|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
173-704 |
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: 1066.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 173 IKKGPAPFYPLEDGTAGEQLHKAMKRYALVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSL 252
Cdd:cd17642 1 IIVGPGPFYPLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 253 QFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYT 332
Cdd:cd17642 81 QFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 333 FVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHG 412
Cdd:cd17642 161 FITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 413 FGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEA 492
Cdd:cd17642 241 FGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 493 VAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPE 572
Cdd:cd17642 321 VAKRFKLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 573 ATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 652
Cdd:cd17642 401 ATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 653 LEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 704
Cdd:cd17642 481 LEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
207-696 |
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: 644.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 207 AFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGI 286
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 287 SQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTShlppGFNEYDFVPESFDRDKTIALIMNSSG 366
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTL----GEEDEDLPPPLKDGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 367 STGLPKGVALPHRTACVRFSHARDPIFGNqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDY 446
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLSQVQTFLYGN-DGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 447 KIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPG 526
Cdd:cd05911 236 KITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 527 AVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKS 606
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 607 LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVD 686
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVFVD 475
|
490
....*....|
gi 1886431185 687 EVPKGLTGKL 696
Cdd:cd05911 476 EIPKSASGKI 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
203-695 |
5.04e-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: 456.31 E-value: 5.04e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 282
Cdd:cd05904 19 PSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 283 SMGISQPTVVFVSKKGLQKILnvqkklPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPgfneydfvPESFDRDKTIALIM 362
Cdd:cd05904 99 QVKDSGAKLAFTTAELAEKLA------SLALPVVLLDSAEFDSLSFSDLLFEADEAEP--------PVVVIKQDDVAALL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 363 NSSGSTGLPKGVALPHR--TACVRFSHARdpiFGNQIIPDTAILSVVPFHH--GFGMFTtLGYLICGFRVVLMYRFEEEL 438
Cdd:cd05904 165 YSSGTTGRSKGVMLTHRnlIAMVAQFVAG---EGSNSDSEDVFLCVLPMFHiyGLSSFA-LGLLRLGATVVVMPRFDLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 439 FLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILIT 518
Cdd:cd05904 241 LLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 519 P---EGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDED 595
Cdd:cd05904 321 FapeKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 596 EHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTA 675
Cdd:cd05904 401 GYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPY 480
|
490 500
....*....|....*....|
gi 1886431185 676 KKLRgGVVFVDEVPKGLTGK 695
Cdd:cd05904 481 KKVR-KVAFVDAIPKSPSGK 499
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
189-708 |
2.46e-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: 385.70 E-value: 2.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 189 GEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAV 268
Cdd:COG0318 2 ADLLRRAAARH---PDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 269 APANDIYNERELLNSMGISQPTVVFVskkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfv 348
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVT------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 349 pesfdrdktiALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGM-FTTLGYLICGFR 427
Cdd:COG0318 103 ----------ALILYTSGTTGRPKGVMLTHRNLL---ANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGAT 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 428 VVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYG 507
Cdd:COG0318 170 LVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVR-IVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 508 LTETTSAILITPE--GDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLH 585
Cdd:COG0318 249 LTETSPVVTVNPEdpGERRPGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 586 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 665
Cdd:COG0318 327 TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELR 406
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1886431185 666 DYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKA 708
Cdd:COG0318 407 AFLRERLARYKVPR-RVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
218-705 |
1.95e-118 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 365.84 E-value: 1.95e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 297
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 GLQKILNVQKKLPIiqKIIIMDSKTDyqGFQSMYTFVTShlppgfNEYDFVPESFDRDKTIALIMnSSGSTGLPKGVALP 377
Cdd:PLN02246 132 YVDKLKGLAEDDGV--TVVTIDDPPE--GCLHFSELTQA------DENELPEVEISPDDVVALPY-SSGTTGLPKGVMLT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 378 HRTACVRFSHARD---PIFGnqIIPDTAILSVVPFHHGFGMFTTLgylICGFRV----VLMYRFEEELFLRSLQDYKIQS 450
Cdd:PLN02246 201 HKGLVTSVAQQVDgenPNLY--FHSDDVILCVLPMFHIYSLNSVL---LCGLRVgaaiLIMPKFEIGALLELIQRHKVTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 451 ALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILI------TPEgDDK 524
Cdd:PLN02246 276 APFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMclafakEPF-PVK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 525 PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRL 604
Cdd:PLN02246 355 SGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 605 KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVF 684
Cdd:PLN02246 435 KELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIH-KVFF 513
|
490 500
....*....|....*....|.
gi 1886431185 685 VDEVPKGLTGKLDARKIREIL 705
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 ... |
357-697 |
4.94e-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: 349.66 E-value: 4.94e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 357 TIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNqiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEE 436
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT---EGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 437 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAIL 516
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 517 ITP--EGDDKPGAVGKVVPFFEAKVVDLDTGkTLGVNQRGELCVRGPMIMSGYVNNPEATnALIDKDGWLHSGDIAYWDE 594
Cdd:cd04433 157 TGPpdDDARKPGSVGRPVPGVEVRIVDPDGG-ELPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 595 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTT 674
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|...
gi 1886431185 675 AKKLRgGVVFVDEVPKGLTGKLD 697
Cdd:cd04433 315 YKVPR-RVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
217-702 |
8.76e-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: 312.19 E-value: 8.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELlnsmgisqptvvfvsk 296
Cdd:cd05936 25 LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPREL---------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 kglQKILNvqkklpiiqkiiimDSktdyqGFQSMYTFVT-SHLPPGFNEYDFVPESFDRDktIALIMNSSGSTGLPKGVA 375
Cdd:cd05936 89 ---EHILN--------------DS-----GAKALIVAVSfTDLLAAGAPLGERVALTPED--VAVLQYTSGTTGVPKGAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 376 LPHR------TACVRfshardpIFGNQIIPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELFLRSLQDYKI 448
Cdd:cd05936 145 LTHRnlvanaLQIKA-------WLEDLLEGDDVVLAALPLFHVFGLTVALLLpLALGATIVLIPRFRPIGVLKEIRKHRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 449 QSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITP-EGDDKPGA 527
Cdd:cd05936 218 TIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVP-IVEGYGLTETSPVVAVNPlDGPRKPGS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 528 VGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSL 607
Cdd:cd05936 297 IGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 608 IKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDE 687
Cdd:cd05936 375 IIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPR-QVEFRDE 453
|
490
....*....|....*
gi 1886431185 688 VPKGLTGKLDARKIR 702
Cdd:cd05936 454 LPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
217-703 |
5.19e-96 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 306.73 E-value: 5.19e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 296
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVT--SHLPPgfnEYDFVPesFDRDkTIALIMNSSGSTGLPKGV 374
Cdd:PRK06187 112 EFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEEllAAASD---TFDFPD--IDEN-DAAAMLYTSGTTGHPKGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 375 ALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVP-FH-HGFGmfttLGY--LICGFRVVLMYRFEEELFLRSLQDYKIQS 450
Cdd:PRK06187 186 VLSHRNL---FLHSLAVCAWLKLSRDDVYLVIVPmFHvHAWG----LPYlaLMAGAKQVIPRRFDPENLLDLIETERVTF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 451 ALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLpGIRQGYGLTETTSAILITPEGDD------K 524
Cdd:PRK06187 259 FFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGI-DLVQGYGMTETSPVVSVLPPEDQlpgqwtK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 525 PGAVGKVVPFFEAKVVDLDtGKTLGVNQR--GELCVRGPMIMSGYVNNPEATNALIDkDGWLHSGDIAYWDEDEHFFIVD 602
Cdd:PRK06187 338 RRSAGRPLPGVEARIVDDD-GDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 603 RLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVttAK-KLRGG 681
Cdd:PRK06187 416 RIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRL--AKfKLPKR 493
|
490 500
....*....|....*....|..
gi 1886431185 682 VVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK06187 494 IAFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
192-697 |
1.73e-93 |
|
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: 297.21 E-value: 1.73e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 192 LHKAMKRYalvPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPA 271
Cdd:cd17631 1 LRRRARRH---PDRTALVFGGRS--LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 272 NDIYNERELLNSMGISQPTVVFvskkglqkilnvqkklpiiqkiiiMDsktdyqgfqsmytfvtshlppgfneydfvpes 351
Cdd:cd17631 76 NFRLTPPEVAYILADSGAKVLF------------------------DD-------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 352 fdrdktIALIMNSSGSTGLPKGVALPHRTacvRFSHARDPIFGNQIIPDTAILSVVPFHHGFGM-FTTLGYLICGFRVVL 430
Cdd:cd17631 100 ------LALLMYTSGTTGRPKGAMLTHRN---LLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 431 MYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlPGIRQGYGLTE 510
Cdd:cd17631 171 LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARG--VKFVQGYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 511 TTSAILITPEGD--DKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGD 588
Cdd:cd17631 249 TSPGVTFLSPEDhrRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 589 IAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYV 668
Cdd:cd17631 327 LGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHC 406
|
490 500
....*....|....*....|....*....
gi 1886431185 669 ASQVTTAKKLRgGVVFVDEVPKGLTGKLD 697
Cdd:cd17631 407 RERLARYKIPK-SVEFVDALPRNATGKIL 434
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
168-710 |
3.67e-93 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 299.97 E-value: 3.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 168 EDAKNIKKGPAPFYPL-EDGTAGEQLHKAMKRYAlvpGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVV 246
Cdd:PLN02330 9 EDNEHIFRSRYPSVPVpDKLTLPDFVLQDAELYA---DKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 247 CSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQkkLPIIqkiiimdsktdYQG 326
Cdd:PLN02330 86 VLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLG--LPVI-----------VLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 327 FQSMYTFV--TSHLPPGFNEYD-FVPESFDRDKTIALIMnSSGSTGLPKGVALPHRTACVRFSHARDPIfGNQIIPDTAI 403
Cdd:PLN02330 153 EEKIEGAVnwKELLEAADRAGDtSDNEEILQTDLCALPF-SSGTTGISKGVMLTHRNLVANLCSSLFSV-GPEMIGQVVT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 404 LSVVPFHHGFGM----FTTL---GylicgfRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNL- 475
Cdd:PLN02330 231 LGLIPFFHIYGItgicCATLrnkG------KVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLk 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 476 -HEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETtSAILIT---PE---GDDKPGAVGKVVPFFEAKVVDLDTGKTL 548
Cdd:PLN02330 305 lQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEH-SCITLThgdPEkghGIAKKNSVGFILPNLEVKFIDPDTGRSL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 549 GVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHP 628
Cdd:PLN02330 384 PKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 629 NIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKA 708
Cdd:PLN02330 464 SVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVR-VVQFVDSIPKSLSGKIMRRLLKEKMLSI 542
|
..
gi 1886431185 709 KK 710
Cdd:PLN02330 543 NK 544
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
203-611 |
5.85e-93 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 295.38 E-value: 5.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAHIEvDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 282
Cdd:pfam00501 9 PDKTALEVGEGR-RLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 283 SMGISQPTVVFV-SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPgfneydFVPESFDRDkTIALI 361
Cdd:pfam00501 88 ILEDSGAKVLITdDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPP------PPPPPPDPD-DLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 362 MNSSGSTGLPKGVALPHR------TACVRFSHARDPIFgnqiiPDTAILSVVPFHHGFGM-FTTLGYLICGFRVVLM--- 431
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRnlvanvLSIKRVRPRGFGLG-----PDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPpgf 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTET 511
Cdd:pfam00501 236 PALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 TSAILITPEGDDK---PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGD 588
Cdd:pfam00501 315 TGVVTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGD 394
|
410 420
....*....|....*....|...
gi 1886431185 589 IAYWDEDEHFFIVDRLKSLIKYK 611
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
203-705 |
1.17e-85 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 280.57 E-value: 1.17e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELL 281
Cdd:PLN02574 53 NGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 282 NSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKT-DYQGFQSMYTFvtshlppgfnEYDFVPESFDRDKTIAL 360
Cdd:PLN02574 133 KRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYDFDSKRiEFPKFYELIKE----------DFDFVPKPVIKQDDVAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 361 IMNSSGSTGLPKGVALPHRTAC------VRFSHARDPIFGNqiipDTAILSVVPFHH--GFGMFTTlGYLICGFRVVLMY 432
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIamvelfVRFEASQYEYPGS----DNVYLAALPMFHiyGLSLFVV-GLLSLGSTIVVMR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 433 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTL-IDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTET 511
Cdd:PLN02574 278 RFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 TSAIL--ITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDI 589
Cdd:PLN02574 358 TAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 590 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVA 669
Cdd:PLN02574 438 AYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVA 517
|
490 500 510
....*....|....*....|....*....|....*.
gi 1886431185 670 SQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:PLN02574 518 KQVAPYKKVR-KVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
215-703 |
2.62e-81 |
|
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: 267.26 E-value: 2.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 215 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFV 294
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 295 SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtSHLPPGFNEYDFV-PESFDRDKTIALIMNSSGSTGLPKG 373
Cdd:cd05926 93 PKGELGPASRAASKLGLAILELALDVGVLIRAPSA------ESLSNLLADKKNAkSEGVPLPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 374 VALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTT-LGYLICGFRVVLMYRFEEELFLRSLQDYKIQ--S 450
Cdd:cd05926 167 VPLTHRNLA---ASATNITNTYKLTPDDRTLVVMPLFHVHGLVASlLSTLAAGGSVVLPPRFSASTFWPDVRDYNATwyT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 451 AllVPTLFSF---FAKSTLIDKYdlSNLHEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTSAILITP--EGDDKP 525
Cdd:cd05926 244 A--VPTIHQIllnRPEPNPESPP--PKLRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEAAHQMTSNPlpPGPRKP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 526 GAVGKvvPF-FEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRL 604
Cdd:cd05926 319 GSVGK--PVgVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 605 KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVtTAKKLRGGVVF 684
Cdd:cd05926 396 KELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHL-AAFKVPKKVYF 474
|
490
....*....|....*....
gi 1886431185 685 VDEVPKGLTGKLDARKIRE 703
Cdd:cd05926 475 VDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
190-703 |
1.33e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 266.00 E-value: 1.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 190 EQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVA 269
Cdd:PRK07656 9 ELLARAARRF---GDKEAYVFG--DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 270 PANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFvTSHLPPGFNEYDFVP 349
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTF-TDFLAAGDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 350 ESFDrdkTIALIMNSSGSTGLPKGVALPHRTAcvrFSHARDpiFGN--QIIPDTAILSVVPFHHGFGMftTLGYLIC--- 424
Cdd:PRK07656 163 VDPD---DVADILFTSGTTGRPKGAMLTHRQL---LSNAAD--WAEylGLTEGDRYLAANPFFHVFGY--KAGVNAPlmr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 425 GFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQ 504
Cdd:PRK07656 233 GATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 505 GYGLTETTSAILITPEGDDK---PGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 581
Cdd:PRK07656 313 GYGLSEASGVTTFNRLDDDRktvAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 582 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 661
Cdd:PRK07656 392 GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1886431185 662 KEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK07656 472 EELIAYCREHL--AKyKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
217-699 |
9.32e-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: 261.26 E-value: 9.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNEREL---LNSMGIsqptvvf 293
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELeyiLNDSGA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 294 vskkglqkilnvqkklpiiqKIIIMDSKTDyqgfqsmytfvtshlppgfneydfvpesfdrdkTIALIMNSSGSTGLPKG 373
Cdd:cd05935 75 --------------------KVAVVGSELD---------------------------------DLALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 374 VALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLI-CGFRVVLMYRFEEELFLRSLQDYKIQSAL 452
Cdd:cd05935 102 CMHTHFSA---AANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVyVGGTYVLMARWDRETALELIEKYKVTFWT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 453 LVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlpGIR--QGYGLTETTSAILITPEGDDKPGAVGk 530
Cdd:cd05935 179 NIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT---GLRfvEGYGLTETMSQTHTNPPLRPKLQCLG- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 531 vVPFF--EAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT-NALIDKDG--WLHSGDIAYWDEDEHFFIVDRLK 605
Cdd:cd05935 255 -IP*FgvDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETeESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 606 SLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL--EHGKTMTEKEIVDYVASQVTTAKKLRgGVV 683
Cdd:cd05935 334 RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLrpEYRGKVTEEDIIEWAREQMAAYKYPR-EVE 412
|
490
....*....|....*.
gi 1886431185 684 FVDEVPKGLTGKLDAR 699
Cdd:cd05935 413 FVDELPRSASGKILWR 428
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
217-703 |
1.10e-79 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 264.51 E-value: 1.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKR-YGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVS 295
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 296 KKGLQKILNVQKKLPIiqKIIIMDSKTDYQGFQSMYTF----VTSHLPPGFNEYDFV-------------PESFDRDkTI 358
Cdd:PRK08314 116 SELAPKVAPAVGNLRL--RHVIVAQYSDYLPAEPEIAVpawlRAEPPLQALAPGGVVawkealaaglappPHTAGPD-DL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHRTacVRFShardpIFGNQI----IPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVLMYR 433
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRT--VMAN-----AVGSVLwsnsTPESVVLAVLPLFHVTGMVHSMnAPIYAGATVVLMPR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 434 FEEELFLRSLQDYKIQSALLVPT-LFSFFAkSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRFH-LPGIR--QGYGLT 509
Cdd:PRK08314 266 WDREAAARLIERYRVTHWTNIPTmVVDFLA-SPGLAERDLSSLRYIGGGGAAMP----EAVAERLKeLTGLDyvEGYGLT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 510 ETTSAILITPEGDDKPGAVGkvVPFF--EAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT-NALIDKDG--WL 584
Cdd:PRK08314 341 ETMAQTHSNPPDRPKLQCLG--IPTFgvDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATaEAFIEIDGkrFF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 585 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL--EHGKTMTEK 662
Cdd:PRK08314 419 RTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLrpEARGKTTEE 498
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1886431185 663 EIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK08314 499 EIIAWAREHMAAYKYPR-IVEFVDSLPKSGSGKILWRQLQE 538
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
214-705 |
1.98e-75 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 253.50 E-value: 1.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 214 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVF 293
Cdd:COG0365 37 ERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 294 VSKKGL---------QKILNVQKKLPIIQKIII---MDSKTDYQGFQSMYTFVTSHLPpgfneyDFVPESFDRDkTIALI 361
Cdd:COG0365 117 TADGGLrggkvidlkEKVDEALEELPSLEHVIVvgrTGADVPMEGDLDWDELLAAASA------EFEPEPTDAD-DPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 362 MNSSGSTGLPKGVALPHR--TACVRFSHARdpIFGnqIIPDTAILSVVP----FHHGFGMFttlGYLICGFRVVLmyrFE 435
Cdd:COG0365 190 LYTSGTTGKPKGVVHTHGgyLVHAATTAKY--VLD--LKPGDVFWCTADigwaTGHSYIVY---GPLLNGATVVL---YE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 436 E-------ELFLRSLQDYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGY 506
Cdd:COG0365 260 GrpdfpdpGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVP-IVDGW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 507 GLTETTSAILITPEGDD-KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM--IMSGYVNNPEAT-NALIDK-D 581
Cdd:COG0365 339 GQTETGGIFISNLPGLPvKPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYrETYFGRfP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 582 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 661
Cdd:COG0365 418 GWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1886431185 662 ---KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:COG0365 498 elaKELQAHVREELGPYAYPR-EIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
176-706 |
4.28e-72 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 244.68 E-value: 4.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 176 GPAPFY-------PLEDGTAGEQLHKAMKRYalvPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCS 248
Cdd:PRK12583 1 MPQPSYyqgggdkPLLTQTIGDAFDATVARF---PDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 249 ENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK--KG------LQKILN----------VQKKLP 310
Cdd:PRK12583 78 PNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafKTsdyhamLQELLPglaegqpgalACERLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 311 IIQKIIIMDSK-----TDYQGFQSMYTFVTSHlppgfnEYDFVPESFDRDKTIAlIMNSSGSTGLPKGVALPHRTacvrf 385
Cdd:PRK12583 158 ELRGVVSLAPApppgfLAWHELQARGETVSRE------ALAERQASLDRDDPIN-IQYTSGTTGFPKGATLSHHN----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 386 shardpIFGNQII-------PDTAILSV-VPFHHGFGM-FTTLGYLICGFRVVL-MYRFEEELFLRSLQDYKIQSALLVP 455
Cdd:PRK12583 226 ------ILNNGYFvaeslglTEHDRLCVpVPLYHCFGMvLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYGVP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 456 TLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKP---GAVGKVV 532
Cdd:PRK12583 300 TMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLErrvETVGRTQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 533 PFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKG 612
Cdd:PRK12583 380 PHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 613 YQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGL 692
Cdd:PRK12583 459 ENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPR-YFRFVDEFPMTV 537
|
570
....*....|....
gi 1886431185 693 TGKLDARKIREILI 706
Cdd:PRK12583 538 TGKVQKFRMREISI 551
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
365-702 |
3.18e-68 |
|
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: 3.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 365 SGSTGLPKGVALPHRTacvrfshardpIFGNQII--------PDTAILSVVPFHHGFGMftTLGYLIC---GFRVVlmyr 433
Cdd:cd05917 11 SGTTGSPKGATLTHHN-----------IVNNGYFigerlgltEQDRLCIPVPLFHCFGS--VLGVLAClthGATMV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 434 FEEELF-----LRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGL 508
Cdd:cd05917 74 FPSPSFdplavLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 509 TETTSAILITPEGDD---KPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLH 585
Cdd:cd05917 154 TETSPVSTQTRTDDSiekRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 586 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 665
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIK 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 1886431185 666 DYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 702
Cdd:cd05917 314 AYCKGKIAHYKVPR-YVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
218-703 |
6.39e-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: 229.44 E-value: 6.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 297
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 GLQKILNVQKKLPIIQKIIIMDSKTDYQ-----GFQSMYTFVTSHlPPGFNEYDFvpesfDrDKTIALIMNSSGSTGLPK 372
Cdd:cd12119 107 FLPLLEAIAPRLPTVEHVVVMTDDAAMPepagvGVLAYEELLAAE-SPEYDWPDF-----D-ENTAAAICYTSGTTGNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 373 GVALPHRTAcvrFSHA---RDPIFGNQIIPDTaILSVVP-FH-HGFGM-FTTLgylICGFRVVLMYRFEE-ELFLRSLQD 445
Cdd:cd12119 180 GVVYSHRSL---VLHAmaaLLTDGLGLSESDV-VLPVVPmFHvNAWGLpYAAA---MVGAKLVLPGPYLDpASLAELIER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 446 YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRFHLPGIR--QGYGLTET----TSAILITP 519
Cdd:cd12119 253 EGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVP----RSLIEAFEERGVRviHAWGMTETsplgTVARPPSE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 520 EGDDKPGAV-------GKVVPFFEAKVVDLDT------GKTlgvnqRGELCVRGPMIMSGYVNNPEATNALiDKDGWLHS 586
Cdd:cd12119 329 HSNLSEDEQlalrakqGRPVPGVELRIVDDDGrelpwdGKA-----VGELQVRGPWVTKSYYKNDEESEAL-TEDGWLRT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 587 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVD 666
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLE 482
|
490 500 510
....*....|....*....|....*....|....*...
gi 1886431185 667 YVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:cd12119 483 FLADKV--AKwWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
197-705 |
7.04e-67 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 228.59 E-value: 7.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 197 KRYALVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMK-RYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY 275
Cdd:PRK06839 10 KRAYLHPDRIAIITE--EEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 276 NERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtshlppgfneyDFVPESFDRD 355
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKID----------------NFVEKNESAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 356 ktiALIMNSSGSTGLPKGVALphrTACVRFSHARDPIFGNQIIPDTAILSVVPFHH--GFGMFTtLGYLICGFRVVLMYR 433
Cdd:PRK06839 152 ---FIICYTSGTTGKPKGAVL---TQENMFWNALNNTFAIDLTMHDRSIVLLPLFHigGIGLFA-FPTLFAGGVIIVPRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 434 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGirQGYGLTETTS 513
Cdd:PRK06839 225 FEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 514 AILITPEGD--DKPGAVGKVVPFFEAKVVDLDTGKtLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAY 591
Cdd:PRK06839 303 TVFMLSEEDarRKVGSIGKPVLFCDYELIDENKNK-VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLAR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 592 WDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQ 671
Cdd:PRK06839 381 VDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLF 460
|
490 500 510
....*....|....*....|....*....|....
gi 1886431185 672 VTTAKKLRgGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:PRK06839 461 LAKYKIPK-EIVFLKELPKNATGKIQKAQLVNQL 493
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
184-630 |
1.27e-66 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 230.76 E-value: 1.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 184 EDGTAGEQLHKAMKRYalvPGTIAFT--DAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGA 261
Cdd:COG1022 9 PADTLPDLLRRRAARF---PDRVALRekEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 262 LFIGVAVAPandIY---NERELLNSMGISQPTVVFVSKKG-LQKILNVQKKLPIIQKIIIMDSKTDYQG-----FQSMYT 332
Cdd:COG1022 86 LAAGAVTVP---IYptsSAEEVAYILNDSGAKVLFVEDQEqLDKLLEVRDELPSLRHIVVLDPRGLRDDprllsLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 333 FVTSHLPPGfnEYDFVPESFDRDkTIALIMNSSGSTGLPKGVALPHR--TACVRFSHARDPIFgnqiiPDTAILSVVPFH 410
Cdd:COG1022 163 LGREVADPA--ELEARRAAVKPD-DLATIIYTSGTTGRPKGVMLTHRnlLSNARALLERLPLG-----PGDRTLSFLPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 411 HGFGMFTTLGYLICGFRVVlmyrFEE--ELFLRSLQDYKIQSALLVP----------------------TLFSFF----- 461
Cdd:COG1022 235 HVFERTVSYYALAAGATVA----FAEspDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrKLFRWAlavgr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 462 -----------------AKSTLIDKYDLSNLHE--------IASGGAPLSKEVGEAvakrFH---LPgIRQGYGLTETTS 513
Cdd:COG1022 311 ryararlagkspslllrLKHALADKLVFSKLREalggrlrfAVSGGAALGPELARF----FRalgIP-VLEGYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 514 AILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWD 593
Cdd:COG1022 386 VITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELD 454
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1886431185 594 EDEHFFIVDRLKSLI-----KYkgyqVAPAELESILLQHPNI 630
Cdd:COG1022 455 EDGFLRITGRKKDLIvtsggKN----VAPQPIENALKASPLI 492
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
182-707 |
1.38e-66 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 229.70 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 182 PLEDGTAGEQLHKAMKRYalvPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENS-----LQFFM 256
Cdd:PRK08315 12 PLLEQTIGQLLDRTAARY---PDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVpewvlTQFAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 257 PVLGAlfIGVAVAPAndiYNEREL---LNSMGISqpTVVFVSK-----------------KGLQKILNVQKKLPIIQKII 316
Cdd:PRK08315 89 AKIGA--ILVTINPA---YRLSELeyaLNQSGCK--ALIAADGfkdsdyvamlyelapelATCEPGQLQSARLPELRRVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 317 IMDSKTdyqgFQSMYTF-----VTSHLPPGfnEYDFVPESFDRDKTIAlIMNSSGSTGLPKGVALPHR---------TAC 382
Cdd:PRK08315 162 FLGDEK----HPGMLNFdellaLGRAVDDA--ELAARQATLDPDDPIN-IQYTSGTTGFPKGATLTHRnilnngyfiGEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 383 VRFSHArDPIfgnqIIPdtailsvVPFHHGFGMftTLGYLIC---GFRVVLMY-RFEEELFLRSLQDYKIQSALLVPTLF 458
Cdd:PRK08315 235 MKLTEE-DRL----CIP-------VPLYHCFGM--VLGNLACvthGATMVYPGeGFDPLATLAAVEEERCTALYGVPTMF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 459 -------SFfakstliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDD---KPGAV 528
Cdd:PRK08315 301 iaeldhpDF-------ARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPlekRVTTV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 529 GKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLI 608
Cdd:PRK08315 374 GRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 609 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEV 688
Cdd:PRK08315 454 IRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPR-YIRFVDEF 532
|
570
....*....|....*....
gi 1886431185 689 PKGLTGKLDARKIREILIK 707
Cdd:PRK08315 533 PMTVTGKIQKFKMREMMIE 551
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
216-703 |
2.17e-66 |
|
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: 224.92 E-value: 2.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 216 DITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPtvvfvs 295
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 296 kkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpeSFDRdktIALIMNSSGSTGLPKGVA 375
Cdd:cd05912 75 -------------------------------------------------------KLDD---IATIMYTSGTTGKPKGVQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 376 LphrTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVP 455
Cdd:cd05912 97 Q---TFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 456 TLFSffaksTLIDKYDL---SNLHEIASGGAPLSKEVGEaVAKRFHLPgIRQGYGLTETTSAIL-ITPE-GDDKPGAVGK 530
Cdd:cd05912 174 TMLQ-----RLLEILGEgypNNLRCILLGGGPAPKPLLE-QCKEKGIP-VYQSYGMTETCSQIVtLSPEdALNKIGSAGK 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 531 VVPFFEAKVVDLDTGKtlgvNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY 610
Cdd:cd05912 247 PLFPVELKIEDDGQPP----YEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIIS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 611 KGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEhgKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVP 689
Cdd:cd05912 322 GGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKL--AKyKVPKKIYFVDELP 397
|
490
....*....|....
gi 1886431185 690 KGLTGKLDARKIRE 703
Cdd:cd05912 398 RTASGKLLRHELKQ 411
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
216-710 |
1.34e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 227.22 E-value: 1.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 216 DITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVS 295
Cdd:PRK06710 49 DITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 296 KKGLQKILNVQKKLPIiqKIIIMDSKTDYQGFQS--MYTFVT------------SHLPPGFNEYD-----FVPESFDRDK 356
Cdd:PRK06710 129 DLVFPRVTNVQSATKI--EHVIVTRIADFLPFPKnlLYPFVQkkqsnlvvkvseSETIHLWNSVEkevntGVEVPCDPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 357 TIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFgNQIIPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLMYRFE 435
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLY-NCKEGEEVVLGVLPFFHVYGMTAVMNLSIMqGYKMVLIPKFD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 436 EELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVaKRFHLPGIRQGYGLTETTSAI 515
Cdd:PRK06710 286 MKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKF-ETVTGGKLVEGYGLTESSPVT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 516 LITPEGDDK-PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDE 594
Cdd:PRK06710 365 HSNFLWEKRvPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 595 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIvDYVASQVTT 674
Cdd:PRK06710 444 DGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEEL-NQFARKYLA 522
|
490 500 510
....*....|....*....|....*....|....*.
gi 1886431185 675 AKKLRGGVVFVDEVPKGLTGKLdarkIREILIKAKK 710
Cdd:PRK06710 523 AYKVPKVYEFRDELPKTTVGKI----LRRVLIEEEK 554
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
217-710 |
6.37e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 225.65 E-value: 6.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 296
Cdd:PRK05605 58 TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 K------------GLQKIL--NVQKKLPIIQKI-------IIMDSKTDYQG-------FQSMytfvTSHLPPGFNEYDFV 348
Cdd:PRK05605 138 KvaptverlrrttPLETIVsvNMIAAMPLLQRLalrlpipALRKARAALTGpapgtvpWETL----VDAAIGGDGSDVSH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 349 PESfdRDKTIALIMNSSGSTGLPKGVALPHRT--ACVRFSHARDPIFGNQiipDTAILSVVPFHHGFG--MFTTLGYLIc 424
Cdd:PRK05605 214 PRP--TPDDVALILYTSGTTGKPKGAQLTHRNlfANAAQGKAWVPGLGDG---PERVLAALPMFHAYGltLCLTLAVSI- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 425 GFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVgeaVAKRFHLPG--I 502
Cdd:PRK05605 288 GGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVST---VELWEKLTGglL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 503 RQGYGLTETTSAILITPEGDD-KPGAVGkvVPF--FEAKVVDLDT-GKTLGVNQRGELCVRGPMIMSGYVNNPEATNALI 578
Cdd:PRK05605 365 VEGYGLTETSPIIVGNPMSDDrRPGYVG--VPFpdTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 579 dKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKT 658
Cdd:PRK05605 443 -LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAA 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 659 MTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKAKK 710
Cdd:PRK05605 522 LDPEGLRAYCREHLTRYKVPR-RFYHVDELPRDQLGKVRRREVREELLEKLG 572
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
217-702 |
1.63e-64 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 220.24 E-value: 1.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSk 296
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 kgLQKILnvqkklpiiqkiiimdsktdyqgfqsmYTfvtshlppgfneydfvpesfdrdktialimnsSGSTGLPKGVAL 376
Cdd:cd05934 83 --PASIL---------------------------YT--------------------------------SGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 377 PHR---TACVRFSHARDpifgnqIIPDTAILSVVPFHHGFGMFTT-LGYLICGFRVVLMYRFEEELFLRSLQDYKIQSAL 452
Cdd:cd05934 102 THAnltFAGYYSARRFG------LGEDDVYLTVLPLFHINAQAVSvLAALSVGATLVLLPRFSASRFWSDVRRYGATVTN 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 453 LVPTLFSFFAKsTLIDKYDLSN-LHEIASGGAPlsKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPGAVGKV 531
Cdd:cd05934 176 YLGAMLSYLLA-QPPSPDDRAHrLRAAYGAPNP--PELHEEFEERFGVR-LLEGYGMTETIVGVIGPRDEPRRPGSIGRP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 532 VPFFEAKVVDlDTGKTLGVNQRGELCVR---GPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLI 608
Cdd:cd05934 252 APGYEVRIVD-DDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 609 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTaKKLRGGVVFVDEV 688
Cdd:cd05934 330 RRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY-FKVPRYIRFVDDL 408
|
490
....*....|....
gi 1886431185 689 PKGLTGKLDARKIR 702
Cdd:cd05934 409 PKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
187-708 |
1.91e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 220.19 E-value: 1.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 187 TAGEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGV 266
Cdd:PRK08316 12 TIGDILRRSARRY---PDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 267 AVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKI-IIMDSKTDYQG----FQSMYTfvtshlppg 341
Cdd:PRK08316 87 VHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLIlSLVLGGREAPGgwldFADWAE--------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 342 fNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHR------TACvrfshardpIFGNQIIPDTAILSVVPFHHGFGM 415
Cdd:PRK08316 158 -AGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRaliaeyVSC---------IVAGDMSADDIPLHALPLYHCAQL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 416 FTTLG-YLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVA 494
Cdd:PRK08316 228 DVFLGpYLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 495 KRfhLPGIR--QGYGLTET--TSAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNN 570
Cdd:PRK08316 308 ER--LPGLRfyNCYGQTEIapLATVLGPEEHLRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 571 PEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAV 650
Cdd:PRK08316 385 PEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 651 VVLEHGKTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARKIREILIKA 708
Cdd:PRK08316 464 VVPKAGATVTEDELIAHCRARL-AGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
218-702 |
5.54e-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: 216.43 E-value: 5.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPtvvfvskk 297
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 glqkilnvqkklpiiqKIIIMDSKTdyqgfqsmytfvtshlppgfneydfvpesfdrdktIALIMNSSGSTGLPKGVALP 377
Cdd:cd05972 74 ----------------KAIVTDAED-----------------------------------PALIYFTSGTTGLPKGVLHT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 378 HRTACVRFSHARDPIfgnQIIPDTAILSVV-PFHHGFGMFTTLGYLICGFRVVL--MYRFEEELFLRSLQDYKIQSALLV 454
Cdd:cd05972 103 HSYPLGHIPTAAYWL---GLRPDDIHWNIAdPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 455 PTLFSFFAKStLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPF 534
Cdd:cd05972 180 PTAYRMLIKQ-DLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 535 FEAKVVDlDTGKTLGVNQRGELCVR--GPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKG 612
Cdd:cd05972 258 YDVAIID-DDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 613 YQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVASQVTTAKKLRgGVVFVDEVP 689
Cdd:cd05972 336 YRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPR-EIEFVEELP 414
|
490
....*....|...
gi 1886431185 690 KGLTGKLDARKIR 702
Cdd:cd05972 415 KTISGKIRRVELR 427
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
196-705 |
1.54e-61 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 214.06 E-value: 1.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 196 MKRYALVPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY 275
Cdd:PRK03640 9 KQRAFLTPDRTAIEFEEKK--VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 276 NERELLNSMGISQPTVVFVSKkglqkilNVQKKLPIIQKIIImdsktdyqgfqsmytfvtSHLPPGFNEYDFVPESFDRD 355
Cdd:PRK03640 87 SREELLWQLDDAEVKCLITDD-------DFEAKLIPGISVKF------------------AELMNGPKEEAEIQEEFDLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 356 KTiALIMNSSGSTGLPKGVALphrTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFE 435
Cdd:PRK03640 142 EV-ATIMYTSGTTGKPKGVIQ---TYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 436 EELFLRSLQDYKIQSALLVPTLFSffaksTLIDKYDLSNLHE----IASGGAPLSKEVGEaVAKRFHLPGIrQGYGLTET 511
Cdd:PRK03640 218 AEKINKLLQTGGVTIISVVSTMLQ-----RLLERLGEGTYPSsfrcMLLGGGPAPKPLLE-QCKEKGIPVY-QSYGMTET 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 TSAILITPEGD--DKPGAVGKvvPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDI 589
Cdd:PRK03640 291 ASQIVTLSPEDalTKLGSAGK--PLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 590 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVleHGKTMTEKEIVDYVA 669
Cdd:PRK03640 368 GYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV--KSGEVTEEELRHFCE 445
|
490 500 510
....*....|....*....|....*....|....*..
gi 1886431185 670 SQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:PRK03640 446 EKL--AKyKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
203-702 |
8.62e-61 |
|
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: 212.61 E-value: 8.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 282
Cdd:cd05959 18 GDKTAFIDDAGS--LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 283 SMGISQPTVVFVSKKGLQKILN-VQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPpgfneyDFVPESFDRDKtIALI 361
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLAAaLTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAE------QLKPAATHADD-PAFW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 362 MNSSGSTGLPKGVALPHRTACVRFSHARDPIFGnqIIPDTAILSVVP--FHHGFG--MFTTLGYlicGFRVVLM-YRFEE 436
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYWTAELYARNVLG--IREDDVCFSAAKlfFAYGLGnsLTFPLSV---GATTVLMpERPTP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 437 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAIL 516
Cdd:cd05959 244 AAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD-ILDGIGSTEMLHIFL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 517 ITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDE 596
Cdd:cd05959 323 SNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 597 HFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVASQVT 673
Cdd:cd05959 401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAleeELKEFVKDRLA 480
|
490 500
....*....|....*....|....*....
gi 1886431185 674 TAKKLRgGVVFVDEVPKGLTGKLDARKIR 702
Cdd:cd05959 481 PYKYPR-WIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
184-703 |
6.80e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 210.61 E-value: 6.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 184 EDGTAGEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALF 263
Cdd:PRK06188 10 SGATYGHLLVSALKRY---PDRPALVLG--DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 264 IG---VAVAPANDIYNERELLNSMGISqpTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtshlpp 340
Cdd:PRK06188 85 AGlrrTALHPLGSLDDHAYVLEDAGIS--TLIVDPAPFVERALALLARVPSLKHVLTLGPVPDGVDLLA----------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 341 GFNEYDFVP-ESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRfshardpifgNQII-------PDTAILSVVPFHHG 412
Cdd:PRK06188 152 AAAKFGPAPlVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATM----------AQIQlaewewpADPRFLMCTPLSHA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 413 FGMFTTLGyLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSffaksTLID-----KYDLSNLHEIASGGAPLSK 487
Cdd:PRK06188 222 GGAFFLPT-LLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIY-----ALLDhpdlrTRDLSSLETVYYGASPMSP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 488 -EVGEAVaKRFHlPGIRQGYGLTETTSAILITPEGDDKP------GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG 560
Cdd:PRK06188 296 vRLAEAI-ERFG-PIFAQYYGQTEAPMVITYLRKRDHDPddpkrlTSCGRPTPGLRVALLD-EDGREVAQGEVGEICVRG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 561 PMIMSGYVNNPEATnALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPD 640
Cdd:PRK06188 373 PLVMDGYWNRPEET-AEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPD 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 641 DDAGELPAAVVVLEHGKTMTEKEIVDYVASQ---VTTAKKlrggVVFVDEVPKGLTGKLDARKIRE 703
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 ... |
213-654 |
9.56e-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: 208.22 E-value: 9.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 213 IEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandIY------NERELLNSmgi 286
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP---IYptssaeQIAYILND--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 287 SQPTVVFVSKK-GLQKIlnvqkklpiiqkiiimdsktdyqgfqsMYTfvtshlppgfneydfvpesfdrdktialimnsS 365
Cdd:cd05907 76 SEAKALFVEDPdDLATI---------------------------IYT--------------------------------S 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 366 GSTGLPKGVALPHRTACvrfSHARDpifGNQIIPDTA---ILSVVPFHHGFGMFTTLgYLICGFRVVLMYRFEEELFLRS 442
Cdd:cd05907 97 GTTGRPKGVMLSHRNIL---SNALA---LAERLPATEgdrHLSFLPLAHVFERRAGL-YVPLLAGARIYFASSAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 443 LQDYKIQSALLVPTLF-SFFA----------KSTLIDKYDLSNLHEIASGGAPLSKEVGEavakRFHLPGI--RQGYGLT 509
Cdd:cd05907 170 LSEVRPTVFLAVPRVWeKVYAaikvkavpglKRKLFDLAVGGRLRFAASGGAPLPAELLH----FFRALGIpvYEGYGLT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 510 ETTSAILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDI 589
Cdd:cd05907 246 ETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDL 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 590 AYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNIFDAGVAGlpddDAGELPAAVVVLE 654
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 ... |
210-703 |
2.66e-58 |
|
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: 206.58 E-value: 2.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 210 DAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNEREL---LNSMGI 286
Cdd:cd05970 41 DAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIvyrIESADI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 287 SQptVVFVSKKGL-QKILNVQKKLPIIQKIIIMdSKTDYQGFQSMYTFVtSHLPPgfneyDFVP---ESFDRDKTIALIM 362
Cdd:cd05970 121 KM--IVAIAEDNIpEEIEKAAPECPSKPKLVWV-GDPVPEGWIDFRKLI-KNASP-----DFERptaNSYPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 363 NSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVL--MYRFEEELF 439
Cdd:cd05970 192 FSSGTTGMPKMVEHDFTYP---LGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIyGQWIAGAAVFVydYDKFDPKAL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 440 LRSLQDYKIQSALLVPTLFSFFAKSTLiDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITP 519
Cdd:cd05970 269 LEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK-LMEGFGQTETTLTIATFP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 520 EGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVR----GPM-IMSGYVNNPEATnALIDKDGWLHSGDIAYWDE 594
Cdd:cd05970 347 WMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRtskgKPVgLFGGYYKDAEKT-AEVWHDGYYHTGDAAWMDE 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 595 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVaSQ 671
Cdd:cd05970 425 DGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEelkKELQDHV-KK 503
|
490 500 510
....*....|....*....|....*....|..
gi 1886431185 672 VTTAKKLRGGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:cd05970 504 VTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
217-703 |
2.08e-57 |
|
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: 201.36 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAM-KRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTvvfvs 295
Cdd:cd05941 12 ITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 296 kkglqkilnvqkklpiiqkiIIMDsktdyqgfqsmytfvtshlppgfneydfvpesfdrdktIALIMNSSGSTGLPKGVA 375
Cdd:cd05941 87 --------------------LVLD--------------------------------------PALILYTSGTTGRPKGVV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 376 LPHR--TACVR-FSHARdpifgnQIIPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVLMYRFEEELFLRSLQDYKIQSA 451
Cdd:cd05941 109 LTHAnlAANVRaLVDAW------RWTEDDVLLHVLPLHHVHGLVNALlCPLFAGASVEFLPKFDPKEVAISRLMPSITVF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 452 LLVPTLFS--------FFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAiLITP-EGD 522
Cdd:cd05941 183 MGVPTIYTrllqyyeaHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHT-LLERYGMTEIGMA-LSNPlDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 523 DKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVD 602
Cdd:cd05941 261 RRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 603 RLKS-LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGK-TMTEKEIVDyVASQVTTAKKLRG 680
Cdd:cd05941 341 RSSVdIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKE-WAKQRLAPYKRPR 419
|
490 500
....*....|....*....|...
gi 1886431185 681 GVVFVDEVPKGLTGKLDARKIRE 703
Cdd:cd05941 420 RLILVDELPRNAMGKVNKKELRK 442
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
218-701 |
1.43e-56 |
|
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: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVskk 297
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 glqkilnvqkklpiiqkiiimDSKTDYQGFQSmytfVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALP 377
Cdd:TIGR01923 78 ---------------------DSLLEEKDFQA----DSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 378 HRTacvRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEelFLRSLQDYKIQSALLVPTL 457
Cdd:TIGR01923 133 FRN---HYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 458 FSFFAKSTLIDkydlSNLHEIASGGAPLSKEVGEAVAKRfHLPgIRQGYGLTETTSAIL-ITPEGDDKPGAVGKVVPFFE 536
Cdd:TIGR01923 208 LNRLLDEGGHN----ENLRKILLGGSAIPAPLIEEAQQY-GLP-IYLSYGMTETCSQVTtATPEMLHARPDVGRPLAGRE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 537 AKV-VDLDTGktlgvnqRGELCVRGPMIMSGYVNNPEATNAlIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQV 615
Cdd:TIGR01923 282 IKIkVDNKEG-------HGEIMVKGANLMKGYLYQGELTPA-FEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 616 APAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEhgKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTG 694
Cdd:TIGR01923 354 YPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKL--AKyKVPIAFEKLDELPYNASG 429
|
....*..
gi 1886431185 695 KLDARKI 701
Cdd:TIGR01923 430 KILRNQL 436
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
186-704 |
2.12e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 201.31 E-value: 2.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 186 GTAGEQLHKAMKRYalvPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG 265
Cdd:PRK07788 49 GPFAGLVAHAARRA---PDRAALIDERGT--LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 266 VAVApandiynereLLNSmGISQPTVVFVSKKglQKIlnvqkklpiiqKIIIMDSKtdyqgfqsmYTFVTSHLPPGFNEY 345
Cdd:PRK07788 124 ARII----------LLNT-GFSGPQLAEVAAR--EGV-----------KALVYDDE---------FTDLLSALPPDLGRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 346 -------DFVPESFDRDKTIA-------------------LIMNSSGSTGLPKGVALPHRTACVrfshardpifgnqiiP 399
Cdd:PRK07788 171 rawggnpDDDEPSGSTDETLDdliagsstaplpkppkpggIVILTSGTTGTPKGAPRPEPSPLA---------------P 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 400 DTAILSVVPFHHGF------GMFTTLGY----LICGFR--VVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFF--AKST 465
Cdd:PRK07788 236 LAGLLSRVPFRAGEttllpaPMFHATGWahltLAMALGstVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRIldLGPE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 466 LIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETTSAILITPEGDDK-PGAVGKVVPFFEAKVVDlDT 544
Cdd:PRK07788 316 VLAKYDTSSLKIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAFATIATPEDLAEaPGTVGRPPKGVTVKILD-EN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 545 GKTLGVNQRGELCVRGPMIMSGYVN--NPEAtnalidKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELES 622
Cdd:PRK07788 394 GNEVPRGVVGRIFVGNGFPFEGYTDgrDKQI------IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 623 ILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 702
Cdd:PRK07788 468 LLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPR-DVVFLDELPRNPTGKVLKRELR 546
|
..
gi 1886431185 703 EI 704
Cdd:PRK07788 547 EM 548
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
192-713 |
1.78e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 199.22 E-value: 1.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 192 LHKAMKRYALVPgtiAFTDahIEVDITYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAP 270
Cdd:PRK05677 30 LKQSCQRFADKP---AFSN--LGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 271 ANDIYNERELLNSMGISQPTVVF------------VSKKGLQKIL--NVQKKLPIIQKIIIMDSKTDYQGFQSMYtfvts 336
Cdd:PRK05677 105 TNPLYTAREMEHQFNDSGAKALVclanmahlaekvLPKTGVKHVIvtEVADMLPPLKRLLINAVVKHVKKMVPAY----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 337 HLPP--GFNE-------YDFVPESFDRDKtIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPDTAILSVV 407
Cdd:PRK05677 180 HLPQavKFNDalakgagQPVTEANPQADD-VAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIAPL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 408 PFHHGFGM-FTTLGYLICGFRVVLMYRFEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPL 485
Cdd:PRK05677 259 PLYHIYAFtFHCMAMMLIGNHNILISNPRDlPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMAL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 486 SKevgeAVAKRF-HLPG--IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM 562
Cdd:PRK05677 339 QL----ATAERWkEVTGcaICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGELCVKGPQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 563 IMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDD 642
Cdd:PRK05677 414 VMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEK 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 643 AGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILIKaKKGGK 713
Cdd:PRK05677 494 SGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPK-AVEFRDELPTTNVGKILRRELRDEELK-KAGLK 562
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
178-697 |
6.82e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 197.57 E-value: 6.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 178 APFYPLEDGTAGEQLHKAMKRYALVPGTIAFtdAHievDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMP 257
Cdd:PRK06178 25 EPEYPHGERPLTEYLRAWARERPQRPAIIFY--GH---VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 258 VLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIiqKIIIMDSKTDyqgfqsmytFVTSH 337
Cdd:PRK06178 100 FFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSL--RHVIVTSLAD---------VLPAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 338 ----LPPGFNE--------YDFVP-----------ESFDRDKTIALimN-SSGSTGLPKGVALPHR-------TAC-VRF 385
Cdd:PRK06178 169 ptlpLPDSLRAprlaaagaIDLLPalractapvplPPPALDALAAL--NyTGGTTGMPKGCEHTQRdmvytaaAAYaVAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 386 SHARDPIFgnqiipdtaiLSVVPFH----HGFGMfttLGYLICGFRVVLMYRFEEELFLRSLQDYKIQS-ALLVPTLFSF 460
Cdd:PRK06178 247 VGGEDSVF----------LSFLPEFwiagENFGL---LFPLFSGATLVLLARWDAVAFMAAVERYRVTRtVMLVDNAVEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 461 FAKSTLIDkYDLSNLHEIasGGAPLSKEVGEAVAKRFH-LPG--IRQG-YGLTETTSAILITP--EGDD-----KPGAVG 529
Cdd:PRK06178 314 MDHPRFAE-YDLSSLRQV--RVVSFVKKLNPDYRQRWRaLTGsvLAEAaWGMTETHTCDTFTAgfQDDDfdllsQPVFVG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 530 KVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK 609
Cdd:PRK06178 391 LPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 610 YKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAK--KLRggvvFVDE 687
Cdd:PRK06178 470 VNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKvpEIR----IVDA 545
|
570
....*....|
gi 1886431185 688 VPKGLTGKLD 697
Cdd:PRK06178 546 LPMTATGKVR 555
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
359-702 |
4.52e-53 |
|
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: 4.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHRTAcvrfshardpIFGNQII-------PDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM 431
Cdd:cd05922 120 ALLLYTSGSTGSPKLVRLSHQNL----------LANARSIaeylgitADDRALTVLPLSYDYGLSVLNTHLLRGATLVLT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 YRFE-EELFLRSLQDYKIQSALLVPTLFSFFAKSTlIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTE 510
Cdd:cd05922 190 NDGVlDDAFWEDLREHGATGLAGVPSTYAMLTRLG-FDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 511 TTSAILITP--EGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGD 588
Cdd:cd05922 269 ATRRMTYLPpeRILEKPGSIGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 589 IAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPdDDAGELPAAVVVLEHGktMTEKEIVDYV 668
Cdd:cd05922 348 LARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDK--IDPKDVLRSL 424
|
330 340 350
....*....|....*....|....*....|....
gi 1886431185 669 ASQVTTAkKLRGGVVFVDEVPKGLTGKLDARKIR 702
Cdd:cd05922 425 AERLPPY-KVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
358-696 |
7.52e-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: 185.78 E-value: 7.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMftTLGYLIC---GFRVVLMYRF 434
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCA---DLTEDDRYLIINPFFHTFGY--KAGIVAClltGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSA 514
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 515 ILITPEGD--DKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYW 592
Cdd:cd17638 157 TMCRPGDDaeTVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 593 DEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQV 672
Cdd:cd17638 226 DERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERL 305
|
330 340
....*....|....*....|....
gi 1886431185 673 TTAKKLRgGVVFVDEVPKGLTGKL 696
Cdd:cd17638 306 ANYKVPR-FVRFLDELPRNASGKV 328
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
187-703 |
5.31e-52 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 189.70 E-value: 5.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 187 TAGEQLHKAMKRYALVPGTIAFTDAhievdITYAEYFEMSVRLAE-AMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG 265
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKT-----ITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 266 VAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQkiIIMDSKTDYQGF--QSMYTFVTSHLPPGFN 343
Cdd:PRK08751 101 LTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQ--VITTGLGDMLGFpkAALVNFVVKYVKKLVP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 344 EYDF-----------------VPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQIIPD--TAIL 404
Cdd:PRK08751 179 EYRIngairfrealalgrkhsMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEgcEVVI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 405 SVVPFHHGFGM------FTTLG---YLICGFRvvlmyrfEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNL 475
Cdd:PRK08751 259 TALPLYHIFALtanglvFMKIGgcnHLISNPR-------DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 476 HEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRG 554
Cdd:PRK08751 332 KMTLGGGMAVQRSVAERWKQVTGLTLV-EAYGLTETSPAACINPlTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 555 ELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAG 634
Cdd:PRK08751 410 ELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVA 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 635 VAGLPDDDAGELpAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK08751 490 AVGVPDEKSGEI-VKVVIVKKDPALTAEDVKAHARANLTGYKQPR-IIEFRKELPKTNVGKILRRELRD 556
|
|
| Ubl_ubiquitin |
cd01803 |
ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes ... |
92-166 |
8.70e-52 |
|
ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like (Ubl) proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ubiquitin (Ub)and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Ub includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric multiubiquitin protein chains.
Pssm-ID: 340501 [Multi-domain] Cd Length: 76 Bit Score: 173.78 E-value: 8.70e-52
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLRLRGG 166
Cdd:cd01803 2 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 76
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
366-708 |
1.43e-51 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 189.78 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 366 GSTGLPKGVALPHrtacvrfshardpifGNQII------------PDTAILSVVPFHHGFGMFTT-LGYLICGFRVVLM- 431
Cdd:PRK07529 223 GTTGMPKLAQHTH---------------GNEVAnawlgalllglgPGDTVFCGLPLFHVNALLVTgLAPLARGAHVVLAt 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 ---YRFEEEL--FLRSLQDYKIQSALLVPTLFSFFAKsTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGY 506
Cdd:PRK07529 288 pqgYRGPGVIanFWKIVERYRINFLSGVPTVYAALLQ-VPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVR-IVEGY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 507 GLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDLD-TGKTL---GVNQRGELCVRGPMIMSGYVNnPEATNALIDKD 581
Cdd:PRK07529 366 GLTEATCVSSVNPpDGERRIGSVGLRLPYQRVRVVILDdAGRYLrdcAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLED 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 582 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 661
Cdd:PRK07529 445 GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATE 524
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 662 KEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGK-----LDARKIREILIKA 708
Cdd:PRK07529 525 AELLAFARDHIAERAAVPKHVRILDALPKTAVGKifkpaLRRDAIRRVLRAA 576
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
198-703 |
6.07e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 186.14 E-value: 6.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 198 RYALV-PGTIAFTdaHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYN 276
Cdd:PRK07786 25 RHALMqPDAPALR--FLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 277 ERELLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQsmYTFVTSHLPPGFNEYDfVPESfdrdk 356
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLG--YEDLLAEAGPAHAPVD-IPND----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 357 TIALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQI-IPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL--MYR 433
Cdd:PRK07786 175 SPALIMYTSGTTGRPKGAVLTHANLT---GQAMTCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIypLGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 434 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETtS 513
Cdd:PRK07786 252 FDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEM-S 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 514 AILITPEGDD---KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDkDGWLHSGDIA 590
Cdd:PRK07786 330 PVTCMLLGEDairKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 591 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG-KTMTEKEIVDYVA 669
Cdd:PRK07786 408 RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLT 487
|
490 500 510
....*....|....*....|....*....|....
gi 1886431185 670 SQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK07786 488 DRLARYKHPK-ALEIVDALPRNPAGKVLKTELRE 520
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
243-702 |
1.03e-50 |
|
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: 184.46 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 243 RIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKIlnVQKKLPIIQ---KIIIM- 318
Cdd:cd05909 33 NVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKL--KLHHLFDVEydaRIVYLe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 319 DSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTiALIMNSSGSTGLPKGVALPHR---------TACVRFShar 389
Cdd:cd05909 111 DLRAKISKADKCKAFLAGKFPPKWLLRIFGVAPVQPDDP-AVILFTSGSEGLPKGVVLSHKnllanveqiTAIFDPN--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 390 dpifgnqiiPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYR-FEEELFLRSLQDYKIQSALLVPTLFSFFAKStlI 467
Cdd:cd05909 187 ---------PEDVVFGALPFFHSFGLTGCLWLpLLSGIKVVFHPNpLDYKKIPELIYDKKATILLGTPTFLRGYARA--A 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 468 DKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILI-TPEGDDKPGAVGKVVPFFEAKVVDLDTGK 546
Cdd:cd05909 256 HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECSPVISVnTPQSPNKEGTVGRPLPGMEVKIVSVETHE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 547 TLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ 626
Cdd:cd05909 335 EVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSE 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 627 H-PNIFDAGVAGLPDDDAGElpaAVVVLEHGKTMTEKEIVDYV-ASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 702
Cdd:cd05909 414 IlPEDNEVAVVSVPDGRKGE---KIVLLTTTTDTDPSSLNDILkNAGISNLAKPS-YIHQVEEIPLLGTGKPDYVTLK 487
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
212-703 |
2.08e-50 |
|
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: 183.27 E-value: 2.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 212 HIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSlqffmPVLGALFIGVAVAPAndiynereLLNSmgisqptv 291
Cdd:cd12118 25 YGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNT-----PAMYELHFGVPMAGA--------VLNA-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 292 vfvskkglqkiLNVQKKLPIIQ--------KIIIMDSKTDYQGFQSMytfvtshlppGFNEYDFVPESfDRDKTIALimN 363
Cdd:cd12118 84 -----------LNTRLDAEEIAfilrhseaKVLFVDREFEYEDLLAE----------GDPDFEWIPPA-DEWDPIAL--N 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 364 -SSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVP-FH-----HGFGMFTTLGYLICgfrvvlMYRFEE 436
Cdd:cd12118 140 yTSGTTGRPKGVVYHHRGA---YLNALANILEWEMKQHPVYLWTLPmFHcngwcFPWTVAAVGGTNVC------LRKVDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 437 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAV-AKRFHlpgIRQGYGLTETTSAI 515
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMeELGFD---VTHVYGLTETYGPA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 516 LI---TPEGDDKPGA----------VGkVVPFFEAKVVDLDT-------GKTLGvnqrgELCVRGPMIMSGYVNNPEATN 575
Cdd:cd12118 288 TVcawKPEWDELPTEerarlkarqgVR-YVGLEEVDVLDPETmkpvprdGKTIG-----EIVFRGNIVMKGYLKNPEATA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 576 ALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 655
Cdd:cd12118 362 EAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKE 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1886431185 656 GKTMTEKEIVDYVASQVTTAKKLRgGVVFvDEVPKGLTGKLDARKIRE 703
Cdd:cd12118 441 GAKVTEEEIIAFCREHLAGFMVPK-TVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
237-710 |
2.79e-50 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 184.87 E-value: 2.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 237 GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNEREL---LNSMGISqpTVVFVSK--KGLQKILNvqkKLPI 311
Cdd:PRK08974 70 GLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELehqLNDSGAK--AIVIVSNfaHTLEKVVF---KTPV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 312 iqKIIIMDSKTDYQGF--QSMYTFVTS---------HLPPG--FNE-------YDFVPESFDRDkTIALIMNSSGSTGLP 371
Cdd:PRK08974 145 --KHVILTRMGDQLSTakGTLVNFVVKyikrlvpkyHLPDAisFRSalhkgrrMQYVKPELVPE-DLAFLQYTGGTTGVA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 372 KGVALPHRTACVRFSHArDPIFGNQIIPDTA-ILSVVPFHHGFGM------FTTLG---YLICGFRVVlmyrfeeELFLR 441
Cdd:PRK08974 222 KGAMLTHRNMLANLEQA-KAAYGPLLHPGKElVVTALPLYHIFALtvncllFIELGgqnLLITNPRDI-------PGFVK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 442 SLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPlskeVGEAVAKRFH-LPGIR--QGYGLTETTSAILIT 518
Cdd:PRK08974 294 ELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMA----VQQAVAERWVkLTGQYllEGYGLTECSPLVSVN 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 519 PEG-DDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEH 597
Cdd:PRK08974 370 PYDlDYYSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 598 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELpAAVVVLEHGKTMTEKEIVDYVASQVTTAK- 676
Cdd:PRK08974 448 LRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLTEEELITHCRRHLTGYKv 526
|
490 500 510
....*....|....*....|....*....|....*.
gi 1886431185 677 -KLrggVVFVDEVPKGLTGKLDARKIR-EILIKAKK 710
Cdd:PRK08974 527 pKL---VEFRDELPKSNVGKILRRELRdEARAKVDN 559
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
177-702 |
3.43e-50 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 184.45 E-value: 3.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 177 PAPFYPLEDGTAGEQLHKAMKRYALVPgtiAFTdaHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFM 256
Cdd:PRK07059 14 PAEIDASQYPSLADLLEESFRQYADRP---AFI--CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 257 PVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK---GLQKILNvqkKLPIiqKIIIMDSKTDYQGFQS-MYT 332
Cdd:PRK07059 89 AIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENfatTVQQVLA---KTAV--KHVVVASMGDLLGFKGhIVN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 333 FVTSHLP--------PGFNEYD----------FVPESFDRDKtIALIMNSSGSTGLPKGVALPHRT--ACVRFSHA-RDP 391
Cdd:PRK07059 164 FVVRRVKkmvpawslPGHVRFNdalaegarqtFKPVKLGPDD-VAFLQYTGGTTGVSKGATLLHRNivANVLQMEAwLQP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 392 IFGNQIIPDT-AILSVVPFHHGFGMftTLGYLI---CGFRVVLMYRFEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTL 466
Cdd:PRK07059 243 AFEKKPRPDQlNFVCALPLYHIFAL--TVCGLLgmrTGGRNILIPNPRDiPGFIKELKKYQVHIFPAVNTLYNALLNNPD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 467 IDKYDLSNLhEIASGGAplsKEVGEAVAKR-FHLPG--IRQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDl 542
Cdd:PRK07059 321 FDKLDFSKL-IVANGGG---MAVQRPVAERwLEMTGcpITEGYGLSETSPVATCNPvDATEFSGTIGLPLPSTEVSIRD- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 543 DTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELES 622
Cdd:PRK07059 396 DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 623 ILLQHPNIFDAGVAGLPDDDAGELPAAVVVlEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 702
Cdd:PRK07059 476 VVASHPGVLEVAAVGVPDEHSGEAVKLFVV-KKDPALTEEDVKAFCKERLTNYKRPK-FVEFRTELPKTNVGKILRRELR 553
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
218-703 |
5.79e-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: 181.04 E-value: 5.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELlnsmgisqptvVFVSKK 297
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHEL-----------AFILRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 GLQKILnvqkklpiiqkiIIMDSktdyqgfqsmytfvtshlppgFNEYDFVPESFDrdktIALIMNSSGSTGLPKGVALP 377
Cdd:cd05903 72 AKAKVF------------VVPER---------------------FRQFDPAAMPDA----VALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 378 HRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHH--GFGMFTTLGYLIcGFRVVLMYRFEEELFLRSLQDYKIQSALLVP 455
Cdd:cd05903 115 HNTL---SASIRQYAERLGLGPGDVFLVASPMAHqtGFVYGFTLPLLL-GAPVVLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 456 TLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRqGYGLTETTSAILITPEGDDKPGAV--GKVVP 533
Cdd:cd05903 191 PFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS-AYGSTECPGAVTSITPAPEDRRLYtdGRPLP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 534 FFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEaTNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGY 613
Cdd:cd05903 270 GVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPD-LTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 614 QVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLT 693
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPS 427
|
490
....*....|
gi 1886431185 694 GKLDARKIRE 703
Cdd:cd05903 428 GKVQKFRLRE 437
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
190-704 |
6.10e-50 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 183.87 E-value: 6.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 190 EQLHKAMKRYALVPgtiAFTDahIEVDITYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAV 268
Cdd:PRK12492 28 EVFERSCKKFADRP---AFSN--LGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 269 APANDIYNERELLNSMGISQP-TVVFVSKKGLQkilnVQKKLP--IIQKII---IMDSKTDYQGFQsMYTFVTS------ 336
Cdd:PRK12492 103 VNTNPLYTAREMRHQFKDSGArALVYLNMFGKL----VQEVLPdtGIEYLIeakMGDLLPAAKGWL-VNTVVDKvkkmvp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 337 --HLPP--GFNE---------YDFVPESFDrdkTIALIMNSSGSTGLPKGVALPHRT---------ACVRfSHARDpifG 394
Cdd:PRK12492 178 ayHLPQavPFKQalrqgrglsLKPVPVGLD---DIAVLQYTGGTTGLAKGAMLTHGNlvanmlqvrACLS-QLGPD---G 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 395 NQIIPD--TAILSVVPFHHGFGmFTT--LGYLICGFRVVLMYRFEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDK 469
Cdd:PRK12492 251 QPLMKEgqEVMIAPLPLYHIYA-FTAncMCMMVSGNHNVLITNPRDiPGFIKELGKWRFSALLGLNTLFVALMDHPGFKD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 470 YDLSNLHEIASGGAPLSKevgeAVAKRF-HLPGIR--QGYGLTETTSAILITPEGD-DKPGAVGKVVPFFEAKVVDlDTG 545
Cdd:PRK12492 330 LDFSALKLTNSGGTALVK----ATAERWeQLTGCTivEGYGLTETSPVASTNPYGElARLGTVGIPVPGTALKVID-DDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 546 KTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILL 625
Cdd:PRK12492 405 NELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 626 QHPNIFDAGVAGLPDDDAGELPAAVVVLEHGkTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 704
Cdd:PRK12492 485 AHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENF-TGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
361-697 |
1.05e-49 |
|
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: 177.08 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 361 IMNSSGSTGLPKGVALPHR---TACVRFSHARdpifgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEE 437
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGnliAANLQLIHAM------GLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 438 LFLRSLQDYKIqsallvpTLFSFFAK--STLIDK-----YDLSNLHEIASGGAPlskevgeAVAKRFH-LPGIR--QGYG 507
Cdd:cd17637 79 EALELIEEEKV-------TLMGSFPPilSNLLDAaeksgVDLSSLRHVLGLDAP-------ETIQRFEeTTGATfwSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 508 LTETTSAILITPEgDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSG 587
Cdd:cd17637 145 QTETSGLVTLSPY-RERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 588 DIAYWDEDEHFFIVDRL--KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 665
Cdd:cd17637 222 DLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELI 301
|
330 340 350
....*....|....*....|....*....|..
gi 1886431185 666 DYVASQVTTAKKLRgGVVFVDEVPKGLTGKLD 697
Cdd:cd17637 302 EFVGSRIARYKKPR-YVVFVEALPKTADGSID 332
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
217-703 |
1.73e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 181.43 E-value: 1.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 296
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSmYTFVTSHLPPGfneydfvpeSFDRDKTIALIMNSSGSTGLPKGV-- 374
Cdd:PRK13391 105 AKLDVARALLKQCPGVRHRLVLDGDGELEGFVG-YAEAVAGLPAT---------PIADESLGTDMLYSSGTTGRPKGIkr 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 375 ALPHR--TACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSAL 452
Cdd:PRK13391 175 PLPEQppDTPLPLTAFLQRLWG--FRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 453 LVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETTSAILI-TPEGDDKPGAVG 529
Cdd:PRK13391 253 LVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWG-PIIHEYYAATEGLGFTACdSEEWLAHPGTVG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 530 KVVpFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSgYVNNPEATNALIDKDG-WLHSGDIAYWDEDEHFFIVDRLKSLI 608
Cdd:PRK13391 332 RAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 609 KYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVASQVTTAKKLRgGVVFV 685
Cdd:PRK13391 409 ISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFCRQRLSRQKCPR-SIDFE 487
|
490
....*....|....*...
gi 1886431185 686 DEVPKGLTGKLDARKIRE 703
Cdd:PRK13391 488 DELPRLPTGKLYKRLLRD 505
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
214-702 |
1.97e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 180.19 E-value: 1.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 214 EVDITYAEYFEMSVRLAEamkryGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVF 293
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 294 VSKKGlqkilnVQKKLPIIQKIIIMDSktdyqgfqsmytfvtSHLPPgfnEYDfvPESfdrdktIALIMNSSGSTGLPKG 373
Cdd:PRK07787 98 GPAPD------DPAGLPHVPVRLHARS---------------WHRYP---EPD--PDA------PALIVYTSGTTGPPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 374 VALPHR--TACV-RFSHARdpifgnQIIPDTAILSVVP-FH-HGFgMFTTLGYLICGFRVVLMYRFEEELFLRSLQDyki 448
Cdd:PRK07787 146 VVLSRRaiAADLdALAEAW------QWTADDVLVHGLPlFHvHGL-VLGVLGPLRIGNRFVHTGRPTPEAYAQALSE--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 449 QSALL--VPTLFSFFAKSTLIDKYdLSNLHEIASGGAPLSKEVGEAVAkrfHLPGIR--QGYGLTETtsaiLIT----PE 520
Cdd:PRK07787 216 GGTLYfgVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLA---ALTGHRpvERYGMTET----LITlstrAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 521 GDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQR--GELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHF 598
Cdd:PRK07787 288 GERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 599 FIVDRlKS--LIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVleHGKTMTEKEIVDYVASQVTTAK 676
Cdd:PRK07787 367 RIVGR-EStdLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSVHK 443
|
490 500
....*....|....*....|....*.
gi 1886431185 677 KLRgGVVFVDEVPKGLTGKLDARKIR 702
Cdd:PRK07787 444 RPR-EVRFVDALPRNAMGKVLKKQLL 468
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
358-702 |
2.09e-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: 177.29 E-value: 2.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGValPHRTACVRFSH---ARDPIFGnqiiPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLM-- 431
Cdd:cd05944 4 VAAYFHTGGTTGTPKLA--QHTHSNEVYNAwmlALNSLFD----PDDVLLCGLPLFHVNGSVVTLLTPLAsGAHVVLAgp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 --YR----FEEelFLRSLQDYKIQSALLVPTLFSffAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQG 505
Cdd:cd05944 78 agYRnpglFDN--FWKLVERYRITSLSTVPTVYA--ALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLP-VVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 506 YGLTETTSAILIT-PEGDDKPGAVGKVVPFFEAKVVDLD----TGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDk 580
Cdd:cd05944 153 YGLTEATCLVAVNpPDGPKRPGSVGLRLPYARVRIKVLDgvgrLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVA- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 581 DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT 660
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1886431185 661 EKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIR 702
Cdd:cd05944 312 EEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
358-702 |
9.74e-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: 177.67 E-value: 9.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRT---ACVRFSHArdpIFGNQiiPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYR 433
Cdd:cd05958 99 ICILAFTSGTTGAPKATMHFHRDplaSADRYAVN---VLRLR--EDDRFVGSPPLAFTFGLGGVLLFpFGVGASGVLLEE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 434 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTS 513
Cdd:cd05958 174 ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIP-IIDGIGSTEMFH 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 514 AILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPmimSGYVNNPEATNALIDKDGWLHSGDIAYWD 593
Cdd:cd05958 253 IFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 594 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVAS 670
Cdd:cd05958 329 PDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAKA 408
|
330 340 350
....*....|....*....|....*....|..
gi 1886431185 671 QVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 702
Cdd:cd05958 409 HIAPYKYPR-AIEFVTELPRTATGKLQRFALR 439
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
218-709 |
1.52e-48 |
|
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: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSkk 297
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 glqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvPESFDRD--KTIALIMNSSGSTGLPKGVA 375
Cdd:cd05969 80 ---------------------------------------------------EELYERTdpEDPTLLHYTSGTTGTPKGVL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 376 LPHR-------TACVRFSHARDPIFGNQIIP----DTAILSVVPFHHGFGMfttlgylicgfrVVLMYRFEEELFLRSLQ 444
Cdd:cd05969 109 HVHDamifyyfTGKYVLDLHPDDIYWCTADPgwvtGTVYGIWAPWLNGVTN------------VVYEGRFDAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 445 DYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETtSAILIT--PE 520
Cdd:cd05969 177 RVKVTVWYTAPTAIRMLMKEgdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP-IHDTWWQTET-GSIMIAnyPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 521 GDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRG--PMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHF 598
Cdd:cd05969 255 MPIKPGSMGKPLPGVKAAVVDEN-GNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 599 FIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVasqvttA 675
Cdd:cd05969 333 WFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFV------R 406
|
490 500 510
....*....|....*....|....*....|....*....
gi 1886431185 676 KKLRGGVV-----FVDEVPKGLTGKLDARkireiLIKAK 709
Cdd:cd05969 407 QKLGAHVApreieFVDNLPKTRSGKIMRR-----VLKAK 440
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
208-703 |
2.82e-48 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 179.32 E-value: 2.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 208 FTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGIS 287
Cdd:PRK04319 65 YLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 288 QPTVVFVSKKGLQKIlnVQKKLPIIQKIIIMDSKTDYQGfqsmytfVTSHLPPGFNEY--DFVPESFDRDKTiALIMNSS 365
Cdd:PRK04319 145 EAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEEGP-------GTLDFNALMEQAsdEFDIEWTDREDG-AILHYTS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 366 GSTGLPKGVALPHRTACVRFSHAR---------------DP---------IFGnqiipdtailsvvPFHHGFGMfttlgy 421
Cdd:PRK04319 215 GSTGKPKGVLHVHNAMLQHYQTGKyvldlheddvywctaDPgwvtgtsygIFA-------------PWLNGATN------ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 422 licgfrVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLIDKYDLSNLHEIASGGAPLSKEV---GEAVakr 496
Cdd:PRK04319 276 ------VIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLmgAGDDLVKKYDLSSLRHILSVGEPLNPEVvrwGMKV--- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 497 FHLPgIRQGYGLTETtSAILI--TPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG--PMIMSGYVNNPE 572
Cdd:PRK04319 347 FGLP-IHDNWWMTET-GGIMIanYPAMDIKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKgwPSMMRGIWNNPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 573 ATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 652
Cdd:PRK04319 424 KYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVA 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 653 LEHGKTMTE---KEIVDYVasqvttaKKLRGGVV------FVDEVPKGLTGKLDAR--KIRE 703
Cdd:PRK04319 503 LRPGYEPSEelkEEIRGFV-------KKGLGAHAapreieFKDKLPKTRSGKIMRRvlKAWE 557
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
216-703 |
3.86e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 177.39 E-value: 3.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 216 DITYAEyFEMSVRLAEAM-KRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiynerellnsMGISQPTVVFV 294
Cdd:PRK06145 27 EISYAE-FHQRILQAAGMlHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN-----------YRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 295 SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPpgfneydFVPESFDRDKTIALIMNSSGSTGLPKGV 374
Cdd:PRK06145 95 LGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLE-------IPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 375 AlpHRTACVRFSHArDPIFGNQIIPDTAILSVVPFHH-GFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALL 453
Cdd:PRK06145 168 M--HSYGNLHWKSI-DHVIALGLTASERLLVVGPLYHvGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 454 VPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGD--DKPGAVGKV 531
Cdd:PRK06145 245 APVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGReiEKIGSTGRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 532 VPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYK 611
Cdd:PRK06145 325 LAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 612 GYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVfVDEVPKG 691
Cdd:PRK06145 403 GENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKV-RDELPRN 481
|
490
....*....|..
gi 1886431185 692 LTGKLDARKIRE 703
Cdd:PRK06145 482 PSGKVLKRVLRD 493
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
185-707 |
4.86e-48 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 178.02 E-value: 4.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 185 DGTAGEQLHKAMKRYalvPGTIAFTDAHiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFI 264
Cdd:PRK06087 22 DASLADYWQQTARAM---PDKIAVVDNH-GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 265 GVAVAPANDIYNERELLNSMGISQPTVVFV-----SKKGLQKILNVQKKLPIIQKIIIMDSKTdyqgfQSMYTFVTSH-L 338
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLA-----PATSSLSLSQiI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 339 PPGFNEYDFVPESFDrdkTIALIMNSSGSTGLPKGVALPHRTacVRFSHaRDPIFGNQIIPDTAILSVVPFHHGFGMF-- 416
Cdd:PRK06087 173 ADYEPLTTAITTHGD---ELAAVLFTSGTEGLPKGVMLTHNN--ILASE-RAYCARLNLTWQDVFMMPAPLGHATGFLhg 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 417 TTLGYLIcGFRVVLMYRFEEELFLRSLQDYKIqSALLVPTLFSFFAKSTL-IDKYDLSNLHEIASGGAPLSKEVgeavAK 495
Cdd:PRK06087 247 VTAPFLI-GARSVLLDIFTPDACLALLEQQRC-TCMLGATPFIYDLLNLLeKQPADLSALRFFLCGGTTIPKKV----AR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 496 RFHLPGIR--QGYGLTETTSAILITPegdDKP-----GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYV 568
Cdd:PRK06087 321 ECQQRGIKllSVYGSTESSPHAVVNL---DDPlsrfmHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 569 NNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPA 648
Cdd:PRK06087 397 DEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSC 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 649 AVVVL-EHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREILIK 707
Cdd:PRK06087 477 AYVVLkAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMR 536
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
206-703 |
8.11e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 176.63 E-value: 8.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 206 IAFTDAHIevdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMG 285
Cdd:PRK08276 5 MAPSGEVV----TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 286 ISQPTVVFVSKKGLQKILNVQKKLPIIQKIIIMDSKTdyqgfqsmytfvtshlPPGFNEY----DFVPESFDRDKTIALI 361
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGP----------------VPGFRSYeealAAQPDTPIADETAGAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 362 MN-SSGSTGLPKGV--ALPHRTACVR-FSHARDPIFGNQIIPDTAILSVVPFHHG----FGMFTtlgyLICGFRVVLMYR 433
Cdd:PRK08276 145 MLySSGTTGRPKGIkrPLPGLDPDEApGMMLALLGFGMYGGPDSVYLSPAPLYHTaplrFGMSA----LALGGTVVVMEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 434 FEEELFLRSLQDYKIQSALLVPTLFSFFAKstLID----KYDLSNLHEIASGGAPLSKEVgeavaKRFHL----PGIRQG 505
Cdd:PRK08276 221 FDAEEALALIERYRVTHSQLVPTMFVRMLK--LPEevraRYDVSSLRVAIHAAAPCPVEV-----KRAMIdwwgPIIHEY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 506 YGLTETTSAILITPEgD--DKPGAVGKVVpFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGW 583
Cdd:PRK08276 294 YASSEGGGVTVITSE-DwlAHPGSVGKAV-LGEVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 584 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE-- 661
Cdd:PRK08276 371 VTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDal 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1886431185 662 -KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK08276 451 aAELIAWLRGRLAHYKCPR-SIDFEDELPRTPTGKLYKRRLRD 492
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
184-705 |
4.44e-47 |
|
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: 4.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 184 EDGTAGEQLHKAMKRYalvPGTIAFTDAHIEvdITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALF 263
Cdd:COG1021 23 RGETLGDLLRRRAERH---PDRIAVVDGERR--LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 264 IG---VAVAPAndiYNERELLNSMGISQPTVVFVSKK----GLQKILN-VQKKLPIIQKIIIMDSKTDYQGFQSMYTFVT 335
Cdd:COG1021 98 AGaipVFALPA---HRRAEISHFAEQSEAVAYIIPDRhrgfDYRALAReLQAEVPSLRHVLVVGDAGEFTSLDALLAAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 336 SHLPPGfneydfvPESFDrdktIALIMNSSGSTGLPKGVALPHRT-AC-VRFShARdpIFGnqIIPDTAILSVVPFHHGF 413
Cdd:COG1021 175 DLSEPR-------PDPDD----VAFFQLSGGTTGLPKLIPRTHDDyLYsVRAS-AE--ICG--LDADTVYLAALPAAHNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 414 GM--FTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGE 491
Cdd:COG1021 239 PLssPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 492 AVAKRFHlPGIRQGYGLTEttSAILITPEGDD---------KPgavgkVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM 562
Cdd:COG1021 319 RVRPALG-CTLQQVFGMAE--GLVNYTRLDDPeevilttqgRP-----ISPDDEVRIVD-EDGNPVPPGEVGELLTRGPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 563 IMSGYVNNPEAtNAL-IDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDD 641
Cdd:COG1021 390 TIRGYYRAPEH-NARaFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDE 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886431185 642 DAGELPAAVVVLeHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:COG1021 469 YLGERSCAFVVP-RGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
359-702 |
6.99e-47 |
|
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: 172.23 E-value: 6.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHRtacVRFSHARDPIFGNQIIPDTAILSVVPFHHGF--GMFTTL-GYLICGFRVVL--MYR 433
Cdd:cd05971 91 ALIIYTSGTTGPPKGALHAHR---VLLGHLPGVQFPFNLFPRDGDLYWTPADWAWigGLLDVLlPSLYFGVPVLAhrMTK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 434 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTE--- 510
Cdd:cd05971 168 FDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVE-VNEFYGQTEcnl 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 511 --TTSAILitpeGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVR--GPMIMSGYVNNPEATNALIdKDGWLHS 586
Cdd:cd05971 247 viGNCSAL----FPIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 587 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KE 663
Cdd:cd05971 321 GDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDalaRE 400
|
330 340 350
....*....|....*....|....*....|....*....
gi 1886431185 664 IVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIR 702
Cdd:cd05971 401 IQELVKTRLAAHEYPR-EIEFVNELPRTATGKIRRRELR 438
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
364-703 |
2.70e-46 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 172.19 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 364 SSGSTGLPKGV----ALPHRTAcvRFSHARDPIFGnqIIPDTAILSVVPFHH----GFGMFT-TLGYLIcgfrvVLMYRF 434
Cdd:PRK12406 160 TSGTTGHPKGVrraaPTPEQAA--AAEQMRALIYG--LKPGIRALLTGPLYHsapnAYGLRAgRLGGVL-----VLQPRF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEELFLRSLQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETT 512
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWG-PVIYEYYGSTESG 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 513 SAILITPEgD--DKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGP-MIMSGYVNNPEAtNALIDKDGWLHSGDI 589
Cdd:PRK12406 310 AVTFATSE-DalSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAgNPDFTYHNKPEK-RAEIDRGGFITSGDV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 590 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVA 669
Cdd:PRK12406 387 GYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLK 466
|
330 340 350
....*....|....*....|....*....|....
gi 1886431185 670 SQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK12406 467 ARLAGYKVPK-HIEIMAELPREDSGKIFKRRLRD 499
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
360-703 |
4.41e-46 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 171.02 E-value: 4.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGV--ALPHRTACVrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEE 437
Cdd:cd05929 129 KMLYSGGTTGRPKGIkrGLPGGPPDN--DTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 438 LFLRSLQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVakrFHL--PGIRQGYGLTETTS 513
Cdd:cd05929 207 EFLRLIERYRVTFAQFVPTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQW---IDWggPIIWEYYGGTEGQG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 514 AILITpeGDD---KPGAVGKVVpFFEAKVVDLDtGKTLGVNQRGELCVRGPMiMSGYVNNPEATNALIDKDGWLHSGDIA 590
Cdd:cd05929 284 LTIIN--GEEwltHPGSVGRAV-LGKVHILDED-GNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 591 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVV---VLEHGKTMTEKEIVDY 667
Cdd:cd05929 359 YLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpaPGADAGTALAEELIAF 438
|
330 340 350
....*....|....*....|....*....|....*.
gi 1886431185 668 VASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:cd05929 439 LRDRLSRYKCPR-SIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
217-695 |
1.58e-45 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 170.06 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSk 296
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 kglqkilnvQKKLPIIQKIiimdskTDYQGFQSMYTF----------VTSHLPPgfneyDFVPESFDRDKtIALIMNSSG 366
Cdd:PRK07514 108 ---------PANFAWLSKI------AAAAGAPHVETLdadgtgslleAAAAAPD-----DFETVPRGADD-LAAILYTSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 367 STGLPKGVALPHRT----ACV-----RFShardpifgnqiiPDTAILSVVPFHHGFGMF-TTLGYLICGFRVVLMYRFEE 436
Cdd:PRK07514 167 TTGRSKGAMLSHGNllsnALTlvdywRFT------------PDDVLIHALPIFHTHGLFvATNVALLAGASMIFLPKFDP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 437 ELFLRSLQdykiQSALL--VPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRF-HlpGIRQGYGLTETts 513
Cdd:PRK07514 235 DAVLALMP----RATVMmgVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTgH--AILERYGMTET-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 514 aILIT--P-EGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIA 590
Cdd:PRK07514 307 -NMNTsnPyDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 591 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVAS 670
Cdd:PRK07514 386 KIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKG 465
|
490 500
....*....|....*....|....*.
gi 1886431185 671 QVttAK-KLRGGVVFVDEVPKGLTGK 695
Cdd:PRK07514 466 RL--ARfKQPKRVFFVDELPRNTMGK 489
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
203-705 |
1.81e-45 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 170.62 E-value: 1.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAHIE----VDITYAEYFEMSVRLAEAMKRYGLNTNHriVVCSE--NSLQFFMPVLGALFIGVAVAPANDIYN 276
Cdd:PRK13295 38 PDKTAVTAVRLGtgapRRFTYRELAALVDRVAVGLARLGVGRGD--VVSCQlpNWWEFTVLYLACSRIGAVLNPLMPIFR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 277 ERELLNSMGISQPTVVFVSK--KGL---QKILNVQKKLPIIQKIIIMDSKTDyQGFQSMYTfvtshlPPGFNEYDFVPES 351
Cdd:PRK13295 116 ERELSFMLKHAESKVLVVPKtfRGFdhaAMARRLRPELPALRHVVVVGGDGA-DSFEALLI------TPAWEQEPDAPAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 352 FDRDKT----IALIMNSSGSTGLPKGVAlphrtacvrfsHARDPIFGNqIIP---------DTAILSVVPFHH--GFgMF 416
Cdd:PRK13295 189 LARLRPgpddVTQLIYTSGTTGEPKGVM-----------HTANTLMAN-IVPyaerlglgaDDVILMASPMAHqtGF-MY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 417 TTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKR 496
Cdd:PRK13295 256 GLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 497 FHLPgIRQGYGLTETTSAILITPEGDDKPGAV--GKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEAT 574
Cdd:PRK13295 336 LGAK-IVSAWGMTENGAVTLTKLDDPDERASTtdGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 575 NalIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLE 654
Cdd:PRK13295 414 G--TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 655 HGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:PRK13295 492 PGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
187-704 |
1.65e-44 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 172.42 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 187 TAGEQLHKAMKRyalVPGTIAFTDAhIEVDITYAEYFEMSVRLAEAMKRYGLNTNHrIVVCSENSLQFFMPVLGALFIGV 266
Cdd:PRK08633 616 PLAEAWIDTAKR---NWSRLAVADS-TGGELSYGKALTGALALARLLKRELKDEEN-VGILLPPSVAGALANLALLLAGK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 267 AVAPANDIYNERELLNSMGISQPTVVFVSKKGLQKI--LNVQKKLPIIQKIIIM-DSKTDYQGFQSMYTFVTSHLPPGFN 343
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLknKGFDLELPENVKVIYLeDLKAKISKVDKLTALLAARLLPARL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 344 EYDFVPESFDRDKTIALIMnSSGSTGLPKGVALPHRTacvrfshardpIFGN-----QIIP---DTAILSVVPFHHGFGM 415
Cdd:PRK08633 771 LKRLYGPTFKPDDTATIIF-SSGSEGEPKGVMLSHHN-----------ILSNieqisDVFNlrnDDVILSSLPFFHSFGL 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 416 -FTTLGYLICGFRVVLMYRFEEELFLRSLQDyKIQSALLV--PTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEA 492
Cdd:PRK08633 839 tVTLWLPLLEGIKVVYHPDPTDALGIAKLVA-KHRATILLgtPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADA 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 493 VAKRFHLPgIRQGYGLTETTSAILI-TP---EGDD------KPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPM 562
Cdd:PRK08633 918 FEEKFGIR-ILEGYGATETSPVASVnLPdvlAADFkrqtgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQ 996
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 563 IMSGYVNNPEATNALI---DKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQhpnIFDAG----- 634
Cdd:PRK08633 997 VMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK---ALGGEevvfa 1073
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 635 VAGLPDDDAGElpaAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 704
Cdd:PRK08633 1074 VTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
218-708 |
2.73e-44 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 167.24 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 297
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 GLQKILNVQKKLPIIQKIIIMDSKtdyqgfqsmytfVTSHLPPGFNEYDFVP--ESFD----RDKTIALIMNSSGSTGLP 371
Cdd:PRK06155 128 LLAALEAADPGDLPLPAVWLLDAP------------ASVSVPAGWSTAPLPPldAPAPaaavQPGDTAAILYTSGTTGPS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 372 KGVALPHrtacvrfshARDPIFGN------QIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQD 445
Cdd:PRK06155 196 KGVCCPH---------AQFYWWGRnsaedlEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 446 YKIQSALLVPTLFSFFAKSTlidKYDLSNLHEIASGGAP-LSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPeGDDK 524
Cdd:PRK06155 267 HGATVTYLLGAMVSILLSQP---ARESDRAHRVRVALGPgVPAALHAAFRERFGVD-LLDGYGSTETNFVIAVTH-GSQR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 525 PGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG--PM-IMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIV 601
Cdd:PRK06155 342 PGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 602 DRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgG 681
Cdd:PRK06155 420 DRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPR-Y 498
|
490 500
....*....|....*....|....*..
gi 1886431185 682 VVFVDEVPKGLTGKLDARKIREILIKA 708
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLREQGVTA 525
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
364-705 |
1.86e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 164.44 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 364 SSGSTGLPKGVALPHRT-ACVRFSHARDpifgnqIIPDT----AILSVVPFHHGFGMfttlgYLIC----GFRVVLMY-- 432
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQmAFVITNHLAD------LMPGTteqdASLVVAPLSHGAGI-----HQLCqvarGAATVLLPse 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 433 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETT 512
Cdd:PRK07470 240 RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLG-KVLVQYFGLGEVT 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 513 SAILITP----EGDDKP----GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAtNALIDKDGWL 584
Cdd:PRK07470 319 GNITVLPpalhDAEDGPdariGTCGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEA-NAKAFRDGWF 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 585 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEI 664
Cdd:PRK07470 397 RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAEL 476
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1886431185 665 VDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:PRK07470 477 LAWLDGKV--ARyKLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| UBI4 |
COG5272 |
Ubiquitin [Posttranslational modification, protein turnover, chaperones]; |
92-179 |
7.10e-43 |
|
Ubiquitin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444084 [Multi-domain] Cd Length: 213 Bit Score: 154.18 E-value: 7.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLRLRGGMEDA- 170
Cdd:COG5272 2 QIFVKTLTGKTITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLEDDRTLADYNIQKESTLHLVTRTLGISEIEl 81
|
....*....
gi 1886431185 171 KNIKKGPAP 179
Cdd:COG5272 82 SNLKLDLDP 90
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
184-697 |
7.17e-43 |
|
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: 7.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 184 EDGTAGEQLHKAMKRYalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALF 263
Cdd:cd05920 13 QDEPLGDLLARSAARH---PDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 264 IGVAVAPANDIYNERELLNSMGISQPTVVFVSKKglqkilnvqkklpiiqkiiimdsktdYQGFQSMYTFVTSHlppgfn 343
Cdd:cd05920 88 LGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDR--------------------------HAGFDHRALARELA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 344 eyDFVPEsfdrdktIALIMNSSGSTGLPKGVALPHR------TACVRFSHardpifgnqIIPDTAILSVVPFHHGFGMFT 417
Cdd:cd05920 136 --ESIPE-------VALFLLSGGTTGTPKLIPRTHNdyaynvRASAEVCG---------LDQDTVYLAVLPAAHNFPLAC 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 418 --TLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAK 495
Cdd:cd05920 198 pgVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 496 RFHlPGIRQGYGLTETtsaiLITPEGDDKPGAV-----GK-VVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVN 569
Cdd:cd05920 278 VLG-CTLQQVFGMAEG----LLNYTRLDDPDEViihtqGRpMSPDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 570 NPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAA 649
Cdd:cd05920 352 APEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCA 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 650 VVVLEHGKT--------MTEKEIVDYvasqvttakKLRGGVVFVDEVPKGLTGKLD 697
Cdd:cd05920 432 FVVLRDPPPsaaqlrrfLRERGLAAY---------KLPDRIEFVDSLPLTAVGKID 478
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
212-702 |
1.32e-42 |
|
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: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 212 HIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTV 291
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 292 VFVSkkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfdrDKTIALIMNSSGSTGLP 371
Cdd:cd05919 86 VVTS-----------------------------------------------------------ADDIAYLLYSSGTTGPP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 372 KGVALPHR---TACVRFSHardPIFGnqIIPDTAILSVVPFHHGFGMFTTL-GYLICGFRVVLM--YRFEEELFLRSLQd 445
Cdd:cd05919 107 KGVMHAHRdplLFADAMAR---EALG--LTPGDRVFSSAKMFFGYGLGNSLwFPLAVGASAVLNpgWPTAERVLATLAR- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 446 YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKP 525
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGP-ILDGIGATEVGHIFLSNRPGAWRL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 526 GAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLK 605
Cdd:cd05919 260 GSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRAD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 606 SLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK---EIVDYVASQVtTAKKLRGGV 682
Cdd:cd05919 338 DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERL-SAHKVPRRI 416
|
490 500
....*....|....*....|
gi 1886431185 683 VFVDEVPKGLTGKLDARKIR 702
Cdd:cd05919 417 AFVDELPRTATGKLQRFKLR 436
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
212-696 |
4.48e-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: 159.14 E-value: 4.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 212 HIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTV 291
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 292 VFVSkkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRDKTiALIMNSSGSTGLP 371
Cdd:cd05914 83 IFVS---------------------------------------------------------DEDDV-ALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 372 KGVALPHRT--ACVRFSHARDPifgnqIIPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELfLRSLQDYKI 448
Cdd:cd05914 105 KGVMLTYRNivSNVDGVKEVVL-----LGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAK-IIALAFAQV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 449 QSALLVPTLFSFF--AKSTLIDKYDLS-----------------------------NLHEIASGGAPLSKEVgEAVAKRF 497
Cdd:cd05914 179 TPTLGVPVPLVIEkiFKMDIIPKLTLKkfkfklakkinnrkirklafkkvheafggNIKEFVIGGAKINPDV-EEFLRTI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 498 HLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGktlgvNQRGELCVRGPMIMSGYVNNPEATNAL 577
Cdd:cd05914 258 GFPYT-IGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPA-----TGEGEIIVRGPNVMKGYYKNPEATAEA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 578 IDKDGWLHSGDIAYWDEDEHFFIVDRLKSLI-KYKGYQVAPAELESILLQHPNIFDAGVaGLPDDDAGEL----PAAVVV 652
Cdd:cd05914 332 FDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLV-VVQEKKLVALayidPDFLDV 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1886431185 653 LEHGKTMTEK----EIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKL 696
Cdd:cd05914 411 KALKQRNIIDaikwEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKI 458
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
360-697 |
5.19e-42 |
|
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: 5.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVP-FHHGFgMFTTLGYLICGFRVVLMYRFEEEL 438
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQAL---LAQALVLAVLQAIDEGTVFLNSGPlFHIGT-LMFTLATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 439 FLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHeiASGGAPLSKEVGEAVAKRF-HLPGirqGYGLTETTSAILI 517
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLR--SSPAAPEWNDMATVDTSPWgRKPG---GYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 518 TPEGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEaTNALIDKDGWLHSGDIAYWDEDEH 597
Cdd:cd17636 155 AALGGGAIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPE-VNARRTRGGWHHTNDLGRREPDGS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 598 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKK 677
Cdd:cd17636 233 LSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKK 312
|
330 340
....*....|....*....|
gi 1886431185 678 LRgGVVFVDEVPKGLTGKLD 697
Cdd:cd17636 313 PK-SVEFADALPRTAGGADD 331
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
218-679 |
2.33e-41 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 159.19 E-value: 2.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPtVVFVSKK 297
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRP-VMLVTDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 GLQK--ILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHL------PPGFNeYDFVPESfdrdktIALIMNSSGSTG 369
Cdd:PLN02860 113 TCSSwyEELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLkqralgTTELD-YAWAPDD------AVLICFTSGTTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 370 LPKGVALPHRtACVRFSHARDPIFGNQiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQ 449
Cdd:PLN02860 186 RPKGVTISHS-ALIVQSLAKIAIVGYG--EDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 450 SALLVPTLFS---FFAKSTLIDKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTET--------------- 511
Cdd:PLN02860 263 SMITVPAMMAdliSLTRKSMTWKVFPS-VRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhdptle 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 TSAILITPEGDDKPGA--------VGKVVPFFEAKVVDLDTGKTlgvnqrGELCVRGPMIMSGYVNNPEATNALIDKDGW 583
Cdd:PLN02860 342 SPKQTLQTVNQTKSSSvhqpqgvcVGKPAPHVELKIGLDESSRV------GRILTRGPHVMLGYWGQNSETASVLSNDGW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 584 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKE 663
Cdd:PLN02860 416 LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNE 495
|
490
....*....|....*.
gi 1886431185 664 IVDYVASQVTTAKKLR 679
Cdd:PLN02860 496 KENAKKNLTLSSETLR 511
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
187-699 |
2.52e-41 |
|
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: 2.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 187 TAGEQLHKAMKRyalVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGV 266
Cdd:cd05923 2 TVFEMLRRAASR---APDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 267 AVAPANDIYNEREL--LNSMGISQPTVVFVSKKGLQKIlnvqkklpiIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGfne 344
Cdd:cd05923 79 VPALINPRLKAAELaeLIERGEMTAAVIAVDAQVMDAI---------FQSGVRVLALSDLVGLGEPESAGPLIEDPP--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 345 ydfvpesfDRDKTIALIMNSSGSTGLPKGVALPHRTACVR---FSHARDPIFGNQiipdTAILSVVPFHHGFGMFTTL-G 420
Cdd:cd05923 147 --------REPEQPAFVFYTSGTTGLPKGAVIPQRAAESRvlfMSTQAGLRHGRH----NVVLGLMPLYHVIGFFAVLvA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 421 YLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKrfHLP 500
Cdd:cd05923 215 ALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ--HLP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 501 GIRQG-YGLTETTSAiLITPegDDKPGAVGKVVPFFEAKVVDLDTG--KTLGVNQRGELCVR--GPMIMSGYVNNPEATN 575
Cdd:cd05923 293 GEKVNiYGTTEAMNS-LYMR--DARTGTEMRPGFFSEVRIVRIGGSpdEALANGEEGELIVAaaADAAFTGYLNQPEATA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 576 ALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 655
Cdd:cd05923 370 KKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1886431185 656 GkTMTEKEIVDY-VASQVTTAKKLRgGVVFVDEVPKGLTGKLDAR 699
Cdd:cd05923 449 G-TLSADELDQFcRASELADFKRPR-RYFFLDELPKNAMNKVLRR 491
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
217-704 |
2.74e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 158.51 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 296
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYER 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQ---SMYTFVTShlppGFNEYDFVPESFDrDktiALIMNSSGSTGLPKG 373
Cdd:PRK07798 109 EFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPgavDYEDALAA----GSPERDFGERSPD-D---LYLLYTGGTTGMPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 374 VALphRTACVRFSH--ARDPIFGNQI------------IPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL--MYRFEEE 437
Cdd:PRK07798 181 VMW--RQEDIFRVLlgGRDFATGEPIedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLlpDVRFDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 438 LFLRSLQDYKIQSALLVPTLFsffAKStLID------KYDLSNLHEIASGGAPLSKEVGEAVAKrfHLPG--IRQGYGLT 509
Cdd:PRK07798 259 EVWRTIEREKVNVITIVGDAM---ARP-LLDaleargPYDLSSLFAIASGGALFSPSVKEALLE--LLPNvvLTDSIGSS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 510 ETTSAILITPegddKPGAVGKVVPFFEA----KVVDLDTGKTL-GVNQRGELCVRGPmIMSGYVNNPEATNAL---IDKD 581
Cdd:PRK07798 333 ETGFGGSGTV----AKGAVHTGGPRFTIgprtVVLDEDGNPVEpGSGEIGWIARRGH-IPLGYYKDPEKTAETfptIDGV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 582 GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 661
Cdd:PRK07798 408 RYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1886431185 662 KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREI 704
Cdd:PRK07798 488 AELRAHCRSSLAGYKVPR-AIWFVDEVQRSPAGKADYRWAKEQ 529
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
218-702 |
2.95e-41 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 157.92 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 297
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 GLQKILNVQKKLPI-IQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEYdfVPESFDrdkTIALIMNSSGSTGLPKGVAL 376
Cdd:PRK08008 119 FYPMYRQIQQEDATpLRHICLTRVALPADDGVSSFTQLKAQQPATLCYA--PPLSTD---DTAEILFTSGTTSRPKGVVI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 377 PHrtACVRFSHardpIFG---NQIIPDTAILSVVP-FHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYK----- 447
Cdd:PRK08008 194 TH--YNLRFAG----YYSawqCALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRatite 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 448 -----IQSALLVPTL----------FSFFakstlidkydlsnLHeiasggapLSKEVGEAVAKRFhlpGIR--QGYGLTE 510
Cdd:PRK08008 268 cipmmIRTLMVQPPSandrqhclreVMFY-------------LN--------LSDQEKDAFEERF---GVRllTSYGMTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 511 TTSAILITPEGDDK--PgAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRG---PMIMSGYVNNPEATNALIDKDGWLH 585
Cdd:PRK08008 324 TIVGIIGDRPGDKRrwP-SIGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 586 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 665
Cdd:PRK08008 402 TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFF 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 1886431185 666 DYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIR 702
Cdd:PRK08008 482 AFCEQNM--AKfKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
359-700 |
2.56e-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: 153.84 E-value: 2.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFE 435
Cdd:cd05930 96 AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY---PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLpeeVRKD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 436 EELFLRSLQDYKIQSALLVPTLFSFFAKStlIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTsaI 515
Cdd:cd05930 173 PEALADLLAEEGITVLHLTPSLLRLLLQE--LELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEAT--V 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 516 LIT----PEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD-----GWL 584
Cdd:cd05930 249 DATyyrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNpfgpgERM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 585 H-SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKE 663
Cdd:cd05930 328 YrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEE 407
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1886431185 664 IVDYVASQ-----VTTAkklrggVVFVDEVPKGLTGKLDARK 700
Cdd:cd05930 408 LRAHLAERlpdymVPSA------FVVLDALPLTPNGKVDRKA 443
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
176-703 |
3.98e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 155.29 E-value: 3.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 176 GPAPFYPLEDGTAGEQlhkamkryalvPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVV----CSEN- 250
Cdd:PRK06164 8 RADTLASLLDAHARAR-----------PDAVALIDE--DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVwlpnCIEWv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 251 SLQFFMPVLGALFIGVavapaNDIYNERELLNSMGISQPTVVFV--SKKGLQ--KILN-VQKK-LPIIQKIIIMDSKTDY 324
Cdd:PRK06164 75 VLFLACARLGATVIAV-----NTRYRSHEVAHILGRGRARWLVVwpGFKGIDfaAILAaVPPDaLPPLRAIAVVDDAADA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 325 QgfqSMYTFVTSHLPPGFNEYDFVP---ESFDRDKTIALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGnqIIPDT 401
Cdd:PRK06164 150 T---PAPAPGARVQLFALPDPAPPAaagERAADPDAGALLFTTSGTTSGPKLVLHRQATL-LRHARAIARAYG--YDPGA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 402 AILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKyDLSNLHE--IA 479
Cdd:PRK06164 224 VLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLfgFA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 480 SGGAPLSKEVGEAVAKRFHLPGIrqgYGLTETTSAILITPEGDD-----KPGAVgKVVPFFEAKVVDLDTGKTLGVNQRG 554
Cdd:PRK06164 303 SFAPALGELAALARARGVPLTGL---YGSSEVQALVALQPATDPvsvriEGGGR-PASPEARVRARDPQDGALLPDGESG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 555 ELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAG 634
Cdd:PRK06164 379 EIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQ 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 635 VAGLpDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTG---KLDARKIRE 703
Cdd:PRK06164 459 VVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREAL-AGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
201-705 |
1.45e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 152.65 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 201 LVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENS-----LQFFMPVLGALFIgvavaPANDIY 275
Cdd:PRK09088 7 LQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSvwlvaLHFACARVGAIYV-----PLNWRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 276 NERELLNSMGISQPTVVfVSKKGLQkilnvqkklpiiqkiiimDSKTDYQGFQSMYTFVTSHLPpgfneyDFVPeSFDRD 355
Cdd:PRK09088 82 SASELDALLQDAEPRLL-LGDDAVA------------------AGRTDVEDLAAFIASADALEP------ADTP-SIPPE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 356 KtIALIMNSSGSTGLPKGVALPHRTAcvrfshardpifgNQIIPDTAILSVVPFHHGF----GMFTTLGyLICGFRVVLM 431
Cdd:PRK09088 136 R-VSLILFTSGTSGQPKGVMLSERNL-------------QQTAHNFGVLGRVDAHSSFlcdaPMFHIIG-LITSVRPVLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 YR--------FEEELFLRSLQD--YKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAP-LSKEVGEAVAKrfhlp 500
Cdd:PRK09088 201 VGgsilvsngFEPKRTLGRLGDpaLGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPhAAEDILGWLDD----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 501 GIRQ--GYGLTETTSAILITPEG---DDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATN 575
Cdd:PRK09088 276 GIPMvdGFGMSEAGTVFGMSVDCdviRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 576 ALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 655
Cdd:PRK09088 355 RAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 656 GKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:PRK09088 435 GAPLDLERIRSHLSTRL--AKyKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
358-705 |
2.65e-39 |
|
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: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHR--TACVRFSHARDPIFGnqiiPDTAILSVVPFHHGfGMFTTLGYLICGFRVVLMYRfe 435
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAAnlLASAAGLHSRLGFGG----GDSWLLSLPLYHVG-GLAILVRSLLAGAELVLLER-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 436 EELFLRSLQDYKIQSALLVPT-LFSFFAKSTLIDkyDLSNLHEIASGGAPLSKEVGEAVAKRfHLPGIrQGYGLTETTSA 514
Cdd:cd17630 75 NQALAEDLAPPGVTHVSLVPTqLQRLLDSGQGPA--ALKSLRAVLLGGAPIPPELLERAADR-GIPLY-TTYGMTETASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 515 ILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEATnaLIDKDGWLHSGDIAYWDE 594
Cdd:cd17630 151 VATKRPDGFGRGGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLRGQLVP--EFNEDGWFTTKDLGELHA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 595 DEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKtmTEKEIVDYVASQVTT 674
Cdd:cd17630 218 DGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA--DPAELRAWLKDKLAR 295
|
330 340 350
....*....|....*....|....*....|.
gi 1886431185 675 AKKLRgGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:cd17630 296 FKLPK-RIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
364-697 |
4.84e-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: 147.17 E-value: 4.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 364 SSGSTGLPKGVALPHRTACVRFSHARDpIFgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEELFLRSL 443
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIESFVCNED-LF--NISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 444 QDYKIQSALLVPTLFSFFAKSTLIDkydlSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDD 523
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 524 KPGAVGKVVPFFEAKVVDLDTGKTlgvnqrGELCVRGPMIMSGYVNNPEatnalIDKDGWLHSGDIAYWDEDEHFFIVDR 603
Cdd:cd17633 161 PPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVRGGF-----SNPDGWMSVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 604 LKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVlehGKTMTEKEIVDYVASQVTTAKKLRgGVV 683
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPK-KII 305
|
330
....*....|....
gi 1886431185 684 FVDEVPKGLTGKLD 697
Cdd:cd17633 306 FVDSLPYTSSGKIA 319
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
361-703 |
8.41e-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: 8.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 361 IMNSSGSTGLPKGVALPHR------TACVRFSHARDP--IFGNqiIPDT-----AILSVV-PFHHGFGMFttlgylicgf 426
Cdd:cd05928 179 IYFTSGTTGSPKMAEHSHSslglglKVNGRYWLDLTAsdIMWN--TSDTgwiksAWSSLFePWIQGACVF---------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 427 rVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLiDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGY 506
Cdd:cd05928 247 -VHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDL-SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEGY 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 507 GLTETTsAILITPEGDD-KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVR-GPM----IMSGYVNNPEATNALIDK 580
Cdd:cd05928 324 GQTETG-LICANFKGMKiKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 581 DGWLhSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL-----EH 655
Cdd:cd05928 402 DFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLapqflSH 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1886431185 656 GKTMTEKEIVDYVASqVTTAKKLRGGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:cd05928 481 DPEQLTKELQQHVKS-VTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
217-628 |
1.53e-38 |
|
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: 150.83 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNT--NHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynereLLNSMGISqpTVVFV 294
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVP---------LYDTLGPE--AIEYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 295 SKKGLQKILNVQKKLPIIQKIIIMDsktdyQGFQsmytfvtshlppgfNEYDFVPESFDrdkTIALIMNSSGSTGLPKGV 374
Cdd:cd05927 75 LNHAEISIVFCDAGVKVYSLEEFEK-----LGKK--------------NKVPPPPPKPE---DLATICYTSGTTGNPKGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 375 ALPHR---TACVRFSHArdPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLmYRFEEELFLRSLQDYKIQSA 451
Cdd:cd05927 133 MLTHGnivSNVAGVFKI--LEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGF-YSGDIRLLLDDIKALKPTVF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 452 LLVPTLF--------------SFFAK---------------------STLIDKYDLS--------NLHEIASGGAPLSKE 488
Cdd:cd05927 210 PGVPRVLnriydkifnkvqakGPLKRklfnfalnyklaelrsgvvraSPFWDKLVFNkikqalggNVRLMLTGSAPLSPE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 489 VGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDL-DTGKT-LGVNQRGELCVRGPMIMSG 566
Cdd:cd05927 290 VLEFLRVALGCP-VLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVpEMNYDaKDPNPRGEVCIRGPNVFSG 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886431185 567 YVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHP 628
Cdd:cd05927 369 YYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSP 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
217-701 |
2.79e-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: 148.16 E-value: 2.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 296
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIADG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfdrdktiALIMNSSGSTGLPKGVAL 376
Cdd:cd05945 97 DDN-----------------------------------------------------------AYIIFTSGSTGRPKGVQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 377 PHRtACVRFSHARDPIFgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL----MYRFEEELFlRSLQDYKIQSAL 452
Cdd:cd05945 118 SHD-NLVSFTNWMLSDF--PLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPvprdATADPKQLF-RFLAEHGITVWV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 453 LVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT---SAILITPE--GDDKPGA 527
Cdd:cd05945 194 STPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATvavTYIEVTPEvlDGYDRLP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 528 VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA---LIDKDGWLHSGDIAYWDEDEHFFIVDRL 604
Cdd:cd05945 274 IGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRTGDLVRLEADGLLFYRGRL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 605 KSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG----KTMTEKE-----IVDYVASQvtta 675
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGaeagLTKAIKAelaerLPPYMIPR---- 428
|
490 500
....*....|....*....|....*.
gi 1886431185 676 kklrgGVVFVDEVPKGLTGKLDARKI 701
Cdd:cd05945 429 -----RFVYLDELPLNANGKIDRKAL 449
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
358-696 |
1.81e-37 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 143.17 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRTACVRFSHARdpIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLMYRFEE 436
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQ--KEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 437 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGA-PLSKEVgeAVAKRFHLPGIRQGYGLTETTSAI 515
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSrAIAADV--RFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 516 LItPEGDDKP--GAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWD 593
Cdd:cd17635 159 CL-PTDDDSIeiNAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 594 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV----LEHGKTMTEKEIVDYVA 669
Cdd:cd17635 236 EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVasaeLDENAIRALKHTIRREL 315
|
330 340
....*....|....*....|....*..
gi 1886431185 670 SQVTTAKKlrggVVFVDEVPKGLTGKL 696
Cdd:cd17635 316 EPYARPST----IVIVTDIPRTQSGKV 338
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
217-701 |
3.46e-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: 146.21 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMgiSQPTVvfvsk 296
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSL--NETEC----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 kglqkilnvqkklpiiqKIIIMDSKTDyqgfqsmytfvtshlppgfneydfvpesfdrdkTIALIMNSSGSTGLPKGVAL 376
Cdd:cd17639 79 -----------------SAIFTDGKPD---------------------------------DLACIMYTSGSTGNPKGVML 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 377 PHRTaCVRFSHARDPIFGNQIIPDTAILSVVPFHH-----------------GFGMFTTLGYLICG--------FRVVLM 431
Cdd:cd17639 109 THGN-LVAGIAGLGDRVPELLGPDDRYLAYLPLAHifelaaenvclyrggtiGYGSPRTLTDKSKRgckgdlteFKPTLM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 Y---------------------RFEEELFLRSLQdYKiQSALLVPTLFSF-----FAKstlIDKYDLSNLHEIASGGAPL 485
Cdd:cd17639 188 VgvpaiwdtirkgvlaklnpmgGLKRTLFWTAYQ-SK-LKALKEGPGTPLldelvFKK---VRAALGGRLRYMLSGGAPL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 486 SKEvgeavAKRF---HLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGK--TLGVNQRGELCVRG 560
Cdd:cd17639 263 SAD-----TQEFlniVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGysTDKPPPRGEILIRG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 561 PMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYK-GYQVAPAELESILLQHPNIFDAGVAGLP 639
Cdd:cd17639 338 PNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADP 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 640 DDDAgelPAAVVVLEHGKTMT-----------------EKEIVDYVASQVTT---AKKLRG-----GVVFVDEV--P-KG 691
Cdd:cd17639 418 DKSY---PVAIVVPNEKHLTKlaekhgvinseweelceDKKLQKAVLKSLAEtarAAGLEKfeipqGVVLLDEEwtPeNG 494
|
570
....*....|...
gi 1886431185 692 L---TGKLDARKI 701
Cdd:cd17639 495 LvtaAQKLKRKEI 507
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
215-703 |
5.20e-37 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 146.18 E-value: 5.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 215 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFV 294
Cdd:PRK05852 42 IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 295 SKKGL-QKILNVQKKLPIiqKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNeydfVPESFDRDKtiALIMNSSGSTGLPKG 373
Cdd:PRK05852 122 DADGPhDRAEPTTRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATS----TPEGLRPDD--AMIMFTGGTTGLPKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 374 VALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFEEELFLRSLQDYKIQS 450
Cdd:PRK05852 194 VPWTHANIA---SSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLparGRFSAHTFWDDIKAVGATW 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 451 ALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTSAILITP-EGDDK--- 524
Cdd:PRK05852 271 YTAVPTIHQILLEraATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVV-CAFGMTEATHQVTTTQiEGIGQten 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 525 ----PGAVGKVVPFfEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFI 600
Cdd:PRK05852 350 pvvsTGLVGRSTGA-QIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 601 VDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVtTAKKLRG 680
Cdd:PRK05852 427 RGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERL-AAFEIPA 505
|
490 500
....*....|....*....|...
gi 1886431185 681 GVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK05852 506 SFQEASGLPHTAKGSLDRRAVAE 528
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
218-635 |
6.81e-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: 6.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRY-GLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerellnsMGISQPTvvfvsk 296
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP-------------LDPAYPA------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLQKILNVqkklpIIQKIIIMDSktDYQGFQSMYTFVTSHLPPGFNEYD------FVPESFDRDKTIALIMNSSGSTGL 370
Cdd:TIGR01733 62 ERLAFILED-----AGARLLLTDS--ALASRLAGLVLPVILLDPLELAALddapapPPPDAPSGPDDLAYVIYTSGSTGR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 371 PKGVALPHRTACVRFSHARDPIFGNqiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMY----RFEEELFLRSLQDY 446
Cdd:TIGR01733 135 PKGVVVTHRSLVNLLAWLARRYGLD---PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 447 KIQSALLVPTLFSFFAKStliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT---SAILITPEGDD 523
Cdd:TIGR01733 212 PVTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTvwsTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 524 KPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATN--------ALIDKDGWLHSGDIAYWD 593
Cdd:TIGR01733 289 RESPVpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfAGGDGARLYRTGDLVRYL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1886431185 594 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGV 635
Cdd:TIGR01733 368 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
217-702 |
1.37e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 144.38 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 296
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLQKILNVQKKLPIIqkiIIMDSKTDyqGFQSMYTFVTSHLPPgfneydfvpesFDRDKTIALIMNSSGSTGLPKGVA- 375
Cdd:PRK13390 105 ALDGLAAKVGADLPLR---LSFGGEID--GFGSFEAALAGAGPR-----------LTEQPCGAVMLYSSGTTGFPKGIQp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 376 -LPHRTAcvrfSHARDPI-------FGnqIIPDTAILSVVPFHHGF-----GMFTTLGYlicgfRVVLMYRFEEELFLRS 442
Cdd:PRK13390 169 dLPGRDV----DAPGDPIvaiarafYD--ISESDIYYSSAPIYHAAplrwcSMVHALGG-----TVVLAKRFDAQATLGH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 443 LQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETTSAILI-TP 519
Cdd:PRK13390 238 VERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG-PIVYEYYSSTEAHGMTFIdSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 520 EGDDKPGAVGKVVpFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDG--WLHSGDIAYWDEDEH 597
Cdd:PRK13390 317 DWLAHPGSVGRSV-LGDLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 598 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE---KEIVDYVASQVTT 674
Cdd:PRK13390 395 LYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDelaRELIDYTRSRIAH 474
|
490 500
....*....|....*....|....*...
gi 1886431185 675 AKKLRgGVVFVDEVPKGLTGKLDARKIR 702
Cdd:PRK13390 475 YKAPR-SVEFVDELPRTPTGKLVKGLLR 501
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
361-704 |
2.89e-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: 144.77 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 361 IMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGnqIIPDTAILS------VVpfHHGFGMFttlGYLICGFRVVLmyrF 434
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYG--IKPGDVWWAasdvgwVV--GHSYIVY---GPLLHGATTVL---Y 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEE--------LFLRSLQDYKIQSALLVPTLFSFFAK----STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGI 502
Cdd:cd05967 305 EGKpvgtpdpgAFWRVIEKYQVNALFTAPTAIRAIRKedpdGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 503 RQgYGLTETTSAILITPEGDD----KPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPM---IMSGYVNNPEA-- 573
Cdd:cd05967 385 DH-WWQTETGWPITANPVGLEplpiKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLPLppgCLLTLWKNDERfk 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 574 TNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL 653
Cdd:cd05967 463 KLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVL 542
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 654 EHGKTMT----EKEIVDYVASQ---VTTAKKlrggVVFVDEVPKGLTGKLDARKIREI 704
Cdd:cd05967 543 KEGVKITaeelEKELVALVREQigpVAAFRL----VIFVKRLPKTRSGKILRRTLRKI 596
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
177-705 |
1.02e-35 |
|
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: 142.42 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 177 PAPFYPLEDGTAGEQLHKAMKRYALVpGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIV-VCSENslQFF 255
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTK-GITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVIlQFDDN--EDF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 256 MPVLGALFIG------VAVAPANDIYNER--------ELLNsmgisQPtVVFVSKKGLQKILNVQKKLPI-IQKIIIMDS 320
Cdd:cd05906 78 IPAFWACVLAgfvpapLTVPPTYDEPNARlrklrhiwQLLG-----SP-VVLTDAELVAEFAGLETLSGLpGIRVLSIEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 321 KTDYQGfqsmytfvtshlppgfnEYDFVPESFDrdkTIALIMNSSGSTGLPKGVALPHRTACVRFSHArdpIFGNQIIPD 400
Cdd:cd05906 152 LLDTAA-----------------DHDLPQSRPD---DLALLMLTSGSTGFPKAVPLTHRNILARSAGK---IQHNGLTPQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 401 TAILSVVPFHH--GFGMFTTLG-YLICG-FRV----VLMyrfEEELFLRSLQDYKIQsallvptlFSF---FAKSTLID- 468
Cdd:cd05906 209 DVFLNWVPLDHvgGLVELHLRAvYLGCQqVHVpteeILA---DPLRWLDLIDRYRVT--------ITWapnFAFALLNDl 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 469 -------KYDLSNLHEIASGGAPLSKEVGEAVA---KRFHLPG--IRQGYGLTETTSAIL--ITPEGDDKPGA-----VG 529
Cdd:cd05906 278 leeiedgTWDLSSLRYLVNAGEAVVAKTIRRLLrllEPYGLPPdaIRPAFGMTETCSGVIysRSFPTYDHSQAlefvsLG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 530 KVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDeDEHFFIVDRLKSLIK 609
Cdd:cd05906 358 RPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTII 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 610 YKGYQVAPAELESILLQHPNI---FDAGVAGLPDDDAGE------LPAAVVVLEHGKTMteKEIVDYVASQVTTAKKLrg 680
Cdd:cd05906 436 VNGVNYYSHEIEAAVEEVPGVepsFTAAFAVRDPGAETEelaiffVPEYDLQDALSETL--RAIRSVVSREVGVSPAY-- 511
|
570 580
....*....|....*....|....*..
gi 1886431185 681 gVVFV--DEVPKGLTGKLDARKIREIL 705
Cdd:cd05906 512 -LIPLpkEEIPKTSLGKIQRSKLKAAF 537
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
218-704 |
1.92e-35 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 142.08 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENS-----LQFFMPVLGALfigvaVAPANDIYNERELLNSMGISQPTVV 292
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTpamyeMHFAVPMAGAV-----LNPINTRLDATSIAAILRHAKPKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 293 FVSKKG---LQKILNV------QKKLPIIQkIIIMDSKT-------DYQGFQSMYTFVTSHLPPGF---NEYDfvPESFD 353
Cdd:PLN03102 116 FVDRSFeplAREVLHLlssedsNLNLPVIF-IHEIDFPKrpsseelDYECLIQRGEPTPSLVARMFriqDEHD--PISLN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 354 RdktialimnSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR 433
Cdd:PLN03102 193 Y---------TSGTTADPKGVVISHRGA---YLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 434 FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKR-FHlpgIRQGYGLTETT 512
Cdd:PLN03102 261 VTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLgFQ---VMHAYGLTEAT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 513 SAILIT---------PEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQR-----GELCVRGPMIMSGYVNNPEATNALI 578
Cdd:PLN03102 338 GPVLFCewqdewnrlPENQQMELKARQGVSILGLADVDVKNKETQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 579 dKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKT 658
Cdd:PLN03102 418 -KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGET 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1886431185 659 MTEKEIVDYVASQVTTAKKLRGG---------VVFVDEVPKGLTGKLDARKIREI 704
Cdd:PLN03102 497 TKEDRVDKLVTRERDLIEYCRENlphfmcprkVVFLQELPKNGNGKILKPKLRDI 551
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
360-696 |
1.88e-34 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 136.88 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMF-TTLGYLICGFRVVLMYR-FEEE 437
Cdd:cd05973 92 VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAV---DLRPEDSFWNAADPGWAYGLYyAITGPLALGHPTILLEGgFSVE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 438 LFLRSLQDYKIQSALLVPTLF-SFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETtSAIL 516
Cdd:cd05973 169 STWRVIERLGVTNLAGSPTAYrLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVP-IHDHYGQTEL-GMVL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 517 ITPEGDDKP---GAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCV---RGP-MIMSGYVNNPEATNAlidkDGWLHSGDI 589
Cdd:cd05973 247 ANHHALEHPvhaGSAGRAMPGWRVAVLDDD-GDELGPGEPGRLAIdiaNSPlMWFRGYQLPDTPAID----GGYYLTGDT 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 590 AYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT---EKEIVD 666
Cdd:cd05973 322 VEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQL 401
|
330 340 350
....*....|....*....|....*....|
gi 1886431185 667 YVASQVTTAKKLRgGVVFVDEVPKGLTGKL 696
Cdd:cd05973 402 HVKKRLSAHAYPR-TIHFVDELPKTPSGKI 430
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
197-703 |
2.19e-34 |
|
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: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 197 KRYALVPGTIAFT----DAHIEVDITYAEYFEMSVRLAEAMKRYGLnTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAN 272
Cdd:cd05931 1 RRAAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 273 DIYNERE---LLNSMGISQPTVVFVSKK---GLQKILNVQKKLPIIQkIIIMDSKTDyqgfqsmytfvtshLPPGfneyD 346
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLTTAAalaAVRAFAASRPAAGTPR-LLVVDLLPD--------------TSAA----D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 347 FVPESFDRDkTIALIMNSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGY-LICG 425
Cdd:cd05931 141 WPPPSPDPD-DIAYLQYTSGSTGTPKGVVVTHRNL---LANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTpLYSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 426 FRVVLM---------YRFeeelfLRSLQDYKIQ-SAllVPTlfsfFA--------KSTLIDKYDLSNLHEIASGGAPLSK 487
Cdd:cd05931 217 GPSVLMspaaflrrpLRW-----LRLISRYRATiSA--APN----FAydlcvrrvRDEDLEGLDLSSWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 488 EVGEAVAKRF---------HLPGirqgYGLTETTSAILITPEGD---------------------DKPGAV-----GKVV 532
Cdd:cd05931 286 ATLRRFAEAFapfgfrpeaFRPS----YGLAEATLFVSGGPPGTgpvvlrvdrdalagravavaaDDPAARelvscGRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 533 PFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNAL------IDKDGWLHSGDIAYWDEDEhFFIVDRLKS 606
Cdd:cd05931 362 PDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLHDGE-LYITGRLKD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 607 LIKYKGYQVAPAELESILLQHPNIFDAGVA---GLPDDDAGELpaaVVVLEHGKTMTE---KEIVDYVASQVTTAKKLR- 679
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPALRPGCVaafSVPDDGEERL---VVVAEVERGADPadlAAIAAAIRAAVAREHGVAp 517
|
570 580
....*....|....*....|....*.
gi 1886431185 680 GGVVFV--DEVPKGLTGKLDARKIRE 703
Cdd:cd05931 518 ADVVLVrpGSIPRTSSGKIQRRACRA 543
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
360-699 |
3.13e-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: 131.35 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQII-----------PDTAILSVVPFHHGFGMFTTLGYLICGFRV 428
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPsedahkaaaaaAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 429 VLM-YRFEEELFLRSLQDYKIQSALLVPTLFsffAKStLIDK------YDLSNLHEIASGGAPLSKEVGEAVAKRFHLPG 501
Cdd:cd05924 87 VLPdDRFDPEEVWRTIEKHKVTSMTIVGDAM---ARP-LIDAlrdagpYDLSSLFAISSGGALLSPEVKQGLLELVPNIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 502 IRQGYGLTETTS-AILITPEGDDKPGAVGKVVPffEAKVVDLDTGKTL-GVNQRGELCVRGpMIMSGYVNNPEAT-NALI 578
Cdd:cd05924 163 LVDAFGSSETGFtGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPpGSGGVGWIARRG-HIPLGYYGDEAKTaETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 579 DKDG--WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG 656
Cdd:cd05924 240 EVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1886431185 657 KTMTEKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDAR 699
Cdd:cd05924 320 AGVDLEELREHCRTRI-ARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
218-703 |
5.89e-33 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 134.11 E-value: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 297
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 GLQKILNVQKKLPIIQKIIIMDSKtdyqgfqsmytfvtSHLP----PGFNEY---------DFVPESFDRDkTIALIMNS 364
Cdd:PRK06018 121 FVPILEKIADKLPSVERYVVLTDA--------------AHMPqttlKNAVAYeewiaeadgDFAWKTFDEN-TAAGMCYT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 365 SGSTGLPKGVALPHRTacvRFSHArdpIFGNQiiPDT-------AILSVVPFHHGFGMFTTLGYLICGFRVVL------- 430
Cdd:PRK06018 186 SGTTGDPKGVLYSHRS---NVLHA---LMANN--GDAlgtsaadTMLPVVPLFHANSWGIAFSAPSMGTKLVMpgakldg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 431 --MYrfeeELflrsLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRFHLPGI--RQGY 506
Cdd:PRK06018 258 asVY----EL----LDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP----RSMIKAFEDMGVevRHAW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 507 GLTET----TSAILiTPEGDDKPGAVGKVV-------PF-FEAKVVDlDTGKTLGVNQR--GELCVRGPMIMSGYVnnpE 572
Cdd:PRK06018 326 GMTEMsplgTLAAL-KPPFSKLPGDARLDVlqkqgypPFgVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYY---R 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 573 ATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 652
Cdd:PRK06018 401 VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQ 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 653 LEHGKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK06018 481 LKPGETATREEILKYMDGKI--AKwWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
196-703 |
7.84e-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: 7.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 196 MKRYALVPGTIAFTDahieVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENslqffMPVLGALFIGVAVAPA---- 271
Cdd:cd05915 8 FGRKEVVSRLHTGEV----HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFN-----HFRHLEAYFAVPGMGAvlht 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 272 -NDIYNERELLNSMGISQPTVVFVSKKGLQKilnVQKKLPIIQKIiiMDSKTDYQGFQSMYTFVTSHLPpgfneyDFVP- 349
Cdd:cd05915 79 aNPRLSPKEIAYILNHAEDKVLLFDPNLLPL---VEAIRGELKTV--QHFVVMDEKAPEGYLAYEEALG------EEADp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 350 ESFDRDKTIALIMnSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQII--PDTAILSVVPFHHGFG-----MFTTLGYL 422
Cdd:cd05915 148 VRVPERAACGMAY-TTGTTGLPKGVVYSHRAL---VLHSLAASLVDGTAlsEKDVVLPVVPMFHVNAwclpyAATLVGAK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 423 ICGFRVVLmyrfEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPlSKEVGEAVaKRFHLPGI 502
Cdd:cd05915 224 QVLPGPRL----DPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSA-APRSLIAR-FERMGVEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 503 RQGYGLTET---TSAILITPEGDDKP-------GAVGKVVPFFEAkvVDLDTGKTLGVNQRGE----LCVRGPMIMSGYV 568
Cdd:cd05915 298 RQGYGLTETspvVVQNFVKSHLESLSeeekltlKAKTGLPIPLVR--LRVADEEGRPVPKDGKalgeVQLKGPWITGGYY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 569 NNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPA 648
Cdd:cd05915 376 GNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPL 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1886431185 649 AVVVLEHGKTmTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:cd05915 456 AVVVPRGEKP-TPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
194-710 |
1.38e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 132.21 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 194 KAMKRYA-LVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMkRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAN 272
Cdd:PRK07638 5 KEYKKHAsLQPNKIAIKEN--DRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 273 DIYNERELLNSMGISQPTVVFVSKKGLQKILNVQKKLpiiqkIIIMDSKTDYQGFQSMYTFVTS--HLP--PGFneydfv 348
Cdd:PRK07638 82 IKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRV-----IEIDEWKRMIEKYLPTYAPIENvqNAPfyMGF------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 349 pesfdrdktialimnSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAIL---SVVPFHHGFGMFTTLgYLicG 425
Cdd:PRK07638 151 ---------------TSGSTGKPKAFLRAQQSWLHSFDCNVHDF---HMKREDSVLiagTLVHSLFLYGAISTL-YV--G 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 426 FRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKstlIDKYdLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQG 505
Cdd:PRK07638 210 QTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYK---ENRV-IENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 506 YGLTETTSAILITPEGDD-KPGAVGKvvPFFEAKV-VDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALiDKDGW 583
Cdd:PRK07638 286 YGASELSFVTALVDEESErRPNSVGR--PFHNVQVrICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAREL-NADGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 584 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVvleHGKTmTEKE 663
Cdd:PRK07638 363 MTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TKQQ 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1886431185 664 IVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLD---ARKIREILIKAKK 710
Cdd:PRK07638 439 LKSFCLQRLSSFKIPK-EWHFVDEIPYTNSGKIArmeAKSWIENQEKIYE 487
|
|
| UBQ |
smart00213 |
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
91-162 |
1.73e-32 |
|
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression
Pssm-ID: 214563 [Multi-domain] Cd Length: 72 Bit Score: 120.06 E-value: 1.73e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 91 WQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:smart00213 1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVLR 72
|
|
| ubiquitin |
pfam00240 |
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
93-164 |
3.44e-32 |
|
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.
Pssm-ID: 459726 [Multi-domain] Cd Length: 72 Bit Score: 119.20 E-value: 3.44e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 93 IFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLRLR 164
Cdd:pfam00240 1 ITVKTLDGKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVLRQR 72
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
217-637 |
3.84e-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: 130.56 E-value: 3.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSk 296
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 kglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRDKTIALIMNSSGSTGLPKGVAL 376
Cdd:cd17640 85 --------------------------------------------------------NDSDDLATIIYTSGTTGNPKGVML 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 377 PHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGfrVVLMY---RFeeelFLRSLQDYKIQSALL 453
Cdd:cd17640 109 THANLLHQIRSLSDIV---PPQPGDRFLSILPIWHSYERSAEYFIFACG--CSQAYtsiRT----LKDDLKRVKPHYIVS 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 454 VPTLF-------------SFFAKSTLIDKYDLSNLHEIA-SGGAPLSKEVgeavAKRFHLPGIR--QGYGLTETTSAILI 517
Cdd:cd17640 180 VPRLWeslysgiqkqvskSSPIKQFLFLFFLSGGIFKFGiSGGGALPPHV----DTFFEAIGIEvlNGYGLTETSPVVSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 518 TPEGDDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEH 597
Cdd:cd17640 256 RRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGE 335
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1886431185 598 FFIVDRLKSLIKYK-GYQVAPAELESILLQHPNIFDAGVAG 637
Cdd:cd17640 336 LVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| Ubl_NEDD8 |
cd01806 |
ubiquitin-like (Ubl) domain found in neural precursor cell expressed developmentally ... |
93-166 |
4.68e-32 |
|
ubiquitin-like (Ubl) domain found in neural precursor cell expressed developmentally down-regulated protein 8 (NEDD8) and similar proteins; NEDD8, also termed Neddylin, or RELATED TO UBIQUITIN (RUB/Rub1p) in plant and yeast, is a ubiquitin-like protein that conjugates to nuclear proteins in a manner analogous to ubiquitination and sentrinization. It modifies a family of molecular scaffold proteins called cullins that are responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. NEDD8 deamidation and its inhibition of Cullin-RING ubiquitin ligases (CRLs) activity are responsible for Cycle-inhibiting factor (Cif)/Cif homolog in Burkholderia pseudomallei (CHBP)-induced cytopathic effect. NEDD8 contains a single conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Polyubiquitination, signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. Ubl NEDD8, contains many of the same lysines (K6, K11, K27, K33, K48) as Ub, where K27 has an role (other than conjugation) in the mechanism of protein neddylation.
Pssm-ID: 340504 [Multi-domain] Cd Length: 74 Bit Score: 118.65 E-value: 4.68e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886431185 93 IFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLRLRGG 166
Cdd:cd01806 1 IKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIFSGKQMNDEKTAADYKIEGGSVLHLVLALRGG 74
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
215-653 |
1.34e-31 |
|
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: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 215 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLG---ALFIGVAVAPANDIYNERELLNSmgiSQPTV 291
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAiwmAGHISVPLYPTLNPDTIRYVLEH---SESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 292 VFVSKkgLQKILNVQKKLP--IIQKII----IMDSKTDYQGFQSMYTFVTSHLPPGfneydfvpesfdrDKTIALIMNSS 365
Cdd:cd05932 82 LFVGK--LDDWKAMAPGVPegLISISLpppsAANCQYQWDDLIAQHPPLEERPTRF-------------PEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 366 GSTGLPKGVAlpHRTACVRFSHARDpIFGNQIIPDTAILSVVPFHHGFG-MFTTLGYLICGFRVVlmyrFEEEL--FLRS 442
Cdd:cd05932 147 GTTGQPKGVM--LTFGSFAWAAQAG-IEHIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVA----FAESLdtFVED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 443 LQDYKIQSALLVPTLFSFFAKStLIDKYDLSNLHEI--------------------------ASGGAPLSkevgEAVAKR 496
Cdd:cd05932 220 VQRARPTLFFSVPRLWTKFQQG-VQDKIPQQKLNLLlkipvvnslvkrkvlkglgldqcrlaGCGSAPVP----PALLEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 497 FHLPG--IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgvnqRGELCVRGPMIMSGYVNNPEAT 574
Cdd:cd05932 295 YRSLGlnILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEAT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 575 NALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNIFDAGV--AGLPDddagelPAAVV 651
Cdd:cd05932 364 AEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVigSGLPA------PLALV 437
|
..
gi 1886431185 652 VL 653
Cdd:cd05932 438 VL 439
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
217-637 |
3.35e-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: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG-VAVAPANDIYNER--ELLNSMGisqPTVVF 293
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGaLSLGIYQDSMAEEvaYLLNYTG---ARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 294 VS-KKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRD------KTIALIMNSSG 366
Cdd:cd17641 89 AEdEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGLYEREvaagkgEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 367 STGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHH-GFGMFTTLGYLICGF------------------- 426
Cdd:cd17641 169 TTGKPKLAMLSHGNF---LGHCAAYLAADPLGPGDEYVSVLPLPWiGEQMYSVGQALVCGFivnfpeepetmmedlreig 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 427 -RVVL--------------------------MYRFEEELFLRSL-QDYKIQSALLVPTLFSFFAKSTLI----DKYDLSN 474
Cdd:cd17641 246 pTFVLlpprvwegiaadvrarmmdatpfkrfMFELGMKLGLRALdRGKRGRPVSLWLRLASWLADALLFrplrDRLGFSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 475 LHEIASGGAPLskevGEAVAKRFHLPGI--RQGYGLTETTSAILITPEGDDKPGAVGkvVPFFEAKVvdldtgktlGVNQ 552
Cdd:cd17641 326 LRSAATGGAAL----GPDTFRFFHAIGVplKQLYGQTELAGAYTVHRDGDVDPDTVG--VPFPGTEV---------RIDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 553 RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK-YKGYQVAPAELESILLQHPNIF 631
Cdd:cd17641 391 VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPYIA 470
|
....*.
gi 1886431185 632 DAGVAG 637
Cdd:cd17641 471 EAVVLG 476
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
217-621 |
1.03e-30 |
|
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: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG---VAVAPANDIYNERELLNSmgiSQPTVVF 293
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGgiaVGIYTTNSPEACQYVAET---SEANILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 294 V-SKKGLQKILNVQKKLPIIQKIII--------MDSKTDYQGFQSMYTFVTSHlppgfnEYDFVPESFDRDKTIALIMNS 364
Cdd:cd05933 86 VeNQKQLQKILQIQDKLPHLKAIIQykeplkekEPNLYSWDEFMELGRSIPDE------QLDAIISSQKPNQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 365 sGSTGLPKGVALPHRT------ACVRFSHARDPIFGNQIIpdtaiLSVVPFHH----GFGMFTTL--------------- 419
Cdd:cd05933 160 -GTTGMPKGVMLSHDNitwtakAASQHMDLRPATVGQESV-----VSYLPLSHiaaqILDIWLPIkvggqvyfaqpdalk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 420 GYLICGFRVV----------LMYRFEEELFLRSLQDYKIQSALLV-------------------PTLFSFFAKSTLIDK- 469
Cdd:cd05933 234 GTLVKTLREVrptafmgvprVWEKIQEKMKAVGAKSGTLKRKIASwakgvgletnlklmggespSPLFYRLAKKLVFKKv 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 470 ---YDLSNLHEIASGGAPLSKEVgeavaKRFHLP---GIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLD 543
Cdd:cd05933 314 rkaLGLDRCQKFFTGAAPISRET-----LEFFLSlniPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPD 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 544 TgktlgvNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQ-VAPAELE 621
Cdd:cd05933 389 A------DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIE 461
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
433-703 |
1.06e-30 |
|
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: 125.37 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 433 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIdKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETT 512
Cdd:cd05974 162 RFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLA-SFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 513 SAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKTlgvnQRGELCV-----RGPMIMSGYVNNPEATNALIdKDGWLHSG 587
Cdd:cd05974 239 ALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPA----TEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 588 DIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHG---KTMTEKEI 664
Cdd:cd05974 314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyepSPETALEI 393
|
250 260 270
....*....|....*....|....*....|....*....
gi 1886431185 665 VDYVASQVTTAKKLRgGVVFVdEVPKGLTGKLDARKIRE 703
Cdd:cd05974 394 FRFSRERLAPYKRIR-RLEFA-ELPKTISGKIRRVELRR 430
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
217-703 |
1.87e-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: 125.90 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 296
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KglqkilnVQKKLPIIQKIIIMDSKTDYQGFQSmytfvtshlppgfneyDFVPESFDRDktIALIMNSSGSTGLPKGVAL 376
Cdd:cd17655 103 H-------LQPPIAFIGLIDLLDEDTIYHEESE----------------NLEPVSKSDD--LAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 377 PHRtACVRFSHArdpiFGNQIIPDTA--ILSVVPFHHGFGMFTTLGYLICGFRVVLmYRFEE----ELFLRSLQDYKIQS 450
Cdd:cd17655 158 EHR-GVVNLVEW----ANKVIYQGEHlrVALFASISFDASVTEIFASLLSGNTLYI-VRKETvldgQALTQYIRQNRITI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 451 ALLVPTLFSFFAKstlIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHL-PGIRQGYGLTETT---SAILITPEGDDKPG 526
Cdd:cd17655 232 IDLTPAHLKLLDA---ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTvdaSIYQYEPETDQQVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 527 -AVGKvvPFFEAKVVDLDT-GKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWL------HSGDIAYWDEDEHF 598
Cdd:cd17655 309 vPIGK--PLGNTRIYILDQyGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 599 FIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVlehgktmTEKEIvdyVASQVTT--AK 676
Cdd:cd17655 387 EFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-------SEKEL---PVAQLREflAR 456
|
490 500 510
....*....|....*....|....*....|..
gi 1886431185 677 KLRGGVV---FV--DEVPKGLTGKLDARKIRE 703
Cdd:cd17655 457 ELPDYMIpsyFIklDEIPLTPNGKVDRKALPE 488
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
200-699 |
1.87e-30 |
|
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: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 200 ALVPGTIAFTDAHIEVdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERE 279
Cdd:cd17651 6 ARTPDAPALVAEGRRL--TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 280 LLNSMGISQPTVVfVSKKGLQKILNVQKKLPIIQKIIIMDSKTDyqgfqsmytfvTSHLPPgfneydfvpesFDRDKTiA 359
Cdd:cd17651 84 LAFMLADAGPVLV-LTHPALAGELAVELVAVTLLDQPGAAAGAD-----------AEPDPA-----------LDADDL-A 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGnqIIPDTAILSVVPFhhGFGMFT--TLGYLICGFRVVLM---YRF 434
Cdd:cd17651 140 YVIYTSGSTGRPKGVVMPHRSL-ANLVAWQARASS--LGPGARTLQFAGL--GFDVSVqeIFSTLCAGATLVLPpeeVRT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSkeVGEAVAKRF-HLPGIR--QGYGLTET 511
Cdd:cd17651 215 DPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLV--LTEDLREFCaGLPGLRlhNHYGPTET 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 TSAILITPEGD----DKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWL--- 584
Cdd:cd17651 293 HVVTALSLPGDpaawPAPPPIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpga 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 585 ---HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTE 661
Cdd:cd17651 372 rmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDA 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 1886431185 662 KEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDAR 699
Cdd:cd17651 452 AELRAALATHL-PEYMVPSAFVLLDALPLTPNGKLDRR 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
200-699 |
3.94e-30 |
|
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: 124.62 E-value: 3.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 200 ALVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNE-- 277
Cdd:cd12117 8 ARTPDAVAVVYG--DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAer 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 278 -RELLNSmgiSQPTVVfVSKKGLQKILNVQKKLPIIQkiiimdsktdyqgfQSMYTFVTSHLPPGFNeydfvPESfdrdk 356
Cdd:cd12117 86 lAFMLAD---AGAKVL-LTDRSLAGRAGGLEVAVVID--------------EALDAGPAGNPAVPVS-----PDD----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 357 tIALIMNSSGSTGLPKGVALPHRtACVRFshARDPIFGnQIIPDTAILSVVPfhHGF--GMFTTLGYLICGFRVVLMyrf 434
Cdd:cd12117 138 -LAYVMYTSGSTGRPKGVAVTHR-GVVRL--VKNTNYV-TLGPDDRVLQTSP--LAFdaSTFEIWGALLNGARLVLA--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEELFL--RSLQDY----KIQSALLVPTLFsffakSTLIDKYD--LSNLHEIASGGAPLS-KEVGEAVAkrfHLPGIR-- 503
Cdd:cd12117 208 PKGTLLdpDALGALiaeeGVTVLWLTAALF-----NQLADEDPecFAGLRELLTGGEVVSpPHVRRVLA---ACPGLRlv 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 504 QGYGLTETT--SAILITPEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALID 579
Cdd:cd12117 280 NGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 580 KDGWL------HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVL 653
Cdd:cd12117 359 ADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 654 EHGktmtekeiVDYVASQVTTAKKLRGG-----VVFVDEVPKGLTGKLDAR 699
Cdd:cd12117 439 EGA--------LDAAELRAFLRERLPAYmvpaaFVVLDELPLTANGKVDRR 481
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
217-703 |
7.26e-30 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 124.49 E-value: 7.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVApandiynereLLNSMGISQPTVVFVSK 296
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL----------LLNTSFAGPALAEVVTR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLQKILNVQKKLPIIQKII--------IMDSkTDYQGFQSMYTFVTSHLPpgfneyDFVPESFDRDKTIALimnSSGST 368
Cdd:PRK13382 139 EGVDTVIYDEEFSATVDRALadcpqatrIVAW-TDEDHDLTVEVLIAAHAG------QRPEPTGRKGRVILL---TSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 369 GLPKGvalphrtacvrfshARDPIFGNqIIPDTAILSVVPFHHG------FGMFTTLGY--------LICgfRVVLMYRF 434
Cdd:PRK13382 209 GTPKG--------------ARRSGPGG-IGTLKAILDRTPWRAEeptvivAPMFHAWGFsqlvlaasLAC--TIVTRRRF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIRQGYGLTETT 512
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMFDRImdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG-DVIYNNYNATEAG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 513 SAILITPEGDDK-PGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVnnPEATNALIDkdGWLHSGDIAY 591
Cdd:PRK13382 351 MIATATPADLRAaPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGYT--SGSTKDFHD--GFMASGDVGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 592 WDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQ 671
Cdd:PRK13382 426 LDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDN 505
|
490 500 510
....*....|....*....|....*....|..
gi 1886431185 672 VTTAKKLRgGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK13382 506 LANYKVPR-DIVVLDELPRGATGKILRRELQA 536
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
346-703 |
4.97e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 122.10 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 346 DFVPESFDRDKTIALIMnSSGSTGLPKGVALPHRTACV-------RFSHARDpifgnqiipDTAILSVVPFHHGFGMFTT 418
Cdd:PRK07867 143 EPPFRVADPDDLFMLIF-TSGTSGDPKAVRCTHRKVASagvmlaqRFGLGPD---------DVCYVSMPLFHSNAVMAGW 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 419 LGYLICGFRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSF-FAKSTLIDkyDLSNLHEIASG--GAPLSKevgEAVAK 495
Cdd:PRK07867 213 AVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYvLATPERPD--DADNPLRIVYGneGAPGDI---ARFAR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 496 RFhlpGIR--QGYGLTETtsAILITPEGDDKPGAVGKVVPffEAKVVDLDTGK------------TLGVNQRGELC-VRG 560
Cdd:PRK07867 288 RF---GCVvvDGFGSTEG--GVAITRTPDTPPGALGPLPP--GVAIVDPDTGTecppaedadgrlLNADEAIGELVnTAG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 561 PMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPD 640
Cdd:PRK07867 361 PGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPD 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886431185 641 DDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVV-FVDEVPKGLTGKLDARKIRE 703
Cdd:PRK07867 440 PVVGDQVMAALVLAPGAKFDPDAFAEFLAAQPDLGPKQWPSYVrVCAELPRTATFKVLKRQLSA 503
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
217-706 |
5.50e-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: 122.60 E-value: 5.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFV-- 294
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITad 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 295 --SKKGlqKILNVQKKL-------PIIQKIIIM------DSKTDYqGFQSMYTFVTSHlPPGFneydfvpESFDRDKTIA 359
Cdd:cd05968 172 gfTRRG--REVNLKEEAdkacaqcPTVEKVVVVrhlgndFTPAKG-RDLSYDEEKETA-GDGA-------ERTESEDPLM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMnSSGSTGLPKGVAlpHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM-----YRF 434
Cdd:cd05968 241 IIY-TSGTTGKPKGTV--HVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYdgapdHPK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEELFlRSLQDYKIQSALLVPTLF-SFFAKST-LIDKYDLSNLHEIASGGAPLSKE----VGEAVAKRfHLPGIRQGYGl 508
Cdd:cd05968 318 ADRLW-RMVEDHEITHLGLSPTLIrALKPRGDaPVNAHDLSSLRVLGSTGEPWNPEpwnwLFETVGKG-RNPIINYSGG- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 509 TETTSAIL----ITPEgddKPGAVGKVVPFFEAKVVDlDTGKTLgVNQRGELCVRGPMI-MS-GYVNNPEA-TNALIDK- 580
Cdd:cd05968 395 TEISGGILgnvlIKPI---KPSSFNGPVPGMKADVLD-ESGKPA-RPEVGELVLLAPWPgMTrGFWRDEDRyLETYWSRf 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 581 -DGWLHsGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTM 659
Cdd:cd05968 470 dNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTP 548
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1886431185 660 TE---KEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLDARKIREILI 706
Cdd:cd05968 549 TEalaEELMERVADELGKPLSPE-RILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
196-714 |
6.91e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 121.88 E-value: 6.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 196 MKRYALVPGTIAfTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY 275
Cdd:PLN02479 26 LERAAVVHPTRK-SVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 276 NERELLNSMGISQPTVVFVSKK------GLQKILNVQK----KLPIIqkIIIMDSKTDYQGFQSM-------YTfvtSHL 338
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEfftlaeEALKILAEKKkssfKPPLL--IVIGDPTCDPKSLQYAlgkgaieYE---KFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 339 PPGFNEYDFVPESfDRDKTIALIMnSSGSTGLPKGVALPHRTACVrFSHARDPIFGnqiIPDTAI-LSVVPFHHGFGM-F 416
Cdd:PLN02479 180 ETGDPEFAWKPPA-DEWQSIALGY-TSGTTASPKGVVLHHRGAYL-MALSNALIWG---MNEGAVyLWTLPMFHCNGWcF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 417 TTLGYLICGFRVVLMYRFEEELFlRSLQDYKIQSALLVPTLFSFFAKSTLIDKY-DLSNLHEIASGGAPLSKEVGEAVAK 495
Cdd:PLN02479 254 TWTLAALCGTNICLRQVTAKAIY-SAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHVMTAGAAPPPSVLFAMSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 496 RfhlpGIR--QGYGLTET---TSAILITPEGDDKPGAVG---------KVVPFFEAKVVDLDTGKTLGVNQR--GELCVR 559
Cdd:PLN02479 333 K----GFRvtHTYGLSETygpSTVCAWKPEWDSLPPEEQarlnarqgvRYIGLEGLDVVDTKTMKPVPADGKtmGEIVMR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 560 GPMIMSGYVNNPEAtNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLP 639
Cdd:PLN02479 409 GNMVMKGYLKNPKA-NEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARP 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 640 DDDAGELPAAVVVLEHG-----KTMTEKEIVDYVASQVtTAKKLRGGVVFvDEVPKGLTGKLDARKIREiliKAKKGGKI 714
Cdd:PLN02479 488 DERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERL-PAYWVPKSVVF-GPLPKTATGKIQKHVLRA---KAKEMGPV 562
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
196-716 |
2.84e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 119.67 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 196 MKRYALV-PGTIAFTdaHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSlqffMPVLGALFiGVAVAPAndi 274
Cdd:PRK08162 24 LERAAEVyPDRPAVI--HGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNI----PAMVEAHF-GVPMAGA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 275 ynereLLNSMGI--SQPTVVFVSKKGLQKILNV--------QKKLPII--QKIIIMD------------SKTDYQGFqsm 330
Cdd:PRK08162 94 -----VLNTLNTrlDAASIAFMLRHGEAKVLIVdtefaevaREALALLpgPKPLVIDvddpeypggrfiGALDYEAF--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 331 ytfvtshLPPGFNEYDFVPEsfdRDKTIALIMN-SSGSTGLPKGVALPHRTAcvrFSHArdpiFGNQI---IPDTAI-LS 405
Cdd:PRK08162 166 -------LASGDPDFAWTLP---ADEWDAIALNyTSGTTGNPKGVVYHHRGA---YLNA----LSNILawgMPKHPVyLW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 406 VVP-FH-----HGFGMFTTLGYLICgfrvvlMYRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSnlHEIA 479
Cdd:PRK08162 229 TLPmFHcngwcFPWTVAARAGTNVC------LRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGID--HPVH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 480 S--GGAPLSKEVGEAVAKRfhlpGIR--QGYGLTET---TSAILITPEGDDKPG---AVGKV---VPFF---EAKVVDLD 543
Cdd:PRK08162 301 AmvAGAAPPAAVIAKMEEI----GFDltHVYGLTETygpATVCAWQPEWDALPLderAQLKArqgVRYPlqeGVTVLDPD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 544 T-------GKTLGvnqrgELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVA 616
Cdd:PRK08162 377 TmqpvpadGETIG-----EIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENIS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 617 PAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFvDEVPKGLTGKL 696
Cdd:PRK08162 451 SIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPK-AVVF-GELPKTSTGKI 528
|
570 580
....*....|....*....|
gi 1886431185 697 DARKIREiliKAKKGGKIAV 716
Cdd:PRK08162 529 QKFVLRE---QAKSLKAIDL 545
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
365-705 |
1.21e-27 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 117.26 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 365 SGSTGLPKGVALPHRTACVRF-SHARdpIFGnqIIPDTAILSvvpF-HHGFG-----MFTTlgyLICGFRVVLMYrfEEE 437
Cdd:cd05918 115 SGSTGKPKGVVIEHRALSTSAlAHGR--ALG--LTSESRVLQ---FaSYTFDvsileIFTT---LAAGGCLCIPS--EED 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 438 L---FLRSLQDYKIQSALLVPTLFSffakstLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLpgiRQGYGLTETT-S 513
Cdd:cd05918 183 RlndLAGFINRLRVTWAFLTPSVAR------LLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRL---INAYGPAECTiA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 514 AILITPEGDDKPGAVGKVVPFFeAKVVDLDT-GKTLGVNQRGELCVRGPMIMSGYVNNPEATN-ALIDKDGWLH------ 585
Cdd:cd05918 254 ATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAaAFIEDPAWLKqegsgr 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 586 ------SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQH-PNIFDAGVAGLPDDDAGELPAAVVVLEHGKT 658
Cdd:cd05918 333 grrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGS 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886431185 659 MTEK--------EIVDYVASQVTTAK-KLRGGV---------VFVDEVPKGLTGKLDARKIREIL 705
Cdd:cd05918 413 SSGSgdgdslflEPSDEFRALVAELRsKLRQRLpsymvpsvfLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
359-704 |
5.99e-27 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 117.76 E-value: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHR---------TACVRFsHARDPIFgnqiipdtailSVVPFHHGFGMFT-TLGYLICGFRV 428
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRnllanraqvAARIDF-SPEDKVF-----------NALPVFHSFGLTGgLVLPLLSGVKV 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 429 VLM-----YRFEEELFlrslqdYKIQSALLV--PTLFSFFAKSTliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlpG 501
Cdd:PRK06814 864 FLYpsplhYRIIPELI------YDTNATILFgtDTFLNGYARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEKF---G 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 502 IR--QGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtgktlGVNQRGELCVRGPMIMSGYV--NNPEATNAL 577
Cdd:PRK06814 933 IRilEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVP-----GIDEGGRLFVRGPNVMLGYLraENPGVLEPP 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 578 idKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ-HPNIFDAGVAgLPDDDAGElpaAVVVLEHG 656
Cdd:PRK06814 1008 --ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVS-IPDARKGE---RIILLTTA 1081
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1886431185 657 KTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDARKIREI 704
Cdd:PRK06814 1082 SDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
358-652 |
1.86e-26 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 115.20 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVvlmyRFEEE 437
Cdd:PLN02736 223 VATICYTSGTTGTPKGVVLTHGNLIANVAGSSLST---KFYPSDVHISYLPLAHIYERVNQIVMLHYGVAV----GFYQG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 438 LFLRSLQDYkiqsALLVPTLFS-------------------------------FFAK----------STLIDKYDLSNLH 476
Cdd:PLN02736 296 DNLKLMDDL----AALRPTIFCsvprlynriydgitnavkesgglkerlfnaaYNAKkqalengknpSPMWDRLVFNKIK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 477 E--------IASGGAPLSKEVGEAVakRFHLPG-IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDTGKT 547
Cdd:PLN02736 372 AklggrvrfMSSGASPLSPDVMEFL--RICFGGrVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNY 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 548 LGVNQ---RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESI 623
Cdd:PLN02736 450 TSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENV 529
|
330 340
....*....|....*....|....*....
gi 1886431185 624 LLQHPNIFDAGVAGlpDDDAGELPAAVVV 652
Cdd:PLN02736 530 YAKCKFVAQCFVYG--DSLNSSLVAVVVV 556
|
|
| Ubl_ubiquitin_like |
cd17039 |
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
93-160 |
2.00e-26 |
|
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.
Pssm-ID: 340559 [Multi-domain] Cd Length: 68 Bit Score: 102.67 E-value: 2.00e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 93 IFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLV 160
Cdd:cd17039 1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYGIKDGSTIHLV 68
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
203-703 |
2.18e-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: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerelln 282
Cdd:cd17653 11 PDAVAVESL--GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 283 smgisqptvvfvskkglqkilnVQKKLPIIQKIIIMDsktdyqgfQSMYTFVtshLPPgfneydfvpesfDRDKTIALIM 362
Cdd:cd17653 77 ----------------------LDAKLPSARIQAILR--------TSGATLL---LTT------------DSPDDLAYII 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 363 NSSGSTGLPKGVALPHR--TACVRFSHARdpiFGNQiiPDTAILSV--VPFHHGFG-MFTTLGYlicGFRVVLmyRFEEE 437
Cdd:cd17653 112 FTSGSTGIPKGVMVPHRgvLNYVSQPPAR---LDVG--PGSRVAQVlsIAFDACIGeIFSTLCN---GGTLVL--ADPSD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 438 LFLRSLQdyKIQSALLVPTLFSffakstLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRfhlPGIRQGYGLTETTSAILI 517
Cdd:cd17653 182 PFAHVAR--TVDALMSTPSILS------TLSPQDFPNLKTIFLGGEAVPPSLLDRWSPG---RRLYNAYGPTECTISSTM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 518 TPEGDDKPGAVGKVVPffEAKVVDLDTGKTL-GVNQRGELCVRGPMIMSGYVNNPEATNA----LIDKDGWLH--SGDIA 590
Cdd:cd17653 251 TELLPGQPVTIGKPIP--NSTCYILDADLQPvPEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyrTGDYG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 591 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDdagELPAAVVvlehgktmteKEIVDYVAS 670
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNG---RLVAFVT----------PETVDVDGL 395
|
490 500 510
....*....|....*....|....*....|....*...
gi 1886431185 671 QVTTAKKLR-----GGVVFVDEVPKGLTGKLDARKIRE 703
Cdd:cd17653 396 RSELAKHLPsyavpDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
218-699 |
1.01e-25 |
|
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: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERELLNSMgisqptvvfvskk 297
Cdd:cd17649 14 SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPL-DPEYPAERLRYM------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 glqkilnvqkklpiiqkiiIMDSKTdyqgfqsmyTFVTSHLPpgfneydfvpesfdrdKTIALIMNSSGSTGLPKGVALP 377
Cdd:cd17649 80 -------------------LEDSGA---------GLLLTHHP----------------RQLAYVIYTSGSTGTPKGVAVS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 378 HrTACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVL----MYRFEEELfLRSLQDYKIQSALL 453
Cdd:cd17649 116 H-GPLAAHCQATAERYG--LTPGDRELQFASFNFDGAHEQLLPPLICGACVVLrpdeLWASADEL-AEMVRELGVTVLDL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 454 VPTLFSFFAKSTLIDKYDL-SNLHEIASGGAPLSKEVgeavAKRFHLPGIR--QGYGLTETT-SAILITPEGDDKPGA-- 527
Cdd:cd17649 192 PPAYLQQLAEEADRTGDGRpPSLRLYIFGGEALSPEL----LRRWLKAPVRlfNAYGPTEATvTPLVWKCEAGAARAGas 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 528 --VGKVVPFFEAKVVDLDTGkTLGVNQRGELCVRGPMIMSGYVNNPEATNA--LIDKDG-----WLHSGDIAYWDEDEHF 598
Cdd:cd17649 268 mpIGRPLGGRSAYILDADLN-PVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRDDGVI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 599 FIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV---------LEHGKTMTEKEIVDYVa 669
Cdd:cd17649 347 EYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLraaaaqpelRAQLRTALRASLPDYM- 425
|
490 500 510
....*....|....*....|....*....|
gi 1886431185 670 sqVTTAkklrggVVFVDEVPKGLTGKLDAR 699
Cdd:cd17649 426 --VPAH------LVFLARLPLTPNGKLDRK 447
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
203-700 |
1.50e-25 |
|
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: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAHIEVdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY-NERell 281
Cdd:cd12116 1 PDATAVRDDDRSL--SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYpADR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 282 nsmgisqptvvfvskkgLQKILNVQKKlpiiqKIIIMDSKTDYQGFQsmYTFVTSHLPPGFNEYDFVPESFDRDKTIALI 361
Cdd:cd12116 76 -----------------LRYILEDAEP-----ALVLTDDALPDRLPA--GLPVLLLALAAAAAAPAAPRTPVSPDDLAYV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 362 MNSSGSTGLPKGVALPHRtACVRFSHA--RDPIFGnqiiPDTAILSVVPFhhGFGMFT--TLGYLICGFRVVLMYR---F 434
Cdd:cd12116 132 IYTSGSTGRPKGVVVSHR-NLVNFLHSmrERLGLG----PGDRLLAVTTY--AFDISLleLLLPLLAGARVVIAPRetqR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLheiaSGGAPLSkevgEAVAKRFHLPGIR--QGYGLTETT 512
Cdd:cd12116 205 DPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTAL----CGGEALP----PDLAARLLSRVGSlwNLYGPTETT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 513 ---SAILITPEgdDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHS--- 586
Cdd:cd12116 277 iwsTAARVTAA--AGPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPgsr 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 587 ----GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELpAAVVVLEHGKTMTEK 662
Cdd:cd12116 354 lyrtGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAA 432
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1886431185 663 EIVDYVASQ-----VTTAkklrggVVFVDEVPKGLTGKLDaRK 700
Cdd:cd12116 433 ALRAHLRATlpaymVPSA------FVRLDALPLTANGKLD-RK 468
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
217-596 |
2.06e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 111.51 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNER-----ELLNSMGISQPTV 291
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLVsqdfgKLRHVLELLTPGL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 292 VFVS-----KKGLQKILNVQKKLPIIQKIIIMDSKTDYQgfqsmyTFVTSHLPPGfneydfVPESFDR--DKTIALIMNS 364
Cdd:PRK08180 150 VFADdgaafARALAAVVPADVEVVAVRGAVPGRAATPFA------ALLATPPTAA------VDAAHAAvgPDTIAKFLFT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 365 SGSTGLPKGVALPHRTACV---------RFSHARDPIfgnqiipdtaILSVVPFHHGFGMFTTLGYlicgfrvVL----- 430
Cdd:PRK08180 218 SGSTGLPKAVINTHRMLCAnqqmlaqtfPFLAEEPPV----------LVDWLPWNHTFGGNHNLGI-------VLynggt 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 431 MY---------RFEEELflRSLQDykIQSALL--VPTLF---------------SFFakstlidkydlSNLHEIASGGAP 484
Cdd:PRK08180 281 LYiddgkptpgGFDETL--RNLRE--ISPTVYfnVPKGWemlvpalerdaalrrRFF-----------SRLKLLFYAGAA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 485 LSKEVGE-----AVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtGKTlgvnqrgELCVR 559
Cdd:PRK08180 346 LSQDVWDrldrvAEATCGERIRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVG-GKL-------EVRVK 417
|
410 420 430
....*....|....*....|....*....|....*...
gi 1886431185 560 GPMIMSGYVNNPEATNALIDKDGWLHSGDIAYW-DEDE 596
Cdd:PRK08180 418 GPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPAD 455
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
217-696 |
2.36e-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: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVcsenslqfFMPV-------------LGALFIGV-------AVAPANDIYN 276
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAI--------YMPMipeaavamlacarIGAVHSVIfggfapeAVAGRIIDSS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 277 ERELLNSMGISQPTVVFVSKKGLQKILNVQkkLPIIQKIIIMD-SKTDYQGFQSM---YTFVTSHLPPGFNeydfvPESF 352
Cdd:cd17634 157 SRLLITADGGVRAGRSVPLKKNVDDALNPN--VTSVEHVIVLKrTGSDIDWQEGRdlwWRDLIAKASPEHQ-----PEAM 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 353 DRDKTIaLIMNSSGSTGLPKGVALPHR----TACVRFSHARDpIFGNQIIPDTAILSVVPFHHgfgmFTTLGYLICGFRV 428
Cdd:cd17634 230 NAEDPL-FILYTSGTTGKPKGVLHTTGgylvYAATTMKYVFD-YGPGDIYWCTADVGWVTGHS----YLLYGPLACGATT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 429 VLmyrFE-------EELFLRSLQDYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKrfHL 499
Cdd:cd17634 304 LL---YEgvpnwptPARMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINPEAYEWYWK--KI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 500 PGIR----QGYGLTETTSAILITPEGDDKPGAVGKVVPFF--EAKVVDlDTGKTLGVNQRGELCVRGP---MIMSGYVNN 570
Cdd:cd17634 379 GKEKcpvvDTWWQTETGGFMITPLPGAIELKAGSATRPVFgvQPAVVD-NEGHPQPGGTEGNLVITDPwpgQTRTLFGDH 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 571 PEATNALIDK-DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAA 649
Cdd:cd17634 458 ERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1886431185 650 VVVLEHGKTMTEK---EIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKL 696
Cdd:cd17634 538 YVVLNHGVEPSPElyaELRNWVRKEIGPLATPD-VVHWVDSLPKTRSGKI 586
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
359-697 |
2.80e-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: 109.71 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDpIFG----NQIIPDTAI---LSVvpfhhgFGMFTTLGyliCGFRVVLM 431
Cdd:cd12115 108 AYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAA-AFSaeelAGVLASTSIcfdLSV------FELFGPLA---TGGKVVLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 yrfEEELFLRSLQDYKiQSALL--VPTlfsffAKSTLIDKYDL-SNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGL 508
Cdd:cd12115 178 ---DNVLALPDLPAAA-EVTLIntVPS-----AAAELLRHDALpASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 509 TETT--SAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWL-- 584
Cdd:cd12115 249 SEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpg 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 585 ----HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT 660
Cdd:cd12115 328 arlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGL 407
|
330 340 350
....*....|....*....|....*....|....*..
gi 1886431185 661 EKEIVDYVAsQVTTAKKLRGGVVFVDEVPKGLTGKLD 697
Cdd:cd12115 408 VEDLRRHLG-TRLPAYMVPSRFVRLDALPLTPNGKID 443
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
359-700 |
2.89e-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: 109.26 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRfeEEL 438
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRGLA---NLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPA--EEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 439 -----FLRSLQDYKIQSALLVPTLFSffakstLIDKYDLSNLHEIASGGAPLSKEvgeaVAKRFHlPGIR--QGYGLTET 511
Cdd:cd17652 171 lpgepLADLLREHRITHVTLPPAALA------ALPPDDLPDLRTLVVAGEACPAE----LVDRWA-PGRRmiNAYGPTET 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 T-SAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWL 584
Cdd:cd17652 240 TvCATMAGPLPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTaerfvaDPFGAPGSRM 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 585 H-SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAgVAGLPDDDAGE--LpAAVVVLEHGKTMTE 661
Cdd:cd17652 319 YrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEA-VVVVRDDRPGDkrL-VAYVVPAPGAAPTA 396
|
330 340 350
....*....|....*....|....*....|....*....
gi 1886431185 662 KEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARK 700
Cdd:cd17652 397 AELRAHLAERL-PGYMVPAAFVVLDALPLTPNGKLDRRA 434
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
365-654 |
3.57e-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: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 365 SGSTGLPKGVALPHRTAcVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFEEELFLR 441
Cdd:COG1020 626 SGSTGRPKGVMVEHRAL-VNLLAWMQRRYG--LGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAppeARRDPAALAE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 442 SLQDYKIQSALLVPTLFsffakSTLID--KYDLSNLHEIASGGAPLSKEVGEAVAKRFhlPGIR--QGYGLTETT--SAI 515
Cdd:COG1020 703 LLARHRVTVLNLTPSLL-----RALLDaaPEALPSLRLVLVGGEALPPELVRRWRARL--PGARlvNLYGPTETTvdSTY 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 516 LITPEGDDKPGAV--GKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA-----LIDKDG--WLHS 586
Cdd:COG1020 776 YEVTPPDADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadPFGFPGarLYRT 854
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 587 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLE 654
Cdd:COG1020 855 GDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPE 922
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
192-716 |
1.12e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 108.94 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 192 LHKAMKRYALVPGTIAFTDAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPA 271
Cdd:PRK05857 17 LDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 272 NDIYNERELLNSMGISQPTVVFV---SKKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFQSMYtfvtshlPPGFNEYDfv 348
Cdd:PRK05857 97 DGNLPIAAIERFCQITDPAAALVapgSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAS-------LAGNADQG-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 349 pesfdRDKTIALIMnSSGSTGLPKGVALPHRT--ACVRFSHARDPIFGNQIIPDTAiLSVVPFHHGFGMFTTLGYLICGf 426
Cdd:PRK05857 168 -----SEDPLAMIF-TSGTTGEPKAVLLANRTffAVPDILQKEGLNWVTWVVGETT-YSPLPATHIGGLWWILTCLMHG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 427 rVVLMYRFEEELFLRS-LQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGaplSKEVGEAVakRF-HLPGIR- 503
Cdd:PRK05857 240 -GLCVTGGENTTSLLEiLTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADV--RFiEATGVRt 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 504 -QGYGLTETTSAILITPEGDD-----KPGAVGKVVPFFEAKVVDLDTG-----KTLGVNQRGELCVRGPMIMSGYVNNPE 572
Cdd:PRK05857 314 aQVYGLSETGCTALCLPTDDGsivkiEAGAVGRPYPGVDVYLAATDGIgptapGAGPSASFGTLWIKSPANMLGYWNNPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 573 ATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV 652
Cdd:PRK05857 394 RTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886431185 653 lehgkTMTEKEIVDYVASQVTTAKKLR---------GGVVFVDEVPKGLTGKLdarkIREILIKAKKGGKIAV 716
Cdd:PRK05857 473 -----ASAELDESAARALKHTIAARFRresepmarpSTIVIVTDIPRTQSGKV----MRASLAAAATADKARV 536
|
|
| Ubl2_ISG15 |
cd01810 |
ubiquitin-like (Ubl) domain 2 found in interferon-stimulated gene 15 (ISG15) and similar ... |
92-164 |
1.14e-24 |
|
ubiquitin-like (Ubl) domain 2 found in interferon-stimulated gene 15 (ISG15) and similar proteins; ISG15, also termed interferon-induced 15 kDa protein, or interferon-induced 17 kDa protein (IP17), or ubiquitin cross-reactive protein (UCRP), is an antiviral interferon-induced ubiquitin-like protein that upon viral infection it modifies cellular and viral proteins by mechanisms similar to ubiquitination. Although ISG15 has properties similar to those of other ubiquitin-like (Ubl) molecules, it is a unique member of the Ubl superfamily, whose expression and conjugation to target proteins are tightly regulated by specific signaling pathways, indicating it may have specialized functions in the immune system. ISG15 contains two tandem Ubl domains with a beta-grasp Ubl fold. This family corresponds to the second Ubl domain.
Pssm-ID: 340508 [Multi-domain] Cd Length: 74 Bit Score: 97.91 E-value: 1.14e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLRLR 164
Cdd:cd01810 2 SIFVRNEKGQSHTYEVRLTQTVDQLKQKVSGREGVHDDQFWLTFEGRPLEDQLPLGEYGLKPQSTIHMNLRLR 74
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
473-628 |
2.65e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 108.53 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 473 SNLHEIASGGAPLSKEVGEAVAKRFHLpgIRQGYGLTETT--SAILITpeGDDKPGAVGKVVPFFEAKVVDLDTGK-TLG 549
Cdd:PTZ00216 428 GRVRAMLSGGGPLSAATQEFVNVVFGM--VIQGWGLTETVccGGIQRT--GDLEPNAVGQLLKGVEMKLLDTEEYKhTDT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 550 VNQRGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK-YKGYQVAPAELESILLQHP 628
Cdd:PTZ00216 504 PEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNE 583
|
|
| PTZ00044 |
PTZ00044 |
ubiquitin; Provisional |
92-166 |
2.89e-24 |
|
ubiquitin; Provisional
Pssm-ID: 185411 [Multi-domain] Cd Length: 76 Bit Score: 96.82 E-value: 2.89e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLRLRGG 166
Cdd:PTZ00044 2 QILIKTLTGKKQSFNFEPDNTVQQVKMALQEKEGIDVKQIRLIYSGKQMSDDLKLSDYKVVPGSTIHMVLQLRGG 76
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
203-705 |
2.91e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 107.38 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAvaPANDIYNEREL-L 281
Cdd:PRK10946 37 SDAIAVICG--ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSeL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 282 NSMGIS-QPTVVFVSKK-----GLQKILNVQKKLPIIQkIIIMDSKTDYQGFQSmytfVTSHLPPGFneyDFVPESFDRd 355
Cdd:PRK10946 113 NAYASQiEPALLIADRQhalfsDDDFLNTLVAEHSSLR-VVLLLNDDGEHSLDD----AINHPAEDF---TATPSPADE- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 356 ktIALIMNSSGSTGLPKgvaLPHRTA-----CVRFShardpifgNQII---PDTAILSVVPFHHGFGMFT--TLGYLICG 425
Cdd:PRK10946 184 --VAFFQLSGGSTGTPK---LIPRTHndyyySVRRS--------VEICgftPQTRYLCALPAAHNYPMSSpgALGVFLAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 426 FRVVLMYRFEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLIDKYDLSNLHEIASGGAPLSkevgEAVAKRfhLPG-- 501
Cdd:PRK10946 251 GTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWlqAIAEGGSRAQLASLKLLQVGGARLS----ETLARR--IPAel 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 502 ---IRQGYGLTE---------TTSAILITPEG-----DDkpgavgkvvpffEAKVVDLDtGKTLGVNQRGELCVRGPMIM 564
Cdd:PRK10946 325 gcqLQQVFGMAEglvnytrldDSDERIFTTQGrpmspDD------------EVWVADAD-GNPLPQGEVGRLMTRGPYTF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 565 SGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAG 644
Cdd:PRK10946 392 RGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 645 ELPAAVVVLEHG-------KTMTEKEIVDYvasqvttakKLRGGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:PRK10946 472 EKSCAFLVVKEPlkavqlrRFLREQGIAEF---------KLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
358-708 |
3.29e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 107.40 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRT--ACVRfSHARDpifGNQIIPDTAILSVVPFHHGFGMfttLGYLI----CGFRVVLM 431
Cdd:PRK09192 178 IAYLQYSSGSTRFPRGVIITHRAlmANLR-AISHD---GLKVRPGDRCVSWLPFYHDMGL---VGFLLtpvaTQLSVDYL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 YrfEEELFLRSLQDYKIQS----ALLVPTLFSF-----FAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGI 502
Cdd:PRK09192 251 P--TRDFARRPLQWLDLISrnrgTISYSPPFGYelcarRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGF 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 503 RQ-----GYGLTETTSAILITPEG----------------------DDKPGAV------GKVVPFFEAKVVDlDTGKTLG 549
Cdd:PRK09192 329 DDkafmpSYGLAEATLAVSFSPLGsgivveevdrdrleyqgkavapGAETRRVrtfvncGKALPGHEIEIRN-EAGMPLP 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 550 VNQRGELCVRGPMIMSGYVNNPEATNALiDKDGWLHSGDIAYWDEDEhFFIVDRLKSLIKYKGYQVAPAELESILLQHPN 629
Cdd:PRK09192 408 ERVVGHICVRGPSLMSGYFRDEESQDVL-AADGWLDTGDLGYLLDGY-LYITGRAKDLIIINGRNIWPQDIEWIAEQEPE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 630 IF--DAGVAGLPDDDaGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFV--DEVPKGLTGKLDARKIREIL 705
Cdd:PRK09192 486 LRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIHALAALVRSEFGVEAAVELVppHSLPRTSSGKLSRAKAKKRY 564
|
...
gi 1886431185 706 IKA 708
Cdd:PRK09192 565 LSG 567
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
356-703 |
3.67e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 107.03 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 356 KTIALIMNSSGSTGLPKGVALPH-------RTACVRFSHARDpifgnqiipDTAILSVVPFHHGFGMFTTLGYLICGFRV 428
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHgrlafagRALTERFGLTRD---------DVCYVSMPLFHSNAVMAGWAPAVASGAAV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 429 VLMYRFEEELFLRSLQDYKIqsallvpTLFSFFAK------STLIDKYDLSNLHEIASGGAPlSKEVGEAVAKRFhlpGI 502
Cdd:PRK13388 221 ALPAKFSASGFLDDVRRYGA-------TYFNYVGKplayilATPERPDDADNPLRVAFGNEA-SPRDIAEFSRRF---GC 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 503 R--QGYGLTETtsAILITPEGDDKPGAVGKvvPFFEAKVVDLDTGKT-----LGVNQR--------GELCVR-GPMIMSG 566
Cdd:PRK13388 290 QveDGYGSSEG--AVIVVREPGTPPGSIGR--GAPGVAIYNPETLTEcavarFDAHGAllnadeaiGELVNTaGAGFFEG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 567 YVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGEL 646
Cdd:PRK13388 366 YYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQ 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 647 PAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFV-DEVPKGLTGKLDARKIRE 703
Cdd:PRK13388 445 VMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYVRIaADLPSTATNKVLKRELIA 502
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
347-659 |
3.72e-24 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 107.98 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 347 FVPESFDrdktIALIMNSSGSTGLPKGVALPHRT--ACVRFSHARDPIFGNQIIPDTAILSVVPFHHgfgmfttlgylic 424
Cdd:PLN02430 215 NPPKPLD----ICTIMYTSGTSGDPKGVVLTHEAvaTFVRGVDLFMEQFEDKMTHDDVYLSFLPLAH------------- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 425 gfrvvLMYRFEEELFLRS-----------------LQDYK-----------------IQSAL--LVPTLFSFFaksTLID 468
Cdd:PLN02430 278 -----ILDRMIEEYFFRKgasvgyyhgdlnalrddLMELKptllagvprvferihegIQKALqeLNPRRRLIF---NALY 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 469 KYDLSNLHE-----------------------------IASGGAPLSKEVgEAVAKRFHLPGIRQGYGLTETTSAILIT- 518
Cdd:PLN02430 350 KYKLAWMNRgyshkkaspmadflafrkvkaklggrlrlLISGGAPLSTEI-EEFLRVTSCAFVVQGYGLTETLGPTTLGf 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 519 PEGDDKPGAVGKVVPFFEAKVVDL-DTG-KTLGVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDE 596
Cdd:PLN02430 429 PDEMCMLGTVGAPAVYNELRLEEVpEMGyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNG 507
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886431185 597 HFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNIFDAGVAGlpdDDAGELPAAVVVLEHGKTM 659
Cdd:PLN02430 508 VLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNEENTN 568
|
|
| Ubl_ZFAND4 |
cd01802 |
ubiquitin-like (Ubl) domain found in AN1-type zinc finger protein 4 (ZFAND4) and similar ... |
93-164 |
4.83e-24 |
|
ubiquitin-like (Ubl) domain found in AN1-type zinc finger protein 4 (ZFAND4) and similar proteins; ZFAND4, also termed AN1-type zinc finger and ubiquitin domain-containing protein-like 1 (ANUBL1), may function as an oncogene that promotes proliferation and regulates relevant tumor suppressor genes in gastric cancer, suggesting a role in gastric cancer initiation and progression. ZFAND4contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal AN1-type zinc finger. Unlike ubiquitin polyproteins and most ubiquitin fusion proteins, the N-terminal Ubl domain of ZFAND4 does not undergo proteolytic processing.
Pssm-ID: 340500 [Multi-domain] Cd Length: 74 Bit Score: 95.86 E-value: 4.83e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 93 IFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLRLR 164
Cdd:cd01802 3 LFIETLTGTAFELRVSPFETVASVKAKIQRLEGIPVSQQHLIWSGRELEDDYCLHDYNITDGSTLKLVLAMR 74
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
217-590 |
2.53e-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: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY-----NERELLNSMGISQPTV 291
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslmsqDLAKLKHLFELLKPGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 292 VFVS-----KKGLQKILNVQKKLPIIQKIIIMDSKTDYQGFqsmytfvtSHLPPGFNeydfVPESFDR--DKTIALIMNS 364
Cdd:cd05921 106 VFAQdaapfARALAAIFPLGTPLVVSRNAVAGRGAISFAEL--------AATPPTAA----VDAAFAAvgPDTVAKFLFT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 365 SGSTGLPKGVALPHRTACVRFSHARD--PIFGNqiiPDTAILSVVPFHHGFGMFTtlgylicGFRVVL-----MY----- 432
Cdd:cd05921 174 SGSTGLPKAVINTQRMLCANQAMLEQtyPFFGE---EPPVLVDWLPWNHTFGGNH-------NFNLVLynggtLYiddgk 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 433 ----RFEEELflRSLQDYKIQSALLVPTLFSFFAK-----STLIDKYdLSNLHEIASGGAPLSKEVGE-----AVAKRFH 498
Cdd:cd05921 244 pmpgGFEETL--RNLREISPTVYFNVPAGWEMLVAalekdEALRRRF-FKRLKLMFYAGAGLSQDVWDrlqalAVATVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 499 LPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtGKTlgvnqrgELCVRGPMIMSGYVNNPEATNALI 578
Cdd:cd05921 321 RIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSG-GKY-------EVRVKGPNVTPGYWRQPELTAQAF 392
|
410
....*....|..
gi 1886431185 579 DKDGWLHSGDIA 590
Cdd:cd05921 393 DEEGFYCLGDAA 404
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
359-697 |
3.11e-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: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDPI-FGNQiipDtailSVVPFHH---GFGMFTTLGYLICGFRVVLM--- 431
Cdd:cd17643 96 AYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFgFNED---D----VWTLFHSyafDFSVWEIWGALLHGGRLVVVpye 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIR--QGYGLT 509
Cdd:cd17643 169 VARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvNMYGIT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 510 ETT---SAILITPegDDKPGA----VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNA--LIDK 580
Cdd:cd17643 249 ETTvhvTFRPLDA--ADLPAAaaspIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfVANP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 581 DG-----WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH 655
Cdd:cd17643 326 FGgpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADD 405
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1886431185 656 GKTMTEKEIVDYVAsQVTTAKKLRGGVVFVDEVPKGLTGKLD 697
Cdd:cd17643 406 GAAADIAELRALLK-ELLPDYMVPARYVPLDALPLTVNGKLD 446
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
348-705 |
3.93e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 103.92 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 348 VPESFDRDktIALIMNSSGSTGLPKGVALPHRTAcvrFSHARDPIFGNQIIPDT-AILSVVPFHHGFGMfttLGYLIcgf 426
Cdd:PRK07768 146 PVETGEDD--LALMQLTSGSTGSPKAVQITHGNL---YANAEAMFVAAEFDVETdVMVSWLPLFHDMGM---VGFLT--- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 427 rvVLMYRFEEELFLRSLqDYkIQSALLVPTLFSF----------FAKSTLI---------DKYDLSNLHEIASGGAPLSK 487
Cdd:PRK07768 215 --VPMYFGAELVKVTPM-DF-LRDPLLWAELISKyrgtmtaapnFAYALLArrlrrqakpGAFDLSSLRFALNGAEPIDP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 488 EVGEA---VAKRFHLP--GIRQGYGLTETTSAILITPEGD---------------------DKPGA-----VGKVVPFFE 536
Cdd:PRK07768 291 ADVEDlldAGARFGLRpeAILPAYGMAEATLAVSFSPCGAglvvdevdadllaalrravpaTKGNTrrlatLGPPLPGLE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 537 AKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNnPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVA 616
Cdd:PRK07768 371 VRVVDED-GQVLPPRGVGVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 617 PAELESILLQHPNIFDAGVA--GLPDDDAGELPAavVVLE---HGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDE---V 688
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAVavRLDAGHSREGFA--VAVEsnaFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGpgsI 526
|
410
....*....|....*..
gi 1886431185 689 PKGLTGKLDARKIREIL 705
Cdd:PRK07768 527 PKTPSGKLRRANAAELV 543
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
361-707 |
4.95e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 104.44 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 361 IMNSSGSTGLPKGVAL---PHRTACVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRV-VLMYRFEE 436
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRsngPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGgIIKNKHIE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 437 ELFLRSLQDYKIQSALLVPTLFSFFAK-----STLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRqGYGLTET 511
Cdd:PTZ00237 339 DDLWNTIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR-GYGQTEI 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 TSAILITPEGDDKP-GAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPM---IMSGYVNNPEATNALIDK-DGWLHS 586
Cdd:PTZ00237 418 GITYLYCYGHINIPyNATGVPSIFIKPSILSED-GKELNVNEIGEVAFKLPMppsFATTFYKNDEKFKQLFSKfPGYYNS 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 587 GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMT------ 660
Cdd:PTZ00237 497 GDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQsidlnk 576
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1886431185 661 -EKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGKLdarkIREILIK 707
Cdd:PTZ00237 577 lKNEINNIITQDIESLAVLR-KIIIVNQLPKTKTGKI----PRQIISK 619
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
203-696 |
1.01e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 102.38 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLN 282
Cdd:PRK13383 49 PGRTAIIDD--DGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 283 SMGISQPTVVFVSKKGLQKILNVQkklpiiQKIIIMDSKTdyqgfqsmytfVTSHlppgfneydfvpESFDRDKTIA--- 359
Cdd:PRK13383 127 ALRAHHISTVVADNEFAERIAGAD------DAVAVIDPAT-----------AGAE------------ESGGRPAVAApgr 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGVAlphrtacvRFSHARDPIFGNQIIPDTAILSV-------VPFHHGFGMFTTLGYLICGFRVVLMY 432
Cdd:PRK13383 178 IVLLTSGTTGKPKGVP--------RAPQLRSAVGVWVTILDRTRLRTgsrisvaMPMFHGLGLGMLMLTIALGGTVLTHR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 433 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKstLIDKYDLSN----LHEIASGGAPLSKEVGeavaKRF---HLPGIRQG 505
Cdd:PRK13383 250 HFDAEAALAQASLHRADAFTAVPVVLARILE--LPPRVRARNplpqLRVVMSSGDRLDPTLG----QRFmdtYGDILYNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 506 YGLTETTSAILITP-EGDDKPGAVGKVVPFFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNpeATNALIDkdGWL 584
Cdd:PRK13383 324 YGSTEVGIGALATPaDLRDAPETVGKPVAGCPVRILDRN-NRPVGPRVTGRIFVGGELAGTRYTDG--GGKAVVD--GMT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 585 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEI 664
Cdd:PRK13383 399 STGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQL 478
|
490 500 510
....*....|....*....|....*....|..
gi 1886431185 665 VDYVASQVTTAKKLRgGVVFVDEVPKGLTGKL 696
Cdd:PRK13383 479 RDYLKDRVSRFEQPR-DINIVSSIPRNPTGKV 509
|
|
| Ubl_AtUPL5_like |
cd16107 |
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) ... |
92-160 |
1.30e-22 |
|
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) and similar proteins; Arabidopsis thaliana AtUPL5, also termed HECT-type E3 ubiquitin transferase UPL5, is an E3 ubiquitin-protein ligase that contains a ubiquitin-like domain (Ubl), a C-type lectin-binding domain, a leucine zipper and a HECT domain. HECT domain containing-ubiquitin-protein ligases have more than one member in different genomes, these proteins have been classified into four sub-families (UPL1/2, UPL3/4, UPL5 and UPL6/7). AtUPL5 fUPL5 regulates leaf senescence in Arabidopsis through degradation of the transcription factor WRKY53.
Pssm-ID: 340524 Cd Length: 70 Bit Score: 91.79 E-value: 1.30e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLV 160
Cdd:cd16107 1 QIFVRTYCGKTIVLHAKASDTVESLHQQIEARTGIPSLEQRLIFGGRQLQHSQSLESCKMENDATLFLV 69
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
200-699 |
1.64e-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: 101.58 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 200 ALVPGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERE 279
Cdd:cd17646 9 ARTPDAPAVVDE--GRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL-DPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 280 LLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQKIIimdsktdyqgfqsmytfvTSHLPPGfneydfVPESFDRDKTIA 359
Cdd:cd17646 86 RLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA------------------LAAPPAT------PPLVPPRPDNLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFhhGF--GMFTTLGYLICGFRVVLMY---RF 434
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY---PLGPGDRVLQKTPL--SFdvSVWELFWPLVAGARLVVARpggHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEELFLRSLQDYKIQSALLVPTLFSFFakstlidkydlsnLHEIASGGAPLSKEV---GEA----VAKRFH-LPGIR--Q 504
Cdd:cd17646 217 DPAYLAALIREHGVTTCHFVPSMLRVF-------------LAEPAAGSCASLRRVfcsGEAlppeLAARFLaLPGAElhN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 505 GYGLTETT---SAILITPEGDDKPGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 581
Cdd:cd17646 284 LYGPTEAAidvTHWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 582 GWLH------SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGE-LPAAVVVLE 654
Cdd:cd17646 363 PFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAArLVGYVVPAA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1886431185 655 HGKTMTEKEIVDYVA-----SQVTTAkklrggVVFVDEVPKGLTGKLDAR 699
Cdd:cd17646 443 GAAGPDTAALRAHLAerlpeYMVPAA------FVVLDALPLTANGKLDRA 486
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
358-703 |
2.04e-22 |
|
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: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRTacvrFSHARDPIfGNQIIPDT--AILSVVPFHHGFGMFTtlGYLICGFRVVLMYRFE 435
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHEN----LVHNMFAI-LNSTEWKTkdRILSWMPLTHDMGLIA--FHLAPLIAGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 436 EELFLR--SLQDYKIQ----SALLVPT----LFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQG 505
Cdd:cd05908 181 TRLFIRrpILWLKKASehkaTIVSSPNfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 506 -----YGLTETTSAILITPEG------------------------DDKPGA----VGKVVPFFEAKVVDlDTGKTLGVNQ 552
Cdd:cd05908 261 ailpvYGLAEASVGASLPKAQspfktitlgrrhvthgepepevdkKDSECLtfveVGKPIDETDIRICD-EDNKILPDGY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 553 RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWdEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFD 632
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 633 AGVA--GLPDDDAGElPAAVVVLEHGKtmTEKEIVDYvASQVTTAKKLRGG-----VVFVDEVPKGLTGKLDARKIRE 703
Cdd:cd05908 419 GRVVacGVNNSNTRN-EEIFCFIEHRK--SEDDFYPL-GKKIKKHLNKRGGwqineVLPIRRIPKTTSGKVKRYELAQ 492
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
217-646 |
2.64e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 102.05 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIY-----NERELLNSMGISQPTV 291
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmshDHAKLKHLFDLVKPRV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 292 VFVSKKGL-QKILNVQKKLPIiqKIIIMDSKTDYQGFQSMYTFVTShlPPGfneyDFVPESFDR--DKTIALIMNSSGST 368
Cdd:PRK12582 161 VFAQSGAPfARALAALDLLDV--TVVHVTGPGEGIASIAFADLAAT--PPT----AAVAAAIAAitPDTVAKYLFTSGST 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 369 GLPKGVALPHRTAC--------VRfshARDPifgNQIIPDtaILSVVPFHH------GFGMFTTLG---YLICGFRVVLM 431
Cdd:PRK12582 233 GMPKAVINTQRMMCaniamqeqLR---PREP---DPPPPV--SLDWMPWNHtmggnaNFNGLLWGGgtlYIDDGKPLPGM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 yrFEEELflRSLQDYKIQSALLVPTLFSFFAKSTLIDKyDL-----SNLHEIASGGAPLSKEVGE-----AVAKRFHLPG 501
Cdd:PRK12582 305 --FEETI--RNLREISPTVYGNVPAGYAMLAEAMEKDD-ALrrsffKNLRLMAYGGATLSDDLYErmqalAVRTTGHRIP 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 502 IRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDldtgktlgVNQRGELCVRGPMIMSGYVNNPEATNALIDKD 581
Cdd:PRK12582 380 FYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAP--------VGDKYEVRVKGPNVTPGYHKDPELTAAAFDEE 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 582 GWLHSGDIA-YWDEDehffivDRLKSLI-------KYK---GYQVAPAELESILLQ--HPNIFDAGVAGLPDDDAGEL 646
Cdd:PRK12582 452 GFYRLGDAArFVDPD------DPEKGLIfdgrvaeDFKlstGTWVSVGTLRPDAVAacSPVIHDAVVAGQDRAFIGLL 523
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
364-705 |
3.61e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 100.94 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 364 SSGSTGLPKGVALPHRTACVrfsHArdpiFGNQIiPDT-------AILSVVP-FH-HGFGmfttLGYL--ICGFRVVL-- 430
Cdd:PRK07008 184 TSGTTGNPKGALYSHRSTVL---HA----YGAAL-PDAmglsardAVLPVVPmFHvNAWG----LPYSapLTGAKLVLpg 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 431 -------MYR-FEEElflrslqdyKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhlpGI 502
Cdd:PRK07008 252 pdldgksLYElIEAE---------RVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEY---GV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 503 R--QGYGLTET----TSAILiTPEGDDKPGAV--------GKVVPFFEAKVVDlDTGKTL---GVNQrGELCVRGPMIMS 565
Cdd:PRK07008 320 EviHAWGMTEMsplgTLCKL-KWKHSQLPLDEqrkllekqGRVIYGVDMKIVG-DDGRELpwdGKAF-GDLQVRGPWVID 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 566 GYVNNpeATNALIDkdGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGE 645
Cdd:PRK07008 397 RYFRG--DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDE 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 646 LPAAVVVLEHGKTMTEKEIVDYVASQVttAK-KLRGGVVFVDEVPKGLTGKLDARKIREIL 705
Cdd:PRK07008 473 RPLLVVVKRPGAEVTREELLAFYEGKV--AKwWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
217-628 |
4.78e-22 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 101.35 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVApanDIY---NERELLNSMGISQPTVVF 293
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVV---TIYaslGEEALCHSLNETEVTTVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 294 VSKKGLQKILNVQKKLPIIQKIIIMD---SKTDYQGFQSMYTFVTShlppgFNEYD------FVPESFDRDKTIALIMNS 364
Cdd:PLN02387 184 CDSKQLKKLIDISSQLETVKRVIYMDdegVDSDSSLSGSSNWTVSS-----FSEVEklgkenPVDPDLPSPNDIAVIMYT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 365 SGSTGLPKGVALPHrtacvrfshardpifGNQIIPDTAILSVVPFHHGFGMFttLGYLicgfrvVLMYRFE---EELFLR 441
Cdd:PLN02387 259 SGSTGLPKGVMMTH---------------GNIVATVAGVMTVVPKLGKNDVY--LAYL------PLAHILElaaESVMAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 442 S-----------LQDY--KIQ------SALLVPTLFSffAKSTLIDK-------------------YDLSNLHEIA---- 479
Cdd:PLN02387 316 VgaaigygspltLTDTsnKIKkgtkgdASALKPTLMT--AVPAILDRvrdgvrkkvdakgglakklFDIAYKRRLAaieg 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 480 ---------------------------------SGGAPLSKEVGEAVAKRFHLPgIRQGYGLTETTSAILITPEGDDKPG 526
Cdd:PLN02387 394 swfgawglekllwdalvfkkiravlggrirfmlSGGAPLSGDTQRFINICLGAP-IGQGYGLTETCAGATFSEWDDTSVG 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 527 AVGKVVPFFEAKVVDLDTGKTLGVNQ---RGELCVRGPMIMSGYVNNPEATNAL--IDKDG--WLHSGDIAYWDEDEHFF 599
Cdd:PLN02387 473 RVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLE 552
|
490 500 510
....*....|....*....|....*....|
gi 1886431185 600 IVDRLKSLIKYK-GYQVAPAELESILLQHP 628
Cdd:PLN02387 553 IIDRKKDIVKLQhGEYVSLGKVEAALSVSP 582
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
217-637 |
1.44e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 99.53 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 296
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLQKILNVQKKLPIIQKIII--------MDSKTDYQG--------FQSMYTfVTSHLPPgfneydfvpesfDRDKTIAL 360
Cdd:PLN02861 158 SKISSILSCLPKCSSNLKTIVsfgdvsseQKEEAEELGvscfsweeFSLMGS-LDCELPP------------KQKTDICT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 361 IMNSSGSTGLPKGVALPHRTACVRFSHARDPIF--GNQIIPDTAILSVVPFHHGFGMF---------TTLGYLICGFRVV 429
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKvtDRVATEEDSYFSYLPLAHVYDQVietyciskgASIGFWQGDIRYL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 430 L-------------MYRFEEELFLRSLQdyKIQSA-LLVPTLFSFF---------------AKSTLIDKYDLSNLHE--- 477
Cdd:PLN02861 305 MedvqalkptifcgVPRVYDRIYTGIMQ--KISSGgMLRKKLFDFAynyklgnlrkglkqeEASPRLDRLVFDKIKEglg 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 478 -----IASGGAPLSKEVgEAVAKRFHLPGIRQGYGLTETTSAILiTPEGDDKP--GAVGKVVPFFEAKVVDL-DTG-KTL 548
Cdd:PLN02861 383 grvrlLLSGAAPLPRHV-EEFLRVTSCSVLSQGYGLTESCGGCF-TSIANVFSmvGTVGVPMTTIEARLESVpEMGyDAL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 549 GVNQRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQH 627
Cdd:PLN02861 461 SDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRC 539
|
490
....*....|
gi 1886431185 628 PNIFDAGVAG 637
Cdd:PLN02861 540 PLIASIWVYG 549
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
361-704 |
6.30e-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: 97.25 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 361 IMNSSGSTGLPKGVAlpHRTA-----------CVrFSHARDPIFGNqiipdTAILSVVPFHHgfgmFTTLGYLICGFRVV 429
Cdd:cd05966 236 ILYTSGSTGKPKGVV--HTTGgyllyaattfkYV-FDYHPDDIYWC-----TADIGWITGHS----YIVYGPLANGATTV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 430 LmyrFE-------EELFLRSLQDYKIQSALLVPTLFSFFAK--STLIDKYDLSNLHEIASGGAPLSKE--------VGEa 492
Cdd:cd05966 304 M---FEgtptypdPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVLGSVGEPINPEawmwyyevIGK- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 493 vakrFHLPgIRQGYGLTETTSaILITP---EGDDKPGAVGKvvPFF--EAKVVDLDTGKtLGVNQRGELCVRGP---MIM 564
Cdd:cd05966 380 ----ERCP-IVDTWWQTETGG-IMITPlpgATPLKPGSATR--PFFgiEPAILDEEGNE-VEGEVEGYLVIKRPwpgMAR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 565 SGYvNNPEA-TNALIDKD-GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDD 642
Cdd:cd05966 451 TIY-GDHERyEDTYFSKFpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDI 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 643 AGELPAAVVVLEHGKTMT---EKEIVDYVASQ---VTTAKKlrggVVFVDEVPKGLTGKLDARKIREI 704
Cdd:cd05966 530 KGEAIYAFVTLKDGEEPSdelRKELRKHVRKEigpIATPDK----IQFVPGLPKTRSGKIMRRILRKI 593
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
217-705 |
1.26e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 96.39 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMK-RYGLNTNHRI----VVCSENSLQFF-MPVLGALFigvavAPANDIYNERELLNSMGISQPT 290
Cdd:PRK05620 39 TTFAAIGARAAALAHALHdELGITGDQRVgsmmYNCAEHLEVLFaVACMGAVF-----NPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 291 VVFVSKKGLQKILNVQKKLPIIQKIIIMDSktdyqgfqSMYTFVTSHLPPGFNEYDFV------PESFD----RDKTIAL 360
Cdd:PRK05620 114 VIVADPRLAEQLGEILKECPCVRAVVFIGP--------SDADSAAAHMPEGIKVYSYEalldgrSTVYDwpelDETTAAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 361 IMNSSGSTGLPKGVALPHRTACVRFSHAR--DPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR-FEEE 437
Cdd:PRK05620 186 ICYSTGTTGAPKGVVYSHRSLYLQSLSLRttDSL---AVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPdLSAP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 438 LFLRSLQDYKIQSALLVPT----LFSFFAKSTLidkyDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIrQGYGLTETTS 513
Cdd:PRK05620 263 TLAKIIATAMPRVAHGVPTlwiqLMVHYLKNPP----ERMSLQEIYVGGSAVPPILIKAWEERYGVDVV-HVWGMTETSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 514 AILIT--PEG------DDKPGAVGKVVPFFEAKVVDldTGKTLGVNQR--GELCVRGPMIMSGYVNNP------------ 571
Cdd:PRK05620 338 VGTVArpPSGvsgearWAYRVSQGRFPASLEYRIVN--DGQVMESTDRneGEIQVRGNWVTASYYHSPteegggaastfr 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 572 ----EATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELP 647
Cdd:PRK05620 416 gedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERP 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 648 AAVVVLEHGKTMTEkeivdyvasqvTTAKKLRGGV-------------VFVDEVPKGLTGKLDARKIREIL 705
Cdd:PRK05620 496 LAVTVLAPGIEPTR-----------ETAERLRDQLrdrlpnwmlpeywTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
218-654 |
1.80e-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: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMK-RYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiYNERE--LLNSMGISQPTVVFV 294
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN--YNLSGdpLIHCLKLSGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 295 skkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRDKTIALIMnSSGSTGLPKGV 374
Cdd:cd05937 85 ----------------------------------------------------------DPDDPAILIY-TSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 375 ALPHR---TACVRFSHardpIFGNQiiPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELFLRSLQDYKIQS 450
Cdd:cd05937 106 AISWRrtlVTSNLLSH----DLNLK--NGDRTYTCMPLYHGTAAFLGACNcLMSGGTLALSRKFSASQFWKDVRDSGATI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 451 ALLVPTLFSFFAkSTLIDKYDLSNLHEIASGGApLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGK 530
Cdd:cd05937 180 IQYVGELCRYLL-STPPSPYDRDHKVRVAWGNG-LRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDFGAGAIGH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 531 VVP----FFEAKVV----DLDTGKTLGVNQRGeLCVRGP------MIM----------SGYVNNPEAT------NALIDK 580
Cdd:cd05937 258 HGLirrwKFENQVVlvkmDPETDDPIRDPKTG-FCVRAPvgepgeMLGrvpfknreafQGYLHNEDATesklvrDVFRKG 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 581 DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAG--LPDDDaGELPAAVVVLE 654
Cdd:cd05937 337 DIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkVPGHD-GRAGCAAITLE 411
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
217-662 |
2.55e-20 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 95.35 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFmPVLGALF----IGVAVAPANDIYNereLLNSMGISQPTVV 292
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFF-ALTFALFkagaVPVLVDPGMGIKN---LKQCLAEAQPDAF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 293 F-VSKKGLQKILNVQKKLPIIQKIIIMDSKtdyqgFQSMYTFVTSHLPPGFNEYDFVPesFDRDKTiALIMNSSGSTGLP 371
Cdd:PRK09274 118 IgIPKAHLARRLFGWGKPSVRRLVTVGGRL-----LWGGTTLATLLRDGAAAPFPMAD--LAPDDM-AAILFTSGSTGTP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 372 KGVALPHRTACVRFSHARDpIFGnqIIPDTAILSVVPFhhgFGMFTtlgyLICGFRVVLMY-------RFEEELFLRSLQ 444
Cdd:PRK09274 190 KGVVYTHGMFEAQIEALRE-DYG--IEPGEIDLPTFPL---FALFG----PALGMTSVIPDmdptrpaTVDPAKLFAAIE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 445 DYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPGIR--QGYGLTE-------TTSAI 515
Cdd:PRK09274 260 RYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLP-PDAEilTPYGATEalpissiESREI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 516 L-----ITPEGDdkpGA-VGKVVPFFEAKVVDLDTG--------KTLGVNQRGELCVRGPMIMSGYVNNPEAT--NALID 579
Cdd:PRK09274 339 LfatraATDNGA---GIcVGRPVDGVEVRIIAISDApipewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATrlAKIPD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 580 KDG--WLHSGDIAYWDEDEHFFI----VDRLKSLIK-YKGYQVapaelESILLQHPNIFDAGVAGLPdDDAGELPAAVVV 652
Cdd:PRK09274 416 GQGdvWHRMGDLGYLDAQGRLWFcgrkAHRVETAGGtLYTIPC-----ERIFNTHPGVKRSALVGVG-VPGAQRPVLCVE 489
|
490
....*....|
gi 1886431185 653 LEHGKTMTEK 662
Cdd:PRK09274 490 LEPGVACSKS 499
|
|
| Ubl2_FAT10 |
cd17053 |
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ... |
92-160 |
4.97e-20 |
|
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins; FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the second Ubl domain of FAT10. Some family members contain only one Ubl domain.
Pssm-ID: 340573 Cd Length: 71 Bit Score: 84.32 E-value: 4.97e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDG-RTLSDYNIQKESTLHLV 160
Cdd:cd17053 2 TVNSKLLTGTVHTLQVSRSTTVAQVKAMIEDQSGVPPNEQILVYNGKRLEDGdKTLGEYGIKTGDTLYLL 71
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
182-699 |
6.94e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.41 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 182 PLEDGTAGEQLHKAM-KRYALVPGTIA--FTDAHIevdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPV 258
Cdd:PRK12316 1995 TPEAYPRGPGVHQRIaEQAARAPEAIAvvFGDQHL----SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVAL 2070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 259 LGALFIGVAVAPANDIYNERELLNSMGISQPTVVfVSKKGLQKILNVQKKLPIIQkiiiMDSKTDYQGFqsmytfvtshl 338
Cdd:PRK12316 2071 LAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL-LTQRHLLERLPLPAGVARLP----LDRDAEWADY----------- 2134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 339 PPGFNEYDFVPEsfdrdkTIALIMNSSGSTGLPKGVALPHrTACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTT 418
Cdd:PRK12316 2135 PDTAPAVQLAGE------NLAYVIYTSGSTGLPKGVAVSH-GALVAHCQAAGERYE--LSPADCELQFMSFSFDGAHEQW 2205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 419 LGYLICGFRVVLM---YRFEEELFlRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLsNLHEIASGGAPLSKEVGEAVAK 495
Cdd:PRK12316 2206 FHPLLNGARVLIRddeLWDPEQLY-DEMERHGVTILDFPPVYLQQLAEHAERDGRPP-AVRVYCFGGEAVPAASLRLAWE 2283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 496 RFHLPGIRQGYGLTETTSAILITPEGDDKPGA-----VGKVVPFFEAKVVDLDTgKTLGVNQRGELCVRGPMIMSGYVNN 570
Cdd:PRK12316 2284 ALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGNRRAYILDADL-NLLAPGMAGELYLGGEGLARGYLNR 2362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 571 PEATNALIDKDGWLH-------SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpDDDA 643
Cdd:PRK12316 2363 PGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGAS 2441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 644 GELPAAVVVLEHGKTMTEKEIVDYVAsQVTTAKKLRGGVVFVDEVPKGLTGKLDAR 699
Cdd:PRK12316 2442 GKQLVAYVVPDDAAEDLLAELRAWLA-ARLPAYMVPAHWVVLERLPLNPNGKLDRK 2496
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
210-701 |
9.64e-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: 9.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 210 DAHIEVD----ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMG 285
Cdd:cd17656 3 DAVAVVFenqkLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 286 ISQPTVVfVSKKGLQKILNVQKKlpiiqkIIIMDSKTDYQGFQSMYTFVtshlppgFNEYDfvpesfdrdktIALIMNSS 365
Cdd:cd17656 83 DSGVRVV-LTQRHLKSKLSFNKS------TILLEDPSISQEDTSNIDYI-------NNSDD-----------LLYIIYTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 366 GSTGLPKGVALPHRTACVRFSHARD---PIFGNQIIPDTAILSVVPFHHGFGMFTTLG--YLIcgfrvvlmyRFEEELFL 440
Cdd:cd17656 138 GTTGKPKGVQLEHKNMVNLLHFEREktnINFSDKVLQFATCSFDVCYQEIFSTLLSGGtlYII---------REETKRDV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 441 RSLQDY----KIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPL--SKEVGEAVAKR-FHLpgiRQGYGLTET-- 511
Cdd:cd17656 209 EQLFDLvkrhNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLviTNEFKEMLHEHnVHL---HNHYGPSEThv 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 TSAILITPEgDDKP--GAVGKvvPFFEAKVVDLDTGKTL---GVnqRGELCVRGPMIMSGYVNNPEATNALIDKDGW--- 583
Cdd:cd17656 286 VTTYTINPE-AEIPelPPIGK--PISNTWIYILDQEQQLqpqGI--VGELYISGASVARGYLNRQELTAEKFFPDPFdpn 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 584 ---LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEhgKTMT 660
Cdd:cd17656 361 ermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME--QELN 438
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1886431185 661 EKEIVDYVASQVtTAKKLRGGVVFVDEVPKGLTGKLDARKI 701
Cdd:cd17656 439 ISQLREYLAKQL-PEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
214-700 |
2.30e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 214 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVF 293
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLL 4653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 294 VSKKGLQKilnvqkkLPIIQKI--IIMDSKTDYQGFQSMYTFVTSHlppgfneydfvPESfdrdktIALIMNSSGSTGLP 371
Cdd:PRK12316 4654 TQSHLLQR-------LPIPDGLasLALDRDEDWEGFPAHDPAVRLH-----------PDN------LAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 372 KGVALPHRtACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM--YRFEEELFLRSLQDYKIQ 449
Cdd:PRK12316 4710 KGVAVSHG-SLVNHLHATGERYE--LTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRddSLWDPERLYAEIHEHRVT 4786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 450 SALLVPTLFSFFAKSTLIDKyDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT-SAILITPEGDDKPGA- 527
Cdd:PRK12316 4787 VLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTvTVLLWKARDGDACGAa 4865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 528 ---VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWLH-SGDIAYWDEDEH 597
Cdd:PRK12316 4866 ympIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALTaerfvpDPFGAPGGRLYrTGDLARYRADGV 4944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 598 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVlehgktmTEKEIVDYVASQVTTAKK 677
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVP-------QDPALADADEAQAELRDE 5017
|
490 500 510
....*....|....*....|....*....|....*.
gi 1886431185 678 LRGGV-------------VFVDEVPKGLTGKLDaRK 700
Cdd:PRK12316 5018 LKAALrerlpeymvpahlVFLARMPLTPNGKLD-RK 5052
|
|
| Ubl_Dsk2p_like |
cd16106 |
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ... |
95-160 |
2.93e-19 |
|
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.
Pssm-ID: 340523 [Multi-domain] Cd Length: 73 Bit Score: 82.30 E-value: 2.93e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 95 VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLV 160
Cdd:cd16106 5 VKCSNGKKFTVEVEPDATVLELKELIAEKSDIPAEQQRLIYKGKILKDEETLSSYKIQDGHTVHLV 70
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
359-623 |
5.12e-19 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 91.70 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVAlphrtacvrfsHARDPIFGN--QI------IPDTAILSVVPFHHGFGMftTLGY---LICGFR 427
Cdd:PRK08043 368 ALILFTSGSEGHPKGVV-----------HSHKSLLANveQIktiadfTPNDRFMSALPLFHSFGL--TVGLftpLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 428 VVLM-----YRFEEELFlrslqdYKIQSALLvptlfsfFAKSTLI-------DKYDLSNLHEIASGGAPLSKEVGEAVAK 495
Cdd:PRK08043 435 VFLYpsplhYRIVPELV------YDRNCTVL-------FGTSTFLgnyarfaNPYDFARLRYVVAGAEKLQESTKQLWQD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 496 RFhlpGIR--QGYGLTETTSAILITPEGDDKPGAVGKVVPFFEAKVVDLDtgktlGVNQRGELCVRGPMIMSGY--VNN- 570
Cdd:PRK08043 502 KF---GLRilEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVP-----GIEQGGRLQLKGPNIMNGYlrVEKp 573
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 571 -----PEATNALIDKD-GWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVApaeLESI 623
Cdd:PRK08043 574 gvlevPTAENARGEMErGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVS---LEMV 629
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
218-623 |
9.24e-19 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 90.85 E-value: 9.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKK 297
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 GLQKILNVQKKLPIIQKIIIM------DSKTDYQGFQSMYTFVTSHLPPG-FNEYDFvpeSFDRDKTIALIMNSSGSTGL 370
Cdd:PLN02614 161 KISELFKTCPNSTEYMKTVVSfggvsrEQKEEAETFGLVIYAWDEFLKLGeGKQYDL---PIKKKSDICTIMYTSGTTGD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 371 PKGVALPHR------TACVRFSHARDPIFGNQIIpdtaILSVVPFHHGFGM-----FTTLGYLIcGFrvvlmYRFEEELF 439
Cdd:PLN02614 238 PKGVMISNEsivtliAGVIRLLKSANAALTVKDV----YLSYLPLAHIFDRvieecFIQHGAAI-GF-----WRGDVKLL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 440 LRSLQDYKIQSALLVPTLFS--------------FFAK-----------------------STLIDKYDLS--------N 474
Cdd:PLN02614 308 IEDLGELKPTIFCAVPRVLDrvysglqkklsdggFLKKfvfdsafsykfgnmkkgqshveaSPLCDKLVFNkvkqglggN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 475 LHEIASGGAPLSKEVgEAVAKRFHLPGIRQGYGLTETTSAILIT-PEGDDKPGAVGKVVPFFEAKVVDLDTGK--TLGVN 551
Cdd:PLN02614 388 VRIILSGAAPLASHV-ESFLRVVACCHVLQGYGLTESCAGTFVSlPDELDMLGTVGPPVPNVDIRLESVPEMEydALAST 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886431185 552 QRGELCVRGPMIMSGYVNNPEATNALIdKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESI 623
Cdd:PLN02614 467 PRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENI 538
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
358-701 |
9.77e-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: 89.54 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRtACVRFSHARDPIFGNQIIPDTAILSVVPFHHG-FGMFTtlgYLICGFRVVLMYRfEE 436
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHH-NLVNLCEWHRPYFGVTPADKSLVYASFSFDASaWEIFP---HLTAGAALHVVPS-ER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 437 ELFLRSLQDYKIQSALLVPTLFSFFAKSTLidKYDLSNLHEIASGGAPLSKevgeAVAKRFHLpgiRQGYGLTETTsaIL 516
Cdd:cd17645 181 RLDLDALNDYFNQEGITISFLPTGAAEQFM--QLDNQSLRVLLTGGDKLKK----IERKGYKL---VNNYGPTENT--VV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 517 ITPEGDDKPGA---VGKvvPFFEAKVVDLDTGKTL---GVNqrGELCVRGPMIMSGYVNNPEAT------NALIDKDGWL 584
Cdd:cd17645 250 ATSFEIDKPYAnipIGK--PIDNTRVYILDEALQLqpiGVA--GELCIAGEGLARGYLNRPELTaekfivHPFVPGERMY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 585 HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVV----LEHG--KT 658
Cdd:cd17645 326 RTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTapeeIPHEelRE 405
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1886431185 659 MTEKEIVDYVASQVttakklrggVVFVDEVPKGLTGKLDARKI 701
Cdd:cd17645 406 WLKNDLPDYMIPTY---------FVHLKALPLTANGKVDRKAL 439
|
|
| Ubl_Rad23 |
cd01805 |
ubiquitin-like (Ubl) domain found in the Rad23 protein family; The Rad23 family includes the ... |
92-157 |
1.46e-18 |
|
ubiquitin-like (Ubl) domain found in the Rad23 protein family; The Rad23 family includes the yeast nucleotide excision repair (NER) proteins, Rad23p (in Saccharomyces cerevisiae) and Rhp23p (in Schizosaccharomyces pombe), their mammalian orthologs HR23A and HR23B, and putative DNA repair proteins from plants. Rad23 proteins play dual roles in DNA repair as well as in proteosomal degradation. They have affinity for both the proteasome and ubiquitinylated proteins and participate in translocating polyubiquitinated proteins to the proteasome. Rad23 proteins carry an ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and two ubiquitin-associated (UBA) domains, as well as a xeroderma pigmentosum group C (XPC) protein-binding domain. The Ubl domain is responsible for the binding to proteasome. The UBA domains are important for binding of ubiquitin (Ub) or multi-ubiquitinated substrates, which suggests Rad23 proteins might be involved in certain pathways of Ub metabolism. Both the Ubl domain and the XPC-binding domain are necessary for efficient NER function of Rad23 proteins.
Pssm-ID: 340503 [Multi-domain] Cd Length: 72 Bit Score: 80.29 E-value: 1.46e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEG-IPPDQQRLIFAGRQLEDGRTLSDYNIQKESTL 157
Cdd:cd01805 2 KITFKTLQQQTFEIEVEPSDTVLELKEKIEQEQGdFPASGQKLIYSGKVLKDDKTLSEYNIKEKDFV 68
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
509-704 |
1.64e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 89.81 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 509 TETtSAILITP-EG--DDKPGAVGKvvPFF--EAKVVDlDTGKTLGVNQRGELCVRGP---MIMSGYvNNPEAtnaLID- 579
Cdd:PRK00174 405 TET-GGIMITPlPGatPLKPGSATR--PLPgiQPAVVD-EEGNPLEGGEGGNLVIKDPwpgMMRTIY-GDHER---FVKt 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 580 -----KDGWLhSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLE 654
Cdd:PRK00174 477 yfstfKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLK 555
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 655 HGKTMTE---KEIVDYVASQV---TTAKKLRggvvFVDEVPKGLTGKLDARKIREI 704
Cdd:PRK00174 556 GGEEPSDelrKELRNWVRKEIgpiAKPDVIQ----FAPGLPKTRSGKIMRRILRKI 607
|
|
| Ubl_UBL4A_like |
cd01807 |
ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, ... |
92-162 |
1.86e-18 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, also termed GdX, is a ubiquitously expressed ubiquitin-like (Ubl) protein that forms a complex with partner proteins and participates in the protein processing through endoplasmic reticulum (ER), acting as a chaperone. As a key component of the BCL2-associated athanogene 6 (BAG6) chaperone complex, UBL4A plays a role in mediating DNA damage signaling and cell death. UBL4A also regulates insulin-induced Akt plasma membrane translocation through promotion of Arp2/3-dependent actin branching. Moreover, UBL4A specifically stabilizes the TC45/STAT3 association and promotes dephosphorylation of STAT3 to repress tumorigenesis. UBL4B is testis-specific, and encoded by an X-derived retrogene Ubl4b, which is specifically expressed in post-meiotic germ cells in mammals. As a germ cell-specific cytoplasmic protein, UBL4B is not present in somatic cells. Moreover, UBL4B is present in elongated spermatids, but not in spermatocytes and round spermatids, suggesting its function is restricted to late spermiogenesis. The function of UBL4A may be compensated by either UBL4B or other Ubl proteins in normal conditions. Both UBL4A and UBL4B contain a conserved Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.
Pssm-ID: 340505 [Multi-domain] Cd Length: 72 Bit Score: 80.10 E-value: 1.86e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd01807 2 LITVKILQGKECTIEVSPTESVLTVKQLVAEQLNVPVSQQRLVFKGKTLADEHSLSDYSIGPGSKIHLVVK 72
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
214-700 |
2.37e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.61 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 214 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERELLNSMgisqptvvf 293
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPL-DPEYPRERLAYM--------- 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 294 VSKKGLQKIL---NVQKKLPII--QKIIIMDSKTDYQGFQSMYTfvtshlppgfneydfvPESFDRDKTIALIMNSSGST 368
Cdd:PRK12467 1667 IEDSGIELLLtqsHLQARLPLPdgLRSLVLDQEDDWLEGYSDSN----------------PAVNLAPQNLAYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 369 GLPKGVALPHrTACVRFSHARDPIFgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMyRFEE----ELFLRSLQ 444
Cdd:PRK12467 1731 GRPKGAGNRH-GALVNRLCATQEAY--QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIA-PPGAhrdpEQLIQLIE 1806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 445 DYKIQSALLVPTLFSFFAKSTLIDKYDLSnLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT------SAILIT 518
Cdd:PRK12467 1807 RQQVTTLHFVPSMLQQLLQMDEQVEHPLS-LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvdvthwTCRRKD 1885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 519 PEGDDkpgAVGKVVPFFEAKVVDLDTGKTL---GVnqRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWLH-SGD 588
Cdd:PRK12467 1886 LEGRD---SVPIGQPIANLSTYILDASLNPvpiGV--AGELYLGGVGLARGYLNRPALTaerfvaDPFGTVGSRLYrTGD 1960
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 589 IAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVagLPDDDAG--ELPAAVVVlehgktmTEKEIVD 666
Cdd:PRK12467 1961 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDGANgkQLVAYVVP-------TDPGLVD 2031
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1886431185 667 YVASQVTTAKKLRGGV-------------VFVDEVPKGLTGKLDaRK 700
Cdd:PRK12467 2032 DDEAQVALRAILKNHLkaslpeymvpahlVFLARMPLTPNGKLD-RK 2077
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
157-671 |
3.14e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 88.78 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 157 LHLVLRLRGGMEDAKNIKKGPAPFYPLEDGTA---GEQLHKAMKRYalvPGTIA--FTDAHIevdiTYAEYFEMSVRLAE 231
Cdd:PRK08279 5 MDLAARLPRRLPDLPGILRGLKRTALITPDSKrslGDVFEEAAARH---PDRPAllFEDQSI----SYAELNARANRYAH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 232 AMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiYNERE--LLNSMGISQPTVVFVSKKGLQKILNVQKKL 309
Cdd:PRK08279 78 WAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN--TQQRGavLAHSLNLVDAKHLIVGEELVEAFEEARADL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 310 PIIQKIIIMDSKTDYQgfqsmytfvtshlPPGFNEYDFVPESFDRD----------KTIALIMNSSGSTGLPKGValphr 379
Cdd:PRK08279 156 ARPPRLWVAGGDTLDD-------------PEGYEDLAAAAAGAPTTnpasrsgvtaKDTAFYIYTSGTTGLPKAA----- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 380 tacvRFSHAR----DPIFGN--QIIPDTAILSVVPFHHGFGMFTTLGYLIC-GFRVVLMYRFEEELFLRSLQDYKIqsal 452
Cdd:PRK08279 218 ----VMSHMRwlkaMGGFGGllRLTPDDVLYCCLPLYHNTGGTVAWSSVLAaGATLALRRKFSASRFWDDVRRYRA---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 453 lvpTLFSFFAKstlIDKYDLS----------NLHEIAsgGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAiLITPEGd 522
Cdd:PRK08279 290 ---TAFQYIGE---LCRYLLNqppkptdrdhRLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYAASEGNVG-FINVFN- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 523 dKPGAVGKVvPFFEAK---VV--DLDTGKTL----------GVNQRGELCV----RGPMimSGYvNNPEATNALI----- 578
Cdd:PRK08279 360 -FDGTVGRV-PLWLAHpyaIVkyDVDTGEPVrdadgrcikvKPGEVGLLIGritdRGPF--DGY-TDPEASEKKIlrdvf 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 579 -DKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAG--LPDDD--AGelpAAVVVL 653
Cdd:PRK08279 435 kKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGveVPGTDgrAG---MAAIVL 511
|
570
....*....|....*...
gi 1886431185 654 EHGKTMTEKEIVDYVASQ 671
Cdd:PRK08279 512 ADGAEFDLAALAAHLYER 529
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
351-644 |
4.53e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 87.95 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 351 SFDRDKT-IALIMNSSGSTGLPKGVALPHRT------ACVRFSharDPIfgnqiiPDTAILSVVPFHHGFGMFT-TLGYL 422
Cdd:PRK06334 177 VSDKDPEdVAVILFTSGTEKLPKGVPLTHANllanqrACLKFF---SPK------EDDVMMSFLPPFHAYGFNScTLFPL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 423 ICGFRVVLMYR-FEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPG 501
Cdd:PRK06334 248 LSGVPVVFAYNpLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 502 IRQGYGLTETTSAILITPEGDDK-PGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYV-NNPEATNALID 579
Cdd:PRK06334 328 LRQGYGTTECSPVITINTVNSPKhESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELG 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886431185 580 KDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHpnifdagvAGLPDDDAG 644
Cdd:PRK06334 408 GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNAADHA 464
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
217-639 |
6.17e-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: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiYNER--ELLNSMGISQPTVVFV 294
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN--YNLRgeSLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 295 skkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvpesfDRdktiALIMNSSGSTGLPKGV 374
Cdd:cd05940 82 ----------------------------------------------------------DA----ALYIYTSGTTGLPKAA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 375 ALPHRTaCVRFSHARDPIFGNqiIPDTAILSVVPFHHGFGMFTTLG-YLICGFRVVLMYRFEEELFLRSLQDYKIqsall 453
Cdd:cd05940 100 IISHRR-AWRGGAFFAGSGGA--LPSDVLYTCLPLYHSTALIVGWSaCLASGATLVIRKKFSASNFWDDIRKYQA----- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 454 vpTLFSFFAKstlIDKY-------DLSNLHEI-ASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAiLITPEGddKP 525
Cdd:cd05940 172 --TIFQYIGE---LCRYllnqppkPTERKHKVrMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSG-FINFFG--KP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 526 GAVGkVVPFFEAKV-------VDLDTGKTL----------GVNQRGELCVR----GPMImsGYVNNPEAT-----NALID 579
Cdd:cd05940 244 GAIG-RNPSLLRKVaplalvkYDLESGEPIrdaegrcikvPRGEPGLLISRinplEPFD--GYTDPAATEkkilrDVFKK 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 580 KDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLP 639
Cdd:cd05940 321 GDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
217-700 |
7.83e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.68 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYnERELLNSMGISQPTVVFVSK 296
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY-PQDRLAYMLDDSGVRLLLTQ 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLQKILNVQKKLPIIqkiiIMDSKTDYqgfqsmytfvTSHLPPGFNEYDFVPESfdrdktIALIMNSSGSTGLPKGVAL 376
Cdd:PRK12467 617 SHLLAQLPVPAGLRSL----CLDEPADL----------LCGYSGHNPEVALDPDN------LAYVIYTSGSTGQPKGVAI 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 377 PHRtACVRF--SHARDPifgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR---FEEELFLRSLQDYKIQSA 451
Cdd:PRK12467 677 SHG-ALANYvcVIAERL----QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVL 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 452 LLVPTLFSFFAKSTLIDKydLSNLHEIASGGAPLskEVGEAVAKRFHLPGIR--QGYGLTETTSAILITPEGDDK--PGA 527
Cdd:PRK12467 752 KIVPSHLQALLQASRVAL--PRPQRALVCGGEAL--QVDLLARVRALGPGARliNHYGPTETTVGVSTYELSDEErdFGN 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 528 VGKVVPFFEAKVVDLDTG-KTLGVNQRGELCVRGPMIMSGYVNNP--EATNALIDKDG-----WLHSGDIAYWDEDEHFF 599
Cdd:PRK12467 828 VPIGQPLANLGLYILDHYlNPVPVGVVGELYIGGAGLARGYHRRPalTAERFVPDPFGadggrLYRTGDLARYRADGVIE 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 600 IVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVV---VLEHGKTMTEKEIVDYVASQVTTAK 676
Cdd:PRK12467 908 YLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaaVADGAEHQATRDELKAQLRQVLPDY 987
|
490 500
....*....|....*....|....
gi 1886431185 677 KLRGGVVFVDEVPKGLTGKLDaRK 700
Cdd:PRK12467 988 MVPAHLLLLDSLPLTPNGKLD-RK 1010
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
355-703 |
1.07e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 85.48 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 355 DKTIALIMNSSGSTGLPKGvALPHRTACVRFSHARDPIFGNqiiPDTAILsVVPFHHGFGMFTTLGYLICGFRVV---LM 431
Cdd:PRK07824 34 DDDVALVVATSGTTGTPKG-AMLTAAALTASADATHDRLGG---PGQWLL-ALPAHHIAGLQVLVRSVIAGSEPVeldVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 YRFEEELFLRSLQ----DYKIQSalLVPTLFSFfAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKrfhlPGIR--QG 505
Cdd:PRK07824 109 AGFDPTALPRAVAelggGRRYTS--LVPMQLAK-ALDDPAATAALAELDAVLVGGGPAPAPVLDAAAA----AGINvvRT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 506 YGLTETTSailitpegddkpGAVGKVVPFFEAKVVDLDTGKTLGvnqrgelcvrGPMIMSGYVNNPEatNALIDKDGWLH 585
Cdd:PRK07824 182 YGMSETSG------------GCVYDGVPLDGVRVRVEDGRIALG----------GPTLAKGYRNPVD--PDPFAEPGWFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 586 SGDIAYWDeDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIV 665
Cdd:PRK07824 238 TDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALR 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1886431185 666 DYVASQ--VTTA-KKLRggvvFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK07824 317 AHVARTldRTAApRELH----VVDELPRRGIGKVDRRALVR 353
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
228-661 |
1.12e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 86.46 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 228 RLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANdiynerellnsmgiSQPTVVFvskkgLQKILNVQK 307
Cdd:PRK09029 40 QLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLN--------------PQLPQPL-----LEELLPSLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 308 klpiIQKIIIMDSKTDYQGfqsmytfVTSHLPPGFNEYDFVPESFDRDKTIALimnSSGSTGLPKGVALPHRT------- 380
Cdd:PRK09029 101 ----LDFALVLEGENTFSA-------LTSLHLQLVEGAHAVAWQPQRLATMTL---TSGSTGLPKAAVHTAQAhlasaeg 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 381 --ACVRFSHArdpifgnqiipDTAILSVvPFHHGFGMFTTLGYLICGFRVVLMyrfEEELFLRSLQDykIQSALLVPT-- 456
Cdd:PRK09029 167 vlSLMPFTAQ-----------DSWLLSL-PLFHVSGQGIVWRWLYAGATLVVR---DKQPLEQALAG--CTHASLVPTql 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 457 --LFSFFAKSTLidkydlsnLHEIASGGAPLSKEVGEAVAKRfhlpGIRQ--GYGLTETTSAILITpEGDDKPGaVGKVV 532
Cdd:PRK09029 230 wrLLDNRSEPLS--------LKAVLLGGAAIPVELTEQAEQQ----GIRCwcGYGLTEMASTVCAK-RADGLAG-VGSPL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 533 PFFEAKVVDldtgktlgvnqrGELCVRGPMIMSGYVNNPEATnALIDKDGWLHSGDIAYWDEDEhFFIVDRLKSLIKYKG 612
Cdd:PRK09029 296 PGREVKLVD------------GEIWLRGASLALGYWRQGQLV-PLVNDEGWFATRDRGEWQNGE-LTILGRLDNLFFSGG 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 613 YQVAPAELESILLQHPNIFDAGVagLPDDDA--GELPAAVVVLEHGKTMTE 661
Cdd:PRK09029 362 EGIQPEEIERVINQHPLVQQVFV--VPVADAefGQRPVAVVESDSEAAVVN 410
|
|
| Ubl_FUBI |
cd01793 |
ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins; FUBI is ... |
92-166 |
2.09e-17 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins; FUBI is a pro-apoptotic regulatory gene FAU encoding ubiquitin-like protein with ribosomal protein S30 as a C-terminal extension. FUBI functions as a tumor suppressor protein that may be involved in the ATP-dependent proteolytic activity of ubiquitin. The N-terminal ubiquitin-like (Ubl) domain of FUBI has the beta-grasp Ubl fold, and it may act as a substitute or an inhibitor of ubiquitin or one of ubiquitin's close relatives UCRP, FAT10, and Nedd8.
Pssm-ID: 340491 Cd Length: 74 Bit Score: 76.94 E-value: 2.09e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886431185 92 QIFVKTltGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLRLRGG 166
Cdd:cd01793 2 QLFVRA--QSLHTLEVSGNETVADIKAHIAALEGIAVEDQVLLYAGAPLEDDVVLGQCGIPDLATLEVAVRLLGG 74
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
358-645 |
2.19e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.53 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRTACVRFSHARDPiFGNQIIPDTAILSVVPFHHGFGMFTTLGYLI-CGFRVVLM---YR 433
Cdd:PRK05691 168 IAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHG-FGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIfSGVPCVLMspaYF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 434 FEEEL-FLRSLQDY--KIQSAllvPT----LFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQ-- 504
Cdd:PRK05691 247 LERPLrWLEAISEYggTISGG---PDfayrLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPds 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 505 ---GYGLTETTSAILITPEG--------DDK--------PGAvGKVV-------PFFEAKVVDLDTGKTLGVNQRGELCV 558
Cdd:PRK05691 324 ffaSYGLAEATLFVSGGRRGqgipalelDAEalarnraePGT-GSVLmscgrsqPGHAVLIVDPQSLEVLGDNRVGEIWA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 559 RGPMIMSGYVNNPEAT-NALIDKDG--WLHSGDIAYWDEDEhFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAG- 634
Cdd:PRK05691 403 SGPSIAHGYWRNPEASaKTFVEHDGrtWLRTGDLGFLRDGE-LFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGr 481
|
330
....*....|.
gi 1886431185 635 VAGLPDDDAGE 645
Cdd:PRK05691 482 VAAFAVNHQGE 492
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
181-699 |
2.38e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 181 YPLEDGtageqLHKAMK-RYALVPGTIAFtdAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVL 259
Cdd:PRK12316 507 YPLQRG-----VHRLFEeQVERTPEAPAL--AFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 260 GALFIGVAVAPANDIYNErELLNSMgisqptvvfVSKKGLQKILN---VQKKLPIIQKIIIMDsktdyqgfqsmYTFVTS 336
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPA-ERLAYM---------LEDSGVQLLLSqshLGRKLPLAAGVQVLD-----------LDRPAA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 337 HLPpgfNEYDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMF 416
Cdd:PRK12316 639 WLE---GYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY---GLGVGDTVLQKTPFSFDVSVW 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 417 TTLGYLICGFRVVLM---YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDkyDLSNLHEIASGGAPLSKEVGEAV 493
Cdd:PRK12316 713 EFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQV 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 494 AKRFHLPGIRQGYGLTETTsaILIT-----PEGDDKPgAVGKVVPFFEAKVVDLDTGKT-LGVnqRGELCVRGPMIMSGY 567
Cdd:PRK12316 791 FAKLPQAGLYNLYGPTEAA--IDVThwtcvEEGGDSV-PIGRPIANLACYILDANLEPVpVGV--LGELYLAGRGLARGY 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 568 VNNPEAT------NALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGL--- 638
Cdd:PRK12316 866 HGRPGLTaerfvpSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVdgk 945
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 639 -------PDDDAGELPAAVvvlehgKTMTEKEIVDY-VASQvttakklrggVVFVDEVPKGLTGKLDAR 699
Cdd:PRK12316 946 qlvgyvvLESEGGDWREAL------KAHLAASLPEYmVPAQ----------WLALERLPLTPNGKLDRK 998
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
197-675 |
2.89e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 85.76 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 197 KRYALVPGTIAFTDAHIEVD-------ITYAEYFEMSVRLAEAMKRYGlNTNHRIVVCSENSLQFFMPVLGALFIG-VAV 268
Cdd:PRK05850 9 ERASLQPDDAAFTFIDYEQDpagvaetLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGlIAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 269 ---APANDIYNERelLNS-MGISQPTVVFVSKKglqkilnvqkklpiiqkiiIMDSKTDYQGFQSMYTfvtshlPPGFNE 344
Cdd:PRK05850 88 plsVPQGGAHDER--VSAvLRDTSPSVVLTTSA-------------------VVDDVTEYVAPQPGQS------APPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 345 YDF---------VPESFDRDKTiALIMNSSGSTGLPKGVALPHRTACVRFSH-ARD--PIFGNQIIPDTAILSVVPFHHG 412
Cdd:PRK05850 141 VDLldldsprgsDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFEQlMSDyfGDTGGVPPPDTTVVSWLPFYHD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 413 FGMFttLGY---LICGFRVVLMyrfEEELFLRSLQDYkIQSALLVPTLFSF---FA------KSTLID--KYDLSNLHEI 478
Cdd:PRK05850 220 MGLV--LGVcapILGGCPAVLT---SPVAFLQRPARW-MQLLASNPHAFSAapnFAfelavrKTSDDDmaGLDLGGVLGI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 479 ASGgaplSKEVGEAVAKRF-------HLP--GIRQGYGLTETTsAILITPEGDDKPGAV---------GKVVPF-FEA-- 537
Cdd:PRK05850 294 ISG----SERVHPATLKRFadrfapfNLRetAIRPSYGLAEAT-VYVATREPGQPPESVrfdyeklsaGHAKRCeTGGgt 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 538 -------------KVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATN-----ALIDK-----DG-WLHSGDIAYWD 593
Cdd:PRK05850 369 plvsygsprsptvRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETErtfgaTLVDPspgtpEGpWLRTGDLGFIS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 594 EDEhFFIVDRLKSLIKYKGYQVAPAELESILLQhpnIFDAGVAGL--PDDDAGELPAAVVVLEHGKTMTE-KEIVDYVAS 670
Cdd:PRK05850 449 EGE-LFIVGRIKDLLIVDGRNHYPDDIEATIQE---ITGGRVAAIsvPDDGTEKLVAIIELKKRGDSDEEaMDRLRTVKR 524
|
....*
gi 1886431185 671 QVTTA 675
Cdd:PRK05850 525 EVTSA 529
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
361-704 |
4.80e-17 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 85.39 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 361 IMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQiipdtailsvvpfhHGFGMFTT-------------LGYLICGFR 427
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGK--------------AGETFFCAsdigwvvghsyivYAPLLAGMA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 428 VVlMYrfeEELFLRS--------LQDYKIQSALLVPTLFSFFAKS--TLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRF 497
Cdd:PRK10524 304 TI-MY---EGLPTRPdagiwwriVEKYKVNRMFSAPTAIRVLKKQdpALLRKHDLSSLRALFLAGEPLDEPTASWISEAL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 498 HLPgIRQGYGLTETTSAIL-ITPEGDDKP---GAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPM----------- 562
Cdd:PRK10524 380 GVP-VIDNYWQTETGWPILaIARGVEDRPtrlGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLppgcmqtvwgd 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 563 ---IMSGYvnnpeatnalidkdgWLHSGDIAY----W---DEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFD 632
Cdd:PRK10524 459 ddrFVKTY---------------WSLFGRQVYstfdWgirDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 633 AGVAGLPDDDAGELPAAVVVLEHGKTMT--------EKEIVDYVASQV-TTAKKLRggVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK10524 524 VAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLgAVARPAR--VWFVSALPKTRSGKLLRRAIQA 601
|
.
gi 1886431185 704 I 704
Cdd:PRK10524 602 I 602
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
619-695 |
6.62e-17 |
|
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: 75.66 E-value: 6.62e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886431185 619 ELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRgGVVFVDEVPKGLTGK 695
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPK-EVVFVDELPKTRSGK 76
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
215-697 |
8.09e-17 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 83.68 E-value: 8.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 215 VDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerelLNSMGISQPTVVFV 294
Cdd:cd17654 15 TTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAP----------IDPASPEQRSLTVM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 295 SKKGLQKIL----NVQKKLPIIQKIIIMDSKTDYqgfqsmytfvtshlppgfneydfvpesfdrdkTIALIMNSSGSTGL 370
Cdd:cd17654 85 KKCHVSYLLqnkeLDNAPLSFTPEHRHFNIRTDE--------------------------------CLAYVIHTSGTTGT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 371 PKGVALPHRtaCVR--FSHARD--PIFGNQIIPDTAIL----SVVPFhhgFGMFTTLGYLICgfrVVLMYRFEEELFLRS 442
Cdd:cd17654 133 PKIVAVPHK--CILpnIQHFRSlfNITSEDILFLTSPLtfdpSVVEI---FLSLSSGATLLI---VPTSVKVLPSKLADI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 443 L-QDYKIQSALLVPTLFSFF----AKSTLIDKydLSNLHEIASGGAPLSKEVgEAVAKRFHLPGIR--QGYGLTETTS-A 514
Cdd:cd17654 205 LfKRHRITVLQATPTLFRRFgsqsIKSTVLSA--TSSLRVLALGGEPFPSLV-ILSSWRGKGNRTRifNIYGITEVSCwA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 515 IL-ITPEGdDKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGpmIMSGYVNNPEATnalidkdgWLHSGDIAYWD 593
Cdd:cd17654 282 LAyKVPEE-DSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRVC--ILDDEVTVPKGT--------MRATGDFVTVK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 594 EDEHFFiVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAgLPDDdagELPAAVVVLEHGKTMTEKEIVDYVASqvt 673
Cdd:cd17654 351 DGELFF-LGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT-LSDQ---QRLIAFIVGESSSSRIHKELQLTLLS--- 422
|
490 500
....*....|....*....|....
gi 1886431185 674 tAKKLRGGVVFVDEVPKGLTGKLD 697
Cdd:cd17654 423 -SHAIPDTFVQIDKLPLTSHGKVD 445
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
243-621 |
2.28e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 83.24 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 243 RIVVCSENSLQFFMPVLGALFIG-VAV---APANDIYNEReLLNSMGISQPTVVFVSKKGLQKILNVQKKLPIIQK--II 316
Cdd:PRK07769 81 RVAILAPQNLDYLIAFFGALYAGrIAVplfDPAEPGHVGR-LHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKERprVI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 317 IMDSKTDYQGfqSMYtfvtshlppgfneydfVPESFDRDkTIALIMNSSGSTGLPKGVALPHRTACVRFSHARDPIFGNQ 396
Cdd:PRK07769 160 AVDAVPDEVG--ATW----------------VPPEANED-TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 397 iipDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---------YRFEEELFLRSLQDYKIQSALlvPTlFSF-FAKSTL 466
Cdd:PRK07769 221 ---GDRGVSWLPFFHDMGLITVLLPALLGHYITFMspaafvrrpGRWIRELARKPGGTGGTFSAA--PN-FAFeHAAARG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 467 IDK-----YDLSNLHEIASGGAPLS----KEVGEAVAKrFHLP--GIRQGYGLTETTSAILITPEGD------------- 522
Cdd:PRK07769 295 LPKdgeppLDLSNVKGLLNGSEPVSpasmRKFNEAFAP-YGLPptAIKPSYGMAEATLFVSTTPMDEeptviyvdrdeln 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 523 ---------DKPGAV-----GKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALI---------- 578
Cdd:PRK07769 374 agrfvevpaDAPNAVaqvsaGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlse 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1886431185 579 -------DKDGWLHSGDIAYWdEDEHFFIVDRLKSLIKYKGYQVAPAELE 621
Cdd:PRK07769 454 shaegapDDALWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
214-700 |
3.64e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.29 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 214 EVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAnDIYNERELLNSMgisqptvvf 293
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPL-DPEYPRERLAYM--------- 3187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 294 VSKKGLQKILNVQ---KKLPIIQ--KIIIMDsKTDYQGfqsmytfvtshlppgfnEYDFVPESFDRDKTIALIMNSSGST 368
Cdd:PRK12467 3188 IEDSGVKLLLTQAhllEQLPAPAgdTALTLD-RLDLNG-----------------YSENNPSTRVMGENLAYVIYTSGST 3249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 369 GLPKGVALPHrTACVRFSHARDPIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---YRFEEELFlRSLQD 445
Cdd:PRK12467 3250 GKPKGVGVRH-GALANHLCWIAEAYE--LDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRdndLWDPEELW-QAIHA 3325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 446 YKIQSALLVPTLFSFFAKSTliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETT-SAILITPEGDDK 524
Cdd:PRK12467 3326 HRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVvTVTLWKCGGDAV 3403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 525 PGA----VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALIDKDGWLH-SGDIAYWD 593
Cdd:PRK12467 3404 CEApyapIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTaerfvaDPFSGSGGRLYrTGDLARYR 3482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 594 EDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEK-------EIVD 666
Cdd:PRK12467 3483 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETlrdhlaaSLPD 3562
|
490 500 510
....*....|....*....|....*....|....*
gi 1886431185 667 Y-VASQvttakklrggVVFVDEVPKGLTGKLDaRK 700
Cdd:PRK12467 3563 YmVPAQ----------LLVLAAMPLGPNGKVD-RK 3586
|
|
| Ubiquitin_like_fold |
cd00196 |
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ... |
93-160 |
5.17e-16 |
|
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.
Pssm-ID: 340450 Cd Length: 68 Bit Score: 72.74 E-value: 5.17e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 93 IFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLV 160
Cdd:cd00196 1 VKVETPSLKKIVVAVPPSTTLRQVLEKVAKRIGLPPDVIRLLFNGQVLDDLMTAKQVGLEPGEELHFV 68
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
203-699 |
7.12e-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: 80.78 E-value: 7.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFTDAhiEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPandiynerelln 282
Cdd:cd12114 1 PDATAVICG--DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVP------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 283 sMGISQPtvvfvsKKGLQKIL---NVqkklpiiqKIIIMDSkTDYQGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTiA 359
Cdd:cd12114 67 -VDIDQP------AARREAILadaGA--------RLVLTDG-PDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDL-A 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGVALPHRtACV--------RFshardpifgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM 431
Cdd:cd12114 130 YVIFTSGSTGTPKGVMISHR-AALntildinrRF----------AVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 YRFEEE---LFLRSLQDYKI---QSallVPTLFSFfakstLIDKY-----DLSNLHEIASGG--APLSKEvgEAVAKRFh 498
Cdd:cd12114 199 DEARRRdpaHWAELIERHGVtlwNS---VPALLEM-----LLDVLeaaqaLLPSLRLVLLSGdwIPLDLP--ARLRALA- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 499 lPGIRQ---GyGLTETT--SailITPEGDDKPGAVgKVVPFfeakvvdldtGKTLGvNQR----------------GELC 557
Cdd:cd12114 268 -PDARLislG-GATEASiwS---IYHPIDEVPPDW-RSIPY----------GRPLA-NQRyrvldprgrdcpdwvpGELW 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 558 VRGPMIMSGYVNNPEATNA--LIDKDG--WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDA 633
Cdd:cd12114 331 IGGRGVALGYLGDPELTAArfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARA 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 634 GVAGLPDDDAGELpAAVVVLEHGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDEVPKGLTGKLDAR 699
Cdd:cd12114 411 VVVVLGDPGGKRL-AAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
181-700 |
1.14e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.93 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 181 YPLEDGTagEQLHKAMKRYALVPGTIAFTDAHIevdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLG 260
Cdd:PRK12316 3053 YPLERGV--HRLFEEQVERTPDAVALAFGEQRL----SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLA 3126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 261 ALFIGVAVAPANDIYNERELLNSMGISqptvvfvskkGLQKILNVQK-KLPIIQKIIIMDSKTDYQGFQSMYtfvtshlp 339
Cdd:PRK12316 3127 ILKAGGAYVPLDPEYPEERLAYMLEDS----------GAQLLLSQSHlRLPLAQGVQVLDLDRGDENYAEAN-------- 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 340 pgfneydfvPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACvrfSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTL 419
Cdd:PRK12316 3189 ---------PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALS---NHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELF 3256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 420 GYLICGFRVVLMYRfEEELFLRSLQDYKIQSALLVPTLFSFFAKSTL--IDKYDLSNLHEIASGGAPLSkevGEAVAKRF 497
Cdd:PRK12316 3257 WPLMSGARVVLAGP-EDWRDPALLVELINSEGVDVLHAYPSMLQAFLeeEDAHRCTSLKRIVCGGEALP---ADLQQQVF 3332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 498 HLPGIRQGYGLTETTSAILITPEGDDKPGA--VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT- 574
Cdd:PRK12316 3333 AGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTa 3411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 575 -----NALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAG----------LP 639
Cdd:PRK12316 3412 erfvpDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAvdgrqlvayvVP 3491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 640 DDDAGELPAAVvvlehgKTMTEKEIVDY-VASQvttakklrggVVFVDEVPKGLTGKLDaRK 700
Cdd:PRK12316 3492 EDEAGDLREAL------KAHLKASLPEYmVPAH----------LLFLERMPLTPNGKLD-RK 3536
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
358-699 |
1.15e-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: 80.20 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGNQIIPdTAILSVVPFhhGFGMFTT--LGYLICGFRVVLM---Y 432
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHRNV-AHAAHAWRREYELDSFP-VRLLQMASF--SFDVFAGdfARSLLNGGTLVICpdeV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 433 RFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFhLPGIR--QGYGLTE 510
Cdd:cd17650 171 KLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARF-GQGMRiiNSYGVTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 511 TTSAILITPEGDDKPGA-----VGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT------NALID 579
Cdd:cd17650 250 ATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTaerfveNPFAP 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 580 KDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHgkTM 659
Cdd:cd17650 329 GERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA--TL 406
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1886431185 660 TEKEIVDYVASQVTTAkKLRGGVVFVDEVPKGLTGKLDAR 699
Cdd:cd17650 407 NTAELRAFLAKELPSY-MIPSYYVQLDALPLTPNGKVDRR 445
|
|
| Rad60-SLD |
pfam11976 |
Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl ... |
91-161 |
2.43e-15 |
|
Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl family member, and although SUMO-1 shares structural similarity to Ub, SUMO's cellular functions remain distinct insomuch as SUMO modification alters protein function through changes in activity, cellular localization, or by protecting substrates from ubiquitination. Rad60 family members contain functionally enigmatic, integral SUMO-like domains (SLDs). Despite their divergence from SUMO, each Rad60 SLD interacts with a subset of SUMO pathway enzymes: SLD2 specifically binds the SUMO E2 conjugating enzyme (Ubc9)), whereas SLD1 binds the SUMO E1 (Fub2, also called Uba2) activating and E3 (Pli1, also called Siz1 and Siz2) specificity enzymes. Structural analysis of PDB:2uyz reveals a mechanistic basis for the near-synonymous roles of Rad60 and SUMO in survival of genotoxic stress and suggest unprecedented DNA-damage-response functions for SLDs in regulating SUMOylation. The Rad60 branch of this family is also known as RENi (Rad60-Esc2-Nip45), and biologically it should be two distinct families SUMO and RENi (Rad60-Esc2-Nip45).
Pssm-ID: 403255 [Multi-domain] Cd Length: 72 Bit Score: 71.05 E-value: 2.43e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 91 WQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQ-RLIFAGRQLEDGRTLSDYNIQKESTLHLVL 161
Cdd:pfam11976 1 IKIILKGKDGKEVFIKVKPTTTVSKLINAYRKKRGIPPSQQvRLIFDGERLDPNSTVEDLDIEDGDTIDVVI 72
|
|
| Ubl_BAG6 |
cd01809 |
ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; ... |
92-162 |
2.63e-15 |
|
ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; BAG6, also termed large proline-rich protein BAG6, or BAG family molecular chaperone regulator 6, or HLA-B-associated transcript 3 (Bat3), or protein Scythe, or protein G3, is a nucleo-cytoplasmic shuttling chaperone protein that is highly conserved in eukaryotes. It functions in two distinct biological pathways, ubiquitin-mediated protein degradation of defective polypeptides and tail-anchored transmembrane protein biogenesis in mammals. BAG6 is a component of the heterotrimeric BAG6 sortase complex composed of BAG6, transmembrane recognition complex 35 (TRC35) and ubiquitin-like protein 4A (UBL4A). The BAG6 complex together with the cochaperone small, glutamine-rich, tetratricopeptide repeat-containing, protein alpha (SGTA) plays a role in the biogenesis of tail-anchored membrane proteins and subsequently shown to regulate the ubiquitination and proteasomal degradation of mislocalized proteins. Moreover, BAG6 acts as an apoptotic regulator that binds reaper, a potent apoptotic inducer. BAG6/reaper is thought to signal apoptosis, in part through regulating the folding and activity of apoptotic signaling molecules. It is also likely a key regulator of the molecular chaperone Heat Shock Protein A2 (HSPA2) stability/function in human germ cells. Furthermore, aspartyl protease-mediated cleavage of BAG6 is necessary for autophagy and fungal resistance in plants. BAG6 contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which provides a platform for discriminating substrates with shorter hydrophobicity stretches as a signal for defective proteins.
Pssm-ID: 340507 [Multi-domain] Cd Length: 71 Bit Score: 70.84 E-value: 2.63e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQkESTLHLVLR 162
Cdd:cd01809 2 EVTVKTLDSQNRTFTVPEEITVKEFKEHIASSVNIPAEKQRLIFQGRVLQDDKKLKEYDVD-GKVIHLVER 71
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
217-703 |
3.10e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.21 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 217 ITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSK 296
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 297 KGLQKILNVQKKLPIIQKIIIMDSKTDYqgfqsmytfvtshlPPGFNEYDfvpesfdrdKTIALIMNSSGSTGLPKGVAL 376
Cdd:PRK05691 1237 HLLERLPQAEGVSAIALDSLHLDSWPSQ--------------APGLHLHG---------DNLAYVIYTSGSTGQPKGVGN 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 377 PHRTACVRFSHARDPIfgnQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEE---ELFLRSLQDYKIQSALL 453
Cdd:PRK05691 1294 THAALAERLQWMQATY---ALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHrdpQRIAELVQQYGVTTLHF 1370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 454 VPTLFSFFAKSTLIDkyDLSNLHEIASGGAPLSKEVGEAVAKRfhLPGIR--QGYGLTETtsAILIT------PEGDDKP 525
Cdd:PRK05691 1371 VPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQR--LPQVQlhNRYGPTET--AINVThwqcqaEDGERSP 1444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 526 gaVGKVVPFFEAKVVDLDTGKT-LGVnqRGELCVRGPMIMSGYVNNP--EATNALIDKDG-----WLHSGDIAYWDEDEH 597
Cdd:PRK05691 1445 --IGRPLGNVLCRVLDAELNLLpPGV--AGELCIGGAGLARGYLGRPalTAERFVPDPLGedgarLYRTGDRARWNADGA 1520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 598 FFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAgLPDDDAGE--------LPAAVVVLEHGKTMTEKEIVDY-V 668
Cdd:PRK05691 1521 LEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAqlvgyytgEAGQEAEAERLKAALAAELPEYmV 1599
|
490 500 510
....*....|....*....|....*....|....*
gi 1886431185 669 ASQvttakklrggVVFVDEVPKGLTGKLDARKIRE 703
Cdd:PRK05691 1600 PAQ----------LIRLDQMPLGPSGKLDRRALPE 1624
|
|
| Ubl_parkin |
cd01798 |
ubiquitin-like (Ubl) domain found in parkin and similar proteins; Parkin, also termed ... |
93-162 |
4.76e-15 |
|
ubiquitin-like (Ubl) domain found in parkin and similar proteins; Parkin, also termed Parkinson juvenile disease protein 2, is a RBR-type E3 ubiquitin-protein ligase that is associated with recessive early onset Parkinson's disease (PD), and exerts a protective effect against dopamine-induced alpha-synuclein-dependent cell toxicity. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Parkin functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPT5, TOMM20, USP30, ZNF746 and AIMP2. It mediates monoubiquitination as well as Lys-6-, Lys-11-, Lys-48- and Lys-63-linked polyubiquitination of substrates depending on the context. Parkin may enhance cell viability and protects dopaminergic neurons from oxidative stress-mediated death by regulating mitochondrial function. It also limits the production of reactive oxygen species (ROS), and regulates cyclin-E during neuronal apoptosis. Moreover, parkin displays a ubiquitin ligase-independent function in transcriptional repression of p53. Parkin contains an N-terminal ubiquitin-like (Ubl) domain and a C-terminal RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain use an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction.
Pssm-ID: 340496 Cd Length: 74 Bit Score: 70.40 E-value: 4.76e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 93 IFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd01798 1 VFVRFNSSHGFPVEVDSDWSILQLKEVVAKRQGVPPDQLRIIFAGKELSDDLTLQNCDLGQQSIVHAVQG 70
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
203-701 |
4.99e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 78.40 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 203 PGTIAFtdAHIEVDITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSlqFFMPV--LGALFIGVAVAPAnDIYNEREL 280
Cdd:PRK04813 16 PDFPAY--DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMS--PEMLAtfLGAVKAGHAYIPV-DVSSPAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 281 LNS-MGISQPTVVFVSKKGLQKILNVqkklPIIQKIIIMDSKtdyqgfqsmytfvtshlppgFNEYDFVPESFDRDKTIA 359
Cdd:PRK04813 91 IEMiIEVAKPSLIIATEELPLEILGI----PVITLDELKDIF--------------------ATGNPYDFDHAVKGDDNY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGVALPHRT-------ACVRFSHARDPIFGNQIiP---DTAILSVVPfhhgfgMFTTLGYLICGFRVV 429
Cdd:PRK04813 147 YIIFTSGTTGKPKGVQISHDNlvsftnwMLEDFALPEGPQFLNQA-PysfDLSVMDLYP------TLASGGTLVALPKDM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 430 LMyRFEEeLFlRSLQDYKI----------QSALLVPTLfsffakstliDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHL 499
Cdd:PRK04813 220 TA-NFKQ-LF-ETLPQLPInvwvstpsfaDMCLLDPSF----------NEEHLPNLTHFLFCGEELPHKTAKKLLERFPS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 500 PGIRQGYGLTETT---SAILITPEGDDK--PGAVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEAT 574
Cdd:PRK04813 287 ATIYNTYGPTEATvavTSIEITDEMLDQykRLPIGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 575 N-ALIDKDGW--LHSGDIAYWDeDEHFFIVDRLKSLIKYKGYQVapaELESI---LLQHPNIFDAGVAGLPDDDAGELPA 648
Cdd:PRK04813 366 AeAFFTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRI---ELEEIeqnLRQSSYVESAVVVPYNKDHKVQYLI 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886431185 649 AVVVLEHGKtmTEKEIvdyvasQVTTA--KKLRGGV---------VFVDEVPKGLTGKLDARKI 701
Cdd:PRK04813 442 AYVVPKEED--FEREF------ELTKAikKELKERLmeymiprkfIYRDSLPLTPNGKIDRKAL 497
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
356-701 |
7.27e-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: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 356 KTIALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLM---Y 432
Cdd:cd17648 94 TDLAYAIYTSGTTGKPKGVLVEHGSV-VNLRTSLSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPpdeM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 433 RFEEELFLRSLQDYKIqsallvpTLFSffAKSTLIDKYDLS---NLHEIASGGAPLSKEVGEAVAKRFhlPG-IRQGYGL 508
Cdd:cd17648 173 RFDPDRFYAYINREKV-------TYLS--GTPSVLQQYDLArlpHLKRVDAAGEEFTAPVFEKLRSRF--AGlIINAYGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 509 TETTSAILITPEGDDKP--GAVGKVVPFFEAKVVDLDTgKTLGVNQRGELCVRGPMIMSGYVNNPEAT------------ 574
Cdd:cd17648 242 TETTVTNHKRFFPGDQRfdKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTaerflpnpfqte 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 575 -------NALIDKDG----WLHSGDIAYwdedehffiVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVagLPDDDA 643
Cdd:cd17648 321 qerargrNARLYKTGdlvrWLPSGELEY---------LGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAV--VAKEDA 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886431185 644 GELPAAVV-------VLEHGkTMTEKEIVDYVASQVTTAkKLRGGVVFVDEVPKGLTGKLDARKI 701
Cdd:cd17648 390 SQAQSRIQkylvgyyLPEPG-HVPESDLLSFLRAKLPRY-MVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
461-696 |
1.58e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 76.73 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 461 FAKStLIDKY-------DLSNLHEIASGGAPLSKE----VGEAVAkRFHL-PG-IRQGYGLTETTSAI------------ 515
Cdd:PRK05851 254 FAYN-LIGKYarrvsdvDLGALRVALNGGEPVDCDgferFATAMA-PFGFdAGaAAPSYGLAESTCAVtvpvpgiglrvd 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 516 -LITPEGD--DKPGAVGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPMIMSGYVNNPEatnalIDKDGWLHSGDIAYW 592
Cdd:PRK05851 332 eVTTDDGSgaRRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 593 DEDEhFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEH---GKTMTEKEIVDYVA 669
Cdd:PRK05851 407 VDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFrgpDEAGARSEVVQRVA 485
|
250 260 270
....*....|....*....|....*....|.
gi 1886431185 670 SQ--VTTAKklrggVVFVD--EVPKGLTGKL 696
Cdd:PRK05851 486 SEcgVVPSD-----VVFVApgSLPRTSSGKL 511
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
472-706 |
2.03e-14 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 76.19 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 472 LSNLHEIASGGAPLSKEVGEAvAKRFHLPgIRQGYGLTETTSAIL-ITPE----GDDkpgAVGKVVPffEAKVvdldtgk 546
Cdd:PRK07445 229 LAQFRTILLGGAPAWPSLLEQ-ARQLQLR-LAPTYGMTETASQIAtLKPDdflaGNN---SSGQVLP--HAQI------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 547 TLGVNQRGELCVRGPMIMSGYVnnPEatnaLIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ 626
Cdd:PRK07445 295 TIPANQTGNITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 627 HPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEkEIVDYVASQVTTAKKLRGGVVfVDEVPKGLTGKLDARKIREILI 706
Cdd:PRK07445 369 TGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE-ELKTAIKDQLSPFKQPKHWIP-VPQLPRNPQGKINRQQLQQIAV 446
|
|
| Ubl2_OASL |
cd16103 |
ubiquitin-like (Ubl) domain 2 found in 2'-5'-oligoadenylate synthase-like protein (OASL) and ... |
92-161 |
2.24e-14 |
|
ubiquitin-like (Ubl) domain 2 found in 2'-5'-oligoadenylate synthase-like protein (OASL) and similar proteins; OASL, also termed 2'-5'-OAS-related protein (2'-5'-OAS-RP), or 59 kDa 2'-5'-oligoadenylate synthase-like protein, or thyroid receptor-interacting protein 14, or TR-interacting protein 14 (TRIP-14), or p59 OASL (p59OASL), is an interferon (IFN)-induced antiviral protein that plays an important role in the IFNs-mediated antiviral signaling pathway. It inhibits respiratory syncytial virus replication and is targeted by the viral nonstructural protein 1 (NS1). It also displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L. Moreover, OASL does not have 2'-5'-OAS activity, but can bind double-stranded RNA (dsRNA) to enhance RIG-I signaling. OASL belongs to the 2'-5' oligoadenylate synthase (OAS) family. While each member of this family has a conserved N-terminal OAS catalytic domain, only OASL has two tandem C-terminal ubiquitin-like (Ubl) repeats, which are required for its antiviral activity. This family corresponds to the second Ubl domain.
Pssm-ID: 340520 [Multi-domain] Cd Length: 72 Bit Score: 68.47 E-value: 2.24e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVL 161
Cdd:cd16103 3 QIFVKFPDGTSKPYAINPEDTILDLKEKIEEQGGPPVEDQILLFQGQELRDKKSLKYYGIKDGDTLQLSL 72
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
454-696 |
6.40e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 75.45 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 454 VPTLFSFFAKSTLIDKYdlSNLHEIASGGAPLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVP 533
Cdd:PRK06060 243 VPNFFARVIDSCSPDSF--RSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLP 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 534 FFEAKVVDLDtGKTLGVNQRGELCVRGPMIMSGYVNNPEatnALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGY 613
Cdd:PRK06060 321 PYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGV 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 614 QVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEKEIVDYVASQVT--TAKKLRGGVVFVDEVPKG 691
Cdd:PRK06060 397 NVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNrlSAFKVPHRFAVVDRLPRT 476
|
....*
gi 1886431185 692 LTGKL 696
Cdd:PRK06060 477 PNGKL 481
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
355-630 |
6.65e-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: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 355 DKTIALIMNSSGSTGLPKGVALPHRTAcVRFSHARDPIFGNQiiPDTAI-LSVVPFHHGFG---MFTTL-----GY---- 421
Cdd:cd17632 222 DDPLALLIYTSGSTGTPKGAMYTERLV-ATFWLKVSSIQDIR--PPASItLNFMPMSHIAGrisLYGTLarggtAYfaaa 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 422 -----------LICGFRVVLMYRFEEELFLR--SLQDYKIQSALLVPTLfSFFAKSTLIDKYDLSNLHEIASGGAPLSKE 488
Cdd:cd17632 299 sdmstlfddlaLVRPTELFLVPRVCDMLFQRyqAELDRRSVAGADAETL-AERVKAELRERVLGGRLLAAVCGSAPLSAE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 489 VGEAVAKRFHLPgIRQGYGLTETTSAILItpegddkpgavGKVV--PFFEAKVVDL-DTG--KTLGVNQRGELCVRGPMI 563
Cdd:cd17632 378 MKAFMESLLDLD-LHDGYGSTEAGAVILD-----------GVIVrpPVLDYKLVDVpELGyfRTDRPHPRGELLVKTDTL 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 564 MSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIKY-KGYQVAPAELESILLQHPNI 630
Cdd:cd17632 446 FPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLV 513
|
|
| Ubl1_ISG15 |
cd01792 |
ubiquitin-like (Ubl) domain 1 found in interferon-stimulated gene 15 (ISG15) and similar ... |
91-162 |
9.10e-14 |
|
ubiquitin-like (Ubl) domain 1 found in interferon-stimulated gene 15 (ISG15) and similar proteins; ISG15, also termed interferon-induced 15 kDa protein, or interferon-induced 17 kDa protein (IP17), or ubiquitin cross-reactive protein (UCRP), is an antiviral interferon-induced ubiquitin-like protein (Ubl) that upon viral infection, modifies cellular and viral proteins by mechanisms similar to ubiquitination. Although ISG15 has properties similar to those of other Ubl molecules, it is a unique member of the Ubl superfamily, whose expression and conjugation to target proteins are tightly regulated by specific signaling pathways, indicating it may have specialized functions in the immune system. ISG15 contains two tandem Ubl domains with a beta-grasp Ubl fold. This family corresponds to the first Ubl domain.
Pssm-ID: 340490 Cd Length: 75 Bit Score: 66.79 E-value: 9.10e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886431185 91 WQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIF--AGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd01792 1 WDLTVKMLTGNEFQVSVSPSMTVSELKAQITQKIGVPAFQQRLAVqpSGVELQDGVRLASQGLGPSSTVLLVVK 74
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
474-609 |
2.84e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 73.21 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 474 NLHEIASGGAPLSKEVGEAVAKRFHLpGIRQGYGLTETTSAILITPEGDDKPGAVG-KVVPFFEAKVVDLDTGKTLGVNQ 552
Cdd:PTZ00342 462 NLEVILNGGGKLSPKIAEELSVLLNV-NYYQGYGLTETTGPIFVQHADDNNTESIGgPISPNTKYKVRTWETYKATDTLP 540
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886431185 553 RGELCVRGPMIMSGYVNNPEATNALIDKDGWLHSGDIAYWDEDEHFFIVDRLKSLIK 609
Cdd:PTZ00342 541 KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| Ubl_TAFs_like |
cd17064 |
ubiquitin-like (Ubl) domain found in plant TBP-associated factors (TAFs) and similar proteins; ... |
92-160 |
5.44e-13 |
|
ubiquitin-like (Ubl) domain found in plant TBP-associated factors (TAFs) and similar proteins; TAFs, also termed transcription initiation factor TFIID subunits, or TAFII250 subunits, are components of the TFIID complex, a multisubunit protein complex involved in promoter recognition and essential for mediating regulation of RNA polymerase transcription. TAFs is the core scaffold of the TFIID complex, which is comprised of the TATA binding protein (TBP) and 12-15 TAFs. TAFs contain a ubiquitin-like (Ubl) domain and a Bromo domain.
Pssm-ID: 340584 [Multi-domain] Cd Length: 72 Bit Score: 64.39 E-value: 5.44e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQ-RLIFAGRQLEDGRTLSDYNIQKESTLHLV 160
Cdd:cd17064 2 KVIVKSLGGKGSLLRVDASETLESLKGKASKKLDDKPSEKvKLFYSGKELEDGKSLAEQNVPPNSLVHLV 71
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
359-630 |
1.06e-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: 70.95 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHRTACVRFSHARDpIFGnqIIPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYRFEEEL 438
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQ-LYG--IRPGEVDLATFPLFALFGPALGLTSVIPDMDPTRPARADPQK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 439 FLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDLSNLHEIASGGAPLSKEVGEAVAKRFHlPG--IRQGYGLTET----- 511
Cdd:cd05910 165 LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLS-DEaeILTPYGATEAlpvss 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 --TSAILITPEGDDKPGA---VGKVVPFFEAKVVDLDTGKTLGVNQR--------GELCVRGPMIMSGYVNNPEATNALI 578
Cdd:cd05910 244 igSRELLATTTAATSGGAgtcVGRPIPGVRVRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAK 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 579 DKDG----WLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNI 630
Cdd:cd05910 324 IDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV 379
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
218-702 |
1.84e-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: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 218 TYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKk 297
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFNL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 298 gLQKILNVQKKLPIIQKIIIMDSKTDYqgfqsMYTfvtshlppgfneydfvpesfdrdktialimnsSGSTGLPKGVALP 377
Cdd:cd05939 84 -LDPLLTQSSTEPPSQDDVNFRDKLFY-----IYT--------------------------------SGTTGLPKAAVIV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 378 HrtacVRF-SHARDPIFGNQIIPDTAILSVVPFHHGFGMFTTLGY-LICGFRVVLMYRFEEELFLRSLQDYKIQSALLVP 455
Cdd:cd05939 126 H----SRYyRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQaLLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 456 TLFSFFAKSTLIDKYDLSNLHEIASGGapLSKEVGEAVAKRFHLPGIRQGYGLTETTSAILitpEGDDKPGAVGkVVPFF 535
Cdd:cd05939 202 EICRYLLAQPPSEEEQKHNVRLAVGNG--LRPQIWEQFVRRFGIPQIGEFYGATEGNSSLV---NIDNHVGACG-FNSRI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 536 EAKV-------VDLDTGKTLgvNQRGELCVR------GPMI-----------MSGYVNNpEATNALIDKDGWLH------ 585
Cdd:cd05939 276 LPSVypirlikVDEDTGELI--RDSDGLCIPcqpgepGLLVgkiiqndplrrFDGYVNE-GATNKKIARDVFKKgdsafl 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 586 SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpdddagELP--------AAVVVLEhgk 657
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV------EVPgvegragmAAIVDPE--- 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1886431185 658 tmtEKEIVDYVASQVTTAKKLRGGVVFV---DEVPKGLTGKLDARKIR 702
Cdd:cd05939 424 ---RKVDLDRFSAVLAKSLPPYARPQFIrllPEVDKTGTFKLQKTDLQ 468
|
|
| Ubl_UBTD |
cd01794 |
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and ... |
99-153 |
2.86e-12 |
|
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and similar proteins; This family represents a group of ubiquitin-like (Ubl) domain-containing proteins evolutionarily conserved and found in metazoa, fungi, and plants. They may regulate the activity and/or specificity of E2 ubiquitin conjugating enzymes belonging to the UBE2D family. Members in this family contain an N-terminal ubiquitin binding domain (UBD) and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.
Pssm-ID: 340492 Cd Length: 69 Bit Score: 62.31 E-value: 2.86e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1886431185 99 TGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQK 153
Cdd:cd01794 7 TGKDLKLSVRSTDTVLQAKRRLQALEGIEPSRQRWFFSGKLLTDKTRIEDAKIPK 61
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
358-699 |
1.07e-11 |
|
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: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 358 IALIMNSSGSTGLPKGVALPHRtACVRFSH---------ARDPIFGNQIIP-DTAILSVVPfhhgfgMFTTLGYLIcgFR 427
Cdd:cd17644 108 LAYVIYTSGSTGKPKGVMIEHQ-SLVNLSHglikeygitSSDRVLQFASIAfDVAAEEIYV------TLLSGATLV--LR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 428 VVLMyRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKYDL-SNLHEIASGGAPLSKEVGEAVAKRF-HLPGIRQG 505
Cdd:cd17644 179 PEEM-RSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 506 YGLTE-TTSAILITPEGDDKPG----AVGKVVPFFEAKVVDlDTGKTLGVNQRGELCVRGPMIMSGYVNNPEATNALIDK 580
Cdd:cd17644 258 YGPTEaTIAATVCRLTQLTERNitsvPIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 581 DGWLHS--------GDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIfdagvaglpdddagelpAAVVV 652
Cdd:cd17644 337 HPFNSSeserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV-----------------KTAVV 399
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886431185 653 LEHGKTMTEKEIVDYVASQVTTA---KKLR-------------GGVVFVDEVPKGLTGKLDAR 699
Cdd:cd17644 400 IVREDQPGNKRLVAYIVPHYEESpstVELRqflkaklpdymipSAFVVLEELPLTPNGKIDRR 462
|
|
| Ubl_UHRF2 |
cd17123 |
ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing ... |
93-162 |
3.49e-11 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); UHRF2, also termed Np95/ICBP90-like RING finger protein (NIRF), or Np95-likeRING finger protein, or nuclear protein 97, or nuclear zinc finger protein Np97, or RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2, was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131(ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) through interacting with HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (Ubl), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a set- and ring-associated (SRA) domain, and a C-terminal RING finger.
Pssm-ID: 340643 Cd Length: 74 Bit Score: 59.50 E-value: 3.49e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 93 IFVKTLTGK-TITLE-VEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd17123 3 IQVRTIDGTeTQTIDdLSRLTKIESLREKIQELFNVRPERQRLFYRGKQLEDGHTLFDYNVGLNDIVQLLIR 74
|
|
| Ubl_SF3a120 |
cd01800 |
ubiquitin-like (Ubl) domain found in splicing factor 3A 120kDa subunit (SF3a120) and similar ... |
98-162 |
5.59e-11 |
|
ubiquitin-like (Ubl) domain found in splicing factor 3A 120kDa subunit (SF3a120) and similar proteins; Mammalian splicing factor SF3a consists of three subunits of 60, 66, and 120 kDa and functions early during pre-mRNA splicing by converting the U2 snRNP to its active form. The 120kDa subunit SF3a120, also termed splicing factor 3A subunit 1 (SF3A1), or spliceosome-associated protein 114 (SAP114), is the U2 snRNP-specific protein that is critical for spliceosome assembly and normal splicing events. During splicing, SF3a120, together with the U2 snRNP and other proteins, are recruited to the 3' splicing site to generate the splicing complex A after the recognition of the 3' splicing site. SF3a120 contains two N-terminal SWAP (suppressor-of-white-apricot) domains, referred to collectively as the SURP module, as well as a C-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.
Pssm-ID: 340498 Cd Length: 84 Bit Score: 59.12 E-value: 5.59e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 98 LTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRL-IFAGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd01800 19 LNGQVLELTLPLTDTISVLKEKIHEELGMPANKQKLqVEGGGFLKDSNSLAFYNLGSGTVLTLSLK 84
|
|
| Ubl1_FAT10 |
cd17052 |
ubiquitin-like (Ubl) domain 1 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ... |
95-163 |
7.52e-11 |
|
ubiquitin-like (Ubl) domain 1 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins; FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the first Ubl domain of FAT10. Some family members contain only one Ubl domain.
Pssm-ID: 340572 [Multi-domain] Cd Length: 74 Bit Score: 58.44 E-value: 7.52e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 95 VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLRL 163
Cdd:cd17052 4 VQSEEWDLMTFDANPQDSVKKINEHVRSKTKVPVQDQVLLLGSKILKPRRRLSSYGIDKEKTIHLTLKV 72
|
|
| Ubl_Ddi1_like |
cd01796 |
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, ... |
92-152 |
1.01e-10 |
|
ubiquitin-like (Ubl) domain found in the eukaryotic Ddi1 family; The eukaryotic Ddi1 family, including yeast aspartyl protease DNA-damage inducible 1 (Ddi1) and Ddi1-like proteins from vertebrates and other eukaryotes, has been characterized by containing an N-terminal ubiquitin-like (Ubl) domain and a conserved retroviral aspartyl-protease-like domain (RVP) that is important in cell-cycle control. Yeast Ddi1 and many family members also contain a C-terminal ubiquitin-association (UBA) domain, however, Ddi1-like proteins from all vertebrates lack the UBA domain. Ddi1, also termed v-SNARE-master 1 (Vsm1), is an ubiquitin receptor involved in the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as an UBA-Ubl shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also termed transporter regulator RS1 (RS1), which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1. Ddi1-like proteins play a significant role in cell cycle control, growth control, and trafficking in yeast and may play a crucial role in embryogenesis in higher eukaryotes.
Pssm-ID: 340494 [Multi-domain] Cd Length: 73 Bit Score: 57.95 E-value: 1.01e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886431185 92 QIFVKTL-TGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQL-EDGRTLSDYNIQ 152
Cdd:cd01796 2 KLTVTTEdDDRLFSLEVSPDMTLEDLKALCEAETGIPAAEQVLLHNGQPLtDDKKTLEALGLK 64
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
360-703 |
1.12e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 64.29 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 360 LIMNSSGSTGLPKGVALPHrTACVRFSHARDPIFgnQIIPDTAILSVVPFHHGFGmfttlgyLICGF--------RVVLM 431
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSW-TEIDREIEAYNEAL--NCEQDETPIVACPVTHSYG-------LICGVlaaltrgsKPVII 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 YRFEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLIDKydlsNLHEIASGGAPLSKEVGEAVAKR-FHLpgiRQGYGLTE 510
Cdd:PRK08308 175 TNKNPKFALNILRNTPQHILYAVPLMLHILGRLLPGTF----QFHAVMTSGTPLPEAWFYKLRERtTYM---MQQYGCSE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 511 TtSAILITPEGDDkPGAVGKVVPFfeakvVDLDTGKtlGVNQRGELCVRgpmimsgyVNNPEatnalidkdgwLHSGDIA 590
Cdd:PRK08308 248 A-GCVSICPDMKS-HLDLGNPLPH-----VSVSAGS--DENAPEEIVVK--------MGDKE-----------IFTKDLG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 591 YWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHgkTMTEKEIVDYVAS 670
Cdd:PRK08308 300 YKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE--EIDPVQLREWCIQ 377
|
330 340 350
....*....|....*....|....*....|...
gi 1886431185 671 QVtTAKKLRGGVVFVDEVPKGLTGKLdARKIRE 703
Cdd:PRK08308 378 HL-APYQVPHEIESVTEIPKNANGKV-SRKLLE 408
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
215-654 |
1.97e-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: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 215 VDITYAEYFEMSVRLAEAM-KRYGLNTNHRIVVCSENSLQFFMPVLGALFIGVAVAPAN--DIYNE-RELLNSMGISQPT 290
Cdd:cd05905 13 TTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEppDISQQlGFLLGTCKVRVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 291 VVFVSKKGLQKILNVQKklpiiQKIIIMDSKtdyqGFQSMYTFVTSHLPPGFNEYDFVPESFDRDKTIALIMNSSGSTGL 370
Cdd:cd05905 93 TVEACLKGLPKKLLKSK-----TAAEIAKKK----GWPKILDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 371 PKGVALPHRTAcvrFSHARDPIFGNQIIPDTAILSVVPFHHGFG-MFTTLGYLICGFRVVLMYRFEEE----LFLRSLQD 445
Cdd:cd05905 164 LSGVAVSHSSL---LAHCRALKEACELYESRPLVTVLDFKSGLGlWHGCLLSVYSGHHTILIPPELMKtnplLWLQTLSQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 446 YKIQSALLvptLFSFFAKSTLIDKYDLSNLHE-----------IASGGAPLSKEVGEAVAKRFHLPGIR----------- 503
Cdd:cd05905 241 YKVRDAYV---KLRTLHWCLKDLSSTLASLKNrdvnlsslrmcMVPCENRPRISSCDSFLKLFQTLGLSpravstefgtr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 504 -------QGYGLTETTSAIL---------ITPEGDDKPGA-----VGKVVPFFEAKVVDLDTGKTLGVNQRGELCVRGPM 562
Cdd:cd05905 318 vnpficwQGTSGPEPSRVYLdmralrhgvVRLDERDKPNSlplqdSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 563 IMSGYVNNPEATNAL------------IDKDGWLHSGDIAYWDEDEHF----------FIVDRLKSLIKYKGYQVAPAEL 620
Cdd:cd05905 398 NASGYFLLDGETNDTfkvfpstrlstgITNNSYARTGLLGFLRPTKCTdlnveehdllFVVGSIDETLEVRGLRHHPSDI 477
|
490 500 510
....*....|....*....|....*....|....*
gi 1886431185 621 E-SILLQHPNIFDAGVAglpddDAGELPaaVVVLE 654
Cdd:cd05905 478 EaTVMRVHPYRGRCAVF-----SITGLV--VVVAE 505
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
216-707 |
2.70e-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: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 216 DITYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLGALFIG---VAVAPanDiYNERELLNSMGISQPTVV 292
Cdd:cd05943 98 EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGaiwSSCSP--D-FGVPGVLDRFGQIEPKVL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 293 F----VSKKG-----LQKILNVQKKLP-IIQKIIIMDSKTDYQG-------FQSMYTFVTSHLPPgfnEYDFVPESFDRD 355
Cdd:cd05943 175 FavdaYTYNGkrhdvREKVAELVKGLPsLLAVVVVPYTVAAGQPdlskiakALTLEDFLATGAAG---ELEFEPLPFDHP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 356 ktiALIMNSSGSTGLPKGVAlpHRTACVRFSHARDPIFGNQIIP-DTailsvvpfhhgFGMFTTLGY---------LICG 425
Cdd:cd05943 252 ---LYILYSSGTTGLPKCIV--HGAGGTLLQHLKEHILHCDLRPgDR-----------LFYYTTCGWmmwnwlvsgLAVG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 426 FRVVL-----MYRFEEELFlrSLQDyKIQSALLV--PTLFSFFAKSTLI--DKYDLSNLHEIASGGAPLSKE----VGEA 492
Cdd:cd05943 316 ATIVLydgspFYPDTNALW--DLAD-EEGITVFGtsAKYLDALEKAGLKpaETHDLSSLRTILSTGSPLKPEsfdyVYDH 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 493 VAKRFHLPGIRQGyglTETTSAILIT-PEGDDKPGAVGKVVPFFEAKVVDlDTGKTLgVNQRGEL-CVRG-PMIMSGYVN 569
Cdd:cd05943 393 IKPDVLLASISGG---TDIISCFVGGnPLLPVYRGEIQCRGLGMAVEAFD-EEGKPV-WGEKGELvCTKPfPSMPVGFWN 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 570 NPEAT---NALIDK-DG-WLHsGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAG 644
Cdd:cd05943 468 DPDGSryrAAYFAKyPGvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGD 546
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 645 ELPAAVVVLEHGKTMTEkEIVDYVASQVTTAKKLR---GGVVFVDEVPKGLTGkldarKIREILIK 707
Cdd:cd05943 547 ERVILFVKLREGVELDD-ELRKRIRSTIRSALSPRhvpAKIIAVPDIPRTLSG-----KKVEVAVK 606
|
|
| Ubl_PLICs |
cd01808 |
ubiquitin-like (Ubl) domain found in eukaryotic protein linking integrin-associated protein ... |
93-162 |
2.77e-10 |
|
ubiquitin-like (Ubl) domain found in eukaryotic protein linking integrin-associated protein (IAP, also known as CD47) with cytoskeleton (PLIC) proteins; The PLIC proteins (or ubiquilins) family contains human homologs of the yeast ubiquitin-like (Ubl) Dsk2 protein, PLIC-1 (also termed ubiquilin-1), PLIC-2 (also termed ubiquilin-2, or Chap1), PLIC-3 (also termed ubiquilin-3) and PLIC-4 (also termed ubiquilin-4, ataxin-1 interacting ubiquitin-like protein, A1Up, connexin43-interacting protein of 75 kDa, or CIP75), and mouse PLIC proteins. They are ubiquitin (Ub)-binding adaptor proteins involved in all protein degradation pathways through delivering ubiquitinated substrates to proteasomes. They also promote autophagy-dependent cell survival during nutrient starvation. PLIC-1 regulates the function of the thrombospondin receptor CD47 and G protein signaling. It plays a role in TLR4-mediated signaling through interacting with the Toll/interleukin-1 receptor (TIR) domain of TLR4. It also inhibits the TLR3-Trif antiviral pathway by reducing the abundance of Trif. Moreover, PLIC-1 binds to gamma-aminobutyric acid receptors (GABAARs) and modulates the Ub-dependent, proteasomal degradation of GABAARs. Furthermore, PLIC-1 acts as a molecular chaperone regulating amyloid precursor protein (APP) biosynthesis, trafficking, and degradation by stimulating K63-linked polyubiquitination of lysine 688 in the APP intracellular domain. In addition, PLIC-1 is involved in the protein aggregation-stress pathway via associating with the Ub-interacting motif (UIM) proteins ataxin 3, HSJ1a, and epidermal growth factor substrate 15 (EPS15). PLIC-2 is a protein that binds the ATPase domain of the HSP70-like Stch protein. It functions as a negative regulator of G protein-coupled receptor (GPCR) endocytosis. It also involved in amyotrophic lateral sclerosis (ALS)-related dementia. PLIC-3 is encoded by UbiquilinN3, a testis-specific gene. It shows high sequence similarity with the Xenopus protein XDRP1, a nuclear phosphoprotein that binds to the N-terminus of cyclin A and inhibits Ca2+-induced degradation of cyclin A, but not cyclin B. PLIC-4 is an ubiquitin-like (Ubl) nuclear protein that interacts with ataxin-1 and further links ataxin-1 with the chaperone and Ub-proteasome pathways. It also binds to the non-ubiquitinated gap junction protein connexin43 (Cx43) and regulates the turnover of Cx43 through the proteasomal pathway. PLIC proteins contain an N-terminal Ubl domain that is responsible for the binding of Ub-interacting motifs (UIMs) expressed by proteasomes and endocytic adaptors, and C-terminal Ub-associated (UBA) domain that interacts with Ub chains present on proteins destined for proteasomal degradation. In addition, mammalian PLIC2 proteins have an extra collagen-like motif region, which is absent in other PLIC proteins and the yeast Dsk2 protein.
Pssm-ID: 340506 [Multi-domain] Cd Length: 73 Bit Score: 56.87 E-value: 2.77e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 93 IFVKTLTGKTiTLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd01808 5 VTVKTPKEKE-DFEVPEDSSVKEFKEEISKKFKAPVEQLVLIFAGKILKDQDTLSQHGIKDGLTVHLVIK 73
|
|
| Ubl_UHRF |
cd01797 |
ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing ... |
93-162 |
3.17e-10 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing proteins, UHRF1 and UHRF2, and similar proteins; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma, gastric cancer, esophageal squamous cell carcinoma, colorectal cancer, prostate cancer, and breast cancer. UHRF1 can acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) through interacting with HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (Ubl), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a set- and ring-associated (SRA) domain, and a C-terminal RING finger.
Pssm-ID: 340495 Cd Length: 74 Bit Score: 56.61 E-value: 3.17e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 93 IFVKTLTG-KTITLEVEPSDT-IENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd01797 3 IQVRTMDGkKEARVDGLSKLTkIEDLRERIEEKFDVEPELQRLFYRGKQLEDGHTLFDYDVGLNDIIQLMVR 74
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
92-151 |
3.87e-10 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 62.22 E-value: 3.87e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEG---IPPDQQRLIFAGRQLEDGRTLSDYNI 151
Cdd:TIGR00601 2 TLTFKTLQQQKFKIDMEPDETVKELKEKIEAEQGkdaYPVAQQKLIYSGKILSDDKTVKEYKI 64
|
|
| Ubl1_OASL |
cd01811 |
ubiquitin-like (Ubl) domain 1 found in 2'-5'-oligoadenylate synthase-like protein (OASL) and ... |
92-160 |
4.02e-10 |
|
ubiquitin-like (Ubl) domain 1 found in 2'-5'-oligoadenylate synthase-like protein (OASL) and similar proteins; OASL, also termed 2'-5'-OAS-related protein (2'-5'-OAS-RP), or 59 kDa 2'-5'-oligoadenylate synthase-like protein, or thyroid receptor-interacting protein 14, or TR-interacting protein 14 (TRIP-14), or p59 OASL (p59OASL), is an interferon (IFN)-induced antiviral protein that plays an important role in the IFNs-mediated antiviral signaling pathway. It inhibits respiratory syncytial virus replication and is targeted by the viral nonstructural protein 1 (NS1). It also displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L. Moreover, OASL does not have 2'-5'-OAS activity, but can bind double-stranded RNA (dsRNA) to enhance RIG-I signaling. OASL belongs to the 2'-5' oligoadenylate synthase (OAS) family. While each member of this family has a conserved N-terminal OAS catalytic domain, only OASL has two tandem C-terminal ubiquitin-like (Ubl) repeats, which is required for its antiviral activity. This family corresponds to the first Ubl domain.
Pssm-ID: 340509 Cd Length: 75 Bit Score: 56.56 E-value: 4.02e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIF--AGR---QLEDGRTLSDYNIQKESTLHLV 160
Cdd:cd01811 2 QVTVKQLGGKSLTLWVNPYDPIWQLKEEIEKEWCIPIYQQRLSFqePGGerqVLRNDKTLADYGIFYDTTILLL 75
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
287-702 |
6.33e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.45 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 287 SQPTVVFVSKKGLQKILNVQKKLPIIQK--IIIMDSKTDYQGfqsmytfvtshlppgfneYDFVPESFDRDKtIALIMNS 364
Cdd:PRK12476 141 AEPTVVLTTTAAAEAVEGFLRNLPRLRRprVIAIDAIPDSAG------------------ESFVPVELDTDD-VSHLQYT 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 365 SGSTGLPKGVALPHRTACVRFSHArdPIFGNQIIPDTAILSVVPFHHGFG----MFTTLgyliCGFRVVLM--------- 431
Cdd:PRK12476 202 SGSTRPPVGVEITHRAVGTNLVQM--ILSIDLLDRNTHGVSWLPLYHDMGlsmiGFPAV----YGGHSTLMsptafvrrp 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 432 YRFEEELFLRSLQDYKIQSAllvPTL-FSFFAKSTLI---DKYDLSNLHEIaSGGAPLSKEVGEAVAKRFH---LP--GI 502
Cdd:PRK12476 276 QRWIKALSEGSRTGRVVTAA---PNFaYEWAAQRGLPaegDDIDLSNVVLI-IGSEPVSIDAVTTFNKAFApygLPrtAF 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 503 RQGYGLTETT------------SAILITPEG----------DDKPGAV-----GKVVPFFEAKVVDLDTGKTLGVNQRGE 555
Cdd:PRK12476 352 KPSYGIAEATlfvatiapdaepSVVYLDREQlgagravrvaADAPNAVahvscGQVARSQWAVIVDPDTGAELPDGEVGE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 556 LCVRGPMIMSGYVNNPEAT-----NAL-------------IDKDGWLHSGDIAYWDEDEhFFIVDRLKSLIKYKGYQVAP 617
Cdd:PRK12476 432 IWLHGDNIGRGYWGRPEETertfgAKLqsrlaegshadgaADDGTWLRTGDLGVYLDGE-LYITGRIADLIVIDGRNHYP 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 618 AELESILLQHPNIFDAG-VAG--LPDDDAGELpaaVVVLEH--GKTMTE-KEIVDYVASQVTTAKKLR-GGVVFVDE--V 688
Cdd:PRK12476 511 QDIEATVAEASPMVRRGyVTAftVPAEDNERL---VIVAERaaGTSRADpAPAIDAIRAAVSRRHGLAvADVRLVPAgaI 587
|
490
....*....|....
gi 1886431185 689 PKGLTGKLDARKIR 702
Cdd:PRK12476 588 PRTTSGKLARRACR 601
|
|
| Ubl_UBTD1 |
cd17120 |
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein 1 (UBTD1); UBTD1 is ... |
95-161 |
8.25e-09 |
|
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein 1 (UBTD1); UBTD1 is the mammalian homolog of the mitochondrial Dc-UbP/UBTD2 protein, both of which contain an N-terminal ubiquitin binding domain (UBD) and a C-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. UBTD1 stably interacts with the UBE2D family of E2 ubiquitin conjugating enzymes. As a tumor suppressor, UBTD1 plays a pivotal role in in regulating cellular senescence that mediates p53 function. It is also involved in MDM2 ubiquitination and degradation.
Pssm-ID: 340640 Cd Length: 69 Bit Score: 52.63 E-value: 8.25e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886431185 95 VKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVL 161
Cdd:cd17120 3 VRLSTGKDVRLSASMSDTIGQLKKQLHAQEGIEPSWQRWFFSGKLLTDKTRLQETKIQKDFVIQVIV 69
|
|
| Ubl_UHRF1 |
cd17122 |
ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing ... |
93-162 |
1.06e-08 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing protein 1(UHRF1); UHRF1, also termed inverted CCAAT box-binding protein of 90 kDa, or nuclear protein 95, or nuclear zinc finger protein Np95 (Np95), or RING finger protein 106, or transcription factor ICBP90, or E3 ubiquitin-protein ligase UHRF1, is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma, gastric cancer, esophageal squamous cell carcinoma, colorectal cancer, prostate cancer, and breast cancer. UHRF1 can acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21.Moreover, UHRF1-dependent repression of factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination ofTIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF1 contains an N-terminal ubiquitin-like domain (Ubl), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET and RING finger associated (SRA) domain, and a C-terminal RING-finger domain. It specifically binds to hemimethylated DNA, double-stranded CpG dinucleotides, and recruits the maintenance methyltransferase DNMT1 to its hemimethylated DNA substrate through its SRA domain. UHRF1-dependent H3K23 ubiquitination has an essential role in maintenance DNA methylation and replication. The tandem Tudor domain directs UHRF1 binding to the heterochromatin mark histone H3K9me3 and the PHD finger targets UHRF1 to unmodified histone H3 in euchromatic regions. The RING-finger domain exhibits both autocatalytic E3 ubiquitin (Ub) ligase activity and activity against histone H3 and DNMT1.
Pssm-ID: 340642 Cd Length: 74 Bit Score: 52.57 E-value: 1.06e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 93 IFVKTLTGK-TITLEVEPSDT-IENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd17122 3 IQVRTMDGKeTHRIDSLSKLTkVEELRQKIQELFGVEPERQRLFYRGKQMEDGHTLFDYSVGLNDIVQLLVR 74
|
|
| Ubl_USP48 |
cd01795 |
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ... |
99-193 |
2.07e-08 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.
Pssm-ID: 340493 [Multi-domain] Cd Length: 99 Bit Score: 52.29 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 99 TGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGR-TLSDYNIQKESTLHL-VLRLRGGMEDAKNIKKg 176
Cdd:cd01795 4 RGERKSLTVSSTTTLKELKLQIMEKFSVAPFDQHLYFNGRELTDDSaTLADLGILPGDVLYLkVDEPPDDPDDADEADV- 82
|
90
....*....|....*..
gi 1886431185 177 PAPFYPlEDGTAGEQLH 193
Cdd:cd01795 83 SRARVP-EEGFKGTALL 98
|
|
| Ubl1_FAF1 |
cd17129 |
ubiquitin-like (Ubl) domain 1 found in FAS-associated factor 1 (FAF1) and similar proteins; ... |
101-160 |
4.05e-08 |
|
ubiquitin-like (Ubl) domain 1 found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also termed UBX domain-containing protein 12 (UBXD12), or UBX domain-containing protein 3A (UBXN3A), belongs to the UBXD family of proteins that contains the ubiquitin (Ub) regulatory domain X (UBX) with a beta-grasp ubiquitin-like (Ubl) fold, but without the C-terminal double glycine motif. The UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, FAF1 contains two tandem Ubl domains, which show high structural similarity with the UBX domain. FAF1 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The FAF1-p97 complex inhibits the proteasomal protein degradation in which p97 acts as a co-chaperone. Moreover, FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. The family corresponds to the first Ubl domain.
Pssm-ID: 340649 Cd Length: 73 Bit Score: 50.72 E-value: 4.05e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 101 KTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI-FAGRQLEDGRTLSDYNIQKESTLHLV 160
Cdd:cd17129 11 RTIDVVLPDTETVGDIKQILENELGIPPCKQILKgWKARTVSDSTVLRSLHLPKENSLYLL 71
|
|
| Ubl_midnolin |
cd01804 |
ubiquitin-like (Ubl) domain found in midnolin and similar proteins; Midnolin, also termed ... |
91-160 |
4.08e-08 |
|
ubiquitin-like (Ubl) domain found in midnolin and similar proteins; Midnolin, also termed midbrain nucleolar protein, is a nucleolar protein that may be involved in regulation of genes related to neurogenesis in the nucleolus. It is strongly expressed at the mesencephalon (midbrain) of the embryo in day 12.5 (E12.5) mice and its expression is developmentally regulated. Midnolin plays a role in cellular signaling of adult tissues and regulates glucokinase enzyme activity in pancreatic beta cells. It can also control development via regulation of mRNA transport in cells. Midnolin contains an N-terminal conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.
Pssm-ID: 340502 Cd Length: 70 Bit Score: 50.73 E-value: 4.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 91 WQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGrTLSDYNIQKESTLHLV 160
Cdd:cd01804 1 INLYIHPTTGGRFELSVPPNETVEGLKRRISKKLKVPKERITLLHKEKQLKDG-TLRENGIGDGSKLTLL 69
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
512-704 |
4.16e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 56.44 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 TSAILITP---EGDDKPGAVgkVVPFFEAKVVDLD-TGKTLGVNQRGELCVRG--PMIMSGYVNNPE--ATNALIDKDGW 583
Cdd:PLN02654 437 TGGFMITPlpgAWPQKPGSA--TFPFFGVQPVIVDeKGKEIEGECSGYLCVKKswPGAFRTLYGDHEryETTYFKPFAGY 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 584 LHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLPDDDAGELPAAVVVLEHGKTMTEke 663
Cdd:PLN02654 515 YFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSE-- 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1886431185 664 ivDYVASQVTTAKKLRGGVVFVDEV------PKGLTGKLDARKIREI 704
Cdd:PLN02654 593 --ELRKSLILTVRNQIGAFAAPDKIhwapglPKTRSGKIMRRILRKI 637
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
181-700 |
6.31e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 56.21 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 181 YPLEDGTAGEQLHKAMKRyalVPGTIAFTDAHIEVdiTYAEYFEMSVRLAEAMKRYGLNTNHRIVVCSENSLQFFMPVLG 260
Cdd:PRK10252 453 VEIPETTLSALVAQQAAK---TPDAPALADARYQF--SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 261 ALFIGVAVAPANDIYNERELLNSMGISQPTVVFVSKkglqkilNVQKKLPIIQKIIImdsktdyqgfqsmYTFVTSHLPP 340
Cdd:PRK10252 528 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA-------DQLPRFADVPDLTS-------------LCYNAPLAPQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 341 gfneyDFVPESFDRDKTIALIMNSSGSTGLPKGVALPHRTACVRFSHARD--PIFGNQII----PDTAILSVVPFHHGFg 414
Cdd:PRK10252 588 -----GAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNhyPLTADDVVlqktPCSFDVSVWEFFWPF- 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 415 mfttlgylICGFRVVLM----YRFEEELfLRSLQDYKIQSALLVPTLFSFFAKSTLID--KYDLSNLHEIASGGAPLSKE 488
Cdd:PRK10252 662 --------IAGAKLVMAepeaHRDPLAM-QQFFAEYGVTTTHFVPSMLAAFVASLTPEgaRQSCASLRQVFCSGEALPAD 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 489 VGEAVAKRFHLPgIRQGYGLTEttSAILIT--P-EGDDKPGAVGKVVPF-FEA-----KVVDlDTGKTLGVNQRGELCVR 559
Cdd:PRK10252 733 LCREWQQLTGAP-LHNLYGPTE--AAVDVSwyPaFGEELAAVRGSSVPIgYPVwntglRILD-ARMRPVPPGVAGDLYLT 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 560 GPMIMSGYVNNPEATNALIDKDGWL------HSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDA 633
Cdd:PRK10252 809 GIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQA 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 634 GVaglpdddagelpAAVVVLEHGKTM-TEKEIVDYVASQ-------VTTAKKLRGG-------VVFV--DEVPKGLTGKL 696
Cdd:PRK10252 889 VT------------HACVINQAAATGgDARQLVGYLVSQsglpldtSALQAQLRERlpphmvpVVLLqlDQLPLSANGKL 956
|
....
gi 1886431185 697 DaRK 700
Cdd:PRK10252 957 D-RK 959
|
|
| Ubl_UBTD2 |
cd17121 |
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein 2 (UBTD2); UBTD2, ... |
92-161 |
8.40e-08 |
|
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein 2 (UBTD2); UBTD2, also termed dendritic cell-derived ubiquitin-like protein (DC-UbP), or ubiquitin-like protein SB72, is a potential ubiquitin shuttle protein firstly identified in dendritic cells and implicated in apoptosis. It binds proteins involved in the ubiquitination pathway and may play an important role in regulating protein ubiquitination and delivery of ubiquitinated substrates in eukaryotic cells. UBTD2 is expressed in tumor cells but not in normal human adult tissue suggesting a role in tumorogenesis. It can potentially regulate the stability of proteins involved in various physiological processes relevant to many disease phenotypes, such as ageing and cancer. UBTD2 reconciles protein ubiquitination and deubiquitination via linking UbE1 and USP5 enzymes.
Pssm-ID: 340641 Cd Length: 75 Bit Score: 49.97 E-value: 8.40e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLHLVL 161
Cdd:cd17121 3 QLRLRLSTGKDLKLAVRSTDTVYHMKRRLHTAEGVEPGSQRWFFSGRPLTDKMKLEELKIPKDYVVQVIV 72
|
|
| Ubl_HR23A |
cd17126 |
ubiquitin-like (Ubl) domain found in UV excision repair protein RAD23 homolog A (HR23A); HR23A, ... |
92-155 |
1.42e-07 |
|
ubiquitin-like (Ubl) domain found in UV excision repair protein RAD23 homolog A (HR23A); HR23A, also termed RAD23A, is a DNA repair protein that binds to 19S subunit of the 26S proteasome and shuttles ubiquitinated proteins to the proteasome for degradation, which is required for efficient nucleotide excision repair (NER), a primary mechanism for removing UV-induced DNA lesions. HR23A also plays a critical role in the interaction of HIV-1 viral protein R (Vpr) with the proteasome, especially facilitating Vpr to promote protein poly-ubiquitination. HR23A contains an N-terminal ubiquitin-like (Ubl) domain that binds proteasomes and two C-terminal ubiquitin-associated (UBA) domains that bind ubiquitin or multi-ubiquitinated substrates. In addition, it has a XPC protein-binding domain that might be necessary for its efficient NER function.
Pssm-ID: 340646 Cd Length: 76 Bit Score: 49.29 E-value: 1.42e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQD---KEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKES 155
Cdd:cd17126 2 TITLKTLQQQTFKIRMEPDETVKVLKEKIEAekgRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKN 68
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
440-702 |
4.22e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 52.84 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 440 LRSLQDYKiQSALL-VPTlfsfFAKsTLIDK-----YDLSNLH-EIAS-GGAPLSKEVGEAVAKRFHLPgIRQGYGLTET 511
Cdd:COG1541 168 LRLMQDFG-PTVLVgTPS----YLL-YLAEVaeeegIDPRDLSlKKGIfGGEPWSEEMRKEIEERWGIK-AYDIYGLTEV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 512 TSAILItpEGDDKPGAVgkvvpFFE----AKVVDLDTGKTLGVNQRGELCVrgpmimsgyvnnpeaTNalIDKDGW---- 583
Cdd:COG1541 241 GPGVAY--ECEAQDGLH-----IWEdhflVEIIDPETGEPVPEGEEGELVV---------------TT--LTKEAMplir 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 584 LHSGDIAYWDEDE---------HFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpdDDAGELPAAVVVLE 654
Cdd:COG1541 297 YRTGDLTRLLPEPcpcgrthprIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVV--DREGGLDELTVRVE 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 655 HGKTMTEKEIVDYVASQVTTAKKLRGGVVFVDevPKGL---TGKldARKIR 702
Cdd:COG1541 375 LAPGASLEALAEAIAAALKAVLGLRAEVELVE--PGSLprsEGK--AKRVI 421
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
359-699 |
4.39e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.63 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 359 ALIMNSSGSTGLPKGVALPHRTACVrfsHARDPI--FGNQiiPDTAILSVVPFHHGFGMFTTLGYLICGFRVVLMYR--F 434
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAM---HCQAVIerFGMR--ADDCELHFYSINFDAASERLLVPLLCGARVVLRAQgqW 2410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 435 EEELFLRSLQDYKIQSALLVPTLFSFFAKsTLIDKYDLSNLHEIASGGAPLSKEvgeavakrfHLPGIRQ---------G 505
Cdd:PRK05691 2411 GAEEICQLIREQQVSILGFTPSYGSQLAQ-WLAGQGEQLPVRMCITGGEALTGE---------HLQRIRQafapqlffnA 2480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 506 YGLTETTSAILITPEGDDKP-GA----VGKVVPFFEAKVVDLD-----TGKTlgvnqrGELCVRGPMIMSGY-------- 567
Cdd:PRK05691 2481 YGPTETVVMPLACLAPEQLEeGAasvpIGRVVGARVAYILDADlalvpQGAT------GELYVGGAGLAQGYhdrpglta 2554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 568 ---VNNPEATNAlidkdGWLH-SGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQHPNIFDAGVAGLpDDDA 643
Cdd:PRK05691 2555 erfVADPFAADG-----GRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPS 2628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 644 GelpaavvvlehgktmteKEIVDYVASQVTTAK-----KLRGGV-----------------VFVDEVPKGLTGKLDAR 699
Cdd:PRK05691 2629 G-----------------KQLAGYLVSAVAGQDdeaqaALREALkahlkqqlpdymvpahlILLDSLPLTANGKLDRR 2689
|
|
| Ubl_HOIL1 |
cd01799 |
ubiquitin-like (Ubl) domain found in heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1) and ... |
102-160 |
5.95e-07 |
|
ubiquitin-like (Ubl) domain found in heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1) and similar proteins; HOIL-1, also termed RBCK1, or HOIL-1L, or RanBP-type and C3HC4-type zinc finger-containing protein 1, HBV-associated factor 4, or Hepatitis B virus X-associated protein 4, or RING finger protein 54 (RNF54), or ubiquitin-conjugating enzyme 7-interacting protein 3, or UbcM4-interacting protein 28 (UIP28), together with E3 ubiquitin-protein ligase RNF31 (also known as HOIP) and SHANK-associated RH domain interacting protein (SHARPIN), forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis through conjugation of linear polyubiquitin chains to NF-kappaB essential modulator (also known as NEMO or IKBKG). HOIL-1 plays a crucial role in TNF-alpha-mediated NF-kappaB activation. It also functions as an ubiquitin-protein ligase E3 that interacts with not only PKCbeta but also PKCzeta. It can recognize heme-oxidized IRP2 (iron regulatory protein2) and is thought to affect the turnover of oxidatively damaged proteins. HOIL-1 contains an N-terminal ubiqutin-like (UBL) domain and an Npl4 zinc-finger (NZF) domain, which regulate the interaction with the LUBAC subunit RNF31 and ubiquitin, respectively. The NZF domain belongs to RanBP2-type zinc finger (zf-RanBP2) domain superfamily. In addition, HOIL-1 has a RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain use an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction.
Pssm-ID: 340497 Cd Length: 81 Bit Score: 47.59 E-value: 5.95e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 102 TITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKEST---LHLV 160
Cdd:cd01799 18 PITLKVRPHTTIASLKRQIFLEYGFPPSVQRWIIGKRLATDDETLLSYGIKDSGDpafLYLV 79
|
|
| Ubl_HR23B |
cd16126 |
ubiquitin-like (Ubl) domain found in UV excision repair protein RAD23 homolog B (HR23B); HR23B, ... |
92-155 |
6.20e-07 |
|
ubiquitin-like (Ubl) domain found in UV excision repair protein RAD23 homolog B (HR23B); HR23B, also termed xeroderma pigmentosum group C (XPC) repair-complementing complex 58 kDa protein (p58), is tightly complexed with XPC protein to form the XPC-HR23B complex. Although it displays a high affinity for both single- and double-stranded DNA, the XPC-HR23B complex functions as a global genome repair (GGR)-specific repair factor that is specifically involved in global genome but not transcription-coupled nucleotide excision repair (NER). HR23B also interacts specifically with S5a subunit of the human 26S proteasome, and plays an important role in shuttling ubiquitinated cargo proteins to the proteasome. HR23B contains an N-terminal ubiquitin-like (Ubl) domain that binds proteasomes and two C-terminal ubiquitin-associated (UBA) domains that bind ubiquitin or multi-ubiquitinated substrates. In addition, it has a XPC protein-binding domain that might be necessary for its efficient NER function.
Pssm-ID: 340543 Cd Length: 78 Bit Score: 47.41 E-value: 6.20e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886431185 92 QIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEG---IPPDQQRLIFAGRQLEDGRTLSDYNIQKES 155
Cdd:cd16126 2 QITLKTLQQQTFKIDIDPEETVKALKEKIESEKGkdaFPVAGQKLIYAGKILNDDTALKEYKIDEKN 68
|
|
| Ubl_NUB1 |
cd17062 |
ubiquitin-like (Ubl) domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, ... |
103-163 |
2.70e-06 |
|
ubiquitin-like (Ubl) domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also termed negative regulator of ubiquitin-like proteins 1, or renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1), which may function in the regulation of cell cycle progression. NUB1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif.
Pssm-ID: 340582 Cd Length: 78 Bit Score: 45.59 E-value: 2.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 103 ITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYNIQKESTLhLVLRL 163
Cdd:cd17062 19 ITLETSLDITGSELREKIAEELGVPEDRIKLISNGKVLKDEKTLAEQGVKNNSQV-MVLVL 78
|
|
| Ubl_ElonginB |
cd01788 |
ubiquitin-like (Ubl) domain found in transcription elongation factor B (Elongin B) and similar ... |
101-168 |
4.53e-06 |
|
ubiquitin-like (Ubl) domain found in transcription elongation factor B (Elongin B) and similar proteins; Elongin B, also termed Elongin 18 kDa subunit, or EloB, or RNA polymerase II transcription factor SIII subunit B (SIII p18), is part of an E3 ubiquitin ligase complex called VEC that activates ubiquitination by the E2 ubiquitin-conjugating enzyme Ubc5. VEC is composed of von Hippel-Lindau tumor suppressor protein (pVHL), elongin C, cullin 2, NEDD8, and Rbx1. ElonginB binds elonginC to form the elonginBC complex which is a positive regulator of RNA polymerase II elongation factor Elongin A. The BC complex then binds VHL (von Hippel-Lindau) tumor suppressor protein to form a VCB ternary complex. Elongin B has a ubiquitin-like (Ubl) domain. Ub has a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair.
Pssm-ID: 340486 Cd Length: 101 Bit Score: 45.75 E-value: 4.53e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 101 KTITLEVEPSDTIENVKAKIqdkEGI---PPDQQRLIFAGRQLEDGRTLSDYNI-------QKESTLHLVLRLRGGME 168
Cdd:cd01788 11 TTIFTDAKESTTVFELKKII---EGIlkrPPEDQRLYKDDQLLDDTKTLGDCGFtsqtaraQAPATLGLAFRADGEFE 85
|
|
| Ubl1_ANKUB1 |
cd17050 |
ubiquitin-like (Ubl) domain 1 found in Ankyrin repeat and ubiquitin domain-containing 1 ... |
93-162 |
5.05e-06 |
|
ubiquitin-like (Ubl) domain 1 found in Ankyrin repeat and ubiquitin domain-containing 1 (ANKUB1) and similar proteins; ANKUB1 is an uncharacterized protein with two tandem ubiquitin-like (Ubl) domains located at the N-terminal of Ankyrin repeats (ANK). The Ubl domain may have an adaptor role in ubiquitin (Ub)-signaling by mediating protein-protein interaction. Ubl proteins have a beta-grasp Ubl fold and attach to other proteins in a Ubl manner with biochemically distinct roles. The ankyrin repeats have been identified in numerous proteins with diverse functions. The family corresponds to the first Ubl domain.
Pssm-ID: 340570 Cd Length: 79 Bit Score: 44.98 E-value: 5.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886431185 93 IFVkTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQR-------LIFAGRQLEDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd17050 3 IFV-AFEGEREPLDVSPGQTVGDVKEMIRDKFHIDLSDGKqgrkflvLTYAGADLQDSWVLSDIGIPPGSTIRCLLR 78
|
|
| Ubl_TMUB1_like |
cd17057 |
ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing ... |
106-162 |
5.38e-06 |
|
ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing proteins TMUB1, TMUB2, and similar proteins; TMUB1, also termed dendritic cell-derived ubiquitin-like protein (DULP), or hepatocyte odd protein shuttling protein, or ubiquitin-like protein SB144, or HOPS, is highly expressed in the nervous system. It is involved in the termination of liver regeneration and plays a negative role in interleukin-6-induced hepatocyte proliferation. The overexpression of Tmub1 has been shown to play a role in the inhibition of cell proliferation. TMUB1 has been implicated in the regulation of locomotor activity and wakefulness in mice, perhaps acting through its interaction with CAMLG. It also facilitates the recycling of AMPA receptors into synaptic membrane in cultured primary neurons. TMUB1 contains transmembrane domains and a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold. TMUB2 is an uncharacterized transmembrane domain and Ubl domain-containing protein that shows high sequence similarity to TMUB1.
Pssm-ID: 340577 Cd Length: 74 Bit Score: 44.52 E-value: 5.38e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 106 EVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQL-EDGRTLSDYNIQKESTLHLVLR 162
Cdd:cd17057 17 YARPEDTVGDFKRRHFPDELAQGKRVRLIYQGQLLrDDSRTLSSYGIQDGSVIHCHIS 74
|
|
| Ubl_HERP |
cd01790 |
ubiquitin-like (Ubl) domain found in homocysteine-inducible endoplasmic reticulum stress ... |
104-160 |
1.18e-05 |
|
ubiquitin-like (Ubl) domain found in homocysteine-inducible endoplasmic reticulum stress protein HERP; HERP is an endoplasmic reticulum (ER) integral membrane protein containing an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold. The Ubl domain is required for the degradation of HERP itself as well as for HERP-mediated anti-apoptotic effects. HERP is induced by the ER stress response pathway and is involved in improving the balance of folding capacity and protein loads in the ER. There are two types of HERP, HERP1 and HERP2, which are encoded by the HERPUD1 and HERPUD2 genes, respectively.
Pssm-ID: 340488 Cd Length: 78 Bit Score: 43.78 E-value: 1.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886431185 104 TLEVEPSDTIENVKAKIQDK-EGIP-PDQQRLIFAGRQLEDGRTLSDYNIQKES----TLHLV 160
Cdd:cd01790 16 TVNCTLGWTVLKLKEHLSEVyPSKPlPEDQKLIYSGKLLEDHQTLKDVLREDDPeqvhTVHLV 78
|
|
| Ubl_MUBs_plant |
cd01814 |
ubiquitin-like (Ubl) domain found in plant membrane-anchored ubiquitin-fold proteins (MUBs); ... |
108-164 |
3.20e-05 |
|
ubiquitin-like (Ubl) domain found in plant membrane-anchored ubiquitin-fold proteins (MUBs); The plant MUBs belong to a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation. They may serve as docking site to facilitate the association of specific E2s to the plasma membrane. MUBs contain a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold.
Pssm-ID: 340512 Cd Length: 89 Bit Score: 43.14 E-value: 3.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 108 EPSDTIENVKAKI-----QDKEGIP--PDQQRLIFAGRQLEDGRTLSDYN-IQKES-----TLHLVLRLR 164
Cdd:cd01814 20 SSATTVATLKEKViaewpKDKENGPksINDVKLIYAGKVLENGKTLADSRtPGKVPpggviTMHVVVRPP 89
|
|
| Ubl_UBLCP1 |
cd01813 |
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ... |
100-152 |
8.42e-05 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) and similar proteins; UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. It is localized in the nucleus and it contains conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which directly interacts with the proteasome. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. UBLCP1 may also play a role in the regulation of phosphorylation state of RNA polymerase II C-terminal domain, a key event during mRNA metabolism.
Pssm-ID: 340511 Cd Length: 74 Bit Score: 41.40 E-value: 8.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886431185 100 GKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI---FAGRQLEDGRTLSDYNIQ 152
Cdd:cd01813 9 GKEYPVTVLSSDTVLDLKQRIFELTGVLPKRQKLLglkVKGKPADDDVKLSSLKLK 64
|
|
| Ubl_UBFD1 |
cd17047 |
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ... |
101-160 |
1.65e-04 |
|
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator.
Pssm-ID: 340567 Cd Length: 70 Bit Score: 40.31 E-value: 1.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 101 KTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGrQLEDGRTLSDYNIQKESTLHLV 160
Cdd:cd17047 10 EKYDVKFPLDSTIAELKEHIETLTGVPPAMQKLMYKG-LLKDDKTLRELKVTKGAKVMVV 68
|
|
| Ubiquitin_2 |
pfam14560 |
Ubiquitin-like domain; This entry contains ubiquitin-like domains. |
109-160 |
2.12e-04 |
|
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
Pssm-ID: 405277 Cd Length: 83 Bit Score: 40.59 E-value: 2.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 109 PSDTIENVKAKIQDKEGIPPDQQRL-------IFAGRQLEDGRTLSDYNIQKESTLHLV 160
Cdd:pfam14560 21 KSLTIEELKEKLELITGTPPSSMRLqlyddddNLVAKLDDDDALLGSYGVRDGMRIHVI 79
|
|
| Ubl_TBK1_like |
cd12219 |
ubiquitin-like (Ubl) domain found in non-canonical Inhibitor of kappa B kinases IKKepsilon and ... |
97-155 |
2.64e-04 |
|
ubiquitin-like (Ubl) domain found in non-canonical Inhibitor of kappa B kinases IKKepsilon and TBK1, and similar proteins; IKKepsilon and TBK1 (TRAF family member-associated NF-kappaB activator-binding kinase 1) are non-canonical members of IKK family. They have been characterized as activators of nuclear factor-kappaB (NF-kappaB), but they are not essential for NF-kappaB activation. They play critical roles in antiviral response via phosphorylation and activation of transcription factors IRF3, IRF7, STAT1 and STAT3. They are also involved in the survival, tumorigenesis and development of various cancers. Both IKKepsilon and TBK1 contain an N-terminal protein kinase domain followed a ubiquitin-like (Ubl) domain. The Ubl domain acts as a protein-protein interaction domain, and has been implicated in regulating kinase activity, which modulates interactions in the interferon pathway.
Pssm-ID: 340518 Cd Length: 77 Bit Score: 39.91 E-value: 2.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886431185 97 TLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLED--GRTLSDYNIQKES 155
Cdd:cd12219 9 VSTCELLKIYLDPTETLAEFQELIAEQTEIPAKNQLLLFEGQLLEEevTLPVSDYPKTTEE 69
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
554-700 |
4.76e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 554 GELCVRGPMIMSGYVNNPEAT-NALIDK------DGWLHSGDIAYWDEDEHFFIVDRLKSLIKYKGYQVAPAELESILLQ 626
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTaLAFVPHpfgapgERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE 4146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886431185 627 HPNIFDAGVA---GLPDDD-AGELPAAVVVLEHG------KTMTEKEIVDYVASQvttakklrgGVVFVDEVPKGLTGKL 696
Cdd:PRK05691 4147 QAEVREAAVAvqeGVNGKHlVGYLVPHQTVLAQGalleriKQRLRAELPDYMVPL---------HWLWLDRLPLNANGKL 4217
|
....
gi 1886431185 697 DaRK 700
Cdd:PRK05691 4218 D-RK 4220
|
|
| Ubl_TECR_like |
cd01801 |
ubiquitin-like (Ubl) domain found in trans-2,3-enoyl-CoA reductase (TECR) and similar proteins; ... |
92-157 |
5.57e-04 |
|
ubiquitin-like (Ubl) domain found in trans-2,3-enoyl-CoA reductase (TECR) and similar proteins; This family includes TECR and many TECR-like proteins, such as TECRL. TECR, also termed very-long-chain enoyl-CoA reductase, or synaptic glycoprotein SC2, or TER, or GPSN2, is a synaptic glycoprotein that catalyzes the fourth reaction in the synthesis of very long-chain fatty acids (VLCFA) which is the reduction step of the microsomal fatty acyl-elongation process. Diseases involving perturbations to normal synthesis and degradation of VLCFA (e.g. adrenoleukodystrophy and Zellweger syndrome) have significant neurological consequences. The mammalian TECR P182L mutation causes nonsyndromic mental retardation. Deletion of the yeast TECR (TSC13) homolog is lethal. TECR contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal catalytic domain. TECRL, also termed steroid 5-alpha-reductase 2-like 2 protein (SRD5A2L2), is associated with life-threatening inherited arrhythmias displaying features of both long QT syndrome (LQTS) and catecholaminergic polymorphic ventricular tachycardia (CPVT). Both TECR and TECRL contain an N-terminal Ubl domain with a beta-grasp Ubl fold, and a C-terminal catalytic domain.
Pssm-ID: 340499 [Multi-domain] Cd Length: 77 Bit Score: 39.19 E-value: 5.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 92 QIFVKTLTGKT--ITLEVEPSDTIENVKAKI-QDKEGIPPDQQRL---IFAGRQLEDGRTLSDYNIQKESTL 157
Cdd:cd01801 1 KIEVVSRKGGKqiITLEVSSSATVADLKKAIhKKKKKLYPERQRLrleVPKGKVLKDDKTLSSYGVKDGSTL 72
|
|
| Ubl_TBCB |
cd01789 |
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor B (TBCB) and similar proteins; ... |
109-160 |
7.23e-04 |
|
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor B (TBCB) and similar proteins; TBCB, also termed cytoskeleton-associated protein 1, or cytoskeleton-associated protein CKAPI, or tubulin-specific chaperone B, is one of protein cofactors A through E that is required for the folding of tubulins prior to their incorporation into microtubules and heterodimer assembly. TBCB comprises an N-terminal ubiquitin-like (Ubl) domain and a C-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain. The Ubl domain of TBCB is essential for proper folding and assembly of tubulin alpha. It has a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. TBC-A through E are necessary for the biogenesis of microtubules and for cell viability.
Pssm-ID: 340487 Cd Length: 80 Bit Score: 38.70 E-value: 7.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 109 PSDTIENVKAKIQDKEGIPPDQQRL-------IFAGRQLEDGRTLSDYNIQKESTLHLV 160
Cdd:cd01789 21 LSLTIGELKEKLELITGTPPSSMKLqlydedgKLIGTLDDDDALLGSYPVRDGMRIHVV 79
|
|
| Ubl_BAG1 |
cd01812 |
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ... |
103-160 |
8.81e-04 |
|
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain.
Pssm-ID: 340510 [Multi-domain] Cd Length: 77 Bit Score: 38.41 E-value: 8.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 103 ITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQL-EDGRTLSDYNIQKESTLHLV 160
Cdd:cd01812 16 LPSQDEDEPTLQDLAEAIEEVTGVPVENQKLIFKGKSLkDPEQPLSALGVKNGSKIMLI 74
|
|
| Ubl_AtNPL4_like |
cd17055 |
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, ... |
105-159 |
1.01e-03 |
|
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana NPL4-like proteins NPL4-1, NPL4-2, and similar proteins; The family includes a group of uncharacterized plant ubiquitin-like (Ubl) domain-containing proteins, including Arabidopsis thaliana NPL4-like protein 1 and NPL4-like protein 2.
Pssm-ID: 340575 Cd Length: 73 Bit Score: 38.35 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1886431185 105 LEVEPSDTIENVKAKIQDKEGIPPDQQRL-IFAGRQL---EDGRTLSDYNIQKESTLHL 159
Cdd:cd17055 14 VEVPDDATVGDLKEKIAEQLSVPVSDQTLsLDPGPDLltaKSSATLSQLGLKHGDMVFL 72
|
|
| Rad60-SLD_2 |
pfam13881 |
Ubiquitin-2 like Rad60 SUMO-like; |
108-162 |
1.80e-03 |
|
Ubiquitin-2 like Rad60 SUMO-like;
Pssm-ID: 372780 Cd Length: 111 Bit Score: 38.44 E-value: 1.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886431185 108 EPSDTIENVKAKI-----QDKEGIPPDQQ--RLIFAGRQLEDGRTLSDYNI------QKESTLHLVLR 162
Cdd:pfam13881 21 SPATTVADLKEKViaqwpKDKENGPKTVNdvKLINAGKILENNKTLGECRLpvgetpGGVTTMHVVVR 88
|
|
| Ubl_UBL7 |
cd01815 |
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 7 (UBL7) and similar proteins; ... |
128-162 |
3.32e-03 |
|
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 7 (UBL7) and similar proteins; UBL7, also termed bone marrow stromal cell ubiquitin-like (Ubl)protein (BMSC-UbP), or ubiquitin-like protein SB132, is a novel Ubl protein that may play roles in regulation of bone marrow stromal cell (BMSC) function or cell differentiation via an evocator-associated and cell-specific pattern. UBL7 contains an N-terminal Ubl domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-associated (UBA) domain. The Ubl domain interacts with 26S proteasome-dependent degradation, and the UBA domain links cellular processes and the ubiquitin system.
Pssm-ID: 340513 Cd Length: 92 Bit Score: 37.53 E-value: 3.32e-03
10 20 30
....*....|....*....|....*....|....*
gi 1886431185 128 PDQQRLIFAGRQLEDGRTLSDYNIQKESTLHlVLR 162
Cdd:cd01815 52 PELIDLIYCGRKLKDDQTLDFYGIQSGSTIH-VLR 85
|
|
| Ubl_IKKA_like |
cd17046 |
ubiquitin-like (Ubl) domain found in inhibitor of nuclear factor kappa-B kinases, IKK-alpha ... |
99-149 |
7.31e-03 |
|
ubiquitin-like (Ubl) domain found in inhibitor of nuclear factor kappa-B kinases, IKK-alpha and IKK-beta, and similar proteins; IKK, also termed IkappaB kinase, is an enzyme complex involved in propagating the cellular response to inflammation. It is part of the upstream nuclear factor kappa-B kinase (NF-kappaB) signal transduction cascade, and plays an important role in regulating the NF-kappaB transcription factor. IKK is composed of three subunits, IKK-alpha/CHUK, IKK-beta/IKBKB, and IKK-gamma/NEMO. The IKK-alpha and IKK-beta subunits together are catalytically active whereas the IKK-gamma subunit serves a regulatory function. IKK-alpha and IKK-beta phosphorylate the IkappaB proteins, marking them for degradation via ubiquitination and allowing NF-kappaB transcription factors to go into the nucleus. IKK-alpha, also known as IKK-A, or IkappaB kinase A (IkBKA), or conserved helix-loop-helix ubiquitous kinase (CHUK), or I-kappa-B kinase 1 (IKK1), or nuclear factor NF-kappa-B inhibitor kinase alpha (NFKBIKA), or transcription factor 16 (TCF-16), belongs to the serine/threonine protein kinase family. In addition to NF-kappaB response, it has many additional cellular targets in an NF-kappaB-independent manner. For instance, it plays a role in epidermal differentiation, as well as in the regulation of the cell cycle protein cyclin D1. IKK-beta, also known as IKK-B, or IkappaB kinase B (IkBKB), or I-kappa-B kinase 2 (IKK2), or nuclear factor NF-kappa-B inhibitor kinase beta (NFKBIKB), belongs to the serine/threonine protein kinase family as well. It interacts with many different protein partners and has been implicated in the treatment of many inflammatory diseases and cancers. Both IKK-alpha and IKK-beta contain an N-terminal catalytic domain followed by a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.
Pssm-ID: 340566 Cd Length: 75 Bit Score: 35.69 E-value: 7.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1886431185 99 TGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFA-GRQLEDGRTLSDY 149
Cdd:cd17046 10 TYRILSYEVTEDTSLSTLQSWIERDTGIPVEDQELLLPtGVSLDPEKPASQC 61
|
|
| |
