|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
7-538 |
0e+00 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 1077.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 7 IMHGPPPFYPLEDGTAGEQLHKAMKRYAQVPGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSL 86
Cdd:cd17642 1 IIVGPGPFYPLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 87 QFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVILDSREDYMGKQSMYS 166
Cdd:cd17642 81 QFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 167 FIESHLPAGFNEYDYIPDSFDRETATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVFGNQIIPDTAILTVIPFHHG 246
Cdd:cd17642 161 FITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 247 FGMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEA 326
Cdd:cd17642 241 FGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 327 VAKRFKLPGIRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPE 406
Cdd:cd17642 321 VAKRFKLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 407 ATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVV 486
Cdd:cd17642 401 ATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 52631875 487 LEEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDARKIREI 538
Cdd:cd17642 481 LEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
41-530 |
0e+00 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 617.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 41 AFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSI 120
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 121 SQPTIVFCSKRALQKILGVQKKLPIIQKIVILDSREDYMGKQSMYSFIEShlpaGFNEYDYIPDSFDRETATALIMNSSG 200
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTL----GEEDEDLPPPLKDGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 201 STGLPKGVELTHKNICVRFSHCRDPVFGNqIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDY 280
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLSQVQTFLYGN-DGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 281 KIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIITPEGDDKPG 360
Cdd:cd05911 236 KITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 361 ACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKS 440
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 441 LIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVD 520
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVFVD 475
|
490
....*....|
gi 52631875 521 EVPKGLTGKI 530
Cdd:cd05911 476 EIPKSASGKI 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
34-530 |
4.19e-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: 450.53 E-value: 4.19e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 34 AQVPGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGlGLQHH-IAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNER 112
Cdd:cd05904 16 SAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRG-GRKGDvVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 113 ELYNSLSISQPTIVFCSKRALQKILGVQkklpiiQKIVILDSREDYMGKQSMYSFIESHLPAgfneydyiPDSFDRETAT 192
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELAEKLASLA------LPVVLLDSAEFDSLSFSDLLFEADEAEP--------PVVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNIC--VRFSHcrdPVFGNQIIPDTAILTVIPFHH--GFGMFTtLGYLTCGFRIVLMYRC 268
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLIamVAQFV---AGEGSNSDSEDVFLCVLPMFHiyGLSSFA-LGLLRLGATVVVMPRF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETT-- 346
Cdd:cd05904 237 DLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTgv 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 347 SAIIITPEGDD-KPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAY 425
Cdd:cd05904 317 VAMCFAPEKDRaKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 426 YDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQ 505
Cdd:cd05904 397 IDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQ 476
|
490 500
....*....|....*....|....*
gi 52631875 506 VTASKRLRgGVKFVDEVPKGLTGKI 530
Cdd:cd05904 477 VAPYKKVR-KVAFVDAIPKSPSGKI 500
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
23-539 |
4.47e-125 |
|
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: 374.15 E-value: 4.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 23 GEQLHKAMKRYaqvPGTIAFTDAhaEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGV 102
Cdd:COG0318 2 ADLLRRAAARH---PDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 103 APTNDIYNERELYNSLSISQPTIVFcskralqkilgvqkklpiiqkivildsredymgkqsmysfieshlpagfneydyi 182
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALV------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 183 pdsfdretaTALIMNSSGSTGLPKGVELTHKNICvrfSHCRDPVFGNQIIPDTAILTVIPFHHGFGM-FTTLGYLTCGFR 261
Cdd:COG0318 102 ---------TALILYTSGTTGRPKGVMLTHRNLL---ANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGAT 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 262 IVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYG 341
Cdd:COG0318 170 LVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVR-IVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 342 LTETTSAIIITPE--GDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLH 419
Cdd:COG0318 249 LTETSPVVTVNPEdpGERRPGSVGRPLPGVEVRIVD-EDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 420 SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVM 499
Cdd:COG0318 327 TGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELR 406
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 52631875 500 DYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREIL 539
Cdd:COG0318 407 AFLRERLARYKVPR-RVEFVDELPRTASGKIDRRALRERY 445
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
32-542 |
3.42e-120 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 364.69 E-value: 3.42e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 32 RYAQVPGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNE 111
Cdd:PLN02246 32 RLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 112 RELYNSLSISQPTIVFCSKRALQKILGVQKKLPIiqKIVILDSRED-YMGKQSMYSFIESHLPagfnEYDYIPDSfdret 190
Cdd:PLN02246 112 AEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGV--TVVTIDDPPEgCLHFSELTQADENELP----EVEISPDD----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 191 ATALIMnSSGSTGLPKGVELTHKNICVRFSHCRD---PVFGnqIIPDTAILTVIPFHHGFGMFTTLgylTCGFR----IV 263
Cdd:PLN02246 181 VVALPY-SSGTTGLPKGVMLTHKGLVTSVAQQVDgenPNLY--FHSDDVILCVLPMFHIYSLNSVL---LCGLRvgaaIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 264 LMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVakRFKLPG--IRQGYG 341
Cdd:PLN02246 255 IMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAF--RAKLPNavLGQGYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 342 LTETTSAIII------TPEgDDKPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKD 415
Cdd:PLN02246 333 MTEAGPVLAMclafakEPF-PVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 416 GWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTE 495
Cdd:PLN02246 412 GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITE 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 52631875 496 QEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREILMMG 542
Cdd:PLN02246 492 DEIKQFVAKQVVFYKRIH-KVFFVDSIPKAPSGKILRKDLRAKLAAG 537
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
192-531 |
2.18e-113 |
|
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: 340.03 E-value: 2.18e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVFGNqiiPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEE 271
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT---EGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 272 LFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTETTSAIII 351
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 352 TP--EGDDKPGACGKVVPFFSAKIVDLDTGkTLGVNQRGELCVKGPMIMKGYVNNPEATSAlIDKDGWLHSGDIAYYDKD 429
Cdd:cd04433 158 GPpdDDARKPGSVGRPVPGVEVRIVDPDGG-ELPPGEIGELVVRGPSVMKGYWNNPEATAA-VDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 430 GHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTAS 509
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPY 315
|
330 340
....*....|....*....|..
gi 52631875 510 KRLRgGVKFVDEVPKGLTGKID 531
Cdd:cd04433 316 KVPR-RVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
48-536 |
5.63e-108 |
|
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: 330.68 E-value: 5.63e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 48 EVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVF 127
Cdd:cd05936 22 GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 128 CSkRALQKILGVQKKLPIIQKIvildSREDymgkqsmysfieshlpagfneydyipdsfdretaTALIMNSSGSTGLPKG 207
Cdd:cd05936 102 VA-VSFTDLLAAGAPLGERVAL----TPED----------------------------------VAVLQYTSGTTGVPKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 208 VELTHKNICVRFSHCRDpVFGNQIIPDTAILTVIPFHHGFGMftTLGYLTC---GFRIVLMYRCEEELFLRSLQDYKIQS 284
Cdd:cd05936 143 AMLTHRNLVANALQIKA-WLEDLLEGDDVVLAALPLFHVFGL--TVALLLPlalGATIVLIPRFRPIGVLKEIRKHRVTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 285 ALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTETTSAIIITP-EGDDKPGACG 363
Cdd:cd05936 220 FPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVP-IVEGYGLTETSPVVAVNPlDGPRKPGSIG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 364 KVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIK 443
Cdd:cd05936 299 IPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMII 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 444 YKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVP 523
Cdd:cd05936 377 VGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPR-QVEFRDELP 455
|
490
....*....|...
gi 52631875 524 KGLTGKIDARKIR 536
Cdd:cd05936 456 KSAVGKILRRELR 468
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
11-546 |
3.30e-93 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 295.35 E-value: 3.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 11 PPPFYPlEDGTAGEQLHKAMKRYAQvpgTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFM 90
Cdd:PLN02330 20 PSVPVP-DKLTLPDFVLQDAELYAD---KVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 91 PVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQkkLPIIqkivildsredYMGKQSMYSFI-- 168
Cdd:PLN02330 96 VALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLG--LPVI-----------VLGEEKIEGAVnw 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 169 ESHLPAGfneyDYIPDSFDRE----TATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfGNQIIPDTAILTVIPFH 244
Cdd:PLN02330 163 KELLEAA----DRAGDTSDNEeilqTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSV-GPEMIGQVVTLGLIPFF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 245 HGFGMF-TTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNL--HEIASGGAPLAK 321
Cdd:PLN02330 238 HIYGITgICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLAP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 322 EVGEAVAKRFKLPGIRQGYGLTETtSAIIIT---PE---GDDKPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGP 395
Cdd:PLN02330 318 ELLTAFEAKFPGVQVQEAYGLTEH-SCITLThgdPEkghGIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 396 MIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDP 475
Cdd:PLN02330 397 CVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52631875 476 DAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREilMMGKKSK 546
Cdd:PLN02330 477 EAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVR-VVQFVDSIPKSLSGKIMRRLLKE--KMLSINK 544
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
51-537 |
6.58e-93 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 293.63 E-value: 6.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSK 130
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 131 RALQKILGVQKKLPIIQKIVILDSREDYMGKQSMYSFiESHLPAGFNEYDYIPdsFDrETATALIMNSSGSTGLPKGVEL 210
Cdd:PRK06187 112 EFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEY-EELLAAASDTFDFPD--ID-ENDAAAMLYTSGTTGHPKGVVL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 211 THKNIcvrFSHCRDPVFGNQIIPDTAILTVIP-FH-HGFGmfttLGYLT--CGFRIVLMYRCEEELFLRSLQDYKIQSAL 286
Cdd:PRK06187 188 SHRNL---FLHSLAVCAWLKLSRDDVYLVIVPmFHvHAWG----LPYLAlmAGAKQVIPRRFDPENLLDLIETERVTFFF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 287 LVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLpGIRQGYGLTETTSAIIITPEGDD------KPG 360
Cdd:PRK06187 261 AVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGI-DLVQGYGMTETSPVVSVLPPEDQlpgqwtKRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 361 ACGKVVPFFSAKIVDLDtGKTLGVNQR--GELCVKGPMIMKGYVNNPEATSALIDkDGWLHSGDIAYYDKDGHFFIVDRL 438
Cdd:PRK06187 340 SAGRPLPGVEARIVDDD-GDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 439 KSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKF 518
Cdd:PRK06187 418 KDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPK-RIAF 496
|
490
....*....|....*....
gi 52631875 519 VDEVPKGLTGKIDARKIRE 537
Cdd:PRK06187 497 VDELPRTSVGKILKRVLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
26-531 |
1.34e-91 |
|
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: 287.58 E-value: 1.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 26 LHKAMKRYaqvPGTIAFTDAhaEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPT 105
Cdd:cd17631 1 LRRRARRH---PDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 106 NDIYNERELYNSLSISQPTIVFcskralqkilgvqkklpiiqkivildsrEDYmgkqsmysfieshlpagfneydyipds 185
Cdd:cd17631 76 NFRLTPPEVAYILADSGAKVLF----------------------------DDL--------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 186 fdretatALIMNSSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHHGFGM-FTTLGYLTCGFRIVL 264
Cdd:cd17631 101 -------ALLMYTSGTTGRPKGAMLTHRNL---LWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 265 MYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAkevgEAVAKRFKLPGIR--QGYGL 342
Cdd:cd17631 171 LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMP----ERLLRALQARGVKfvQGYGM 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 343 TETTSAIIITPEGD--DKPGACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHS 420
Cdd:cd17631 247 TETSPGVTFLSPEDhrRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 421 GDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMD 500
Cdd:cd17631 325 GDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIA 404
|
490 500 510
....*....|....*....|....*....|.
gi 52631875 501 YVAGQVTASKRLRgGVKFVDEVPKGLTGKID 531
Cdd:cd17631 405 HCRERLARYKIPK-SVEFVDALPRNATGKIL 434
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
34-445 |
1.05e-89 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 281.89 E-value: 1.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 34 AQVPGTIAFTDAHAEvNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERE 113
Cdd:pfam00501 6 ARTPDKTALEVGEGR-RLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 114 LYNSLSISQPTIVFCSKRA-LQKILGVQKKLPIIQKIVILDSREDYMGKqsmysfiESHLPAGFNEYDYIPDSFDRETAT 192
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEE-------PLPEEAKPADVPPPPPPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNI------CVRFSHCRDPVFgnqiiPDTAILTVIPFHHGFGM-FTTLGYLTCGFRIVLM 265
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHRNLvanvlsIKRVRPRGFGLG-----PDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 ---YRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKlPGIRQGYGL 342
Cdd:pfam00501 233 pgfPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 343 TETTSAIIITPEGDDK---PGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLH 419
Cdd:pfam00501 312 TETTGVVTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYR 391
|
410 420
....*....|....*....|....*.
gi 52631875 420 SGDIAYYDKDGHFFIVDRLKSLIKYK 445
Cdd:pfam00501 392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
37-547 |
1.13e-86 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 278.65 E-value: 1.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 37 PGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGlGLQHH--IAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNEREL 114
Cdd:PLN02574 53 NGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVM-GVRQGdvVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 115 YNSLSISQPTIVFCSKRALQKI--LGVqkklPIIQKIVILDSREDYMGKQSMYSFIEShlpagfnEYDYIPDSFDRETAT 192
Cdd:PLN02574 132 KKRVVDCSVGLAFTSPENVEKLspLGV----PVIGVPENYDFDSKRIEFPKFYELIKE-------DFDFVPKPVIKQDDV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNIC------VRFSHCRDPVFGNqiipDTAILTVIPFHH--GFGMFTTlGYLTCGFRIVL 264
Cdd:PLN02574 201 AAIMYSSGTTGASKGVVLTHRNLIamvelfVRFEASQYEYPGS----DNVYLAALPMFHiyGLSLFVV-GLLSLGSTIVV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 265 MYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTL-VDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLT 343
Cdd:PLN02574 276 MRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 344 ETTSAII--ITPEGDDKPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSG 421
Cdd:PLN02574 356 ESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 422 DIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDY 501
Cdd:PLN02574 436 DIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINY 515
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 52631875 502 VAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREILMMGKKSKL 547
Cdd:PLN02574 516 VAKQVAPYKKVR-KVVFVQSIPKSPAGKILRRELKRSLTNSVSSRL 560
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
24-537 |
4.02e-85 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 272.93 E-value: 4.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 24 EQLHKAMKRYaqvPGTIAFTDAhaEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVA 103
Cdd:PRK07656 9 ELLARAARRF---GDKEAYVFG--DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 104 PTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVILDSREDYMGKQSMYSFiESHLPAGFNEYDYIP 183
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTF-TDFLAAGDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 184 DsfdRETATALIMNSSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHHGFGMftTLGYLTC---GF 260
Cdd:PRK07656 163 V---DPDDVADILFTSGTTGRPKGAMLTHRQL---LSNAADWAEYLGLTEGDRYLAANPFFHVFGY--KAGVNAPlmrGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 261 RIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGY 340
Cdd:PRK07656 235 TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 341 GLTETTSAIIITPEGDDK---PGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGW 417
Cdd:PRK07656 315 GLSEASGVTTFNRLDDDRktvAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 418 LHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQE 497
Cdd:PRK07656 394 LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 52631875 498 VMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK07656 474 LIAYCREHLAKYKVPR-SIEFLDELPKNATGKVLKRALRE 512
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
51-533 |
7.43e-82 |
|
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: 262.03 E-value: 7.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVfcsk 130
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 131 ralqkilgvqkklpiiqkiVILDSREDymgkqsmysfieshlpagfneydyipdsfdretaTALIMNSSGSTGLPKGVEL 210
Cdd:cd05935 78 -------------------VVGSELDD----------------------------------LALIPYTSGTTGLPKGCMH 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 211 THKNICVRFSHcrdPVFGNQIIPDTAILTVIPFHHGFGMFTTLGY-LTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVP 289
Cdd:cd05935 105 THFSAAANALQ---SAVWTGLTPSDVILACLPLFHVTGFVGSLNTaVYVGGTYVLMARWDRETALELIEKYKVTFWTNIP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 290 TLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEavaKRFKLPGIR--QGYGLTETTSAIIITPEGDDKPGACGkvVP 367
Cdd:cd05935 182 TMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAE---KLLKLTGLRfvEGYGLTETMSQTHTNPPLRPKLQCLG--IP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 368 FFS--AKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATS-ALIDKDG--WLHSGDIAYYDKDGHFFIVDRLKSLI 442
Cdd:cd05935 257 *FGvdARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEeSFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMI 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 443 KYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTM--TEQEVMDYVAGQVTASKRLRgGVKFVD 520
Cdd:cd05935 337 NVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGkvTEEDIIEWAREQMAAYKYPR-EVEFVD 415
|
490
....*....|...
gi 52631875 521 EVPKGLTGKIDAR 533
Cdd:cd05935 416 ELPRSASGKILWR 428
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
36-537 |
6.94e-80 |
|
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: 258.78 E-value: 6.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 36 VPGTIAFTDAHAevnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELY 115
Cdd:cd05926 3 APALVVPGSTPA---LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 116 NSLSISQPTIVFCSKRALQKILGVQKKLpiiqKIVILDSREDYMGKQSmySFIESHLPAGFNEYDYI-PDSFDRETATAL 194
Cdd:cd05926 80 FYLADLGSKLVLTPKGELGPASRAASKL----GLAILELALDVGVLIR--APSAESLSNLLADKKNAkSEGVPLPDDLAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 195 IMNSSGSTGLPKGVELTHKNICVRFSHCRDpvfGNQIIPDTAILTVIPFHHGFGMFTT-LGYLTCGFRIVLMYRCEEELF 273
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAASATNITN---TYKLTPDDRTLVVMPLFHVHGLVASlLSTLAAGGSVVLPPRFSASTF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 274 LRSLQDYKIQ--SAllVPTLFSFFAKSTLVDKYD-LSNLHEIASGGAPLAKEVGEAVAKRFKLPGIrQGYGLTETTSAII 350
Cdd:cd05926 231 WPDVRDYNATwyTA--VPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEAAHQMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 351 ITP--EGDDKPGACGKVvpfFSAKIVDLD-TGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYD 427
Cdd:cd05926 308 SNPlpPGPRKPGSVGKP---VGVEVRILDeDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 428 KDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVT 507
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLA 464
|
490 500 510
....*....|....*....|....*....|
gi 52631875 508 ASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:cd05926 465 AFKVPK-KVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
31-537 |
4.34e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 255.66 E-value: 4.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 31 KRYAQVPGTIAFTDAhaevnITYSEYFEMACRLAETMKRYgLGLQH--HIAVCSENSLQFFMPVCGALFIGVGVAPTNDI 108
Cdd:PRK08314 21 RRYPDKTAIVFYGRA-----ISYRELLEEAERLAGYLQQE-CGVRKgdRVLLYMQNSPQFVIAYYAILRANAVVVPVNPM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 109 YNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIiqKIVILDSREDYMGKQSMYSF-----IESHLPAGFNEyDYIP 183
Cdd:PRK08314 95 NREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRL--RHVIVAQYSDYLPAEPEIAVpawlrAEPPLQALAPG-GVVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 184 --DSFDRE------TAT----ALIMNSSGSTGLPKGVELTHKNICVRfshcrdpVFGNQI----IPDTAILTVIPFHHGF 247
Cdd:PRK08314 172 wkEALAAGlappphTAGpddlAVLPYTSGTTGVPKGCMHTHRTVMAN-------AVGSVLwsnsTPESVVLAVLPLFHVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 248 GMFTTL-GYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPT-LFSFFAkSTLVDKYDLSNLHEIASGGAPLAkevgE 325
Cdd:PRK08314 245 GMVHSMnAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTmVVDFLA-SPGLAERDLSSLRYIGGGGAAMP----E 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 326 AVAKR-FKLPGIR--QGYGLTETTSAIIITPEGDDKPGACGkvVPFFS--AKIVDLDTGKTLGVNQRGELCVKGPMIMKG 400
Cdd:PRK08314 320 AVAERlKELTGLDyvEGYGLTETMAQTHSNPPDRPKLQCLG--IPTFGvdARVIDPETLEELPPGEVGEIVVHGPQVFKG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 401 YVNNPEATS-ALIDKDG--WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDA 477
Cdd:PRK08314 398 YWNRPEATAeAFIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRR 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52631875 478 GELPAAVVVLEEGK--TMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK08314 478 GETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPR-IVEFVDSLPKSGSGKILWRQLQE 538
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
50-546 |
3.92e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 245.71 E-value: 3.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 50 NITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCS 129
Cdd:PRK06710 49 DITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 130 KRALQKILGVQKKLPIiqKIVILDSREDYMG--KQSMYSFI------------ESHLPAGFNEYDYIPDS-----FDRET 190
Cdd:PRK06710 129 DLVFPRVTNVQSATKI--EHVIVTRIADFLPfpKNLLYPFVqkkqsnlvvkvsESETIHLWNSVEKEVNTgvevpCDPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 191 ATALIMNSSGSTGLPKGVELTHKNICvrfshcRDPVFG-----NQIIPDTAILTVIPFHHGFGMFTTLGY-LTCGFRIVL 264
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLV------SNTLMGvqwlyNCKEGEEVVLGVLPFFHVYGMTAVMNLsIMQGYKMVL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 265 MYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVaKRFKLPGIRQGYGLTE 344
Cdd:PRK06710 281 IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKF-ETVTGGKLVEGYGLTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 345 TTSAIIITPEGDDK-PGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDI 423
Cdd:PRK06710 360 SSPVTHSNFLWEKRvPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 424 AYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEvMDYVA 503
Cdd:PRK06710 439 GYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEE-LNQFA 517
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 52631875 504 GQVTASKRLRGGVKFVDEVPKGLTGKIdarkIREILMMGKKSK 546
Cdd:PRK06710 518 RKYLAAYKVPKVYEFRDELPKTTVGKI----LRRVLIEEEKRK 556
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
51-540 |
7.32e-72 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 239.63 E-value: 7.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFfmPVC--GALFIGVGVAPTNDIYNERELYNSLSISQPTIVFC 128
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA--VIAmlACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 129 SKRAL---------QKILGVQKKLPIIQKIVILDSREDYMGKQSMYSFIEshlpagfnEYDYIPDSFDRE----TATALI 195
Cdd:COG0365 118 ADGGLrggkvidlkEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDE--------LLAAASAEFEPEptdaDDPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 196 MNSSGSTGLPKGVELTHknicvrfshcRDPVfgnqiipdTAILTVIPFHHGFG----MFTT--------LGYLTCG-FRI 262
Cdd:COG0365 190 LYTSGTTGKPKGVVHTH----------GGYL--------VHAATTAKYVLDLKpgdvFWCTadigwatgHSYIVYGpLLN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 263 ---VLMYR-----CEEELFLRSLQDYKIQSALLVPTLFSFFAKS--TLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFK 332
Cdd:COG0365 252 gatVVLYEgrpdfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 333 LPgIRQGYGLTETTSAIIITPEGDD-KPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPM--IMKGYVNNPEAT- 408
Cdd:COG0365 332 VP-IVDGWGQTETGGIFISNLPGLPvKPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYr 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 409 SALIDK-DGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVL 487
Cdd:COG0365 410 ETYFGRfPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVL 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 52631875 488 EEGKTMTE---QEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREILM 540
Cdd:COG0365 490 KPGVEPSDelaKELQAHVREELGPYAYPR-EIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-536 |
9.73e-71 |
|
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: 230.24 E-value: 9.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 199 SGSTGLPKGVELTHKNI---------CVRFShcrdpvfgnqiiPDTAILTVIPFHHGFGMftTLGYLTC---GFRIVLMy 266
Cdd:cd05917 11 SGTTGSPKGATLTHHNIvnngyfigeRLGLT------------EQDRLCIPVPLFHCFGS--VLGVLAClthGATMVFP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 267 rceEELF-----LRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYG 341
Cdd:cd05917 76 ---SPSFdplavLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 342 LTETTSAIIITPEGDD---KPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWL 418
Cdd:cd05917 153 MTETSPVSTQTRTDDSiekRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 419 HSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEV 498
Cdd:cd05917 233 HTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDI 312
|
330 340 350
....*....|....*....|....*....|....*...
gi 52631875 499 MDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:cd05917 313 KAYCKGKIAHYKVPR-YVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
16-538 |
1.40e-68 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 230.85 E-value: 1.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 16 PLEDGTAGEQLHKAMKRYaqvPGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENS-----LQFFM 90
Cdd:PRK08315 12 PLLEQTIGQLLDRTAARY---PDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVpewvlTQFAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 91 PVCGALFIGVgvaptNDIYNERELYNSLSISQPTIVFCSKR--------ALQKI---LGVQ-------KKLPIIQKIVIL 152
Cdd:PRK08315 89 AKIGAILVTI-----NPAYRLSELEYALNQSGCKALIAADGfkdsdyvaMLYELapeLATCepgqlqsARLPELRRVIFL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 153 DSrEDYMGkqsMYSFieSHLPAGFNEYDyiPDSFDRETATaL-------IMNSSGSTGLPKGVELTHKNI---------C 216
Cdd:PRK08315 164 GD-EKHPG---MLNF--DELLALGRAVD--DAELAARQAT-LdpddpinIQYTSGTTGFPKGATLTHRNIlnngyfigeA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 217 VRFSH----CrdpvfgnqiIPdtailtvIPFHHGFGM-FTTLGYLTCGFRIVLMyrceEELF-----LRSLQDYKIQSAL 286
Cdd:PRK08315 235 MKLTEedrlC---------IP-------VPLYHCFGMvLGNLACVTHGATMVYP----GEGFdplatLAAVEEERCTALY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 287 LVPTLF-------SFfakstlvDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIITPEGDD-- 357
Cdd:PRK08315 295 GVPTMFiaeldhpDF-------ARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPle 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 358 -KPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVD 436
Cdd:PRK08315 368 kRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 437 RLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGV 516
Cdd:PRK08315 448 RIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPR-YI 526
|
570 580
....*....|....*....|..
gi 52631875 517 KFVDEVPKGLTGKIDARKIREI 538
Cdd:PRK08315 527 RFVDEFPMTVTGKIQKFKMREM 548
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
18-477 |
7.74e-68 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 229.99 E-value: 7.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 18 EDGTAGEQLHKAMKRYaqvPGTIAFT--DAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGA 95
Cdd:COG1022 9 PADTLPDLLRRRAARF---PDRVALRekEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 96 LFIG---VGVAPTNdiyNERELYNSLSISQPTIVFCSKRA-LQKILGVQKKLPIIQKIVILDSREDYMGKQSMYsfIESH 171
Cdd:COG1022 86 LAAGavtVPIYPTS---SAEEVAYILNDSGAKVLFVEDQEqLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLLS--LDEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 172 LPAGFNEYDyiPDSFDRETA------TALIMNSSGSTGLPKGVELTHKNIC--VRFSHCRDPVFgnqiiPDTAILTVIPF 243
Cdd:COG1022 161 LALGREVAD--PAELEARRAavkpddLATIIYTSGTTGRPKGVMLTHRNLLsnARALLERLPLG-----PGDRTLSFLPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 244 HHGFGMFTTLGYLTCGFRIVLmyrCEE-ELFLRSLQDYKIQSALLVP----------------------TLFSFF----- 295
Cdd:COG1022 234 AHVFERTVSYYALAAGATVAF---AESpDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrKLFRWAlavgr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 296 -----------------AKSTLVDKYDLSNLHE--------IASGGAPLAKEVGeavakRF----KLPgIRQGYGLTETT 346
Cdd:COG1022 311 ryararlagkspslllrLKHALADKLVFSKLREalggrlrfAVSGGAALGPELA-----RFfralGIP-VLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 347 SAIIITPEGDDKPGACGKVVPFFSAKIVDldtgktlgvnqRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYY 426
Cdd:COG1022 385 PVITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGEL 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52631875 427 DKDGHFFIVDRLKSLI-----KYkgyqVPPAELESILLQHPFIFDAGVAG----------IPDPDA 477
Cdd:COG1022 454 DEDGFLRITGRKKDLIvtsggKN----VAPQPIENALKASPLIEQAVVVGdgrpflaaliVPDFEA 515
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
16-538 |
8.41e-68 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 228.89 E-value: 8.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 16 PLEDGTAGEQLHKAMKRYaqvPGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGA 95
Cdd:PRK12583 14 PLLTQTIGDAFDATVARF---PDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 96 LFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSKR--------ALQKILG----------VQKKLPIIQKIVILDSREd 157
Cdd:PRK12583 91 ARIGAILVNINPAYRASELEYALGQSGVRWVICADAfktsdyhaMLQELLPglaegqpgalACERLPELRGVVSLAPAP- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 158 ymgkqsmysfieshlPAGFNEYDYIPDSFDRETATAL--------------IMNSSGSTGLPKGVELTHKNIcvrfshcr 223
Cdd:PRK12583 170 ---------------PPGFLAWHELQARGETVSREALaerqasldrddpinIQYTSGTTGFPKGATLSHHNI-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 224 dpVFGNQIIPDTAILT-------VIPFHHGFGM-FTTLGYLTCGFRIVLmyrcEEELF-----LRSLQDYKIQSALLVPT 290
Cdd:PRK12583 227 --LNNGYFVAESLGLTehdrlcvPVPLYHCFGMvLANLGCMTVGACLVY----PNEAFdplatLQAVEEERCTALYGVPT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 291 LFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIITPEGDDKP---GACGKVVP 367
Cdd:PRK12583 301 MFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLErrvETVGRTQP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 368 FFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGY 447
Cdd:PRK12583 381 HLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 448 QVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLT 527
Cdd:PRK12583 460 NIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPR-YFRFVDEFPMTVT 538
|
570
....*....|.
gi 52631875 528 GKIDARKIREI 538
Cdd:PRK12583 539 GKVQKFRMREI 549
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
48-539 |
1.46e-67 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 226.67 E-value: 1.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 48 EVNITYSEYFEMACRLAETMkRYGLGLQ--HHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTI 125
Cdd:PRK06839 25 EEEMTYKQLHEYVSKVAAYL-IYELNVKkgERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 126 VFCSKRALQKILGVQKKLPIIQKIVILDSREdymgkqsmysfIESHLPAGFNEydyipdsfDRETATALIMNSSGSTGLP 205
Cdd:PRK06839 104 LFVEKTFQNMALSMQKVSYVQRVISITSLKE-----------IEDRKIDNFVE--------KNESASFIICYTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 206 KGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHH--GFGMFTtLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQ 283
Cdd:PRK06839 165 KGAVLTQENM---FWNALNNTFAIDLTMHDRSIVLLPLFHigGIGLFA-FPTLFAGGVIIVPRKFEPTKALSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 284 SALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGirQGYGLTETTSAIIITPEGD--DKPGA 361
Cdd:PRK06839 241 VVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSPTVFMLSEEDarRKVGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 362 CGKVVPFFSAKIVDLDTGKtLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSL 441
Cdd:PRK06839 319 IGKPVLFCDYELIDENKNK-VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 442 IKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRGGVkFVDE 521
Cdd:PRK06839 397 IISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIV-FLKE 475
|
490
....*....|....*...
gi 52631875 522 VPKGLTGKIDARKIREIL 539
Cdd:PRK06839 476 LPKNATGKIQKAQLVNQL 493
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-536 |
2.43e-66 |
|
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: 221.01 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 190 TATALIMNSSGSTGLPKGVELTHKNIC---VRFSHcrdpVFGnqIIPDTAILTVIPFHHGFGMFTT-LGYLTCGFRIVLM 265
Cdd:cd05934 81 VDPASILYTSGTTGPPKGVVITHANLTfagYYSAR----RFG--LGEDDVYLTVLPLFHINAQAVSvLAALSVGATLVLL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 YRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIAsgGAPLAKEVGEAVAKRFKLPgIRQGYGLTET 345
Cdd:cd05934 155 PRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAY--GAPNPPELHEEFEERFGVR-LLEGYGMTET 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 346 TSAIIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVK---GPMIMKGYVNNPEATSALIdKDGWLHSGD 422
Cdd:cd05934 232 IVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGD 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 423 IAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYV 502
Cdd:cd05934 310 LGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFC 389
|
330 340 350
....*....|....*....|....*....|....
gi 52631875 503 AGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:cd05934 390 EGQLAYFKVPR-YIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
10-540 |
8.54e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 223.72 E-value: 8.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 10 GPPPFYPLEDGTAGEQLHKAMKRYAQVPGTIAFTDAhaevnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFF 89
Cdd:PRK05605 22 WTPHDLDYGDTTLVDLYDNAVARFGDRPALDFFGAT-----TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 90 MPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSKRA------------LQKILGVQ--KKLPIIQKIV----- 150
Cdd:PRK05605 97 VAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVaptverlrrttpLETIVSVNmiAAMPLLQRLAlrlpi 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 151 --ILDSREDYMGKQSMYSFIESHLPAGFNEYDYIPDSFDRE-TATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVF 227
Cdd:PRK05605 177 paLRKARAALTGPAPGTVPWETLVDAAIGGDGSDVSHPRPTpDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 228 GnqiIPDTA--ILTVIPFHHGFGMftTLGyLT----CGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLV 301
Cdd:PRK05605 257 G---LGDGPerVLAALPMFHAYGL--TLC-LTlavsIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 302 DKYDLSNLHEIASGGAPLAKEVgeaVAKRFKLPG--IRQGYGLTETTSAIIITPEGDD-KPGACGkvVPFFS--AKIVDL 376
Cdd:PRK05605 331 RGVDLSGVRNAFSGAMALPVST---VELWEKLTGglLVEGYGLTETSPIIVGNPMSDDrRPGYVG--VPFPDteVRIVDP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 377 DT-GKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELE 455
Cdd:PRK05605 406 EDpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 456 SILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRGGVKFvDEVPKGLTGKIDARKI 535
Cdd:PRK05605 485 EVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHV-DELPRDQLGKVRRREV 563
|
....*
gi 52631875 536 REILM 540
Cdd:PRK05605 564 REELL 568
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
52-537 |
2.01e-65 |
|
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: 221.35 E-value: 2.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 52 TYSEYFEMACRLAETMKRYGLGLQHHIAVCSENS-----LQFFMPVCGALFIGVgvaptndiyNERelynsLSISQPT-- 124
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNThrhleLYYAVPGMGAVLHTI---------NPR-----LFPEQIAyi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 125 -------IVFCSKRALQKILGVQKKLPIIQKIVILDSREDYMGKQSM--YSFiESHLPAGFNEYDYiPDsFDrETATALI 195
Cdd:cd12119 93 inhaedrVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVgvLAY-EELLAAESPEYDW-PD-FD-ENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 196 MNSSGSTGLPKGVELTHKNIcvrFSHC-------------RDpvfgnqiipdtAILTVIP-FH-HGFGM-FTTLGyltCG 259
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSL---VLHAmaalltdglglseSD-----------VVLPVVPmFHvNAWGLpYAAAM---VG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 260 FRIVLMYR-CEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPlakeVGEAVAKRFKLPGIR- 337
Cdd:cd12119 232 AKLVLPGPyLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSA----VPRSLIEAFEERGVRv 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 -QGYGLTETT---SAIIITPEGDDKPGAC--------GKVVPFFSAKIVDLDT------GKTlgvnqRGELCVKGPMIMK 399
Cdd:cd12119 308 iHAWGMTETSplgTVARPPSEHSNLSEDEqlalrakqGRPVPGVELRIVDDDGrelpwdGKA-----VGELQVRGPWVTK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 400 GYVNNPEATSALiDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGE 479
Cdd:cd12119 383 SYYKNDEESEAL-TEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGE 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 480 LPAAVVVLEEGKTMTEQEVMDYVAGQVtASKRLRGGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:cd12119 462 RPLAVVVLKEGATVTAEELLEFLADKV-AKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
26-537 |
1.08e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 220.79 E-value: 1.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 26 LHKAMKRYAQVPgtiAFTDAHAevNITYSEYFEMACRLAETmkryglgLQHH--------IAVCSENSLQFFMPVCGALF 97
Cdd:PRK05677 30 LKQSCQRFADKP---AFSNLGK--TLTYGELYKLSGAFAAW-------LQQHtdlkpgdrIAVQLPNVLQYPVAVFGAMR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 98 IGVGVAPTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIiqKIVILDSREDYMG--KQSMYSFIESHL--- 172
Cdd:PRK05677 98 AGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGV--KHVIVTEVADMLPplKRLLINAVVKHVkkm 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 173 -PA-------GFNEY----------DYIPDSFDretaTALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVFGNQIIPD 234
Cdd:PRK05677 176 vPAyhlpqavKFNDAlakgagqpvtEANPQADD----VAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 235 TAILTVIPFHH--GFGMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEI 312
Cdd:PRK05677 252 EILIAPLPLYHiyAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 313 ASGGAPLAKevgeAVAKRFK-LPG--IRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGE 389
Cdd:PRK05677 332 LSGGMALQL----ATAERWKeVTGcaICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID-DDGNELPLGEVGE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 390 LCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGV 469
Cdd:PRK05677 407 LCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAA 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 470 AGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK05677 487 IGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPK-AVEFRDELPTTNVGKILRRELRD 553
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
51-537 |
1.93e-64 |
|
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: 215.67 E-value: 1.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQptivfcsk 130
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 131 ralqkilgvqkklpiiqkiVILDsredymgkqsmysfieshlpagfneydyipdsfdretATALIMNSSGSTGLPKGVEL 210
Cdd:cd05912 74 -------------------VKLD-------------------------------------DIATIMYTSGTTGKPKGVQQ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 211 THKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPT 290
Cdd:cd05912 98 TFGNH---WWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 291 LFSFFAKSTLvDKYDlSNLHEIASGGAPLAKEVGEaVAKRFKLPgIRQGYGLTETTSAII-ITPE-GDDKPGACGKvvPF 368
Cdd:cd05912 175 MLQRLLEILG-EGYP-NNLRCILLGGGPAPKPLLE-QCKEKGIP-VYQSYGMTETCSQIVtLSPEdALNKIGSAGK--PL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 369 FSA--KIVDLDTGKtlgvNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKG 446
Cdd:cd05912 249 FPVelKIEDDGQPP----YEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 447 YQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEegKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGL 526
Cdd:cd05912 324 ENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPK-KIYFVDELPRTA 400
|
490
....*....|.
gi 52631875 527 TGKIDARKIRE 537
Cdd:cd05912 401 SGKLLRHELKQ 411
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
192-536 |
1.07e-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: 214.51 E-value: 1.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKnicVRFSHCRDPVFGNQIIPDTAILTVI-PFHHGFGMFTTLGYLTCGFRIVL--MYRC 268
Cdd:cd05972 83 PALIYFTSGTTGLPKGVLHTHS---YPLGHIPTAAYWLGLRPDDIHWNIAdPGWAKGAWSSFFGPWLLGATVFVyeGPRF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLvDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTETTSA 348
Cdd:cd05972 160 DAERILELLERYGVTSFCGPPTAYRMLIKQDL-SSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 349 IIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVK--GPMIMKGYVNNPEATSALIdKDGWLHSGDIAYY 426
Cdd:cd05972 238 VGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYR 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 427 DKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTE---QEVMDYVA 503
Cdd:cd05972 316 DEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQGHVK 395
|
330 340 350
....*....|....*....|....*....|...
gi 52631875 504 GQVTASKRLRgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:cd05972 396 KVLAPYKYPR-EIEFVEELPKTISGKIRRVELR 427
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
21-537 |
2.36e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 215.95 E-value: 2.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 21 TAGEQLHKAMKRYaqvPGTIAFtdAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGV 100
Cdd:PRK08316 12 TIGDILRRSARRY---PDKTAL--VFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 101 GVAPTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIV--ILDSREDYMGKQSMYSFIEShlpagfnE 178
Cdd:PRK08316 87 VHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILslVLGGREAPGGWLDFADWAEA-------G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 179 YDYIPDSFDRETATALIMNSSGSTGLPKGVELTHKNICVRFSHCrdpVFGNQIIPDTAILTVIPFHHGFGMFTTLG-YLT 257
Cdd:PRK08316 160 SVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSC---IVAGDMSADDIPLHALPLYHCAQLDVFLGpYLY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 258 CGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRfkLPGIR 337
Cdd:PRK08316 237 VGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRER--LPGLR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 --QGYGLTETTS-AIIITP-EGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALId 413
Cdd:PRK08316 315 fyNCYGQTEIAPlATVLGPeEHLRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 414 KDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTM 493
Cdd:PRK08316 393 RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATV 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 52631875 494 TEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK08316 473 TEDELIAHCRARLAGFKVPK-RVIFVDELPRNPSGKILKRELRE 515
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
49-489 |
1.28e-62 |
|
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: 212.07 E-value: 1.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 49 VNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPtndiynereLYNSLSISQPTIVFC 128
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP---------IYPTSSAEQIAYILN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 129 SKRAlqkilgvqkklpiiqKIVILDSREDymgkqsmysfieshlpagfneydyipdsfdretaTALIMNSSGSTGLPKGV 208
Cdd:cd05907 75 DSEA---------------KALFVEDPDD----------------------------------LATIIYTSGTTGRPKGV 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 209 ELTHKNICvrfSHCRDpvfGNQIIPDTA---ILTVIPFHHGFGMFTTLGY-LTCGFRIVLmyrCEEELFLRS-LQDYKIQ 283
Cdd:cd05907 106 MLSHRNIL---SNALA---LAERLPATEgdrHLSFLPLAHVFERRAGLYVpLLAGARIYF---ASSAETLLDdLSEVRPT 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 284 SALLVPTLF-SFFA----------KSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKrFKLPgIRQGYGLTETTSAIIIT 352
Cdd:cd05907 177 VFLAVPRVWeKVYAaikvkavpglKRKLFDLAVGGRLRFAASGGAPLPAELLHFFRA-LGIP-VYEGYGLTETSAVVTLN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 353 PEGDDKPGACGKVVPFFSAKIVDldtgktlgvnqRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHF 432
Cdd:cd05907 255 PPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFL 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 433 FIVDRLKSLIKY-KGYQVPPAELESILLQHPFIFDAGVAGipdpDAGELPAAVVVLEE 489
Cdd:cd05907 324 HITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG----DGRPFLVALIVPDP 377
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
193-537 |
9.41e-61 |
|
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: 206.76 E-value: 9.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTL-GYLTCGFRIVLMYR-CEE 270
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHANL---AANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALlCPLFAGASVEFLPKfDPK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 271 ELFLRSLQDykiQSALL--VPTLFS--------FFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGY 340
Cdd:cd05941 169 EVAISRLMP---SITVFmgVPTIYTrllqyyeaHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHT-LLERY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 341 GLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHS 420
Cdd:cd05941 245 GMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKT 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 421 GDIAYYDKDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGK-TMTEQEV 498
Cdd:cd05941 325 GDLGVVDEDGYYWILGRSSVdIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEEL 404
|
330 340 350
....*....|....*....|....*....|....*....
gi 52631875 499 MDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:cd05941 405 KEWAKQRLAPYKRPR-RLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
11-537 |
1.89e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 208.30 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 11 PPPFYPL-EDGTAGEQLHKAMKRYAQVPgtiAFTDAhaEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFF 89
Cdd:PRK06188 2 ATMADLLhSGATYGHLLVSALKRYPDRP---ALVLG--DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 90 MPVCGALFIG---VGVAPTNDIYNERELYNSLSISqpTIVFCSKRALQKILGVQKKLPIIQKIVILDSREDYMGkqsmys 166
Cdd:PRK06188 77 MAIGAAQLAGlrrTALHPLGSLDDHAYVLEDAGIS--TLIVDPAPFVERALALLARVPSLKHVLTLGPVPDGVD------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 167 fieshLPAGFNEYDYIP-DSFDRETATALIMNSSGSTGLPKGVELTHKNIcvrfshcrdpVFGNQII-------PDTAIL 238
Cdd:PRK06188 149 -----LLAAAAKFGPAPlVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSI----------ATMAQIQlaewewpADPRFL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 239 TVIPFHHGFGMFTTLGYLTCGFrIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSffaksTLVD-----KYDLSNLHEIA 313
Cdd:PRK06188 214 MCTPLSHAGGAFFLPTLLRGGT-VIVLAKFDPAEVLRAIEEQRITATFLVPTMIY-----ALLDhpdlrTRDLSSLETVY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 314 SGGAPLAK-EVGEAVaKRFKlPGIRQGYGLTETTSAIIITPEGDDKP------GACGKVVPFFSAKIVDlDTGKTLGVNQ 386
Cdd:PRK06188 288 YGASPMSPvRLAEAI-ERFG-PIFAQYYGQTEAPMVITYLRKRDHDPddpkrlTSCGRPTPGLRVALLD-EDGREVAQGE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 387 RGELCVKGPMIMKGYVNNPEATsALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFD 466
Cdd:PRK06188 365 VGEICVRGPLVMDGYWNRPEET-AEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQ 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52631875 467 AGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYV---AGQVTASKRlrggVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK06188 444 VAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVkerKGSVHAPKQ----VDFVDSLPLTALGKPDKKALRA 513
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
37-536 |
1.67e-59 |
|
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: 205.30 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 37 PGTIAFTDAHAEvnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYN 116
Cdd:cd05959 18 GDKTAFIDDAGS--LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 117 SLSISQPTIVFCSKRALQKI-LGVQKKLPIIQKIVILDSREDYMGKQSMYSFIESHLPaGFNEYDYIPDSfdretaTALI 195
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLaAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAE-QLKPAATHADD------PAFW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 196 MNSSGSTGLPKGVELTHKNICVRFSHCRDPVFGnqIIPDTAILTVIPFHHGFGMFTTLGY-LTCGFRIVLM-YRCEEELF 273
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYWTAELYARNVLG--IREDDVCFSAAKLFFAYGLGNSLTFpLSVGATTVLMpERPTPAAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 274 LRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTETTSAIIITP 353
Cdd:cd05959 247 FKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD-ILDGIGSTEMLHIFLSNR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 354 EGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFF 433
Cdd:cd05959 326 PGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 434 IVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTE---QEVMDYVAGQVTASK 510
Cdd:cd05959 404 YAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEaleEELKEFVKDRLAPYK 483
|
490 500
....*....|....*....|....*.
gi 52631875 511 RLRgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:cd05959 484 YPR-WIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
30-539 |
4.42e-59 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 203.66 E-value: 4.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 30 MKRYAQVPGTIAFTDAHAEvnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIY 109
Cdd:PRK03640 9 KQRAFLTPDRTAIEFEEKK--VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 110 NERELYNSLSISQPTIVFCSKRALQKILGVQkklpiiqkivildsREDYmgkqsmysfieSHLPAG-FNEYDYIPDSFDR 188
Cdd:PRK03640 87 SREELLWQLDDAEVKCLITDDDFEAKLIPGI--------------SVKF-----------AELMNGpKEEAEIQEEFDLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 189 ETATalIMNSSGSTGLPKGVELTHKNicvRFSHCRDPVFGNQIIPDTAILTVIPFHH--GFG-MFTTLGYltcGFRIVLM 265
Cdd:PRK03640 142 EVAT--IMYTSGTTGKPKGVIQTYGN---HWWSAVGSALNLGLTEDDCWLAAVPIFHisGLSiLMRSVIY---GMRVVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 YRCEEELFLRSLQDYKIQSALLVPTLFSffaksTLVDKYDLSNLHE----IASGGAPLAKEVGEaVAKRFKLPGIrQGYG 341
Cdd:PRK03640 214 EKFDAEKINKLLQTGGVTIISVVSTMLQ-----RLLERLGEGTYPSsfrcMLLGGGPAPKPLLE-QCKEKGIPVY-QSYG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 342 LTETTSAIIITPEGD--DKPGACGKvvPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLH 419
Cdd:PRK03640 287 MTETASQIVTLSPEDalTKLGSAGK--PLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 420 SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEgkTMTEQEVM 499
Cdd:PRK03640 364 TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSG--EVTEEELR 441
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 52631875 500 DYVAGQVtASKRLRGGVKFVDEVPKGLTGKIDARKIREIL 539
Cdd:PRK03640 442 HFCEEKL-AKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
16-530 |
3.19e-58 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 204.80 E-value: 3.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 16 PLEDGTAGEQLHKAMKRYA-QVPGTIA-----FTDAHAE-VNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQF 88
Cdd:PRK07529 17 PLAARDLPASTYELLSRAAaRHPDAPAlsfllDADPLDRpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 89 FMPVCGALFIGVgVAPTNDIYNERELYNSLSISQPTIVFCSK-----RALQKILGVQKKLPIIQKIVILDSREDYMG-KQ 162
Cdd:PRK07529 97 HFALWGGEAAGI-ANPINPLLEPEQIAELLRAAGAKVLVTLGpfpgtDIWQKVAEVLAALPELRTVVEVDLARYLPGpKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 163 SMYSFIESHLPAGFNEYDyipDSFDRETATALIMNSS-------------GSTGLPKGVELTHKNIcVRFSHCRDPVFGN 229
Cdd:PRK07529 176 LAVPLIRRKAHARILDFD---AELARQPGDRLFSGRPigpddvaayfhtgGTTGMPKLAQHTHGNE-VANAWLGALLLGL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 230 QiiPDTAILTVIPFHHGFGMFTT-LGYLTCGFRIVLM----YRCEEEL--FLRSLQDYKIQSALLVPTLFSFFAKsTLVD 302
Cdd:PRK07529 252 G--PGDTVFCGLPLFHVNALLVTgLAPLARGAHVVLAtpqgYRGPGVIanFWKIVERYRINFLSGVPTVYAALLQ-VPVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 303 KYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTETTSAIIITP-EGDDKPGACGKVVPFFSAKIVDLD-TGK 380
Cdd:PRK07529 329 GHDISSLRYALCGAAPLPVEVFRRFEAATGVR-IVEGYGLTEATCVSSVNPpDGERRIGSVGLRLPYQRVRVVILDdAGR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 381 TL---GVNQRGELCVKGPMIMKGYVNNPEATSALIDkDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESI 457
Cdd:PRK07529 408 YLrdcAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLE-DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEA 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52631875 458 LLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKI 530
Cdd:PRK07529 487 LLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAERAAVPKHVRILDALPKTAVGKI 559
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
24-537 |
3.79e-57 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 200.28 E-value: 3.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 24 EQLHKAMKRYAQVPgtiAFTDAhAEVnITYSEYFEMACRLAETMKRyGLGLQH--HIAVCSENSLQFFMPVCGALFIGVG 101
Cdd:PRK08974 27 DMFEQAVARYADQP---AFINM-GEV-MTFRKLEERSRAFAAYLQN-GLGLKKgdRVALMMPNLLQYPIALFGILRAGMI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 102 VAPTNDIYNERELYNSLSIS-QPTIVFCSKRA--LQKILgvqKKLPIiqKIVILDSREDYM--GKQSMYSFI-------- 168
Cdd:PRK08974 101 VVNVNPLYTPRELEHQLNDSgAKAIVIVSNFAhtLEKVV---FKTPV--KHVILTRMGDQLstAKGTLVNFVvkyikrlv 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 169 -ESHLPAG--FNE-------YDYIPDSFDREtATALIMNSSGSTGLPKGVELTHKNICVRFSHCR---DPVF--GNQIIp 233
Cdd:PRK08974 176 pKYHLPDAisFRSalhkgrrMQYVKPELVPE-DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKaayGPLLhpGKELV- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 234 dtaiLTVIPFHHGFG-MFTTLGYLTCGFRIVLMYRCEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHE 311
Cdd:PRK08974 254 ----VTALPLYHIFAlTVNCLLFIELGGQNLLITNPRDiPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 312 IASGGAPlakeVGEAVAKRF-KLPGIR--QGYGLTETTSAIIITPEG-DDKPGACGKVVPFFSAKIVDlDTGKTLGVNQR 387
Cdd:PRK08974 330 SVGGGMA----VQQAVAERWvKLTGQYllEGYGLTECSPLVSVNPYDlDYYSGSIGLPVPSTEIKLVD-DDGNEVPPGEP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 388 GELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDA 467
Cdd:PRK08974 405 GELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52631875 468 GVAGIPDPDAGELPAAVVVLEEgKTMTEQEVMDYVAGQVTASK--RLrggVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK08974 484 AAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKvpKL---VEFRDELPKSNVGKILRRELRD 551
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
13-531 |
8.75e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 199.50 E-value: 8.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 13 PFYPLEDGTAGEQLHKAMKRYAQVPGTIAFtdAHAevnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPV 92
Cdd:PRK06178 26 PEYPHGERPLTEYLRAWARERPQRPAIIFY--GHV---ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 93 CGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFC------------SKRALQKIL--GVQKKLPIIQKIVILDS-RED 157
Cdd:PRK06178 101 FGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLAldqlapvveqvrAETSLRHVIvtSLADVLPAEPTLPLPDSlRAP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 158 YMGKQSMYSFIESHLPAGFNEYDYIPDsFDretATALIMNSSGSTGLPKGVELTHknicvrfshcRDPVF--------GN 229
Cdd:PRK06178 181 RLAAAGAIDLLPALRACTAPVPLPPPA-LD---ALAALNYTGGTTGMPKGCEHTQ----------RDMVYtaaaayavAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 230 QIIPDTAILTVIPFH----HGFGMfttLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQS-ALLVPTLFSFFAKSTLVDkY 304
Cdd:PRK06178 247 VGGEDSVFLSFLPEFwiagENFGL---LFPLFSGATLVLLARWDAVAFMAAVERYRVTRtVMLVDNAVELMDHPRFAE-Y 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 305 DLSNLHEIasGGAPLAKEVGEAVAKRFK-LPG--IRQG-YGLTETTSAIIITP--EGDD-----KPGACGKVVPFFSAKI 373
Cdd:PRK06178 323 DLSSLRQV--RVVSFVKKLNPDYRQRWRaLTGsvLAEAaWGMTETHTCDTFTAgfQDDDfdllsQPVFVGLPVPGTEFKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 374 VDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAE 453
Cdd:PRK06178 401 CDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSE 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 454 LESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRggVKFVDEVPKGLTGKID 531
Cdd:PRK06178 480 VEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE--IRIVDALPMTATGKVR 555
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
21-537 |
1.33e-56 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 198.95 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 21 TAGEQLHKAMKRYAQVPGTIAFTDAhaevnITYSEyfemACRLAETMKRYGLGLQH-----HIAVCSENSLQFFMPVCGA 95
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKT-----ITYRE----ADQLVEQFAAYLLGELQlkkgdRVALMMPNCLQYPIATFGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 96 LFIGVGVAPTNDIYNERELYNSLSISQPTIV-----FCSkrALQKILGvqkKLPIIQkiVILDSREDYMG--KQSMYSFI 168
Cdd:PRK08751 97 LRAGLTVVNVNPLYTPRELKHQLIDSGASVLvvidnFGT--TVQQVIA---DTPVKQ--VITTGLGDMLGfpKAALVNFV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 169 ESHLPAGFNEYdYIPDSFDRETATAL------------------IMNSSGSTGLPKGVELTHKNICVRFSHCRDPVFGNQ 230
Cdd:PRK08751 170 VKYVKKLVPEY-RINGAIRFREALALgrkhsmptlqiepddiafLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 231 IIPD--TAILTVIPFHHGFGM------FTTLGyltcGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVD 302
Cdd:PRK08751 249 KLEEgcEVVITALPLYHIFALtanglvFMKIG----GCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 303 KYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIrQGYGLTETTSAIIITP-EGDDKPGACGKVVPFFSAKIVDlDTGKT 381
Cdd:PRK08751 325 QIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLV-EAYGLTETSPAACINPlTLKEYNGSIGLPIPSTDACIKD-DAGTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 382 LGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQH 461
Cdd:PRK08751 403 LAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52631875 462 PFIFDAGVAGIPDPDAGELpAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK08751 483 PGVLEVAAVGVPDEKSGEI-VKVVIVKKDPALTAEDVKAHARANLTGYKQPR-IIEFRKELPKTNVGKILRRELRD 556
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
40-537 |
2.35e-56 |
|
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: 197.72 E-value: 2.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 40 IAFTDAHAEVNI-TYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSL 118
Cdd:cd05970 36 LVWCDDAGEERIfTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 119 SISQPTIVFC--SKRALQKILGVQKKLPIIQKIVildsredYMGKQSMYSFIESHlpagfNEYDYIPDSFDRETA----- 191
Cdd:cd05970 116 ESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLV-------WVGDPVPEGWIDFR-----KLIKNASPDFERPTAnsypc 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 ---TALIMNSSGSTGLPKGVELTHkniCVRFSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTL-GYLTCGFRIVL--M 265
Cdd:cd05970 184 gedILLVYFSSGTTGMPKMVEHDF---TYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIyGQWIAGAAVFVydY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 YRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLvDKYDLSNLHEIASGGAPLAKEVGEavakRFK-LPGI--RQGYGL 342
Cdd:cd05970 261 DKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLRYCTTAGEALNPEVFN----TFKeKTGIklMEGFGQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 343 TETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDtGKTLGVNQRGELCV----KGPM-IMKGYVNNPEATSALIdKDGW 417
Cdd:cd05970 336 TETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIrtskGKPVgLFGGYYKDAEKTAEVW-HDGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 418 LHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTE-- 495
Cdd:cd05970 414 YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEel 493
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 52631875 496 -QEVMDYVAgQVTASKRLRGGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:cd05970 494 kKELQDHVK-KVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-536 |
8.15e-54 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 188.80 E-value: 8.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNIcvrfshcrdpVFGNQII-------PDTAILTVIPFHHGFGMFTTLGYLTCGFRIVL 264
Cdd:cd05922 119 LALLLYTSGSTGSPKLVRLSHQNL----------LANARSIaeylgitADDRALTVLPLSYDYGLSVLNTHLLRGATLVL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 265 MYRCE-EELFLRSLQDYKIQSALLVPTLFSFFAKSTLvDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLT 343
Cdd:cd05922 189 TNDGVlDDAFWEDLREHGATGLAGVPSTYAMLTRLGF-DPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQT 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 344 ETTSAIIITP--EGDDKPGACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSG 421
Cdd:cd05922 268 EATRRMTYLPpeRILEKPGSIGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTG 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 422 DIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPdAGELPAAVVVLEEGktMTEQEVMDY 501
Cdd:cd05922 347 DLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDK--IDPKDVLRS 423
|
330 340 350
....*....|....*....|....*....|....*
gi 52631875 502 VAGQVTASKrLRGGVKFVDEVPKGLTGKIDARKIR 536
Cdd:cd05922 424 LAERLPPYK-VPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
24-538 |
1.03e-53 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 191.19 E-value: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 24 EQLHKAMKRYAQVPgtiAFTDAHaeVNITYSEYFemacRLAETMKRYglgLQHH--------IAVCSENSLQFFMPVCGA 95
Cdd:PRK12492 28 EVFERSCKKFADRP---AFSNLG--VTLSYAELE----RHSAAFAAY---LQQHtdlvpgdrIAVQMPNVLQYPIAVFGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 96 LFIGVGVAPTNDIYNERELYNSLSISqptivfcSKRAL--QKILG--VQKKLPiiqkivilDSREDYMGKQSMYSFIES- 170
Cdd:PRK12492 96 LRAGLIVVNTNPLYTAREMRHQFKDS-------GARALvyLNMFGklVQEVLP--------DTGIEYLIEAKMGDLLPAa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 171 -------------------HLP--AGFNE---------YDYIPDSFDRetaTALIMNSSGSTGLPKGVELTHKNICVRFS 220
Cdd:PRK12492 161 kgwlvntvvdkvkkmvpayHLPqaVPFKQalrqgrglsLKPVPVGLDD---IAVLQYTGGTTGLAKGAMLTHGNLVANML 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 221 HCRDPVfgNQIIPD---------TAILTVIPFHHGFGmFTT--LGYLTCGFRIVLMYRCEE-ELFLRSLQDYKIQSALLV 288
Cdd:PRK12492 238 QVRACL--SQLGPDgqplmkegqEVMIAPLPLYHIYA-FTAncMCMMVSGNHNVLITNPRDiPGFIKELGKWRFSALLGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 289 PTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKevgeAVAKRFK-LPGIR--QGYGLTETTSAIIITPEGD-DKPGACGK 364
Cdd:PRK12492 315 NTLFVALMDHPGFKDLDFSALKLTNSGGTALVK----ATAERWEqLTGCTivEGYGLTETSPVASTNPYGElARLGTVGI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 365 VVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKY 444
Cdd:PRK12492 391 PVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 445 KGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGkTMTEQEVMDYVAGQVTASKRLRGGVkFVDEVPK 524
Cdd:PRK12492 470 SGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIV-LRDSLPM 547
|
570
....*....|....
gi 52631875 525 GLTGKIDARKIREI 538
Cdd:PRK12492 548 TPVGKILRRELRDI 561
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
51-536 |
1.30e-53 |
|
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: 189.08 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGlQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSK 130
Cdd:cd05909 8 LTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 131 RALQKilGVQKKLPIIQ---KIVIL-DSREDYMGKQSMYSFIESHLPagFNEYDYIPDSFDRETA-TALIMNSSGSTGLP 205
Cdd:cd05909 87 QFIEK--LKLHHLFDVEydaRIVYLeDLRAKISKADKCKAFLAGKFP--PKWLLRIFGVAPVQPDdPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 206 KGVELTHKNICVRFSHCRDPVfgnQIIPDTAILTVIPFHHGFGMFTTLGY-LTCGFRIV-----LMYRCEEELflrsLQD 279
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIF---DPNPEDVVFGALPFFHSFGLTGCLWLpLLSGIKVVfhpnpLDYKKIPEL----IYD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 280 YKIQSALLVPTLFSFFAKStlVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTETTSAIII-TPEGDDK 358
Cdd:cd05909 236 KKATILLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECSPVISVnTPQSPNK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 359 PGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRL 438
Cdd:cd05909 313 EGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 439 KSLIKYKGYQVPPAELESILLQH-PFIFDAGVAGIPDPDAGElpaAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRGGVK 517
Cdd:cd05909 392 SRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE---KIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIH 468
|
490
....*....|....*....
gi 52631875 518 FVDEVPKGLTGKIDARKIR 536
Cdd:cd05909 469 QVEEIPLLGTGKPDYVTLK 487
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-536 |
6.65e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 183.84 E-value: 6.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNIcVRFSHC--RDPVFGnqiiPDTAILTVIPFHHGFGMFTTLGY-LTCGFRIVLM---- 265
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNE-VYNAWMlaLNSLFD----PDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLAgpag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 YRCEEEL--FLRSLQDYKIQSALLVPTLFSffAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLT 343
Cdd:cd05944 80 YRNPGLFdnFWKLVERYRITSLSTVPTVYA--ALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLP-VVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 344 ETTSAIIIT-PEGDDKPGACGKVVPFFSAKIVDLD----TGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDkDGWL 418
Cdd:cd05944 157 EATCLVAVNpPDGPKRPGSVGLRLPYARVRIKVLDgvgrLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVA-DGWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 419 HSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEV 498
Cdd:cd05944 236 NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEEL 315
|
330 340 350
....*....|....*....|....*....|....*...
gi 52631875 499 MDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDARKIR 536
Cdd:cd05944 316 LAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
42-536 |
2.04e-52 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 186.43 E-value: 2.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 42 FTDAHAEVN-ITYSEYFEMACRLAETMkrYGLGLQ--HHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSL 118
Cdd:PRK08008 28 FESSGGVVRrYSYLELNEEINRTANLF--YSLGIRkgDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWIL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 119 SISQPTIVFCSKRALQKILGVQKKLPI-IQKIVILDSREDYMGKQSMYSFIESHLPAGFNEYdyIPDSFDRetaTALIMN 197
Cdd:PRK08008 106 QNSQASLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPADDGVSSFTQLKAQQPATLCYA--PPLSTDD---TAEILF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 198 SSGSTGLPKGVELTHKNIcvRFS-HCRDpvFGNQIIPDTAILTVIP-FHHGFGMFTTLGYLTCGFRIVLMYRCEEELFLR 275
Cdd:PRK08008 181 TSGTTSRPKGVVITHYNL--RFAgYYSA--WQCALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 276 SLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGgAPLAKEVGEAVAKRFklpGIR--QGYGLTETTSAIIITP 353
Cdd:PRK08008 257 QVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMFY-LNLSDQEKDAFEERF---GVRllTSYGMTETIVGIIGDR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 354 EGDDK-------PGACgkvvpfFSAKIVDlDTGKTLGVNQRGELCVKG---PMIMKGYVNNPEATSALIDKDGWLHSGDI 423
Cdd:PRK08008 333 PGDKRrwpsigrPGFC------YEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 424 AYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVA 503
Cdd:PRK08008 406 GYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCE 485
|
490 500 510
....*....|....*....|....*....|...
gi 52631875 504 GQVTASKrLRGGVKFVDEVPKGLTGKIDARKIR 536
Cdd:PRK08008 486 QNMAKFK-VPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
192-530 |
8.39e-52 |
|
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: 180.00 E-value: 8.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfgnQIIPDTAILTVIPFHHGFGMftTLGYLTC---GFRIVLMYRC 268
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCA---DLTEDDRYLIINPFFHTFGY--KAGIVAClltGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSA 348
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 349 IIITPEGD--DKPGACGKVVPFFSAKIVDldtgktlgvnqRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYY 426
Cdd:cd17638 157 TMCRPGDDaeTVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 427 DKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQV 506
Cdd:cd17638 226 DERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERL 305
|
330 340
....*....|....*....|....
gi 52631875 507 TASKRLRgGVKFVDEVPKGLTGKI 530
Cdd:cd17638 306 ANYKVPR-FVRFLDELPRNASGKV 328
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
195-531 |
1.17e-51 |
|
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: 179.39 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 195 IMNSSGSTGLPKGVELTHKN-ICVRFShcRDPVFGnqIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEELF 273
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNlIAANLQ--LIHAMG--LTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 274 LRSLQDYKIqsallvpTLFSFFAK--STLVDK-----YDLSNLHEIASGGAPlakevgeAVAKRF-KLPGIR--QGYGLT 343
Cdd:cd17637 81 LELIEEEKV-------TLMGSFPPilSNLLDAaeksgVDLSSLRHVLGLDAP-------ETIQRFeETTGATfwSLYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 344 ETtSAIIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDI 423
Cdd:cd17637 147 ET-SGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 424 AYYDKDGHFFIVDRL--KSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDY 501
Cdd:cd17637 224 GRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEF 303
|
330 340 350
....*....|....*....|....*....|
gi 52631875 502 VAGQVTASKRLRgGVKFVDEVPKGLTGKID 531
Cdd:cd17637 304 VGSRIARYKKPR-YVVFVEALPKTADGSID 332
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
16-536 |
1.79e-51 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 184.84 E-value: 1.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 16 PLEDGTAGEQLHKAMKRYAQVPGTIAFTDAhaevnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGA 95
Cdd:PRK07059 19 ASQYPSLADLLEESFRQYADRPAFICMGKA-----ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 96 LFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSK---RALQKILGvqkKLPIiqKIVILDSREDYMG-KQSMYSFIESH 171
Cdd:PRK07059 94 LRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLEnfaTTVQQVLA---KTAV--KHVVVASMGDLLGfKGHIVNFVVRR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 172 L----PA-------GFNeyDYIPD----SFDRETAT----ALIMNSSGSTGLPKGVELTHKNIC---VRFSHCRDPVFGN 229
Cdd:PRK07059 169 VkkmvPAwslpghvRFN--DALAEgarqTFKPVKLGpddvAFLQYTGGTTGVSKGATLLHRNIVanvLQMEAWLQPAFEK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 230 QIIPDT-AILTVIPFHHGFGMfTTLGYLT--CGFRIVLMYRCEE-ELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYD 305
Cdd:PRK07059 247 KPRPDQlNFVCALPLYHIFAL-TVCGLLGmrTGGRNILIPNPRDiPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 306 LSNLheIASGGAPLAkeVGEAVAKR-FKLPG--IRQGYGLTETTSAIIITP-EGDDKPGACGKVVPFFSAKIVDlDTGKT 381
Cdd:PRK07059 326 FSKL--IVANGGGMA--VQRPVAERwLEMTGcpITEGYGLSETSPVATCNPvDATEFSGTIGLPLPSTEVSIRD-DDGND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 382 LGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQH 461
Cdd:PRK07059 401 LPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASH 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52631875 462 PFIFDAGVAGIPDPDAGELPAAVVVLEEgKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:PRK07059 481 PGVLEVAAVGVPDEHSGEAVKLFVVKKD-PALTEEDVKAFCKERLTNYKRPK-FVEFRTELPKTNVGKILRRELR 553
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
48-536 |
1.44e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 177.49 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 48 EVNITYSEYFEMACRLAEtmkryGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVf 127
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAW- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 128 cskralqkiLGV----QKKLPIIQkiVILDSREDymgkqsmysfiesHLPAGfneydyiPDsfdrETATALIMNSSGSTG 203
Cdd:PRK07787 97 ---------LGPapddPAGLPHVP--VRLHARSW-------------HRYPE-------PD----PDAPALIVYTSGTTG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 204 LPKGVELTHKNICVrfshCRDPVFGN-QIIPDTAILTVIP-FH-HGFgMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDy 280
Cdd:PRK07787 142 PPKGVVLSRRAIAA----DLDALAEAwQWTADDVLVHGLPlFHvHGL-VLGVLGPLRIGNRFVHTGRPTPEAYAQALSE- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 281 kiQSALL--VPTLFSFFAKSTLVDKYdLSNLHEIASGGAPLAKEVGEAVAKrfkLPGIR--QGYGLTETTSAIIITPEGD 356
Cdd:PRK07787 216 --GGTLYfgVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAA---LTGHRpvERYGMTETLITLSTRADGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 357 DKPGACGKVVPFFSAKIVDlDTGKTLGVNQR--GELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFI 434
Cdd:PRK07787 290 RRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 435 VDRlKS--LIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGktMTEQEVMDYVAGQVTASKRL 512
Cdd:PRK07787 369 VGR-EStdLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD--VAADELIDFVAQQLSVHKRP 445
|
490 500
....*....|....*....|....
gi 52631875 513 RgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:PRK07787 446 R-EVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
51-537 |
1.87e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 178.16 E-value: 1.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNdiynerelynsLSISQPTIVFCSK 130
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN-----------YRLAADEVAYILG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 131 RALQKILGVQKKLPII----QKIVILDSRedymGKQSMYSFIESHLPAGfneydyiPDSFDRETATALIMNSSGSTGLPK 206
Cdd:PRK06145 97 DAGAKLLLVDEEFDAIvaleTPKIVIDAA----AQADSRRLAQGGLEIP-------PQAAVAPTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 207 GVELTHKNICVRFShcrDPVFGNQIIPDTAILTVIPFHH-GFGMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSA 285
Cdd:PRK06145 166 GVMHSYGNLHWKSI---DHVIALGLTASERLLVVGPLYHvGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 286 LLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIITPEGD--DKPGACG 363
Cdd:PRK06145 243 WMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGReiEKIGSTG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 364 KVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIK 443
Cdd:PRK06145 323 RALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMII 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 444 YKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVP 523
Cdd:PRK06145 401 SGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPR-QLKVRDELP 479
|
490
....*....|....
gi 52631875 524 KGLTGKIDARKIRE 537
Cdd:PRK06145 480 RNPSGKVLKRVLRD 493
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
37-537 |
2.98e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 177.58 E-value: 2.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 37 PGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYN 116
Cdd:PRK13391 11 PDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 117 SLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVILDSREDYMGKQSMYSFIEShLPAgfneyDYIPDsfdrETATALIM 196
Cdd:PRK13391 91 IVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAG-LPA-----TPIAD----ESLGTDML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 197 NSSGSTGLPKGV--ELTHKNICVRFS--HCRDPVFGnqIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEEL 272
Cdd:PRK13391 161 YSSGTTGRPKGIkrPLPEQPPDTPLPltAFLQRLWG--FRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 273 FLRSLQDYKIQSALLVPTLFSFFAK--STLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKlPGIRQGYGLTETTSAII 350
Cdd:PRK13391 239 YLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWG-PIIHEYYAATEGLGFTA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 351 I-TPEGDDKPGACGKVVpFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKgYVNNPEATSALIDKDG-WLHSGDIAYYDK 428
Cdd:PRK13391 318 CdSEEWLAHPGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 429 DGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTE---QEVMDYVAGQ 505
Cdd:PRK13391 395 DGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFCRQR 474
|
490 500 510
....*....|....*....|....*....|..
gi 52631875 506 VTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK13391 475 LSRQKCPR-SIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
20-538 |
3.60e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 178.20 E-value: 3.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 20 GTAGEQLHKAMKRYaqvPGTIAFTDAHAEvnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIG 99
Cdd:PRK07788 49 GPFAGLVAHAARRA---PDRAALIDERGT--LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 100 VGVAptndiynereLYNSLSiSQPTIVFCSKRalqkiLGVQKklpiiqkIVI-------LDSREDYMGKQSMYSFIESHL 172
Cdd:PRK07788 124 ARII----------LLNTGF-SGPQLAEVAAR-----EGVKA-------LVYddeftdlLSALPPDLGRLRAWGGNPDDD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 173 PAGFNEYDYIPDSFDRETATAL---------IMNSSGSTGLPKGVELTHKNICVrfshcrdpvfgnqiiPDTAILTVIPF 243
Cdd:PRK07788 181 EPSGSTDETLDDLIAGSSTAPLpkppkpggiVILTSGTTGTPKGAPRPEPSPLA---------------PLAGLLSRVPF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 244 HHGF------GMFTTLGYLTC------GFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLVDKYDLSNL 309
Cdd:PRK07788 246 RAGEttllpaPMFHATGWAHLtlamalGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRIldLGPEVLAKYDTSSL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 310 HEIASGGAPLAKEVGEAVAKRFKlPGIRQGYGLTETTSAIIITPEGDDK-PGACGKVVPFFSAKIVDlDTGKTLGVNQRG 388
Cdd:PRK07788 326 KIIFVSGSALSPELATRALEAFG-PVLYNLYGSTEVAFATIATPEDLAEaPGTVGRPPKGVTVKILD-ENGNEVPRGVVG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 389 ELCVKGPMIMKGYVN--NPEAtsalidKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFD 466
Cdd:PRK07788 404 RIFVGNGFPFEGYTDgrDKQI------IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52631875 467 AGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREI 538
Cdd:PRK07788 478 AAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPR-DVVFLDELPRNPTGKVLKRELREM 548
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
193-536 |
4.69e-49 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 175.70 E-value: 4.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKnicVRFSHCRDPVFGNQIIPDTAIL---------------TVIPFHHgFGMfTTLGYLT 257
Cdd:cd05971 91 ALIIYTSGTTGPPKGALHAHR---VLLGHLPGVQFPFNLFPRDGDLywtpadwawigglldVLLPSLY-FGV-PVLAHRM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 258 CGFrivlmyrcEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIR 337
Cdd:cd05971 166 TKF--------DPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVE-VN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 QGYGLTETTSAIIITPE-GDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVK--GPMIMKGYVNNPEATSALIdK 414
Cdd:cd05971 237 EFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKM-A 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 415 DGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMT 494
Cdd:cd05971 315 GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPS 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 52631875 495 EQ---EVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:cd05971 395 DAlarEIQELVKTRLAAHEYPR-EIEFVNELPRTATGKIRRRELR 438
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
40-537 |
5.67e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 176.63 E-value: 5.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 40 IAFTDAHaevnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLS 119
Cdd:PRK08276 5 MAPSGEV----VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 120 ISQPTIVFCSKRALQKILGVQKKLPiiqkiviLDSREDYMGKQSmysfieshlPAGFNEYD-----YIPDSFDRETATAL 194
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELP-------AGVPLLLVVAGP---------VPGFRSYEealaaQPDTPIADETAGAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 195 IMNSSGSTGLPKGV--ELTHKNICVR-FSHCRDPVFGNQIIPDTAILTVIPFHHG----FGMFTtlgyLTCGFRIVLMYR 267
Cdd:PRK08276 145 MLYSSGTTGRPKGIkrPLPGLDPDEApGMMLALLGFGMYGGPDSVYLSPAPLYHTaplrFGMSA----LALGGTVVVMEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 268 CEEELFLRSLQDYKIQSALLVPTLFSFFAKstLVD----KYDLSNLHEIASGGAPLAKEVgeavaKRFKL----PGIRQG 339
Cdd:PRK08276 221 FDAEEALALIERYRVTHSQLVPTMFVRMLK--LPEevraRYDVSSLRVAIHAAAPCPVEV-----KRAMIdwwgPIIHEY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 340 YGLTETTSAIIITPEgD--DKPGACGKVVpFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGW 417
Cdd:PRK08276 294 YASSEGGGVTVITSE-DwlAHPGSVGKAV-LGEVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 418 LHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTE-- 495
Cdd:PRK08276 371 VTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDal 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 52631875 496 -QEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK08276 451 aAELIAWLRGRLAHYKCPR-SIDFEDELPRTPTGKLYKRRLRD 492
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
178-536 |
6.30e-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: 175.36 E-value: 6.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 178 EYDYIPDS--------FDRETA---TALIMNSSGSTGLPKGVELTHKN---ICVRFSHcrdPVFGNQiiPDTAILTVIPF 243
Cdd:cd05958 74 ELAYILDKaritvalcAHALTAsddICILAFTSGTTGAPKATMHFHRDplaSADRYAV---NVLRLR--EDDRFVGSPPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 244 HHGFGMFTTLGY-LTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKE 322
Cdd:cd05958 149 AFTFGLGGVLLFpFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 323 VGEAVAKRFKLPgIRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMimkGYV 402
Cdd:cd05958 229 LHRAWKEATGIP-IIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGPT---GCR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 403 NNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPA 482
Cdd:cd05958 304 YLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVK 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 52631875 483 AVVVLEEGKTMTEQ---EVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:cd05958 384 AFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPR-AIEFVTELPRTATGKLQRFALR 439
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
52-537 |
1.24e-48 |
|
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: 174.49 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 52 TYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELynslsisqptiVFCSKR 131
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHEL-----------AFILRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 132 ALQKILGVqkklpiiqkivildsredymgkqsmysfieshlPAGFNEYDYIPDSfdreTATALIMNSSGSTGLPKGVELT 211
Cdd:cd05903 72 AKAKVFVV---------------------------------PERFRQFDPAAMP----DAVALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 212 HKNI-CVRFSHCRDPVFGNQiipdTAILTVIPFHHGFGMfttLGYLTC----GFRIVLMYRCEEELFLRSLQDYKIQSAL 286
Cdd:cd05903 115 HNTLsASIRQYAERLGLGPG----DVFLVASPMAHQTGF---VYGFTLplllGAPVVLQDIWDPDKALALMREHGVTFMM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 287 LVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRqGYGLTETTSAIIITPEGDDKPGAC--GK 364
Cdd:cd05903 188 GATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS-AYGSTECPGAVTSITPAPEDRRLYtdGR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 365 VVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALiDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKY 444
Cdd:cd05903 267 PLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 445 KGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVDEVPK 524
Cdd:cd05903 345 GGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPR 424
|
490
....*....|...
gi 52631875 525 GLTGKIDARKIRE 537
Cdd:cd05903 425 TPSGKVQKFRLRE 437
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
46-530 |
1.25e-48 |
|
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: 174.94 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 46 HAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTI 125
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 126 VFCSKRalqkilgvqkklpiiqkivildsrEDymgkqsmysfieshlpagfneydyipdsfdretaTALIMNSSGSTGLP 205
Cdd:cd05914 83 IFVSDE------------------------DD----------------------------------VALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 206 KGVELTHKNICVRFSHCRDPVFgnqIIPDTAILTVIPFHHGFGMFTTLGY-LTCGFRIVLMYRCEEELfLRSLQDYKIQS 284
Cdd:cd05914 105 KGVMLTYRNIVSNVDGVKEVVL---LGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAK-IIALAFAQVTP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 285 ALLVPTLFSFF--AKSTLVDKYDLS-----------------------------NLHEIASGGAPLAKEVgEAVAKRFKL 333
Cdd:cd05914 181 TLGVPVPLVIEkiFKMDIIPKLTLKkfkfklakkinnrkirklafkkvheafggNIKEFVIGGAKINPDV-EEFLRTIGF 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 334 PGIrQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDTGktlgvNQRGELCVKGPMIMKGYVNNPEATSALID 413
Cdd:cd05914 260 PYT-IGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPA-----TGEGEIIVRGPNVMKGYYKNPEATAEAFD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 414 KDGWLHSGDIAYYDKDGHFFIVDRLKSLI-KYKGYQVPPAELESILLQHPFIFDAGVA---------GIPDPDAGELPAA 483
Cdd:cd05914 334 KDGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVvqekklvalAYIDPDFLDVKAL 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 52631875 484 VVVLEEGKTMteQEVMDYVAGQVTASKRLrGGVKFV-DEVPKGLTGKI 530
Cdd:cd05914 414 KQRNIIDAIK--WEVRDKVNQKVPNYKKI-SKVKIVkEEFEKTPKGKI 458
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
193-538 |
9.46e-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: 171.92 E-value: 9.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICVR---------------FSHCRDPVFgnqiIPDTAILTVIPFHHGFGMFTTLGylt 257
Cdd:cd05969 92 TLLHYTSGTTGTPKGVLHVHDAMIFYyftgkyvldlhpddiYWCTADPGW----VTGTVYGIWAPWLNGVTNVVYEG--- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 258 cgfrivlmyRCEEELFLRSLQDYKIQSALLVPTLFSFFAKS--TLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPg 335
Cdd:cd05969 165 ---------RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVP- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 336 IRQGYGLTETTSAIIIT-PEGDDKPGACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKG--PMIMKGYVNNPEATSALI 412
Cdd:cd05969 235 IHDTWWQTETGSIMIANyPCMPIKPGSMGKPLPGVKAAVVDEN-GNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 413 dKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKT 492
Cdd:cd05969 314 -IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 52631875 493 MTEQ---EVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREI 538
Cdd:cd05969 393 PSDElkeEIINFVRQKLGAHVAPR-EIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
26-539 |
9.64e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 174.07 E-value: 9.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 26 LHKAMKRYAQVPGTIaftdaHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPT 105
Cdd:PRK07470 13 LRQAARRFPDRIALV-----WGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 106 NDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVILDSREdymGKQSMYSFIESHLPAGFNeydyiPDS 185
Cdd:PRK07470 88 NFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGAR---AGLDYEALVARHLGARVA-----NAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 186 FDRETAtALIMNSSGSTGLPKGVELTHKNIC-VRFSHCRDpvfgnqIIPDT----AILTVIPFHHGFGMFTtLGYLTCGF 260
Cdd:PRK07470 160 VDHDDP-CWFFFTSGTTGRPKAAVLTHGQMAfVITNHLAD------LMPGTteqdASLVVAPLSHGAGIHQ-LCQVARGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 261 RIVLMY--RCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGE-AVAKRFKLpgIR 337
Cdd:PRK07470 232 ATVLLPseRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKrALAKLGKV--LV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 QGYGLTETTSAIIITP----EGDDKP----GACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATS 409
Cdd:PRK07470 310 QYFGLGEVTGNITVLPpalhDAEDGPdariGTCGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 410 ALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEE 489
Cdd:PRK07470 389 KAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARD 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 52631875 490 GKTMTEQEVMDYVAGQVtASKRLRGGVKFVDEVPKGLTGKIDARKIREIL 539
Cdd:PRK07470 468 GAPVDEAELLAWLDGKV-ARYKLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
32-537 |
1.06e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 174.20 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 32 RYAQV-PGTIAFTdaHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYN 110
Cdd:PRK07786 25 RHALMqPDAPALR--FLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 111 ERELYNSLSISQPTIVFcSKRALQKIL-GVQKKLPIIQKIVIL--DSREDYMGKQSMYSFI-ESHLPAGfneydyIPdsf 186
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVV-TEAALAPVAtAVRDIVPLLSTVVVAggSSDDSVLGYEDLLAEAgPAHAPVD------IP--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 187 drETATALIMNSSGSTGLPKGVELTHKNICVRFSHCrdpVFGNQI-IPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVL- 264
Cdd:PRK07786 173 --NDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTC---LRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIy 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 265 -MYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSnLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLT 343
Cdd:PRK07786 248 pLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 344 ETtSAIIITPEGDD---KPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDkDGWLHS 420
Cdd:PRK07786 327 EM-SPVTCMLLGEDairKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 421 GDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLE-EGKTMTEQEVM 499
Cdd:PRK07786 404 GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRnDDAALTLEDLA 483
|
490 500 510
....*....|....*....|....*....|....*...
gi 52631875 500 DYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK07786 484 EFLTDRLARYKHPK-ALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
27-537 |
1.22e-47 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 174.31 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 27 HKAMKRYAQVPG----TIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGV 102
Cdd:PRK04319 46 YEAIDRHADGGRkdkvALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 103 APTNDIYNERELYNSLSISQPTIVFCSKRALQKIlgVQKKLPIIQKIVILDSREDYMGKQsmYSFIEshlpagfnEYDYI 182
Cdd:PRK04319 126 GPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEEGPGT--LDFNA--------LMEQA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 183 PDSF-----DRETAtALIMNSSGSTGLPKGVELTHKNICVRFSHCR---------------DP--VFGnqiipdTAILTV 240
Cdd:PRK04319 194 SDEFdiewtDREDG-AILHYTSGSTGKPKGVLHVHNAMLQHYQTGKyvldlheddvywctaDPgwVTG------TSYGIF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 241 IPFHHGFGMfttlgyltcgfrIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLVDKYDLSNLHEIASGGAP 318
Cdd:PRK04319 267 APWLNGATN------------VIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLmgAGDDLVKKYDLSSLRHILSVGEP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 319 LAKEV---GEAVakrFKLPgIRQGYGLTETtSAIII--TPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVK 393
Cdd:PRK04319 335 LNPEVvrwGMKV---FGLP-IHDNWWMTET-GGIMIanYPAMDIKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 394 G--PMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAG 471
Cdd:PRK04319 409 KgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIG 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52631875 472 IPDPDAGELPAAVVVLEEGKTMTEQ---EVMDYVagqvtaSKRLRGGV-----KFVDEVPKGLTGKIDAR--KIRE 537
Cdd:PRK04319 488 KPDPVRGEIIKAFVALRPGYEPSEElkeEIRGFV------KKGLGAHAapreiEFKDKLPKTRSGKIMRRvlKAWE 557
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
26-538 |
1.33e-47 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 178.58 E-value: 1.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 26 LHKAMKRYA-QVPGTIAFTDAHAeVNITYSEYFEMACRLAETMKRyGLGLQHHIAVCSENSlqffmpVCGAL----FIGV 100
Cdd:PRK08633 617 LAEAWIDTAkRNWSRLAVADSTG-GELSYGKALTGALALARLLKR-ELKDEENVGILLPPS------VAGALanlaLLLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 101 GVAPTNDIY--NERELYNSLSISQPTIVFCSKRALQKI--LGVQKKLPIIQKIVILdsrEDYMGKQSMYSFIE-----SH 171
Cdd:PRK08633 689 GKVPVNLNYtaSEAALKSAIEQAQIKTVITSRKFLEKLknKGFDLELPENVKVIYL---EDLKAKISKVDKLTallaaRL 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 172 LPAGFNEYDYIPDSFDRETATalIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVFGNQiipDTAILTVIPFHHGFGM-F 250
Cdd:PRK08633 766 LPARLLKRLYGPTFKPDDTAT--IIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRN---DDVILSSLPFFHSFGLtV 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 251 TTLGYLTCGFRIVLMYRCEEELFLRSLQDyKIQSALLV--PTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVA 328
Cdd:PRK08633 841 TLWLPLLEGIKVVYHPDPTDALGIAKLVA-KHRATILLgtPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFE 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 329 KRFKLPgIRQGYGLTETTSAIII-TP---EGDD------KPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIM 398
Cdd:PRK08633 920 EKFGIR-ILEGYGATETSPVASVnLPdvlAADFkrqtgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVM 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 399 KGYVNNPEATSALI---DKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQhpFIFDAG----VAG 471
Cdd:PRK08633 999 KGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK--ALGGEEvvfaVTA 1076
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52631875 472 IPDPDAGElpaAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDARKIREI 538
Cdd:PRK08633 1077 VPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
19-540 |
6.81e-47 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 171.85 E-value: 6.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 19 DGTAGEQLHKAMKryaQVPGTIAFTDAHAeVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFI 98
Cdd:PRK06087 22 DASLADYWQQTAR---AMPDKIAVVDNHG-ASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 99 GVGVAPTNDIYNERELYNSLSISQPTIVFC-----SKRALQKILGVQKKLPIIQKIVILDSREDYMGKQSMYSFIESHLP 173
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 174 AGfneyDYIPDSFDRetaTALIMNSSGSTGLPKGVELTHKNICvrFSHcRDPVFGNQIIPDTAILTVIPFHHGFGMF--T 251
Cdd:PRK06087 178 LT----TAITTHGDE---LAAVLFTSGTEGLPKGVMLTHNNIL--ASE-RAYCARLNLTWQDVFMMPAPLGHATGFLhgV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 252 TLGYLTcGFRIVLMYRCEEELFLRSLQDYKIqSALLVPTLFSFFAKSTL-VDKYDLSNLHEIASGGAPLAKEVGEAVAKR 330
Cdd:PRK06087 248 TAPFLI-GARSVLLDIFTPDACLALLEQQRC-TCMLGATPFIYDLLNLLeKQPADLSALRFFLCGGTTIPKKVARECQQR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 331 fklpGIR--QGYGLTETTSAIIITPegdDKP-----GACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVN 403
Cdd:PRK06087 326 ----GIKllSVYGSTESSPHAVVNL---DDPlsrfmHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 404 NPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAA 483
Cdd:PRK06087 398 EPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCA 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 484 VVVL-EEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDARKIREILM 540
Cdd:PRK06087 478 YVVLkAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIM 535
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
46-537 |
8.87e-47 |
|
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: 170.56 E-value: 8.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 46 HAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENS-----LQFFMPVCGALFIgvgvaPTNDIYNERELYNSLSI 120
Cdd:cd12118 25 YGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTpamyeLHFGVPMAGAVLN-----ALNTRLDAEEIAFILRH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 121 SQPtivfcskralqkilgvqkklpiiqKIVILDSREDYmgkqsmysfiESHLPAGFNEYDYIPDSFDRETATaliMN-SS 199
Cdd:cd12118 100 SEA------------------------KVLFVDREFEY----------EDLLAEGDPDFEWIPPADEWDPIA---LNyTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 200 GSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEELFLRSLQD 279
Cdd:cd12118 143 GTTGRPKGVVYHHRGA---YLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKVDAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 280 YKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAkevgEAVAKRFKLPGIR--QGYGLTETTSAIII---TPE 354
Cdd:cd12118 220 HKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPP----AAVLAKMEELGFDvtHVYGLTETYGPATVcawKPE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 355 GDDKPG---ACGKV---VPFFSA---KIVDLDT-------GKTLGvnqrgELCVKGPMIMKGYVNNPEATSALIdKDGWL 418
Cdd:cd12118 296 WDELPTeerARLKArqgVRYVGLeevDVLDPETmkpvprdGKTIG-----EIVFRGNIVMKGYLKNPEATAEAF-RGGWF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 419 HSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEV 498
Cdd:cd12118 370 HSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEI 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 52631875 499 MDYvagqvtASKRLRG-----GVKFvDEVPKGLTGKIDARKIRE 537
Cdd:cd12118 450 IAF------CREHLAGfmvpkTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
53-537 |
3.13e-46 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 169.49 E-value: 3.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 53 YSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSKRA 132
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 133 LQkilGVQKKLPIIQKIVILDSREDYmgkQSMYSFIESHL--PAGFNEYDYIPDSFDRETATAL-----IMNSSGSTGLP 205
Cdd:PRK12406 94 LH---GLASALPAGVTVLSVPTPPEI---AAAYRISPALLtpPAGAIDWEGWLAQQEPYDGPPVpqpqsMIYTSGTTGHP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 206 KGV-------ELTHKNICVRFShcrdpVFGnqIIPDTAILTVIPFHH----GFGMFTtlgyLTCGFRIVLMYRCEEELFL 274
Cdd:PRK12406 168 KGVrraaptpEQAAAAEQMRAL-----IYG--LKPGIRALLTGPLYHsapnAYGLRA----GRLGGVLVLQPRFDPEELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 275 RSLQDYKIQSALLVPTLFSFFAK--STLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKlPGIRQGYGLTETTSAIIIT 352
Cdd:PRK12406 237 QLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWG-PVIYEYYGSTESGAVTFAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 353 PEgD--DKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGP-MIMKGYVNNPEATSAlIDKDGWLHSGDIAYYDKD 429
Cdd:PRK12406 316 SE-DalSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAgNPDFTYHNKPEKRAE-IDRGGFITSGDVGYLDAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 430 GHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVtAS 509
Cdd:PRK12406 393 GYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARL-AG 471
|
490 500
....*....|....*....|....*...
gi 52631875 510 KRLRGGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK12406 472 YKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
69-537 |
3.23e-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: 168.71 E-value: 3.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 69 RYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGvaPTNDIYNERELYNSLSISQP--TIVFCSKRALQKILGVQKKLPII 146
Cdd:cd05929 16 RLLLLDVYSIALNRNARAAAAEGVWIADGVYIY--LINSILTVFAAAAAWKCGACpaYKSSRAPRAEACAIIEIKAAALV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 147 QKIvildsredYMGKqsmysFIESHLPAGFNEYDYIPDS-FDRETATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDP 225
Cdd:cd05929 94 CGL--------FTGG-----GALDGLEDYEAAEGGSPETpIEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 226 VFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAK--STLVDK 303
Cdd:cd05929 161 ALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKlpEAVRNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 304 YDLSNLHEIASGGAPLAKEVGEAVAKRFKlPGIRQGYGLTETTSAIIITpeGDD---KPGACGKVVpFFSAKIVDLDtGK 380
Cdd:cd05929 241 YDLSSLKRVIHAAAPCPPWVKEQWIDWGG-PIIWEYYGGTEGQGLTIIN--GEEwltHPGSVGRAV-LGKVHILDED-GN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 381 TLGVNQRGELCVKGPMiMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQ 460
Cdd:cd05929 316 EVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 461 HPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQ---EVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:cd05929 395 HPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTAlaeELIAFLRDRLSRYKCPR-SIEFVAELPRDDTGKLYRRLLRD 473
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
20-539 |
5.23e-45 |
|
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: 166.69 E-value: 5.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 20 GTAGEQLHKAMKRYAQVpGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHH-IAVCSENslQFFMPVCGALFI 98
Cdd:cd05906 10 RTLLELLLRAAERGPTK-GITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSvILQFDDN--EDFIPAFWACVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 99 G------VGVAPTNDIYNERE--LYNSLSI-SQPTIVfCSKRALQKILGVQKKLPI-IQKIVILDSREDYMGkqsmysfi 168
Cdd:cd05906 87 AgfvpapLTVPPTYDEPNARLrkLRHIWQLlGSPVVL-TDAELVAEFAGLETLSGLpGIRVLSIEELLDTAA-------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 169 ESHLPAGfneydyipdsfdRETATALIMNSSGSTGLPKGVELTHKNICVRfshCRDPVFGNQIIPDTAILTVIPFHHgfg 248
Cdd:cd05906 158 DHDLPQS------------RPDDLALLMLTSGSTGFPKAVPLTHRNILAR---SAGKIQHNGLTPQDVFLNWVPLDH--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 249 mftTLGYLTCGFRIVLmYRCEE------------ELFLRSLQDYKIQsallvptlFSF---FAKSTLVD--------KYD 305
Cdd:cd05906 220 ---VGGLVELHLRAVY-LGCQQvhvpteeiladpLRWLDLIDRYRVT--------ITWapnFAFALLNDlleeiedgTWD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 306 LSNLHEIASGGAPLAKEVGEAVA---KRFKLPG--IRQGYGLTETTSAII--ITPEGDDKPGA-----CGKVVPFFSAKI 373
Cdd:cd05906 288 LSSLRYLVNAGEAVVAKTIRRLLrllEPYGLPPdaIRPAFGMTETCSGVIysRSFPTYDHSQAlefvsLGRPIPGVSMRI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 374 VDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDkDGHFFIVDRLKSLIKYKGYQVPPAE 453
Cdd:cd05906 368 VD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 454 LESILLQHPFI---FDAGVAgIPDPDAGELPAAVVVLEEgktMTEQEVMDYVAGQVTASKRLRGGVK--FV-----DEVP 523
Cdd:cd05906 446 IEAAVEEVPGVepsFTAAFA-VRDPGAETEELAIFFVPE---YDLQDALSETLRAIRSVVSREVGVSpaYLiplpkEEIP 521
|
570
....*....|....*.
gi 52631875 524 KGLTGKIDARKIREIL 539
Cdd:cd05906 522 KTSLGKIQRSKLKAAF 537
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
191-536 |
3.47e-43 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 159.55 E-value: 3.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 191 ATALIMNSSGSTGLPKGVELTHKN---ICVRFshCRdPVFGnqIIPDTAILTVIPFHHGFGMFTTL-GYLTCGFRIVLM- 265
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDpllFADAM--AR-EALG--LTPGDRVFSSAKMFFGYGLGNSLwFPLAVGASAVLNp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 -YRCEEELFLRSLQdYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTE 344
Cdd:cd05919 167 gWPTAERVLATLAR-FRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGP-ILDGIGATE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 345 TTSAIIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIA 424
Cdd:cd05919 245 VGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKF 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 425 YYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTE---QEVMDY 501
Cdd:cd05919 323 CRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRH 402
|
330 340 350
....*....|....*....|....*....|....*
gi 52631875 502 VAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:cd05919 403 LLERLSAHKVPR-RIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
42-530 |
1.12e-42 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 159.27 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 42 FTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSIS 121
Cdd:PRK07514 20 FIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 122 QPTIVFCSKRALQKILGVQKKLPIIQkIVILDsrEDYMGkqsmySFIE--SHLPAGFNEYDYIPDSFdretatALIMNSS 199
Cdd:PRK07514 100 EPALVVCDPANFAWLSKIAAAAGAPH-VETLD--ADGTG-----SLLEaaAAAPDDFETVPRGADDL------AAILYTS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 200 GSTGLPKGVELTHKNI---------CVRFShcrdpvfgnqiiPDTAILTVIPFHHGFGMF-TTLGYLTCGFRIVLMYRCE 269
Cdd:PRK07514 166 GTTGRSKGAMLSHGNLlsnaltlvdYWRFT------------PDDVLIHALPIFHTHGLFvATNVALLAGASMIFLPKFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 270 EELFLRSLQdykiQSALL--VPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRfklPG--IRQGYGLTET 345
Cdd:PRK07514 234 PDAVLALMP----RATVMmgVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQER---TGhaILERYGMTET 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 346 tsaIIIT--P-EGDDKPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGD 422
Cdd:PRK07514 307 ---NMNTsnPyDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 423 IAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYV 502
Cdd:PRK07514 384 LGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAAL 463
|
490 500 510
....*....|....*....|....*....|.
gi 52631875 503 AGQVTA---SKRlrggVKFVDEVPKGLTGKI 530
Cdd:PRK07514 464 KGRLARfkqPKR----VFFVDELPRNTMGKV 490
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
18-539 |
3.04e-42 |
|
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: 158.77 E-value: 3.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 18 EDGTAGEQLHKAMKRYaqvPGTIAFTDAHAEvnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFmPVCGALF 97
Cdd:COG1021 23 RGETLGDLLRRRAERH---PDRIAVVDGERR--LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFV-IVFFALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 98 iGVGVAPTNDIYNER--ELYNSLSISQPTIVFCSK-------RALQKilGVQKKLPIIQKIVILDSREDYMGKQSMYSfi 168
Cdd:COG1021 97 -RAGAIPVFALPAHRraEISHFAEQSEAVAYIIPDrhrgfdyRALAR--ELQAEVPSLRHVLVVGDAGEFTSLDALLA-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 169 eshLPAGFNEYDyiPDSFDretaTALIMNSSGSTGLPKGVELTHKN----------ICvRFShcrdpvfgnqiiPDTAIL 238
Cdd:COG1021 172 ---APADLSEPR--PDPDD----VAFFQLSGGTTGLPKLIPRTHDDylysvrasaeIC-GLD------------ADTVYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 239 TVIPFHHGFGM--FTTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGG 316
Cdd:COG1021 230 AALPAAHNFPLssPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 317 APLAKEVGEAVAKRFklpGIR--QGYGLTE----TTS-----AIIITPEG-----DDKpgacgkvvpffsAKIVDlDTGK 380
Cdd:COG1021 310 AKLSPELARRVRPAL---GCTlqQVFGMAEglvnYTRlddpeEVILTTQGrpispDDE------------VRIVD-EDGN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 381 TLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQ 460
Cdd:COG1021 374 PVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52631875 461 HPFIFDAGVAGIPDPDAGELPAAVVVLeEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDARKIREIL 539
Cdd:COG1021 454 HPAVHDAAVVAMPDEYLGERSCAFVVP-RGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
23-531 |
3.89e-42 |
|
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: 157.49 E-value: 3.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 23 GEQLHKAMKRYAQ-VPGTIAFTDAhaEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMpVCGALFiGVG 101
Cdd:cd05920 14 DEPLGDLLARSAArHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVV-LFFALL-RLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 102 VAPTNDIYNER--ELYNSLSISQPTIvfcskralqkilgvqkklpiiqkIVILDSREDYMGKQSMYSFIESHlpagfney 179
Cdd:cd05920 90 AVPVLALPSHRrsELSAFCAHAEAVA-----------------------YIVPDRHAGFDHRALARELAESI-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 180 dyiPDsfdretaTALIMNSSGSTGLPKGVELTHKNIC--VRFSH--CRdpvfgnqIIPDTAILTVIPFHHGFGMFT--TL 253
Cdd:cd05920 139 ---PE-------VALFLLSGGTTGTPKLIPRTHNDYAynVRASAevCG-------LDQDTVYLAVLPAAHNFPLACpgVL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 254 GYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKl 333
Cdd:cd05920 202 GTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLG- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 334 PGIRQGYGLTE---------TTSAIIITPEGddKPgacgkVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNN 404
Cdd:cd05920 281 CTLQQVFGMAEgllnytrldDPDEVIIHTQG--RP-----MSPDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYRA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 405 PEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAV 484
Cdd:cd05920 353 PEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAF 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 52631875 485 VVLEEGKTMTEQeVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKID 531
Cdd:cd05920 433 VVLRDPPPSAAQ-LRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKID 478
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
37-544 |
2.45e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 155.35 E-value: 2.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 37 PGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENS-----LQFFMPVCGALFIgvgvaPTNDIYNE 111
Cdd:PRK09088 9 PQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSvwlvaLHFACARVGAIYV-----PLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 112 RELYNSLSISQPTIvfcskralqkilgvqkklpIIQKIVILDSREDYMGKQSMYSFIESHLPAgfneydyIPDSFDREtA 191
Cdd:PRK09088 84 SELDALLQDAEPRL-------------------LLGDDAVAAGRTDVEDLAAFIASADALEPA-------DTPSIPPE-R 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNI---CVRFShcrdpVFGnQIIPDTAILTVIPFHHGFGMFTTL-GYLTCGFRIVLMYR 267
Cdd:PRK09088 137 VSLILFTSGTSGQPKGVMLSERNLqqtAHNFG-----VLG-RVDAHSSFLCDAPMFHIIGLITSVrPVLAVGGSILVSNG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 268 CEEELFLRSLQD--YKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAP-LAKEVGEAVAKrfklpGIRQ--GYGL 342
Cdd:PRK09088 211 FEPKRTLGRLGDpaLGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPhAAEDILGWLDD-----GIPMvdGFGM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 343 TETTSAIIITPEG---DDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLH 419
Cdd:PRK09088 286 SEAGTVFGMSVDCdviRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 420 SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVM 499
Cdd:PRK09088 365 TGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIR 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 52631875 500 DYVAGQVtASKRLRGGVKFVDEVPKGLTGKIDARKIREILMMGKK 544
Cdd:PRK09088 445 SHLSTRL-AKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
34-539 |
2.04e-40 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 154.06 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 34 AQVPGTIAFTDAHAEVN----ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIY 109
Cdd:PRK13295 35 ASCPDKTAVTAVRLGTGaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 110 NERELYNSLSISQPTIVFCSKR-----ALQKILGVQKKLPIIQKIVILDSREDYmgkqsmySFiESHL--PAGFNEYDyI 182
Cdd:PRK13295 115 RERELSFMLKHAESKVLVVPKTfrgfdHAAMARRLRPELPALRHVVVVGGDGAD-------SF-EALLitPAWEQEPD-A 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 183 PDSFDRETA----TALIMNSSGSTGLPKGVELTHknicvrfshcrDPVFGNqIIP---------DTAILTVIPFHH--GF 247
Cdd:PRK13295 186 PAILARLRPgpddVTQLIYTSGTTGEPKGVMHTA-----------NTLMAN-IVPyaerlglgaDDVILMASPMAHqtGF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 248 gMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAV 327
Cdd:PRK13295 254 -MYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 328 AKRFKLPgIRQGYGLTETTSAIIITPEGDDKPGAC--GKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNP 405
Cdd:PRK13295 333 RAALGAK-IVSAWGMTENGAVTLTKLDDPDERASTtdGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 406 EATSalIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVV 485
Cdd:PRK13295 411 QLNG--TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFV 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 52631875 486 VLEEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDARKIREIL 539
Cdd:PRK13295 489 VPRPGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
51-477 |
2.08e-40 |
|
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: 153.91 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGL--GLQHHIAVCSENSLQFF--MPVCGAlFIGVGVAptndiynereLYNSLSISqpTIV 126
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIisELACYA-YSLVTVP----------LYDTLGPE--AIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 127 FCSKRALQKILGVQKKLPIIQKIVILDsredyMGKQsmysfieshlpagfNEYDYIPDsfDRETaTALIMNSSGSTGLPK 206
Cdd:cd05927 73 YILNHAEISIVFCDAGVKVYSLEEFEK-----LGKK--------------NKVPPPPP--KPED-LATICYTSGTTGNPK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 207 GVELTHKNICVRFSHCRD-PVFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLmYRCEEELFLRSLQDYKIQSA 285
Cdd:cd05927 131 GVMLTHGNIVSNVAGVFKiLEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGF-YSGDIRLLLDDIKALKPTVF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 286 LLVPTLF--------------SFFAK---------------------STLVDKYDLS--------NLHEIASGGAPLAKE 322
Cdd:cd05927 210 PGVPRVLnriydkifnkvqakGPLKRklfnfalnyklaelrsgvvraSPFWDKLVFNkikqalggNVRLMLTGSAPLSPE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 323 VGEAVAKRFKLPgIRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDL-DTGKT-LGVNQRGELCVKGPMIMKG 400
Cdd:cd05927 290 VLEFLRVALGCP-VLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVpEMNYDaKDPNPRGEVCIRGPNVFSG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 401 YVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPFIFDAGVAG-------- 471
Cdd:cd05927 369 YYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYGdslksflv 448
|
....*....
gi 52631875 472 ---IPDPDA 477
Cdd:cd05927 449 aivVPDPDV 457
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
191-531 |
2.49e-40 |
|
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: 148.99 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 191 ATALIMNSSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIP-FHHGFgMFTTLGYLTCGFRIVLMYRCE 269
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQAL---LAQALVLAVLQAIDEGTVFLNSGPlFHIGT-LMFTLATFHAGGTNVFVRRVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 270 EELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHeiASGGAPLAKEVGEAVAKRF-KLPGirqGYGLTETTSA 348
Cdd:cd17636 77 AEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLR--SSPAAPEWNDMATVDTSPWgRKPG---GYGQTEVMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 349 IIITPEGDDKPGACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDK 428
Cdd:cd17636 152 ATFAALGGGAIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 429 DGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTA 508
Cdd:cd17636 230 DGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIAS 309
|
330 340
....*....|....*....|...
gi 52631875 509 SKRLRgGVKFVDEVPKGLTGKID 531
Cdd:cd17636 310 YKKPK-SVEFADALPRTAGGADD 331
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
193-539 |
5.90e-40 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 147.86 E-value: 5.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfgNQIIPDTAILTViPFHHGFGMFTTLGYLTCGFRIVLMYRceEEL 272
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRL--GFGGGDSWLLSL-PLYHVGGLAILVRSLLAGAELVLLER--NQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 273 FLRSLQDYKIQSALLVPT-----LFSFFAKSTLVdkydlsNLHEIASGGAPLAKEVGEAVAKRfklpGIR--QGYGLTET 345
Cdd:cd17630 78 LAEDLAPPGVTHVSLVPTqlqrlLDSGQGPAALK------SLRAVLLGGAPIPPELLERAADR----GIPlyTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 346 TSAIIITPEGDDKPGACGKVVPffsakivdldtGKTLGVNQRGELCVKGPMIMKGYVNNPEatSALIDKDGWLHSGDIAY 425
Cdd:cd17630 148 ASQVATKRPDGFGRGGVGVLLP-----------GRELRIVEDGEIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDLGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 426 YDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKtmTEQEVMDYVAGQ 505
Cdd:cd17630 215 LHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA--DPAELRAWLKDK 292
|
330 340 350
....*....|....*....|....*....|....
gi 52631875 506 VTASKRLRgGVKFVDEVPKGLTGKIDARKIREIL 539
Cdd:cd17630 293 LARFKLPK-RIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1-538 |
6.69e-40 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 152.22 E-value: 6.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 1 MEDAKNIMHGPP--PFyPLEDGTAGEQLHKAMKRYAQVPGTIAftdahAEVNITYSEYFEMACRLAETMKRYGLGLQHHI 78
Cdd:PRK06155 1 GEPLGAGLAARAvdPL-PPSERTLPAMLARQAERYPDRPLLVF-----GGTRWTYAEAARAAAAAAHALAAAGVKRGDRV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 79 AVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVILDSREdy 158
Cdd:PRK06155 75 ALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 159 mgkqsmysfiESHLPAGFNeYDYIPDSFDRETA-------TALIMNSSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQI 231
Cdd:PRK06155 153 ----------SVSVPAGWS-TAPLPPLDAPAPAaavqpgdTAAILYTSGTTGPSKGVCCPHAQF---YWWGRNSAEDLEI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 232 IPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTlvdKYDLSNLHE 311
Cdd:PRK06155 219 GADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQP---ARESDRAHR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 312 IASGGAP-LAKEVGEAVAKRFKLPgIRQGYGLTEtTSAIIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGEL 390
Cdd:PRK06155 296 VRVALGPgVPAALHAAFRERFGVD-LLDGYGSTE-TNFVIAVTHGSQRPGSMGRLAPGFEARVVD-EHDQELPDGEPGEL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 391 CVKG--PM-IMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDA 467
Cdd:PRK06155 373 LLRAdePFaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAA 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52631875 468 GVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVT--ASKRLrggVKFVDEVPKGLTGKIDARKIREI 538
Cdd:PRK06155 452 AVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAyfAVPRY---VEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
46-538 |
4.23e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 150.04 E-value: 4.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 46 HAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTI 125
Cdd:PRK07798 24 CGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 126 VFCSKRALQKILGVQKKLPIIQKIVILD--SREDYMGKQSMYsfiESHLPAGFNEYDYIPDSFDretaTALIMNSSGSTG 203
Cdd:PRK07798 104 LVYEREFAPRVAEVLPRLPKLRTLVVVEdgSGNDLLPGAVDY---EDALAAGSPERDFGERSPD----DLYLLYTGGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 204 LPKGVELTHKNICVRFSHCRDPVFGNQI------------IPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCE-- 269
Cdd:PRK07798 177 MPKGVMWRQEDIFRVLLGGRDFATGEPIedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLLPDVRfd 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 270 -EELfLRSLQDYKIQSALLV------PTLFSFFAKSTlvdkYDLSNLHEIASGGAPLAKEVGEAVAKRfkLPG--IRQGY 340
Cdd:PRK07798 257 aDEV-WRTIEREKVNVITIVgdamarPLLDALEARGP----YDLSSLFAIASGGALFSPSVKEALLEL--LPNvvLTDSI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 341 GLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDTGKTL-GVNQRGELCVKGPmIMKGYVNNPEATSAL---IDKDG 416
Cdd:PRK07798 330 GSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEpGSGEIGWIARRGH-IPLGYYKDPEKTAETfptIDGVR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 417 WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQ 496
Cdd:PRK07798 409 YAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA 488
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 52631875 497 EVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREI 538
Cdd:PRK07798 489 ELRAHCRSSLAGYKVPR-AIWFVDEVQRSPAGKADYRWAKEQ 529
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
46-538 |
1.31e-38 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 149.40 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 46 HAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENS-----LQFFMPVCGALFigvgvaptNDIyNERelynslsI 120
Cdd:PLN03102 35 YGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTpamyeMHFAVPMAGAVL--------NPI-NTR-------L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 121 SQPTIVFCSKRALQKILGVQKKL-PIIQKIVILDSREDYMGKQSMYSFIESHLP--AGFNEYDY---------IPDSFDR 188
Cdd:PLN03102 99 DATSIAAILRHAKPKILFVDRSFePLAREVLHLLSSEDSNLNLPVIFIHEIDFPkrPSSEELDYecliqrgepTPSLVAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 189 ------ETATALIMNSSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRI 262
Cdd:PLN03102 179 mfriqdEHDPISLNYTSGTTADPKGVVISHRGA---YLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 263 VLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKevgeAVAKRFKLPG--IRQGY 340
Cdd:PLN03102 256 VCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPA----ALVKKVQRLGfqVMHAY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 341 GLTETTSAIIIT---------PEGDDKPGACGKVVPFFSAKIVDLDTGKTLGVNQR-----GELCVKGPMIMKGYVNNPE 406
Cdd:PLN03102 332 GLTEATGPVLFCewqdewnrlPENQQMELKARQGVSILGLADVDVKNKETQESVPRdgktmGEIVIKGSSIMKGYLKNPK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 407 ATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVV 486
Cdd:PLN03102 412 ATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52631875 487 LEEGKTMTEQEVMDYVAGQVTASKRLRGG---------VKFVDEVPKGLTGKIDARKIREI 538
Cdd:PLN03102 491 LEKGETTKEDRVDKLVTRERDLIEYCRENlphfmcprkVVFLQELPKNGNGKILKPKLRDI 551
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
198-531 |
4.53e-38 |
|
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: 142.54 E-value: 4.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 198 SSGSTGLPKGVELTHKNICVRFSHCRDpvfGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEELFLRSL 277
Cdd:cd17633 8 TSGTTGLPKAYYRSERSWIESFVCNED---LFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 278 QDYKIQSALLVPTLFSFFAKSTLVDkydlSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIITPEGDD 357
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 358 KPGACGKVVPFFSAKIVDLDTGKTlgvnqrGELCVKGPMIMKGYVNNPEatsalIDKDGWLHSGDIAYYDKDGHFFIVDR 437
Cdd:cd17633 161 PPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVRGGF-----SNPDGWMSVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 438 LKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVvleEGKTMTEQEVMDYVAGQVTASKRLRgGVK 517
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLTYKQLKRFLKQKLSRYEIPK-KII 305
|
330
....*....|....
gi 52631875 518 FVDEVPKGLTGKID 531
Cdd:cd17633 306 FVDSLPYTSSGKIA 319
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
51-471 |
6.74e-38 |
|
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: 145.58 E-value: 6.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFcsk 130
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 131 ralqkilgvqkklpiiqkiviLDSREDYMgkqsmysfieshlpagfneydyipdsfdretatALIMNSSGSTGLPKGVEL 210
Cdd:cd17640 83 ---------------------VENDSDDL---------------------------------ATIIYTSGTTGNPKGVML 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 211 THKNICVRFSHCRDPVfgnQIIPDTAILTVIPFHHGFGMFTTLGYLTCGfrIVLMYrCEEELFLRSLQDYKIQSALLVPT 290
Cdd:cd17640 109 THANLLHQIRSLSDIV---PPQPGDRFLSILPIWHSYERSAEYFIFACG--CSQAY-TSIRTLKDDLKRVKPHYIVSVPR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 291 LF-------------SFFAKSTLVDKYDLSNLHEIA-SGGAPLAKEVgeavAKRFKLPGIR--QGYGLTETTSAIIITPE 354
Cdd:cd17640 183 LWeslysgiqkqvskSSPIKQFLFLFFLSGGIFKFGiSGGGALPPHV----DTFFEAIGIEvlNGYGLTETSPVVSARRL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 355 GDDKPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFI 434
Cdd:cd17640 259 KCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVL 338
|
410 420 430
....*....|....*....|....*....|....*...
gi 52631875 435 VDRLKSLIKYK-GYQVPPAELESILLQHPFIFDAGVAG 471
Cdd:cd17640 339 TGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
195-537 |
7.02e-38 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 146.46 E-value: 7.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 195 IMNSSGSTGLPKGVELTHKNICVRFSHC--------RDPVFGNqiIPDT-----AILTVI-PFHHGfgmfttlgylTCGF 260
Cdd:cd05928 179 IYFTSGTTGSPKMAEHSHSSLGLGLKVNgrywldltASDIMWN--TSDTgwiksAWSSLFePWIQG----------ACVF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 261 rIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLvDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGY 340
Cdd:cd05928 247 -VHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDL-SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEGY 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 341 GLTETTsAIIITPEGDD-KPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVK-GPM----IMKGYVNNPEATSALIDK 414
Cdd:cd05928 324 GQTETG-LICANFKGMKiKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 415 DGWLhSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVL------E 488
Cdd:cd05928 402 DFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLapqflsH 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 52631875 489 EGKTMTeQEVMDYVAgQVTASKRLRGGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:cd05928 481 DPEQLT-KELQQHVK-SVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
28-547 |
1.73e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 144.54 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 28 KAMKRYA-QVPGTIAFTDAhaEVNITYSEYFEMACR----LAETMKRyglglQHHIAVCSENSLQFFMPVCGALFIGVGV 102
Cdd:PRK07638 5 KEYKKHAsLQPNKIAIKEN--DRVLTYKDWFESVCKvanwLNEKESK-----NKTIAILLENRIEFLQLFAGAAMAGWTC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 103 APTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKlpiiqkivILDSREdYMGKqsmysfIESHLPAGFNEYDYI 182
Cdd:PRK07638 78 VPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGR--------VIEIDE-WKRM------IEKYLPTYAPIENVQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 183 PDSFdretatalIMN-SSGSTGLPKGVELTHKNICVRFShCRDPVFgnQIIPDTAIL---TVIPFHHGFGMFTTLgYLtc 258
Cdd:PRK07638 143 NAPF--------YMGfTSGSTGKPKAFLRAQQSWLHSFD-CNVHDF--HMKREDSVLiagTLVHSLFLYGAISTL-YV-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 259 GFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVdkydLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQ 338
Cdd:PRK07638 209 GQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRV----IENKMKIISSGAKWEAEAKEKIKNIFPYAKLYE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 339 GYGLTETTSAIIITPEGDD-KPGACGKvvPFFSAKI-VDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALiDKDG 416
Cdd:PRK07638 285 FYGASELSFVTALVDEESErRPNSVGR--PFHNVQVrICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAREL-NADG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 417 WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVvleEGKTmTEQ 496
Cdd:PRK07638 362 WMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TKQ 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 52631875 497 EVMDYVAGQVTASKRLRGGVkFVDEVPKGLTGKIDARKIREILMMGKKSKL 547
Cdd:PRK07638 438 QLKSFCLQRLSSFKIPKEWH-FVDEIPYTNSGKIARMEAKSWIENQEKIYE 487
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
26-533 |
1.91e-37 |
|
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: 144.57 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 26 LHKAMKRYA-QVPGTIAFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAP 104
Cdd:cd05923 3 VFEMLRRAAsRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 105 TNDIYNERElynslsisqptIVFCSKRALQKILGVQKKLPIIQKIVILDSREDYMGKQSMYSFIESHLPAgfneydyIPD 184
Cdd:cd05923 83 INPRLKAAE-----------LAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPL-------IED 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 185 SFDRETATALIMNSSGSTGLPKGVELTHKNICVR---FSHCRDPVFGNQiipdTAILTVIPFHHGFGMFTTL-GYLTCGF 260
Cdd:cd05923 145 PPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRvlfMSTQAGLRHGRH----NVVLGLMPLYHVIGFFAVLvAALALDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 261 RIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRfkLPGIRQG- 339
Cdd:cd05923 221 TYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQH--LPGEKVNi 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 340 YGLTETTSAIIITpegDDKPGACGKVVPFFSAKIVDLDTG--KTLGVNQRGELCVK--GPMIMKGYVNNPEATSALIdKD 415
Cdd:cd05923 299 YGTTEAMNSLYMR---DARTGTEMRPGFFSEVRIVRIGGSpdEALANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 416 GWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGkTMTE 495
Cdd:cd05923 375 GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSA 453
|
490 500 510
....*....|....*....|....*....|....*....
gi 52631875 496 QEVMDYVAGQVTAS-KRLRGGVkFVDEVPKGLTGKIDAR 533
Cdd:cd05923 454 DELDQFCRASELADfKRPRRYF-FLDELPKNAMNKVLRR 491
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
189-535 |
1.31e-36 |
|
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: 141.23 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 189 ETATALIMNSSGSTGLPKGVELTHKN-------ICVRFSHCRDPVFGNQIipdtailtviPFHHGFGMFTTLGYLTCGFR 261
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNlvsftnwMLSDFPLGPGDVFLNQA----------PFSFDLSVMDLYPALASGAT 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 262 IVL----MYRCEEELFlRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIR 337
Cdd:cd05945 166 LVPvprdATADPKQLF-RFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 QGYGLTETT---SAIIITPE--GDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSA-- 410
Cdd:cd05945 245 NTYGPTEATvavTYIEVTPEvlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaf 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 411 -LIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEE 489
Cdd:cd05945 324 fPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 52631875 490 G---------KTMTEQEVMDYVAGQvtaskrlrggvKFV--DEVPKGLTGKIDARKI 535
Cdd:cd05945 404 GaeagltkaiKAELAERLPPYMIPR-----------RFVylDELPLNANGKIDRKAL 449
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
192-530 |
1.52e-36 |
|
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: 138.93 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNICVRFSHCRdpVFGNQIIPDTAILTVIPFHHGFGMfttLGYLTC----GFRIVLMYR 267
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQ--KEGLNWVVGDVTYLPLPATHIGGL---WWILTClihgGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 268 CEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGA-PLAKEVgeAVAKRFKLPGIRQGYGLTETT 346
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSrAIAADV--RFIEATGLTNTAQVYGLSETG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 347 SAIIItPEGDDKP--GACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIA 424
Cdd:cd17635 156 TALCL-PTDDDSIeiNAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 425 YYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAG 504
Cdd:cd17635 233 ERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALKHTIR 312
|
330 340
....*....|....*....|....*.
gi 52631875 505 QVTASKRLRGGVKFVDEVPKGLTGKI 530
Cdd:cd17635 313 RELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
31-537 |
2.05e-36 |
|
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: 142.38 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 31 KRYAQVPGTIAFT----DAHAEVNITYSEYFEMACRLAEtmkryglGLQHH------IAVCSENSLQFFMPVCGALFIGV 100
Cdd:cd05931 1 RRAAARPDRPAYTflddEGGREETLTYAELDRRARAIAA-------RLQAVgkpgdrVLLLAPPGLDFVAAFLGCLYAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 101 gVA-----PTNDIYNEReLYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVIL--DSREDymgkqsmysfieshlp 173
Cdd:cd05931 74 -IAvplppPTPGRHAER-LAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLvvDLLPD---------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 174 agfNEYDYIPDSFDRETATALIMNSSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTL 253
Cdd:cd05931 136 ---TSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNL---LANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 254 GY-LTCGFRIVLM---------YRceeelFLRSLQDYKIQ-SAllVPTlfsfFAKSTLVDK--------YDLSNLHEIAS 314
Cdd:cd05931 210 LTpLYSGGPSVLMspaaflrrpLR-----WLRLISRYRATiSA--APN----FAYDLCVRRvrdedlegLDLSSWRVALN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 315 GGAPLAKEVGEAVAKRFKLPGIRQ-----GYGLTETTSAIIITPEGD---------------------DKPGA-----CG 363
Cdd:cd05931 279 GAEPVRPATLRRFAEAFAPFGFRPeafrpSYGLAEATLFVSGGPPGTgpvvlrvdrdalagravavaaDDPAArelvsCG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 364 KVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEAT------SALIDKDGWLHSGDIAYYdKDGHFFIVDR 437
Cdd:cd05931 359 RPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATaetfgaLAATDEGGWLRTGDLGFL-HDGELYITGR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 438 LKSLIKYKGYQVPPAELESILLQHPFIFDAGVA---GIPDPDAGELpaaVVVLEEGKTMTE---QEVMDYVAGQVTASKR 511
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATAEEAHPALRPGCVaafSVPDDGEERL---VVVAEVERGADPadlAAIAAAIRAAVAREHG 514
|
570 580
....*....|....*....|....*....
gi 52631875 512 LR-GGVKFV--DEVPKGLTGKIDARKIRE 537
Cdd:cd05931 515 VApADVVLVrpGSIPRTSSGKIQRRACRA 543
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
193-537 |
7.49e-36 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 140.79 E-value: 7.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICvrfSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTL-GYLTCGFRIVLMYRCE-- 269
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIA---SSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALlATLASGGAVLLPARGRfs 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 270 EELFLRSLQDYKIQSALLVPTLFSFFAK--STLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIrQGYGLTETTS 347
Cdd:PRK05852 256 AHTFWDDIKAVGATWYTAVPTIHQILLEraATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVV-CAFGMTEATH 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 348 AIIITP-EG---DDKPGACGKVVPFFSA---KIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHS 420
Cdd:PRK05852 335 QVTTTQiEGigqTENPVVSTGLVGRSTGaqiRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRT 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 421 GDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMD 500
Cdd:PRK05852 413 GDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQ 492
|
330 340 350
....*....|....*....|....*....|....*..
gi 52631875 501 YVAGQVtASKRLRGGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK05852 493 FCRERL-AAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
193-534 |
8.77e-36 |
|
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: 138.81 E-value: 8.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfgnQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLmyrCEEEL 272
Cdd:cd05930 96 AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY---PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVV---LPEEV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 273 ------FLRSLQDYKIQSALLVPTLFSFFAKStlVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETT 346
Cdd:cd05930 170 rkdpeaLADLLAEEGITVLHLTPSLLRLLLQE--LELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEAT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 347 ---SAIIITPEGDDKPGAC-GKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKD-----GW 417
Cdd:cd05930 248 vdaTYYRVPPDDEEDGRVPiGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNpfgpgER 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 418 LH-SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQ 496
Cdd:cd05930 327 MYrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEE 406
|
330 340 350
....*....|....*....|....*....|....*...
gi 52631875 497 EVMDYVAGQVTASKRLRGGVkFVDEVPKGLTGKIDARK 534
Cdd:cd05930 407 ELRAHLAERLPDYMVPSAFV-VLDALPLTPNGKVDRKA 443
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
273-538 |
1.03e-35 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 141.30 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 273 FLRSLQDYKIQSALLVPTLFSFFAK----STLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQgYGLTETTSA 348
Cdd:cd05967 317 FWRVIEKYQVNALFTAPTAIRAIRKedpdGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDH-WWQTETGWP 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 349 IIITPEGDD----KPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPM---IMKGYVNNPEA--TSALIDKDGWLH 419
Cdd:cd05967 396 ITANPVGLEplpiKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLPLppgCLLTLWKNDERfkKLYLSKFPGYYD 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 420 SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMT----E 495
Cdd:cd05967 475 TGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaeelE 554
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 52631875 496 QEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREI 538
Cdd:cd05967 555 KELVALVREQIGPVAAFR-LVIFVKRLPKTRSGKILRRTLRKI 596
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
8-537 |
1.34e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 139.88 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 8 MHGPPPFYPLEDGTAGEQlhkamkryaqvPGTIAFTDAhaEVNITYSEYFEMACRLAETMKRYGLGLQHHIAV----CSE 83
Cdd:PRK06164 6 APRADTLASLLDAHARAR-----------PDAVALIDE--DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVwlpnCIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 84 N-SLQFFMPVCGALFIGVgvaptNDIYNERELYNSLSISQPTIVFCSKR----ALQKIL-GVQKK-LPIIQKIVILDSRE 156
Cdd:PRK06164 73 WvVLFLACARLGATVIAV-----NTRYRSHEVAHILGRGRARWLVVWPGfkgiDFAAILaAVPPDaLPPLRAIAVVDDAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 157 DYM------GKQSMYSFIESHLPAGFNEYDYIPDsfdretATALIMNSSGSTGLPKGVE------LTHKNICVRfshcrd 224
Cdd:PRK06164 148 DATpapapgARVQLFALPDPAPPAAAGERAADPD------AGALLFTTSGTTSGPKLVLhrqatlLRHARAIAR------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 225 pVFGnqIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKy 304
Cdd:PRK06164 216 -AYG--YDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 305 DLSNLHE--IASGGAPLAKEVGEAVAKRFKLPGIrqgYGLTETTSAIIITPEGDDKP----GACGKVVPFFSAKIVDLDT 378
Cdd:PRK06164 292 DFPSARLfgFASFAPALGELAALARARGVPLTGL---YGSSEVQALVALQPATDPVSvrieGGGRPASPEARVRARDPQD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 379 GKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESIL 458
Cdd:PRK06164 369 GALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHAL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 459 LQHPFIFDAGVAGIpDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKrLRGGVKFVDEVPKGLTG---KIDARKI 535
Cdd:PRK06164 449 EALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFK-VPARVQVVEAFPVTESAngaKIQKHRL 526
|
..
gi 52631875 536 RE 537
Cdd:PRK06164 527 RE 528
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
51-455 |
2.20e-35 |
|
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: 140.18 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIG---VGVAPTNDiyNERELYNSLSISQPTIVF 127
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGgiaVGIYTTNS--PEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 128 CSKRALQKILGVQKKLPIIQKIVILdsREDYMGKQ----SMYSFIESHLPAGFNEYDYIPDSFDRETATALIMNSsGSTG 203
Cdd:cd05933 87 ENQKQLQKILQIQDKLPHLKAIIQY--KEPLKEKEpnlySWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTS-GTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 204 LPKGVELTHKNIC------VRFSHCRDPVFGNQIIpdtaiLTVIPFHH----GFGMFTTL---------------GYLTC 258
Cdd:cd05933 164 MPKGVMLSHDNITwtakaaSQHMDLRPATVGQESV-----VSYLPLSHiaaqILDIWLPIkvggqvyfaqpdalkGTLVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 259 GFRIV----------LMYRCEEELFLRSLQDYKIQSALLV-------------------PTLFSFFAKSTLVDK----YD 305
Cdd:cd05933 239 TLREVrptafmgvprVWEKIQEKMKAVGAKSGTLKRKIASwakgvgletnlklmggespSPLFYRLAKKLVFKKvrkaLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 306 LSNLHEIASGGAPLAKEVgeavaKRFKLP---GIRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDTgktl 382
Cdd:cd05933 319 LDRCQKFFTGAAPISRET-----LEFFLSlniPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDA---- 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52631875 383 gvNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQ-VPPAELE 455
Cdd:cd05933 390 --DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIE 461
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
193-536 |
2.54e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 138.60 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGV--ELTHKNIcvrfSHCRDPV-------FGnqIIPDTAILTVIPFHHGF-----GMFTTLGYltc 258
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIqpDLPGRDV----DAPGDPIvaiarafYD--ISESDIYYSSAPIYHAAplrwcSMVHALGG--- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 259 gfRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAK--STLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKlPGI 336
Cdd:PRK13390 222 --TVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG-PIV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 337 RQGYGLTETTSAIII-TPEGDDKPGACGKVVpFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKD 415
Cdd:PRK13390 299 YEYYSSTEAHGMTFIdSPDWLAHPGSVGRSV-LGDLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPA 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 416 G--WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTM 493
Cdd:PRK13390 377 HpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 52631875 494 TEQ---EVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIR 536
Cdd:PRK13390 457 SDElarELIDYTRSRIAHYKAPR-SVEFVDELPRTPTGKLVKGLLR 501
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
51-471 |
2.74e-35 |
|
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: 139.48 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENS-----LQFFMPVCGALFIGVgvapTNDIYNErELYNSLSISQPTI 125
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRpewvwAELAAQAIGALSLGI----YQDSMAE-EVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 126 VFCS-KRALQKILGVQKKLPIIQKIVILDSREDYMGKQSMYSFIESHLPAGFNEYDYIPDSFDRETA------TALIMNS 198
Cdd:cd17641 87 VIAEdEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGLYEREVAagkgedVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 199 SGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHH-GFGMFTTLGYLTCGF----------------- 260
Cdd:cd17641 167 SGTTGKPKLAMLSHGNF---LGHCAAYLAADPLGPGDEYVSVLPLPWiGEQMYSVGQALVCGFivnfpeepetmmedlre 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 261 ---RIVL--------------------------MYRCEEELFLRSL-QDYKIQSALLVPTLFSFFAKSTLV----DKYDL 306
Cdd:cd17641 244 igpTFVLlpprvwegiaadvrarmmdatpfkrfMFELGMKLGLRALdRGKRGRPVSLWLRLASWLADALLFrplrDRLGF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 307 SNLHEIASGGAPLakevGEAVAKRFKLPGI--RQGYGLTETTSAIIITPEGDDKPGACGkvVPFfsakivdldTGKTLGV 384
Cdd:cd17641 324 SRLRSAATGGAAL----GPDTFRFFHAIGVplKQLYGQTELAGAYTVHRDGDVDPDTVG--VPF---------PGTEVRI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 385 NQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIK-YKGYQVPPAELESILLQHPF 463
Cdd:cd17641 389 DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPY 468
|
....*...
gi 52631875 464 IFDAGVAG 471
Cdd:cd17641 469 IAEAVVLG 476
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
193-493 |
8.81e-35 |
|
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: 137.35 E-value: 8.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNIcVRFSHCRDPVFGNQIIPDTAILTVIPFHHGFG-MFT--------TLGY-----LT- 257
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNL-VAGIAGLGDRVPELLGPDDRYLAYLPLAHIFElAAEnvclyrggTIGYgsprtLTd 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 258 ------CG----FRIVLM---------YR--CEEEL-----FLRSLQD--YKIQSALLVPTLFSF------FAKstlVDK 303
Cdd:cd17639 170 kskrgcKGdlteFKPTLMvgvpaiwdtIRkgVLAKLnpmggLKRTLFWtaYQSKLKALKEGPGTPlldelvFKK---VRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 304 YDLSNLHEIASGGAPLAKEvgeavAKRFK---LPGIRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDTGK 380
Cdd:cd17639 247 ALGGRLRYMLSGGAPLSAD-----TQEFLnivLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 381 --TLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYK-GYQVPPAELESI 457
Cdd:cd17639 322 ysTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESI 401
|
330 340 350
....*....|....*....|....*....|....*.
gi 52631875 458 LLQHPFIfdAGVAGIPDPDAgELPAAVVVLEEGKTM 493
Cdd:cd17639 402 YRSNPLV--NNICVYADPDK-SYPVAIVVPNEKHLT 434
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
28-513 |
9.50e-35 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 138.01 E-value: 9.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 28 KAMKRYAQVPGTIAFTDAHAEVNiTYSEYFEMACRLAETMKRYGLGLQHHIAVCSENS---LQFFMPVCgalFIGVGVAP 104
Cdd:PLN02860 11 QCLTRLATLRGNAVVTISGNRRR-TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSdlyLEWLLAVA---CAGGIVAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 105 TNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQK-KLPIIQKIVILDSREDYMGKQSMYSFIESHL------PAGFN 177
Cdd:PLN02860 87 LNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELQNdRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLkqralgTTELD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 178 eYDYIPDSfdretaTALIMNSSGSTGLPKGVELTHKNICVR-------FSHCRDPVFgnqiipdtaiLTVIPFHHGFGMF 250
Cdd:PLN02860 167 -YAWAPDD------AVLICFTSGTTGRPKGVTISHSALIVQslakiaiVGYGEDDVY----------LHTAPLCHIGGLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 251 TTLGYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSN--LHEIASGGAPLAKEVGEAVA 328
Cdd:PLN02860 230 SALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFpsVRKILNGGGSLSSRLLPDAK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 329 KRFKLPGIRQGYGLTETTSAI-------------IITPEGDDKP---------GAC-GKVVPFFSAKIVDLDTGKTlgvn 385
Cdd:PLN02860 310 KLFPNAKLFSAYGMTEACSSLtfmtlhdptlespKQTLQTVNQTksssvhqpqGVCvGKPAPHVELKIGLDESSRV---- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 386 qrGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIF 465
Cdd:PLN02860 386 --GRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVA 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 52631875 466 DAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLR 513
Cdd:PLN02860 464 SVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKENAKKNLTLSSETLR 511
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
189-530 |
1.16e-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: 135.72 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 189 ETATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfgnQIIPDTAILTVIPFHHGFGMF-TTLGYLTCGFRIVLMYR 267
Cdd:cd05973 87 DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAV---DLRPEDSFWNAADPGWAYGLYyAITGPLALGHPTILLEG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 268 C-EEELFLRSLQDYKIQSALLVPTLF-SFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTET 345
Cdd:cd05973 164 GfSVESTWRVIERLGVTNLAGSPTAYrLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVP-IHDHYGQTEL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 346 tSAIIITPEGDDKP---GACGKVVPFFSAKIVDLDtGKTLGVNQRGELCV---KGP-MIMKGYVNNPEATSAlidkDGWL 418
Cdd:cd05973 243 -GMVLANHHALEHPvhaGSAGRAMPGWRVAVLDDD-GDELGPGEPGRLAIdiaNSPlMWFRGYQLPDTPAID----GGYY 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 419 HSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLE---EGKTMTE 495
Cdd:cd05973 317 LTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRgghEGTPALA 396
|
330 340 350
....*....|....*....|....*....|....*
gi 52631875 496 QEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKI 530
Cdd:cd05973 397 DELQLHVKKRLSAHAYPR-TIHFVDELPKTPSGKI 430
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
49-537 |
1.76e-34 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 136.81 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 49 VNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFC 128
Cdd:PRK06018 38 VRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 129 SKRALQKILGVQKKLPIIQKIVILDSREdymgkqsmysfiesHLPA-------GFNEY------DYIPDSFDRETATALI 195
Cdd:PRK06018 118 DLTFVPILEKIADKLPSVERYVVLTDAA--------------HMPQttlknavAYEEWiaeadgDFAWKTFDENTAAGMC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 196 MnSSGSTGLPKGVELTHKnicvrfSHCRDPVFGNQiiPDT-------AILTVIPFHHGFGMFTTLGYLTCGFRIVL---- 264
Cdd:PRK06018 184 Y-TSGTTGDPKGVLYSHR------SNVLHALMANN--GDAlgtsaadTMLPVVPLFHANSWGIAFSAPSMGTKLVMpgak 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 265 -----MYrceeELflrsLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAkevgEAVAKRFKLPGI--R 337
Cdd:PRK06018 255 ldgasVY----EL----LDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP----RSMIKAFEDMGVevR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 QGYGLTETT---SAIIITPEGDDKPGACGKVV-------PF-FSAKIVDlDTGKTLGVNQR--GELCVKGPMIMKGYVnn 404
Cdd:PRK06018 323 HAWGMTEMSplgTLAALKPPFSKLPGDARLDVlqkqgypPFgVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYY-- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 405 pEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAV 484
Cdd:PRK06018 400 -RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLI 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 52631875 485 VVLEEGKTMTEQEVMDYVAGQVtASKRLRGGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK06018 479 VQLKPGETATREEILKYMDGKI-AKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
183-469 |
8.10e-34 |
|
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: 132.77 E-value: 8.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 183 PDSFDRETATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPvfgNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRI 262
Cdd:TIGR01733 113 PDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARR---YGLDPDDRVLQFASLSFDASVEEIFGALLAGATL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 263 VLMY----RCEEELFLRSLQDYKIQSALLVPTLFSFFAkstLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQ 338
Cdd:TIGR01733 190 VVPPedeeRDDAALLAALIAEHPVTVLNLTPSLLALLA---AALPPALASLRLVILGGEALTPALVDRWRARGPGARLIN 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 339 GYGLTETT---SAIIITPEGDDKPGAC--GKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATS---- 409
Cdd:TIGR01733 267 LYGPTETTvwsTATLVDPDDAPRESPVpiGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAerfv 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52631875 410 ----ALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGV 469
Cdd:TIGR01733 346 pdpfAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
267-537 |
1.49e-32 |
|
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: 129.61 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 267 RCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVdKYDLSnLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTETT 346
Cdd:cd05974 162 RFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLA-SFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 347 SAIIITPEGDDKPGACGKVVPFFSAKIVDLDTGKTlgvnQRGELCV----KGPM-IMKGYVNNPEATSALIdKDGWLHSG 421
Cdd:cd05974 239 ALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPA----TEGEVALdlgdTRPVgLMKGYAGDPDKTAHAM-RGGYYRTG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 422 DIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEG---KTMTEQEV 498
Cdd:cd05974 314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyepSPETALEI 393
|
250 260 270
....*....|....*....|....*....|....*....
gi 52631875 499 MDYVAGQVTASKRLRgGVKFVdEVPKGLTGKIDARKIRE 537
Cdd:cd05974 394 FRFSRERLAPYKRIR-RLEFA-ELPKTISGKIRRVELRR 430
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
183-537 |
1.59e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 127.87 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 183 PDSFDRETATALIM--NSSGSTGLPKGVELTHKNICV-------RFSHCRDpvfgnqiipDTAILTVIPFHHGFGMFTTL 253
Cdd:PRK07867 143 EPPFRVADPDDLFMliFTSGTSGDPKAVRCTHRKVASagvmlaqRFGLGPD---------DVCYVSMPLFHSNAVMAGWA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 254 GYLTCGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSF-FAKSTLVDkyDLSNLHEIASGGAPLAKEVgEAVAKRFk 332
Cdd:PRK07867 214 VALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYvLATPERPD--DADNPLRIVYGNEGAPGDI-ARFARRF- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 333 lpGIR--QGYGLTETtsAIIITPEGDDKPGACGKVVPffSAKIVDLDTGK------------TLGVNQRGELC-VKGPMI 397
Cdd:PRK07867 290 --GCVvvDGFGSTEG--GVAITRTPDTPPGALGPLPP--GVAIVDPDTGTecppaedadgrlLNADEAIGELVnTAGPGG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 398 MKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDA 477
Cdd:PRK07867 364 FEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVV 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52631875 478 GELPAAVVVLEEGKTMTEQEVMDYVAGQVT-ASKRLRGGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK07867 443 GDQVMAALVLAPGAKFDPDAFAEFLAAQPDlGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-533 |
1.14e-30 |
|
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: 122.88 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 194 LIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVFGNQII-----------PDTAILTVIPFHHGFGMFTTLGYLTCGFRI 262
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPsedahkaaaaaAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 263 VLM-YRCEEELFLRSLQDYKIQSALLVPTLFsffAKStLVDK------YDLSNLHEIASGGAPLAKEVGEAVAKRFKLPG 335
Cdd:cd05924 87 VLPdDRFDPEEVWRTIEKHKVTSMTIVGDAM---ARP-LIDAlrdagpYDLSSLFAISSGGALLSPEVKQGLLELVPNIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 336 IRQGYGLTETTSAIIITPEGddKPGACGKVVPFFSAKIVDLDTGKTL--GVNQRGELCVKGpMIMKGYVNNPEATSAL-- 411
Cdd:cd05924 163 LVDAFGSSETGFTGSGHSAG--SGPETGPFTRANPDTVVLDDDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETfp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 412 -IDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEG 490
Cdd:cd05924 240 eVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 52631875 491 KTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDAR 533
Cdd:cd05924 320 AGVDLEELREHCRTRIARYKLPK-QVVFVDEIERSPAGKADYR 361
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
46-547 |
7.44e-30 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 123.42 E-value: 7.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 46 HAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSEN-----SLQFFMPVCGALFIGVGV---APTNDIYNERELYNS 117
Cdd:PLN02479 41 HGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNipamyEAHFGVPMAGAVVNCVNIrlnAPTIAFLLEHSKSEV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 118 LSISQP--TIVFCSKRALQKILGVQKKLPIIqkIVILDSREDYMGKQSMYSF----IESHLPAGFNEYDYIPDSfDRETA 191
Cdd:PLN02479 121 VMVDQEffTLAEEALKILAEKKKSSFKPPLL--IVIGDPTCDPKSLQYALGKgaieYEKFLETGDPEFAWKPPA-DEWQS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMnSSGSTGLPKGVELTHKNICVRfshcrdpVFGNQII---PDTAI-LTVIPFHHGFGM-FT-TLGYLtCGFRIVLM 265
Cdd:PLN02479 198 IALGY-TSGTTASPKGVVLHHRGAYLM-------ALSNALIwgmNEGAVyLWTLPMFHCNGWcFTwTLAAL-CGTNICLR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 YRCEEELFlRSLQDYKIQSALLVPTLFSFFAKSTLVDKY-DLSNL-HEIASGGAPLAKEVGEAVAKRFKlpgIRQGYGLT 343
Cdd:PLN02479 269 QVTAKAIY-SAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVvHVMTAGAAPPPSVLFAMSEKGFR---VTHTYGLS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 344 ETTSAIII---TPEGDDKPGA------CGKVVPFFSAK---IVDLDTGKTLGVNQR--GELCVKGPMIMKGYVNNPEATS 409
Cdd:PLN02479 345 ETYGPSTVcawKPEWDSLPPEeqarlnARQGVRYIGLEgldVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANE 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 410 ALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEE 489
Cdd:PLN02479 425 EAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKP 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52631875 490 G-----KTMTEQEVMDYVAGQVTASKRLRGGVkfVDEVPKGLTGKIDARKIR-EILMMG--KKSKL 547
Cdd:PLN02479 504 GvdksdEAALAEDIMKFCRERLPAYWVPKSVV--FGPLPKTATGKIQKHVLRaKAKEMGpvKKSRL 567
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
51-537 |
1.07e-28 |
|
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: 119.35 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSK 130
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 131 RalqkilgVQKKLPIIQKIvildsreDYMGKQSMYSFIESHLPagfneydyiPDSfdRETATALIMNSSGSTGLPKGVEL 210
Cdd:cd17655 103 H-------LQPPIAFIGLI-------DLLDEDTIYHEESENLE---------PVS--KSDDLAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 211 THKNIcvrfSHCRDpvFGNQIIPDTAILTVI---PFHHGFGMFTTLGYLTCGFRIVLmYRCEE----ELFLRSLQDYKIQ 283
Cdd:cd17655 158 EHRGV----VNLVE--WANKVIYQGEHLRVAlfaSISFDASVTEIFASLLSGNTLYI-VRKETvldgQALTQYIRQNRIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 284 SALLVPTLFSFFAKstlVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKL-PGIRQGYGLTETT---SAIIITPEGDDKP 359
Cdd:cd17655 231 IIDLTPAHLKLLDA---ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTvdaSIYQYEPETDQQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 360 G-ACGKvvPFFSAKIVDLDT-GKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWL------HSGDIAYYDKDGH 431
Cdd:cd17655 308 SvPIGK--PLGNTRIYILDQyGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 432 FFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVV------LEEGKTMTEQEVMDYvagq 505
Cdd:cd17655 386 IEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVsekelpVAQLREFLARELPDY---- 461
|
490 500 510
....*....|....*....|....*....|..
gi 52631875 506 VTASKRLRggvkfVDEVPKGLTGKIDARKIRE 537
Cdd:cd17655 462 MIPSYFIK-----LDEIPLTPNGKVDRKALPE 488
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
30-537 |
1.68e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 119.28 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 30 MKRYAQV-PGTIAFTdaHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENS-----LQFFMPVCGALFigvgva 103
Cdd:PRK08162 24 LERAAEVyPDRPAVI--HGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIpamveAHFGVPMAGAVL------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 104 ptndiynerelyNSLSI--SQPTIVFCSKRALQKILGVQ-----------KKLPIIQKIVILDSREDYMGKQSMYSF-IE 169
Cdd:PRK08162 96 ------------NTLNTrlDAASIAFMLRHGEAKVLIVDtefaevarealALLPGPKPLVIDVDDPEYPGGRFIGALdYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 170 SHLPAGFNEYDYIP--DSFDretatALIMN-SSGSTGLPKGVELTHK--------NIcVRFSHCRDPVFgnqiipdtaiL 238
Cdd:PRK08162 164 AFLASGDPDFAWTLpaDEWD-----AIALNyTSGTTGNPKGVVYHHRgaylnalsNI-LAWGMPKHPVY----------L 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 239 TVIP-FH-----HGFGMFTTLGYLTCgfrivlMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSnlHEI 312
Cdd:PRK08162 228 WTLPmFHcngwcFPWTVAARAGTNVC------LRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGID--HPV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 313 AS--GGAPLAKEVGEAVAKR-FKLpgiRQGYGLTETTSAIIIT---PEGDDKPGACGKV------VPFF---SAKIVDLD 377
Cdd:PRK08162 300 HAmvAGAAPPAAVIAKMEEIgFDL---THVYGLTETYGPATVCawqPEWDALPLDERAQlkarqgVRYPlqeGVTVLDPD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 378 T-------GKTLGvnqrgELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVP 450
Cdd:PRK08162 377 TmqpvpadGETIG-----EIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENIS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 451 PAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKFvDEVPKGLTGKI 530
Cdd:PRK08162 451 SIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPK-AVVF-GELPKTSTGKI 528
|
....*..
gi 52631875 531 DARKIRE 537
Cdd:PRK08162 529 QKFVLRE 535
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
194-540 |
3.05e-28 |
|
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: 119.13 E-value: 3.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 194 LIMNSSGSTGLPKGVELTHKNICVRFShcRDPVFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLM-----YRC 268
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAA--QDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYdgapdHPK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEELFlRSLQDYKIQSALLVPTLF-SFFAKST-LVDKYDLSNLHEIASGGAPLAKE----VGEAVAKRfKLPGIRQGYGl 342
Cdd:cd05968 318 ADRLW-RMVEDHEITHLGLSPTLIrALKPRGDaPVNAHDLSSLRVLGSTGEPWNPEpwnwLFETVGKG-RNPIINYSGG- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 343 TETTSAII----ITPEgddKPGACGKVVPFFSAKIVDlDTGKTLgVNQRGELCVKGPMI--MKGYVNNPEA-TSALIDK- 414
Cdd:cd05968 395 TEISGGILgnvlIKPI---KPSSFNGPVPGMKADVLD-ESGKPA-RPEVGELVLLAPWPgmTRGFWRDEDRyLETYWSRf 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 415 -DGWLHsGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTM 493
Cdd:cd05968 470 dNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTP 548
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 52631875 494 TE---QEVMDYVA---GQVTASKRLRggvkFVDEVPKGLTGKIDARKIREILM 540
Cdd:cd05968 549 TEalaEELMERVAdelGKPLSPERIL----FVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
199-539 |
1.07e-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: 116.10 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 199 SGSTGLPKGVELTHKNICVRF-SHCRdpVFGnqIIPDTAILTvipF-HHGFG-----MFTTLgylTCGFRIvlmyrC--- 268
Cdd:cd05918 115 SGSTGKPKGVVIEHRALSTSAlAHGR--ALG--LTSESRVLQ---FaSYTFDvsileIFTTL---AAGGCL-----Cips 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEEL---FLRSLQDYKIQSALLVPTLFSffakstLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLpgiRQGYGLTET 345
Cdd:cd05918 180 EEDRlndLAGFINRLRVTWAFLTPSVAR------LLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRL---INAYGPAEC 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 346 T-SAIIITPEGDDKPGACGKVVPFfSAKIVDLDT-GKTLGVNQRGELCVKGPMIMKGYVNNPEATS-ALIDKDGWLH--- 419
Cdd:cd05918 251 TiAATVSPVVPSTDPRNIGRPLGA-TCWVVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAaAFIEDPAWLKqeg 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 420 ---------SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQH-PFIFDAGVAGIPDPDAGELPAAVVVLEE 489
Cdd:cd05918 330 sgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDGSSSPQLVAFVVL 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 490 GKTMTEQEVMDYVAGQVTAS-----KRLRGGVK-------------FVDEVPKGLTGKIDARKIREIL 539
Cdd:cd05918 410 DGSSSGSGDGDSLFLEPSDEfralvAELRSKLRqrlpsymvpsvflPLSHLPLTASGKIDRRALRELA 477
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
32-539 |
1.14e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 116.63 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 32 RYAQvPGTIAFTDAhaEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMpVCGALFiGVGVAPTNDIYNE 111
Cdd:PRK10946 33 RHAA-SDAIAVICG--ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYI-TFFALL-KLGVAPVNALFSH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 112 RELYNSLSISQ--PTIVFCSKR-AL----QKILGVQKKLPIIQkiVILDSREDymGKQSMYSFIEShlPAGfnEYDYIPD 184
Cdd:PRK10946 108 QRSELNAYASQiePALLIADRQhALfsddDFLNTLVAEHSSLR--VVLLLNDD--GEHSLDDAINH--PAE--DFTATPS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 185 SFDRetaTALIMNSSGSTGLPKGVELTHKNI--CVRFSH--CrdpvfgnQIIPDTAILTVIPFHHGFGMFT--TLGYLTC 258
Cdd:PRK10946 180 PADE---VAFFQLSGGSTGTPKLIPRTHNDYyySVRRSVeiC-------GFTPQTRYLCALPAAHNYPMSSpgALGVFLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 259 GFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLVDKYDLSNLHEIASGGAPLAkevgEAVAKRF-KLPG 335
Cdd:PRK10946 250 GGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWlqAIAEGGSRAQLASLKLLQVGGARLS----ETLARRIpAELG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 336 IR--QGYGLTE---------TTSAIIITPEG-----DDKpgacgkvvpffsAKIVDLDtGKTLGVNQRGELCVKGPMIMK 399
Cdd:PRK10946 326 CQlqQVFGMAEglvnytrldDSDERIFTTQGrpmspDDE------------VWVADAD-GNPLPQGEVGRLMTRGPYTFR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 400 GYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGE 479
Cdd:PRK10946 393 GYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGE 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52631875 480 LPAAVVVLEEG-------KTMTEQEVMDYvagqvtaskRLRGGVKFVDEVPKGLTGKIDARKIREIL 539
Cdd:PRK10946 473 KSCAFLVVKEPlkavqlrRFLREQGIAEF---------KLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
194-537 |
3.01e-27 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 115.63 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 194 LIMNSSGSTGLPKGVelthknicvrfshcRDPVFGNqIIPDTAILTVIPFHHG------FGMFTTLGY--------LTCg 259
Cdd:PRK13382 200 VILLTSGTTGTPKGA--------------RRSGPGG-IGTLKAILDRTPWRAEeptvivAPMFHAWGFsqlvlaasLAC- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 260 fRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFF--AKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKlPGIR 337
Cdd:PRK13382 264 -TIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRImdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG-DVIY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 QGYGLTETTSAIIITPEGDDK-PGACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVnnPEATSALIDkdG 416
Cdd:PRK13382 342 NNYNATEAGMIATATPADLRAaPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGYT--SGSTKDFHD--G 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 417 WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQ 496
Cdd:PRK13382 417 FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPE 496
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 52631875 497 EVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK13382 497 TLKQHVRDNLANYKVPR-DIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
34-533 |
3.42e-27 |
|
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: 114.75 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 34 AQVPGTIAFTDAHAEVniTYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERE 113
Cdd:cd17651 6 ARTPDAPALVAEGRRL--TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 114 LYNSLSISQPTIVfcskrALQKilGVQKKLPIIQKIVILDSREDymgkqsmysfieshLPAGfneydyIPDSFDRETA-- 191
Cdd:cd17651 84 LAFMLADAGPVLV-----LTHP--ALAGELAVELVAVTLLDQPG--------------AAAG------ADAEPDPALDad 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 -TALIMNSSGSTGLPKGVELTHKNIC--VRFsHCRdpVFGnqIIPDTAILTVIPFhhGFGMFT--TLGYLTCGFRIVLM- 265
Cdd:cd17651 137 dLAYVIYTSGSTGRPKGVVMPHRSLAnlVAW-QAR--ASS--LGPGARTLQFAGL--GFDVSVqeIFSTLCAGATLVLPp 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 --YRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAkeVGEAVAKRFK-LPGIR--QGY 340
Cdd:cd17651 210 eeVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLV--LTEDLREFCAgLPGLRlhNHY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 341 GLTETTSAIIITPEGD----DKPGACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDG 416
Cdd:cd17651 288 GPTETHVVTALSLPGDpaawPAPPPIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 417 WL------HSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEG 490
Cdd:cd17651 367 FVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 52631875 491 KTMTEQEVMDYVAGQVTASKRLRGGVKfVDEVPKGLTGKIDAR 533
Cdd:cd17651 447 APVDAAELRAALATHLPEYMVPSAFVL-LDALPLTPNGKLDRR 488
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
49-490 |
4.95e-27 |
|
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: 114.49 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 49 VNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFM---PVCGALFIGVGVAPTndiynerelynslsISQPTI 125
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFItdlAIWMAGHISVPLYPT--------------LNPDTI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 126 VFCSKRALQKILGVQKklpiiqkiviLDSREDYMG--KQSMYSFIESHLPAGFNEYDY------------IPDSFDRETA 191
Cdd:cd05932 71 RYVLEHSESKALFVGK----------LDDWKAMAPgvPEGLISISLPPPSAANCQYQWddliaqhppleeRPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TalIMNSSGSTGLPKGVELTHKNICvrFShCRDPVFGNQIIPDTAILTVIPFHHGFG-MFTTLGYLTCGFRIVLMyrceE 270
Cdd:cd05932 141 T--LIYTSGTTGQPKGVMLTFGSFA--WA-AQAGIEHIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVAFA----E 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 271 EL--FLRSLQDYKIQSALLVPTLFSFFAK--------------------STLVDKYDLSNL-----HEIASGGAPLAKEV 323
Cdd:cd05932 212 SLdtFVEDVQRARPTLFFSVPRLWTKFQQgvqdkipqqklnlllkipvvNSLVKRKVLKGLgldqcRLAGCGSAPVPPAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 324 GEAVaKRFKLPgIRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDldtgktlgvnqRGELCVKGPMIMKGYVN 403
Cdd:cd05932 292 LEWY-RSLGLN-ILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYYK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 404 NPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPFIFDAGVAGIPDPDagelPA 482
Cdd:cd05932 359 DPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA----PL 434
|
....*...
gi 52631875 483 AVVVLEEG 490
Cdd:cd05932 435 ALVVLSEE 442
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
188-538 |
6.97e-27 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 115.83 E-value: 6.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 188 RETATALIMNSSGSTGLPKGVELTHKNIC---------VRFSHcRDPVFgnqiipdtailTVIPFHHGFGMFT-TLGYLT 257
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLanraqvaarIDFSP-EDKVF-----------NALPVFHSFGLTGgLVLPLL 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 258 CGFRIVLM-----YRCEEELFlrslqdYKIQSALLV--PTLFSFFAKSTlvDKYDLSNLHEIASGGAPLAKEVGEAVAKR 330
Cdd:PRK06814 859 SGVKVFLYpsplhYRIIPELI------YDTNATILFgtDTFLNGYARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEK 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 331 FklpGIR--QGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDtgktlGVNQRGELCVKGPMIMKGYV--NNPE 406
Cdd:PRK06814 931 F---GIRilEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVP-----GIDEGGRLFVRGPNVMLGYLraENPG 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 407 ATSALidKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESI---LLQhpfifDAG--VAGIPDPDAGElp 481
Cdd:PRK06814 1003 VLEPP--ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELaaeLWP-----DALhaAVSIPDARKGE-- 1073
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52631875 482 aAVVVLEEGKTMTEQEVMDYV----AGQVTASKRlrggVKFVDEVPKGLTGKIDARKIREI 538
Cdd:PRK06814 1074 -RIILLTTASDATRAAFLAHAkaagASELMVPAE----IITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
126-489 |
7.05e-27 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 115.20 E-value: 7.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 126 VFCSKRALQKILGVQKKLPIIQKIVILDSREDYM-------GKQSM-YSFIESHLPAgfNEYDYIPDsfdRETATALIMN 197
Cdd:PLN02736 154 IFCVPQTLNTLLSCLSEIPSVRLIVVVGGADEPLpslpsgtGVEIVtYSKLLAQGRS--SPQPFRPP---KPEDVATICY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 198 SSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLmYRCEeelFLRSL 277
Cdd:PLN02736 229 TSGTTGTPKGVVLTHGNL---IANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGF-YQGD---NLKLM 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 278 QDYkiqsALLVPTLFS-------------------------------FFAK----------STLVDKYDLSNLHE----- 311
Cdd:PLN02736 302 DDL----AALRPTIFCsvprlynriydgitnavkesgglkerlfnaaYNAKkqalengknpSPMWDRLVFNKIKAklggr 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 312 ---IASGGAPLAKEVGEAVakRFKLPG-IRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDTGKTLGVNQ- 386
Cdd:PLN02736 378 vrfMSSGASPLSPDVMEFL--RICFGGrVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQp 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 387 --RGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPF 463
Cdd:PLN02736 456 ypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVYAKCKF 535
|
410 420
....*....|....*....|....*.
gi 52631875 464 IFDAGVAGipDPDAGELPAAVVVLEE 489
Cdd:PLN02736 536 VAQCFVYG--DSLNSSLVAVVVVDPE 559
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
191-533 |
1.71e-26 |
|
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: 112.68 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 191 ATALIMNSSGSTGLPKGVELTHKNIcVRFshCRDPVFGnQIIPDTAILTVIPfhHGF--GMFTTLGYLTCGFRIVLmyrC 268
Cdd:cd12117 137 DLAYVMYTSGSTGRPKGVAVTHRGV-VRL--VKNTNYV-TLGPDDRVLQTSP--LAFdaSTFEIWGALLNGARLVL---A 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEELFL--RSLQDY----KIQSALLVPTLFSffaksTLVDKYD--LSNLHEIASGG----APLAKEVGEAVakrfklPGI 336
Cdd:cd12117 208 PKGTLLdpDALGALiaeeGVTVLWLTAALFN-----QLADEDPecFAGLRELLTGGevvsPPHVRRVLAAC------PGL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 337 R--QGYGLTETT--SAIIITPEGDDKPGAC--GKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSA 410
Cdd:cd12117 277 RlvNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 411 LIDKDGWL------HSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAV 484
Cdd:cd12117 356 RFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAY 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 52631875 485 VVLEEGKtmTEQEVMDYVAgqvtasKRLRGG-----VKFVDEVPKGLTGKIDAR 533
Cdd:cd12117 436 VVAEGAL--DAAELRAFLR------ERLPAYmvpaaFVVLDELPLTANGKVDRR 481
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
179-539 |
2.96e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 113.30 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 179 YDYIPdsfdRETATAL-IMNSSGSTGLPKGVELTHKN--ICVRFSH-CRDPVFGNQIIPDTAILTVIPFHHGFgmfttLG 254
Cdd:PTZ00237 246 YEYVP----VESSHPLyILYTSGTTGNSKAVVRSNGPhlVGLKYYWrSIIEKDIPTVVFSHSSIGWVSFHGFL-----YG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 255 YLTCGFRIVlMY-------RCEEELFLRSLQDYKIQSALLVPTLFSFFAK-----STLVDKYDLSNLHEIASGGAPLAKE 322
Cdd:PTZ00237 317 SLSLGNTFV-MFeggiiknKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYDLSNLKEIWCGGEVIEES 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 323 VGEAVAKRFKLPGIRqGYGLTETTSAIIITPEGDDKP-GACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPM---IM 398
Cdd:PTZ00237 396 IPEYIENKLKIKSSR-GYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSED-GKELNVNEIGEVAFKLPMppsFA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 399 KGYVNNPEATSALIDK-DGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDA 477
Cdd:PTZ00237 474 TTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDC 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52631875 478 GELPAAVVVLEEGKTMT-------EQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIdarkIREIL 539
Cdd:PTZ00237 554 YNVPIGLLVLKQDQSNQsidlnklKNEINNIITQDIESLAVLR-KIIIVNQLPKTKTGKI----PRQII 617
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
30-537 |
5.47e-26 |
|
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: 111.37 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 30 MKRYAQVPGTIAFTDahaeVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSEN-----SLQFFMPVCGALFIGVgvap 104
Cdd:cd05915 8 FGRKEVVSRLHTGEV----HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNhfrhlEAYFAVPGMGAVLHTA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 105 tNDIYNERELYNSLSISQPTIVFCSkralQKILGVQKklpiiQKIVILDSREDYMGKQSMYSFIESHLPAGFNEYDYIpD 184
Cdd:cd05915 80 -NPRLSPKEIAYILNHAEDKVLLFD----PNLLPLVE-----AIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADP-V 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 185 SFDRETATALIMnSSGSTGLPKGVELTHknicvRFSHCRDPVFG--NQII--PDTAILTVIPFHHGFG---MFTTLGYlt 257
Cdd:cd05915 149 RVPERAACGMAY-TTGTTGLPKGVVYSH-----RALVLHSLAASlvDGTAlsEKDVVLPVVPMFHVNAwclPYAATLV-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 258 CGFRIVLMYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAkevgEAVAKRFKLPGIR 337
Cdd:cd05915 221 GAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAP----RSLIARFERMGVE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 --QGYGLTET---TSAIIITPEGDDKP-------GACGKVVPFfsAKIVDLDTGKTLGVNQRGE----LCVKGPMIMKGY 401
Cdd:cd05915 297 vrQGYGLTETspvVVQNFVKSHLESLSeeekltlKAKTGLPIP--LVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 402 VNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELP 481
Cdd:cd05915 375 YGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERP 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 52631875 482 AAVVVLEEGKTmTEQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:cd05915 455 LAVVVPRGEKP-TPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
194-530 |
6.89e-26 |
|
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: 111.90 E-value: 6.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 194 LIMNSSGSTGLPKGVELTHKNICVR----FSHCRDPVFGNQIIPDTAILTVIPfhhgfGMFTTLGYLTCGfRIVLMYRC- 268
Cdd:cd17634 236 FILYTSGTTGKPKGVLHTTGGYLVYaattMKYVFDYGPGDIYWCTADVGWVTG-----HSYLLYGPLACG-ATTLLYEGv 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 ----EEELFLRSLQDYKIQSALLVPTLFSFFAKS--TLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRF---KLPGIRQG 339
Cdd:cd17634 310 pnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIgkeKCPVVDTW 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 340 YGlTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDT-GKTLGVNQRGELCVKGP---MIMKGYVNNPE-ATSALIDK 414
Cdd:cd17634 390 WQ-TETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNeGHPQPGGTEGNLVITDPwpgQTRTLFGDHERfEQTYFSTF 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 415 DGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMT 494
Cdd:cd17634 469 KGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPS 548
|
330 340 350
....*....|....*....|....*....|....*....
gi 52631875 495 EQ---EVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKI 530
Cdd:cd17634 549 PElyaELRNWVRKEIGPLATPD-VVHWVDSLPKTRSGKI 586
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
182-493 |
1.72e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 110.84 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 182 IPDSFDretATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfgNQII----PDTAILTVIPFHH------------ 245
Cdd:PTZ00216 259 IPENND---DLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRL--NDLIgppeEDETYCSYLPLAHimefgvtnifla 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 246 -----GFGMFTTLGYLT---CG----FRIVL---------MYR--CEEEL-----FLRSLQDYKIQSALlvptlfsffak 297
Cdd:PTZ00216 334 rgaliGFGSPRTLTDTFarpHGdlteFRPVFligvprifdTIKkaVEAKLppvgsLKRRVFDHAYQSRL----------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 298 STLVDKYDL----------------SNLHEIASGGAPLAKEVGEAVAKRFKLpgIRQGYGLTETTSAIIITPEGDDKPGA 361
Cdd:PTZ00216 403 RALKEGKDTpywnekvfsapravlgGRVRAMLSGGGPLSAATQEFVNVVFGM--VIQGWGLTETVCCGGIQRTGDLEPNA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 362 CGKVVPFFSAKIVDLDTGK-TLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKS 440
Cdd:PTZ00216 481 VGQLLKGVEMKLLDTEEYKhTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKA 560
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 52631875 441 LIK-YKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELpAAVVVLEEGKTM 493
Cdd:PTZ00216 561 LAKnCLGEYIALEALEALYGQNELVVPNGVCVLVHPARSYI-CALVLTDEAKAM 613
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
51-464 |
2.30e-25 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 110.59 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAptnDIY---NERELYNSLSISQPTIVF 127
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVV---TIYaslGEEALCHSLNETEVTTVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 128 CSKRALQKILGVQKKLPIIQKIVILDSRED-------YMGKQSMYSFIE-------SHLPAGFneydyiPDSFDretaTA 193
Cdd:PLN02387 184 CDSKQLKKLIDISSQLETVKRVIYMDDEGVdsdsslsGSSNWTVSSFSEveklgkeNPVDPDL------PSPND----IA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 194 LIMNSSGSTGLPKGVELTHKNICVRFSHCRdpvfgnQIIPDTA----ILTVIPFHHGFG------MFTT---LGY---LT 257
Cdd:PLN02387 254 VIMYTSGSTGLPKGVMMTHGNIVATVAGVM------TVVPKLGkndvYLAYLPLAHILElaaesvMAAVgaaIGYgspLT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 258 cgfrivlmyrceeelflrsLQDY--KIQ------SALLVPTLFSFF----------------AKSTLVDK-YDLSNLHEI 312
Cdd:PLN02387 328 -------------------LTDTsnKIKkgtkgdASALKPTLMTAVpaildrvrdgvrkkvdAKGGLAKKlFDIAYKRRL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 313 A-------------------------------------SGGAPLAKEVGEAVAKRFKLPgIRQGYGLTETTSAIIITPEG 355
Cdd:PLN02387 389 AaiegswfgawglekllwdalvfkkiravlggrirfmlSGGAPLSGDTQRFINICLGAP-IGQGYGLTETCAGATFSEWD 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 356 DDKPGACGKVVPFFSAKIVDLDTGKTLGVNQ---RGELCVKGPMIMKGYVNNPEATSAL--IDKDG--WLHSGDIAYYDK 428
Cdd:PLN02387 468 DTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHP 547
|
490 500 510
....*....|....*....|....*....|....*..
gi 52631875 429 DGHFFIVDRLKSLIKYK-GYQVPPAELESILLQHPFI 464
Cdd:PLN02387 548 DGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYV 584
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
195-538 |
4.86e-25 |
|
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: 109.19 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 195 IMNSSGSTGLPKGVE-----------LTHKNIcvrFSHCRDPVFGNqiipdTAILTVIPFHHgfgmFTTLGYLTCGfRIV 263
Cdd:cd05966 236 ILYTSGSTGKPKGVVhttggyllyaaTTFKYV---FDYHPDDIYWC-----TADIGWITGHS----YIVYGPLANG-ATT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 264 LMY----------RceeelFLRSLQDYKIQSALLVPTLFSFFAK--STLVDKYDLSNLHEIASGGAPLAKE--------V 323
Cdd:cd05966 303 VMFegtptypdpgR-----YWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVLGSVGEPINPEawmwyyevI 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 324 GEavakrFKLPgIRQGYGLTETTSaIIITP---EGDDKPGACGKvvPFF--SAKIVDLDTGKtLGVNQRGELCVKGPM-- 396
Cdd:cd05966 378 GK-----ERCP-IVDTWWQTETGG-IMITPlpgATPLKPGSATR--PFFgiEPAILDEEGNE-VEGEVEGYLVIKRPWpg 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 397 IMKGYVNNPEA--TSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPD 474
Cdd:cd05966 448 MARTIYGDHERyeDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPH 527
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52631875 475 PDAGELPAAVVVLEEGKTMT---EQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGKIDARKIREI 538
Cdd:cd05966 528 DIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEIGPIATPD-KIQFVPGLPKTRSGKIMRRILRKI 593
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
34-530 |
7.02e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 108.16 E-value: 7.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 34 AQVPGTIAFTDAHAEvnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERE 113
Cdd:PRK13383 46 ARWPGRTAIIDDDGA--LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 114 LYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVIldSREDYMGKQSMysfieshLPAGfneydyipdsfdretatA 193
Cdd:PRK13383 124 LAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATA--GAEESGGRPAV-------AAPG-----------------R 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 194 LIMNSSGSTGLPKGVElthknicvRFSHCRDPVFGNQIIPDTAILTV-------IPFHHGFGMFTTLGYLTCGFRIVLMY 266
Cdd:PRK13383 178 IVLLTSGTTGKPKGVP--------RAPQLRSAVGVWVTILDRTRLRTgsrisvaMPMFHGLGLGMLMLTIALGGTVLTHR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 267 RCEEELFLRSLQDYKIQSALLVPTLFSFFAKstLVDKYDLSN----LHEIASGGAPLAKEVGEAVAKRFKlPGIRQGYGL 342
Cdd:PRK13383 250 HFDAEAALAQASLHRADAFTAVPVVLARILE--LPPRVRARNplpqLRVVMSSGDRLDPTLGQRFMDTYG-DILYNGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 343 TETTSAIIITP-EGDDKPGACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNpeATSALIDkdGWLHSG 421
Cdd:PRK13383 327 TEVGIGALATPaDLRDAPETVGKPVAGCPVRILDRN-NRPVGPRVTGRIFVGGELAGTRYTDG--GGKAVVD--GMTSTG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 422 DIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDY 501
Cdd:PRK13383 402 DMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDY 481
|
490 500
....*....|....*....|....*....
gi 52631875 502 VAGQVTASKRLRgGVKFVDEVPKGLTGKI 530
Cdd:PRK13383 482 LKDRVSRFEQPR-DINIVSSIPRNPTGKV 509
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
138-539 |
7.20e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 108.26 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 138 GVQKKLPIIQKIVILdSREDYMGKQSM-YSFIESHLPAGFNEYDYiPdSFDRETATALIMnSSGSTGLPKGVELTHKNIC 216
Cdd:PRK07008 127 ALAPQCPNVKGWVAM-TDAAHLPAGSTpLLCYETLVGAQDGDYDW-P-RFDENQASSLCY-TSGTTGNPKGALYSHRSTV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 217 VrfsHcrdpVFGNQIiPDT-------AILTVIP-FH-HGFGmfttLGY---LTcGFRIVL---------MYrceeELFlr 275
Cdd:PRK07008 203 L---H----AYGAAL-PDAmglsardAVLPVVPmFHvNAWG----LPYsapLT-GAKLVLpgpdldgksLY----ELI-- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 276 slQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTE-----TTSAIi 350
Cdd:PRK07008 264 --EAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVE-VIHAWGMTEmsplgTLCKL- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 351 iTPEGDDKPGAC--------GKVVPFFSAKIVDlDTGKTL---GVNQrGELCVKGPMIMKGYVNNpeATSALIDkdGWLH 419
Cdd:PRK07008 340 -KWKHSQLPLDEqrkllekqGRVIYGVDMKIVG-DDGRELpwdGKAF-GDLQVRGPWVIDRYFRG--DASPLVD--GWFP 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 420 SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVM 499
Cdd:PRK07008 413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELL 492
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 52631875 500 DYVAGQVtASKRLRGGVKFVDEVPKGLTGKIDARKIREIL 539
Cdd:PRK07008 493 AFYEGKV-AKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
325-537 |
8.30e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 108.19 E-value: 8.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 325 EAVAKRFklpGIR--QGYGLTETtsAIIITPEGDDKPGACGKvvPFFSAKIVDLDTGKT-----LGVNQR--------GE 389
Cdd:PRK13388 281 AEFSRRF---GCQveDGYGSSEG--AVIVVREPGTPPGSIGR--GAPGVAIYNPETLTEcavarFDAHGAllnadeaiGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 390 LCVK-GPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAG 468
Cdd:PRK13388 354 LVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVA 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 469 VAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRGG-VKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK13388 433 VYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRyVRIAADLPSTATNKVLKRELIA 502
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
192-531 |
1.30e-24 |
|
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: 106.62 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPV-FGNQiipDTAILtvipFHH---GFGMFTTLGYLTCGFRIVLM-- 265
Cdd:cd17643 95 LAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFgFNED---DVWTL----FHSyafDFSVWEIWGALLHGGRLVVVpy 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 -YRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIR--QGYGL 342
Cdd:cd17643 168 eVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvNMYGI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 343 TETT---SAIIITPegDDKPGA----CGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPE--ATSALID 413
Cdd:cd17643 248 TETTvhvTFRPLDA--ADLPAAaaspIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPEltAERFVAN 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 414 KDG-----WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLE 488
Cdd:cd17643 325 PFGgpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD 404
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 52631875 489 EGKTMTEQEVMDYVAGQVTASKRLRGGVkFVDEVPKGLTGKID 531
Cdd:cd17643 405 DGAAADIAELRALLKELLPDYMVPARYV-PLDALPLTVNGKLD 446
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
45-533 |
5.75e-24 |
|
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: 104.76 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 45 AHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPtndiynerelynsLSISQPT 124
Cdd:cd17649 7 VFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP-------------LDPEYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 125 ivfcskralqkilgvqkklpiiqkivildSREDYMGKQSMYSFIESHLPAGFneydyipdsfdretatALIMNSSGSTGL 204
Cdd:cd17649 74 -----------------------------ERLRYMLEDSGAGLLLTHHPRQL----------------AYVIYTSGSTGT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 205 PKGVELTHKNICvrfSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVL----MYRCEEELfLRSLQDY 280
Cdd:cd17649 109 PKGVAVSHGPLA---AHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLrpdeLWASADEL-AEMVREL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 281 KIQSALLVPTLFSFFAKStLVDKYDLS--NLHEIASGGAPLAkevGEAVAKRFKLPgIR--QGYGLTETT-SAIIITPEG 355
Cdd:cd17649 185 GVTVLDLPPAYLQQLAEE-ADRTGDGRppSLRLYIFGGEALS---PELLRRWLKAP-VRlfNAYGPTEATvTPLVWKCEA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 356 DDKPGA----CGKVVPFFSAKIVDLDTGkTLGVNQRGELCVKGPMIMKGYVNNPEATSA--LIDKDG-----WLHSGDIA 424
Cdd:cd17649 260 GAARAGasmpIGRPLGGRSAYILDADLN-PVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLA 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 425 YYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELpAAVVVLEEGKTMTE--QEVMDYV 502
Cdd:cd17649 339 RWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL-VAYVVLRAAAAQPElrAQLRTAL 417
|
490 500 510
....*....|....*....|....*....|....
gi 52631875 503 AGQVTAS---KRLrggvKFVDEVPKGLTGKIDAR 533
Cdd:cd17649 418 RASLPDYmvpAHL----VFLARLPLTPNGKLDRK 447
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
190-531 |
1.14e-23 |
|
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: 103.94 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 190 TATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDpVFGNQIIPDTAILTVIPFHHG-FGMFTTLgylTCGFRIVLMyrc 268
Cdd:cd12115 105 DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAA-AFSAEELAGVLASTSICFDLSvFELFGPL---ATGGKVVLA--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEELFLRSLQDYKiQSALL--VPTlfsffAKSTLVDKYDL-SNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTET 345
Cdd:cd12115 178 DNVLALPDLPAAA-EVTLIntVPS-----AAAELLRHDALpASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSED 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 346 T--SAIIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWL----- 418
Cdd:cd12115 252 TtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarl 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 419 -HSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQE 497
Cdd:cd12115 331 yRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVED 410
|
330 340 350
....*....|....*....|....*....|....
gi 52631875 498 VMDYVAGQVTASKrLRGGVKFVDEVPKGLTGKID 531
Cdd:cd12115 411 LRRHLGTRLPAYM-VPSRFVRLDALPLTPNGKID 443
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
193-534 |
2.69e-23 |
|
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: 102.72 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICvrfSHCRDPVFGNQIIPDTAILTvipfhhgfgmFTTLGY----------LTCGFRI 262
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRGLA---NLAAAQIAAFDVGPGSRVLQ----------FASPSFdasvwellmaLLAGATL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 263 VLMYRceEEL-----FLRSLQDYKIQSALLVPTLFSffakstLVDKYDLSNLHEIASGGAPLAKEVgeavAKRFKlPGIR 337
Cdd:cd17652 163 VLAPA--EELlpgepLADLLREHRITHVTLPPAALA------ALPPDDLPDLRTLVVAGEACPAEL----VDRWA-PGRR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 --QGYGLTETT-SAIIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDK 414
Cdd:cd17652 230 miNAYGPTETTvCATMAGPLPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 415 D------GWLH-SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVL 487
Cdd:cd17652 309 DpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVP 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 52631875 488 EEGKTMTEQEVMDYVAgqvtasKRLRG-----GVKFVDEVPKGLTGKIDARK 534
Cdd:cd17652 389 APGAAPTAAELRAHLA------ERLPGymvpaAFVVLDALPLTPNGKLDRRA 434
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
199-497 |
4.99e-23 |
|
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: 103.78 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 199 SGSTGLPKGVELTHKNICVRFSHCRDpVFGnqIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLmyrCEEE------L 272
Cdd:COG1020 626 SGSTGRPKGVMVEHRALVNLLAWMQR-RYG--LGPGDRVLQFASLSFDASVWEIFGALLSGATLVL---APPEarrdpaA 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 273 FLRSLQDYKIQSALLVPTLFsffakSTLVD--KYDLSNLHEIASGGAPLAKEVGEAVAKRFklPGIR--QGYGLTETT-S 347
Cdd:COG1020 700 LAELLARHRVTVLNLTPSLL-----RALLDaaPEALPSLRLVLVGGEALPPELVRRWRARL--PGARlvNLYGPTETTvD 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 348 AIIITPEGDDKPGAC---GKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSA-----LIDKDG--W 417
Cdd:COG1020 773 STYYEVTPPDADGGSvpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadPFGFPGarL 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 418 LHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQE 497
Cdd:COG1020 852 YRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAAL 931
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
37-534 |
5.37e-22 |
|
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: 98.90 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 37 PGTIAFTDAHAEVniTYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYN 116
Cdd:cd12116 1 PDATAVRDDDRSL--SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 117 SLSISQPTIVFCSKRALQkilgvqkklPIIQKIVILDSREDYMGkqsmYSFIESHLPAGFNEydyipdsfdretaTALIM 196
Cdd:cd12116 79 ILEDAEPALVLTDDALPD---------RLPAGLPVLLLALAAAA----AAPAAPRTPVSPDD-------------LAYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 197 NSSGSTGLPKGVELTHKNIcVRFSHC--RDPVFGnqiiPDTAILTVIPFhhGFGMFT--TLGYLTCGFRIVLmyrCEEEL 272
Cdd:cd12116 133 YTSGSTGRPKGVVVSHRNL-VNFLHSmrERLGLG----PGDRLLAVTTY--AFDISLleLLLPLLAGARVVI---APRET 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 273 ------FLRSLQDYKIQSALLVPTLFSFFAKStlvDKYDLSNLHEIASGGA---PLAKEVGEAVAKRFKLpgirqgYGLT 343
Cdd:cd12116 203 qrdpeaLARLIEAHSITVMQATPATWRMLLDA---GWQGRAGLTALCGGEAlppDLAARLLSRVGSLWNL------YGPT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 344 ETT---SAIIITPEgdDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKDGWLHS 420
Cdd:cd12116 274 ETTiwsTAARVTAA--AGPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 421 -------GDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELpAAVVVLEEGKTM 493
Cdd:cd12116 351 gsrlyrtGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAP 429
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 52631875 494 TEQEVMDYVAGQVTASkRLRGGVKFVDEVPKGLTGKIDaRK 534
Cdd:cd12116 430 DAAALRAHLRATLPAY-MVPSAFVRLDALPLTANGKLD-RK 468
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
51-422 |
6.17e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 99.57 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNER-----ELYNSLSISQPTI 125
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLVsqdfgKLRHVLELLTPGL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 126 VFCS-----KRALQKI--LGVqkklpiiqKIVILDSREDYMGKQSMYSFIESHLPAGfneydyIPDSFDRETA--TALIM 196
Cdd:PRK08180 150 VFADdgaafARALAAVvpADV--------EVVAVRGAVPGRAATPFAALLATPPTAA------VDAAHAAVGPdtIAKFL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 197 NSSGSTGLPKGVELTHKNICV---------RFSHCRDPVfgnqiipdtaILTVIPFHHGFGMFTTLGyltcgfrIVL--- 264
Cdd:PRK08180 216 FTSGSTGLPKAVINTHRMLCAnqqmlaqtfPFLAEEPPV----------LVDWLPWNHTFGGNHNLG-------IVLyng 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 265 --MYRCE----EELF---LRSLQDykIQSALL--VPTLFSFFAKS-----TLVDKYdLSNLHEIASGGAPLAKEVG---E 325
Cdd:PRK08180 279 gtLYIDDgkptPGGFdetLRNLRE--ISPTVYfnVPKGWEMLVPAlerdaALRRRF-FSRLKLLFYAGAALSQDVWdrlD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 326 AVAKRF---KLPgIRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDtGKTlgvnqrgELCVKGPMIMKGYV 402
Cdd:PRK08180 356 RVAEATcgeRIR-MMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVG-GKL-------EVRVKGPNVTPGYW 426
|
410 420
....*....|....*....|
gi 52631875 403 NNPEATSALIDKDGWLHSGD 422
Cdd:PRK08180 427 RAPELTAEAFDEEGYYRSGD 446
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
193-460 |
7.64e-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: 98.71 E-value: 7.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICvrfSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTtlGYLTCGFRIVLMYRCEEEL 272
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENLV---HNMFAILNSTEWKTKDRILSWMPLTHDMGLIA--FHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 273 FLR--SLQDYKIQ----SALLVPT----LFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQG--- 339
Cdd:cd05908 184 FIRrpILWLKKASehkaTIVSSPNfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNail 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 340 --YGLTETTSAIIITPEG----------------------DDKPGAC------GKVVPFFSAKIVDlDTGKTLGVNQRGE 389
Cdd:cd05908 264 pvYGLAEASVGASLPKAQspfktitlgrrhvthgepepevDKKDSECltfvevGKPIDETDIRICD-EDNKILPDGYIGH 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52631875 390 LCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYdKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQ 460
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEE 412
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
81-543 |
1.79e-21 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 97.93 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 81 CSENSLQFFMPVC-GALFigvgvAPTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVILDSredym 159
Cdd:PRK05620 74 CAEHLEVLFAVACmGAVF-----NPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGP----- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 160 gkqSMYSFIESHLPAGFNEYDY------IPDSFD----RETATALIMNSSGSTGLPKGVELTHKNICVRFSHCR--DPVf 227
Cdd:PRK05620 144 ---SDADSAAAHMPEGIKVYSYealldgRSTVYDwpelDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRttDSL- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 228 gnQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMYR-CEEELFLRSLQDYKIQSALLVPT----LFSFFAKSTLvd 302
Cdd:PRK05620 220 --AVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPdLSAPTLAKIIATAMPRVAHGVPTlwiqLMVHYLKNPP-- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 303 kyDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIrQGYGLTETTSAIIIT--PEGddKPGAC--------GKVVPFFSAK 372
Cdd:PRK05620 296 --ERMSLQEIYVGGSAVPPILIKAWEERYGVDVV-HVWGMTETSPVGTVArpPSG--VSGEArwayrvsqGRFPASLEYR 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 373 IVDldTGKTLGVNQR--GELCVKGPMIMKGYVNNP----------------EATSALIDKDGWLHSGDIAYYDKDGHFFI 434
Cdd:PRK05620 371 IVN--DGQVMESTDRneGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 435 VDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQevmdyvagqvTAsKRLRG 514
Cdd:PRK05620 449 HDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRE----------TA-ERLRD 517
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 52631875 515 GVK-------------FVDEVPKGLTGKIDARKIREILMMGK 543
Cdd:PRK05620 518 QLRdrlpnwmlpeywtFVDEIDKTSVGKFDKKDLRQHLADGD 559
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
189-455 |
1.91e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 97.76 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 189 ETATALIMNSSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDT-AILTVIPFHHGFGMfttLGYLTcgfriVLMYR 267
Cdd:PRK07768 151 EDDLALMQLTSGSTGSPKAVQITHGNL---YANAEAMFVAAEFDVETdVMVSWLPLFHDMGM---VGFLT-----VPMYF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 268 CEEELFLRSLqDYkIQSALLVPTLFSF----------FAKSTLV---------DKYDLSNLHEIASGGAPLAKEVGEA-- 326
Cdd:PRK07768 220 GAELVKVTPM-DF-LRDPLLWAELISKyrgtmtaapnFAYALLArrlrrqakpGAFDLSSLRFALNGAEPIDPADVEDll 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 327 -VAKRFKLP--GIRQGYGLTETTSAIIITP-------------------------EGDDKPGAC-GKVVPFFSAKIVDLD 377
Cdd:PRK07768 298 dAGARFGLRpeAILPAYGMAEATLAVSFSPcgaglvvdevdadllaalrravpatKGNTRRLATlGPPLPGLEVRVVDED 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 378 tGKTLGVNQRGELCVKGPMIMKGYVNnPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELE 455
Cdd:PRK07768 378 -GQVLPPRGVGVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
198-542 |
2.31e-21 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 97.77 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 198 SSGSTGLPKGVELTHKNICVRFS-HCRDpvfGNQIIPDTAILTVIPFHHGFG---MFttLGYLTCGFRIVLMYrcEEELF 273
Cdd:PRK09192 184 SSGSTRFPRGVIITHRALMANLRaISHD---GLKVRPGDRCVSWLPFYHDMGlvgFL--LTPVATQLSVDYLP--TRDFA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 274 LRSLQDYKIQS----ALLVPTLFSF-----FAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQ-----G 339
Cdd:PRK09192 257 RRPLQWLDLISrnrgTISYSPPFGYelcarRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDkafmpS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 340 YGLTETTSAIIITPEG----------------------DDKPGA------CGKVVPFFSAKIVDlDTGKTLGVNQRGELC 391
Cdd:PRK09192 337 YGLAEATLAVSFSPLGsgivveevdrdrleyqgkavapGAETRRvrtfvnCGKALPGHEIEIRN-EAGMPLPERVVGHIC 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 392 VKGPMIMKGYVNNPEATSALiDKDGWLHSGDIAYYdKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIF--DAGV 469
Cdd:PRK09192 416 VRGPSLMSGYFRDEESQDVL-AADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAA 493
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52631875 470 AGIPDPDaGElpaAVVVLEEGKTMTEQEVMDYVAgQVTASKRLRGGVKFVDEV------PKGLTGKIDARKIREILMMG 542
Cdd:PRK09192 494 FSIAQEN-GE---KIVLLVQCRISDEERRGQLIH-ALAALVRSEFGVEAAVELvpphslPRTSSGKLSRAKAKKRYLSG 567
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
28-535 |
3.00e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 96.89 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 28 KAMKRYAQV-PGTIAFtdAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSlqFFMPVC--GALFIGVGVAP 104
Cdd:PRK04813 6 ETIEEFAQTqPDFPAY--DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMS--PEMLATflGAVKAGHAYIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 105 TnDIYNERELYNS-LSISQPTIVFCSKRALQKILGVQkklpiiqkIVILDSREDymgkqsmysfieshlpAGFNEYDYIP 183
Cdd:PRK04813 82 V-DVSSPAERIEMiIEVAKPSLIIATEELPLEILGIP--------VITLDELKD----------------IFATGNPYDF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 184 DSFDRETATALIMNSSGSTGLPKGVELTHKNIcVRFSH--CRD------PVFGNQIiP---DTAILTVIPfhhgfgmftt 252
Cdd:PRK04813 137 DHAVKGDDNYYIIFTSGTTGKPKGVQISHDNL-VSFTNwmLEDfalpegPQFLNQA-PysfDLSVMDLYP---------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 253 lgYLTCGFRIVLMYRCE----EELFlRSLQDYKI----------QSALLVPTLfsffakstlvDKYDLSNLHEIASGGAP 318
Cdd:PRK04813 205 --TLASGGTLVALPKDMtanfKQLF-ETLPQLPInvwvstpsfaDMCLLDPSF----------NEEHLPNLTHFLFCGEE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 319 LAKEVGEAVAKRFKLPGIRQGYGLTETT---SAIIITPEGDDK--PGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVK 393
Cdd:PRK04813 272 LPHKTAKKLLERFPSATIYNTYGPTEATvavTSIEITDEMLDQykRLPIGYAKPDSPLLIID-EEGTKLPDGEQGEIVIS 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 394 GPMIMKGYVNNPEATS-ALIDKDGW--LHSGDIAYYDkDGHFFIVDRLKSLIKYKGYQVppaELESI---LLQHPFIFDA 467
Cdd:PRK04813 351 GPSVSKGYLNNPEKTAeAFFTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRI---ELEEIeqnLRQSSYVESA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 468 GVAGIPDPDAGELPAAVVVLEEGK-----TMTEQ-------EVMDYVAGQvtaskrlrggvKFV--DEVPKGLTGKIDAR 533
Cdd:PRK04813 427 VVVPYNKDHKVQYLIAYVVPKEEDferefELTKAikkelkeRLMEYMIPR-----------KFIyrDSLPLTPNGKIDRK 495
|
..
gi 52631875 534 KI 535
Cdd:PRK04813 496 AL 497
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
189-495 |
8.78e-21 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 95.74 E-value: 8.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 189 ETATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDpVFGnqIIPDTAILTVIPFhhgFGMFTtlgyLTCGFRIVLMY-- 266
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALRE-DYG--IEPGEIDLPTFPL---FALFG----PALGMTSVIPDmd 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 267 -----RCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKevgeAVAKRFK--LPG---I 336
Cdd:PRK09274 243 ptrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPI----AVIERFRamLPPdaeI 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 337 RQGYGLTE-------TTSAII-----ITPEGDdkpGAC-GKVVPFFSAKIVDLDTG--------KTLGVNQRGELCVKGP 395
Cdd:PRK09274 319 LTPYGATEalpissiESREILfatraATDNGA---GICvGRPVDGVEVRIIAISDApipewddaLRLATGEIGEIVVAGP 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 396 MIMKGYVNNPEATSA--LIDKDG--WLHSGDIAYYDKDGHFFIVDRlKS--LIKYKG--YQVPpaeLESILLQHPFIFDA 467
Cdd:PRK09274 396 MVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCGR-KAhrVETAGGtlYTIP---CERIFNTHPGVKRS 471
|
330 340
....*....|....*....|....*...
gi 52631875 468 GVAGIPDPdAGELPAAVVVLEEGKTMTE 495
Cdd:PRK09274 472 ALVGVGVP-GAQRPVLCVELEPGVACSK 498
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
300-538 |
8.88e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 95.98 E-value: 8.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 300 LVDKYDLSNLHEIASGGAPLAKE--------VGEAvakrfKLPgIRQGYGLTETtSAIIITP-EG--DDKPGACGKvvPF 368
Cdd:PRK00174 360 HPKKYDLSSLRLLGSVGEPINPEawewyykvVGGE-----RCP-IVDTWWQTET-GGIMITPlPGatPLKPGSATR--PL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 369 F--SAKIVDlDTGKTLGVNQRGELCVKGP---MIMKGYvNNPEAtsaLID------KDGWLhSGDIAYYDKDGHFFIVDR 437
Cdd:PRK00174 431 PgiQPAVVD-EEGNPLEGGEGGNLVIKDPwpgMMRTIY-GDHER---FVKtyfstfKGMYF-TGDGARRDEDGYYWITGR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 438 LKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTE---QEVMDYVAGQVTASKRLRg 514
Cdd:PRK00174 505 VDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDelrKELRNWVRKEIGPIAKPD- 583
|
250 260
....*....|....*....|....
gi 52631875 515 GVKFVDEVPKGLTGKIDARKIREI 538
Cdd:PRK00174 584 VIQFAPGLPKTRSGKIMRRILRKI 607
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
195-493 |
1.39e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 95.65 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 195 IMNSSGSTGLPKGVELTHKN--ICVRFSHCRDPVFGNQIIPDTAILTVIPFHHgfgmfttlgyltcgfrivLMYRCEEEL 272
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAvaTFVRGVDLFMEQFEDKMTHDDVYLSFLPLAH------------------ILDRMIEEY 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 273 FLRS-----------------LQDYK-----------------IQSAL--LVPTLFSFFaksTLVDKYDLSNLHE----- 311
Cdd:PLN02430 287 FFRKgasvgyyhgdlnalrddLMELKptllagvprvferihegIQKALqeLNPRRRLIF---NALYKYKLAWMNRgyshk 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 312 ------------------------IASGGAPLAKEVgEAVAKRFKLPGIRQGYGLTETTSAIIIT-PEGDDKPGACGKVV 366
Cdd:PLN02430 364 kaspmadflafrkvkaklggrlrlLISGGAPLSTEI-EEFLRVTSCAFVVQGYGLTETLGPTTLGfPDEMCMLGTVGAPA 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 367 PFFSAKIVDL-DTG-KTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKY 444
Cdd:PLN02430 443 VYNELRLEEVpEMGyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKL 521
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 52631875 445 -KGYQVPPAELESILLQHPFIFDAGVAGipDPDAGELpAAVVVLEEGKTM 493
Cdd:PLN02430 522 sQGEYVALEYLENVYGQNPIVEDIWVYG--DSFKSML-VAVVVPNEENTN 568
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-533 |
3.36e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.41 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 11 PPPFYPLEDGTAGEQLHKAmkryAQVPGTIA--FTDAHaevnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQF 88
Cdd:PRK12316 1995 TPEAYPRGPGVHQRIAEQA----ARAPEAIAvvFGDQH----LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFEL 2066
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 89 FMPVCGALFIGVGVAPTNDIY-NERELYnSLSISQPTIVFCSKralqkilGVQKKLPIIQKIVILD-SREDYMgkqsmys 166
Cdd:PRK12316 2067 VVALLAVLKAGGAYVPLDPNYpAERLAY-MLEDSGAALLLTQR-------HLLERLPLPAGVARLPlDRDAEW------- 2131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 167 fieSHLPAGFNEYDYIPDSFdretatALIMNSSGSTGLPKGVELTHKNICvrfSHCRDPVFGNQIIPDTAILTVIPFHHG 246
Cdd:PRK12316 2132 ---ADYPDTAPAVQLAGENL------AYVIYTSGSTGLPKGVAVSHGALV---AHCQAAGERYELSPADCELQFMSFSFD 2199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 247 FGMFTTLGYLTCGFRIVLM---YRCEEELFlRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLsNLHEIASGGAPLAKEV 323
Cdd:PRK12316 2200 GAHEQWFHPLLNGARVLIRddeLWDPEQLY-DEMERHGVTILDFPPVYLQQLAEHAERDGRPP-AVRVYCFGGEAVPAAS 2277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 324 GEAVAKRFKLPGIRQGYGLTETTSAIIITPEGDDKPGAC-----GKVVPFFSAKIVDLDTgKTLGVNQRGELCVKGPMIM 398
Cdd:PRK12316 2278 LRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAayvpiGRALGNRRAYILDADL-NLLAPGMAGELYLGGEGLA 2356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 399 KGYVNNPEATSALIDKDGWLH-------SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAG 471
Cdd:PRK12316 2357 RGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA 2436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52631875 472 IpDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKrLRGGVKFVDEVPKGLTGKIDAR 533
Cdd:PRK12316 2437 Q-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYM-VPAHWVVLERLPLNPNGKLDRK 2496
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
192-460 |
5.93e-20 |
|
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: 92.37 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTV--IPFHHGFG-MFTTLGYltcGFRIVLmyRC 268
Cdd:cd17653 107 LAYIIFTSGSTGIPKGVMVPHRGV---LNYVSQPPARLDVGPGSRVAQVlsIAFDACIGeIFSTLCN---GGTLVL--AD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEELFLRSLQdyKIQSALLVPTLFSffaksTLvDKYDLSNLHEIASGGAPLAKEVGEAVAKRfklPGIRQGYGLTETTSA 348
Cdd:cd17653 179 PSDPFAHVAR--TVDALMSTPSILS-----TL-SPQDFPNLKTIFLGGEAVPPSLLDRWSPG---RRLYNAYGPTECTIS 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 349 IIITPEGDDKPGACGKVVPFFSAKIVDLDTGKTLgVNQRGELCVKGPMIMKGYVNNPEATSA----LIDKDGWLH--SGD 422
Cdd:cd17653 248 STMTELLPGQPVTIGKPIPNSTCYILDADLQPVP-EGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyrTGD 326
|
250 260 270
....*....|....*....|....*....|....*...
gi 52631875 423 IAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQ 460
Cdd:cd17653 327 YGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQ 364
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
193-458 |
6.90e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 94.46 E-value: 6.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPvFGNQIIPDTAILTVIPFHHGFGMF-TTLGYLTCGFRIVLM---YRC 268
Cdd:PRK05691 169 AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHG-FGIDLNPDDVIVSWLPLYHDMGLIgGLLQPIFSGVPCVLMspaYFL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEEL-FLRSLQDY--KIQSAllvPT----LFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQ--- 338
Cdd:PRK05691 248 ERPLrWLEAISEYggTISGG---PDfayrLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPdsf 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 339 --GYGLTETTSAIIITPEG--------DDK--------PGA------CGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKG 394
Cdd:PRK05691 325 faSYGLAEATLFVSGGRRGqgipalelDAEalarnraePGTgsvlmsCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASG 404
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52631875 395 PMIMKGYVNNPEATS-ALIDKDG--WLHSGDIAYYdKDGHFFIVDRLKSLIKYKGYQVPPAELESIL 458
Cdd:PRK05691 405 PSIAHGYWRNPEASAkTFVEHDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
34-533 |
7.48e-20 |
|
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: 92.72 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 34 AQVPGTIAFTDAHAEVniTYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLqfFMPVC--GALFIGVGVAPTNDIYNE 111
Cdd:cd17646 9 ARTPDAPAVVDEGRTL--TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSA--DLVVAllAVLKAGAAYLPLDPGYPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 112 RELYNSLSISQPTIVFcSKRALQKILGVQKKLPIIQKIVIldsredymgkqsmysfieSHLPAGFNEYDYIPDsfdretA 191
Cdd:cd17646 85 DRLAYMLADAGPAVVL-TTADLAARLPAGGDVALLGDEAL------------------AAPPATPPLVPPRPD------N 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNICVRFSHCRDpvfGNQIIPDTAILTVIPFhhGF--GMFTTLGYLTCGFRIVLmyrCE 269
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQD---EYPLGPGDRVLQKTPL--SFdvSVWELFWPLVAGARLVV---AR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 270 EEL------FLRSLQDYKIQSALLVPTLFSFFakstlvdkydlsnLHEIASGGAPLAKEV---GEA----VAKRF-KLPG 335
Cdd:cd17646 212 PGGhrdpayLAALIREHGVTTCHFVPSMLRVF-------------LAEPAAGSCASLRRVfcsGEAlppeLAARFlALPG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 336 IR--QGYGLTETT---SAIIITPEGDDKPGACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSA 410
Cdd:cd17646 279 AElhNLYGPTEAAidvTHWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 411 LIDKDGWLH------SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGE-LPAA 483
Cdd:cd17646 358 RFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAArLVGY 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 52631875 484 VVVLEEGKTMTEQEVMDYVAGQVTASKrLRGGVKFVDEVPKGLTGKIDAR 533
Cdd:cd17646 438 VVPAAGAAGPDTAALRAHLAERLPEYM-VPAAFVVLDALPLTANGKLDRA 486
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
192-461 |
8.15e-20 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 92.57 E-value: 8.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNICVRFSHCRDpvFGNQIIPDTAILTVIPFH-HGFGMFTTLGYLTcGFRIVLMYRCEE 270
Cdd:PRK06334 185 VAVILFTSGTEKLPKGVPLTHANLLANQRACLK--FFSPKEDDVMMSFLPPFHaYGFNSCTLFPLLS-GVPVVFAYNPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 271 ELFLRSLQDyKIQSALL--VPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSA 348
Cdd:PRK06334 262 PKKIVEMID-EAKVTFLgsTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 349 IIITPEGDDKPGAC-GKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSAL-IDKDGWLHSGDIAYY 426
Cdd:PRK06334 341 ITINTVNSPKHESCvGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYVTGDLGYV 420
|
250 260 270
....*....|....*....|....*....|....*
gi 52631875 427 DKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQH 461
Cdd:PRK06334 421 DRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
193-535 |
1.75e-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: 91.08 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNIcVRFSHCRDPVFGNQIIPDTAILTVIPFHHG-FGMFTtlgYLTCGFRIVLMYRcEEE 271
Cdd:cd17645 107 AYVIYTSGSTGLPKGVMIEHHNL-VNLCEWHRPYFGVTPADKSLVYASFSFDASaWEIFP---HLTAGAALHVVPS-ERR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 272 LFLRSLQDYKIQSALLVPTLFSFFAKSTLvdKYDLSNLHEIASGGAPLAKevgeAVAKRFKLpgiRQGYGLTETTsaIII 351
Cdd:cd17645 182 LDLDALNDYFNQEGITISFLPTGAAEQFM--QLDNQSLRVLLTGGDKLKK----IERKGYKL---VNNYGPTENT--VVA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 352 TPEGDDKPGA---CGKvvPFFSAKIVDLDTGKTL---GVNqrGELCVKGPMIMKGYVNNPEATSALIDKDGWL------H 419
Cdd:cd17645 251 TSFEIDKPYAnipIGK--PIDNTRVYILDEALQLqpiGVA--GELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 420 SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEG------KTM 493
Cdd:cd17645 327 TGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEipheelREW 406
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 52631875 494 TEQEVMDYVAGQVTASkrlrggvkfVDEVPKGLTGKIDARKI 535
Cdd:cd17645 407 LKNDLPDYMIPTYFVH---------LKALPLTANGKVDRKAL 439
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
44-535 |
4.15e-19 |
|
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: 90.23 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 44 DAHAEV----NITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLS 119
Cdd:cd17656 3 DAVAVVfenqKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 120 ISQPTIVFcSKRALQKILGVQKKLPIIQKIVIldSREDymGKQSMYSFIESHLpagfneydyipdsfdretatALIMNSS 199
Cdd:cd17656 83 DSGVRVVL-TQRHLKSKLSFNKSTILLEDPSI--SQED--TSNIDYINNSDDL--------------------LYIIYTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 200 GSTGLPKGVELTHKNICVRFSHCRDPvfgnqiipdtailTVIPFHHGFGMFTTLGYLTCGFRIV-------LMYRCEEE- 271
Cdd:cd17656 138 GTTGKPKGVQLEHKNMVNLLHFEREK-------------TNINFSDKVLQFATCSFDVCYQEIFstllsggTLYIIREEt 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 272 -LFLRSLQDY----KIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLakEVGEAVAKRFKLPGI--RQGYGLTE 344
Cdd:cd17656 205 kRDVEQLFDLvkrhNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQL--VITNEFKEMLHEHNVhlHNHYGPSE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 345 T--TSAIIITPEgDDKP--GACGKvvPFFSAKIVDLDTGKTL---GVnqRGELCVKGPMIMKGYVNNPEATSALIDKDGW 417
Cdd:cd17656 283 ThvVTTYTINPE-AEIPelPPIGK--PISNTWIYILDQEQQLqpqGI--VGELYISGASVARGYLNRQELTAEKFFPDPF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 418 ------LHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEgk 491
Cdd:cd17656 358 dpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ-- 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 52631875 492 TMTEQEVMDYVAGQVtASKRLRGGVKFVDEVPKGLTGKIDARKI 535
Cdd:cd17656 436 ELNISQLREYLAKQL-PEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
37-533 |
4.44e-19 |
|
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: 90.02 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 37 PGTIAFtdAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPtndiynerelyn 116
Cdd:cd12114 1 PDATAV--ICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVP------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 117 sLSISQPtivfcSKRaLQKILGVQKKlpiiqKIVILDSREDymgKQSMYSFIESHLPAGFNEYDYIPDSFDRE-TATALI 195
Cdd:cd12114 67 -VDIDQP-----AAR-REAILADAGA-----RLVLTDGPDA---QLDVAVFDVLILDLDALAAPAPPPPVDVApDDLAYV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 196 MNSSGSTGLPKGVELTHKN-------ICVRFshcrdpvfgnQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLMyRC 268
Cdd:cd12114 132 IFTSGSTGTPKGVMISHRAalntildINRRF----------AVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLP-DE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEE----LFLRSLQDYKI---QSallVPTLFSFfakstLVDKY-----DLSNLHEIASGGAPLAKEVGEAVAKRFklPGI 336
Cdd:cd12114 201 ARRrdpaHWAELIERHGVtlwNS---VPALLEM-----LLDVLeaaqaLLPSLRLVLLSGDWIPLDLPARLRALA--PDA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 337 RQ---GyGLTETTSAIIITPEGDDKPGAcgKVVPFfsakivdldtGKTLGvNQR----------------GELCVKGPMI 397
Cdd:cd12114 271 RLislG-GATEASIWSIYHPIDEVPPDW--RSIPY----------GRPLA-NQRyrvldprgrdcpdwvpGELWIGGRGV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 398 MKGYVNNPEATSA--LIDKDG--WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIP 473
Cdd:cd12114 337 ALGYLGDPELTAArfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLG 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 474 DPDAGELpAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDAR 533
Cdd:cd12114 417 DPGGKRL-AAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
193-537 |
7.31e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 88.18 E-value: 7.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVFGnqiiPDTAILTViPFHHGFGMFTTL-----GY------LTCGFR 261
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHDRLGG----PGQWLLAL-PAHHIAGLQVLVrsviaGSepveldVSAGFD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 262 IVLMYRCEEELflRSLQDYkiqsALLVPTLFSFfAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKrfklPGIR--QG 339
Cdd:PRK07824 113 PTALPRAVAEL--GGGRRY----TSLVPMQLAK-ALDDPAATAALAELDAVLVGGGPAPAPVLDAAAA----AGINvvRT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 340 YGLTETTsaiiitpegddkpGAC---GKVVPFFSAKIVDldtgktlgvnqrGELCVKGPMIMKGYVNNPEatSALIDKDG 416
Cdd:PRK07824 182 YGMSETS-------------GGCvydGVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVD--PDPFAEPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 417 WLHSGDIAYYDkDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQ 496
Cdd:PRK07824 235 WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE 313
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 52631875 497 EVMDYVAGQ--VTASKRlrgGVKFVDEVPKGLTGKIDARKIRE 537
Cdd:PRK07824 314 ALRAHVARTldRTAAPR---ELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-513 |
1.01e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.61 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 2 EDAKNIMHG---PPPFYPLedgtaGEQLHKAMK-RYAQVPGTIAFTdaHAEVNITYSEYFEMACRLAETMKRYGLGLQHH 77
Cdd:PRK12467 1554 AERRQILEGwnaTHTGYPL-----ARLVHQLIEdQAAATPEAVALV--FGEQELTYGELNRRANRLAHRLIALGVGPEVL 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 78 IAVCSENSLQFFMPVCGALFIGVGVAPTNDIY-NERELYnslSISQPTI-VFCSKRALQKilgvqkKLPII--QKIVILD 153
Cdd:PRK12467 1627 VGIAVERSLEMVVGLLAILKAGGAYVPLDPEYpRERLAY---MIEDSGIeLLLTQSHLQA------RLPLPdgLRSLVLD 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 154 SREDYMGKQSMYSFIEShlPAGFNeydyipdsfdretaTALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfgnQIIP 233
Cdd:PRK12467 1698 QEDDWLEGYSDSNPAVN--LAPQN--------------LAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY---QLSA 1758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 234 DTAILTVIPFHHGFGMFTTLGYLTCGFRIVL----MYRCEEElFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSnL 309
Cdd:PRK12467 1759 ADVVLQFTSFAFDVSVWELFWPLINGARLVIappgAHRDPEQ-LIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS-L 1836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 310 HEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIITP--EGDDKPGAC---GKVVPFFSAKIVDlDTGKTLGV 384
Cdd:PRK12467 1837 RRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTcrRKDLEGRDSvpiGQPIANLSTYILD-ASLNPVPI 1915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 385 NQRGELCVKGPMIMKGYVNNPEAT------SALIDKDGWLH-SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESI 457
Cdd:PRK12467 1916 GVAGELYLGGVGLARGYLNRPALTaerfvaDPFGTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEAR 1995
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 52631875 458 LLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGktmteqeVMDYVAGQVTASKRLR 513
Cdd:PRK12467 1996 LREQGGVREAVVIAQDGANGKQLVAYVVPTDPG-------LVDDDEAQVALRAILK 2044
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
190-538 |
1.40e-18 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 89.24 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 190 TATALIMNSSGSTGLPKGVElthknicvrfshcRDpVFGNQIIPDTAILTVIPFHHGFGMFTT--LGYLTCGFRIV---- 263
Cdd:PRK10524 233 NEPSYILYTSGTTGKPKGVQ-------------RD-TGGYAVALATSMDTIFGGKAGETFFCAsdIGWVVGHSYIVyapl 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 264 ------LMY-----RCEEELFLRSLQDYKIQSALLVPTLFSFFAKS--TLVDKYDLSNLHEIASGGAPLAKEVGEAVAKR 330
Cdd:PRK10524 299 lagmatIMYeglptRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQdpALLRKHDLSSLRALFLAGEPLDEPTASWISEA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 331 FKLPgIRQGYGLTETTSAII-ITPEGDDKP---GACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMimkgyvnNPE 406
Cdd:PRK10524 379 LGVP-VIDNYWQTETGWPILaIARGVEDRPtrlGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPL-------PPG 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 407 ATSALIDKDG------WLHSGDIAY-------YDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIP 473
Cdd:PRK10524 451 CMQTVWGDDDrfvktyWSLFGRQVYstfdwgiRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVK 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52631875 474 DPDAGELPAAVVVLEEGKTMT--------EQEVMDYVAGQVTASKRlRGGVKFVDEVPKGLTGKIDARKIREI 538
Cdd:PRK10524 531 DALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVAR-PARVWFVSALPKTRSGKLLRRAIQAI 602
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
193-457 |
1.49e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 89.38 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfgnQIIPDTAILTVIPFHHGFGMftTLGYLT---CGFRIVLM---- 265
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIA---DFTPNDRFMSALPLFHSFGL--TVGLFTpllTGAEVFLYpspl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 -YRCEEELFlrslqdYKIQSALLvptlfsfFAKSTLV-------DKYDLSNLHEIASGGAPLAKEVGEAVAKRFklpGIR 337
Cdd:PRK08043 443 hYRIVPELV------YDRNCTVL-------FGTSTFLgnyarfaNPYDFARLRYVVAGAEKLQESTKQLWQDKF---GLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 --QGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDtgktlGVNQRGELCVKGPMIMKGY--VNNP---EATSA 410
Cdd:PRK08043 507 ilEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVP-----GIEQGGRLQLKGPNIMNGYlrVEKPgvlEVPTA 581
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 52631875 411 L----IDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVppaELESI 457
Cdd:PRK08043 582 EnargEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMV---SLEMV 629
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
193-534 |
1.71e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 89.84 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNICvrfSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLM---YRCE 269
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVGVRHGALA---NHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRdndLWDP 3316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 270 EELFlRSLQDYKIQSALLVPTLFSFFAKSTlvDKYDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETT-SA 348
Cdd:PRK12467 3317 EELW-QAIHAHRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVvTV 3393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 349 IIITPEGDDKPGAC----GKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEAT------SALIDKDGWL 418
Cdd:PRK12467 3394 TLWKCGGDAVCEAPyapiGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTaerfvaDPFSGSGGRL 3472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 419 H-SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQ- 496
Cdd:PRK12467 3473 YrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETl 3552
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 52631875 497 ------EVMDY-VAGQVTASKRLrggvkfvdevPKGLTGKIDaRK 534
Cdd:PRK12467 3553 rdhlaaSLPDYmVPAQLLVLAAM----------PLGPNGKVD-RK 3586
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-495 |
1.81e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.02 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 15 YPLEDGtageqLHKAMKRYAQV-PGTIAFtdAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVC 93
Cdd:PRK12316 507 YPLQRG-----VHRLFEEQVERtPEAPAL--AFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 94 GALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSKRalqkilgVQKKLPIIQKIVILD-SREDymgkqsmySFIESHl 172
Cdd:PRK12316 580 AILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSH-------LGRKLPLAAGVQVLDlDRPA--------AWLEGY- 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 173 PAGFNEYDYIPDSFdretatALIMNSSGSTGLPKGVELTHKNICVRFSHCRDpVFGNQIIpdTAILTVIPFHHGFGMFTT 252
Cdd:PRK12316 644 SEENPGTELNPENL------AYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQ-AYGLGVG--DTVLQKTPFSFDVSVWEF 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 253 LGYLTCGFRIVL----MYRCEEELFLRSLQDyKIQSALLVPTLFSFFAKSTLVDkyDLSNLHEIASGGAPLAKEVGEAVA 328
Cdd:PRK12316 715 FWPLMSGARLVVaapgDHRDPAKLVELINRE-GVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVF 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 329 KRFKLPGIRQGYGLTETTsaIIIT-----PEGDDKPgACGKVVPFFSAKIVDLDTGKT-LGVnqRGELCVKGPMIMKGYV 402
Cdd:PRK12316 792 AKLPQAGLYNLYGPTEAA--IDVThwtcvEEGGDSV-PIGRPIANLACYILDANLEPVpVGV--LGELYLAGRGLARGYH 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 403 NNPEAT------SALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIpdpD 476
Cdd:PRK12316 867 GRPGLTaerfvpSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---D 943
|
490
....*....|....*....
gi 52631875 477 AGELPAAVVVLEEGKTMTE 495
Cdd:PRK12316 944 GKQLVGYVVLESEGGDWRE 962
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
48-534 |
2.11e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.63 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 48 EVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIY-NERELYnSLSISQPTIV 126
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYpRERLAY-MMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 127 FCSKRALQKilgvqkkLPIIQKI--VILDSREDYmgkqsmysfieshlpAGFNEYDyiPDSFDRETATALIMNSSGSTGL 204
Cdd:PRK12316 4653 LTQSHLLQR-------LPIPDGLasLALDRDEDW---------------EGFPAHD--PAVRLHPDNLAYVIYTSGSTGR 4708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 205 PKGVELTHKNIcVRFSHCRDPVFGnqIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLM--YRCEEELFLRSLQDYKI 282
Cdd:PRK12316 4709 PKGVAVSHGSL-VNHLHATGERYE--LTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRddSLWDPERLYAEIHEHRV 4785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 283 QSALLVPTLFSFFAKSTLVDKyDLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIII-TPEGDDKPGA 361
Cdd:PRK12316 4786 TVLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLwKARDGDACGA 4864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 362 ----CGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDKD------GWLH-SGDIAYYDKDG 430
Cdd:PRK12316 4865 aympIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgGRLYrTGDLARYRADG 4943
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 431 HFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEgktmteqEVMDYVAGQVTASK 510
Cdd:PRK12316 4944 VIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDP-------ALADADEAQAELRD 5016
|
490 500 510
....*....|....*....|....*....|....*..
gi 52631875 511 RLRGGVK-------------FVDEVPKGLTGKIDaRK 534
Cdd:PRK12316 5017 ELKAALRerlpeymvpahlvFLARMPLTPNGKLD-RK 5052
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
22-534 |
5.22e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.29 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 22 AGEQLHKAMKRYA-QVPGTIAFTdaHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGV 100
Cdd:PRK12467 510 APDCVHQLIEAQArQHPERPALV--FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGG 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 101 GVAPTNDIYNERELYNSLSISQPTIVFCskralQKILGVQKKLPIIQKIVILDSREDYMgkqsmysfieSHLPAGFNEYD 180
Cdd:PRK12467 588 AYVPLDPEYPQDRLAYMLDDSGVRLLLT-----QSHLLAQLPVPAGLRSLCLDEPADLL----------CGYSGHNPEVA 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 181 YIPDSFdretatALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfgnQIIPDTAILTVIPFHHGFGMFTTLGYLTCGF 260
Cdd:PRK12467 653 LDPDNL------AYVIYTSGSTGQPKGVAISHGALANYVCVIAERL---QLAADDSMLMVSTFAFDLGVTELFGALASGA 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 261 RIVLM-YRC--EEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKydLSNLHEIASGGAplAKEVGEAVAKRFKLPGIR 337
Cdd:PRK12467 724 TLHLLpPDCarDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVCGGE--ALQVDLLARVRALGPGAR 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 --QGYGLTETTSAIIITPEGDD----KPGACGKVVPFFSAKIVDLDTgKTLGVNQRGELCVKGPMIMKGYVNNP--EATS 409
Cdd:PRK12467 800 liNHYGPTETTVGVSTYELSDEerdfGNVPIGQPLANLGLYILDHYL-NPVPVGVVGELYIGGAGLARGYHRRPalTAER 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 410 ALIDKDG-----WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAV 484
Cdd:PRK12467 879 FVPDPFGadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYL 958
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 52631875 485 V---VLEEGKTMTEQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDaRK 534
Cdd:PRK12467 959 VpaaVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLD-RK 1010
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
180-484 |
5.55e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 87.48 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 180 DYIPDSF---------DRETaTALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVFGNQiipDTAILTVIPFHHGFGMF 250
Cdd:PRK07769 162 DAVPDEVgatwvppeaNEDT-IAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQE---GDRGVSWLPFFHDMGLI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 251 TTLGYLTCGFRIVLM---------YRCEEELFLRSLQDYKIQSALlvPTlFSF-FAKSTLVDK-----YDLSNLHEIASG 315
Cdd:PRK07769 238 TVLLPALLGHYITFMspaafvrrpGRWIRELARKPGGTGGTFSAA--PN-FAFeHAAARGLPKdgeppLDLSNVKGLLNG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 316 GAPLA----KEVGEAVAKrFKLP--GIRQGYGLTETTSAIIITPEGD----------------------DKPGA-----C 362
Cdd:PRK07769 315 SEPVSpasmRKFNEAFAP-YGLPptAIKPSYGMAEATLFVSTTPMDEeptviyvdrdelnagrfvevpaDAPNAvaqvsA 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 363 GKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALI-----------------DKDGWLHSGDIAY 425
Cdd:PRK07769 394 GKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRTGDYGV 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 426 YdKDGHFFIVDRLKSLIKYKGYQVPPAELE-SILLQHPFIFDAGVAGIPDPdAGELPAAV 484
Cdd:PRK07769 474 Y-FDGELYITGRVKDLVIIDGRNHYPQDLEyTAQEATKALRTGYVAAFSVP-ANQLPQVV 531
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
453-529 |
6.82e-18 |
|
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: 77.97 E-value: 6.82e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52631875 453 ELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQEVMDYVAGQVTASKRLRgGVKFVDEVPKGLTGK 529
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPK-EVVFVDELPKTRSGK 76
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
178-530 |
7.38e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 86.60 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 178 EYDYIPDSFDRETATALIMN-SSGSTGLPKGVELTHKNIcvrFShcrdpvfgnqiIPDT---------------AILTVI 241
Cdd:PRK05857 156 DAASLAGNADQGSEDPLAMIfTSGTTGEPKAVLLANRTF---FA-----------VPDIlqkeglnwvtwvvgeTTYSPL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 242 PFHHGFGMFTTLGYLTCGFRIVLmyRCEEELFLRS-LQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGA-PL 319
Cdd:PRK05857 222 PATHIGGLWWILTCLMHGGLCVT--GGENTTSLLEiLTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSrAI 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 320 AKEVgeavakRF-KLPGIR--QGYGLTETTSAIIITPEGDD-----KPGACGKVVPFFSAKIVDLDTG-----KTLGVNQ 386
Cdd:PRK05857 300 AADV------RFiEATGVRtaQVYGLSETGCTALCLPTDDGsivkiEAGAVGRPYPGVDVYLAATDGIgptapGAGPSAS 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 387 RGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFD 466
Cdd:PRK05857 374 FGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVRE 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 467 AGVAGIPDPDAGELPA-AVVVLEEGKTMTEQEVMDYVAGQV---TASKRLRGGVKFVDEVPKGLTGKI 530
Cdd:PRK05857 453 AACYEIPDEEFGALVGlAVVASAELDESAARALKHTIAARFrreSEPMARPSTIVIVTDIPRTQSGKV 520
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
240-539 |
1.00e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.82 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 240 VIPFHHGFGMFTTL-GYLTCGFRIVLMYRC--EEELFLRSLQDYKIQsalLVPTLFSFFAKSTLvdkYDLSNLHEIASGG 316
Cdd:PRK07445 166 VLPLYHVSGLMQFMrSFLTGGKLVILPYKRlkSGQELPPNPSDFFLS---LVPTQLQRLLQLRP---QWLAQFRTILLGG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 317 APLAKEVGEAvAKRFKLPgIRQGYGLTETTSAII-ITPE----GDDkpgACGKVVPffSAKIvdldtgkTLGVNQRGELC 391
Cdd:PRK07445 240 APAWPSLLEQ-ARQLQLR-LAPTYGMTETASQIAtLKPDdflaGNN---SSGQVLP--HAQI-------TIPANQTGNIT 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 392 VKGPMIMKGYVnnPEatsaLIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAG 471
Cdd:PRK07445 306 IQAQSLALGYY--PQ----ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLG 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 472 IPDPDAGELPAAVVVLEEGKTmTEQEVMDYVAGQVTASKRLRGGVKfVDEVPKGLTGKIDARKIREIL 539
Cdd:PRK07445 380 LPDPHWGEVVTAIYVPKDPSI-SLEELKTAIKDQLSPFKQPKHWIP-VPQLPRNPQGKINRQQLQQIA 445
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
51-485 |
1.59e-17 |
|
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: 85.56 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIY-----NERELYNSLSISQPTI 125
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYslmsqDLAKLKHLFELLKPGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 126 VFCS-----KRALQKILGVQKKLpiiqkiviLDSREDYMGKQSMySFIE-SHLPAGFNeydyIPDSFDRET--ATALIMN 197
Cdd:cd05921 106 VFAQdaapfARALAAIFPLGTPL--------VVSRNAVAGRGAI-SFAElAATPPTAA----VDAAFAAVGpdTVAKFLF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 198 SSGSTGLPKGVELTHKNIC---VRFSHCRdPVFGNqiiPDTAILTVIPFHHGFGMfttlgylTCGFRIVL-----MY--- 266
Cdd:cd05921 173 TSGSTGLPKAVINTQRMLCanqAMLEQTY-PFFGE---EPPVLVDWLPWNHTFGG-------NHNFNLVLynggtLYidd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 267 ------RCEEELflRSLQDYKIQSALLVPTLFSFFAK-----STLVDKYdLSNLHEIASGGAPLAKEVGE---AVAKRFK 332
Cdd:cd05921 242 gkpmpgGFEETL--RNLREISPTVYFNVPAGWEMLVAalekdEALRRRF-FKRLKLMFYAGAGLSQDVWDrlqALAVATV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 333 LPGIR--QGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDtGKTlgvnqrgELCVKGPMIMKGYVNNPEATSA 410
Cdd:cd05921 319 GERIPmmAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSG-GKY-------EVRVKGPNVTPGYWRQPELTAQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 411 LIDKDGWLHSGD-IAYYDKD----GHFF---IVDRLKsLIKYKGYQVPPAELESILLQHPFIFDAGVAGipdPDAGELPA 482
Cdd:cd05921 391 AFDEEGFYCLGDaAKLADPDdpakGLVFdgrVAEDFK-LASGTWVSVGPLRARAVAACAPLVHDAVVAG---EDRAEVGA 466
|
...
gi 52631875 483 AVV 485
Cdd:cd05921 467 LVF 469
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
52-489 |
2.51e-17 |
|
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: 84.79 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 52 TYSEYFEMACRLAETMK-RYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNdiYNERE--LYNSLSISQPTIVFc 128
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN--YNLSGdpLIHCLKLSGSRFVI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 129 skralqkilgvqkklpiiqkivildsredymgkqsmysfieshlpagfneydYIPDSFdretatALIMNSSGSTGLPKGV 208
Cdd:cd05937 84 ----------------------------------------------------VDPDDP------AILIYTSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 209 ELTHKNiCVRFSHCRDPVFGNQiiPDTAILTVIPFHHGFGMFTTLGY-LTCGFRIVLMYRCEEELFLRSLQDYKIQSALL 287
Cdd:cd05937 106 AISWRR-TLVTSNLLSHDLNLK--NGDRTYTCMPLYHGTAAFLGACNcLMSGGTLALSRKFSASQFWKDVRDSGATIIQY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 288 VPTLFSFFAkSTLVDKYDLSNLHEIASGGApLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIITPEGDDKPGACGKVVP 367
Cdd:cd05937 183 VGELCRYLL-STPPSPYDRDHKVRVAWGNG-LRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 368 ----FFSAKIV----DLDTGKTLGVNQRGeLCVKGP------MIMK----------GYVNNPEATSALIDK------DGW 417
Cdd:cd05937 261 irrwKFENQVVlvkmDPETDDPIRDPKTG-FCVRAPvgepgeMLGRvpfknreafqGYLHNEDATESKLVRdvfrkgDIY 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52631875 418 LHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPD-AGELPAAVVVLEE 489
Cdd:cd05937 340 FRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGhDGRAGCAAITLEE 412
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
52-457 |
2.69e-17 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 85.46 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 52 TYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFF--MPVCGALfiGVGVAPTNDIYNERELYNSLSISQPTIVFCS 129
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIisMEACNAH--GLYCVPLYDTLGAGAVEFIISHSEVSIVFVE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 130 KRALQKILGVQKKLPIIQKIVIL---DSREDYMGKQSM----YSFIESHLPAGFNEYDyIPdsFDRETATALIMNSSGST 202
Cdd:PLN02614 159 EKKISELFKTCPNSTEYMKTVVSfggVSREQKEEAETFglviYAWDEFLKLGEGKQYD-LP--IKKKSDICTIMYTSGTT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 203 GLPKGVELTHKNICVRFS---HCRDPVFGNQIIPDTaILTVIPFHHGFGMFTTLGYLTCGFRIVLmYRCEEELFLRSLQD 279
Cdd:PLN02614 236 GDPKGVMISNESIVTLIAgviRLLKSANAALTVKDV-YLSYLPLAHIFDRVIEECFIQHGAAIGF-WRGDVKLLIEDLGE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 280 YKIQSALLVPTLFS--------------FFAK-----------------------STLVDKYDLS--------NLHEIAS 314
Cdd:PLN02614 314 LKPTIFCAVPRVLDrvysglqkklsdggFLKKfvfdsafsykfgnmkkgqshveaSPLCDKLVFNkvkqglggNVRIILS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 315 GGAPLAKEVgEAVAKRFKLPGIRQGYGLTETTSAIIIT-PEGDDKPGACGKVVPFFSAKIVDLDTGK--TLGVNQRGELC 391
Cdd:PLN02614 394 GAAPLASHV-ESFLRVVACCHVLQGYGLTESCAGTFVSlPDELDMLGTVGPPVPNVDIRLESVPEMEydALASTPRGEIC 472
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52631875 392 VKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKY-KGYQVPPAELESI 457
Cdd:PLN02614 473 IRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENI 538
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
51-508 |
9.84e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.39 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNdiYNERE--LYNSLSISQPTIVFC 128
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN--TQQRGavLAHSLNLVDAKHLIV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 129 SKRALQKILGVQKKLPIIQKIVILDSreDYMGKQSMYSFIESHLpAGFNEYDyiPDSFDRETA--TALIMNSSGSTGLPK 206
Cdd:PRK08279 141 GEELVEAFEEARADLARPPRLWVAGG--DTLDDPEGYEDLAAAA-AGAPTTN--PASRSGVTAkdTAFYIYTSGTTGLPK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 207 GVELTHKNiCVRFSHcrdpVFGN--QIIPDTAILTVIPFHHGFGMFTTLG-YLTCGFRIVLMYRCEEELFLRSLQDYKIq 283
Cdd:PRK08279 216 AAVMSHMR-WLKAMG----GFGGllRLTPDDVLYCCLPLYHNTGGTVAWSsVLAAGATLALRRKFSASRFWDDVRRYRA- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 284 sallvpTLFSFF-----------AKSTlvdkyDLSN-LHEIAsgGAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIi 351
Cdd:PRK08279 290 ------TAFQYIgelcryllnqpPKPT-----DRDHrLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFI- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 352 tpEGDDKPGACGKVvPFFSAK---IV--DLDTGKTLgvnqRGE--LCVK------GPMIMK--------GYvNNPEATSA 410
Cdd:PRK08279 356 --NVFNFDGTVGRV-PLWLAHpyaIVkyDVDTGEPV----RDAdgRCIKvkpgevGLLIGRitdrgpfdGY-TDPEASEK 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 411 LI------DKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDA-GELPAA 483
Cdd:PRK08279 428 KIlrdvfkKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTdGRAGMA 507
|
490 500
....*....|....*....|....*
gi 52631875 484 VVVLEEGKTMTEQEVMDYVAGQVTA 508
Cdd:PRK08279 508 AIVLADGAEFDLAALAAHLYERLPA 532
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
51-535 |
1.54e-16 |
|
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: 82.02 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNdiYNER--ELYNSLSISQPtivfc 128
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN--YNLRgeSLAHCLNVSSA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 129 skralqkilgvqkklpiiqKIVILDsredymgkqsmysfieshlpagfneydyipdsfdretaTALIMNSSGSTGLPKGV 208
Cdd:cd05940 77 -------------------KHLVVD--------------------------------------AALYIYTSGTTGLPKAA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 209 ELTHKNiCVRFSHCRDPVFGNqiIPDTAILTVIPFHHGFGMftTLGYLTC---GFRIVLMYRCEEELFLRSLQDYKIQSA 285
Cdd:cd05940 100 IISHRR-AWRGGAFFAGSGGA--LPSDVLYTCLPLYHSTAL--IVGWSAClasGATLVIRKKFSASNFWDDIRKYQATIF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 286 LLVPTLFSFFAKSTLVDKYDLSNLHEIASGGapLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIitpEGDDKPGACGKV 365
Cdd:cd05940 175 QYIGELCRYLLNQPPKPTERKHKVRMIFGNG--LRPDIWEEFKERFGVPRIAEFYAATEGNSGFI---NFFGKPGAIGRN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 366 VPF----FSAKIV--DLDTGKTLgvnqRGE--LCVK------GPMIMK--------GYVNNPEATSALI-----DKDGWL 418
Cdd:cd05940 250 PSLlrkvAPLALVkyDLESGEPI----RDAegRCIKvprgepGLLISRinplepfdGYTDPAATEKKILrdvfkKGDAWF 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 419 HSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDA-GELPAAVVVLEEGKTMTEQE 497
Cdd:cd05940 326 NTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTdGRAGMAAIVLQPNEEFDLSA 405
|
490 500 510
....*....|....*....|....*....|....*...
gi 52631875 498 VMDYVAGQVTASKRLRgGVKFVDEVPKglTGKIDARKI 535
Cdd:cd05940 406 LAAHLEKNLPGYARPL-FLRLQPEMEI--TGTFKQQKV 440
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-534 |
1.60e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.47 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 15 YPLEDGTagEQLHKAMKRYAQVPGTIAFTDAHaevnITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCG 94
Cdd:PRK12316 3053 YPLERGV--HRLFEEQVERTPDAVALAFGEQR----LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLA 3126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 95 ALFIGVGVAPTNDIYNERELYNSLSISqptivfcskRALQKILGVQKKLPIIQKIVILDSREDymgkqsmysfieshlPA 174
Cdd:PRK12316 3127 ILKAGGAYVPLDPEYPEERLAYMLEDS---------GAQLLLSQSHLRLPLAQGVQVLDLDRG---------------DE 3182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 175 GFNEYDyiPDSFDRETATALIMNSSGSTGLPKGVELTHKNICvrfSHCRDPVFGNQIIPDTAILTVIPFHHGFGMFTTLG 254
Cdd:PRK12316 3183 NYAEAN--PAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALS---NHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFW 3257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 255 YLTCGFRIVLMYRcEEELFLRSLQDYKIQSALLVPTLFSFFAKSTL--VDKYDLSNLHEIASGGAPLAkevGEAVAKRFK 332
Cdd:PRK12316 3258 PLMSGARVVLAGP-EDWRDPALLVELINSEGVDVLHAYPSMLQAFLeeEDAHRCTSLKRIVCGGEALP---ADLQQQVFA 3333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 333 LPGIRQGYGLTETTSAIIITPEGDDKPGA--CGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSA 410
Cdd:PRK12316 3334 GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAE 3412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 411 LIDKDGW------LHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGipdpDAGELPAAV 484
Cdd:PRK12316 3413 RFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAY 3488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 52631875 485 VVLEEGKTMTeQEVMDYVAGQVTASKRLRGGVKFVDEVPKGLTGKIDaRK 534
Cdd:PRK12316 3489 VVPEDEAGDL-REALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLD-RK 3536
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
49-471 |
8.86e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 80.27 E-value: 8.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 49 VNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVFC 128
Cdd:PLN02861 76 VWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 129 SKRALQKILGVQKKLPI-IQKIVILDSREDYMGKQ------SMYSFIESHLpAGFNEYDYIPDsfdRETATALIMNSSGS 201
Cdd:PLN02861 156 QESKISSILSCLPKCSSnLKTIVSFGDVSSEQKEEaeelgvSCFSWEEFSL-MGSLDCELPPK---QKTDICTIMYTSGT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 202 TGLPKGVELTHKNICVR---------------------FS-----HCRDPVFGNQIIPDTAiltVIPFHHGfgmftTLGY 255
Cdd:PLN02861 232 TGEPKGVILTNRAIIAEvlstdhllkvtdrvateedsyFSylplaHVYDQVIETYCISKGA---SIGFWQG-----DIRY 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 256 LT-----------CGfrivlMYRCEEELFLRSLQdyKIQSA-LLVPTLFSFF---------------AKSTLVDKYDLSN 308
Cdd:PLN02861 304 LMedvqalkptifCG-----VPRVYDRIYTGIMQ--KISSGgMLRKKLFDFAynyklgnlrkglkqeEASPRLDRLVFDK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 309 LHE--------IASGGAPLAKEVgEAVAKRFKLPGIRQGYGLTETTSAIIiTPEGDDKP--GACGKVVPFFSAKIVDL-D 377
Cdd:PLN02861 377 IKEglggrvrlLLSGAAPLPRHV-EEFLRVTSCSVLSQGYGLTESCGGCF-TSIANVFSmvGTVGVPMTTIEARLESVpE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 378 TG-KTLGVNQRGELCVKGPMIMKGYVNNPEATSALIdKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKY-KGYQVPPAELE 455
Cdd:PLN02861 455 MGyDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLE 533
|
490
....*....|....*.
gi 52631875 456 SILLQHPFIFDAGVAG 471
Cdd:PLN02861 534 NTYSRCPLIASIWVYG 549
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-485 |
1.14e-15 |
|
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: 79.43 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 183 PDSF---DRETATALIMNSSGSTGLPKGVELTHKNICVRFSHCRDpVFGnqIIPDTAILTVIPFhhgFGMFT-TLGYLTC 258
Cdd:cd05910 75 PDAFigiPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQ-LYG--IRPGEVDLATFPL---FALFGpALGLTSV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 259 gfrIVLM-----YRCEEELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVaKRFKL 333
Cdd:cd05910 149 ---IPDMdptrpARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARL-RKMLS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 334 PG--IRQGYGLTETTSAIII---------TPEGDDKPGAC-GKVVPFFSAKIVDLDTGKTLGVNQR--------GELCVK 393
Cdd:cd05910 225 DEaeILTPYGATEALPVSSIgsrellattTAATSGGAGTCvGRPIPGVRVRIIEIDDEPIAEWDDTlelprgeiGEITVT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 394 GPMIMKGYVNNPEATSALIDKDG----WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGV 469
Cdd:cd05910 305 GPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384
|
330
....*....|....*.
gi 52631875 470 AGIPDPdAGELPAAVV 485
Cdd:cd05910 385 VGVGKP-GCQLPVLCV 399
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
193-533 |
1.10e-14 |
|
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: 76.32 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHKNIcVRFSHCRDPVFG----------NQIIPDTAILTVIPfhhgfgmfTTLGYLTCGFRI 262
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMIEHQSL-VNLSHGLIKEYGitssdrvlqfASIAFDVAAEEIYV--------TLLSGATLVLRP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 263 VLMYRCEEElFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKYDL-SNLHEIASGGAPLAKEVGEAVAKRF-KLPGIRQGY 340
Cdd:cd17644 180 EEMRSSLED-FVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 341 GLTETTSAIII------TPEGDDKPgACGKVVPFFSAKIVDlDTGKTLGVNQRGELCVKGPMIMKGYVNNPEATSALIDK 414
Cdd:cd17644 259 GPTEATIAATVcrltqlTERNITSV-PIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 415 DGWLHS--------GDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIfdagvagipdpdagelPAAVVV 486
Cdd:cd17644 337 HPFNSSeserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV----------------KTAVVI 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52631875 487 LEEGKTMTEQEVMdYVAGQVTAS---KRLRGGVK-----------FV--DEVPKGLTGKIDAR 533
Cdd:cd17644 401 VREDQPGNKRLVA-YIVPHYEESpstVELRQFLKaklpdymipsaFVvlEELPLTPNGKIDRR 462
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
190-508 |
5.64e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 74.59 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 190 TATALIMNSSGSTGLPKGVELTHKNICVRFSHC-RD--PVFGNQIIPDTAILTVIPFHHGFGMFttLGY---LTCGFRIV 263
Cdd:PRK05850 160 PSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmSDyfGDTGGVPPPDTTVVSWLPFYHDMGLV--LGVcapILGGCPAV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 264 LMyrcEEELFLRSLQDYkIQSALLVPTLFSF---FA------KSTLVD--KYDLSNLHEIASGgaplAKEVGEAVAKRF- 331
Cdd:PRK05850 238 LT---SPVAFLQRPARW-MQLLASNPHAFSAapnFAfelavrKTSDDDmaGLDLGGVLGIISG----SERVHPATLKRFa 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 332 ------KLP--GIRQGYGLTETTSAIIITPEGDD----------------KPGACGKVVPFFS--------AKIVDLDTG 379
Cdd:PRK05850 310 drfapfNLRetAIRPSYGLAEATVYVATREPGQPpesvrfdyeklsaghaKRCETGGGTPLVSygsprsptVRIVDPDTC 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 380 KTLGVNQRGELCVKGPMIMKGYVNNPEAT-----------SALIDKDGWLHSGDIAYYDkDGHFFIVDRLKSLIKYKGYQ 448
Cdd:PRK05850 390 IECPAGTVGEIWVHGDNVAAGYWQKPEETertfgatlvdpSPGTPEGPWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRN 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52631875 449 VPPAELESILLQhpfIFDAGVAGI--PDPDAGELPAAVVVLEEGKtmTEQEVMDY---VAGQVTA 508
Cdd:PRK05850 469 HYPDDIEATIQE---ITGGRVAAIsvPDDGTEKLVAIIELKKRGD--SDEEAMDRlrtVKREVTS 528
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
41-461 |
1.19e-13 |
|
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: 73.28 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 41 AFTDAHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSI 120
Cdd:cd17654 7 IIDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 121 SQptivfcSKRALQKILGVQKKLPIIQKIVILDSREDYmgkqsmysfieshlpagfneydyipdsfdretATALIMNSSG 200
Cdd:cd17654 87 CH------VSYLLQNKELDNAPLSFTPEHRHFNIRTDE--------------------------------CLAYVIHTSG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 201 STGLPKGVELTHKNICVRFSHCRD--PVFGNQIIPDTAILTVIPFHHGFGMFTTLGyltCGFRIV-LMYRCEEELFLRSL 277
Cdd:cd17654 129 TTGTPKIVAVPHKCILPNIQHFRSlfNITSEDILFLTSPLTFDPSVVEIFLSLSSG---ATLLIVpTSVKVLPSKLADIL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 278 -QDYKIQSALLVPTLFSFFAKSTLVDKY--DLSNLHEIASGGAPLAKEVgEAVAKRFKLPGIR--QGYGLTETTS-AII- 350
Cdd:cd17654 206 fKRHRITVLQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPFPSLV-ILSSWRGKGNRTRifNIYGITEVSCwALAy 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 351 ITPEGdDKPGACGKVVPFFSAKIVDLDTGKTLGVNQRGELcvKGPMIMKGYVNNPEATsalidkdgWLHSGDIAYYdKDG 430
Cdd:cd17654 285 KVPEE-DSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGL--NRVCILDDEVTVPKGT--------MRATGDFVTV-KDG 352
|
410 420 430
....*....|....*....|....*....|.
gi 52631875 431 HFFIVDRLKSLIKYKGYQVPPAELESILLQH 461
Cdd:cd17654 353 ELFFLGRKDSQIKRRGKRINLDLIQQVIESC 383
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
180-530 |
1.61e-13 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 73.53 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 180 DYIPDSFDretATALIMNSSGSTGLPKGVELTHKNICVRF-SHCRDPVfgnQIIPDTAILTVIPFHHGFGMFTTLGY-LT 257
Cdd:PRK06060 138 GYEPMGGD---ALAYATYTSGTTGPPKAAIHRHADPLTFVdAMCRKAL---RLTPEDTGLCSARMYFAYGLGNSVWFpLA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 258 CGFRIV---LMYRCEEELFLRSlqdyKIQSALL--VPTLFSFFAKSTLVDKYdlSNLHEIASGGAPLAKEVGEAVAKRFK 332
Cdd:PRK06060 212 TGGSAVinsAPVTPEAAAILSA----RFGPSVLygVPNFFARVIDSCSPDSF--RSLRCVVSAGEALELGLAERLMEFFG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 333 LPGIRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDLDtGKTLGVNQRGELCVKGPMIMKGYVNNPEatsALI 412
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPV 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 413 DKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKT 492
Cdd:PRK06060 362 ANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAT 441
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 52631875 493 MTEQeVMDYV----AGQVTASKrLRGGVKFVDEVPKGLTGKI 530
Cdd:PRK06060 442 IDGS-VMRDLhrglLNRLSAFK-VPHRFAVVDRLPRTPNGKL 481
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
192-470 |
1.74e-13 |
|
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: 72.50 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 192 TALIMNSSGSTGLPKGVELTHKNIcVRFSHCRDPVFGNQIIPdTAILTVIPFhhGFGMFT---TLGYLTCGfrivLMYRC 268
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHRNV-AHAAHAWRREYELDSFP-VRLLQMASF--SFDVFAgdfARSLLNGG----TLVIC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 269 EEELFL------RSLQDYKIQSALLVPTLFSFFAKSTLVDKYDLSNLHEIASGGAPLAKEVGEAVAKRFkLPGIR--QGY 340
Cdd:cd17650 167 PDEVKLdpaalyDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARF-GQGMRiiNSY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 341 GLTETTSAIIITPEGDDKPGACGKV---VPFFSAKIVDLDTGKTL---GVnqRGELCVKGPMIMKGYVNNPEATSALIDK 414
Cdd:cd17650 246 GVTEATIDSTYYEEGRDPLGDSANVpigRPLPNTAMYVLDERLQPqpvGV--AGELYIGGAGVARGYLNRPELTAERFVE 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52631875 415 DGW------LHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVA 470
Cdd:cd17650 324 NPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA 385
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
24-537 |
2.46e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.28 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 24 EQLHKAMkryAQVPGTIAFTdaHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVA 103
Cdd:PRK05691 1135 ELLNEQA---RQTPERIALV--WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYV 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 104 PTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVILDSREDYmgkqsmysfieshlPAGFNEYDyip 183
Cdd:PRK05691 1210 PLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWPSQ--------------APGLHLHG--- 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 184 DSFdretatALIMNSSGSTGLPKGVELTHKNICVRFSHCRDPVfgnQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIV 263
Cdd:PRK05691 1273 DNL------AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATY---ALDDSDVLMQKAPISFDVSVWECFWPLITGCRLV 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 264 LMYRCEE---ELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDkyDLSNLHEIASGGAPLAKEVGEAVAKRfkLPGIR--Q 338
Cdd:PRK05691 1344 LAGPGEHrdpQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQR--LPQVQlhN 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 339 GYGLTETtsAIIIT------PEGDDKPgaCGKVVPFFSAKIVDLDTGKT-LGVnqRGELCVKGPMIMKGYVNNPEATSA- 410
Cdd:PRK05691 1420 RYGPTET--AINVThwqcqaEDGERSP--IGRPLGNVLCRVLDAELNLLpPGV--AGELCIGGAGLARGYLGRPALTAEr 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 411 -LIDKDG-----WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAgIPDPDAGELPAAV 484
Cdd:PRK05691 1494 fVPDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGY 1572
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52631875 485 VVLEEG--------KTMTEQEVMDY-VAGQVTAskrlrggvkfVDEVPKGLTGKIDARKIRE 537
Cdd:PRK05691 1573 YTGEAGqeaeaerlKAALAAELPEYmVPAQLIR----------LDQMPLGPSGKLDRRALPE 1624
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
178-464 |
4.03e-13 |
|
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: 71.72 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 178 EYDYIPDSFDRetaTALIMNSSGSTGLPKGVELTHKNIcVRFSHCRDPVFGNQiiPDTAI-LTVIPFHHGFGMFTTLGYL 256
Cdd:cd17632 214 PLFRPEPDDDP---LALLIYTSGSTGTPKGAMYTERLV-ATFWLKVSSIQDIR--PPASItLNFMPMSHIAGRISLYGTL 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 257 TCG----F-------------------RIVLMYRCEEELFLR--SLQDYKIQSALLVPTLfSFFAKSTLVDKYDLSNLHE 311
Cdd:cd17632 288 ARGgtayFaaasdmstlfddlalvrptELFLVPRVCDMLFQRyqAELDRRSVAGADAETL-AERVKAELRERVLGGRLLA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 312 IASGGAPLAKEVGEAVAKRFKLPgIRQGYGLTETTSAIIItpegddkpgacGKVV--PFFSAKIVDL-DTG--KTLGVNQ 386
Cdd:cd17632 367 AVCGSAPLSAEMKAFMESLLDLD-LHDGYGSTEAGAVILD-----------GVIVrpPVLDYKLVDVpELGyfRTDRPHP 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52631875 387 RGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPFI 464
Cdd:cd17632 435 RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLV 513
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
308-443 |
4.10e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 72.06 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 308 NLHEIASGGAPLAKEVGEAVAKRFKLpGIRQGYGLTETTSAIIITPEGDDKPGACG-KVVPFFSAKIVDLDTGKTLGVNQ 386
Cdd:PTZ00342 462 NLEVILNGGGKLSPKIAEELSVLLNV-NYYQGYGLTETTGPIFVQHADDNNTESIGgPISPNTKYKVRTWETYKATDTLP 540
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 52631875 387 RGELCVKGPMIMKGYVNNPEATSALIDKDGWLHSGDIAYYDKDGHFFIVDRLKSLIK 443
Cdd:PTZ00342 541 KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
51-480 |
7.56e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 71.23 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 51 ITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAP--------TNDIYNERELYNSLsisQ 122
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPvspayslmSHDHAKLKHLFDLV---K 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 123 PTIVFCSK-----RALQ--KILGVQkklpiiqkIVILDSREDYMGKQSMYSFIESHLPAGFNEydyipdSFDRET--ATA 193
Cdd:PRK12582 158 PRVVFAQSgapfaRALAalDLLDVT--------VVHVTGPGEGIASIAFADLAATPPTAAVAA------AIAAITpdTVA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 194 LIMNSSGSTGLPKGVELTHKNIC--------VRfshCRDPvfgNQIIPDtaILTVIPFHHGFGmfttlGylTCGFRIVL- 264
Cdd:PRK12582 224 KYLFTSGSTGMPKAVINTQRMMCaniamqeqLR---PREP---DPPPPV--SLDWMPWNHTMG-----G--NANFNGLLw 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 265 ----MY----RCEEELF---LRSLQDYKIQSALLVPTLFSFFAKSTLVDKyDL-----SNLHEIASGGAPLAKEVGE--- 325
Cdd:PRK12582 289 gggtLYiddgKPLPGMFeetIRNLREISPTVYGNVPAGYAMLAEAMEKDD-ALrrsffKNLRLMAYGGATLSDDLYErmq 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 326 AVAKRF---KLPgIRQGYGLTETTSAIIITPEGDDKPGACGKVVPFFSAKIVDldtgktlgVNQRGELCVKGPMIMKGYV 402
Cdd:PRK12582 368 ALAVRTtghRIP-FYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAP--------VGDKYEVRVKGPNVTPGYH 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 403 NNPEATSALIDKDGWLHSGDIA-YYDKDghffivDRLKSLI-------KYK---GYQVPPAELESILLQ--HPFIFDAGV 469
Cdd:PRK12582 439 KDPELTAAAFDEEGFYRLGDAArFVDPD------DPEKGLIfdgrvaeDFKlstGTWVSVGTLRPDAVAacSPVIHDAVV 512
|
490
....*....|.
gi 52631875 470 AGIPDPDAGEL 480
Cdd:PRK12582 513 AGQDRAFIGLL 523
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
111-536 |
7.67e-13 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 70.93 E-value: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 111 EReLYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQK--IVILDSREDYMGKqsmysfieshlpagfneyDYIPDSFDR 188
Cdd:PRK12476 132 ER-LDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRprVIAIDAIPDSAGE------------------SFVPVELDT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 189 EtATALIMNSSGSTGLPKGVELTHKNICVRFShcrdpvfgnQII-------PDTAILTVIPFHHGFG----MFTTLgylt 257
Cdd:PRK12476 193 D-DVSHLQYTSGSTRPPVGVEITHRAVGTNLV---------QMIlsidlldRNTHGVSWLPLYHDMGlsmiGFPAV---- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 258 CGFRIVLM---------YRCEEELFLRSLQDYKIQSAllvPTL-FSFFAKSTLV---DKYDLSNLHEIaSGGAPL---AK 321
Cdd:PRK12476 259 YGGHSTLMsptafvrrpQRWIKALSEGSRTGRVVTAA---PNFaYEWAAQRGLPaegDDIDLSNVVLI-IGSEPVsidAV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 322 EVGEAVAKRFKLP--GIRQGYGLTETT------------SAIIITPEG----------DDKPGA-----CGKVVPFFSAK 372
Cdd:PRK12476 335 TTFNKAFAPYGLPrtAFKPSYGIAEATlfvatiapdaepSVVYLDREQlgagravrvaADAPNAvahvsCGQVARSQWAV 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 373 IVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEAT-----------------SALIDKDG-WLHSGDIAYYdKDGHFFI 434
Cdd:PRK12476 415 IVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegshADGAADDGtWLRTGDLGVY-LDGELYI 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 435 VDRLKSLIKYKGYQVPPAELE-SILLQHPFIFDAGVAGIPDPdAGELPAAVVVLEE--GKTMTE-QEVMDYVAGQVTASK 510
Cdd:PRK12476 494 TGRIADLIVIDGRNHYPQDIEaTVAEASPMVRRGYVTAFTVP-AEDNERLVIVAERaaGTSRADpAPAIDAIRAAVSRRH 572
|
490 500
....*....|....*....|....*....
gi 52631875 511 RLR-GGVKFVDE--VPKGLTGKIDARKIR 536
Cdd:PRK12476 573 GLAvADVRLVPAgaIPRTTSGKLARRACR 601
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
193-535 |
5.09e-12 |
|
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: 68.20 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 193 ALIMNSSGSTGLPKGVELTHK---NICVRFSHcrdpVFGNQIIPDTAILTVIPFHHGFGMFTTLGYLTCGFRIVLM---Y 266
Cdd:cd17648 97 AYAIYTSGTTGKPKGVLVEHGsvvNLRTSLSE----RYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPpdeM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 267 RCEEELFLRSLQDYKIqsallvpTLFSffAKSTLVDKYDLS---NLHEIASGGAPLAKEVGEAVAKRFKLPgIRQGYGLT 343
Cdd:cd17648 173 RFDPDRFYAYINREKV-------TYLS--GTPSVLQQYDLArlpHLKRVDAAGEEFTAPVFEKLRSRFAGL-IINAYGPT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 344 ETT-SAIIITPEGDD-KPGACGKVVPFFSAKIVDLDTgKTLGVNQRGELCVKGPMIMKGYVNNPEATS------------ 409
Cdd:cd17648 243 ETTvTNHKRFFPGDQrFDKSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTAerflpnpfqteq 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 410 -------ALIDKDG----WLHSGDIAYydkdghffiVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAG 478
Cdd:cd17648 322 erargrnARLYKTGdlvrWLPSGELEY---------LGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQA 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52631875 479 ELPA-----AVVVLEEGkTMTEQEVMDYVAGQVTAS---KRLrggVKfVDEVPKGLTGKIDARKI 535
Cdd:cd17648 393 QSRIqkylvGYYLPEPG-HVPESDLLSFLRAKLPRYmvpARL---VR-LEGIPVTINGKLDVRAL 452
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
63-517 |
7.44e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 67.59 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 63 LAETMKRYGLGLQHH-------IAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELynslsisqptivfcskralqk 135
Cdd:PRK09029 34 LCARIDQLAAGFAQQgvvegsgVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL--------------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 136 ilgvQKKLPIIQKIVILDSREDymgkqSMYSFIESHLPAGFNEYDYIPDSFDRetaTALIMNSSGSTGLPKGVELTHKNi 215
Cdd:PRK09029 93 ----EELLPSLTLDFALVLEGE-----NTFSALTSLHLQLVEGAHAVAWQPQR---LATMTLTSGSTGLPKAAVHTAQA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 216 cvrfsH-------CRDPVFGNQiipDTAILTvIPFHHGFGMFTTLGYLTCGFRIVLMyrcEEELFLRSLQDykIQSALLV 288
Cdd:PRK09029 160 -----HlasaegvLSLMPFTAQ---DSWLLS-LPLFHVSGQGIVWRWLYAGATLVVR---DKQPLEQALAG--CTHASLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 289 PT----LFSFFAKSTLvdkydlsnLHEIASGGAPLAKEVGEAVAKRfklpGIRQ--GYGLTETTSAIIITpEGDDKPGAc 362
Cdd:PRK09029 226 PTqlwrLLDNRSEPLS--------LKAVLLGGAAIPVELTEQAEQQ----GIRCwcGYGLTEMASTVCAK-RADGLAGV- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 363 GKVVPFFSAKIVDldtgktlgvnqrGELCVKGPMIMKGYVNNPEATSaLIDKDGWLHSGDIAYYDkDGHFFIVDRLKSLI 442
Cdd:PRK09029 292 GSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 443 KYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKtmTEQEVMDYVAGQVTASKR----------- 511
Cdd:PRK09029 358 FSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEA--AVVNLAEWLQDKLARFQQpvayyllppel 435
|
....*.
gi 52631875 512 LRGGVK 517
Cdd:PRK09029 436 KNGGIK 441
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
194-537 |
8.45e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.90 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 194 LIMNSSGSTGLPKGVELTHKNICvrfshcRDPVFGNQIIPDTAILTVI---PFHHGFGMFT-TLGYLTCGFRIVLMYRCE 269
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRSWTEID------REIEAYNEALNCEQDETPIvacPVTHSYGLICgVLAALTRGSKPVIITNKN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 270 EELFLRSLQDYKIQSALLVPTLFSFFAKSTLVDKydlsNLHEIASGGAPLAKEVGEAVAKRFKLpgIRQGYGLTETtSAI 349
Cdd:PRK08308 179 PKFALNILRNTPQHILYAVPLMLHILGRLLPGTF----QFHAVMTSGTPLPEAWFYKLRERTTY--MMQQYGCSEA-GCV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 350 IITPEGDDkPGACGKVVPFfsakiVDLDTGKtlGVNQRGELCVKgpmimkgyVNNPEatsalidkdgwLHSGDIAYYDKD 429
Cdd:PRK08308 252 SICPDMKS-HLDLGNPLPH-----VSVSAGS--DENAPEEIVVK--------MGDKE-----------IFTKDLGYKSER 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 430 GHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEgkTMTEQEVMDYVAGQVtAS 509
Cdd:PRK08308 305 GTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE--EIDPVQLREWCIQHL-AP 381
|
330 340
....*....|....*....|....*...
gi 52631875 510 KRLRGGVKFVDEVPKGLTGKIdARKIRE 537
Cdd:PRK08308 382 YQVPHEIESVTEIPKNANGKV-SRKLLE 408
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
346-538 |
1.11e-10 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 64.15 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 346 TSAIIITP---EGDDKPGACgkVVPFFSAK--IVDlDTGKTLGVNQRGELCVKG--PMIMKGYVNNPE--ATSALIDKDG 416
Cdd:PLN02654 437 TGGFMITPlpgAWPQKPGSA--TFPFFGVQpvIVD-EKGKEIEGECSGYLCVKKswPGAFRTLYGDHEryETTYFKPFAG 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 417 WLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEEGKTMTEQ 496
Cdd:PLN02654 514 YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 52631875 497 ---EVMDYVAGQVTASKRlRGGVKFVDEVPKGLTGKIDARKIREI 538
Cdd:PLN02654 594 lrkSLILTVRNQIGAFAA-PDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
49-536 |
3.51e-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: 62.37 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 49 VNITYSEYFEMACRLAETM-KRYGLGLQHHIAVCSENSLQFFMPVCGALFIGVGVAPTNDIYNERELYNSLSISQPTIVF 127
Cdd:cd05905 13 TTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 128 ----CSKRALQKILGVQKKLPIIQKIV---ILDsredymgkqsmysFIESHLPAGFNEYDYIPDSFDRETATALIMNSSG 200
Cdd:cd05905 93 tveaCLKGLPKKLLKSKTAAEIAKKKGwpkILD-------------FVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 201 STGLPKGVELTHKNIcvrFSHCRDPVFGNQIIPDTAILTVIPFHHGFG-MFTTL-----GYLTCGFRIVLMYRCEEeLFL 274
Cdd:cd05905 160 SDGSLSGVAVSHSSL---LAHCRALKEACELYESRPLVTVLDFKSGLGlWHGCLlsvysGHHTILIPPELMKTNPL-LWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 275 RSLQDYKIQSALLvptLFSFFAKSTLVDKYDLSNLHE------------IASGGAPLAKeVGEAVAKRFKLPGIRQGYGL 342
Cdd:cd05905 236 QTLSQYKVRDAYV---KLRTLHWCLKDLSSTLASLKNrdvnlsslrmcmVPCENRPRIS-SCDSFLKLFQTLGLSPRAVS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 343 TETTSAII---------------------------ITPEGDDKPGA-----CGKVVPFFSAKIVDLDTGKTLGVNQRGEL 390
Cdd:cd05905 312 TEFGTRVNpficwqgtsgpepsrvyldmralrhgvVRLDERDKPNSlplqdSGKVLPGAQVAIVNPETKGLCKDGEIGEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 391 CVKGPMIMKGY------------VNNPEATSALIDKDGWLHSGDIAY----------YDKDGHFFIVDRLKSLIKYKGYQ 448
Cdd:cd05905 392 WVNSPANASGYflldgetndtfkVFPSTRLSTGITNNSYARTGLLGFlrptkctdlnVEEHDLLFVVGSIDETLEVRGLR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 449 VPPAELE-SILLQHPFIFDAGVAgipdpDAGELpaaVVVLEEGKTMTEQEVMDY---VAGQVTASKRLRGG-VKFVD--E 521
Cdd:cd05905 472 HHPSDIEaTVMRVHPYRGRCAVF-----SITGL---VVVVAEQPPGSEEEALDLvplVLNAILEEHQVIVDcVALVPpgS 543
|
570
....*....|....*
gi 52631875 522 VPKGLTGKIDARKIR 536
Cdd:cd05905 544 LPKNPLGEKQRMEIR 558
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
301-543 |
6.49e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 61.71 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 301 VDKYDLSNLHEIASGGAPLAKE----VGEAVAkRFKL-PG-IRQGYGLTETTSAI-------------IITPEGD--DKP 359
Cdd:PRK05851 266 VSDVDLGALRVALNGGEPVDCDgferFATAMA-PFGFdAGaAAPSYGLAESTCAVtvpvpgiglrvdeVTTDDGSgaRRH 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 360 GACGKVVPFFSAKIVDLDTGKTLGVNQRGELCVKGPMIMKGYVNNPEatsalIDKDGWLHSGDIAYYdKDGHFFIVDRLK 439
Cdd:PRK05851 345 AVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL-VDGGLVVCGRAK 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 440 SLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLE---EGKTMTEQEVMDYVAGQ--VTASKrlrg 514
Cdd:PRK05851 419 ELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEfrgPDEAGARSEVVQRVASEcgVVPSD---- 494
|
250 260 270
....*....|....*....|....*....|.
gi 52631875 515 gVKFVD--EVPKGLTGKIDARKIREILMMGK 543
Cdd:PRK05851 495 -VVFVApgSLPRTSSGKLRRLAVKRSLEAAD 524
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
20-485 |
7.75e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.11 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 20 GTAGEQ-----LHKAM-KRYAQVPGTIAFTdaHAEVNITYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVC 93
Cdd:PRK05691 2179 GEAGEArldqtLHGLFaAQAARTPQAPALT--FAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLL 2256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 94 GALFIGVGVAPTNDIYNERELYNSLSISQPTIVFcSKRALQKILGvqkKLPiiqkivildsreDYMGKQSMysfiESHLP 173
Cdd:PRK05691 2257 AILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL-SDRALFEALG---ELP------------AGVARWCL----EDDAA 2316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 174 AGFNEYDYIPDSFDRETATALIMNSSGSTGLPKGVELTHKNICVrfsHCRDPV--FGNQiiPDTAILTVIPFHHGFGMFT 251
Cdd:PRK05691 2317 ALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAM---HCQAVIerFGMR--ADDCELHFYSINFDAASER 2391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 252 TLGYLTCGFRIVL----MYRCEEELFLrsLQDYKIQSALLVPTLFSFFAKsTLVDKYDLSNLHEIASGGAPLAKEVGEAV 327
Cdd:PRK05691 2392 LLVPLLCGARVVLraqgQWGAEEICQL--IREQQVSILGFTPSYGSQLAQ-WLAGQGEQLPVRMCITGGEALTGEHLQRI 2468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 328 AKRFKLPGIRQGYGLTETTSAIIITPEGDDKP-GAC----GKVVPFFSAKIVDLD-----TGKTlgvnqrGELCVKGPMI 397
Cdd:PRK05691 2469 RQAFAPQLFFNAYGPTETVVMPLACLAPEQLEeGAAsvpiGRVVGARVAYILDADlalvpQGAT------GELYVGGAGL 2542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 398 MKGYVNNPEATSALIDKDGWLH-------SGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVA 470
Cdd:PRK05691 2543 AQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVL 2622
|
490
....*....|....*
gi 52631875 471 GIPDPDAGELPAAVV 485
Cdd:PRK05691 2623 ALDTPSGKQLAGYLV 2637
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
316-536 |
1.77e-08 |
|
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: 57.05 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 316 GAPLAKEVGEAVAKRFKLPGIRQGYGLTETTSAIIitpEGDDKPGACGkVVPFFSAKI-------VDLDTGKTLgvNQRG 388
Cdd:cd05939 226 GNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLV---NIDNHVGACG-FNSRILPSVypirlikVDEDTGELI--RDSD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 389 ELCVK------GPMIMK-----------GYVNNpEATSALIDKDGWLH------SGDIAYYDKDGHFFIVDRLKSLIKYK 445
Cdd:cd05939 300 GLCIPcqpgepGLLVGKiiqndplrrfdGYVNE-GATNKKIARDVFKKgdsaflSGDVLVMDELGYLYFKDRTGDTFRWK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 446 GYQVPPAELESILLQHPFIFDAGVAGIPDPDA-GELPAAVVVLEEGKTMTEQEVMDyVAGQVTASKR---LRggvkFVDE 521
Cdd:cd05939 379 GENVSTTEVEGILSNVLGLEDVVVYGVEVPGVeGRAGMAAIVDPERKVDLDRFSAV-LAKSLPPYARpqfIR----LLPE 453
|
250
....*....|....*
gi 52631875 522 VPKGLTGKIDARKIR 536
Cdd:cd05939 454 VDKTGTFKLQKTDLQ 468
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
190-503 |
1.96e-08 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 56.92 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 190 TATALIMNSSGSTGLPKGVELTHKNI--CVRFSHcrdpVFGnqIIPDTAILTVIPFHHGFGMFttLGYLTC---GFRIVL 264
Cdd:cd05938 144 KSPALYIYTSGTTGLPKAARISHLRVlqCSGFLS----LCG--VTADDVIYITLPLYHSSGFL--LGIGGCielGATCVL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 265 MYRCEEELFLRSLQDYKIQSALLVPTLFSFFAKS--TLVDKYDLSNLhEIASGgapLAKEVGEAVAKRFKLPGIRQGYGL 342
Cdd:cd05938 216 KPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQpqSPNDRDHKVRL-AIGNG---LRADVWREFLRRFGPIRIREFYGS 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 343 TETTSAIIITPegdDKPGACGKVVPF----FSAKIVDLDTGKTLGVNQRGELCVK------GPMIMK--------GYVNN 404
Cdd:cd05938 292 TEGNIGFFNYT---GKIGAVGRVSYLykllFPFELIKFDVEKEEPVRDAQGFCIPvakgepGLLVAKitqqspflGYAGD 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 405 PEATSaliDK---------DGWLHSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDP 475
Cdd:cd05938 369 KEQTE---KKllrdvfkkgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVP 445
|
330 340
....*....|....*....|....*....
gi 52631875 476 D-AGELPAAVVVLEEGKTMTEQEVMDYVA 503
Cdd:cd05938 446 GhEGRIGMAAVKLKPGHEFDGKKLYQHVR 474
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
15-470 |
7.48e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.48 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 15 YPLEDGTAgeQLHKAmkRYAQVPGTIAFTDAHAEVNitYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCG 94
Cdd:PRK05691 3716 YPLEQSYV--RLFEA--QVAAHPQRIAASCLDQQWS--YAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVG 3789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 95 ALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSKRALQKILGVQKKLPIIQKIVILdsredyMGKQSMYSFIESHLPA 174
Cdd:PRK05691 3790 SFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLDELGCANRPRLL------VWEEVQAGEVASHNPG 3863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 175 GFNEydyiPDSFdretatALIMNSSGSTGLPKGVELTHKN-------------------ICVRFSHCRD---------PV 226
Cdd:PRK05691 3864 IYSG----PDNL------AYVIYTSGSTGLPKGVMVEQRGmlnnqlskvpylalseadvIAQTASQSFDisvwqflaaPL 3933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 227 FGNQ--IIPDTAIltvipfHHGFGMfttlgyltcgfrivlmyrceeelfLRSLQDYKIQSALLVPTLFSFFAKStlvDKY 304
Cdd:PRK05691 3934 FGARveIVPNAIA------HDPQGL------------------------LAHVQAQGITVLESVPSLIQGMLAE---DRQ 3980
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 305 DLSNLHEIASGGAPLAKEVGEAVAKRFKLPGIRQGYGltettsaiiitpegddkPGACGKVVPFFSakiVDLD--TGKTL 382
Cdd:PRK05691 3981 ALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYG-----------------PAECSDDVAFFR---VDLAstRGSYL 4040
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 383 GV-----NQR----------------GELCVKGPMIMKGYVNNPEATS-ALIDK------DGWLHSGDIAYYDKDGHFFI 434
Cdd:PRK05691 4041 PIgsptdNNRlylldealelvplgavGELCVAGTGVGRGYVGDPLRTAlAFVPHpfgapgERLYRTGDLARRRSDGVLEY 4120
|
490 500 510
....*....|....*....|....*....|....*.
gi 52631875 435 VDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVA 470
Cdd:PRK05691 4121 VGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVA 4156
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
135-540 |
9.63e-06 |
|
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: 48.42 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 135 KILGVQKKLPIIQKIVIL-----DSREDY--MGKQSMYSFIESHLPAGFNEYDYIPdsFDretATALIMNSSGSTGLPK- 206
Cdd:cd05943 192 KVAELVKGLPSLLAVVVVpytvaAGQPDLskIAKALTLEDFLATGAAGELEFEPLP--FD---HPLYILYSSGTTGLPKc 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 207 ------GVELTH-KNICVrfsHCrDPVFGNQIIpdtailtvipfhhgfgMFTTLGY---------LTCGFRIVL-----M 265
Cdd:cd05943 267 ivhgagGTLLQHlKEHIL---HC-DLRPGDRLF----------------YYTTCGWmmwnwlvsgLAVGATIVLydgspF 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 266 YRCEEELFlrSLQDyKIQSALLV--PTLFSFFAKSTLV--DKYDLSNLHEIASGGAPLAKE----VGEAVAKRFKLPGIR 337
Cdd:cd05943 327 YPDTNALW--DLAD-EEGITVFGtsAKYLDALEKAGLKpaETHDLSSLRTILSTGSPLKPEsfdyVYDHIKPDVLLASIS 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 338 QGyglTETTSAIIIT-PEGDDKPGACGKVVPFFSAKIVDlDTGKTLgVNQRGEL-CVKG-PMIMKGYVNNPEAT---SAL 411
Cdd:cd05943 404 GG---TDIISCFVGGnPLLPVYRGEIQCRGLGMAVEAFD-EEGKPV-WGEKGELvCTKPfPSMPVGFWNDPDGSryrAAY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 412 IDK-DG-WLHsGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGVAGIPDPDAGELPAAVVVLEE 489
Cdd:cd05943 479 FAKyPGvWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLRE 557
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 490 GKTMTEQevmdyVAGQVTASKRLRGGVKFV-------DEVPKGLTGKIDARKIREILM 540
Cdd:cd05943 558 GVELDDE-----LRKRIRSTIRSALSPRHVpakiiavPDIPRTLSGKKVEVAVKKIIA 610
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
15-469 |
3.05e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 46.96 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 15 YPLEDGTAGEQLHKAMKRyaqVPGTIAFTDAHAEVniTYSEYFEMACRLAETMKRYGLGLQHHIAVCSENSLQFFMPVCG 94
Cdd:PRK10252 453 VEIPETTLSALVAQQAAK---TPDAPALADARYQF--SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 95 ALFIGVGVAPTNDIYNERELYNSLSISQPTIVFCSKralqkilGVQKKLPIIQKIVILDSRedymgkqsmysfieSHLPA 174
Cdd:PRK10252 528 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA-------DQLPRFADVPDLTSLCYN--------------APLAP 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 175 GfneyDYIPDSFDRETATALIMNSSGSTGLPKGVELTHKNICVRFSHCRD--PvfgnqIIPDTAILTVIPFHHGFGMFTT 252
Cdd:PRK10252 587 Q----GAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNhyP-----LTADDVVLQKTPCSFDVSVWEF 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 253 LGYLTCGFRIVLM----YRCEEELfLRSLQDYKIQSALLVPTLFSFFAKSTLVD--KYDLSNLHEIASGGAPLAKEVGEA 326
Cdd:PRK10252 658 FWPFIAGAKLVMAepeaHRDPLAM-QQFFAEYGVTTTHFVPSMLAAFVASLTPEgaRQSCASLRQVFCSGEALPADLCRE 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52631875 327 VAKRFKLPgIRQGYGLTEttSAIIIT--P-EGDDKPGACGKVVPF-FSA-----KIVDlDTGKTLGVNQRGELCVKGPMI 397
Cdd:PRK10252 737 WQQLTGAP-LHNLYGPTE--AAVDVSwyPaFGEELAAVRGSSVPIgYPVwntglRILD-ARMRPVPPGVAGDLYLTGIQL 812
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52631875 398 MKGYVNNPEATSALIDKDGWL------HSGDIAYYDKDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPFIFDAGV 469
Cdd:PRK10252 813 AQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVT 890
|
|
| |
