDISSQLETVKRVIYMDdegVDSDSSLSGSSNWTVSS-----FSEVEklgkenPVDPDLPSPNDIAVIMYT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 SGSTGLPKGVALPHrtacvrfshardpifGNQIIPDTAILSVVPFHHGFGMFttLGYLicgfrvVLMYRFE---EELFLR 275
Cdd:PLN02387 259 SGSTGLPKGVMMTH---------------GNIVATVAGVMTVVPKLGKNDVY--LAYL------PLAHILElaaESVMAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 276 S-----------LQDY--KIQ------SALLVPTLFSffAKSTLIDK-------------------YDLSNLHEIA---- 313
Cdd:PLN02387 316 VgaaigygspltLTDTsnKIKkgtkgdASALKPTLMT--AVPAILDRvrdgvrkkvdakgglakklFDIAYKRRLAaieg 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 314 ---------------------------------SGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPG 360
Cdd:PLN02387 394 swfgawglekllwdalvfkkiravlggrirfmlSGGAPLSGDTQRFINICLGAP-IGQGYGLTETCAGATFSEWDDTSVG 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 361 AVGKVVPFFEAKVVDLDTGKTLGVNQ---RGELCVRGPMIMSGYVNNPEATNAL--IDKDG--WLHSGDIAYWDEDEHFF 433
Cdd:PLN02387 473 RVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLE 552
|
490 500 510
....*....|....*....|....*....|
gi 110555473 434 IVDRLKSLIKYK-GYQVAPAELESILLQHP 462
Cdd:PLN02387 553 IIDRKKDIVKLQhGEYVSLGKVEAALSVSP 582
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
34-533 |
2.20e-22 |
|
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: 100.43 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 34 ALVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERE 113
Cdd:cd17646 9 ARTPDAPAVVDE--GRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL-DPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 114 LLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIimdsktdyqgfqsmytfvTSHLPPGfneydfVPESFDRDKTIA 193
Cdd:cd17646 86 RLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA------------------LAAPPAT------PPLVPPRPDNLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFhhGF--GMFTTLGYLICGFRVVLMY---RF 268
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY---PLGPGDRVLQKTPL--SFdvSVWELFWPLVAGARLVVARpggHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEELFLRSLQDYKIQSALLVPTLFSFFakstlidkydlsnLHEIASGGAPLSKEV---GEA----VAKRFH-LPGIR--Q 338
Cdd:cd17646 217 DPAYLAALIREHGVTTCHFVPSMLRVF-------------LAEPAAGSCASLRRVfcsGEAlppeLAARFLaLPGAElhN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 339 GYGLTETT---SAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 415
Cdd:cd17646 284 LYGPTEAAidvTHWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 416 GWLH------SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGE-LPAAVVVLE 488
Cdd:cd17646 363 PFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAArLVGYVVPAA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 110555473 489 HGKTMTEKEIVDYVA-----SQVTTAkklrggVVFVDEVPKGLTGKLDAR 533
Cdd:cd17646 443 GAAGPDTAALRAHLAerlpeYMVPAA------FVVLDALPLTANGKLDRA 486
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
51-471 |
8.55e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 99.53 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 130
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLQKILNVQKKLPIIQKIII--------MDSKTDYQG--------FQSMYTfVTSHLPPgfneydfvpesfDRDKTIAL 194
Cdd:PLN02861 158 SKISSILSCLPKCSSNLKTIVsfgdvsseQKEEAEELGvscfsweeFSLMGS-LDCELPP------------KQKTDICT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 195 IMNSSGSTGLPKGVALPHRTACVRFSHARDPIF--GNQIIPDTAILSVVPFHHGFGMF---------TTLGYLICGFRVV 263
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKvtDRVATEEDSYFSYLPLAHVYDQVietyciskgASIGFWQGDIRYL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 264 L-------------MYRFEEELFLRSLQdyKIQSA-LLVPTLFSFF---------------AKSTLIDKYDLSNLHE--- 311
Cdd:PLN02861 305 MedvqalkptifcgVPRVYDRIYTGIMQ--KISSGgMLRKKLFDFAynyklgnlrkglkqeEASPRLDRLVFDKIKEglg 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 312 -----IASGGAPLSKEVgEAVAKRFHLPGIRQGYGLTETTSAILiTPEGDDKP--GAVGKVVPFFEAKVVDL-DTG-KTL 382
Cdd:PLN02861 383 grvrlLLSGAAPLPRHV-EEFLRVTSCSVLSQGYGLTESCGGCF-TSIANVFSmvGTVGVPMTTIEARLESVpEMGyDAL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 383 GVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQH 461
Cdd:PLN02861 461 SDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRC 539
|
490
....*....|
gi 110555473 462 PNIFDAGVAG 471
Cdd:PLN02861 540 PLIASIWVYG 549
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
51-539 |
6.53e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 96.39 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMK-RYGLNTNHRI----VVCSENSLQFF-MPVLGALFigvavAPANDIYNERELLNSMGISQPT 124
Cdd:PRK05620 39 TTFAAIGARAAALAHALHdELGITGDQRVgsmmYNCAEHLEVLFaVACMGAVF-----NPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 125 VVFVSKKGLQKILNVQKKLPIIQKIIIMDSktdyqgfqSMYTFVTSHLPPGFNEYDFV------PESFD----RDKTIAL 194
Cdd:PRK05620 114 VIVADPRLAEQLGEILKECPCVRAVVFIGP--------SDADSAAAHMPEGIKVYSYEalldgrSTVYDwpelDETTAAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 195 IMNSSGSTGLPKGVALPHRTACVRFSHAR--DPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR-FEEE 271
Cdd:PRK05620 186 ICYSTGTTGAPKGVVYSHRSLYLQSLSLRttDSL---AVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPdLSAP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 272 LFLRSLQDYKIQSALLVPT----LFSFFAKSTLidkyDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTS 347
Cdd:PRK05620 263 TLAKIIATAMPRVAHGVPTlwiqLMVHYLKNPP----ERMSLQEIYVGGSAVPPILIKAWEERYGVDVV-HVWGMTETSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 348 AILIT--PEG------DDKPGAVGKVVPFFEAKVVDldTGKTLGVNQR--GELCVRGPMIMSGYVNNP------------ 405
Cdd:PRK05620 338 VGTVArpPSGvsgearWAYRVSQGRFPASLEYRIVN--DGQVMESTDRneGEIQVRGNWVTASYYHSPteegggaastfr 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 406 ----EATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELP 481
Cdd:PRK05620 416 gedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERP 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110555473 482 AAVVVLEHGKTMTEkeivdyvasqvTTAKKLRGGV-------------VFVDEVPKGLTGKLDARKIREIL 539
Cdd:PRK05620 496 LAVTVLAPGIEPTR-----------ETAERLRDQLrdrlpnwmlpeywTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
195-538 |
6.55e-21 |
|
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: 96.48 E-value: 6.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 195 IMNSSGSTGLPKGVAlpHRTA-----------CVrFSHARDPIFGNqiipdTAILSVVPFHHgfgmFTTLGYLICGFRVV 263
Cdd:cd05966 236 ILYTSGSTGKPKGVV--HTTGgyllyaattfkYV-FDYHPDDIYWC-----TADIGWITGHS----YIVYGPLANGATTV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 264 LmyrFE-------EELFLRSLQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKE--------VGEa 326
Cdd:cd05966 304 M---FEgtptypdPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVLGSVGEPINPEawmwyyevIGK- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 327 vakrFHLPgIRQGYGLTETTSaILITP---EGDDKPGAVGKvvPFF--EAKVVDLDTGKtLGVNQRGELCVRGP---MIM 398
Cdd:cd05966 380 ----ERCP-IVDTWWQTETGG-IMITPlpgATPLKPGSATR--PFFgiEPAILDEEGNE-VEGEVEGYLVIKRPwpgMAR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 399 SGYvNNPEA-TNALIDKD-GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDD 476
Cdd:cd05966 451 TIY-GDHERyEDTYFSKFpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDI 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 477 AGELPAAVVVLEHGKTMT---EKEIVDYVASQ---VTTAKKlrggVVFVDEVPKGLTGKLDARKIREI 538
Cdd:cd05966 530 KGEAIYAFVTLKDGEEPSdelRKELRKHVRKEigpIATPDK----IQFVPGLPKTRSGKIMRRILRKI 593
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
52-488 |
1.02e-20 |
|
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: 95.19 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMK-RYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiYNERE--LLNSMGISQPTVVFV 128
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN--YNLSGdpLIHCLKLSGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 129 skkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRDKTIALIMnSSGSTGLPKGV 208
Cdd:cd05937 85 ----------------------------------------------------------DPDDPAILIY-TSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 209 ALPHR---TACVRFSHardpIFGNQiiPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELFLRSLQDYKIQS 284
Cdd:cd05937 106 AISWRrtlVTSNLLSH----DLNLK--NGDRTYTCMPLYHGTAAFLGACNcLMSGGTLALSRKFSASQFWKDVRDSGATI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 285 ALLVPTLFSFFAkSTLIDKYDLSNLHEIASGGApLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGK 364
Cdd:cd05937 180 IQYVGELCRYLL-STPPSPYDRDHKVRVAWGNG-LRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDFGAGAIGH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 365 VVP----FFEAKVV----DLDTGKTLGVNQRGeLCVRGP------MIM----------SGYVNNPEAT------NALIDK 414
Cdd:cd05937 258 HGLirrwKFENQVVlvkmDPETDDPIRDPKTG-FCVRAPvgepgeMLGrvpfknreafQGYLHNEDATesklvrDVFRKG 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110555473 415 DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAG--LPDDDaGELPAAVVVLE 488
Cdd:cd05937 337 DIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkVPGHD-GRAGCAAITLE 411
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-533 |
3.12e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.41 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 16 PLEDGTAGEQLHKAM-KRYALVPGTIA--FTDAHIevdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPV 92
Cdd:PRK12316 1995 TPEAYPRGPGVHQRIaEQAARAPEAIAvvFGDQHL----SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVAL 2070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 93 LGALFIGVAVAPANDIYNERELLNSMGISQPTVVfVSKKGLQKILNVQKKLPIIQkiiiMDSKTDYQGFqsmytfvtshl 172
Cdd:PRK12316 2071 LAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL-LTQRHLLERLPLPAGVARLP----LDRDAEWADY----------- 2134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 173 PPGFNEYDFVPEsfdrdkTIALIMNSSGSTGLPKGVALPHrTACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTT 252
Cdd:PRK12316 2135 PDTAPAVQLAGE------NLAYVIYTSGSTGLPKGVAVSH-GALVAHCQAAGERYE--LSPADCELQFMSFSFDGAHEQW 2205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 253 LGYLICGFRVVLM---YRFEEELFlRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLsNLHEIASGGAPLSKEVGEAVAK 329
Cdd:PRK12316 2206 FHPLLNGARVLIRddeLWDPEQLY-DEMERHGVTILDFPPVYLQQLAEHAERDGRPP-AVRVYCFGGEAVPAASLRLAWE 2283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 330 RFHLPGIRQGYGLTETTSAILITPEGDDKPGA-----VGKVVPFFEAKVVDLDTgKTLGVNQRGELCVRGPMIMSGYVNN 404
Cdd:PRK12316 2284 ALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGNRRAYILDADL-NLLAPGMAGELYLGGEGLARGYLNR 2362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 405 PEATNALIDKDGWLH-------SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpDDDA 477
Cdd:PRK12316 2363 PGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGAS 2441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 110555473 478 GELPAAVVVLEHGKTMTEKEIVDYVAsQVTTAKKLRGGVVFVDEVPKGLTGKLDAR 533
Cdd:PRK12316 2442 GKQLVAYVVPDDAAEDLLAELRAWLA-ARLPAYMVPAHWVVLERLPLNPNGKLDRK 2496
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
51-496 |
4.96e-20 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 93.42 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFmPVLGALF----IGVAVAPANDIYNereLLNSMGISQPTVV 126
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFF-ALTFALFkagaVPVLVDPGMGIKN---LKQCLAEAQPDAF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 127 F-VSKKGLQKILNVQKKLPIIQKIIIMDSKtdyqgFQSMYTFVTSHLPPGFNEYDFVPesFDRDKTiALIMNSSGSTGLP 205
Cdd:PRK09274 118 IgIPKAHLARRLFGWGKPSVRRLVTVGGRL-----LWGGTTLATLLRDGAAAPFPMAD--LAPDDM-AAILFTSGSTGTP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 206 KGVALPHRTACVRFSHARDpIFGnqIIPDTAILSVVPFhhgFGMFTtlgyLICGFRVVLMY-------RFEEELFLRSLQ 278
Cdd:PRK09274 190 KGVVYTHGMFEAQIEALRE-DYG--IEPGEIDLPTFPL---FALFG----PALGMTSVIPDmdptrpaTVDPAKLFAAIE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 279 DYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIR--QGYGLTE-------TTSAI 349
Cdd:PRK09274 260 RYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLP-PDAEilTPYGATEalpissiESREI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 350 L-----ITPEGDdkpGA-VGKVVPFFEAKVVDLDTG--------KTLGVNQRGELCVRGPMIMSGYVNNPEAT--NALID 413
Cdd:PRK09274 339 LfatraATDNGA---GIcVGRPVDGVEVRIIAISDApipewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATrlAKIPD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 414 KDG--WLHSGDIAYWDEDEHFFI----VDRLKSLIK-YKGYQVapaelESILLQHPNIFDAGVAGLPdDDAGELPAAVVV 486
Cdd:PRK09274 416 GQGdvWHRMGDLGYLDAQGRLWFcgrkAHRVETAGGtLYTIPC-----ERIFNTHPGVKRSALVGVG-VPGAQRPVLCVE 489
|
490
....*....|
gi 110555473 487 LEHGKTMTEK 496
Cdd:PRK09274 490 LEPGVACSKS 499
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
44-535 |
6.03e-20 |
|
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: 92.92 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 44 DAHIEVD----ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMG 119
Cdd:cd17656 3 DAVAVVFenqkLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 120 ISQPTVVfVSKKGLQKILNVQKKlpiiqkIIIMDSKTDYQGFQSMYTFVtshlppgFNEYDfvpesfdrdktIALIMNSS 199
Cdd:cd17656 83 DSGVRVV-LTQRHLKSKLSFNKS------TILLEDPSISQEDTSNIDYI-------NNSDD-----------LLYIIYTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 200 GSTGLPKGVALPHRTACVRFSHARD---PIFGNQIIPDTAILSVVPFHHGFGMFTTLG--YLIcgfrvvlmyRFEEELFL 274
Cdd:cd17656 138 GTTGKPKGVQLEHKNMVNLLHFEREktnINFSDKVLQFATCSFDVCYQEIFSTLLSGGtlYII---------REETKRDV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 275 RSLQDY----KIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPL--SKEVGEAVAKR-FHLpgiRQGYGLTET-- 345
Cdd:cd17656 209 EQLFDLvkrhNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLviTNEFKEMLHEHnVHL---HNHYGPSEThv 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 TSAILITPEgDDKP--GAVGKvvPFFEAKVVDLDTGKTL---GVnqRGELCVRGPMIMSGYVNNPEATNALIDKDGW--- 417
Cdd:cd17656 286 VTTYTINPE-AEIPelPPIGK--PISNTWIYILDQEQQLqpqGI--VGELYISGASVARGYLNRQELTAEKFFPDPFdpn 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 418 ---LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEhgKTMT 494
Cdd:cd17656 361 ermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME--QELN 438
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 110555473 495 EKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARKI 535
Cdd:cd17656 439 ISQLREYLAKQL-PEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
48-534 |
1.06e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 48 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVF 127
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLL 4653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 128 VSKKGLQKilnvqkkLPIIQKI--IIMDSKTDYQGFQSMYTFVTSHlppgfneydfvPESfdrdktIALIMNSSGSTGLP 205
Cdd:PRK12316 4654 TQSHLLQR-------LPIPDGLasLALDRDEDWEGFPAHDPAVRLH-----------PDN------LAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 206 KGVALPHRtACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM--YRFEEELFLRSLQDYKIQ 283
Cdd:PRK12316 4710 KGVAVSHG-SLVNHLHATGERYE--LTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRddSLWDPERLYAEIHEHRVT 4786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 284 SALLVPTLFSFFAKSTLIDKyDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT-SAILITPEGDDKPGA- 361
Cdd:PRK12316 4787 VLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTvTVLLWKARDGDACGAa 4865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 362 ---VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWLH-SGDIAYWDEDEH 431
Cdd:PRK12316 4866 ympIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALTaerfvpDPFGAPGGRLYrTGDLARYRADGV 4944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 432 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVlehgktmTEKEIVDYVASQVTTAKK 511
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVP-------QDPALADADEAQAELRDE 5017
|
490 500 510
....*....|....*....|....*....|....*.
gi 110555473 512 LRGGV-------------VFVDEVPKGLTGKLDaRK 534
Cdd:PRK12316 5018 LKAALrerlpeymvpahlVFLARMPLTPNGKLD-RK 5052
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
52-457 |
4.85e-19 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 90.85 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 131
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 GLQKILNVQKKLPIIQKIIIM------DSKTDYQGFQSMYTFVTSHLPPG-FNEYDFvpeSFDRDKTIALIMNSSGSTGL 204
Cdd:PLN02614 161 KISELFKTCPNSTEYMKTVVSfggvsrEQKEEAETFGLVIYAWDEFLKLGeGKQYDL---PIKKKSDICTIMYTSGTTGD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 205 PKGVALPHR------TACVRFSHARDPIFGNQIIpdtaILSVVPFHHGFGM-----FTTLGYLIcGFrvvlmYRFEEELF 273
Cdd:PLN02614 238 PKGVMISNEsivtliAGVIRLLKSANAALTVKDV----YLSYLPLAHIFDRvieecFIQHGAAI-GF-----WRGDVKLL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 274 LRSLQDYKIQSALLVPTLFS--------------FFAK-----------------------STLIDKYDLS--------N 308
Cdd:PLN02614 308 IEDLGELKPTIFCAVPRVLDrvysglqkklsdggFLKKfvfdsafsykfgnmkkgqshveaSPLCDKLVFNkvkqglggN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 309 LHEIASGGAPLSKEVgEAVAKRFHLPGIRQGYGLTETTSAILIT-PEGDDKPGAVGKVVPFFEAKVVDLDTGK--TLGVN 385
Cdd:PLN02614 388 VRIILSGAAPLASHV-ESFLRVVACCHVLQGYGLTESCAGTFVSlPDELDMLGTVGPPVPNVDIRLESVPEMEydALAST 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110555473 386 QRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESI 457
Cdd:PLN02614 467 PRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENI 538
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
193-457 |
6.60e-19 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 90.54 E-value: 6.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVAlphrtacvrfsHARDPIFGN--QI------IPDTAILSVVPFHHGFGMftTLGY---LICGFR 261
Cdd:PRK08043 368 ALILFTSGSEGHPKGVV-----------HSHKSLLANveQIktiadfTPNDRFMSALPLFHSFGL--TVGLftpLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 262 VVLM-----YRFEEELFlrslqdYKIQSALLvptlfsfFAKSTLI-------DKYDLSNLHEIASGGAPLSKEVGEAVAK 329
Cdd:PRK08043 435 VFLYpsplhYRIVPELV------YDRNCTVL-------FGTSTFLgnyarfaNPYDFARLRYVVAGAEKLQESTKQLWQD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 330 RFhlpGIR--QGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtgktlGVNQRGELCVRGPMIMSGY--VNN- 404
Cdd:PRK08043 502 KF---GLRilEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVP-----GIEQGGRLQLKGPNIMNGYlrVEKp 573
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 110555473 405 -----PEATNALIDKD-GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVApaeLESI 457
Cdd:PRK08043 574 gvlevPTAENARGEMErGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVS---LEMV 629
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
192-535 |
9.64e-19 |
|
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: 88.77 E-value: 9.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRtACVRFSHARDPIFGNQIIPDTAILSVVPFH-HGFGMFTtlgYLICGFRVVLMYRfEE 270
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHH-NLVNLCEWHRPYFGVTPADKSLVYASFSFDaSAWEIFP---HLTAGAALHVVPS-ER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 271 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLidKYDLSNLHEIASGGAPLSKevgeAVAKRFHLpgiRQGYGLTETTsaIL 350
Cdd:cd17645 181 RLDLDALNDYFNQEGITISFLPTGAAEQFM--QLDNQSLRVLLTGGDKLKK----IERKGYKL---VNNYGPTENT--VV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 351 ITPEGDDKPGA---VGKvvPFFEAKVVDLDTGKTL---GVNqrGELCVRGPMIMSGYVNNPEAT------NALIDKDGWL 418
Cdd:cd17645 250 ATSFEIDKPYAnipIGK--PIDNTRVYILDEALQLqpiGVA--GELCIAGEGLARGYLNRPELTaekfivHPFVPGERMY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 419 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV----LEHG--KT 492
Cdd:cd17645 326 RTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTapeeIPHEelRE 405
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 110555473 493 MTEKEIVDYVASQVttakklrggVVFVDEVPKGLTGKLDARKI 535
Cdd:cd17645 406 WLKNDLPDYMIPTY---------FVHLKALPLTANGKVDRKAL 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
48-534 |
1.15e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.61 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 48 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERELLNSMgisqptvvf 127
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPL-DPEYPRERLAYM--------- 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 128 VSKKGLQKIL---NVQKKLPII--QKIIIMDSKTDYQGFQSMYTfvtshlppgfneydfvPESFDRDKTIALIMNSSGST 202
Cdd:PRK12467 1667 IEDSGIELLLtqsHLQARLPLPdgLRSLVLDQEDDWLEGYSDSN----------------PAVNLAPQNLAYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 203 GLPKGVALPHrTACVRFSHARDPIFgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMyRFEE----ELFLRSLQ 278
Cdd:PRK12467 1731 GRPKGAGNRH-GALVNRLCATQEAY--QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIA-PPGAhrdpEQLIQLIE 1806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 279 DYKIQSALLVPTLFSFFAKSTLIDKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT------SAILIT 352
Cdd:PRK12467 1807 RQQVTTLHFVPSMLQQLLQMDEQVEHPLS-LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvdvthwTCRRKD 1885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 353 PEGDDkpgAVGKVVPFFEAKVVDLDTGKTL---GVnqRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWLH-SGD 422
Cdd:PRK12467 1886 LEGRD---SVPIGQPIANLSTYILDASLNPvpiGV--AGELYLGGVGLARGYLNRPALTaerfvaDPFGTVGSRLYrTGD 1960
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 423 IAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVagLPDDDAG--ELPAAVVVlehgktmTEKEIVD 500
Cdd:PRK12467 1961 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDGANgkQLVAYVVP-------TDPGLVD 2031
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 110555473 501 YVASQVTTAKKLRGGV-------------VFVDEVPKGLTGKLDaRK 534
Cdd:PRK12467 2032 DDEAQVALRAILKNHLkaslpeymvpahlVFLARMPLTPNGKLD-RK 2077
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
343-538 |
1.47e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 89.04 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 343 TETtSAILITP-EG--DDKPGAVGKvvPFF--EAKVVDlDTGKTLGVNQRGELCVRGP---MIMSGYvNNPEAtnaLID- 413
Cdd:PRK00174 405 TET-GGIMITPlPGatPLKPGSATR--PLPgiQPAVVD-EEGNPLEGGEGGNLVIKDPwpgMMRTIY-GDHER---FVKt 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 414 -----KDGWLhSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLE 488
Cdd:PRK00174 477 yfstfKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLK 555
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110555473 489 HGKTMTE---KEIVDYVASQV---TTAKKLRggvvFVDEVPKGLTGKLDARKIREI 538
Cdd:PRK00174 556 GGEEPSDelrKELRNWVRKEIgpiAKPDVIQ----FAPGLPKTRSGKIMRRILRKI 607
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
185-478 |
3.39e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 87.56 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 185 SFDRDKT-IALIMNSSGSTGLPKGVALPHRT------ACVRFSharDPIfgnqiiPDTAILSVVPFHHGFGMFT-TLGYL 256
Cdd:PRK06334 177 VSDKDPEdVAVILFTSGTEKLPKGVPLTHANllanqrACLKFF---SPK------EDDVMMSFLPPFHAYGFNScTLFPL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 257 ICGFRVVLMYR-FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPG 335
Cdd:PRK06334 248 LSGVPVVFAYNpLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 336 IRQGYGLTETTSAILITPEGDDK-PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYV-NNPEATNALID 413
Cdd:PRK06334 328 LRQGYGTTECSPVITINTVNSPKhESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELG 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110555473 414 KDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHpnifdagvAGLPDDDAG 478
Cdd:PRK06334 408 GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNAADHA 464
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
51-473 |
3.68e-18 |
|
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: 87.02 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiYNER--ELLNSMGISQPTVVFV 128
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN--YNLRgeSLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 129 skkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRdktiALIMNSSGSTGLPKGV 208
Cdd:cd05940 82 ----------------------------------------------------------DA----ALYIYTSGTTGLPKAA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 209 ALPHRTaCVRFSHARDPIFGNqiIPDTAILSVVPFHHGFGMFTTLG-YLICGFRVVLMYRFEEELFLRSLQDYKIqsall 287
Cdd:cd05940 100 IISHRR-AWRGGAFFAGSGGA--LPSDVLYTCLPLYHSTALIVGWSaCLASGATLVIRKKFSASNFWDDIRKYQA----- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 288 vpTLFSFFAKstlIDKY-------DLSNLHEI-ASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAiLITPEGddKP 359
Cdd:cd05940 172 --TIFQYIGE---LCRYllnqppkPTERKHKVrMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSG-FINFFG--KP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 360 GAVGkVVPFFEAKV-------VDLDTGKTL----------GVNQRGELCVR----GPMImsGYVNNPEAT-----NALID 413
Cdd:cd05940 244 GAIG-RNPSLLRKVaplalvkYDLESGEPIrdaegrcikvPRGEPGLLISRinplEPFD--GYTDPAATEkkilrDVFKK 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 414 KDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLP 473
Cdd:cd05940 321 GDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
51-534 |
3.89e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.68 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYnERELLNSMGISQPTVVFVSK 130
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY-PQDRLAYMLDDSGVRLLLTQ 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLQKILNVQKKLPIIqkiiIMDSKTDYqgfqsmytfvTSHLPPGFNEYDFVPESfdrdktIALIMNSSGSTGLPKGVAL 210
Cdd:PRK12467 617 SHLLAQLPVPAGLRSL----CLDEPADL----------LCGYSGHNPEVALDPDN------LAYVIYTSGSTGQPKGVAI 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 211 PHRtACVRF--SHARDPifgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR---FEEELFLRSLQDYKIQSA 285
Cdd:PRK12467 677 SHG-ALANYvcVIAERL----QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVL 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 286 LLVPTLFSFFAKSTLIDKydLSNLHEIASGGAPLskEVGEAVAKRFHLPGIR--QGYGLTETTSAILITPEGDDK--PGA 361
Cdd:PRK12467 752 KIVPSHLQALLQASRVAL--PRPQRALVCGGEAL--QVDLLARVRALGPGARliNHYGPTETTVGVSTYELSDEErdFGN 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 362 VGKVVPFFEAKVVDLDTG-KTLGVNQRGELCVRGPMIMSGYVNNP--EATNALIDKDG-----WLHSGDIAYWDEDEHFF 433
Cdd:PRK12467 828 VPIGQPLANLGLYILDHYlNPVPVGVVGELYIGGAGLARGYHRRPalTAERFVPDPFGadggrLYRTGDLARYRADGVIE 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 434 IVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVV---VLEHGKTMTEKEIVDYVASQVTTAK 510
Cdd:PRK12467 908 YLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaaVADGAEHQATRDELKAQLRQVLPDY 987
|
490 500
....*....|....*....|....
gi 110555473 511 KLRGGVVFVDEVPKGLTGKLDaRK 534
Cdd:PRK12467 988 MVPAHLLLLDSLPLTPNGKLD-RK 1010
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
62-495 |
6.67e-18 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 86.46 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 62 RLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiynerellnsmgiSQPTVVFvskkgLQKILNVQK 141
Cdd:PRK09029 40 QLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLN--------------PQLPQPL-----LEELLPSLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 142 klpiIQKIIIMDSKTDYQGfqsmytfVTSHLPPGFNEYDFVPESFDRDKTIALimnSSGSTGLPKGVALPHRT------- 214
Cdd:PRK09029 101 ----LDFALVLEGENTFSA-------LTSLHLQLVEGAHAVAWQPQRLATMTL---TSGSTGLPKAAVHTAQAhlasaeg 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 215 --ACVRFSHArdpifgnqiipDTAILSVvPFHHGFGMFTTLGYLICGFRVVLMyrfEEELFLRSLQDykIQSALLVPT-- 290
Cdd:PRK09029 167 vlSLMPFTAQ-----------DSWLLSL-PLFHVSGQGIVWRWLYAGATLVVR---DKQPLEQALAG--CTHASLVPTql 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 291 --LFSFFAKSTLidkydlsnLHEIASGGAPLSKEVGEAVAKRfhlpGIRQ--GYGLTETTSAILITpEGDDKPGaVGKVV 366
Cdd:PRK09029 230 wrLLDNRSEPLS--------LKAVLLGGAAIPVELTEQAEQQ----GIRCwcGYGLTEMASTVCAK-RADGLAG-VGSPL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 367 PFFEAKVVDldtgktlgvnqrGELCVRGPMIMSGYVNNPEATnALIDKDGWLHSGDIAYWDEDEhFFIVDRLKSLIKYKG 446
Cdd:PRK09029 296 PGREVKLVD------------GEIWLRGASLALGYWRQGQLV-PLVNDEGWFATRDRGEWQNGE-LTILGRLDNLFFSGG 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 110555473 447 YQVAPAELESILLQHPNIFDAGVagLPDDDA--GELPAAVVVLEHGKTMTE 495
Cdd:PRK09029 362 EGIQPEEIERVINQHPLVQQVFV--VPVADAefGQRPVAVVESDSEAAVVN 410
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
189-537 |
6.88e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 85.48 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 189 DKTIALIMNSSGSTGLPKGvALPHRTACVRFSHARDPIFGNqiiPDTAILsVVPFHHGFGMFTTLGYLICGFRVV---LM 265
Cdd:PRK07824 34 DDDVALVVATSGTTGTPKG-AMLTAAALTASADATHDRLGG---PGQWLL-ALPAHHIAGLQVLVRSVIAGSEPVeldVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 YRFEEELFLRSLQ----DYKIQSalLVPTLFSFfAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKrfhlPGIR--QG 339
Cdd:PRK07824 109 AGFDPTALPRAVAelggGRRYTS--LVPMQLAK-ALDDPAATAALAELDAVLVGGGPAPAPVLDAAAA----AGINvvRT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 340 YGLTETTSailitpegddkpGAVGKVVPFFEAKVVDLDTGKTLGvnqrgelcvrGPMIMSGYVNNPEatNALIDKDGWLH 419
Cdd:PRK07824 182 YGMSETSG------------GCVYDGVPLDGVRVRVEDGRIALG----------GPTLAKGYRNPVD--PDPFAEPGWFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 420 SGDIAYWDeDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 499
Cdd:PRK07824 238 TDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALR 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 110555473 500 DYVASQ--VTTA-KKLRggvvFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK07824 317 AHVARTldRTAApRELH----VVDELPRRGIGKVDRRALVR 353
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
51-505 |
7.47e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 86.85 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiYNERE--LLNSMGISQPTVVFV 128
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN--TQQRGavLAHSLNLVDAKHLIV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 129 SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQgfqsmytfvtshlPPGFNEYDFVPESFDRD----------KTIALIMNS 198
Cdd:PRK08279 141 GEELVEAFEEARADLARPPRLWVAGGDTLDD-------------PEGYEDLAAAAAGAPTTnpasrsgvtaKDTAFYIYT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 SGSTGLPKGValphrtacvRFSHAR----DPIFGN--QIIPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLMYRFEEE 271
Cdd:PRK08279 208 SGTTGLPKAA---------VMSHMRwlkaMGGFGGllRLTPDDVLYCCLPLYHNTGGTVAWSSVLAaGATLALRRKFSAS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 272 LFLRSLQDYKIqsallvpTLFSFFAKstlIDKYDLS----------NLHEIAsgGAPLSKEVGEAVAKRFHLPGIRQGYG 341
Cdd:PRK08279 279 RFWDDVRRYRA-------TAFQYIGE---LCRYLLNqppkptdrdhRLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 342 LTETTSAiLITPEGddKPGAVGKVvPFFEAK---VV--DLDTGKTL----------GVNQRGELCV----RGPMimSGYv 402
Cdd:PRK08279 347 ASEGNVG-FINVFN--FDGTVGRV-PLWLAHpyaIVkyDVDTGEPVrdadgrcikvKPGEVGLLIGritdRGPF--DGY- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 403 NNPEATNALI------DKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAG--LPD 474
Cdd:PRK08279 420 TDPEASEKKIlrdvfkKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGveVPG 499
|
490 500 510
....*....|....*....|....*....|...
gi 110555473 475 DD--AGelpAAVVVLEHGKTMTEKEIVDYVASQ 505
Cdd:PRK08279 500 TDgrAG---MAAIVLADGAEFDLAALAAHLYER 529
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
192-479 |
1.11e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.53 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRTACVRFSHARDPiFGNQIIPDTAILSVVPFHHGFGMFTTLGYLI-CGFRVVLM---YR 267
Cdd:PRK05691 168 IAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHG-FGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIfSGVPCVLMspaYF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 268 FEEEL-FLRSLQDY--KIQSAllvPT----LFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQ-- 338
Cdd:PRK05691 247 LERPLrWLEAISEYggTISGG---PDfayrLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPds 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 339 ---GYGLTETTSAILITPEG--------DDK--------PGAvGKVV-------PFFEAKVVDLDTGKTLGVNQRGELCV 392
Cdd:PRK05691 324 ffaSYGLAEATLFVSGGRRGqgipalelDAEalarnraePGT-GSVLmscgrsqPGHAVLIVDPQSLEVLGDNRVGEIWA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 393 RGPMIMSGYVNNPEAT-NALIDKDG--WLHSGDIAYWDEDEhFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAG- 468
Cdd:PRK05691 403 SGPSIAHGYWRNPEASaKTFVEHDGrtWLRTGDLGFLRDGE-LFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGr 481
|
330
....*....|.
gi 110555473 469 VAGLPDDDAGE 479
Cdd:PRK05691 482 VAAFAVNHQGE 492
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-533 |
1.20e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 15 YPLEDGtageqLHKAMK-RYALVPGTIAFtdAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVL 93
Cdd:PRK12316 507 YPLQRG-----VHRLFEeQVERTPEAPAL--AFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 94 GALFIGVAVAPANDIYNErELLNSMgisqptvvfVSKKGLQKILN---VQKKLPIIQKIIIMDsktdyqgfqsmYTFVTS 170
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPA-ERLAYM---------LEDSGVQLLLSqshLGRKLPLAAGVQVLD-----------LDRPAA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 171 HLPpgfNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMF 250
Cdd:PRK12316 639 WLE---GYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY---GLGVGDTVLQKTPFSFDVSVW 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 251 TTLGYLICGFRVVLM---YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDkyDLSNLHEIASGGAPLSKEVGEAV 327
Cdd:PRK12316 713 EFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQV 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 328 AKRFHLPGIRQGYGLTETTsaILIT-----PEGDDKPgAVGKVVPFFEAKVVDLDTGKT-LGVnqRGELCVRGPMIMSGY 401
Cdd:PRK12316 791 FAKLPQAGLYNLYGPTEAA--IDVThwtcvEEGGDSV-PIGRPIANLACYILDANLEPVpVGV--LGELYLAGRGLARGY 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 402 VNNPEAT------NALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGL--- 472
Cdd:PRK12316 866 HGRPGLTaerfvpSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVdgk 945
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110555473 473 -------PDDDAGELPAAVvvlehgKTMTEKEIVDY-VASQvttakklrggVVFVDEVPKGLTGKLDAR 533
Cdd:PRK12316 946 qlvgyvvLESEGGDWREAL------KAHLAASLPEYmVPAQ----------WLALERLPLTPNGKLDRK 998
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
31-509 |
1.73e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 85.76 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 31 KRYALVPGTIAFTDAHIEVD-------ITYAEYFEMSVRLAEAMKRYGlNTNHRIVVCSENSLQFFMPVLGALFIG-VAV 102
Cdd:PRK05850 9 ERASLQPDDAAFTFIDYEQDpagvaetLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGlIAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 103 ---APANDIYNERelLNS-MGISQPTVVFVSKKglqkilnvqkklpiiqkiiIMDSKTDYQGFQSMYTfvtshlPPGFNE 178
Cdd:PRK05850 88 plsVPQGGAHDER--VSAvLRDTSPSVVLTTSA-------------------VVDDVTEYVAPQPGQS------APPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 179 YDF---------VPESFDRDKTiALIMNSSGSTGLPKGVALPHRTACVRFSH-ARD--PIFGNQIIPDTAILSVVPFHHG 246
Cdd:PRK05850 141 VDLldldsprgsDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFEQlMSDyfGDTGGVPPPDTTVVSWLPFYHD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 247 FGMFttLGY---LICGFRVVLMyrfEEELFLRSLQDYkIQSALLVPTLFSF---FA------KSTLID--KYDLSNLHEI 312
Cdd:PRK05850 220 MGLV--LGVcapILGGCPAVLT---SPVAFLQRPARW-MQLLASNPHAFSAapnFAfelavrKTSDDDmaGLDLGGVLGI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 313 ASGgaplSKEVGEAVAKRF-------HLP--GIRQGYGLTETTsAILITPEGDDKPGAV---------GKVVPF-FEA-- 371
Cdd:PRK05850 294 ISG----SERVHPATLKRFadrfapfNLRetAIRPSYGLAEAT-VYVATREPGQPPESVrfdyeklsaGHAKRCeTGGgt 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 372 -------------KVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATN-----ALIDK-----DG-WLHSGDIAYWD 427
Cdd:PRK05850 369 plvsygsprsptvRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETErtfgaTLVDPspgtpEGpWLRTGDLGFIS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 428 EDEhFFIVDRLKSLIKYKGYQVAPAELESILLQhpnIFDAGVAGL--PDDDAGELPAAVVVLEHGKTMTE-KEIVDYVAS 504
Cdd:PRK05850 449 EGE-LFIVGRIKDLLIVDGRNHYPDDIEATIQE---ITGGRVAAIsvPDDGTEKLVAIIELKKRGDSDEEaMDRLRTVKR 524
|
....*
gi 110555473 505 QVTTA 509
Cdd:PRK05850 525 EVTSA 529
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
195-538 |
2.79e-17 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 85.00 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 195 IMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQiipdtailsvvpfhHGFGMFTT-------------LGYLICGFR 261
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGK--------------AGETFFCAsdigwvvghsyivYAPLLAGMA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 262 VVlMYrfeEELFLRS--------LQDYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRF 331
Cdd:PRK10524 304 TI-MY---EGLPTRPdagiwwriVEKYKVNRMFSAPTAIRVLKKQdpALLRKHDLSSLRALFLAGEPLDEPTASWISEAL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 332 HLPgIRQGYGLTETTSAIL-ITPEGDDKP---GAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPM----------- 396
Cdd:PRK10524 380 GVP-VIDNYWQTETGWPILaIARGVEDRPtrlGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLppgcmqtvwgd 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 397 ---IMSGYvnnpeatnalidkdgWLHSGDIAY----W---DEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFD 466
Cdd:PRK10524 459 ddrFVKTY---------------WSLFGRQVYstfdWgirDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 467 AGVAGLPDDDAGELPAAVVVLEHGKTMT--------EKEIVDYVASQV-TTAKKLRggVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK10524 524 VAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLgAVARPAR--VWFVSALPKTRSGKLLRRAIQA 601
|
.
gi 110555473 538 I 538
Cdd:PRK10524 602 I 602
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
49-531 |
3.61e-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: 84.06 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 49 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerelLNSMGISQPTVVFV 128
Cdd:cd17654 15 TTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAP----------IDPASPEQRSLTVM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 129 SKKGLQKIL----NVQKKLPIIQKIIIMDSKTDYqgfqsmytfvtshlppgfneydfvpesfdrdkTIALIMNSSGSTGL 204
Cdd:cd17654 85 KKCHVSYLLqnkeLDNAPLSFTPEHRHFNIRTDE--------------------------------CLAYVIHTSGTTGT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 205 PKGVALPHRtaCVR--FSHARD--PIFGNQIIPDTAIL----SVVPFhhgFGMFTTLGYLICgfrVVLMYRFEEELFLRS 276
Cdd:cd17654 133 PKIVAVPHK--CILpnIQHFRSlfNITSEDILFLTSPLtfdpSVVEI---FLSLSSGATLLI---VPTSVKVLPSKLADI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 277 L-QDYKIQSALLVPTLFSFF----AKSTLIDKydLSNLHEIASGGAPLSKEVgEAVAKRFHLPGIR--QGYGLTETTS-A 348
Cdd:cd17654 205 LfKRHRITVLQATPTLFRRFgsqsIKSTVLSA--TSSLRVLALGGEPFPSLV-ILSSWRGKGNRTRifNIYGITEVSCwA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 349 IL-ITPEGdDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGpmIMSGYVNNPEATnalidkdgWLHSGDIAYWD 427
Cdd:cd17654 282 LAyKVPEE-DSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRVC--ILDDEVTVPKGT--------MRATGDFVTVK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 428 EDEHFFiVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAgLPDDdagELPAAVVVLEHGKTMTEKEIVDYVASqvt 507
Cdd:cd17654 351 DGELFF-LGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT-LSDQ---QRLIAFIVGESSSSRIHKELQLTLLS--- 422
|
490 500
....*....|....*....|....
gi 110555473 508 tAKKLRGGVVFVDEVPKGLTGKLD 531
Cdd:cd17654 423 -SHAIPDTFVQIDKLPLTSHGKVD 445
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
77-455 |
1.29e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 83.24 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 77 RIVVCSENSLQFFMPVLGALFIG-VAV---APANDIYNEReLLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQK--II 150
Cdd:PRK07769 81 RVAILAPQNLDYLIAFFGALYAGrIAVplfDPAEPGHVGR-LHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKERprVI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 151 IMDSKTDYQGfqSMYtfvtshlppgfneydfVPESFDRDkTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQ 230
Cdd:PRK07769 160 AVDAVPDEVG--ATW----------------VPPEANED-TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 231 iipDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---------YRFEEELFLRSLQDYKIQSALlvPTlFSF-FAKSTL 300
Cdd:PRK07769 221 ---GDRGVSWLPFFHDMGLITVLLPALLGHYITFMspaafvrrpGRWIRELARKPGGTGGTFSAA--PN-FAFeHAAARG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 301 IDK-----YDLSNLHEIASGGAPLS----KEVGEAVAKrFHLP--GIRQGYGLTETTSAILITPEGD------------- 356
Cdd:PRK07769 295 LPKdgeppLDLSNVKGLLNGSEPVSpasmRKFNEAFAP-YGLPptAIKPSYGMAEATLFVSTTPMDEeptviyvdrdeln 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 357 ---------DKPGAV-----GKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALI---------- 412
Cdd:PRK07769 374 agrfvevpaDAPNAVaqvsaGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlse 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 110555473 413 -------DKDGWLHSGDIAYWdEDEHFFIVDRLKSLIKYKGYQVAPAELE 455
Cdd:PRK07769 454 shaegapDDALWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
453-529 |
1.32e-16 |
|
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: 74.50 E-value: 1.32e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110555473 453 ELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGK 529
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPK-EVVFVDELPKTRSGK 76
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
48-534 |
1.94e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.29 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 48 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERELLNSMgisqptvvf 127
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPL-DPEYPRERLAYM--------- 3187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 128 VSKKGLQKILNVQ---KKLPIIQ--KIIIMDsKTDYQGfqsmytfvtshlppgfnEYDFVPESFDRDKTIALIMNSSGST 202
Cdd:PRK12467 3188 IEDSGVKLLLTQAhllEQLPAPAgdTALTLD-RLDLNG-----------------YSENNPSTRVMGENLAYVIYTSGST 3249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 203 GLPKGVALPHrTACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFEEELFlRSLQD 279
Cdd:PRK12467 3250 GKPKGVGVRH-GALANHLCWIAEAYE--LDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRdndLWDPEELW-QAIHA 3325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 280 YKIQSALLVPTLFSFFAKSTliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT-SAILITPEGDDK 358
Cdd:PRK12467 3326 HRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVvTVTLWKCGGDAV 3403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 359 PGA----VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWLH-SGDIAYWD 427
Cdd:PRK12467 3404 CEApyapIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTaerfvaDPFSGSGGRLYrTGDLARYR 3482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 428 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK-------EIVD 500
Cdd:PRK12467 3483 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETlrdhlaaSLPD 3562
|
490 500 510
....*....|....*....|....*....|....*
gi 110555473 501 Y-VASQvttakklrggVVFVDEVPKGLTGKLDaRK 534
Cdd:PRK12467 3563 YmVPAQ----------LLVLAAMPLGPNGKVD-RK 3586
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-534 |
6.17e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.93 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 15 YPLEDGTagEQLHKAMKRYALVPGTIAFTDAHIevdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLG 94
Cdd:PRK12316 3053 YPLERGV--HRLFEEQVERTPDAVALAFGEQRL----SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLA 3126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 95 ALFIGVAVAPANDIYNERELLNSMGISqptvvfvskkGLQKILNVQK-KLPIIQKIIIMDSKTDYQGFQSMYtfvtshlp 173
Cdd:PRK12316 3127 ILKAGGAYVPLDPEYPEERLAYMLEDS----------GAQLLLSQSHlRLPLAQGVQVLDLDRGDENYAEAN-------- 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 174 pgfneydfvPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTL 253
Cdd:PRK12316 3189 ---------PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALS---NHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELF 3256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 254 GYLICGFRVVLMYRfEEELFLRSLQDYKIQSALLVPTLFSFFAKSTL--IDKYDLSNLHEIASGGAPLSkevGEAVAKRF 331
Cdd:PRK12316 3257 WPLMSGARVVLAGP-EDWRDPALLVELINSEGVDVLHAYPSMLQAFLeeEDAHRCTSLKRIVCGGEALP---ADLQQQVF 3332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 332 HLPGIRQGYGLTETTSAILITPEGDDKPGA--VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT- 408
Cdd:PRK12316 3333 AGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTa 3411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 409 -----NALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAG----------LP 473
Cdd:PRK12316 3412 erfvpDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAvdgrqlvayvVP 3491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110555473 474 DDDAGELPAAVvvlehgKTMTEKEIVDY-VASQvttakklrggVVFVDEVPKGLTGKLDaRK 534
Cdd:PRK12316 3492 EDEAGDLREAL------KAHLKASLPEYmVPAH----------LLFLERMPLTPNGKLD-RK 3536
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
37-533 |
8.83e-16 |
|
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: 80.01 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerelln 116
Cdd:cd12114 1 PDATAVICG--DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVP------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 117 sMGISQPtvvfvsKKGLQKILNVQKklpiiQKIIIMDSkTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTiALIM 196
Cdd:cd12114 67 -VDIDQP------AARREAILADAG-----ARLVLTDG-PDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDL-AYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 197 NSSGSTGLPKGVALPHRtACV--------RFshardpifgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRF 268
Cdd:cd12114 133 FTSGSTGTPKGVMISHR-AALntildinrRF----------AVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEE---LFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGG--APLSKEvgEAVAKRFhlPGIRQ---Gy 340
Cdd:cd12114 202 RRRdpaHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwIPLDLP--ARLRALA--PDARLislG- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 341 GLTETT--SAILITPEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA--LIDK 414
Cdd:cd12114 277 GATEASiwSIYHPIDEVPPDWRSIpyGRPLANQRYRVLD-PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAArfVTHP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 415 DG--WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELpAAVVVLEHGKT 492
Cdd:cd12114 356 DGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRL-AAFVVPDNDGT 434
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 110555473 493 MTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDAR 533
Cdd:cd12114 435 PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
192-533 |
1.58e-15 |
|
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: 79.05 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGNQIIPdTAILSVVPFhhGFGMFTT--LGYLICGFRVVLM---Y 266
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHRNV-AHAAHAWRREYELDSFP-VRLLQMASF--SFDVFAGdfARSLLNGGTLVICpdeV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 267 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhLPGIR--QGYGLTE 344
Cdd:cd17650 171 KLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARF-GQGMRiiNSYGVTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 345 TTSAILITPEGDDKPGA-----VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALID 413
Cdd:cd17650 250 ATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTaerfveNPFAP 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 414 KDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHgkTM 493
Cdd:cd17650 329 GERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA--TL 406
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 110555473 494 TEKEIVDYVASQVTTAkKLRGGVVFVDEVPKGLTGKLDAR 533
Cdd:cd17650 407 NTAELRAFLAKELPSY-MIPSYYVQLDALPLTPNGKVDRR 445
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
51-537 |
1.71e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.21 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 51 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 130
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 131 KGLQKILNVQKKLPIIQKIIIMDSKTDYqgfqsmytfvtshlPPGFNEYDfvpesfdrdKTIALIMNSSGSTGLPKGVAL 210
Cdd:PRK05691 1237 HLLERLPQAEGVSAIALDSLHLDSWPSQ--------------APGLHLHG---------DNLAYVIYTSGSTGQPKGVGN 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 211 PHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEE---ELFLRSLQDYKIQSALL 287
Cdd:PRK05691 1294 THAALAERLQWMQATY---ALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHrdpQRIAELVQQYGVTTLHF 1370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 288 VPTLFSFFAKSTLIDkyDLSNLHEIASGGAPLSKEVGEAVAKRfhLPGIR--QGYGLTETtsAILIT------PEGDDKP 359
Cdd:PRK05691 1371 VPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQR--LPQVQlhNRYGPTET--AINVThwqcqaEDGERSP 1444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 360 gaVGKVVPFFEAKVVDLDTGKT-LGVnqRGELCVRGPMIMSGYVNNP--EATNALIDKDG-----WLHSGDIAYWDEDEH 431
Cdd:PRK05691 1445 --IGRPLGNVLCRVLDAELNLLpPGV--AGELCIGGAGLARGYLGRPalTAERFVPDPLGedgarLYRTGDRARWNADGA 1520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 432 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAgLPDDDAGE--------LPAAVVVLEHGKTMTEKEIVDY-V 502
Cdd:PRK05691 1521 LEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAqlvgyytgEAGQEAEAERLKAALAAELPEYmV 1599
|
490 500 510
....*....|....*....|....*....|....*
gi 110555473 503 ASQvttakklrggVVFVDEVPKGLTGKLDARKIRE 537
Cdd:PRK05691 1600 PAQ----------LIRLDQMPLGPSGKLDRRALPE 1624
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
190-535 |
4.92e-15 |
|
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: 77.44 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 190 KTIALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---Y 266
Cdd:cd17648 94 TDLAYAIYTSGTTGKPKGVLVEHGSV-VNLRTSLSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPpdeM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 267 RFEEELFLRSLQDYKIqsallvpTLFSffAKSTLIDKYDLS---NLHEIASGGAPLSKEVGEAVAKRFhlPG-IRQGYGL 342
Cdd:cd17648 173 RFDPDRFYAYINREKV-------TYLS--GTPSVLQQYDLArlpHLKRVDAAGEEFTAPVFEKLRSRF--AGlIINAYGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 343 TETTSAILITPEGDDKP--GAVGKVVPFFEAKVVDLDTgKTLGVNQRGELCVRGPMIMSGYVNNPEAT------------ 408
Cdd:cd17648 242 TETTVTNHKRFFPGDQRfdKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTaerflpnpfqte 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 409 -------NALIDKDG----WLHSGDIAYwdedehffiVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVagLPDDDA 477
Cdd:cd17648 321 qerargrNARLYKTGdlvrWLPSGELEY---------LGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAV--VAKEDA 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110555473 478 GELPAAVV-------VLEHGkTMTEKEIVDYVASQVTTAkKLRGGVVFVDEVPKGLTGKLDARKI 535
Cdd:cd17648 390 SQAQSRIQkylvgyyLPEPG-HVPESDLLSFLRAKLPRY-MVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
37-535 |
5.70e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 77.63 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 37 PGTIAFtdAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSlqFFMPV--LGALFIGVAVAPAnDIYNEREL 114
Cdd:PRK04813 16 PDFPAY--DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMS--PEMLAtfLGAVKAGHAYIPV-DVSSPAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 115 LNS-MGISQPTVVFVSKKGLQKILNVqkklPIIQKIIIMDSKtdyqgfqsmytfvtshlppgFNEYDFVPESFDRDKTIA 193
Cdd:PRK04813 91 IEMiIEVAKPSLIIATEELPLEILGI----PVITLDELKDIF--------------------ATGNPYDFDHAVKGDDNY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMNSSGSTGLPKGVALPHRT-------ACVRFSHARDPIFGNQIiP---DTAILSVVPfhhgfgMFTTLGYLICGFRVV 263
Cdd:PRK04813 147 YIIFTSGTTGKPKGVQISHDNlvsftnwMLEDFALPEGPQFLNQA-PysfDLSVMDLYP------TLASGGTLVALPKDM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 264 LMyRFEEeLFlRSLQDYKI----------QSALLVPTLfsffakstliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHL 333
Cdd:PRK04813 220 TA-NFKQ-LF-ETLPQLPInvwvstpsfaDMCLLDPSF----------NEEHLPNLTHFLFCGEELPHKTAKKLLERFPS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 334 PGIRQGYGLTETT---SAILITPEGDDK--PGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT 408
Cdd:PRK04813 287 ATIYNTYGPTEATvavTSIEITDEMLDQykRLPIGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 409 N-ALIDKDGW--LHSGDIAYWDeDEHFFIVDRLKSLIKYKGYQVapaELESI---LLQHPNIFDAGVAGLPDDDAGELPA 482
Cdd:PRK04813 366 AeAFFTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRI---ELEEIeqnLRQSSYVESAVVVPYNKDHKVQYLI 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110555473 483 AVVVLEHGKtmTEKEIvdyvasQVTTA--KKLRGGV---------VFVDEVPKGLTGKLDARKI 535
Cdd:PRK04813 442 AYVVPKEED--FEREF------ELTKAikKELKERLmeymiprkfIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
295-530 |
9.57e-15 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 76.73 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 295 FAKStLIDKY-------DLSNLHEIASGGAPLSKE----VGEAVAkRFHL-PG-IRQGYGLTETTSAI------------ 349
Cdd:PRK05851 254 FAYN-LIGKYarrvsdvDLGALRVALNGGEPVDCDgferFATAMA-PFGFdAGaAAPSYGLAESTCAVtvpvpgiglrvd 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 350 -LITPEGD--DKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEatnalIDKDGWLHSGDIAYW 426
Cdd:PRK05851 332 eVTTDDGSgaRRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 427 DEDEhFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH---GKTMTEKEIVDYVA 503
Cdd:PRK05851 407 VDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFrgpDEAGARSEVVQRVA 485
|
250 260 270
....*....|....*....|....*....|.
gi 110555473 504 SQ--VTTAKklrggVVFVD--EVPKGLTGKL 530
Cdd:PRK05851 486 SEcgVVPSD-----VVFVApgSLPRTSSGKL 511
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
306-540 |
1.27e-14 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 76.19 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 306 LSNLHEIASGGAPLSKEVGEAvAKRFHLPgIRQGYGLTETTSAIL-ITPE----GDDkpgAVGKVVPffEAKVvdldtgk 380
Cdd:PRK07445 229 LAQFRTILLGGAPAWPSLLEQ-ARQLQLR-LAPTYGMTETASQIAtLKPDdflaGNN---SSGQVLP--HAQI------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 381 TLGVNQRGELCVRGPMIMSGYVnnPEatnaLIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ 460
Cdd:PRK07445 295 TIPANQTGNITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 461 HPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEkEIVDYVASQVTTAKKLRGGVVfVDEVPKGLTGKLDARKIREILI 540
Cdd:PRK07445 369 TGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE-ELKTAIKDQLSPFKQPKHWIP-VPQLPRNPQGKINRQQLQQIAV 446
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
288-530 |
3.81e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 75.45 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 288 VPTLFSFFAKSTLIDKYdlSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVP 367
Cdd:PRK06060 243 VPNFFARVIDSCSPDSF--RSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 368 FFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEatnALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGY 447
Cdd:PRK06060 321 PYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGV 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 448 QVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVT--TAKKLRGGVVFVDEVPKG 525
Cdd:PRK06060 397 NVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNrlSAFKVPHRFAVVDRLPRT 476
|
....*
gi 110555473 526 LTGKL 530
Cdd:PRK06060 477 PNGKL 481
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
189-464 |
4.01e-14 |
|
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: 75.18 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 189 DKTIALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGNQiiPDTAI-LSVVPFHHGFG---MFTTL-----GY---- 255
Cdd:cd17632 222 DDPLALLIYTSGSTGTPKGAMYTERLV-ATFWLKVSSIQDIR--PPASItLNFMPMSHIAGrisLYGTLarggtAYfaaa 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 256 -----------LICGFRVVLMYRFEEELFLR--SLQDYKIQSALLVPTLfSFFAKSTLIDKYDLSNLHEIASGGAPLSKE 322
Cdd:cd17632 299 sdmstlfddlaLVRPTELFLVPRVCDMLFQRyqAELDRRSVAGADAETL-AERVKAELRERVLGGRLLAAVCGSAPLSAE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 323 VGEAVAKRFHLPgIRQGYGLTETTSAILItpegddkpgavGKVV--PFFEAKVVDL-DTG--KTLGVNQRGELCVRGPMI 397
Cdd:cd17632 378 MKAFMESLLDLD-LHDGYGSTEAGAVILD-----------GVIVrpPVLDYKLVDVpELGyfRTDRPHPRGELLVKTDTL 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 398 MSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNI 464
Cdd:cd17632 446 FPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLV 513
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
308-443 |
1.22e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 73.98 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 308 NLHEIASGGAPLSKEVGEAVAKRFHLpGIRQGYGLTETTSAILITPEGDDKPGAVG-KVVPFFEAKVVDLDTGKTLGVNQ 386
Cdd:PTZ00342 462 NLEVILNGGGKLSPKIAEELSVLLNV-NYYQGYGLTETTGPIFVQHADDNNTESIGgPISPNTKYKVRTWETYKATDTLP 540
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 110555473 387 RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK 443
Cdd:PTZ00342 541 KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
52-536 |
1.17e-12 |
|
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: 70.15 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 52 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKk 131
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFNL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 132 gLQKILNVQKKLPIIQKIIIMDSKTDYqgfqsMYTfvtshlppgfneydfvpesfdrdktialimnsSGSTGLPKGVALP 211
Cdd:cd05939 84 -LDPLLTQSSTEPPSQDDVNFRDKLFY-----IYT--------------------------------SGTTGLPKAAVIV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 212 HrtacVRF-SHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELFLRSLQDYKIQSALLVP 289
Cdd:cd05939 126 H----SRYyRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQaLLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 290 TLFSFFAKSTLIDKYDLSNLHEIASGGapLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILitpEGDDKPGAVGkVVPFF 369
Cdd:cd05939 202 EICRYLLAQPPSEEEQKHNVRLAVGNG--LRPQIWEQFVRRFGIPQIGEFYGATEGNSSLV---NIDNHVGACG-FNSRI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 370 EAKV-------VDLDTGKTLgvNQRGELCVR------GPMI-----------MSGYVNNpEATNALIDKDGWLH------ 419
Cdd:cd05939 276 LPSVypirlikVDEDTGELI--RDSDGLCIPcqpgepGLLVgkiiqndplrrFDGYVNE-GATNKKIARDVFKKgdsafl 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 420 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpdddagELP--------AAVVVLEhgk 491
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV------EVPgvegragmAAIVDPE--- 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 110555473 492 tmtEKEIVDYVASQVTTAKKLRGGVVFV---DEVPKGLTGKLDARKIR 536
Cdd:cd05939 424 ---RKVDLDRFSAVLAKSLPPYARPQFIrllPEVDKTGTFKLQKTDLQ 468
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-464 |
1.27e-12 |
|
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: 69.80 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDpIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEEL 272
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQ-LYG--IRPGEVDLATFPLFALFGPALGLTSVIPDMDPTRPARADPQK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 273 FLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPG--IRQGYGLTET----- 345
Cdd:cd05910 165 LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLS-DEaeILTPYGATEAlpvss 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 --TSAILITPEGDDKPGA---VGKVVPFFEAKVVDLDTGKTLGVNQR--------GELCVRGPMIMSGYVNNPEATNALI 412
Cdd:cd05910 244 igSRELLATTTAATSGGAgtcVGRPIPGVRVRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAK 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 110555473 413 DKDG----WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNI 464
Cdd:cd05910 324 IDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV 379
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
192-533 |
6.77e-12 |
|
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: 67.85 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 192 IALIMNSSGSTGLPKGVALPHRtACVRFSH---------ARDPIFGNQIIP-DTAILSVVPfhhgfgMFTTLGYLIcgFR 261
Cdd:cd17644 108 LAYVIYTSGSTGKPKGVMIEHQ-SLVNLSHglikeygitSSDRVLQFASIAfDVAAEEIYV------TLLSGATLV--LR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 262 VVLMyRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDL-SNLHEIASGGAPLSKEVGEAVAKRF-HLPGIRQG 339
Cdd:cd17644 179 PEEM-RSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 340 YGLTE-TTSAILITPEGDDKPG----AVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDK 414
Cdd:cd17644 258 YGPTEaTIAATVCRLTQLTERNitsvPIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 415 DGWLHS--------GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIfdagvaglpdddagelpAAVVV 486
Cdd:cd17644 337 HPFNSSeserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV-----------------KTAVV 399
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110555473 487 LEHGKTMTEKEIVDYVASQVTTA---KKLR-------------GGVVFVDEVPKGLTGKLDAR 533
Cdd:cd17644 400 IVREDQPGNKRLVAYIVPHYEESpstVELRqflkaklpdymipSAFVVLEELPLTPNGKIDRR 462
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
194-537 |
7.34e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 64.29 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 194 LIMNSSGSTGLPKGVALPHrTACVRFSHARDPIFgnQIIPDTAILSVVPFHHGFGmfttlgyLICGF--------RVVLM 265
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSW-TEIDREIEAYNEAL--NCEQDETPIVACPVTHSYG-------LICGVlaaltrgsKPVII 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKydlsNLHEIASGGAPLSKEVGEAVAKR-FHLpgiRQGYGLTE 344
Cdd:PRK08308 175 TNKNPKFALNILRNTPQHILYAVPLMLHILGRLLPGTF----QFHAVMTSGTPLPEAWFYKLRERtTYM---MQQYGCSE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 345 TtSAILITPEGDDkPGAVGKVVPFfeakvVDLDTGKtlGVNQRGELCVRgpmimsgyVNNPEatnalidkdgwLHSGDIA 424
Cdd:PRK08308 248 A-GCVSICPDMKS-HLDLGNPLPH-----VSVSAGS--DENAPEEIVVK--------MGDKE-----------IFTKDLG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 425 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHgkTMTEKEIVDYVAS 504
Cdd:PRK08308 300 YKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE--EIDPVQLREWCIQ 377
|
330 340 350
....*....|....*....|....*....|...
gi 110555473 505 QVtTAKKLRGGVVFVDEVPKGLTGKLdARKIRE 537
Cdd:PRK08308 378 HL-APYQVPHEIESVTEIPKNANGKV-SRKLLE 408
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
49-488 |
1.16e-10 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 63.91 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 49 VDITYAEYFEMSVRLAEAM-KRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAN--DIYNE-RELLNSMGISQPT 124
Cdd:cd05905 13 TTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEppDISQQlGFLLGTCKVRVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 125 VVFVSKKGLQKILNVQKklpiiQKIIIMDSKtdyqGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGL 204
Cdd:cd05905 93 TVEACLKGLPKKLLKSK-----TAAEIAKKK----GWPKILDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 205 PKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFG-MFTTLGYLICGFRVVLMYRFEEE----LFLRSLQD 279
Cdd:cd05905 164 LSGVAVSHSSL---LAHCRALKEACELYESRPLVTVLDFKSGLGlWHGCLLSVYSGHHTILIPPELMKtnplLWLQTLSQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 280 YKIQSALLvptLFSFFAKSTLIDKYDLSNLHE-----------IASGGAPLSKEVGEAVAKRFHLPGIR----------- 337
Cdd:cd05905 241 YKVRDAYV---KLRTLHWCLKDLSSTLASLKNrdvnlsslrmcMVPCENRPRISSCDSFLKLFQTLGLSpravstefgtr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 338 -------QGYGLTETTSAIL---------ITPEGDDKPGA-----VGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPM 396
Cdd:cd05905 318 vnpficwQGTSGPEPSRVYLdmralrhgvVRLDERDKPNSlplqdSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 397 IMSGYVNNPEATNAL------------IDKDGWLHSGDIAYWDEDEHF----------FIVDRLKSLIKYKGYQVAPAEL 454
Cdd:cd05905 398 NASGYFLLDGETNDTfkvfpstrlstgITNNSYARTGLLGFLRPTKCTdlnveehdllFVVGSIDETLEVRGLRHHPSDI 477
|
490 500 510
....*....|....*....|....*....|....*
gi 110555473 455 E-SILLQHPNIFDAGVAglpddDAGELPaaVVVLE 488
Cdd:cd05905 478 EaTVMRVHPYRGRCAVF-----SITGLV--VVVAE 505
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
50-541 |
1.86e-10 |
|
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: 63.44 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 50 DITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG---VAVAPanDiYNERELLNSMGISQPTVV 126
Cdd:cd05943 98 EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGaiwSSCSP--D-FGVPGVLDRFGQIEPKVL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 127 F----VSKKG-----LQKILNVQKKLP-IIQKIIIMDSKTDYQG-------FQSMYTFVTSHLPPgfnEYDFVPESFDRD 189
Cdd:cd05943 175 FavdaYTYNGkrhdvREKVAELVKGLPsLLAVVVVPYTVAAGQPdlskiakALTLEDFLATGAAG---ELEFEPLPFDHP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 190 ktiALIMNSSGSTGLPKGVAlpHRTACVRFSHARDPIFGNQIIP-DTailsvvpfhhgFGMFTTLGY---------LICG 259
Cdd:cd05943 252 ---LYILYSSGTTGLPKCIV--HGAGGTLLQHLKEHILHCDLRPgDR-----------LFYYTTCGWmmwnwlvsgLAVG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 260 FRVVL-----MYRFEEELFlrSLQDyKIQSALLV--PTLFSFFAKSTLI--DKYDLSNLHEIASGGAPLSKE----VGEA 326
Cdd:cd05943 316 ATIVLydgspFYPDTNALW--DLAD-EEGITVFGtsAKYLDALEKAGLKpaETHDLSSLRTILSTGSPLKPEsfdyVYDH 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 327 VAKRFHLPGIRQGyglTETTSAILIT-PEGDDKPGAVGKVVPFFEAKVVDlDTGKTLgVNQRGEL-CVRG-PMIMSGYVN 403
Cdd:cd05943 393 IKPDVLLASISGG---TDIISCFVGGnPLLPVYRGEIQCRGLGMAVEAFD-EEGKPV-WGEKGELvCTKPfPSMPVGFWN 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 404 NPEAT---NALIDK-DG-WLHsGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAG 478
Cdd:cd05943 468 DPDGSryrAAYFAKyPGvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGD 546
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110555473 479 ELPAAVVVLEHGKTMTEkEIVDYVASQVTTAKKLR---GGVVFVDEVPKGLTGkldarKIREILIK 541
Cdd:cd05943 547 ERVILFVKLREGVELDD-ELRKRIRSTIRSALSPRhvpAKIIAVPDIPRTLSG-----KKVEVAVK 606
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
121-536 |
4.10e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.45 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 121 SQPTVVFVSKKGLQKILNVQKKLPIIQK--IIIMDSKTDYQGfqsmytfvtshlppgfneYDFVPESFDRDKtIALIMNS 198
Cdd:PRK12476 141 AEPTVVLTTTAAAEAVEGFLRNLPRLRRprVIAIDAIPDSAG------------------ESFVPVELDTDD-VSHLQYT 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 199 SGSTGLPKGVALPHRTACVRFSHArdPIFGNQIIPDTAILSVVPFHHGFG----MFTTLgyliCGFRVVLM--------- 265
Cdd:PRK12476 202 SGSTRPPVGVEITHRAVGTNLVQM--ILSIDLLDRNTHGVSWLPLYHDMGlsmiGFPAV----YGGHSTLMsptafvrrp 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 266 YRFEEELFLRSLQDYKIQSAllvPTL-FSFFAKSTLI---DKYDLSNLHEIaSGGAPLSKEVGEAVAKRFH---LP--GI 336
Cdd:PRK12476 276 QRWIKALSEGSRTGRVVTAA---PNFaYEWAAQRGLPaegDDIDLSNVVLI-IGSEPVSIDAVTTFNKAFApygLPrtAF 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 337 RQGYGLTETT------------SAILITPEG----------DDKPGAV-----GKVVPFFEAKVVDLDTGKTLGVNQRGE 389
Cdd:PRK12476 352 KPSYGIAEATlfvatiapdaepSVVYLDREQlgagravrvaADAPNAVahvscGQVARSQWAVIVDPDTGAELPDGEVGE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 390 LCVRGPMIMSGYVNNPEAT-----NAL-------------IDKDGWLHSGDIAYWDEDEhFFIVDRLKSLIKYKGYQVAP 451
Cdd:PRK12476 432 IWLHGDNIGRGYWGRPEETertfgAKLqsrlaegshadgaADDGTWLRTGDLGVYLDGE-LYITGRIADLIVIDGRNHYP 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 452 AELESILLQHPNIFDAG-VAG--LPDDDAGELpaaVVVLEH--GKTMTE-KEIVDYVASQVTTAKKLR-GGVVFVDE--V 522
Cdd:PRK12476 511 QDIEATVAEASPMVRRGyVTAftVPAEDNERL---VIVAERaaGTSRADpAPAIDAIRAAVSRRHGLAvADVRLVPAgaI 587
|
490
....*....|....
gi 110555473 523 PKGLTGKLDARKIR 536
Cdd:PRK12476 588 PRTTSGKLARRACR 601
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
346-538 |
2.76e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 56.44 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 TSAILITP---EGDDKPGAVgkVVPFFEAKVVDLD-TGKTLGVNQRGELCVRG--PMIMSGYVNNPE--ATNALIDKDGW 417
Cdd:PLN02654 437 TGGFMITPlpgAWPQKPGSA--TFPFFGVQPVIVDeKGKEIEGECSGYLCVKKswPGAFRTLYGDHEryETTYFKPFAGY 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 418 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEke 497
Cdd:PLN02654 515 YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSE-- 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110555473 498 ivDYVASQVTTAKKLRGGVVFVDEV------PKGLTGKLDARKIREI 538
Cdd:PLN02654 593 --ELRKSLILTVRNQIGAFAAPDKIhwapglPKTRSGKIMRRILRKI 637
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
15-534 |
4.16e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 56.21 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 15 YPLEDGTAGEQLHKAMKRyalVPGTIAFTDAHIEVdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLG 94
Cdd:PRK10252 453 VEIPETTLSALVAQQAAK---TPDAPALADARYQF--SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 95 ALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKkglqkilNVQKKLPIIQKIIImdsktdyqgfqsmYTFVTSHLPP 174
Cdd:PRK10252 528 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA-------DQLPRFADVPDLTS-------------LCYNAPLAPQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 175 gfneyDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARD--PIFGNQII----PDTAILSVVPFHHGFg 248
Cdd:PRK10252 588 -----GAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNhyPLTADDVVlqktPCSFDVSVWEFFWPF- 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 249 mfttlgylICGFRVVLM----YRFEEELfLRSLQDYKIQSALLVPTLFSFFAKSTLID--KYDLSNLHEIASGGAPLSKE 322
Cdd:PRK10252 662 --------IAGAKLVMAepeaHRDPLAM-QQFFAEYGVTTTHFVPSMLAAFVASLTPEgaRQSCASLRQVFCSGEALPAD 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 323 VGEAVAKRFHLPgIRQGYGLTEttSAILIT--P-EGDDKPGAVGKVVPF-FEA-----KVVDlDTGKTLGVNQRGELCVR 393
Cdd:PRK10252 733 LCREWQQLTGAP-LHNLYGPTE--AAVDVSwyPaFGEELAAVRGSSVPIgYPVwntglRILD-ARMRPVPPGVAGDLYLT 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 394 GPMIMSGYVNNPEATNALIDKDGWL------HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDA 467
Cdd:PRK10252 809 GIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQA 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 468 GVaglpdddagelpAAVVVLEHGKTM-TEKEIVDYVASQ-------VTTAKKLRGG-------VVFV--DEVPKGLTGKL 530
Cdd:PRK10252 889 VT------------HACVINQAAATGgDARQLVGYLVSQsglpldtSALQAQLRERlpphmvpVVLLqlDQLPLSANGKL 956
|
....
gi 110555473 531 DaRK 534
Cdd:PRK10252 957 D-RK 959
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
193-533 |
2.93e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.63 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 193 ALIMNSSGSTGLPKGVALPHRTACVrfsHARDPI--FGNQiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR--F 268
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAM---HCQAVIerFGMR--ADDCELHFYSINFDAASERLLVPLLCGARVVLRAQgqW 2410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 269 EEELFLRSLQDYKIQSALLVPTLFSFFAKsTLIDKYDLSNLHEIASGGAPLSKEvgeavakrfHLPGIRQ---------G 339
Cdd:PRK05691 2411 GAEEICQLIREQQVSILGFTPSYGSQLAQ-WLAGQGEQLPVRMCITGGEALTGE---------HLQRIRQafapqlffnA 2480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 340 YGLTETTSAILITPEGDDKP-GA----VGKVVPFFEAKVVDLD-----TGKTlgvnqrGELCVRGPMIMSGY-------- 401
Cdd:PRK05691 2481 YGPTETVVMPLACLAPEQLEeGAasvpIGRVVGARVAYILDADlalvpQGAT------GELYVGGAGLAQGYhdrpglta 2554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 402 ---VNNPEATNAlidkdGWLH-SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpDDDA 477
Cdd:PRK05691 2555 erfVADPFAADG-----GRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPS 2628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110555473 478 GelpaavvvlehgktmteKEIVDYVASQVTTAK-----KLRGGV-----------------VFVDEVPKGLTGKLDAR 533
Cdd:PRK05691 2629 G-----------------KQLAGYLVSAVAGQDdeaqaALREALkahlkqqlpdymvpahlILLDSLPLTANGKLDRR 2689
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
274-536 |
3.91e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 52.46 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 274 LRSLQDYKiQSALL-VPTlfsfFAKsTLIDK-----YDLSNLH-EIAS-GGAPLSKEVGEAVAKRFHLPgIRQGYGLTET 345
Cdd:COG1541 168 LRLMQDFG-PTVLVgTPS----YLL-YLAEVaeeegIDPRDLSlKKGIfGGEPWSEEMRKEIEERWGIK-AYDIYGLTEV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 346 TSAILItpEGDDKPGAVgkvvpFFE----AKVVDLDTGKTLGVNQRGELCVrgpmimsgyvnnpeaTNalIDKDGW---- 417
Cdd:COG1541 241 GPGVAY--ECEAQDGLH-----IWEdhflVEIIDPETGEPVPEGEEGELVV---------------TT--LTKEAMplir 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 418 LHSGDIAYWDEDE---------HFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpdDDAGELPAAVVVLE 488
Cdd:COG1541 297 YRTGDLTRLLPEPcpcgrthprIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVV--DREGGLDELTVRVE 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 110555473 489 HGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDevPKGL---TGKldARKIR 536
Cdd:COG1541 375 LAPGASLEALAEAIAAALKAVLGLRAEVELVE--PGSLprsEGK--AKRVI 421
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
388-534 |
3.32e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 388 GELCVRGPMIMSGYVNNPEAT-NALIDK------DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ 460
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTaLAFVPHpfgapgERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE 4146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110555473 461 HPNIFDAGVA---GLPDDD-AGELPAAVVVLEHG------KTMTEKEIVDYVASQvttakklrgGVVFVDEVPKGLTGKL 530
Cdd:PRK05691 4147 QAEVREAAVAvqeGVNGKHlVGYLVPHQTVLAQGalleriKQRLRAELPDYMVPL---------HWLWLDRLPLNANGKL 4217
|
....
gi 110555473 531 DaRK 534
Cdd:PRK05691 4218 D-RK 4220
|
|
| |
