|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1196-1674 |
4.41e-137 |
|
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: 433.95 E-value: 4.41e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1196 QVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLT 1275
Cdd:cd05911 2 QIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1276 SPKIVFTVSSSAANLMEAAKELKMNLKVVVM-DKLDGYESVEENVMKGHDTREIIEFKCHVTNPDDVALIVPSSGTTGLP 1354
Cdd:cd05911 82 KPKVIFTDPDGLEKVKEAAKELGPKDKIIVLdDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1355 KGTEISHYSL-----FCCLHPYKNRTLVGHTCIVTPtMRWHYGVLMAFrLVAANAKKLIVPDNDDAENFCQLIEKYQITW 1429
Cdd:cd05911 162 KGVCLSHRNLianlsQVQTFLYGNDGSNDVILGFLP-LYHIYGLFTTL-ASLLNGATVIIMPKFDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1430 FGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVVSaQNKFT--KLGSVG 1507
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILT-VNPDGddKPGSVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1508 YVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFIN 1587
Cdd:cd05911 319 RLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1588 FRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRGGVKIVDQLP 1667
Cdd:cd05911 399 YKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVFVDEIP 478
|
....*..
gi 1820754837 1668 RTTTGKI 1674
Cdd:cd05911 479 KSASGKI 485
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
54-537 |
3.35e-118 |
|
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: 381.95 E-value: 3.35e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 54 AQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSL 133
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 134 TKPKIVFVNGESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVlRSQDTAWiDEFECAKlTSPKHVAAIVCSSGT 213
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSP-TLGEEDE-DLPPPLK-DGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 214 SGFPKGTEISHAAMINYMAHVKVHdLKGHVSmwtPSMRWYC--------GLFIVIKAILdCSKRIIVPDYDDDEGLCRFI 285
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTF-LYGNDG---SNDVILGflplyhiyGLFTTLASLL-NGATVIIMPKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 286 EKYEVSWfrcdSCFP----IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDYGGLCArQT 361
Cdd:cd05911 233 EKYKITF----LYLVppiaAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILT-VN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 362 KYS--KPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEV 439
Cdd:cd05911 308 PDGddKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 440 FLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYCRL 519
Cdd:cd05911 388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQL 467
|
490
....*....|....*...
gi 1820754837 520 HAGVKFMEKLPRTATGKI 537
Cdd:cd05911 468 RGGVVFVDEIPKSASGKI 485
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
619-1099 |
6.26e-109 |
|
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: 356.14 E-value: 6.26e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 619 QIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHV--VSKLSarYFLS 696
Cdd:cd05911 2 QIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIytADELA--HQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 697 LMSPKVVFVNEESAENLMEAAKEENLQVRVMVIGSLPGFV-SLANILEEQVSRAEIDGFRCtKIDNPHDLAMICSSSGTT 775
Cdd:cd05911 80 ISKPKVIFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVlSIEDLLSPTLGEEDEDLPPP-LKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 776 GMPKGTELSYaslYNSITPVEEVHAKNEICAWVPTIR-------WHGGLNQCIEVIMSNAKWIIFSDDNIkeIALCEIIQ 848
Cdd:cd05911 159 GLPKGVCLSH---RNLIANLSQVQTFLYGNDGSNDVIlgflplyHIYGLFTTLASLLNGATVIIMPKFDS--ELFLDLIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 849 KHGVTWLGTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAGG-LCVSQAKNSK 927
Cdd:cd05911 234 KYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGiLTVNPDGDDK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 928 PGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRI 1007
Cdd:cd05911 314 PGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1008 SDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYCKLQAGIKF 1087
Cdd:cd05911 394 KELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGGVVF 473
|
490
....*....|..
gi 1820754837 1088 VNDFPRISTGKI 1099
Cdd:cd05911 474 VDEIPKSASGKI 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1172-1679 |
4.51e-108 |
|
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: 354.23 E-value: 4.51e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1172 IPKRPvNIAEETLKFLKSKPDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMY 1251
Cdd:cd05904 1 LPTDL-PLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1252 IGAISNTWDHELTPMTARNFLTLTSPKIVFTVSSSAANLMEAAkelkmnLKVVVMDKLDG---YESVEENVMKGHDTREI 1328
Cdd:cd05904 80 LGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLA------LPVVLLDSAEFdslSFSDLLFEADEAEPPVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1329 iefkchVTNPDDVALIVPSSGTTGLPKGTEISHYSLF---CCLHPYKNRTLVGHTCIVTPTMRWH-YG-VLMAFRLVAAN 1403
Cdd:cd05904 154 ------VIKQDDVAALLYSSGTTGRSKGVMLTHRNLIamvAQFVAGEGSNSDSEDVFLCVLPMFHiYGlSSFALGLLRLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1404 AKKLIVPDNDdAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITN 1483
Cdd:cd05904 228 ATVVVMPRFD-LEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1484 HYGMTDTACVVSAQNKF----TKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSD 1559
Cdd:cd05904 307 GYGMTESTGVVAMCFAPekdrAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1560 GWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTE 1639
Cdd:cd05904 387 GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTE 466
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1820754837 1640 QELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQL 1679
Cdd:cd05904 467 DEIMDFVAKQVAPYKKVR-KVAFVDAIPKSPSGKILRKEL 505
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1184-1682 |
4.82e-105 |
|
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: 346.82 E-value: 4.82e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1184 LKFLKSKPDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHEL 1263
Cdd:cd17642 24 MKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1264 TPMTARNFLTLTSPKIVFTVSSSAANLMEAAKELKMNLKVVVMD---KLDGYESVEeNVMKGHDTREIIE--FKCHVTNP 1338
Cdd:cd17642 104 NERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDskeDYKGYQCLY-TFITQNLPPGFNEydFKPPSFDR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1339 D-DVALIVPSSGTTGLPKGTEISHYSLFC----CLHPYKNRTLVGHTCIVTpTMRWHYGVLM---------AFRLVaana 1404
Cdd:cd17642 183 DeQVALIMNSSGSTGLPKGVQLTHKNIVArfshARDPIFGNQIIPDTAILT-VIPFHHGFGMfttlgylicGFRVV---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1405 kklIVPDNDDaENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNH 1484
Cdd:cd17642 258 ---LMYKFEE-ELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVVSAQNK-FTKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLR 1563
Cdd:cd17642 334 YGLTETTSAILITPEgDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1564 TGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELI 1643
Cdd:cd17642 414 SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVM 493
|
490 500 510
....*....|....*....|....*....|....*....
gi 1820754837 1644 SYVEKNLPDYCRLRGGVKIVDQLPRTTTGKIARKQLRDM 1682
Cdd:cd17642 494 DYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1202-1683 |
2.65e-100 |
|
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: 330.23 E-value: 2.65e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVF 1281
Cdd:COG0318 22 GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1282 TvsssaanlmeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchvtnpddvALIVPSSGTTGLPKGTEISH 1361
Cdd:COG0318 102 T-----------------------------------------------------------ALILYTSGTTGRPKGVMLTH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1362 YSLFCCLHPYKNRTLVGHTCIVTPTMRWH--YGVLMAFRLVAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIK 1439
Cdd:COG0318 123 RNLLANAAAIAAALGLTPGDVVLVALPLFhvFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1440 FIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACVVS---AQNKFTKLGSVGYVSSNVRIK 1516
Cdd:COG0318 203 LLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTvnpEDPGERRPGSVGRPLPGVEVR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1517 MVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFDsDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPA 1596
Cdd:COG0318 282 IVDEDGRE-LPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1597 EIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIAR 1676
Cdd:COG0318 360 EVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPR-RVEFVDELPRTASGKIDR 438
|
....*..
gi 1820754837 1677 KQLRDMY 1683
Cdd:COG0318 439 RALRERY 445
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
42-542 |
4.35e-93 |
|
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: 311.86 E-value: 4.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 42 VLEKLRSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNE 121
Cdd:cd05904 11 SFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 122 LSPMTARYFLSLTKPKIVFVNGESAECLAQVVKEnnmdtrlVVFADSAGFVGRAAtltavlrSQDTAWIDEFECAK-LTS 200
Cdd:cd05904 91 STPAEIAKQVKDSGAKLAFTTAELAEKLASLALP-------VVLLDSAEFDSLSF-------SDLLFEADEAEPPVvVIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 201 PKHVAAIVCSSGTSGFPKGTEISHAAMINYMAHVkvhdLKGHVSMWTPSMRWYC--------GLFIVIKAILDCSKRIIV 272
Cdd:cd05904 157 QDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQF----VAGEGSNSDSEDVFLCvlpmfhiyGLSSFALGLLRLGATVVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 273 -PDYDDDEGLcRFIEKYEVSWFrcdSCFP---IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSY 348
Cdd:cd05904 233 mPRFDLEELL-AAIERYKVTHL---PVVPpivLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 349 GMTDYGGLCAR----QTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGW 424
Cdd:cd05904 309 GMTESTGVVAMcfapEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 425 LHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELD 504
Cdd:cd05904 389 LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDE 468
|
490 500 510
....*....|....*....|....*....|....*....
gi 1820754837 505 ITDLV-KQNMPwYCRLHAgVKFMEKLPRTATGKIAKKQL 542
Cdd:cd05904 469 IMDFVaKQVAP-YKKVRK-VAFVDAIPKSPSGKILRKEL 505
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
38-550 |
3.07e-88 |
|
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: 295.95 E-value: 3.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 38 VGALVLEKLRSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNP 117
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 118 WDNELSPMTARYFLSLTKPKIVFVngesaeclaqvvkennmdtrlvvfadsagfvgraatltavlrsqdtawidefecak 197
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 198 ltspkhvAAIVCSSGTSGFPKGTEISHAAMI-NYMAHVKVHDLkghvsmwTPSMRWYC--------GLFIVIKAILDCSK 268
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNLLaNAAAIAAALGL-------TPGDVVLValplfhvfGLTVGLLAPLLAGA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 269 RIIVPDYDDDEGLCRFIEKYEVSWFrcdSCFP---IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLpHTDVI 345
Cdd:COG0318 169 TLVLLPRFDPERVLELIERERVTVL---FGVPtmlARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 346 LSYGMTDYGGLCA---RQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDsD 422
Cdd:COG0318 245 EGYGLTETSPVVTvnpEDPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-D 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 423 GWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTE 502
Cdd:COG0318 323 GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDA 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 503 LDITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLKQIAKSYA 550
Cdd:COG0318 403 EELRAFLRERLARYKVPRR-VEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
42-545 |
1.68e-86 |
|
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: 293.66 E-value: 1.68e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 42 VLEKLRSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNE 121
Cdd:cd17642 23 AMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 122 LSPMTARYFLSLTKPKIVFVNGESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDTAwideFECAKLTSP 201
Cdd:cd17642 103 YNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPG----FNEYDFKPP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 202 -----KHVAAIVCSSGTSGFPKGTEISHAAMINYMAHVKVHDLKGHVSMWTPSMR---WY--CGLFIVIkAILDCSKRII 271
Cdd:cd17642 179 sfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTvipFHhgFGMFTTL-GYLICGFRVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 272 VPDYDDDEGLCRFIEKYEV-SWFRCDSCFPIrLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGM 350
Cdd:cd17642 258 LMYKFEEELFLRSLQDYKVqSALLVPTLFAF-FAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 351 TDY-GGLCARQTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGD 429
Cdd:cd17642 337 TETtSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 430 LGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLV 509
Cdd:cd17642 417 IAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYV 496
|
490 500 510
....*....|....*....|....*....|....*.
gi 1820754837 510 KQNMPWYCRLHAGVKFMEKLPRTATGKIAKKQLKQI 545
Cdd:cd17642 497 ASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1202-1680 |
5.99e-86 |
|
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: 289.85 E-value: 5.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMtarNFLtLTSPKIVF 1281
Cdd:cd05936 22 GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV-------VVPL---NPL-YTPRELEH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1282 TVSSSAANLMEAAKELKmnlkvvvmDKLDGYESVEENVmkghdtreiiefkchVTNPDDVALIVPSSGTTGLPKGTEISH 1361
Cdd:cd05936 91 ILNDSGAKALIVAVSFT--------DLLAAGAPLGERV---------------ALTPEDVAVLQYTSGTTGVPKGAMLTH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1362 YSLFC----CLHPYKNRTLVGHTCIVTPTMrWH-YG---VLMAFrlVAANAKKLIVPdNDDAENFCQLIEKYQITWFGTD 1433
Cdd:cd05936 148 RNLVAnalqIKAWLEDLLEGDDVVLAALPL-FHvFGltvALLLP--LALGATIVLIP-RFRPIGVLKEIRKHRVTIFPGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1434 PFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACVVSAqNKFT---KLGSVGYVS 1510
Cdd:cd05936 224 PTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAV-NPLDgprKPGSIGIPL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1511 SNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFDsDGWLRTGDLAYYDDNGEIYIVDRISDFINFRS 1590
Cdd:cd05936 302 PGTEVKIVDDDGEE-LPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1591 INVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTT 1670
Cdd:cd05936 380 FNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPR-QVEFRDELPKSA 458
|
490
....*....|
gi 1820754837 1671 TGKIARKQLR 1680
Cdd:cd05936 459 VGKILRRELR 468
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
620-1099 |
1.52e-82 |
|
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: 281.43 E-value: 1.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 620 IDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvVSKLSARY----FL 695
Cdd:cd05904 25 IDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT----ANPLSTPAeiakQV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 696 SLMSPKVVFVneeSAENlmeAAKEENLQVRVMVIGSLPgFVSLANILEEQvsrAEIDGFRCTKIDNPHDLAMICSSSGTT 775
Cdd:cd05904 101 KDSGAKLAFT---TAEL---AEKLASLALPVVLLDSAE-FDSLSFSDLLF---EADEAEPPVVVIKQDDVAALLYSSGTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 776 GMPKGTELSYASLynsITPVEEVHAkneicAWVPTIRWHG------------GLNQCIEVIMSN-AKWIIFSDDNIKEia 842
Cdd:cd05904 171 GRSKGVMLTHRNL---IAMVAQFVA-----GEGSNSDSEDvflcvlpmfhiyGLSSFALGLLRLgATVVVMPRFDLEE-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 843 LCEIIQKHGVTWLGTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAGG---LC 919
Cdd:cd05904 241 LLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGvvaMC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 920 VSQAKNS-KPGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDEN 998
Cdd:cd05904 321 FAPEKDRaKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 999 GEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWY 1078
Cdd:cd05904 401 GYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPY 480
|
490 500
....*....|....*....|.
gi 1820754837 1079 CKLQAgIKFVNDFPRISTGKI 1099
Cdd:cd05904 481 KKVRK-VAFVDAIPKSPSGKI 500
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1340-1674 |
3.60e-82 |
|
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: 273.78 E-value: 3.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1340 DVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRTLVGHTCIVTPTMRW-HYGVLMAFRLVAANAKKLIVPDNDDAENF 1418
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLfHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1419 CQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNhYGMTDTACVVS--- 1495
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNG-YGLTETGGTVAtgp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1496 AQNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTkQAFDSDGWLRTGDLAYYDDNGE 1575
Cdd:cd04433 160 PDDDARKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1576 IYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCR 1655
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKV 317
|
330
....*....|....*....
gi 1820754837 1656 LRgGVKIVDQLPRTTTGKI 1674
Cdd:cd04433 318 PR-RVVFVDALPRTASGKI 335
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
588-1100 |
2.02e-81 |
|
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: 279.03 E-value: 2.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 588 VLIGTGETHPVCA-NVGEL---VLNRLSSKPDFVGQIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHL 663
Cdd:cd17642 1 IIVGPGPFYPLEDgTAGEQlhkAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 664 NTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNEESAENLMEAAKEENLQVRVMVIGS---LPGFVSLAN 740
Cdd:cd17642 81 QFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSkedYKGYQCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 741 ILEEQVSRA-EIDGFRCTKIDNPHDLAMICSSSGTTGMPKGTELSY----ASLYNSITPVEeVHAKNEICAWVPTIRWHG 815
Cdd:cd17642 161 FITQNLPPGfNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHknivARFSHARDPIF-GNQIIPDTAILTVIPFHH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 816 GLNQCIEVIMSNAKWIIFSDDNIKEIALCEIIQKHGVTW-LGTDTNFAILyVKMNIFQKYPMPSLRKMVITGAPFTKELH 894
Cdd:cd17642 240 GFGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSaLLVPTLFAFF-AKSTLVDKYDLSNLHEIASGGAPLSKEVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 895 ETVAKIMPHTQILQCYGLTDA-GGLCVSQAKNSKPGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKN 973
Cdd:cd17642 319 EAVAKRFKLPGIRQGYGLTETtSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 974 PEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAF 1053
Cdd:cd17642 399 PEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAV 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1820754837 1054 VQKVVEKEVTEEELHDLVNKNLPWYCKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd17642 479 VVLEAGKTMTEKEVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKID 525
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1201-1683 |
4.48e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 277.45 E-value: 4.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1201 TGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTARnfltLTSPKIV 1280
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAV-------LHPINIR----LKPEEIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1281 FT----------VSSSAANLMEAAKE-LKMNLKVVVMDKLDGYESVE-----ENVMKGH-DTREIIEFKchvtnPDDVAL 1343
Cdd:PRK06187 97 YIlndaedrvvlVDSEFVPLLAAILPqLPTVRTVIVEGDGPAAPLAPevgeyEELLAAAsDTFDFPDID-----ENDAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1344 IVPSSGTTGLPKGTEISHYSLF-----CCLHPYKNRTLVGhtCIVTP---TMRWHYGVlMAFrLVAAnakKLIVPDNDDA 1415
Cdd:PRK06187 172 MLYTSGTTGHPKGVVLSHRNLFlhslaVCAWLKLSRDDVY--LVIVPmfhVHAWGLPY-LAL-MAGA---KQVIPRRFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1416 ENFCQLIEKYQITWFGTDPFMIikfiksQLLEKYRLPT------LKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTD 1489
Cdd:PRK06187 245 ENLLDLIETERVTFFFAVPTIW------QMLLKAPRAYfvdfssLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1490 TACVVSA-------QNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNK--IGELRVKAITIMQGYHKNPETTKQAFDsDG 1560
Cdd:PRK06187 318 TSPVVSVlppedqlPGQWTKRRSAGRPLPGVEARIVDDDGDE-LPPDGgeVGEIIVRGPWLMQGYWNRPEATAETID-GG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1561 WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQ 1640
Cdd:PRK06187 396 WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAK 475
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1820754837 1641 ELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK06187 476 ELRAFLRGRLAKFKLPK-RIAFVDELPRTSVGKILKRVLREQY 517
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
623-1100 |
5.84e-80 |
|
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: 272.07 E-value: 5.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvvskLSARYflslmspkv 702
Cdd:COG0318 20 FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP-------LNPRL--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 vfvneeSAENLMEAAkeENLQVRVMVIgslpgfvslanileeqvsraeidgfrctkidnphdlAMICSSSGTTGMPKGTE 782
Cdd:COG0318 84 ------TAEELAYIL--EDSGARALVT------------------------------------ALILYTSGTTGRPKGVM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 783 LSYASLYNSITPVEEVHAKNE---ICAWVPtirWH--GGLNQCI-EVIMSNAKWIIFSDDNIKEIAlcEIIQKHGVTWLG 856
Cdd:COG0318 120 LTHRNLLANAAAIAAALGLTPgdvVLVALP---LFhvFGLTVGLlAPLLAGATLVLLPRFDPERVL--ELIERERVTVLF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 857 TDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYGLTDAGGLCVS---QAKNSKPGSCGF 933
Cdd:COG0318 195 GVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVnpeDPGERRPGSVGR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 934 VTKGIRIKIADEkTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDsDGWLHTKDIGYYDENGEIFFVNRISDFINY 1013
Cdd:COG0318 274 PLPGVEVRIVDE-DGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1014 KAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPR 1093
Cdd:COG0318 352 GGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARY-KVPRRVEFVDELPR 430
|
....*..
gi 1820754837 1094 ISTGKID 1100
Cdd:COG0318 431 TASGKID 437
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1191-1676 |
1.62e-79 |
|
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: 269.87 E-value: 1.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTARn 1270
Cdd:cd17631 9 PDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAV-------FVPLNFR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 fltLTSPKIVFTVSSSAAnlmeaakelkmnlKVVVmdkldgyesveenvmkghdtreiiefkchvtnpDDVALIVPSSGT 1350
Cdd:cd17631 79 ---LTPPEVAYILADSGA-------------KVLF---------------------------------DDLALLMYTSGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISHYSLF----CCLHPYK----NRTLVG----HT----CIVTPTMrwHYGVlmafrlvaanakKLIVPDNDD 1414
Cdd:cd17631 110 TGRPKGAMLTHRNLLwnavNALAALDlgpdDVLLVVaplfHIgglgVFTLPTL--LRGG------------TVVILRKFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1415 AENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKlpDVFITNHYGMTDT---A 1491
Cdd:cd17631 176 PETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETspgV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1492 CVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFDsDGWLRTGDLAYYD 1571
Cdd:cd17631 254 TFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGRE-VPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1572 DNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLP 1651
Cdd:cd17631 332 EDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLA 411
|
490 500
....*....|....*....|....*
gi 1820754837 1652 DYCRLRgGVKIVDQLPRTTTGKIAR 1676
Cdd:cd17631 412 RYKIPK-SVEFVDALPRNATGKILK 435
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1197-1680 |
3.62e-79 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 272.62 E-value: 3.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1197 VDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTS 1276
Cdd:PLN02246 43 IDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1277 PKIVFTVSSSAANLMEAAKElkMNLKVVVMDKL-DGYESVEENVMKghDTREIIEFKCHvtnPDDVALIVPSSGTTGLPK 1355
Cdd:PLN02246 123 AKLIITQSCYVDKLKGLAED--DGVTVVTIDDPpEGCLHFSELTQA--DENELPEVEIS---PDDVVALPYSSGTTGLPK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1356 GTEISHYSLFcclhpyknrtlvghTCIV------TPTMRWHYG-----VLMAFRLVAAN----------AKKLIVPDNDD 1414
Cdd:PLN02246 196 GVMLTHKGLV--------------TSVAqqvdgeNPNLYFHSDdvilcVLPMFHIYSLNsvllcglrvgAAILIMPKFEI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1415 AEnFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVV 1494
Cdd:PLN02246 262 GA-LLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGPVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1495 S-----AQNKF-TKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLA 1568
Cdd:PLN02246 341 AmclafAKEPFpVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1569 YYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEK 1648
Cdd:PLN02246 421 YIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAK 500
|
490 500 510
....*....|....*....|....*....|..
gi 1820754837 1649 NLPDYCRLRgGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:PLN02246 501 QVVFYKRIH-KVFFVDSIPKAPSGKILRKDLR 531
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1206-1589 |
2.32e-75 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 257.24 E-value: 2.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFTVSS 1285
Cdd:pfam00501 23 TYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 -SAANLMEAAKELKMNLKVVVMDKLDGYESVEENVMKGHDTREIIEFKChvTNPDDVALIVPSSGTTGLPKGTEISHYSL 1364
Cdd:pfam00501 103 lKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPP--PDPDDLAYIIYTSGTTGKPKGVMLTHRNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1365 ------FCCLHPYKNRTLVGHTCIVTPTMRWHYGVLMAFRLVAANAKKLIVPDND---DAENFCQLIEKYQITWFGTDPF 1435
Cdd:pfam00501 181 vanvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFpalDPAALLELIERYKVTVLYGVPT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1436 MIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVfITNHYGMTDTACVVSA----QNKFTKLGSVGYVSS 1511
Cdd:pfam00501 261 LLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVTTplplDEDLRSLGSVGRPLP 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1512 NVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFR 1589
Cdd:pfam00501 340 GTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
42-543 |
1.98e-74 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 258.76 E-value: 1.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 42 VLEKLRSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIS---NPW 118
Cdd:PLN02246 29 CFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTttaNPF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 119 DNelSPMTARYFLSlTKPKIVFVNGESAECLAQVVKENNMdtrLVVFADSA--GFVGRAATLTAvlrsqdtawiDEFECA 196
Cdd:PLN02246 109 YT--PAEIAKQAKA-SGAKLIITQSCYVDKLKGLAEDDGV---TVVTIDDPpeGCLHFSELTQA----------DENELP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 197 KLT-SPKHVAAIVCSSGTSGFPKGTEISHAAMINYMA----------HVKVHDLkghVSMWTPSMRWYCglfivIKAILD 265
Cdd:PLN02246 173 EVEiSPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqvdgenpnlYFHSDDV---ILCVLPMFHIYS-----LNSVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 266 CSKR-----IIVPDYDDDEgLCRFIEKYEVSWfrcdSCF--PIRL--VKFGVLSKYRLPTLKILLFGGAHFKGELQQTLV 336
Cdd:PLN02246 245 CGLRvgaaiLIMPKFEIGA-LLELIQRHKVTI----APFvpPIVLaiAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 337 KLLPHTDVILSYGMTDYG---GLC---ARQTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYN 410
Cdd:PLN02246 320 AKLPNAVLGQGYGMTEAGpvlAMClafAKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 411 NPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMA 490
Cdd:PLN02246 400 DPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVA 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 491 FVAKVPGKEVTELDITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLK 543
Cdd:PLN02246 480 FVVRSNGSEITEDEIKQFVAKQVVFYKRIHK-VFFVDSIPKAPSGKILRKDLR 531
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1178-1683 |
4.53e-73 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 255.81 E-value: 4.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1178 NIAEETL-KFLKSKPDSIgqvdAL-----TGKVQ--TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGT 1249
Cdd:COG0365 9 NIAYNCLdRHAEGRGDKV----ALiwegeDGEERtlTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLAC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1250 MYIGAISNTwdheLTPMTA----RNFLTLTSPKIVFTVSSSA---------ANLMEAAKELKMNLKVVVMDKLDGYESVE 1316
Cdd:COG0365 85 ARIGAVHSP----VFPGFGaealADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1317 -----ENVMKGHDTreiiEFKCHVTNPDDVALIVPSSGTTGLPKGTEISHyslfcclhpyknRTLVGHTCIvtpTMRWH- 1390
Cdd:COG0365 161 gdldwDELLAAASA----EFEPEPTDADDPLFILYTSGTTGKPKGVVHTH------------GGYLVHAAT---TAKYVl 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1391 ---------------------YGVLMAFR----LVAANAKklivPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKS-- 1443
Cdd:COG0365 222 dlkpgdvfwctadigwatghsYIVYGPLLngatVVLYEGR----PDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAgd 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1444 QLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDT-ACVVSAQNKF-TKLGSVGYVSSNVRIKMVDlD 1521
Cdd:COG0365 298 EPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAV-GVPIVDGWGQTETgGIFISNLPGLpVKPGSMGKPVPGYDVAVVD-E 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1522 TEEALGPNKIGELRVKA--ITIMQGYHKNPETTKQAF--DSDGWLRTGDLAYYDDNGEIYIVDRISDFINfRS-INVSPA 1596
Cdd:COG0365 376 DGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVIN-VSgHRIGTA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1597 EIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTE---QELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGK 1673
Cdd:COG0365 455 EIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDelaKELQAHVREELGPYAYPR-EIEFVDELPKTRSGK 533
|
570
....*....|
gi 1820754837 1674 IARKQLRDMY 1683
Cdd:COG0365 534 IMRRLLRKIA 543
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1191-1681 |
1.40e-70 |
|
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: 246.07 E-value: 1.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARN 1270
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 FLTLTSPKIVFTVSSSAANLMEAAKELKMNLKVVVMDKLDGYESVEENVMKGHDTREIIEFKCHVTNPDDVALIVPSSGT 1350
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISHYSLFC---------CLHPyKNRTLvghtcIVTPTMRWH--YGVLMAFRLVAANAkklIVPDNDDAENFC 1419
Cdd:cd05926 161 TGRPKGVPLTHRNLAAsatnitntyKLTP-DDRTL-----VVMPLFHVHglVASLLSTLAAGGSV---VLPPRFSASTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1420 QLIEKYQITWFGTDPfMIIKFIKSQLLEKYR--LPTLKVILSSGAHLRKEHLEVMREKL--PdVFITnhYGMTDTACVVS 1495
Cdd:cd05926 232 PDVRDYNATWYTAVP-TIHQILLNRPEPNPEspPPKLRFIRSCSASLPPAVLEALEATFgaP-VLEA--YGMTEAAHQMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1496 AqNKFT----KLGSVGyVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYD 1571
Cdd:cd05926 308 S-NPLPpgprKPGSVG-KPVGVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1572 DNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLP 1651
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLA 464
|
490 500 510
....*....|....*....|....*....|
gi 1820754837 1652 DYcRLRGGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd05926 465 AF-KVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1188-1682 |
1.96e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 246.35 E-value: 1.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1188 KSKPDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDvFLI-LLGTMYIGAIS---NTwdhEL 1263
Cdd:PRK07656 16 RRFGDKEAYVFG--DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPH-WVIaALGALKAGAVVvplNT---RY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1264 TPMTARNFLTLTSPKIVFTVSSSAANLMEAAKELKmNLKVVVM-------DKLDGYESVEENVMKGHDTREIIEFKchvt 1336
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLFLGVDYSATTRLP-ALEHVVIceteeddPHTEKMKTFTDFLAAGDPAERAPEVD---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1337 nPDDVALIVPSSGTTGLPKGTEISH---YSLFCCLHPY-----KNRTLVG----HT-----CIVTPTMRwhygvlmafrl 1399
Cdd:PRK07656 165 -PDDVADILFTSGTTGRPKGAMLTHrqlLSNAADWAEYlglteGDRYLAAnpffHVfgykaGVNAPLMR----------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1400 vaaNAKKLIVPDNDDAENFcQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDV 1479
Cdd:PRK07656 233 ---GATILPLPVFDPDEVF-RLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1480 FITNHYGMTDtACVVSAQNKF-----TKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQ 1554
Cdd:PRK07656 309 IVLTGYGLSE-ASGVTTFNRLdddrkTVAGTIGTAIAGVENKIVNELGEE-VPVGEVGELLVRGPNVMKGYYDDPEATAA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1555 AFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPN 1634
Cdd:PRK07656 387 AIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 1635 KSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRDM 1682
Cdd:PRK07656 467 AELTEEELIAYCREHLAKYKVPR-SIEFLDELPKNATGKVLKRALREK 513
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
629-1014 |
3.62e-70 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 242.22 E-value: 3.62e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhVVSKLSA---RYFLSLMSPKVVFV 705
Cdd:pfam00501 23 TYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP---LNPRLPAeelAYILEDSGAKVLIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 706 NEESAENLMEAAKEENLQVRVMVIGSLPGFVSLANILEEQVSRAeiDGFRCTKIDNPHDLAMICSSSGTTGMPKGTELSY 785
Cdd:pfam00501 100 DDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAD--VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 786 ASLYNSIT-------PVEEVHAKNEICAWVPTirWHG-GLNQCIEVIMSN-AKWIIFSDDNIKEI-ALCEIIQKHGVTWL 855
Cdd:pfam00501 178 RNLVANVLsikrvrpRGFGLGPDDRVLSTLPL--FHDfGLSLGLLGPLLAgATVVLPPGFPALDPaALLELIERYKVTVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 856 GTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHtQILQCYGLTDAGGLCVSQA----KNSKPGSC 931
Cdd:pfam00501 256 YGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVTTPLpldeDLRSLGSV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 932 GFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFI 1011
Cdd:pfam00501 335 GRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQI 414
|
...
gi 1820754837 1012 NYK 1014
Cdd:pfam00501 415 KLG 417
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
606-1099 |
1.27e-68 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 241.81 E-value: 1.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 606 VLNRLSSKPDFVGQIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGII------ 679
Cdd:PLN02246 29 CFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTttanpf 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 680 CPWDHVVSKLSARyflslmSPKVVFVNEESAENLMEAAKEENlqVRVMVIGSLP----GFVSLANILEEQVSRAEIdgfr 755
Cdd:PLN02246 109 YTPAEIAKQAKAS------GAKLIITQSCYVDKLKGLAEDDG--VTVVTIDDPPegclHFSELTQADENELPEVEI---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 756 ctkidNPHDLAMICSSSGTTGMPKGTELSYASLYNSITpvEEVHAKNeicawvPTIRWHGGlnqciEVIMSNAKWI-IFS 834
Cdd:PLN02246 177 -----SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA--QQVDGEN------PNLYFHSD-----DVILCVLPMFhIYS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 835 DDNIK----------------EI-ALCEIIQKHGVTWLGTDTNFAILYVKMNIFQKYPMPSLRkMVITG-APFTKELHET 896
Cdd:PLN02246 239 LNSVLlcglrvgaailimpkfEIgALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIR-MVLSGaAPLGKELEDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 897 VAKIMPHTQILQCYGLTDAG---GLCVSQAKNS---KPGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGY 970
Cdd:PLN02246 318 FRAKLPNAVLGQGYGMTEAGpvlAMCLAFAKEPfpvKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 971 HKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELP 1050
Cdd:PLN02246 398 LNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVP 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1820754837 1051 LAFVQKVVEKEVTEEELHDLVNKNLPWYCKLQAgIKFVNDFPRISTGKI 1099
Cdd:PLN02246 478 VAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHK-VFFVDSIPKAPSGKI 525
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
203-537 |
4.97e-66 |
|
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: 227.55 E-value: 4.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 203 HVAAIVCSSGTSGFPKGTEISHAAMINYMAHVKVHDLKGH--VSMWTPSMRWYCGLFIVIKAILdCSKRIIVPDYDDDEG 280
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEgdVFLSTLPLFHIGGLFGLLGALL-AGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 281 LCRFIEKYEVSWFrcdSCFP---IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLlPHTDVILSYGMTDYGG-- 355
Cdd:cd04433 80 ALELIEREKVTIL---LGVPtllARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGtv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 356 -LCARQTKYSKPGSCGFVCETGRLKVVDPNTGKvLGANKTGEIWAKSSYMMNGYYNNPEATRrALDSDGWLHTGDLGYYD 434
Cdd:cd04433 156 aTGPPDDDARKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEATA-AVDEDGWYRTGDLGRLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 435 NDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMP 514
Cdd:cd04433 234 EDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLA 313
|
330 340
....*....|....*....|....*.
gi 1820754837 515 wycrLHAGVK---FMEKLPRTATGKI 537
Cdd:cd04433 314 ----PYKVPRrvvFVDALPRTASGKI 335
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1164-1681 |
6.77e-65 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 231.02 E-value: 6.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1164 ILIGKELSIPKRPVNIAEETlkflkskPDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVF 1243
Cdd:PLN02330 22 VPVPDKLTLPDFVLQDAELY-------ADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1244 LILLGTMYIGAisntwdheltpmtarnfltltspkiVFTVSSSAANLMEAAKELKM-NLKVVVMDKLDgYESV------- 1315
Cdd:PLN02330 95 IVALGIMAAGG-------------------------VFSGANPTALESEIKKQAEAaGAKLIVTNDTN-YGKVkglglpv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1316 ----EENVMKGHDTREIIEF--KCHVTNPDDVAL-----IVP-SSGTTGLPKGTEISHYSLFC--CLHPYKNRT-LVGHT 1380
Cdd:PLN02330 149 ivlgEEKIEGAVNWKELLEAadRAGDTSDNEEILqtdlcALPfSSGTTGISKGVMLTHRNLVAnlCSSLFSVGPeMIGQV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1381 CIVTPTMRWH-YGVLMAFRLVAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKV--I 1457
Cdd:PLN02330 229 VTLGLIPFFHiYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1458 LSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVV------SAQNKFTKLGSVGYVSSNVRIKMVDLDTEEALGPNKI 1531
Cdd:PLN02330 309 MTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITlthgdpEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1532 GELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQA 1611
Cdd:PLN02330 389 GELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDA 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1612 AVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PLN02330 469 AVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVR-VVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
47-452 |
1.11e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 226.42 E-value: 1.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAqVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMT 126
Cdd:pfam00501 6 ARTPDKTA-LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 127 ARYFLSLTKPKIVFVNGESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDTAWIDEfecakLTSPKHVAA 206
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPP-----PPDPDDLAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 207 IVCSSGTSGFPKGTEISHAAMINYMAHVKVHDLKGHVSMWTPSMRWY------CGLFIVIKAILDCSKRIIVPDYD---D 277
Cdd:pfam00501 160 IIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTlplfhdFGLSLGLLGPLLAGATVVLPPGFpalD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 278 DEGLCRFIEKYEVSWFrcdSCFP---IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTdVILSYGMTDYG 354
Cdd:pfam00501 240 PAALLELIERYKVTVL---YGVPtllNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 355 GLCA----RQTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDL 430
Cdd:pfam00501 316 GVVTtplpLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDL 395
|
410 420
....*....|....*....|..
gi 1820754837 431 GYYDNDGEVFLVDRMSEFINYR 452
Cdd:pfam00501 396 GRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
764-1100 |
4.23e-63 |
|
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: 219.08 E-value: 4.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 764 DLAMICSSSGTTGMPKGTELSYASLYNSITPVEEVHAKNE---ICAWVPTIrWHGGLNQCIEVIMSNAKWIIFSDDNIKE 840
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEgdvFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 841 IalCEIIQKHGVTWLGTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETvAKIMPHTQILQCYGLTDAGG--- 917
Cdd:cd04433 80 A--LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLER-FEEAPGIKLVNGYGLTETGGtva 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 918 LCVSQAKNSKPGSCGFVTKGIRIKIADEKTGIaLGPKERGEICIKSEFMMKGYHKNPEQTkEAFDSDGWLHTKDIGYYDE 997
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 998 NGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPW 1077
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|...
gi 1820754837 1078 YcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd04433 315 Y-KVPRRVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
47-539 |
4.34e-63 |
|
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: 222.49 E-value: 4.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMT 126
Cdd:cd17631 6 RRHPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 127 ARYFLSLTKPKIVFvngesaeclaqvvkennmdtrlvvfadsagfvgraatltavlrsQDTAWIdefecakltspkhvaa 206
Cdd:cd17631 84 VAYILADSGAKVLF--------------------------------------------DDLALL---------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 207 iVCSSGTSGFPKGTEISHAAMI-NYMAHVKVHDLkghvsmwTPSMRWYCGLFIVIKAILDCS---------KRIIVPDYD 276
Cdd:cd17631 104 -MYTSGTTGRPKGAMLTHRNLLwNAVNALAALDL-------GPDDVLLVVAPLFHIGGLGVFtlptllrggTVVILRKFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 277 DDEGLcRFIEKYEVSwfrcdSCF--P---IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKllphTDVILS--YG 349
Cdd:cd17631 176 PETVL-DLIERHRVT-----SFFlvPtmiQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA----RGVKFVqgYG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 350 MTD-YGGLCARQTK--YSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDsDGWLH 426
Cdd:cd17631 246 MTEtSPGVTFLSPEdhRRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFH 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 427 TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDIT 506
Cdd:cd17631 324 TGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELI 403
|
490 500 510
....*....|....*....|....*....|...
gi 1820754837 507 DLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAK 539
Cdd:cd17631 404 AHCRERLARY-KIPKSVEFVDALPRNATGKILK 435
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1188-1685 |
2.31e-60 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 218.17 E-value: 2.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1188 KSKPDSIGQVDALTGKVQTYADMSE--RSIKCALWlKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTP 1265
Cdd:PLN02574 50 HNHNGDTALIDSSTGFSISYSELQPlvKSMAAGLY-HVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1266 MTARNFLTLTSPKIVFTVSSSAANLMEaakelkmnLKVVVMDKLDGYeSVEENVMKGHDTREIIEFKCH-----VTNPDD 1340
Cdd:PLN02574 129 GEIKKRVVDCSVGLAFTSPENVEKLSP--------LGVPVIGVPENY-DFDSKRIEFPKFYELIKEDFDfvpkpVIKQDD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1341 VALIVPSSGTTGLPKGTEISHYSLFCCLH--------PYKNRTLVGHTCIVTPtMRWHYGV-LMAFRLVAANAKkLIVPD 1411
Cdd:PLN02574 200 VAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfeasQYEYPGSDNVYLAALP-MFHIYGLsLFVVGLLSLGST-IVVMR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1412 NDDAENFCQLIEKYQITWFGTDPFMIIKFIKS-QLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDT 1490
Cdd:PLN02574 278 RFDASDMVKVIDRFKVTHFPVVPPILMALTKKaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1491 ACVVSA---QNKFTKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDL 1567
Cdd:PLN02574 358 TAVGTRgfnTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1568 AYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVE 1647
Cdd:PLN02574 438 AYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVA 517
|
490 500 510
....*....|....*....|....*....|....*...
gi 1820754837 1648 KNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRDMYVN 1685
Cdd:PLN02574 518 KQVAPYKKVR-KVVFVQSIPKSPAGKILRRELKRSLTN 554
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
37-544 |
1.45e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 214.67 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 37 NVGALVLEKLRSRPEFIAQVEavTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGIC---THNHLESYvplLAALYLGA 113
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYF--DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFdwnSHEYLEAY---FAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 114 ISNPWDNELSPMTARYFLSLTKPKIVFVNGESAECLAQVvkENNMDT-RLVVFA---DSAGFVGRAATLTAVLRSQDTA- 188
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAI--LPQLPTvRTVIVEgdgPAAPLAPEVGEYEELLAAASDTf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 189 -WIDefecaklTSPKHVAAIVCSSGTSGFPKGTEISHAAM----INYMAHVKVHDlkGHVSM-WTP---SMRWycGLFIV 259
Cdd:PRK06187 160 dFPD-------IDENDAAAMLYTSGTTGHPKGVVLSHRNLflhsLAVCAWLKLSR--DDVYLvIVPmfhVHAW--GLPYL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 260 ikAILDCSKRIIVPDYDDDEgLCRFIEKYEVSWFrcdscfpirlvkFGV------LSKYRLPT------LKILLFGGAHF 327
Cdd:PRK06187 229 --ALMAGAKQVIPRRFDPEN-LLDLIETERVTFF------------FAVptiwqmLLKAPRAYfvdfssLRLVIYGGAAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 328 KGELQQTLVKLLpHTDVILSYGMTDYGGL--CAR-----QTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANK--TGEIW 398
Cdd:PRK06187 294 PPALLREFKEKF-GIDLVQGYGMTETSPVvsVLPpedqlPGQWTKRRSAGRPLPGVEARIVDDD-GDELPPDGgeVGEII 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 399 AKSSYMMNGYYNNPEATRRALDsDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVP 478
Cdd:PRK06187 372 VRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIG 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 479 VPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNM-PWYCRLHagVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK06187 451 VPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLaKFKLPKR--IAFVDELPRTSVGKILKRVLRE 515
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
61-543 |
1.72e-59 |
|
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: 212.81 E-value: 1.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPwdneLSPM-TAR---YFLSLTKP 136
Cdd:cd05936 22 GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP----LNPLyTPReleHILNDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 137 KIVFVNGESAECLAQvvkennmdtrlvvfadsagfvGRAATLTAVLRSQDtawidefecakltspkhVAAIVCSSGTSGF 216
Cdd:cd05936 98 KALIVAVSFTDLLAA---------------------GAPLGERVALTPED-----------------VAVLQYTSGTTGV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 217 PKGTEISHAAMI-N---YMAHVKVHDLKGHVSM----------WTPSMRwycgLFIVIKAILdcskrIIVPDYDDdEGLC 282
Cdd:cd05936 140 PKGAMLTHRNLVaNalqIKAWLEDLLEGDDVVLaalplfhvfgLTVALL----LPLALGATI-----VLIPRFRP-IGVL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 283 RFIEKYEVSWFrcdscfP------IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLlphTDVILS--YGMTDYG 354
Cdd:cd05936 210 KEIRKHRVTIF------PgvptmyIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEEL---TGVPIVegYGLTETS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 355 --GLCARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDsDGWLHTGDLGY 432
Cdd:cd05936 281 pvVAVNPLDGPRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 433 YDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDlvkqn 512
Cdd:cd05936 359 MDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIA----- 433
|
490 500 510
....*....|....*....|....*....|....*...
gi 1820754837 513 mpwYCRLH-AGVK------FMEKLPRTATGKIAKKQLK 543
Cdd:cd05936 434 ---FCREQlAGYKvprqveFRDELPKSAVGKILRRELR 468
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1206-1683 |
9.97e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 212.49 E-value: 9.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMtarNFLtLTSPKIVFTVSS 1285
Cdd:PRK08316 38 TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV-------HVPV---NFM-LTGEELAYILDH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLM----------EAAKELKMNLKVVVMDKLDGYESVE--ENVMKGHDTREIIEFKCHVTNpDDVALIVPSSGTTGL 1353
Cdd:PRK08316 107 SGARAFlvdpalaptaEAALALLPVDTLILSLVLGGREAPGgwLDFADWAEAGSVAEPDVELAD-DDLAQILYTSGTESL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1354 PKGTEISHYSLfccLHPYknrtlVGhtCIVTPTMR-----------WHYGVLMAFRL--VAANAKKLIVpDNDDAENFCQ 1420
Cdd:PRK08316 186 PKGAMLTHRAL---IAEY-----VS--CIVAGDMSaddiplhalplYHCAQLDVFLGpyLYVGATNVIL-DAPDPELILR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1421 LIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTD---TACVVSAQ 1497
Cdd:PRK08316 255 TIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEiapLATVLGPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1498 NKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIY 1577
Cdd:PRK08316 335 EHLRRPGSAGRPVLNVETRVVDDDGND-VAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYIT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1578 IVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPnevdeqHPK------AFVVQVPNKSVTEQELISYVEKNLP 1651
Cdd:PRK08316 413 VVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLP------DPKwieavtAVVVPKAGATVTEDELIAHCRARLA 486
|
490 500 510
....*....|....*....|....*....|..
gi 1820754837 1652 DYcRLRGGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK08316 487 GF-KVPKRVIFVDELPRNPSGKILKRELRERY 517
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1206-1681 |
4.50e-58 |
|
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: 207.57 E-value: 4.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTArnflTLTSPKIVFTVSS 1285
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAV-------YVPLTT----LLGPKDIEYRLEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAAnlmeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefKCHVTNPDDVALIVPSSGTTGLPKGTEISHYSLF 1365
Cdd:cd05972 71 AGA-------------------------------------------KAIVTDAEDPALIYFTSGTTGLPKGVLHTHSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1366 CclHPYKNRTLVG------HTCIVTPTmrWHYGVLMAFRLVAANAKKLIVPDND--DAENFCQLIEKYQITWFGTDPfMI 1437
Cdd:cd05972 108 G--HIPTAAYWLGlrpddiHWNIADPG--WAKGAWSSFFGPWLLGATVFVYEGPrfDAERILELLERYGVTSFCGPP-TA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1438 IKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACVVsAQNKFTKL--GSVGYVSSNVRI 1515
Cdd:cd05972 183 YRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTV-GNFPDMPVkpGSMGRPTPGYDV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1516 KMVDLDTEEaLGPNKIGEL--RVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINV 1593
Cdd:cd05972 261 AIIDDDGRE-LPPGEEGDIaiKLPPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1594 SPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTE---QELISYVEKNLPDYCRLRgGVKIVDQLPRTT 1670
Cdd:cd05972 339 GPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYPR-EIEFVEELPKTI 417
|
490
....*....|.
gi 1820754837 1671 TGKIARKQLRD 1681
Cdd:cd05972 418 SGKIRRVELRD 428
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1205-1681 |
1.72e-57 |
|
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: 208.64 E-value: 1.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1205 QTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPmtarnfltltsPKIVFT-- 1282
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFP-----------EQIAYIin 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1283 --------VSSSAANLMEAAK-ELKMNLKVVVMD--------KLDGYESVEENVMKGHDTREIIEFKchvtnPDDVALIV 1345
Cdd:cd12119 95 haedrvvfVDRDFLPLLEAIApRLPTVEHVVVMTddaampepAGVGVLAYEELLAAESPEYDWPDFD-----ENTAAAIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1346 PSSGTTGLPKGTEISHYSLFccLHPY----KNRTLVGHTCIVTP-TMRWH---YGvlMAFRLVAANAKkLIVPD-NDDAE 1416
Cdd:cd12119 170 YTSGTTGNPKGVVYSHRSLV--LHAMaallTDGLGLSESDVVLPvVPMFHvnaWG--LPYAAAMVGAK-LVLPGpYLDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1417 NFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKlpDVFITNHYGMTDTACVV-- 1494
Cdd:cd12119 245 SLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER--GVRVIHAWGMTETSPLGtv 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1495 ----------SAQNKFTKLGSVGYVSSNVRIKMVDLDTEEAlgPNK---IGELRVKAITIMQGYHKNPETTkQAFDSDGW 1561
Cdd:cd12119 323 arppsehsnlSEDEQLALRAKQGRPVPGVELRIVDDDGREL--PWDgkaVGELQVRGPWVTKSYYKNDEES-EALTEDGW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1562 LRTGDLAYYDDNGEIYIVDRISDFInfRSIN--VSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTE 1639
Cdd:cd12119 400 LRTGDVATIDEDGYLTITDRSKDVI--KSGGewISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1820754837 1640 QELISYVEKN-----LPDYcrlrggVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd12119 478 EELLEFLADKvakwwLPDD------VVFVDEIPKTSTGKIDKKALRE 518
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
36-546 |
2.23e-57 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 209.58 E-value: 2.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 36 TNVGALVLEK-LRSRPEFIAQV-EAVTGAET--TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYL 111
Cdd:COG0365 8 LNIAYNCLDRhAEGRGDKVALIwEGEDGEERtlTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 112 GAISNPwdneLSPMTA----RYFLSLTKPKIVFVNGESAEC---------LAQVVKENNMDTRLVVFADSAGFVGRAATL 178
Cdd:COG0365 88 GAVHSP----VFPGFGaealADRIEDAEAKVLITADGGLRGgkvidlkekVDEALEELPSLEHVIVVGRTGADVPMEGDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 179 T--AVLRSQDtawiDEFECAKlTSPKHVAAIVCSSGTSGFPKGTEISHAAMI--NYMAHVKVHDLK-GHVSMWTPSMRWY 253
Cdd:COG0365 164 DwdELLAAAS----AEFEPEP-TDADDPLFILYTSGTTGKPKGVVHTHGGYLvhAATTAKYVLDLKpGDVFWCTADIGWA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 254 CGLFIVIKAILDCSKRIIV----PDYDDDEGLCRFIEKYEVSWFrcdsCFP---IR-LVKFG--VLSKYRLPTLKILLFG 323
Cdd:COG0365 239 TGHSYIVYGPLLNGATVVLyegrPDFPDPGRLWELIEKYGVTVF----FTAptaIRaLMKAGdePLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 324 GAHFKGELQQTLVKllpHTDV-ILS-YGMTDYGG--LCARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWA 399
Cdd:COG0365 315 GEPLNPEVWEWWYE---AVGVpIVDgWGQTETGGifISNLPGLPVKPGSMGKPVPGYDVAVVDED-GNPVPPGEEGELVI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 400 KSSY--MMNGYYNNPEATRRAL--DSDGWLHTGDLGYYDNDGEVFLVDRMSEFIN---YRaikISPAEIEALIQQHPAVF 472
Cdd:COG0365 391 KGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINvsgHR---IGTAEIESALVSHPAVA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 473 QVAVVPVPHNINEEHAMAFVAKVPGKEVTE---LDITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLKQIA 546
Cdd:COG0365 468 EAAVVGVPDEIRGQVVKAFVVLKPGVEPSDelaKELQAHVREELGPYAYPRE-IEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1206-1679 |
1.43e-56 |
|
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: 203.48 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTwdheLTPMtarnfltLTSPKIVFTVSS 1285
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVP----INPM-------LKERELEYILND 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAAKELkmnlkvvvmdkldgyesveenvmkghdtreiiefkchvtnpDDVALIVPSSGTTGLPKGTEISHYSLF 1365
Cdd:cd05935 72 SGAKVAVVGSEL-----------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1366 CCLHPYKNRTLVGHTCIVTPTMRWHYGVLMAFRLVAANA--KKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKS 1443
Cdd:cd05935 111 ANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYvgGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1444 QLLEKYRLPTLKVILSSGAHLRKEHLEVMReKLPDVFITNHYGMTDTaCVVSAQNKFT--KLGSVGYVSSNVRIKMVDLD 1521
Cdd:cd05935 191 PEFKTRDLSSLKVLTGGGAPMPPAVAEKLL-KLTGLRFVEGYGLTET-MSQTHTNPPLrpKLQCLGIP*FGVDARVIDIE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1522 TEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDG---WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEI 1598
Cdd:cd05935 269 TGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1599 ETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVP--NKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIAR 1676
Cdd:cd05935 349 EAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPeyRGKVTEEDIIEWAREQMAAYKYPR-EVEFVDELPRSASGKILW 427
|
...
gi 1820754837 1677 KQL 1679
Cdd:cd05935 428 RLL 430
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
609-1100 |
2.69e-56 |
|
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: 202.46 E-value: 2.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 609 RLSSKPDFVGQIDAftGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhVVSK 688
Cdd:cd17631 4 RARRHPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP---LNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 689 LSA---RYFLSLMSPKVVFvneesaenlmeaakeenlqvrvmvigslpgfvslanileeqvsraeidgfrctkidnpHDL 765
Cdd:cd17631 79 LTPpevAYILADSGAKVLF----------------------------------------------------------DDL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 766 AMICSSSGTTGMPKGTELSYASLY----NSITP----VEEV--------HAKNEICAWVPTIrWHGGLNqcieVIMSNak 829
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHRNLLwnavNALAAldlgPDDVllvvaplfHIGGLGVFTLPTL-LRGGTV----VILRK-- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 830 wiiFSDDNIkeIALceiIQKHGVTWLgtdtnFA---ILYVKMNI--FQKYPMPSLRKMVITGAPFTKELHETVAKImpHT 904
Cdd:cd17631 174 ---FDPETV--LDL---IERHRVTSF-----FLvptMIQALLQHprFATTDLSSLRAVIYGGAPMPERLLRALQAR--GV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 905 QILQCYGLTDAGGL-CVSQAKN--SKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAF 981
Cdd:cd17631 239 KFVQGYGMTETSPGvTFLSPEDhrRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 982 DsDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKE 1061
Cdd:cd17631 318 R-DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAE 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 1820754837 1062 VTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd17631 397 LDEDELIAHCRERLARY-KIPKSVEFVDALPRNATGKIL 434
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1206-1681 |
3.11e-56 |
|
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: 201.81 E-value: 3.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAisntwdhELTPMTARnfltLTSPKIVFTVSS 1285
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGA-------EAVLLNTR----LTPNELAFQLKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLmeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchvtnpDDVALIVPSSGTTGLPKGTEIS---HY 1362
Cdd:cd05912 72 SDVKL------------------------------------------------DDIATIMYTSGTTGKPKGVQQTfgnHW 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1363 --SLFCCLhpykNRTLVGHTCIVTPTMRWHYGVLMAFRLVAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKF 1440
Cdd:cd05912 104 wsAIGSAL----NLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1441 IKsQLLEKYRlPTLKVILSSGAHLRKEHLEVMREK-LPdvfITNHYGMTDTA---CVVSAQNKFTKLGSVGYVSSNVRIK 1516
Cdd:cd05912 180 LE-ILGEGYP-NNLRCILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCsqiVTLSPEDALNKIGSAGKPLFPVELK 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1517 MVDLDTEealgPNKIGELRVKAITIMQGYHKNPETTKQAFDsDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPA 1596
Cdd:cd05912 255 IEDDGQP----PYEVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1597 EIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQvpNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIAR 1676
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS--ERPISEEELIAYCSEKLAKYKVPK-KIYFVDELPRTASGKLLR 406
|
....*
gi 1820754837 1677 KQLRD 1681
Cdd:cd05912 407 HELKQ 411
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1206-1680 |
3.57e-56 |
|
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: 201.75 E-value: 3.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTARnfltltspkivftvss 1285
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV-------LVPINTA---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 saanlmeaakelkmnlkvvvmdkldgyesveenvMKGHDTREIIEF-KCHVTNPDDVALIVpSSGTTGLPKGTEISHYSL 1364
Cdd:cd05934 62 ----------------------------------LRGDELAYIIDHsGAQLVVVDPASILY-TSGTTGPPKGVVITHANL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1365 F---------CCLHPyknrtlvGHTCIvTPTMRWH-----YGVLMAFrlvAANAKKLIVPdNDDAENFCQLIEKYQITWF 1430
Cdd:cd05934 107 TfagyysarrFGLGE-------DDVYL-TVLPLFHinaqaVSVLAAL---SVGATLVLLP-RFSASRFWSDVRRYGATVT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1431 GTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAhLRKEHLEVmrEKLPDVFITNHYGMTDT-ACVVSAQNKFTKLGSVGYV 1509
Cdd:cd05934 175 NYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPN-PPELHEEF--EERFGVRLLEGYGMTETiVGVIGPRDEPRRPGSIGRP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1510 SSNVRIKMVDLDTEEaLGPNKIGELRVKAI---TIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFI 1586
Cdd:cd05934 252 APGYEVRIVDDDGQE-LPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1587 NFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQL 1666
Cdd:cd05934 330 RRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPR-YIRFVDDL 408
|
490
....*....|....
gi 1820754837 1667 PRTTTGKIARKQLR 1680
Cdd:cd05934 409 PKTPTEKVAKAQLR 422
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
623-1100 |
1.02e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 203.49 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGIL---TENHLNTcvpVLAILYIGGIICPwdhVVSKLSA---RYFLS 696
Cdd:PRK06187 27 FDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFdwnSHEYLEA---YFAVPKIGAVLHP---INIRLKPeeiAYILN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 697 LMSPKVVFVNEESaENLMEAAKEENLQVRVMVI---GSLPGFVSLANILEEQVSRAEidgfrcTKIDNPH----DLAMIC 769
Cdd:PRK06187 101 DAEDRVVLVDSEF-VPLLAAILPQLPTVRTVIVegdGPAAPLAPEVGEYEELLAAAS------DTFDFPDidenDAAAML 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 770 SSSGTTGMPKGTELSYASLY-NSITpveevhakneICAWvptIRWH--------------GGLNQCIEVIMSNAKWII-- 832
Cdd:PRK06187 174 YTSGTTGHPKGVVLSHRNLFlHSLA----------VCAW---LKLSrddvylvivpmfhvHAWGLPYLALMAGAKQVIpr 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 833 -FSDDNIkeialCEIIQKHGVTWLgtdtnFAILYVkMNIFQKYPMP------SLRKMVITGAPFTKEL-HETVAKImpHT 904
Cdd:PRK06187 241 rFDPENL-----LDLIETERVTFF-----FAVPTI-WQMLLKAPRAyfvdfsSLRLVIYGGAALPPALlREFKEKF--GI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 905 QILQCYGLTDAGGL-CVS------QAKNSKPGSCGFVTKGIRIKIADEKtGIALGP--KERGEICIKSEFMMKGYHKNPE 975
Cdd:PRK06187 308 DLVQGYGMTETSPVvSVLppedqlPGQWTKRRSAGRPLPGVEARIVDDD-GDELPPdgGEVGEIIVRGPWLMQGYWNRPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 976 QTKEAFDsDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQ 1055
Cdd:PRK06187 387 ATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVV 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1820754837 1056 KVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:PRK06187 466 LKPGATLDAKELRAFLRGRLAKF-KLPKRIAFVDELPRTSVGKIL 509
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
65-544 |
2.51e-55 |
|
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: 201.39 E-value: 2.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFV-NG 143
Cdd:cd05926 16 TYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTpKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 144 ESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLtavlrSQDTAWIDEFECAKLTSPKHVAAIVCSSGTSGFPKGTEIS 223
Cdd:cd05926 96 ELGPASRAASKLGLAILELALDVGVLIRAPSAESL-----SNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 224 HAAMINYMAHV-KVHDLkghvsmwTPSMRWYC--------GLFIVIKAILDCSKRIIVPDydddeglcRF--------IE 286
Cdd:cd05926 171 HRNLAASATNItNTYKL-------TPDDRTLVvmplfhvhGLVASLLSTLAAGGSVVLPP--------RFsastfwpdVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 287 KYEVSWFrcdSCFP----IRLVKFGVLSKYRLPTLKILLFGGA-----HFKgELQQTLvkllpHTDVILSYGMTDygglC 357
Cdd:cd05926 236 DYNATWY---TAVPtihqILLNRPEPNPESPPPKLRFIRSCSAslppaVLE-ALEATF-----GAPVLEAYGMTE----A 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 358 ARQ-------TKYSKPGSCGFvcETG-RLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGD 429
Cdd:cd05926 303 AHQmtsnplpPGPRKPGSVGK--PVGvEVRILDED-GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 430 LGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLV 509
Cdd:cd05926 380 LGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFC 459
|
490 500 510
....*....|....*....|....*....|....*
gi 1820754837 510 KQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:cd05926 460 RKHLAAF-KVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
37-544 |
3.29e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 201.67 E-value: 3.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 37 NVGALVLEKLRSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISN 116
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFG--DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 117 PWDNELSPMTARYFLSLTKPKIVFVNGESAECLAQVVKENNMDTRLVVFADSAG--FVGRAATLTAVLRSQDtawiDEFE 194
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDdpHTEKMKTFTDFLAAGD----PAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 195 CAKLTsPKHVAAIVCSSGTSGFPKGTEISHAAMI-NYMAHVKVHDLkghvsmwTPSMRWYCGL-----FIVIKAILDCSK 268
Cdd:PRK07656 160 APEVD-PDDVADILFTSGTTGRPKGAMLTHRQLLsNAADWAEYLGL-------TEGDRYLAANpffhvFGYKAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 269 R----IIVPDYDDDEGLcRFIEKYEVSwfrcdsCFPirlvkfGV------------LSKYRLPTLKILLFGGAHFKGELQ 332
Cdd:PRK07656 232 RgatiLPLPVFDPDEVF-RLIETERIT------VLP------GPptmynsllqhpdRSAEDLSSLRLAVTGAASMPVALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 333 QTLVKLLPHTDVILSYGMTDYGG---LCARQTKYSK-PGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGY 408
Cdd:PRK07656 299 ERFESELGVDIVLTGYGLSEASGvttFNRLDDDRKTvAGTIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 409 YNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHA 488
Cdd:PRK07656 378 YDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 489 MAFVAKVPGKEVTELDITDlvkqnmpwYCRLH-AG------VKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK07656 458 KAYVVLKPGAELTEEELIA--------YCREHlAKykvprsIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1191-1681 |
1.22e-54 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 199.42 E-value: 1.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIS---NTwdheltpmt 1267
Cdd:PRK03640 16 PDRTAIEFE--EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAvllNT--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1268 arnflTLTSPKIVFTVSSSAANLMEAAKELkmnlkvvvMDKLDGYESVE-ENVMKGhdTREIIEFK--CHVtnpDDVALI 1344
Cdd:PRK03640 85 -----RLSREELLWQLDDAEVKCLITDDDF--------EAKLIPGISVKfAELMNG--PKEEAEIQeeFDL---DEVATI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1345 VPSSGTTGLPKG---TEISHY------SLfcclhpykNRTLVGHTCIVTPTMRWH------------YGvlMAFRLVaan 1403
Cdd:PRK03640 147 MYTSGTTGKPKGviqTYGNHWwsavgsAL--------NLGLTEDDCWLAAVPIFHisglsilmrsviYG--MRVVLV--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1404 akklivpDNDDAENFCQLIEKYQITWFGTDPFMIikfikSQLLEKYRL----PTLKVILSSGAHLRKEHLEVMREK-LPd 1478
Cdd:PRK03640 214 -------EKFDAEKINKLLQTGGVTIISVVSTML-----QRLLERLGEgtypSSFRCMLLGGGPAPKPLLEQCKEKgIP- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1479 VFITnhYGMTDTA---CVVSAQNKFTKLGSVGYVSSNVRIKMVDlDTEEAlGPNKIGELRVKAITIMQGYHKNPETTKQA 1555
Cdd:PRK03640 281 VYQS--YGMTETAsqiVTLSPEDALTKLGSAGKPLFPCELKIEK-DGVVV-PPFEEGEIVVKGPNVTKGYLNREDATRET 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1556 FDsDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQvpNK 1635
Cdd:PRK03640 357 FQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SG 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1636 SVTEQELISYVEKNLPDYcrlrggvKI------VDQLPRTTTGKIARKQLRD 1681
Cdd:PRK03640 434 EVTEEELRHFCEEKLAKY-------KVpkrfyfVEELPRNASGKLLRHELKQ 478
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
41-544 |
1.33e-53 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 197.89 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 41 LVLEKLRSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAI---SNP 117
Cdd:PLN02330 33 FVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVfsgANP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 118 WDNElSPMTARyfLSLTKPKIVFVNGESAEclaqvvKENNMDTRLVVFADS--AGFVGRAATLTAVLRSQDTAWIDEFEC 195
Cdd:PLN02330 113 TALE-SEIKKQ--AEAAGAKLIVTNDTNYG------KVKGLGLPVIVLGEEkiEGAVNWKELLEAADRAGDTSDNEEILQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 196 AKLtspkhvAAIVCSSGTSGFPKGTEISHAAMINYMAHVKVH---DLKGHVSMW--TPSMRWYCGLFIVIKAILDCSKRI 270
Cdd:PLN02330 184 TDL------CALPFSSGTTGISKGVMLTHRNLVANLCSSLFSvgpEMIGQVVTLglIPFFHIYGITGICCATLRNKGKVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 271 IVPDYDDDEGLCRFIEKyEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKI--LLFGGAHFKGELQQTLVKLLPHTDVILSY 348
Cdd:PLN02330 258 VMSRFELRTFLNALITQ-EVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIMTAAAPLAPELLTAFEAKFPGVQVQEAY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 349 GMTDYG------GLCARQTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSD 422
Cdd:PLN02330 337 GLTEHScitlthGDPEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDED 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 423 GWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTE 502
Cdd:PLN02330 417 GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1820754837 503 LDITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PLN02330 497 EDILNFVAANVAHYKKVRV-VQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
48-545 |
4.25e-53 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 196.99 E-value: 4.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 48 SRPEFIAQVEAVTGAETTFAEMTE--KSVKCALWlREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPM 125
Cdd:PLN02574 51 NHNGDTALIDSSTGFSISYSELQPlvKSMAAGLY-HVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 126 TARYFLSLTKPKIVFVNGESAECLAQV------VKEN-NMDTRLVVFA-------DSAGFVGRAatltaVLRSQDtawid 191
Cdd:PLN02574 130 EIKKRVVDCSVGLAFTSPENVEKLSPLgvpvigVPENyDFDSKRIEFPkfyelikEDFDFVPKP-----VIKQDD----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 192 efecakltspkhVAAIVCSSGTSGFPKGTEISHAAMINYM-------AHVKVHDLKGHVSMWTPSMRWYCGLFIVIKAIL 264
Cdd:PLN02574 200 ------------VAAIMYSSGTTGASKGVVLTHRNLIAMVelfvrfeASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 265 DCSKRIIVPDYDDDEGLCRFIEKYEVSWFRCDSCFPIRLVKF--GVLSKYrLPTLKILLFGGAHFKGELQQTLVKLLPHT 342
Cdd:PLN02574 268 SLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKakGVCGEV-LKSLKQVSCGAAPLSGKFIQDFVQTLPHV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 343 DVILSYGMTDYGGLCAR---QTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRAL 419
Cdd:PLN02574 347 DFIQGYGMTESTAVGTRgfnTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 420 DSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKE 499
Cdd:PLN02574 427 DKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGST 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1820754837 500 VTELDITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLKQI 545
Cdd:PLN02574 507 LSQEAVINYVAKQVAPYKKVRK-VVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1202-1681 |
5.73e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 196.52 E-value: 5.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAIS-NT--------WDHELTPMTARNF 1271
Cdd:PRK05677 47 GKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVvNTnplytareMEHQFNDSGAKAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1272 LTLTS---------PK--IVFTVSSSAANLMEAAKELKMNL------KVVVMDKLDGYESVEENVMKGHDtREIIEFKCH 1334
Cdd:PRK05677 127 VCLANmahlaekvlPKtgVKHVIVTEVADMLPPLKRLLINAvvkhvkKMVPAYHLPQAVKFNDALAKGAG-QPVTEANPQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1335 vtnPDDVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKN--RTLVGHTC--IVTPTMRWH-YGVLM--AFRLVAANAKKL 1407
Cdd:PRK05677 206 ---ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRAlmGSNLNEGCeiLIAPLPLYHiYAFTFhcMAMMLIGNHNIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1408 IvPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEvMREKLPDVFITNHYGM 1487
Cdd:PRK05677 283 I-SNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAE-RWKEVTGCAICEGYGM 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1488 TDTACVVSAqNKFT--KLGSVGYVSSNVRIKMVDLDTEE-ALGpnKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRT 1564
Cdd:PRK05677 361 TETSPVVSV-NPSQaiQVGTIGIPVPSTLCKVIDDDGNElPLG--EVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1565 GDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELIS 1644
Cdd:PRK05677 438 GDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVME 517
|
490 500 510
....*....|....*....|....*....|....*..
gi 1820754837 1645 YVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK05677 518 HMRANLTGYKVPK-AVEFRDELPTTNVGKILRRELRD 553
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
597-1099 |
6.03e-53 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 195.97 E-value: 6.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 597 PVCANVGELVLNRLSSKPDFVGQIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIG 676
Cdd:PLN02330 25 PDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 677 GIIC---PWDHVvSKLSARyfLSLMSPKVVFVNEESAEnlmeaaKEENLQVRVMVIG--SLPGFVSLANILEEqvsraei 751
Cdd:PLN02330 105 GVFSganPTALE-SEIKKQ--AEAAGAKLIVTNDTNYG------KVKGLGLPVIVLGeeKIEGAVNWKELLEA------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 752 dGFRCT-KIDNPH----DLAMICSSSGTTGMPKGTELSY----ASLYNSITPV-EEVHAKNEICAWVPTIRWHGGLNQCI 821
Cdd:PLN02330 169 -ADRAGdTSDNEEilqtDLCALPFSSGTTGISKGVMLTHrnlvANLCSSLFSVgPEMIGQVVTLGLIPFFHIYGITGICC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 822 EVIMSNAKWIIFSDDNIKeIALCEIIqKHGVTWLGTDTNFAILYVKMNIFQKYPMPSLR-KMVITGA-PFTKELHETVAK 899
Cdd:PLN02330 248 ATLRNKGKVVVMSRFELR-TFLNALI-TQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlQAIMTAAaPLAPELLTAFEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 900 IMPHTQILQCYGLTDAGGLCVSQAKNSK------PGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKN 973
Cdd:PLN02330 326 KFPGVQVQEAYGLTEHSCITLTHGDPEKghgiakKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 974 PEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAF 1053
Cdd:PLN02330 406 KEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAAC 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1820754837 1054 VQKVVEKEVTEEELHDLVNKNLPWYCKLQAgIKFVNDFPRISTGKI 1099
Cdd:PLN02330 486 VVINPKAKESEEDILNFVAANVAHYKKVRV-VQFVDSIPKSLSGKI 530
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1201-1683 |
8.29e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 194.35 E-value: 8.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1201 TGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTM----YIGAISntwdHELTPMTARNFLTLTS 1276
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARrsglYYTPIN----WHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1277 PKIVFTVSSSAANLMEAAKELKMNLKVVVMDK--LDGYESVEENVMKGHDTReiiefkchvtnPDDV---ALIVPSSGTT 1351
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAgpVPGFRSYEEALAAQPDTP-----------IADEtagADMLYSSGTT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1352 GLPKGT--EISHyslfccLHP----YKNRTLVGHTCIVTPTMR-------WHYGVLMAFRLVAANAKKLIVPDNDDAENF 1418
Cdd:PRK08276 153 GRPKGIkrPLPG------LDPdeapGMMLALLGFGMYGGPDSVylspaplYHTAPLRFGMSALALGGTVVVMEKFDAEEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1419 CQLIEKYQITWFGTDPFMIIKFIK--SQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVfITNHYGMTDT--ACVV 1494
Cdd:PRK08276 227 LALIERYRVTHSQLVPTMFVRMLKlpEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPI-IHEYYASSEGggVTVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1495 SAQNKFTKLGSVGY-VSSNVRIkmVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDN 1573
Cdd:PRK08276 306 TSEDWLAHPGSVGKaVLGEVRI--LDEDGNE-LPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDED 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1574 GEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAfVVQvPNKSVT-----EQELISYVEK 1648
Cdd:PRK08276 383 GYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQ-PADGADagdalAAELIAWLRG 460
|
490 500 510
....*....|....*....|....*....|....*
gi 1820754837 1649 NLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK08276 461 RLAHYKCPR-SIDFEDELPRTPTGKLYKRRLRDRY 494
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
622-1100 |
9.25e-53 |
|
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: 193.16 E-value: 9.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 622 AFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIicpwdhVVsklsaryflsLMSPK 701
Cdd:cd05936 19 IFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV------VV----------PLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 702 vvFVNEESAENLmeaakeENLQVRVMVIgslpgFVSLANILEEQVSRAEidgfrcTKIDNPHDLAMICSSSGTTGMPKGT 781
Cdd:cd05936 83 --YTPRELEHIL------NDSGAKALIV-----AVSFTDLLAAGAPLGE------RVALTPEDVAVLQYTSGTTGVPKGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 782 ELSYASLYNSITPVEevhakneicAWVPTIRWHG-----------------GLNQCIE-----VIMSNakwiiFSDdnik 839
Cdd:cd05936 144 MLTHRNLVANALQIK---------AWLEDLLEGDdvvlaalplfhvfgltvALLLPLAlgatiVLIPR-----FRP---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 840 eIALCEIIQKHGVTWL-GTDTnfaiLYVKMN---IFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYGLTDA 915
Cdd:cd05936 206 -IGVLKEIRKHRVTIFpGVPT----MYIALLnapEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTET 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 916 G-GLCVSQAKNS-KPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDsDGWLHTKDIG 993
Cdd:cd05936 280 SpVVAVNPLDGPrKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 994 YYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNK 1073
Cdd:cd05936 358 YMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCRE 437
|
490 500
....*....|....*....|....*..
gi 1820754837 1074 NLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd05936 438 QLAGY-KVPRQVEFRDELPKSAVGKIL 463
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
624-1100 |
1.57e-52 |
|
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: 193.30 E-value: 1.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 624 TGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVV 703
Cdd:cd05926 11 STPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 704 FVNEESAENLMEAAKEenLQVRVMVIGSLPGFVSLANIlEEQVSRAEIDGFRCTKIDNPH--DLAMICSSSGTTGMPKGT 781
Cdd:cd05926 91 LTPKGELGPASRAASK--LGLAILELALDVGVLIRAPS-AESLSNLLADKKNAKSEGVPLpdDLALILHTSGTTGRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 782 ELSYASLYNSITPVEEVHA--KNEICAWV-PTIRWHGGLNQCIEVIMSNAKWII--------FSDDnikeialceiIQKH 850
Cdd:cd05926 168 PLTHRNLAASATNITNTYKltPDDRTLVVmPLFHVHGLVASLLSTLAAGGSVVLpprfsastFWPD----------VRDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 851 GVTWL-GTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYGLTDAGGLCVSQ---AKNS 926
Cdd:cd05926 238 NATWYtAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAHQMTSNplpPGPR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 927 KPGSCGFVTkGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNR 1006
Cdd:cd05926 317 KPGSVGKPV-GVEVRILDED-GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1007 ISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIK 1086
Cdd:cd05926 395 IKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAF-KVPKKVY 473
|
490
....*....|....
gi 1820754837 1087 FVNDFPRISTGKID 1100
Cdd:cd05926 474 FVDELPKTATGKIQ 487
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1190-1679 |
1.81e-52 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 193.15 E-value: 1.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1190 KPDSIgqvdALTGKVQ--TYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPM 1266
Cdd:PRK06839 15 HPDRI----AIITEEEemTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1267 TARNFLTLTSPKIVFTVSSSAAnlmeAAKELKMNLKVVVMDKLDGyesveenvMKGHDTREIIEFKchVTNPDDVALIVP 1346
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTFQN----MALSMQKVSYVQRVISITS--------LKEIEDRKIDNFV--EKNESASFIICY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1347 SSGTTGLPKGTEISHYSLFC-CLHPYKNRTLVGHTCIVTPTMRWHYGVLMAFRLVAANAK-KLIVPDNDDAENFCQLIEK 1424
Cdd:PRK06839 157 TSGTTGKPKGAVLTQENMFWnALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGgVIIVPRKFEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1425 YQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKlpDVFITNHYGMTDTACVV---SAQNKFT 1501
Cdd:PRK06839 237 HKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR--GFLFGQGFGMTETSPTVfmlSEEDARR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1502 KLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDR 1581
Cdd:PRK06839 315 KVGSIGKPVLFCDYELIDENKNK-VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1582 ISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYcRLRGGVK 1661
Cdd:PRK06839 393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKY-KIPKEIV 471
|
490
....*....|....*...
gi 1820754837 1662 IVDQLPRTTTGKIARKQL 1679
Cdd:PRK06839 472 FLKELPKNATGKIQKAQL 489
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
601-1099 |
8.41e-52 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 193.02 E-value: 8.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 601 NVGELVLNR-LSSKPD-----FVGqiDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILY 674
Cdd:COG0365 9 NIAYNCLDRhAEGRGDkvaliWEG--EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 675 IGGIICPwdhVVSKLSA---RYFLSLMSPKVVFVNEESA---------ENLMEAAKEENLQVRVMVIG------SLPGFV 736
Cdd:COG0365 87 IGAVHSP---VFPGFGAealADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVGrtgadvPMEGDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 737 SLANILEEQVSRAEidgfrCTKIDnPHDLAMICSSSGTTGMPKGTE------LSYASLYNS----ITPveevhakNEICA 806
Cdd:COG0365 164 DWDELLAAASAEFE-----PEPTD-ADDPLFILYTSGTTGKPKGVVhthggyLVHAATTAKyvldLKP-------GDVFW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 807 WVPTIRW---H-----GGLNQCIEVIMSNAKwIIFSDDNikeiALCEIIQKHGVTWLGTD-TNF-AILYVKMNIFQKYPM 876
Cdd:COG0365 231 CTADIGWatgHsyivyGPLLNGATVVLYEGR-PDFPDPG----RLWELIEKYGVTVFFTApTAIrALMKAGDEPLKKYDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 877 PSLRKMVITGAPFTKELHETVAKimpHT--QILQCYGLTDAGGLCVSQAKNS--KPGSCGFVTKGIRIKIADEkTGIALG 952
Cdd:COG0365 306 SSLRLLGSAGEPLNPEVWEWWYE---AVgvPIVDGWGQTETGGIFISNLPGLpvKPGSMGKPVPGYDVAVVDE-DGNPVP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 953 PKERGEICIKSEF--MMKGYHKNPEQTKEAF--DSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLE 1028
Cdd:COG0365 382 PGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALV 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 1029 LHPSILKAVVVPVPHETDIELPLAFV---QKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:COG0365 462 SHPAVAEAAVVGVPDEIRGQVVKAFVvlkPGVEPSDELAKELQAHVREELGPY-AYPREIEFVDELPKTRSGKI 534
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1206-1680 |
5.82e-51 |
|
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: 187.20 E-value: 5.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISN----TW-DHELTPMtarnfLTLTSPKIV 1280
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNpilpFFrEHELAFI-----LRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1281 FTVSSsaanlmeaakelkmnlkvvvmdkldgyesveenvMKGHDtreiiefkcHVTNPDDVALIVPSSGTTGLPKGTEIS 1360
Cdd:cd05903 78 VVPER----------------------------------FRQFD---------PAAMPDAVALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1361 HYSLFCCLHPYKNR-TLVGHTCIVTPTMRWH-----YGVLMAFRLVAAnakkLIVPDNDDAENFCQLIEKYQITWFGTDP 1434
Cdd:cd05903 115 HNTLSASIRQYAERlGLGPGDVFLVASPMAHqtgfvYGFTLPLLLGAP----VVLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1435 FMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACVVSA-----QNKFtkLGSVGYV 1509
Cdd:cd05903 191 PFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSitpapEDRR--LYTDGRP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1510 SSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDsDGWLRTGDLAYYDDNGEIYIVDRISDFINFR 1589
Cdd:cd05903 268 LPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDIIIRG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1590 SINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKN------LPDYcrlrggVKIV 1663
Cdd:cd05903 346 GENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgvakqyWPER------LVHV 419
|
490
....*....|....*..
gi 1820754837 1664 DQLPRTTTGKIARKQLR 1680
Cdd:cd05903 420 DDLPRTPSGKVQKFRLR 436
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1189-1682 |
1.11e-49 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 186.41 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1189 SKPDSIGQVDALTGKVQ----TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTW----- 1259
Cdd:PRK13295 36 SCPDKTAVTAVRLGTGAprrfTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLmpifr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1260 DHELTPMtarnfLTLTSPKIV--------FTVSSSAANLMEAAKELKmnlKVVVMDKlDGYESVEENVM-----KGHDTR 1326
Cdd:PRK13295 116 ERELSFM-----LKHAESKVLvvpktfrgFDHAAMARRLRPELPALR---HVVVVGG-DGADSFEALLItpaweQEPDAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1327 EIieFKCHVTNPDDVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRTLVG--HTCIVTPTMRwH-----YGVLMAFRL 1399
Cdd:PRK13295 187 AI--LARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGadDVILMASPMA-HqtgfmYGLMMPVML 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1400 VAanakKLIVPDNDDAENFCQLIEKYQITW-FGTDPFmIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPD 1478
Cdd:PRK13295 264 GA----TAVLQDIWDPARAAELIRTEGVTFtMASTPF-LTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1479 VfITNHYGMTDTACVVsaqnkFTKLGSV--------GYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPE 1550
Cdd:PRK13295 339 K-IVSAWGMTENGAVT-----LTKLDDPderasttdGCPLPGVEVRVVDADGAP-LPAGQIGRLQVRGCSNFGGYLKRPQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1551 TTkqAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVV 1630
Cdd:PRK13295 412 LN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVV 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1631 QVPNKSVTEQELISYVEKN------LPDycRLrggvKIVDQLPRTTTGKIARKQLRDM 1682
Cdd:PRK13295 490 PRPGQSLDFEEMVEFLKAQkvakqyIPE--RL----VVRDALPRTPSGKIQKFRLREM 541
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1338-1680 |
2.21e-49 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 179.78 E-value: 2.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1338 PDDVALIVPSSGTTGLPKGTEISHYSLFcclhpyKNRTLVGHT---------CIVTPTmrWH-YGVLMAFRLVAANAKKL 1407
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIV------NNGYFIGERlglteqdrlCIPVPL--FHcFGSVLGVLACLTHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1408 IVPDND-DAENFCQLIEKYQIT-WFGTdPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHY 1485
Cdd:cd05917 73 VFPSPSfDPLAVLEAIEKEKCTaLHGV-PTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1486 GMTDTACVVSAQNK----FTKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGW 1561
Cdd:cd05917 152 GMTETSPVSTQTRTddsiEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1562 LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQE 1641
Cdd:cd05917 232 LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEED 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1820754837 1642 LISYVEKNL-----PDYcrlrggVKIVDQLPRTTTGKIARKQLR 1680
Cdd:cd05917 312 IKAYCKGKIahykvPRY------VFFVDEFPLTVSGKIQKFKLR 349
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1200-1680 |
2.25e-49 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 184.89 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1200 LTGKVQ--TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTARnfltLTSP 1277
Cdd:PRK08008 31 SGGVVRrySYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI-------MVPINAR----LLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1278 KIVFTVSSSAANLM--EAA---------KELKMNLKVVVMdkLDGYESVEENVMKGHD--TREIIEFKCHVT-NPDDVAL 1343
Cdd:PRK08008 100 ESAWILQNSQASLLvtSAQfypmyrqiqQEDATPLRHICL--TRVALPADDGVSSFTQlkAQQPATLCYAPPlSTDDTAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1344 IVPSSGTTGLPKGTEISHYSLF---------CCLHpYKNRTLvghTCIVTPTMRWHYGVLMAFRLVAAnakKLIVPDNDD 1414
Cdd:PRK08008 178 ILFTSGTTSRPKGVVITHYNLRfagyysawqCALR-DDDVYL---TVMPAFHIDCQCTAAMAAFSAGA---TFVLLEKYS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1415 AENFCQLIEKYQITWFGTDPfMIIKFIKSQllekyrlPTLkvilssgAHLRKEHL-EVM-------REKlpDVFIT---- 1482
Cdd:PRK08008 251 ARAFWGQVCKYRATITECIP-MMIRTLMVQ-------PPS-------ANDRQHCLrEVMfylnlsdQEK--DAFEErfgv 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1483 ---NHYGMTDTACVVSAQNKFTK--LGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAI---TIMQGYHKNPETTKQ 1554
Cdd:PRK08008 314 rllTSYGMTETIVGIIGDRPGDKrrWPSIGRPGFCYEAEIRDDHNRP-LPAGEIGEICIKGVpgkTIFKEYYLDPKATAK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1555 AFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPN 1634
Cdd:PRK08008 393 VLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1635 KSVTEQELISYVEKNL-----PDYcrlrggVKIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK08008 473 ETLSEEEFFAFCEQNMakfkvPSY------LEIRKDLPRNCSGKIIKKNLK 517
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1206-1680 |
6.62e-49 |
|
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: 182.95 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFTVSS 1285
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAAKelKMNLKVVVMDKLDGYESVEENVMKGHDTREIIE-FKCHVTNPDDVALIVPSSGTTGLPKGTEISHYSL 1364
Cdd:cd05959 111 LAPVLAAALT--KSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEqLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1365 FCCLHPYKNRTLV---GHTCIVTPTMRWHYGV--LMAFRLvAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIK 1439
Cdd:cd05959 189 YWTAELYARNVLGireDDVCFSAAKLFFAYGLgnSLTFPL-SVGATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1440 FIKSQLLEKYRLPTLKVILSSGahlrkehlevmrEKLP-DVF--ITNHYGMTDTACVVSAQ-------NK--FTKLGSVG 1507
Cdd:cd05959 268 MLAAPNLPSRDLSSLRLCVSAG------------EALPaEVGerWKARFGLDILDGIGSTEmlhiflsNRpgRVRYGTTG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1508 YVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSdGWLRTGDLAYYDDNGEIYIVDRISDFIN 1587
Cdd:cd05959 336 KPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1588 FRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVP---NKSVTEQELISYVEKNLPDYCRLRgGVKIVD 1664
Cdd:cd05959 414 VSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyeDSEALEEELKEFVKDRLAPYKYPR-WIVFVD 492
|
490
....*....|....*.
gi 1820754837 1665 QLPRTTTGKIARKQLR 1680
Cdd:cd05959 493 ELPKTATGKIQRFKLR 508
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1202-1681 |
1.36e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 183.24 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTwdheLTPMTA----RNFLTLTS 1276
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP----VNPMNReeelAHYVTDSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1277 PKIVFTVSSSAANLMEAAKELKMNlKVVV-----MDKLDGYESVEENVMKGHDTREIIEFKC---------------HVT 1336
Cdd:PRK08314 109 ARVAIVGSELAPKVAPAVGNLRLR-HVIVaqysdYLPAEPEIAVPAWLRAEPPLQALAPGGVvawkealaaglapppHTA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1337 NPDDVALIVPSSGTTGLPKGteishyslfcCLHPYknRTlVGHTciVTPTMRW--------HYGVLMAFRL--------- 1399
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKG----------CMHTH--RT-VMAN--AVGSVLWsnstpesvVLAVLPLFHVtgmvhsmna 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1400 -VAANAKKLIVP--DNDDAEnfcQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRkehlEVMREKL 1476
Cdd:PRK08314 253 pIYAGATVVLMPrwDREAAA---RLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMP----EAVAERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1477 PDVFITNH---YGMTDTAcvvsAQNKF-----TKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKN 1548
Cdd:PRK08314 326 KELTGLDYvegYGLTETM----AQTHSnppdrPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1549 PETTKQAF-DSDG--WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHP 1625
Cdd:PRK08314 402 PEATAEAFiEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETV 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1626 KAFVVQVPNK--SVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK08314 482 KAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPR-IVEFVDSLPKSGSGKILWRQLQE 538
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1185-1685 |
1.86e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 181.81 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1185 KFLKSKPDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELT 1264
Cdd:PRK13391 5 IHAQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1265 PMTARNFLTLTSPKIVFTVSSSAANLMEAAKEL-KMNLKVVV--MDKLDGYESVEENVMKGHDTReiiefkchvtNPDDV 1341
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSAAKLDVARALLKQCpGVRHRLVLdgDGELEGFVGYAEAVAGLPATP----------IADES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1342 --ALIVPSSGTTGLPKGT--EISH------YSLFCCLHPyknrtLVGH---TCIVTPTMRWHYGVLMAFRLVAANAKKLI 1408
Cdd:PRK13391 155 lgTDMLYSSGTTGRPKGIkrPLPEqppdtpLPLTAFLQR-----LWGFrsdMVYLSPAPLYHSAPQRAVMLVIRLGGTVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1409 VPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIK--SQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVfITNHYG 1486
Cdd:PRK13391 230 VMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1487 MTDT--ACVVSAQNKFTKLGSVGYVSSNVrIKMVDLDTEEaLGPNKIGELRVKAITIMQgYHKNPETTKQAFDSDG-WLR 1563
Cdd:PRK13391 309 ATEGlgFTACDSEEWLAHPGTVGRAMFGD-LHILDDDGAE-LPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWST 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1564 TGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTE---Q 1640
Cdd:PRK13391 386 VGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaA 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1820754837 1641 ELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRDMYVN 1685
Cdd:PRK13391 466 ELIAFCRQRLSRQKCPR-SIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1206-1684 |
6.15e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 181.51 E-value: 6.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAI---------SNTWDHELTPMTARNFLTLTS 1276
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIlvninpayrASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1277 pkivFTVSSSAANLMEAAKELKMN------------LK-VVVMDKLD--GYESVEENVMKGHD-TREIIEFKCHVTNPDD 1340
Cdd:PRK12583 127 ----FKTSDYHAMLQELLPGLAEGqpgalacerlpeLRgVVSLAPAPppGFLAWHELQARGETvSREALAERQASLDRDD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1341 VALIVPSSGTTGLPKGTEISHYSLFcclhpyKNRTLVG-------HTCIVTPTMRWH-YGVLMAFRLVAANAKKLIVP-D 1411
Cdd:PRK12583 203 PINIQYTSGTTGFPKGATLSHHNIL------NNGYFVAeslglteHDRLCVPVPLYHcFGMVLANLGCMTVGACLVYPnE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1412 NDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRkehLEVMRE-----KLPDVFITnhYG 1486
Cdd:PRK12583 277 AFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCP---IEVMRRvmdemHMAEVQIA--YG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1487 MTDTAcVVSAQNKFT-----KLGSVGYVSSNVRIKMVDLDTEeALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGW 1561
Cdd:PRK12583 352 MTETS-PVSLQTTAAddlerRVETVGRTQPHLEVKVVDPDGA-TVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1562 LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQE 1641
Cdd:PRK12583 430 MHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEE 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 1642 LISYVEKNL-----PDYCRlrggvkIVDQLPRTTTGKIARKQLRDMYV 1684
Cdd:PRK12583 510 LREFCKARIahfkvPRYFR------FVDEFPMTVTGKVQKFRMREISI 551
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
47-548 |
6.40e-48 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 180.06 E-value: 6.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAQVeaVTGAETTFAEMTEKSVKCALWLR-EQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPM 125
Cdd:PRK06839 13 YLHPDRIAII--TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 126 TARYFLSLTKPKIVFVNGEsaeclaqvvkennmdtrlvvFADSAGFVGRAATLTAVLRSQDTAWIDEFECAKLTSPKHVA 205
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKT--------------------FQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 206 A-IVC-SSGTSGFPKGTEISHAAMI-NYMAHVKVHDLKGH-VSMWTPSMRWYCGLFIVIKAILDCSKRIIVPDYDDDEGL 281
Cdd:PRK06839 151 SfIICyTSGTTGKPKGAVLTQENMFwNALNNTFAIDLTMHdRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 282 CRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLV-KLLPHTDvilSYGMTDYGG---LC 357
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIdRGFLFGQ---GFGMTETSPtvfML 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 358 ARQTKYSKPGSCGFVCETGRLKVVDPNTGKVlGANKTGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDG 437
Cdd:PRK06839 308 SEEDARRKVGSIGKPVLFCDYELIDENKNKV-EVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 438 EVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYc 517
Cdd:PRK06839 386 FVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKY- 464
|
490 500 510
....*....|....*....|....*....|.
gi 1820754837 518 RLHAGVKFMEKLPRTATGKIAKKQLKQIAKS 548
Cdd:PRK06839 465 KIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
61-543 |
1.24e-47 |
|
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: 177.10 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPwdnelspmtaryflsltkpkivf 140
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVP----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 141 vngesaeclaqvvkennMDTRLvvfadsagfvgRAATLTAVLRSQDTAWIdefecakLTSPkhvAAIVCSSGTSGFPKGT 220
Cdd:cd05934 58 -----------------INTAL-----------RGDELAYIIDHSGAQLV-------VVDP---ASILYTSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 221 EISHAAMIN---YMAHVKV-------------HDLKGHVSMWTPSmrWYCGLFIVIkaildcskriivpdydddegLCRF 284
Cdd:cd05934 100 VITHANLTFagyYSARRFGlgeddvyltvlplFHINAQAVSVLAA--LSVGATLVL--------------------LPRF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 285 --------IEKYEVSWFRC----------------DSCFPIRLVKFGvlskyrlPTLKILL------FGgahfkgelqqt 334
Cdd:cd05934 158 sasrfwsdVRRYGATVTNYlgamlsyllaqppspdDRAHRLRAAYGA-------PNPPELHeefeerFG----------- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 335 lVKLLPhtdvilSYGMTDYG-GLCARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSY---MMNGYYN 410
Cdd:cd05934 220 -VRLLE------GYGMTETIvGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD-GQELPAGEPGELVIRGLRgwgFFKGYYN 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 411 NPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMA 490
Cdd:cd05934 292 MPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKA 370
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 491 FVAKVPGKEVTELDITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLK 543
Cdd:cd05934 371 VVVLRPGETLDPEELFAFCEGQLAYFKVPRY-IRFVDDLPKTPTEKVAKAQLR 422
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1206-1680 |
1.36e-47 |
|
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: 177.31 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISntwdhelTPMtarnFLTLTSPKIVFTVSS 1285
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVI-------CPL----FSAFGPEAIRDRLEN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAAKELKmnlkvvvmDKLDgyesveenvmkghdtreiiefkchvtnPDDVALIVPSSGTTGLPKGTEISH---- 1361
Cdd:cd05969 71 SEAKVLITTEELY--------ERTD---------------------------PEDPTLLHYTSGTTGTPKGVLHVHdami 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1362 -------YSLfcCLHPYKNRTLVGHTCIVTPTMrwhYGVLMAFrlvaANAKKLIVPDND-DAENFCQLIEKYQITWFGTD 1433
Cdd:cd05969 116 fyyftgkYVL--DLHPDDIYWCTADPGWVTGTV---YGIWAPW----LNGVTNVVYEGRfDAESWYGIIERVKVTVWYTA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1434 PFMIIKFIKS--QLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACVVSAQ--NKFTKLGSVGYV 1509
Cdd:cd05969 187 PTAIRMLMKEgdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETGSIMIANypCMPIKPGSMGKP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1510 SSNVRIKMVDLDTEEaLGPNKIGELRVKA--ITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFIN 1587
Cdd:cd05969 266 LPGVKAAVVDENGNE-LPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1588 FRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQ---ELISYVEKNLPDYCRLRgGVKIVD 1664
Cdd:cd05969 344 TSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPR-EIEFVD 422
|
490
....*....|....*.
gi 1820754837 1665 QLPRTTTGKIARKQLR 1680
Cdd:cd05969 423 NLPKTRSGKIMRRVLK 438
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1175-1683 |
2.53e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 178.64 E-value: 2.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1175 RPVNIAEETLKFLKSKPDSIgqVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGA 1254
Cdd:PRK06188 10 SGATYGHLLVSALKRYPDRP--ALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1255 iSNTWDHeltPMTAR-NFLTLTSPKIVFTVSSSAANLMEAAKELK---MNLKVVV--------MDKLDGYESVEENVMKG 1322
Cdd:PRK06188 88 -RRTALH---PLGSLdDHAYVLEDAGISTLIVDPAPFVERALALLarvPSLKHVLtlgpvpdgVDLLAAAAKFGPAPLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1323 HDTreiiefkchvtnPDDVALIVPSSGTTGLPKGTEISHyslfcclhpyknRTLVGHTCIVTPTMRW--HYGVLMAFRLV 1400
Cdd:PRK06188 164 AAL------------PPDIAGLAYTGGTTGKPKGVMGTH------------RSIATMAQIQLAEWEWpaDPRFLMCTPLS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1401 AANAKK----------LIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLE 1470
Cdd:PRK06188 220 HAGGAFflptllrggtVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1471 VMREKLPDVFiTNHYGMTDTACVVSAQNKF-------TKLGSVGYVSSNVRIKMVDLDTEEAlGPNKIGELRVKAITIMQ 1543
Cdd:PRK06188 300 EAIERFGPIF-AQYYGQTEAPMVITYLRKRdhdpddpKRLTSCGRPTPGLRVALLDEDGREV-AQGEVGEICVRGPLVMD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1544 GYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQ 1623
Cdd:PRK06188 378 GYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGE 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1624 HPKAFVVQVPNKSVTEQELISYVeknlpdycRLRGG-------VKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK06188 457 AVTAVVVLRPGAAVDAAELQAHV--------KERKGsvhapkqVDFVDSLPLTALGKPDKKALRARY 515
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1201-1681 |
2.73e-47 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 176.47 E-value: 2.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1201 TGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISntwdhelTPMtarnFLTLTSPKIV 1280
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIA-------VPL----FALFGPEALE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1281 FTVSSSAAnlmeaakelkmnlKVVVMDKldgyesveenvmkghdtreiiefkchvtnPDDVALIVPSSGTTGLPKGteis 1360
Cdd:cd05971 72 YRLSNSGA-------------SALVTDG-----------------------------SDDPALIIYTSGTTGPPKG---- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1361 hyslfcCLHPYknRTLVGHT---------------CIVTPT-------------MRWHYGVlmafRLVAANAKKLivpdn 1412
Cdd:cd05971 106 ------ALHAH--RVLLGHLpgvqfpfnlfprdgdLYWTPAdwawigglldvllPSLYFGV----PVLAHRMTKF----- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1413 dDAENFCQLIEKYQITWFGTDP--FMIIKFIKSQLlEKYRLpTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDT 1490
Cdd:cd05971 169 -DPKAALDLMSRYGVTTAFLPPtaLKMMRQQGEQL-KHAQV-KLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTEC 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1491 ACVVSAQNKF--TKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVK---AITiMQGYHKNPETTKQAFDSDgWLRTG 1565
Cdd:cd05971 245 NLVIGNCSALfpIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVElpdPVA-FLGYWNNPSATEKKMAGD-WLLTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1566 DLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQ---EL 1642
Cdd:cd05971 322 DLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEI 401
|
490 500 510
....*....|....*....|....*....|....*....
gi 1820754837 1643 ISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd05971 402 QELVKTRLAAHEYPR-EIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1202-1679 |
2.99e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 179.46 E-value: 2.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAI---------SNTWDHELTPMTARNFL 1272
Cdd:PRK06710 47 GKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIvvqtnplytERELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1273 TL-----------TSPKIVFTVSSSAANLMEAAKEL--------KMNLKVVVMDK--LDGYESVEENVMKGhdtreiIEF 1331
Cdd:PRK06710 127 CLdlvfprvtnvqSATKIEHVIVTRIADFLPFPKNLlypfvqkkQSNLVVKVSESetIHLWNSVEKEVNTG------VEV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1332 KCHVTNpdDVALIVPSSGTTGLPKGTEISHYSLFcclhpykNRTLVG----HTCI--------VTPTmrWH-YGVLMAFR 1398
Cdd:PRK06710 201 PCDPEN--DLALLQYTGGTTGFPKGVMLTHKNLV-------SNTLMGvqwlYNCKegeevvlgVLPF--FHvYGMTAVMN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1399 LVAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMrEKLPD 1478
Cdd:PRK06710 270 LSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKF-ETVTG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1479 VFITNHYGMTDTACVVSAQNKFTKL--GSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKqAF 1556
Cdd:PRK06710 349 GKLVEGYGLTESSPVTHSNFLWEKRvpGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA-AV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1557 DSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKS 1636
Cdd:PRK06710 428 LQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTE 507
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1820754837 1637 VTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK06710 508 CSEEELNQFARKYLAAY-KVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
623-1099 |
1.08e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 176.63 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:PRK07656 26 FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNEESAEnLMEAAKEENLQVRVMVI---GSLPGFVSLANILEEQVSRAEiDGFRCTKIDnPHDLAMICSSSGTTGMPK 779
Cdd:PRK07656 106 LFVLGLFLG-VDYSATTRLPALEHVVIcetEEDDPHTEKMKTFTDFLAAGD-PAERAPEVD-PDDVADILFTSGTTGRPK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 780 GTELSYASLYNSITPVEE---VHAKNEICAWVP---TIRWHGGLNQCIeviMSNAKWII---FSDDNIkeialCEIIQKH 850
Cdd:PRK07656 183 GAMLTHRQLLSNAADWAEylgLTEGDRYLAANPffhVFGYKAGVNAPL---MRGATILPlpvFDPDEV-----FRLIETE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 851 GVTWL-GTDT--NFAILYVKMNifqKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAGGL-CVSQAKNS 926
Cdd:PRK07656 255 RITVLpGPPTmyNSLLQHPDRS---AEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVtTFNRLDDD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 927 K---PGSCGFVTKGIRIKIADEkTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFF 1003
Cdd:PRK07656 332 RktvAGTIGTAIAGVENKIVNE-LGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1004 VNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQA 1083
Cdd:PRK07656 411 VDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKY-KVPR 489
|
490
....*....|....*.
gi 1820754837 1084 GIKFVNDFPRISTGKI 1099
Cdd:PRK07656 490 SIEFLDELPKNATGKV 505
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
629-1039 |
4.84e-46 |
|
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: 173.17 E-value: 4.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvvsklsaRYFLSlmspkvvfvnee 708
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP----------IYPTS------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAEnlmeaakeenlQVrvmvigslpgfvslANILEEQVSRAEIdgfrctkIDNPHDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd05907 65 SAE-----------QI--------------AYILNDSEAKALF-------VEDPDDLATIIYTSGTTGRPKGVMLSHRNI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 -YNSITPVEEVHAKNE----------------ICAWVPTIRWHgglnqCIeVIMSNAKWIIfsdDNIKEI---------- 841
Cdd:cd05907 113 lSNALALAERLPATEGdrhlsflplahvferrAGLYVPLLAGA-----RI-YFASSAETLL---DDLSEVrptvflavpr 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 842 ---ALCEIIQKHGVTWLgtdtnfailyvKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKI-MPhtqILQCYGLTD-AG 916
Cdd:cd05907 184 vweKVYAAIKVKAVPGL-----------KRKLFDLAVGGRLRFAASGGAPLPAELLHFFRALgIP---VYEGYGLTEtSA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 917 GLCVSQAKNSKPGSCGFVTKGIRIKIADEktgialgpkerGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYD 996
Cdd:cd05907 250 VVTLNPPGDNRIGTVGKPLPGVEVRIADD-----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEID 318
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1820754837 997 ENGEIFFVNRISD-FINYKAIKLSSAEIEGVLELHPSILKAVVV 1039
Cdd:cd05907 319 EDGFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQAVVI 362
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1340-1681 |
5.48e-46 |
|
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: 172.86 E-value: 5.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1340 DVALIVPSSGTTGLPKGTEISHYSLFC---CLHPYKNRTLVGHTCIVTPtmrWHY------GVLMAFRlvaANAKKLIVP 1410
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAAnvrALVDAWRWTEDDVLLHVLP---LHHvhglvnALLCPLF---AGASVEFLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1411 DNDDAENFCQLIEKyQITWFgtdpfMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVM-REKLP-DVF-----ITN 1483
Cdd:cd05941 164 KFDPKEVAISRLMP-SITVF-----MGVPTIYTRLLQYYEAHFTDPQFARAAAAERLRLMVSgSAALPvPTLeeweaITG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1484 H-----YGMTDTacVVSAQNKFT---KLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQA 1555
Cdd:cd05941 238 HtllerYGMTEI--GMALSNPLDgerRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1556 FDSDGWLRTGDLAYYDDNGEIYIVDRIS-DFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPN 1634
Cdd:cd05941 316 FTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAG 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1820754837 1635 K-SVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd05941 396 AaALSLEELKEWAKQRLAPYKRPR-RLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
63-542 |
3.03e-45 |
|
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: 170.35 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSltkpkivfvn 142
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILN---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 143 gesaeclaqvvkennmdtrlvvfaDSAgfvgraATLTAVLRSQDTawidefecakltspkhVAAIVCSSGTSGFPKGTEI 222
Cdd:cd05935 71 ------------------------DSG------AKVAVVGSELDD----------------LALIPYTSGTTGLPKGCMH 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 223 SH-AAMINYMAHVKVHDLKG-----------HVSMWTPSMRW--YCGLFIVIKAILDcskriivpdyddDEGLCRFIEKY 288
Cdd:cd05935 105 THfSAAANALQSAVWTGLTPsdvilaclplfHVTGFVGSLNTavYVGGTYVLMARWD------------RETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 289 EVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPhTDVILSYGMTDyggLCArQTKYSKPG- 367
Cdd:cd05935 173 KVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG-LRFVEGYGLTE---TMS-QTHTNPPLr 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 368 ---SC-GFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDG---WLHTGDLGYYDNDGEVF 440
Cdd:cd05935 248 pklQClGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFF 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 441 LVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGK--EVTELDITDLVKQNMPWYCR 518
Cdd:cd05935 328 FVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMAAYKY 407
|
490 500
....*....|....*....|....
gi 1820754837 519 LHAgVKFMEKLPRTATGKIAKKQL 542
Cdd:cd05935 408 PRE-VEFVDELPRSASGKILWRLL 430
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1202-1681 |
3.24e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 173.32 E-value: 3.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAI---------SNTWDHELTPMTAR-- 1269
Cdd:PRK08974 46 GEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIvvnvnplytPRELEHQLNDSGAKai 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1270 ----NFLTlTSPKIVF------TVSSSAANLMEAAKELKMNL------KVVVMDKLDGYESVEENVMKGhdtREIIEFKC 1333
Cdd:PRK08974 126 vivsNFAH-TLEKVVFktpvkhVILTRMGDQLSTAKGTLVNFvvkyikRLVPKYHLPDAISFRSALHKG---RRMQYVKP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1334 HVTNpDDVALIVPSSGTTGLPKGTEISH----YSLFCCLHPYKNRTLVGHTCIVTPTMRWHYGVLMAFRL--VAANAKKL 1407
Cdd:PRK08974 202 ELVP-EDLAFLQYTGGTTGVAKGAMLTHrnmlANLEQAKAAYGPLLHPGKELVVTALPLYHIFALTVNCLlfIELGGQNL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1408 IVPDNDDAENFCQLIEKYQIT-----------WFGTDPFMIIKFiksqllekyrlPTLKVILSSGAHLRKEHLEVMrEKL 1476
Cdd:PRK08974 281 LITNPRDIPGFVKELKKYPFTaitgvntlfnaLLNNEEFQELDF-----------SSLKLSVGGGMAVQQAVAERW-VKL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1477 PDVFITNHYGMTDTACVVSAQ--NKFTKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQ 1554
Cdd:PRK08974 349 TGQYLLEGYGLTECSPLVSVNpyDLDYYSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1555 AFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQvPN 1634
Cdd:PRK08974 428 VI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVK-KD 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1820754837 1635 KSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK08974 506 PSLTEEELITHCRRHLTGY-KVPKLVEFRDELPKSNVGKILRRELRD 551
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
600-1039 |
4.07e-45 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 173.75 E-value: 4.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 600 ANVGELVLNRLSSKPDfvgqIDAFTGKE------CTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAIL 673
Cdd:COG1022 11 DTLPDLLRRRAARFPD----RVALREKEdgiwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 674 YIGGIICPwdhVVSKLSA---RYFLSLMSPKVVFV-NEESAENLMEAAKE-ENLQvRVMVI-----GSLPGFVSLANILE 743
Cdd:COG1022 87 AAGAVTVP---IYPTSSAeevAYILNDSGAKVLFVeDQEQLDKLLEVRDElPSLR-HIVVLdprglRDDPRLLSLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 744 ---EQVSRAEIDgFRCTKIDnPHDLAMICSSSGTTGMPKGTELSYAS-LYN--SITPVEEVHAKNEICAWVPTirWHGGl 817
Cdd:COG1022 163 lgrEVADPAELE-ARRAAVK-PDDLATIIYTSGTTGRPKGVMLTHRNlLSNarALLERLPLGPGDRTLSFLPL--AHVF- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 818 NQCIEV--IMSNAKwIIFSDD------NIKEI-----------------ALCEIIQKHG------VTW---LGTDTNFAI 863
Cdd:COG1022 238 ERTVSYyaLAAGAT-VAFAESpdtlaeDLREVkptfmlavprvwekvyaGIQAKAEEAGglkrklFRWalaVGRRYARAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 864 ---------LYVKMNIFQKYPMPSLR-------KMVITGApftkelhetvAKIMPHTQ---------ILQCYGLTDAGG- 917
Cdd:COG1022 317 lagkspsllLRLKHALADKLVFSKLRealggrlRFAVSGG----------AALGPELArffralgipVLEGYGLTETSPv 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 918 LCVSQAKNSKPGSCGFVTKGIRIKIADEktgialgpkerGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDE 997
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 998 NGEIFFVNRISDfinykAIKLSS------AEIEGVLELHPSILKAVVV 1039
Cdd:COG1022 456 DGFLRITGRKKD-----LIVTSGgknvapQPIENALKASPLIEQAVVV 498
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1191-1681 |
9.73e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 171.38 E-value: 9.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTARn 1270
Cdd:PRK07470 21 PDRIALVWG--DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV-------WVPTNFR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 fltLTSPKIVFTVSSSAANLM----------EAAKELKMNLK-VVVMDKLDGYESVEENVMKGHDTReiieFKCHVTNPD 1339
Cdd:PRK07470 91 ---QTPDEVAYLAEASGARAMichadfpehaAAVRAASPDLThVVAIGGARAGLDYEALVARHLGAR----VANAAVDHD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1340 DVALIVPSSGTTGLPKGTEISHYSL-------FCCLHP---YKNRTLVghtciVTPTMrwHYGVLMAFRLVAANAKKLIV 1409
Cdd:PRK07470 164 DPCWFFFTSGTTGRPKAAVLTHGQMafvitnhLADLMPgttEQDASLV-----VAPLS--HGAGIHQLCQVARGAATVLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1410 P-DNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVfITNHYGM- 1487
Cdd:PRK07470 237 PsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLg 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1488 --TDTACVVSAQNKF------TKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFdSD 1559
Cdd:PRK07470 316 evTGNITVLPPALHDaedgpdARIGTCGFERTGMEVQIQDDEGRE-LPPGETGEICVIGPAVFAGYYNNPEANAKAF-RD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1560 GWLRTGDLAYYDDNGEIYIVDRISD-FINFRSiNVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVT 1638
Cdd:PRK07470 394 GWFRTGDLGHLDARGFLYITGRASDmYISGGS-NVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD 472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1820754837 1639 EQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK07470 473 EAELLAWLDGKVARY-KLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1191-1679 |
1.51e-44 |
|
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: 168.48 E-value: 1.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPmtarn 1270
Cdd:cd05930 1 PDAVAVVDG--DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA-------YVP----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 fLTLTSPK--IVFTVSSSAAnlmeaakelkmnlKVVVmdkldgyesveenvmkghdtreiiefkchvTNPDDVALIVPSS 1348
Cdd:cd05930 67 -LDPSYPAerLAYILEDSGA-------------KLVL------------------------------TDPDDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1349 GTTGLPKGTEISHYSLFcclhpyknRTLVGHTCIVTPTMRWHYGVLMAFRLVAA---------NAKKLIVPDND---DAE 1416
Cdd:cd05930 103 GSTGKPKGVMVEHRGLV--------NLLLWMQEAYPLTPGDRVLQFTSFSFDVSvweifgallAGATLVVLPEEvrkDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1417 NFCQLIEKYQIT-WFGTdPFMIIKFIksQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTD-----T 1490
Cdd:cd05930 175 ALADLLAEEGITvLHLT-PSLLRLLL--QELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEatvdaT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1491 ACVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWL------RT 1564
Cdd:cd05930 252 YYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRP-VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRT 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1565 GDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELIS 1644
Cdd:cd05930 331 GDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRA 410
|
490 500 510
....*....|....*....|....*....|....*
gi 1820754837 1645 YVEKNLPDYCRLRGGVkIVDQLPRTTTGKIARKQL 1679
Cdd:cd05930 411 HLAERLPDYMVPSAFV-VLDALPLTPNGKVDRKAL 444
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1202-1682 |
1.51e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 171.54 E-value: 1.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAIS-NT--------WDHELTPMTARNF 1271
Cdd:PRK12492 47 GVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVvNTnplytareMRHQFKDSGARAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1272 L-----------TLTSPKIVFTVSSSAANLMEAAKELKMNL------KVVVMDKLDGYESVEENVMKGHDTReiieFKCH 1334
Cdd:PRK12492 127 VylnmfgklvqeVLPDTGIEYLIEAKMGDLLPAAKGWLVNTvvdkvkKMVPAYHLPQAVPFKQALRQGRGLS----LKPV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1335 VTNPDDVALIVPSSGTTGLPKGTEISHYSL-------FCCL--HPYKNRTLV--GHTCIVTPTMRWHygvLMAFR----- 1398
Cdd:PRK12492 203 PVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanmlqvRACLsqLGPDGQPLMkeGQEVMIAPLPLYH---IYAFTancmc 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1399 -LVAANAKKLIVpDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMrEKLP 1477
Cdd:PRK12492 280 mMVSGNHNVLIT-NPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERW-EQLT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1478 DVFITNHYGMTDTACVVSAQ--NKFTKLGSVGYVSSNVRIKMVDLD-TEEALGPNkiGELRVKAITIMQGYHKNPETTKQ 1554
Cdd:PRK12492 358 GCTIVEGYGLTETSPVASTNpyGELARLGTVGIPVPGTALKVIDDDgNELPLGER--GELCIKGPQVMKGYWQQPEATAE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1555 AFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVqVPN 1634
Cdd:PRK12492 436 ALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVV-ARD 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 1635 KSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQLRDM 1682
Cdd:PRK12492 515 PGLSVEELKAYCKENFTGY-KVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
63-544 |
2.99e-44 |
|
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: 169.35 E-value: 2.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGIC---THNHLESY--VPLLaalylGAISNPWDNELSPMTARYFLSLTKPK 137
Cdd:cd12119 25 RYTYAEVAERARRLANALRRLGVKPGDRVATLawnTHRHLELYyaVPGM-----GAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 138 IVFVNGESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLT----AVLRSQDT--AW--IDEfecakltspkHVAAIVC 209
Cdd:cd12119 100 VVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVlayeELLAAESPeyDWpdFDE----------NTAAAIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 210 -SSGTSGFPKGTEISHAAMI------------------NYMAHVKVHdlkgHVSMW-TPSMRWYCGlfivikaildcSKR 269
Cdd:cd12119 170 yTSGTTGNPKGVVYSHRSLVlhamaalltdglglsesdVVLPVVPMF----HVNAWgLPYAAAMVG-----------AKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 270 IIVPDYDDDEGLCRFIEKYEVSWfrcDSCFPIrlVKFGVLS-----KYRLPTLKILLFGGAhfkgELQQTLVKLLP--HT 342
Cdd:cd12119 235 VLPGPYLDPASLAELIEREGVTF---AAGVPT--VWQGLLDhleanGRDLSSLRRVVIGGS----AVPRSLIEAFEerGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 343 DVILSYGMTDYGGLC------ARQTKYSKPGSCGFVCETGR------LKVVDPNTGKVLGANKT-GEIWAKSSYMMNGYY 409
Cdd:cd12119 306 RVIHAWGMTETSPLGtvarppSEHSNLSEDEQLALRAKQGRpvpgveLRIVDDDGRELPWDGKAvGELQVRGPWVTKSYY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 410 NNPEATRrALDSDGWLHTGDLGYYDNDGEVFLVDRMSEfinyrAIK-----ISPAEIEALIQQHPAVFQVAVVPVPHNIN 484
Cdd:cd12119 386 KNDEESE-ALTEDGWLRTGDVATIDEDGYLTITDRSKD-----VIKsggewISSVELENAIMAHPAVAEAAVIGVPHPKW 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 485 EEHAMAFVAKVPGKEVTELDITDLVKQNMP-WYcrLHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:cd12119 460 GERPLAVVVLKEGATVTAEELLEFLADKVAkWW--LPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1188-1681 |
3.14e-44 |
|
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: 169.98 E-value: 3.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1188 KSKPDSIGQV---DALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELT 1264
Cdd:cd05970 28 KEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1265 P--MTARnfltLTSPKIVFTVSSSAANLME----AAKELKMNLKVVVM--DKLDGYESVEENVMkghDTREIIEFK--CH 1334
Cdd:cd05970 108 AkdIVYR----IESADIKMIVAIAEDNIPEeiekAAPECPSKPKLVWVgdPVPEGWIDFRKLIK---NASPDFERPtaNS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1335 VTNPDDVALIVPSSGTTGLPKGTEISHyslfccLHPyknrtlVGHtcIVTpTMRWH------------------------ 1390
Cdd:cd05970 181 YPCGEDILLVYFSSGTTGMPKMVEHDF------TYP------LGH--IVT-AKYWQnvregglhltvadtgwgkavwgki 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1391 YGVLMAfrlvaanAKKLIVPDND--DAENFCQLIEKYQITWFGTDPfMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEH 1468
Cdd:cd05970 246 YGQWIA-------GAAVFVYDYDkfDPKALLEKLSKYGVTTFCAPP-TIYRFLIREDLSRYDLSSLRYCTTAGEALNPEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1469 LEVMREKlPDVFITNHYGMTDTA-CVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEAlgpnKIGE-----LRV---KAI 1539
Cdd:cd05970 318 FNTFKEK-TGIKLMEGFGQTETTlTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSC----EAGEegeivIRTskgKPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1540 TIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNE 1619
Cdd:cd05970 393 GLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDP 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 1620 VDEQHPKAFVVQV----PNKSVtEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd05970 472 IRGQVVKATIVLAkgyePSEEL-KKELQDHVKKVTAPYKYPR-IVEFVDELPKTISGKIRRVEIRE 535
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1206-1615 |
3.71e-44 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 171.05 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISntwdhelTPMtarnFLTLTS--------- 1276
Cdd:COG1022 42 TWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT-------VPI----YPTSSAeevayilnd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1277 --PKIVFtVSSS--AANLMEAAKELKMNLKVVVMDKLDGYEsvEENVM---------KGHDTREIIEFKCHVTNPDDVAL 1343
Cdd:COG1022 111 sgAKVLF-VEDQeqLDKLLEVRDELPSLRHIVVLDPRGLRD--DPRLLsldellalgREVADPAELEARRAAVKPDDLAT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1344 IVPSSGTTGLPKGTEISHYSLFCCLHpyknrtlVGHTCI-VTPTMR-------WH-------YGVLMA-FRLVAANAKKL 1407
Cdd:COG1022 188 IIYTSGTTGRPKGVMLTHRNLLSNAR-------ALLERLpLGPGDRtlsflplAHvfertvsYYALAAgATVAFAESPDT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1408 IVPDnddaenfcqlIEKYQITWFGTDPFMIIKfIKSQLLEK-YRLPTLKVIL-------------------SSGAHLRKE 1467
Cdd:COG1022 261 LAED----------LREVKPTFMLAVPRVWEK-VYAGIQAKaEEAGGLKRKLfrwalavgrryararlagkSPSLLLRLK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1468 H-------LEVMREKL---------------PDVF---------ITNHYGMTDTACVVSAQ-NKFTKLGSVGYVSSNVRI 1515
Cdd:COG1022 330 HaladklvFSKLREALggrlrfavsggaalgPELArffralgipVLEGYGLTETSPVITVNrPGDNRIGTVGPPLPGVEV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1516 KmvdldteeaLGPNkiGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFInfrsI---- 1591
Cdd:COG1022 410 K---------IAED--GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLI----Vtsgg 474
|
490 500
....*....|....*....|....*
gi 1820754837 1592 -NVSPAEIETVLMTHPAVLQAAVLG 1615
Cdd:COG1022 475 kNVAPQPIENALKASPLIEQAVVVG 499
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1206-1615 |
3.90e-44 |
|
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: 167.39 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISntwdhelTPMtarnFLTLTSPKIVFTVSS 1285
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVP-------VPI----YPTSSAEQIAYILND 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAAnlmeaakelkmnlKVVVmdkldgyesveenvmkghdtreiiefkchVTNPDDVALIVPSSGTTGLPKGTEISH---- 1361
Cdd:cd05907 76 SEA-------------KALF-----------------------------VEDPDDLATIIYTSGTTGRPKGVMLSHrnil 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1362 ---YSLFCCLHPYKNRTLVGH--TCIVTPTMRWHYGVLMA-FRLVAANAKKLIVPDnddaenfcqlIEKYQITWFGTDPF 1435
Cdd:cd05907 114 snaLALAERLPATEGDRHLSFlpLAHVFERRAGLYVPLLAgARIYFASSAETLLDD----------LSEVRPTVFLAVPR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1436 MIIKF-----------IKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMReKLpDVFITNHYGMTDTACVVSAQNKFT-KL 1503
Cdd:cd05907 184 VWEKVyaaikvkavpgLKRKLFDLAVGGRLRFAASGGAPLPAELLHFFR-AL-GIPVYEGYGLTETSAVVTLNPPGDnRI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1504 GSVGYVSSNVRIKmVDLDteealgpnkiGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRIS 1583
Cdd:cd05907 262 GTVGKPLPGVEVR-IADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKK 330
|
410 420 430
....*....|....*....|....*....|...
gi 1820754837 1584 D-FINFRSINVSPAEIETVLMTHPAVLQAAVLG 1615
Cdd:cd05907 331 DlIITSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
47-549 |
4.73e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 169.84 E-value: 4.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAQVeaVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPwdneLSPMT 126
Cdd:PRK06178 44 RERPQRPAII--FYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVP----VSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 127 A----RYFLSLTKPKIVFVngesAECLAQVVKENNMDTRL-VVFADSAGFVgRAATLTAVL-------RSQDTAWIDEFE 194
Cdd:PRK06178 118 RehelSYELNDAGAEVLLA----LDQLAPVVEQVRAETSLrHVIVTSLADV-LPAEPTLPLpdslrapRLAAAGAIDLLP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 195 C---------AKLTSPKHVAAIVCSSGTSGFPKGTEISHAAMInYMAHVKVhdLKGHVSMWTPSMRWYCGLFIVIKAILD 265
Cdd:PRK06178 193 AlractapvpLPPPALDALAALNYTGGTTGMPKGCEHTQRDMV-YTAAAAY--AVAVVGGEDSVFLSFLPEFWIAGENFG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 266 cskrIIVPDYD----------DDEGLCRFIEKYEVSwfrcdscfpirlVKFGVLSKY----RLPTLkillfgGAHFKGEL 331
Cdd:PRK06178 270 ----LLFPLFSgatlvllarwDAVAFMAAVERYRVT------------RTVMLVDNAvelmDHPRF------AEYDLSSL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 332 QQTLV-----KLLPH--------TDVIL---SYGMTDYGG----LCARQTK----YSKPGSCGFVCETGRLKVVDPNTGK 387
Cdd:PRK06178 328 RQVRVvsfvkKLNPDyrqrwralTGSVLaeaAWGMTETHTcdtfTAGFQDDdfdlLSQPVFVGLPVPGTEFKICDFETGE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 388 VLGANKTGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQ 467
Cdd:PRK06178 408 LLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 468 HPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYCRlhAGVKFMEKLPRTATGKIAKKQLKQIAK 547
Cdd:PRK06178 487 HPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKV--PEIRIVDALPMTATGKVRKQDLQALAE 564
|
..
gi 1820754837 548 SY 549
Cdd:PRK06178 565 EL 566
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1190-1681 |
1.05e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 167.29 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1190 KPDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTAR 1269
Cdd:PRK09088 8 QPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAI-------YVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1270 nfltLTSPKIVFTVSSSAANLM-----EAAKELKMNLKVVVMDKLDGYESveenvmkghDTREIIEfkchvtnPDDVALI 1344
Cdd:PRK09088 81 ----LSASELDALLQDAEPRLLlgddaVAAGRTDVEDLAAFIASADALEP---------ADTPSIP-------PERVSLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1345 VPSSGTTGLPKGTEISHYSLFCCLHPYKNRTLVGHTCI--VTPTMRWHYGVLMAFRLVAANAKKLIVPDNDDAenfcqli 1422
Cdd:PRK09088 141 LFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSflCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEP------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1423 eKYQITWFGtDPFMIIK--FIKSQLLEKYR---------LPTLKVILSSGA-HLRKEHLEVMREKLPDVfitNHYGMTDT 1490
Cdd:PRK09088 214 -KRTLGRLG-DPALGIThyFCVPQMAQAFRaqpgfdaaaLRHLTALFTGGApHAAEDILGWLDDGIPMV---DGFGMSEA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1491 ACV----VSAQNKFTKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGD 1566
Cdd:PRK09088 289 GTVfgmsVDCDVIRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1567 LAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYV 1646
Cdd:PRK09088 368 IARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHL 447
|
490 500 510
....*....|....*....|....*....|....*
gi 1820754837 1647 EKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK09088 448 STRLAKY-KVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
614-1099 |
2.11e-43 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 168.10 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 614 PDFVGQIDAFTGKECTYAEMRERSIKCALWLRKH-GIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSAR 692
Cdd:PLN02574 53 NGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 693 YFLSLMSPKVVFVNEESAENLMEaakeenlqVRVMVIGsLPGFVSLANILEEQVSRAEI---DGFRCTK-IDNPHDLAMI 768
Cdd:PLN02574 133 KRVVDCSVGLAFTSPENVEKLSP--------LGVPVIG-VPENYDFDSKRIEFPKFYELikeDFDFVPKpVIKQDDVAAI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 769 CSSSGTTGMPKGTELSYASLYNSI--------TPVEEVHAKNEICAWVPTIRWHGgLNQCIEVIMSNAKWIIF-----SD 835
Cdd:PLN02574 204 MYSSGTTGASKGVVLTHRNLIAMVelfvrfeaSQYEYPGSDNVYLAALPMFHIYG-LSLFVVGLLSLGSTIVVmrrfdAS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 836 DNIKeialceIIQKHGVTwlgtdtNFAILYVKMNIFQKY-------PMPSLRKMVITGAPFTKELHETVAKIMPHTQILQ 908
Cdd:PLN02574 283 DMVK------VIDRFKVT------HFPVVPPILMALTKKakgvcgeVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 909 CYGLTDA---GGLCVSQAKNSKPGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDG 985
Cdd:PLN02574 351 GYGMTEStavGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 986 WLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEE 1065
Cdd:PLN02574 431 WLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQE 510
|
490 500 510
....*....|....*....|....*....|....
gi 1820754837 1066 ELHDLVNKNLPWYCKLQAGIkFVNDFPRISTGKI 1099
Cdd:PLN02574 511 AVINYVAKQVAPYKKVRKVV-FVQSIPKSPAGKI 543
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1202-1683 |
8.65e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 165.72 E-value: 8.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISntwdhelTPMTARnfltLTSPKIVF 1281
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIA-------VPVNFR----LTPPEIAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1282 TVSSSAA----------NLMEAAKELKMNLKVVVM------DKLDGYESVEENVMKGHDTREIiefkchvtnPDDV-ALI 1344
Cdd:PRK07786 109 LVSDCGAhvvvteaalaPVATAVRDIVPLLSTVVVaggssdDSVLGYEDLLAEAGPAHAPVDI---------PNDSpALI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1345 VPSSGTTGLPKGTEISHYSL----FCCLhpYKNRTLVGHTCIVTPTMRWH---YGVLMAFRLVAAnaKKLIVPDND-DAE 1416
Cdd:PRK07786 180 MYTSGTTGRPKGAVLTHANLtgqaMTCL--RTNGADINSDVGFVGVPLFHiagIGSMLPGLLLGA--PTVIYPLGAfDPG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1417 NFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLpTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTA---CV 1493
Cdd:PRK07786 256 QLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSpvtCM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1494 VSAQNKFTKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSdGWLRTGDLAYYDDN 1573
Cdd:PRK07786 335 LLGEDAIRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1574 GEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFV-VQVPNKSVTEQELISYVEKNLPD 1652
Cdd:PRK07786 413 GYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRLAR 492
|
490 500 510
....*....|....*....|....*....|.
gi 1820754837 1653 YCRLRgGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK07786 493 YKHPK-ALEIVDALPRNPAGKVLKTELRERY 522
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
65-545 |
1.75e-42 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 163.59 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAEclaqvvkENNMDTRlVVFADSAGFVGRAATLTavlrsqdTAWIDEFecakltspkhVAAIVCSSGTSGFPKGTeish 224
Cdd:PRK03640 109 FEA-------KLIPGIS-VKFAELMNGPKEEAEIQ-------EEFDLDE----------VATIMYTSGTTGKPKGV---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 aaMINYMAHvkvhdlkghvsmWTPSM------------RWYC--------GLFIVIKAILDCSKRIIVPDYDDDEGLcRF 284
Cdd:PRK03640 160 --IQTYGNH------------WWSAVgsalnlglteddCWLAavpifhisGLSILMRSVIYGMRVVLVEKFDAEKIN-KL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 285 IEKYEVSWFRCDSCFPIRLVKfgVLSKYRLP-TLK-ILLFGGAHFKGELQQTLVKLLPhtdVILSYGMTDYGG-LCARQT 361
Cdd:PRK03640 225 LQTGGVTIISVVSTMLQRLLE--RLGEGTYPsSFRcMLLGGGPAPKPLLEQCKEKGIP---VYQSYGMTETASqIVTLSP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 362 KYS--KPGSCG---FVCEtgrLKVVDpnTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDsDGWLHTGDLGYYDND 436
Cdd:PRK03640 300 EDAltKLGSAGkplFPCE---LKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 437 GEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPhniNEEHAM---AFVakVPGKEVTELDITDLVKQNM 513
Cdd:PRK03640 374 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVP---DDKWGQvpvAFV--VKSGEVTEEELRHFCEEKL 448
|
490 500 510
....*....|....*....|....*....|..
gi 1820754837 514 PWYcRLHAGVKFMEKLPRTATGKIAKKQLKQI 545
Cdd:PRK03640 449 AKY-KVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1206-1683 |
2.19e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 163.52 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTARnfltLTSPKIVFTVSS 1285
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAV-------FLPINYR----LAADEVAYILGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAAKELKMNLKVVVMDKLDGYESVEENVMKGHDTREIIEfkCHVTNPDDVALIVPSSGTTGLPKGTEISHYSLF 1365
Cdd:PRK06145 98 AGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLEIPP--QAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1366 -------CCLHPYKNRTLVghtcIVTPTmrWHYGvlmAFRL----VAANAKKLIVPDNDDAENFCQLIEKYQIT--WFGt 1432
Cdd:PRK06145 176 wksidhvIALGLTASERLL----VVGPL--YHVG---AFDLpgiaVLWVGGTLRIHREFDPEAVLAAIERHRLTcaWMA- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1433 dPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTA---CVVSAQNKFTKLGSVGYV 1509
Cdd:PRK06145 246 -PVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCsgdTLMEAGREIEKIGSTGRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1510 SSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFR 1589
Cdd:PRK06145 325 LAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1590 SINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRT 1669
Cdd:PRK06145 403 GENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASF-KVPRQLKVRDELPRN 481
|
490
....*....|....
gi 1820754837 1670 TTGKIARKQLRDMY 1683
Cdd:PRK06145 482 PSGKVLKRVLRDEL 495
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
762-1099 |
3.23e-42 |
|
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: 158.98 E-value: 3.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 762 PHDLAMICSSSGTTGMPKGTELSYASLYN---SITPVEEVHAKNEICAWVPtirwhggLNQCIEVIMSN------AKWII 832
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNngyFIGERLGLTEQDRLCIPVP-------LFHCFGSVLGVlaclthGATMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 833 FSDDNIKEIALCEIIQKHGVTWL-GTDTNF-AILYVKMniFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCY 910
Cdd:cd05917 74 FPSPSFDPLAVLEAIEKEKCTALhGVPTMFiAELEHPD--FDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 911 GLTDAGGLCVSQAKNSKP----GSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGW 986
Cdd:cd05917 152 GMTETSPVSTQTRTDDSIekrvNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 987 LHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEE 1066
Cdd:cd05917 232 LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEED 311
|
330 340 350
....*....|....*....|....*....|...
gi 1820754837 1067 LHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:cd05917 312 IKAYCKGKIAHY-KVPRYVFFVDEFPLTVSGKI 343
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
65-544 |
4.49e-42 |
|
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: 160.20 E-value: 4.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIsnpwdnelspmtaryflsltkpkIVFVNge 144
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE-----------------------AVLLN-- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 saeclaqvvkennmdTRLVvfadsagfvgrAATLTAVLRSQDTAWIDefecakltspkhVAAIVCSSGTSGFPKGTEISH 224
Cdd:cd05912 58 ---------------TRLT-----------PNELAFQLKDSDVKLDD------------IATIMYTSGTTGKPKGVQQTF 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AamiNYMAHVKVHDLkghvSM-WTPSMRWYC--------GLFIVIKA-ILDCSkrIIVPDYDDDEGLCRFIEKYEVSWFR 294
Cdd:cd05912 100 G---NHWWSAIGSAL----NLgLTEDDNWLCalplfhisGLSILMRSvIYGMT--VYLVDKFDAEQVLHLINSGKVTIIS 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 295 CDSCFPIRLVKfgVLSKYRLPTLK-ILLFGGAHFKGELQQTLVKLLPhtdVILSYGMTD-YGGLCARQTKYS--KPGSCG 370
Cdd:cd05912 171 VVPTMLQRLLE--ILGEGYPNNLRcILLGGGPAPKPLLEQCKEKGIP---VYQSYGMTEtCSQIVTLSPEDAlnKIGSAG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 371 ---FVCEtgrLKVVDPNTGKvlgaNKTGEIWAKSSYMMNGYYNNPEATRRALDsDGWLHTGDLGYYDNDGEVFLVDRMSE 447
Cdd:cd05912 246 kplFPVE---LKIEDDGQPP----YEVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSD 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 448 FINYRAIKISPAEIEALIQQHPAVFQVAVVPVPhniNEEHAMAFVAKVPG-KEVTELDITDlvkqnmpwYCRLH-AGVK- 524
Cdd:cd05912 318 LIISGGENIYPAEIEEVLLSHPAIKEAGVVGIP---DDKWGQVPVAFVVSeRPISEEELIA--------YCSEKlAKYKv 386
|
490 500
....*....|....*....|....*
gi 1820754837 525 -----FMEKLPRTATGKIAKKQLKQ 544
Cdd:cd05912 387 pkkiyFVDELPRTASGKLLRHELKQ 411
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1206-1679 |
5.02e-42 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 161.08 E-value: 5.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFTVSs 1285
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 saanlmeaakelKMNLKVVVMDKLDGYESVEEnvmkgHDTREIIEFkchvtNPDDVALIVPSSGTTGLPKGTEISHYSlf 1365
Cdd:TIGR01923 80 ------------LLEEKDFQADSLDRIEAAGR-----YETSLSASF-----NMDQIATLMFTSGTTGKPKAVPHTFRN-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1366 cclHpYKNRTLVGHTCIVTPTMRW-------HY-GVLMAFRLVAaNAKKLIVPDNDDAenFCQLIEKYQITWFGTDPFMI 1437
Cdd:TIGR01923 136 ---H-YASAVGSKENLGFTEDDNWllslplyHIsGLSILFRWLI-EGATLRIVDKFNQ--LLEMIANERVTHISLVPTQL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1438 ikfiKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITnhYGMTDTAC-VVSAQNKFTK-LGSVGYVSSNVRI 1515
Cdd:TIGR01923 209 ----NRLLDEGGHNENLRKILLGGSAIPAPLIEEAQQYGLPIYLS--YGMTETCSqVTTATPEMLHaRPDVGRPLAGREI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1516 KMVDLDTEEalgpnkIGELRVKAITIMQGYHKNPETTkQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSP 1595
Cdd:TIGR01923 283 KIKVDNKEG------HGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1596 AEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQvpNKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIA 1675
Cdd:TIGR01923 356 EEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVS--ESDISQAKLIAYLTEKLAKY-KVPIAFEKLDELPYNASGKIL 432
|
....
gi 1820754837 1676 RKQL 1679
Cdd:TIGR01923 433 RNQL 436
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
61-542 |
7.70e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 162.82 E-value: 7.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWL-REQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPwdneLSPMTA----RYFLSLTK 135
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP----VNPMNReeelAHYVTDSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 136 PKIVFVNGESAECLAQVVKennmDTRL--VVFADSAG------------FVGRAATLTAVLRSQDTAWIDEFECAKLTSP 201
Cdd:PRK08314 109 ARVAIVGSELAPKVAPAVG----NLRLrhVIVAQYSDylpaepeiavpaWLRAEPPLQALAPGGVVAWKEALAAGLAPPP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 202 KHV-----AAIVCSSGTSGFPKGTEISH-AAMINYMAHVKVHDLKG-----------HV-----SMWTPSmrwYCGLFIV 259
Cdd:PRK08314 185 HTAgpddlAVLPYTSGTTGVPKGCMHTHrTVMANAVGSVLWSNSTPesvvlavlplfHVtgmvhSMNAPI---YAGATVV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 260 IKAILDcskRiivpdydddEGLCRFIEKYEVS-WfrcdSCFPIRLVKF---GVLSKYRLPTLKILLFGGAHFKGELQQtl 335
Cdd:PRK08314 262 LMPRWD---R---------EAAARLIERYRVThW----TNIPTMVVDFlasPGLAERDLSSLRYIGGGGAAMPEAVAE-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 336 vKLLPHT--DVILSYGMTDygglCARQTKYSKPGSCGFVCetgrL---------KVVDPNTGKVLGANKTGEIWAKSSYM 404
Cdd:PRK08314 324 -RLKELTglDYVEGYGLTE----TMAQTHSNPPDRPKLQC----LgiptfgvdaRVIDPETLEELPPGEVGEIVVHGPQV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 405 MNGYYNNPEATRRA---LDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPH 481
Cdd:PRK08314 395 FKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPD 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 482 NINEEHAMAFVAKVPGKE--VTELDITDLVKQNMPWY--CRLhagVKFMEKLPRTATGKIAKKQL 542
Cdd:PRK08314 475 PRRGETVKAVVVLRPEARgkTTEEEIIAWAREHMAAYkyPRI---VEFVDSLPKSGSGKILWRQL 536
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1180-1679 |
1.29e-41 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 161.14 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1180 AEETLKFLKSK-PDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsnt 1258
Cdd:cd05923 3 VFEMLRRAASRaPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1259 wdheLTPMTARnfltLTSPKIVFTVSSSaanlmEAAKELKMNLKVVVMDKLDGY---ESVEENVMKGHDTREIIEFKCHV 1335
Cdd:cd05923 80 ----PALINPR----LKAAELAELIERG-----EMTAAVIAVDAQVMDAIFQSGvrvLALSDLVGLGEPESAGPLIEDPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1336 TNPDDVALIVPSSGTTGLPKGTEISHYS-----LFCC-----LHPYKNRTLvghtcivtPTMRWHYgvLMAFR--LVAAN 1403
Cdd:cd05923 147 REPEQPAFVFYTSGTTGLPKGAVIPQRAaesrvLFMStqaglRHGRHNVVL--------GLMPLYH--VIGFFavLVAAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1404 A--KKLIVPDNDDAENFCQLIEKYQIT-WFGTdPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVF 1480
Cdd:cd05923 217 AldGTYVVVEEFDPADALKLIEQERVTsLFAT-PTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1481 iTNHYGMTDTACVVSAQNkfTKLGSVGY--VSSNVRIKMVDLDTEEALGPNKIGELRVKAIT--IMQGYHKNPETTKQAF 1556
Cdd:cd05923 296 -VNIYGTTEAMNSLYMRD--ARTGTEMRpgFFSEVRIVRIGGSPDEALANGEEGELIVAAAAdaAFTGYLNQPEATAKKL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1557 dSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNkS 1636
Cdd:cd05923 373 -QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-T 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1820754837 1637 VTEQELISY-VEKNLPDYCRLRGGVkIVDQLPRTTTGKIARKQL 1679
Cdd:cd05923 451 LSADELDQFcRASELADFKRPRRYF-FLDELPKNAMNKVLRRQL 493
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
211-543 |
1.58e-41 |
|
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: 157.05 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 211 SGTSGFPKGTEISHAAMINYMAHVKVH-DLKGHVSMWTPSMRWYCglFIVIKAILDC----SKRIIVPDYDDDEGLCRFI 285
Cdd:cd05917 11 SGTTGSPKGATLTHHNIVNNGYFIGERlGLTEQDRLCIPVPLFHC--FGSVLGVLAClthgATMVFPSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 286 EKyevswFRCDSCF--P---IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDYGGLCARQ 360
Cdd:cd05917 89 EK-----EKCTALHgvPtmfIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 361 TKYSKP----GSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDND 436
Cdd:cd05917 164 RTDDSIekrvNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDED 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 437 GEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNM--- 513
Cdd:cd05917 244 GYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIahy 323
|
330 340 350
....*....|....*....|....*....|..
gi 1820754837 514 --PWYcrlhagVKFMEKLPRTATGKIAKKQLK 543
Cdd:cd05917 324 kvPRY------VFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
47-551 |
2.65e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 160.87 E-value: 2.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAQVEAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPM 125
Cdd:PRK08316 19 RSARRYPDKTALVFGDRSwTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 126 TARYFLSLTKPKIVFVngESAecLAQVVKENnmdtrlvvfADSAGFVGRAATLTAVLRSQDTAWIDeFECAKLTSPKH-- 203
Cdd:PRK08316 99 ELAYILDHSGARAFLV--DPA--LAPTAEAA---------LALLPVDTLILSLVLGGREAPGGWLD-FADWAEAGSVAep 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 204 --------VAAIVCSSGTSGFPKGTEISHAAMI-NYMAHVKVHDLKGHVSMwTPSMRWY-CglfivikAILDC------- 266
Cdd:PRK08316 165 dveladddLAQILYTSGTESLPKGAMLTHRALIaEYVSCIVAGDMSADDIP-LHALPLYhC-------AQLDVflgpyly 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 267 --SKRIIVPDYDDDEGLcRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDV 344
Cdd:PRK08316 237 vgATNVILDAPDPELIL-RTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 345 ILSYGMTDYGGLCA---RQTKYSKPGSCG----FVcETgrlKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRR 417
Cdd:PRK08316 316 YNCYGQTEIAPLATvlgPEEHLRRPGSAGrpvlNV-ET---RVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 418 ALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPG 497
Cdd:PRK08316 391 AF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 498 KEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQIAKSYAT 551
Cdd:PRK08316 470 ATVTEDELIAHCRARLAGF-KVPKRVIFVDELPRNPSGKILKRELRERYAGAFT 522
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1191-1682 |
2.70e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 161.25 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDAlTGKVqTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAisntwdheltpmtaRN 1270
Cdd:PRK07788 63 PDRAALIDE-RGTL-TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGA--------------RI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 FLTLTSpkivftvsSSAANLMEAAKELKmnLKVVVMD------------KLDGYESVEENVMKGHDTR-------EIIEF 1331
Cdd:PRK07788 127 ILLNTG--------FSGPQLAEVAAREG--VKALVYDdeftdllsalppDLGRLRAWGGNPDDDEPSGstdetldDLIAG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1332 KCH---VTNPDDVALIVPSSGTTGLPKGTEISHYSLFCCLH------PYKNRtlvGHTCIVTP---TMRW-HYGVLMAFR 1398
Cdd:PRK07788 197 SSTaplPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAgllsrvPFRAG---ETTLLPAPmfhATGWaHLTLAMALG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1399 lvaanaKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIK--SQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKL 1476
Cdd:PRK07788 274 ------STVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDlgPEVLAKYDTSSLKIIFVSGSALSPELATRALEAF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1477 PDVfITNHYGMTD--TACVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYH--KNPETT 1552
Cdd:PRK07788 348 GPV-LYNLYGSTEvaFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNE-VPRGVVGRIFVGNGFPFEGYTdgRDKQII 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1553 kqafdsDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQV 1632
Cdd:PRK07788 426 ------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKA 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1633 PNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRDM 1682
Cdd:PRK07788 500 PGAALDEDAIKDYVRDNLARYKVPR-DVVFLDELPRNPTGKVLKRELREM 548
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1201-1679 |
2.73e-41 |
|
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: 158.95 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1201 TGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGaisntwdHELTPmtarnfLTLTSPKiv 1280
Cdd:cd05945 13 GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG-------HAYVP------LDASSPA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1281 ftvsSSAANLMEAAKelkmnLKVVVMDkldgyesveenvmkghdtreiiefkchvtnPDDVALIVPSSGTTGLPKGTEIS 1360
Cdd:cd05945 78 ----ERIREILDAAK-----PALLIAD------------------------------GDDNAYIIFTSGSTGRPKGVQIS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1361 HYSLFCCLHPYKNRTLVGHTCIVTPTMRWHYGV-LMAFRLVAANAKKLIVPDNDDAENFCQL---IEKYQIT-WFGTdPF 1435
Cdd:cd05945 119 HDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLsVMDLYPALASGATLVPVPRDATADPKQLfrfLAEHGITvWVST-PS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1436 MIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTaCVVSAQNKFTK-----LGSV--GY 1508
Cdd:cd05945 198 FAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEA-TVAVTYIEVTPevldgYDRLpiGY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1509 VSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFDSD---GWLRTGDLAYYDDNGEIYIVDRISDF 1585
Cdd:cd05945 277 AKPGAKLVILDEDGRP-VPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1586 INFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVvqVPNKSVTEQ---ELISYVEKNLPDYCRLRGGVkI 1662
Cdd:cd05945 356 VKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFV--VPKPGAEAGltkAIKAELAERLPPYMIPRRFV-Y 432
|
490
....*....|....*..
gi 1820754837 1663 VDQLPRTTTGKIARKQL 1679
Cdd:cd05945 433 LDELPLNANGKIDRKAL 449
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
47-544 |
3.31e-41 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 161.07 E-value: 3.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAQVEAvTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMT 126
Cdd:PRK06087 34 RAMPDKIAVVDN-HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 127 ARYFLSLTKPKIVF----VNGESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDTawIDEFECAkltSPK 202
Cdd:PRK06087 113 LVWVLNKCQAKMFFaptlFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYEP--LTTAITT---HGD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 203 HVAAIVCSSGTSGFPKGTEISHAAMI-NYMAHVKVHDLKGHVSMWTPSMRWYCGLFI--VIKAILDCSKRIIVPDYDDDE 279
Cdd:PRK06087 188 ELAAVLFTSGTEGLPKGVMLTHNNILaSERAYCARLNLTWQDVFMMPAPLGHATGFLhgVTAPFLIGARSVLLDIFTPDA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 280 GLcRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGEL----QQTLVKLLPhtdvilSYGMTDygg 355
Cdd:PRK06087 268 CL-ALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVarecQQRGIKLLS------VYGSTE--- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 356 lcARQTKYSKPGSC--------GFVCETGRLKVVDPNTGKVLGANKtGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHT 427
Cdd:PRK06087 338 --SSPHAVVNLDDPlsrfmhtdGYAAAGVEIKVVDEARKTLPPGCE-GEEASRGPNVFMGYLDEPELTARALDEEGWYYS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 428 GDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVakVPGKEVTELDITD 507
Cdd:PRK06087 415 GDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYV--VLKAPHHSLTLEE 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1820754837 508 LVKqnmpWYCRLHAG-------VKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK06087 493 VVA----FFSRKRVAkykypehIVVIDKLPRTASGKIQKFLLRK 532
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1206-1676 |
3.47e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 159.14 E-value: 3.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFtvss 1285
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 saanlmeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchVTNPDDVALIVPSSGTTGLPKGTEISHYSL- 1364
Cdd:cd05914 85 -------------------------------------------------VSDEDDVALINYTSGTTGNSKGVMLTYRNIv 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1365 ----FC-CLHPYK--NRTL----VGHT--CIVTPTMRWHYGV--------------LMAFRLVAANA------------K 1405
Cdd:cd05914 116 snvdGVkEVVLLGkgDKILsilpLHHIypLTFTLLLPLLNGAhvvfldkipsakiiALAFAQVTPTLgvpvplviekifK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1406 KLIVPDNDDAENFCQLIEKYQITwfgtdpfMIIKFIKSQLLEKYRlPTLKVILSSGAHLRKEHLEVMRE-KLPdvfITNH 1484
Cdd:cd05914 196 MDIIPKLTLKKFKFKLAKKINNR-------KIRKLAFKKVHEAFG-GNIKEFVIGGAKINPDVEEFLRTiGFP---YTIG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVVSAQNK-FTKLGSVGYVSSNVRIKMVDLDTEealgpNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLR 1563
Cdd:cd05914 265 YGMTETAPIISYSPPnRIRLGSAGKVIDGVEVRIDSPDPA-----TGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFH 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1564 TGDLAYYDDNGEIYIVDRISDFINFRS-INVSPAEIETVLMTHPAVL-----------QAAVLGIPNEVDEQHPKafvvQ 1631
Cdd:cd05914 340 TGDLGKIDAEGYLYIRGRKKEMIVLSSgKNIYPEEIEAKINNMPFVLeslvvvqekklVALAYIDPDFLDVKALK----Q 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1820754837 1632 VPNKSVTEQELISYVEKNLPDYCRLrGGVKIV-DQLPRTTTGKIAR 1676
Cdd:cd05914 416 RNIIDAIKWEVRDKVNQKVPNYKKI-SKVKIVkEEFEKTPKGKIKR 460
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
30-546 |
3.75e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 161.09 E-value: 3.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 30 PILKKCtnVGALVLEKLRSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAAL 109
Cdd:PRK12583 14 PLLTQT--IGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 110 YLGAI---SNP--WDNELSpmtarYFLSLTKPKIVFV------------------NGESAECLAQVVKENNMDTRLVVFA 166
Cdd:PRK12583 92 RIGAIlvnINPayRASELE-----YALGQSGVRWVICadafktsdyhamlqellpGLAEGQPGALACERLPELRGVVSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 167 --DSAGFVGRAATLTavlRSQDTAWIDEFECAKLTSPKHVAAIVCSSGTSGFPKGTEISHAAMIN--YMAHVKVHdLKGH 242
Cdd:PRK12583 167 paPPPGFLAWHELQA---RGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNngYFVAESLG-LTEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 243 VSMWTPSMRWYCglFIVIKAILDC---SKRIIVP-DYDDDEGLCRFIEKYevswfRCDSCFPIRLVKFGVL-----SKYR 313
Cdd:PRK12583 243 DRLCVPVPLYHC--FGMVLANLGCmtvGACLVYPnEAFDPLATLQAVEEE-----RCTALYGVPTMFIAELdhpqrGNFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 314 LPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDYGGLcARQTKYSKP-----GSCGFVCETGRLKVVDPNtGKV 388
Cdd:PRK12583 316 LSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPV-SLQTTAADDlerrvETVGRTQPHLEVKVVDPD-GAT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 389 LGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQH 468
Cdd:PRK12583 394 VPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTH 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 469 PAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQIA 546
Cdd:PRK12583 474 PAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHF-KVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1206-1681 |
4.59e-41 |
|
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: 159.39 E-value: 4.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFTVSS 1285
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAanlmeaakelkmnlkvvvmdkldgYESVeenVMKGHDTREIIEfkchVTNPDDVALIVPSSGTTGLPKGTEISHYSLF 1365
Cdd:cd12118 111 FE------------------------YEDL---LAEGDPDFEWIP----PADEWDPIALNYTSGTTGRPKGVVYHHRGAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1366 ccLHPYKNrtlvghtcIVTPTMRwHYGV----LMAFRL--------VAANAKKLIVPDNDDAENFCQLIEKYQITWFGTD 1433
Cdd:cd12118 160 --LNALAN--------ILEWEMK-QHPVylwtLPMFHCngwcfpwtVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1434 PFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITnhYGMTDTACVVSA--------------QNK 1499
Cdd:cd12118 229 PTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHV--YGLTETYGPATVcawkpewdelpteeRAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1500 FTKLGSVGYVSSNvRIKMVDLDTEEALGPN--KIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIY 1577
Cdd:cd12118 307 LKARQGVRYVGLE-EVDVLDPETMKPVPRDgkTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1578 IVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLR 1657
Cdd:cd12118 385 IKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPK 464
|
490 500
....*....|....*....|....
gi 1820754837 1658 GGVkiVDQLPRTTTGKIARKQLRD 1681
Cdd:cd12118 465 TVV--FGELPKTSTGKIQKFVLRD 486
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
629-1099 |
4.83e-41 |
|
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: 157.88 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNEE 708
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 saenlmeaakeenlqvrvmvigslpgfvslanileeqvsraeidgfrctkidnphDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd05972 82 -------------------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYP 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 YNSITPVEEVH--AKNEI-----------CAWVPTIrwhGGLNQCIEVIMSNAKWiiFSDDNIkeialCEIIQKHGVT-W 854
Cdd:cd05972 107 LGHIPTAAYWLglRPDDIhwniadpgwakGAWSSFF---GPWLLGATVFVYEGPR--FDAERI-----LELLERYGVTsF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 855 LGTDTNFAILyVKMNIFQkYPMPSLRKMVITGAPFTKE-----LHETVAKIMPHtqilqcYGLTDAGGLC-VSQAKNSKP 928
Cdd:cd05972 177 CGPPTAYRML-IKQDLSS-YKFSHLRLVVSAGEPLNPEviewwRAATGLPIRDG------YGQTETGLTVgNFPDMPVKP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 929 GSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEF--MMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNR 1006
Cdd:cd05972 249 GSMGRPTPGYDVAIIDDD-GRELPPGEEGDIAIKLPPpgLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1007 ISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV---QKVVEKEVTEEELHDLVNKNLPWYcKLQA 1083
Cdd:cd05972 327 ADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVvltSGYEPSEELAEELQGHVKKVLAPY-KYPR 405
|
490
....*....|....*.
gi 1820754837 1084 GIKFVNDFPRISTGKI 1099
Cdd:cd05972 406 EIEFVEELPKTISGKI 421
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1188-1680 |
7.61e-41 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 159.91 E-value: 7.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1188 KSKPDSIGQVDAlTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISN----TWDHE- 1262
Cdd:PRK06087 34 RAMPDKIAVVDN-HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVpllpSWREAe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1263 ----LTPMTARNFLTLTspkiVFTVSSSAANLMEAAKELKMNLKVVVMDK-------------LDGYESVEENVMkghdt 1325
Cdd:PRK06087 113 lvwvLNKCQAKMFFAPT----LFKQTRPVDLILPLQNQLPQLQQIVGVDKlapatsslslsqiIADYEPLTTAIT----- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1326 reiiefkchvTNPDDVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRT-LVGHTCIVTPT-----MRWHYGVLMAFRL 1399
Cdd:PRK06087 184 ----------THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLnLTWQDVFMMPAplghaTGFLHGVTAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1400 VAanakKLIVPDNDDAENFCQLIEKYQITW-FGTDPFM--IIKFIKSQlleKYRLPTLKVILSSGAHLRKEHLEVMRE-- 1474
Cdd:PRK06087 254 GA----RSVLLDIFTPDACLALLEQQRCTCmLGATPFIydLLNLLEKQ---PADLSALRFFLCGGTTIPKKVARECQQrg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1475 -KLPDVfitnhYGMTDT---ACVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPE 1550
Cdd:PRK06087 327 iKLLSV-----YGSTESsphAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKT-LPPGCEGEEASRGPNVFMGYLDEPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1551 TTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVV 1630
Cdd:PRK06087 401 LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1631 -QVPNKSVTEQELISYV-EKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK06087 481 lKAPHHSLTLEEVVAFFsRKRVAKY-KYPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1202-1682 |
9.61e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 160.17 E-value: 9.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDN---NLDVFLILLgtmYIGAI---SN---TwDHELTPM------ 1266
Cdd:PRK05605 55 GATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNcpqHIVAFYAVL---RLGAVvveHNplyT-AHELEHPfedhga 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1267 --------TARNFLTL---TSPKIVFTVSSSAAnlMEAAKELKMNLKVVVM----DKLDG-------YESVEENVMKGHD 1324
Cdd:PRK05605 131 rvaivwdkVAPTVERLrrtTPLETIVSVNMIAA--MPLLQRLALRLPIPALrkarAALTGpapgtvpWETLVDAAIGGDG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1325 TREiiefKCHVTNPDDVALIVPSSGTTGLPKGTEISHYSLFCCLH---------PYKNRTLVGhtciVTPtMRWHYGVLM 1395
Cdd:PRK05605 209 SDV----SHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkawvpglGDGPERVLA----ALP-MFHAYGLTL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1396 AFRLVAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQllEKYRLPTLKVILS-SGAHLRKEHLEVMRE 1474
Cdd:PRK05605 280 CLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAA--EERGVDLSGVRNAfSGAMALPVSTVELWE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1475 KLPDVFITNHYGMTDTACVVSAqNKFTKLGSVGYV-----SSNVRIkmVDLDT-EEALGPNKIGELRVKAITIMQGYHKN 1548
Cdd:PRK05605 358 KLTGGLLVEGYGLTETSPIIVG-NPMSDDRRPGYVgvpfpDTEVRI--VDPEDpDETMPDGEEGELLVRGPQVFKGYWNR 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1549 PETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAF 1628
Cdd:PRK05605 435 PEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAA 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 1629 VVQVPNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRDM 1682
Cdd:PRK05605 514 VVLEPGAALDPEGLRAYCREHLTRYKVPR-RFYHVDELPRDQLGKVRRREVREE 566
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1206-1680 |
1.53e-40 |
|
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: 156.47 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPmtarnfltltsPKIVFTVSS 1285
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHP-----------DDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchVTNPDDVALIVPSSGTTGLPKGTEISH--YS 1363
Cdd:cd05919 81 CEARLV-------------------------------------------VTSADDIAYLLYSSGTTGPPKGVMHAHrdPL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1364 LFCCLHPYKNRTLV-GHTCIVTPTMRWHYGV---LMAFRLVAANAkkLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIK 1439
Cdd:cd05919 118 LFADAMAREALGLTpGDRVFSSAKMFFGYGLgnsLWFPLAVGASA--VLNPGWPTAERVLATLARFRPTVLYGVPTFYAN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1440 FIKSQLLEKYRLPTLKVILSSGAHLRKEhlevMREKLPDVF---ITNHYGMTDTACV-VSAQNKFTKLGSVGYVSSNVRI 1515
Cdd:cd05919 196 LLDSCAGSPDALRSLRLCVSAGEALPRG----LGERWMEHFggpILDGIGATEVGHIfLSNRPGAWRLGSTGRPVPGYEI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1516 KMVDLDTEEAlGPNKIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSP 1595
Cdd:cd05919 272 RLVDEEGHTI-PPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1596 AEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVV----QVPNKSVTEQeLISYVEKNLPDYCRLRgGVKIVDQLPRTTT 1671
Cdd:cd05919 350 VEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVlkspAAPQESLARD-IHRHLLERLSAHKVPR-RIAFVDELPRTAT 427
|
....*....
gi 1820754837 1672 GKIARKQLR 1680
Cdd:cd05919 428 GKLQRFKLR 436
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
1206-1682 |
1.60e-40 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 158.08 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFtVSS 1285
Cdd:TIGR02262 32 SYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVF-VSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAA--KELKMNLKVVVMDKLDGYESVEENVMKGHDtreiiEFKCHVTNPDDVALIVPSSGTTGLPKGTEISHYS 1363
Cdd:TIGR02262 111 ALLPVIKAAlgKSPHLEHRVVVGRPEAGEVQLAELLATESE-----QFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1364 LFCCLHPYKNRTL---VGHTCIVTPTMRWHYGV--LMAFRLvAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMII 1438
Cdd:TIGR02262 186 PYWTAELYARNTLgirEDDVCFSAAKLFFAYGLgnALTFPM-SVGATTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1439 KFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACV-VSAQNKFTKLGSVGYVSSNVRIKM 1517
Cdd:TIGR02262 265 AMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARF-GVDIVDGIGSTEMLHIfLSNLPGDVRYGTSGKPVPGYRLRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1518 VDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSdGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAE 1597
Cdd:TIGR02262 344 VG-DGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1598 IETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARK 1677
Cdd:TIGR02262 422 IESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPR-WIVFVDDLPKTATGKIQRF 500
|
....*
gi 1820754837 1678 QLRDM 1682
Cdd:TIGR02262 501 KLREG 505
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1191-1682 |
2.26e-40 |
|
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: 158.39 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDaltGKVQ-TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheltPMTA- 1268
Cdd:COG1021 39 PDRIAVVD---GERRlSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI---------PVFAl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1269 --------RNFLTLTSPKIVFTVSSS--------AANLMEAAKELKMnlkVVVMDKLDGYESVEENVMKGHDTREIiefk 1332
Cdd:COG1021 107 pahrraeiSHFAEQSEAVAYIIPDRHrgfdyralARELQAEVPSLRH---VLVVGDAGEFTSLDALLAAPADLSEP---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1333 chVTNPDDVALIVPSSGTTGLPKGTEISH----YSL-----FCCLHPYkNRTLV----GH----TCivtPtmrwhyGVLM 1395
Cdd:COG1021 180 --RPDPDDVAFFQLSGGTTGLPKLIPRTHddylYSVrasaeICGLDAD-TVYLAalpaAHnfplSS---P------GVLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1396 AF----RLVAAnakklivpDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEV 1471
Cdd:COG1021 248 VLyaggTVVLA--------PDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1472 MREKLPdVFITNHYGMTDTACVvsaqnkFTKLG--------SVGY-VSSNVRIKMVDlDTEEALGPNKIGELRVKA-ITI 1541
Cdd:COG1021 320 VRPALG-CTLQQVFGMAEGLVN------YTRLDdpeeviltTQGRpISPDDEVRIVD-EDGNPVPPGEVGELLTRGpYTI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1542 mQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVD 1621
Cdd:COG1021 392 -RGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYL 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1622 EQHPKAFVVqVPNKSVTEQELISYV-EKN-----LPDycRLRggvkIVDQLPRTTTGKIARKQLRDM 1682
Cdd:COG1021 471 GERSCAFVV-PRGEPLTLAELRRFLrERGlaafkLPD--RLE----FVDALPLTAVGKIDKKALRAA 530
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1340-1676 |
2.45e-40 |
|
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: 153.04 E-value: 2.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1340 DVALIVPSSGTTGLPKGTEISH---YSLFCCLHPYKNRTLVGHTCIVTP---TMRWHYGVLMAFRLVAAnakklIVPDND 1413
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrqtLRAAAAWADCADLTEDDRYLIINPffhTFGYKAGIVACLLTGAT-----VVPVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1414 -DAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTAC 1492
Cdd:cd17638 76 fDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1493 VV---SAQNKFTKLGSVGYVSSNVRIKMVDldteealgpnkIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAY 1569
Cdd:cd17638 156 ATmcrPGDDAETVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1570 YDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKN 1649
Cdd:cd17638 225 LDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRER 304
|
330 340
....*....|....*....|....*..
gi 1820754837 1650 LPDYCRLRgGVKIVDQLPRTTTGKIAR 1676
Cdd:cd17638 305 LANYKVPR-FVRFLDELPRNASGKVMK 330
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
65-543 |
4.86e-40 |
|
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: 156.31 E-value: 4.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGIC---THNHLESY--VPllaalYLGAISNPWDNELSPMTARYFLSLTKPKIV 139
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLapnTPAMYELHfgVP-----MAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 140 FVNGESA-ECLaqvVKENNMDTRLVVFADsagfvgraatltavlrsqdtawidefECAKLtspkhvaAIVCSSGTSGFPK 218
Cdd:cd12118 106 FVDREFEyEDL---LAEGDPDFEWIPPAD--------------------------EWDPI-------ALNYTSGTTGRPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 219 GTEISH-AAMINYMAHVKVHDLKGH-VSMWTPSM----RWyCGLFIV--IKAILDCSKRIivpdydDDEGLCRFIEKYEV 290
Cdd:cd12118 150 GVVYHHrGAYLNALANILEWEMKQHpVYLWTLPMfhcnGW-CFPWTVaaVGGTNVCLRKV------DAKAIYDLIEKHKV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 291 SWFrcdSCFPIRLVkfgVLSKYRLPTLKillfggaHFKGELQQTLVKLLPHT-----------DVILSYGMTDYGGL--- 356
Cdd:cd12118 223 THF---CGAPTVLN---MLANAPPSDAR-------PLPHRVHVMTAGAPPPAavlakmeelgfDVTHVYGLTETYGPatv 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 357 CARQTKY-SKPGScgfvcETGRLK--------------VVDPNTGKVLGAN-KT-GEIWAKSSYMMNGYYNNPEATRRAL 419
Cdd:cd12118 290 CAWKPEWdELPTE-----ERARLKarqgvryvgleevdVLDPETMKPVPRDgKTiGEIVFRGNIVMKGYLKNPEATAEAF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 420 dSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKE 499
Cdd:cd12118 365 -RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAK 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 500 VTELDITDlvkqnmpwYCRLH-AG------VKFMEkLPRTATGKIAKKQLK 543
Cdd:cd12118 444 VTEEEIIA--------FCREHlAGfmvpktVVFGE-LPKTSTGKIQKFVLR 485
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
36-477 |
9.01e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 157.95 E-value: 9.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 36 TNVGALVLEKLRSRPEFIAQVEAVTGA--ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGA 113
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 114 ISNPWDNELSPMTARYFLSLTKPKIVFVngESAECLAQV--VKENNMDTRLVVFADSAGFVG--RAATLTAVLRS-QDTA 188
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFV--EDQEQLDKLleVRDELPSLRHIVVLDPRGLRDdpRLLSLDELLALgREVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 189 WIDEFE-CAKLTSPKHVAAIVCSSGTSGFPKGTEISHAAMI-NYMAHVKVHDLKG-----------HV--SMWTpSMRWY 253
Cdd:COG1022 169 DPAELEaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLsNARALLERLPLGPgdrtlsflplaHVfeRTVS-YYALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 254 CGLFIV----IKAILDCSKRI------IVPdydddeglcRFIEK-Y--------EVSWFR----------CDSCFPIRLV 304
Cdd:COG1022 248 AGATVAfaesPDTLAEDLREVkptfmlAVP---------RVWEKvYagiqakaeEAGGLKrklfrwalavGRRYARARLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 305 --KFGVLSKYRLPTLKILLFGG--AHFKGELQQTLV---KLLPHTD---------VILSYGMTDYGG-LCARQTKYSKPG 367
Cdd:COG1022 319 gkSPSLLLRLKHALADKLVFSKlrEALGGRLRFAVSggaALGPELArffralgipVLEGYGLTETSPvITVNRPGDNRIG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 368 SCGFVCETGRLKVVDpntgkvlgankTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSE 447
Cdd:COG1022 399 TVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKD 467
|
490 500 510
....*....|....*....|....*....|....*
gi 1820754837 448 FInyraI-----KISPAEIEALIQQHPAVFQVAVV 477
Cdd:COG1022 468 LI----VtsggkNVAPQPIENALKASPLIEQAVVV 498
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
60-543 |
9.36e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 155.83 E-value: 9.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 60 TGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAA----LYLGAISnpWdnELSPMTARYFLSLTK 135
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAArrsgLYYTPIN--W--HLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 136 PKIVFVNGESAECLAQVVKE--NNMDTRLVVFADSAGFvgraATLTAVLRSQDTawidefecaklTSPKHVAA---IVCS 210
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAElpAGVPLLLVVAGPVPGF----RSYEEALAAQPD-----------TPIADETAgadMLYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 211 SGTSGFPKG-----TEISHAAMINYMAHVKVHDLKGhvsmwTPSMRWYC---------GLFIVikAILDCSKRIIVPDYD 276
Cdd:PRK08276 149 SGTTGRPKGikrplPGLDPDEAPGMMLALLGFGMYG-----GPDSVYLSpaplyhtapLRFGM--SALALGGTVVVMEKF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 277 DDEGLCRFIEKYEVSwfrcDSCF-PI---RLVKF--GVLSKYRLPTLKILLFGGAHFKGELQQTLVkllphtD-----VI 345
Cdd:PRK08276 222 DAEEALALIERYRVT----HSQLvPTmfvRMLKLpeEVRARYDVSSLRVAIHAAAPCPVEVKRAMI------DwwgpiIH 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 346 LSYGMTDYGGLCA--RQTKYSKPGSCGFVCeTGRLKVVDPNtGKVLGANKTGEIwakssYM-MNG----YYNNPEATRRA 418
Cdd:PRK08276 292 EYYASSEGGGVTVitSEDWLAHPGSVGKAV-LGEVRILDED-GNELPPGEIGTV-----YFeMDGypfeYHNDPEKTAAA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 419 LDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGK 498
Cdd:PRK08276 365 RNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGA 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 499 EVTELDITDLVKqnmpwYCRLH-AGVK------FMEKLPRTATGKIAKKQLK 543
Cdd:PRK08276 445 DAGDALAAELIA-----WLRGRlAHYKcprsidFEDELPRTPTGKLYKRRLR 491
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
625-1099 |
1.22e-39 |
|
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: 153.60 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 625 GKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDhVVSKLSA-RYFLSLMSPKVV 703
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPIN-TALRGDElAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 704 FVneesaenlmeaakeenlqvrvmvigslpgfvslanileeqvsraeidgfrctkidnphDLAMICSSSGTTGMPKGTEL 783
Cdd:cd05934 80 VV----------------------------------------------------------DPASILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 784 SYASLYNS----------------ITPVEEVHAKNEICAWVPTIrWHGGLNQCIEVIMSNAKWiifsDDnikeialceiI 847
Cdd:cd05934 102 THANLTFAgyysarrfglgeddvyLTVLPLFHINAQAVSVLAAL-SVGATLVLLPRFSASRFW----SD----------V 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 848 QKHGVTWlgtdtnFAILYVKMNIFQKYPmPS-------LRkmVITGAPFTKELHETVAKIMpHTQILQCYGLTDAG-GLC 919
Cdd:cd05934 167 RRYGATV------TNYLGAMLSYLLAQP-PSpddrahrLR--AAYGAPNPPELHEEFEERF-GVRLLEGYGMTETIvGVI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 920 VSQAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEF---MMKGYHKNPEQTKEAFdSDGWLHTKDIGYYD 996
Cdd:cd05934 237 GPRDEPRRPGSIGRPAPGYEVRIVDDD-GQELPAGEPGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 997 ENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLP 1076
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLA 394
|
490 500
....*....|....*....|...
gi 1820754837 1077 WYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:cd05934 395 YF-KVPRYIRFVDDLPKTPTEKV 416
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1206-1684 |
2.23e-39 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 155.74 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWD-----HEL----------TPMTARN 1270
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINpayrlSELeyalnqsgckALIAADG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 FLTltspkivftvSSSAANLMEAAKELKM------------NLKVVV---MDKLDGYESVEENV-MKGHDTREIIEFKCH 1334
Cdd:PRK08315 125 FKD----------SDYVAMLYELAPELATcepgqlqsarlpELRRVIflgDEKHPGMLNFDELLaLGRAVDDAELAARQA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1335 VTNPDDVALIVPSSGTTGLPKGTEISHYSLFcclhpyKNRTLVGHTCIVTPTMR-------WH-YGVLMAfRLVAANAKK 1406
Cdd:PRK08315 195 TLDPDDPINIQYTSGTTGFPKGATLTHRNIL------NNGYFIGEAMKLTEEDRlcipvplYHcFGMVLG-NLACVTHGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1407 LIVPDND--DAENFCQLIEKYQIT-WFGTdPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRkehLEVMREKLPDVF--- 1480
Cdd:PRK08315 268 TMVYPGEgfDPLATLAAVEEERCTaLYGV-PTMFIAELDHPDFARFDLSSLRTGIMAGSPCP---IEVMKRVIDKMHmse 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1481 ITNHYGMTDTAcVVSAQNKFT-----KLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQA 1555
Cdd:PRK08315 344 VTIAYGMTETS-PVSTQTRTDdplekRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1556 FDSDGWLRTGDLAYYDDNGEIYIVDRISDFInfrsI----NVSPAEIETVLMTHPAVLQAAVLGIPNEvdeqhpK----- 1626
Cdd:PRK08315 423 IDADGWMHTGDLAVMDEEGYVNIVGRIKDMI----IrggeNIYPREIEEFLYTHPKIQDVQVVGVPDE------Kygeev 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 1627 -AFVVQVPNKSVTEQELIsyveknlpDYCRLRGG-------VKIVDQLPRTTTGKIARKQLRDMYV 1684
Cdd:PRK08315 493 cAWIILRPGATLTEEDVR--------DFCRGKIAhykipryIRFVDEFPMTVTGKIQKFKMREMMI 550
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
625-1099 |
3.47e-39 |
|
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: 153.37 E-value: 3.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 625 GKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVF 704
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 705 VNEESaenlmeaakeenlqvrvmvigslpgfvslanileeqvsraeidgfrctkidnphDLAMICSSSGTTGMPKGTELS 784
Cdd:cd05914 85 VSDED------------------------------------------------------DVALINYTSGTTGNSKGVMLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 785 YASLYNSITPVEEV---HAKNEICAWVPtirWHGGLNQCIEVIM--SNAKWIIFSDD----------------------- 836
Cdd:cd05914 111 YRNIVSNVDGVKEVvllGKGDKILSILP---LHHIYPLTFTLLLplLNGAHVVFLDKipsakiialafaqvtptlgvpvp 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 837 -NIKEIALCEIIQKHGVTWLgtdtNFAiLYVKMNIFQKYPMP----------SLRKMVITGAPFTKELHETVAKI-MPHT 904
Cdd:cd05914 188 lVIEKIFKMDIIPKLTLKKF----KFK-LAKKINNRKIRKLAfkkvheafggNIKEFVIGGAKINPDVEEFLRTIgFPYT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 905 QilqCYGLTDAGGLCVSQAKNS-KPGSCGFVTKGIRIKIADEKTgialgPKERGEICIKSEFMMKGYHKNPEQTKEAFDS 983
Cdd:cd05914 263 I---GYGMTETAPIISYSPPNRiRLGSAGKVIDGVEVRIDSPDP-----ATGEGEIIVRGPNVMKGYYKNPEATAEAFDK 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 984 DGWLHTKDIGYYDENGEIFFVNRISDFI---NYKAIklSSAEIEGVLELHPSILKAVVVpVPHETDIELPLAF------- 1053
Cdd:cd05914 335 DGWFHTGDLGKIDAEGYLYIRGRKKEMIvlsSGKNI--YPEEIEAKINNMPFVLESLVV-VQEKKLVALAYIDpdfldvk 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 1054 -VQKVVEKEVTEEELHDLVNKNLPWYCKLqAGIKFVN-DFPRISTGKI 1099
Cdd:cd05914 412 aLKQRNIIDAIKWEVRDKVNQKVPNYKKI-SKVKIVKeEFEKTPKGKI 458
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1188-1680 |
4.16e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 154.01 E-value: 4.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1188 KSKPDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMT 1267
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1268 ARNFLTLTSPKIVftVSSSAANLMEAAKELKMNLKVVVMDKLDGYESVEeNVMKGHDTReIIEFKCHvtnpddvALIVPS 1347
Cdd:PRK13390 88 ADYIVGDSGARVL--VASAALDGLAAKVGADLPLRLSFGGEIDGFGSFE-AALAGAGPR-LTEQPCG-------AVMLYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1348 SGTTGLPKGT--EISHYSLFCCLHPYKN--RTLVGHT---CIVTPTMRWHYGVLMAFRLVAANAKKLIVPDNDDAENFCQ 1420
Cdd:PRK13390 157 SGTTGFPKGIqpDLPGRDVDAPGDPIVAiaRAFYDISesdIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQATLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1421 LIEKYQITWFGTDPFMIIKFIK--SQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKL-PDVF----ITNHYGMTdtacV 1493
Cdd:PRK13390 237 HVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLgPIVYeyysSTEAHGMT----F 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1494 VSAQNKFTKLGSVGYvSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDG--WLRTGDLAYYD 1571
Cdd:PRK13390 313 IDSPDWLAHPGSVGR-SVLGDLHICDDDGNE-LPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1572 DNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPN-EVDEQhPKAFVVQVPNKSVTEQ---ELISYVE 1647
Cdd:PRK13390 391 EDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpEMGEQ-VKAVIQLVEGIRGSDElarELIDYTR 469
|
490 500 510
....*....|....*....|....*....|...
gi 1820754837 1648 KNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK13390 470 SRIAHYKAPR-SVEFVDELPRTPTGKLVKGLLR 501
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
65-546 |
5.29e-39 |
|
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: 152.27 E-value: 5.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAEclaqvvkennmdtrlvvfadsagfvgraatltavlrsqdtawidefecakLTSPKHVAAIVCSSGTSGFPKGTEISH 224
Cdd:cd05969 82 LYE--------------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AAMINYMAHVKVH-DLKGHVSMW-TPSMRWYCGLFI-VIKAILDCSKRIIVPDYDDDEGLCRFIEKYEVS-WFRCDSCFP 300
Cdd:cd05969 112 DAMIFYYFTGKYVlDLHPDDIYWcTADPGWVTGTVYgIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTvWYTAPTAIR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 301 iRLVKFGV--LSKYRLPTLKILLFGGAHFKGELQQTLVKLL--PHTDvilSYGMTDYGG--LCARQTKYSKPGSCGFVCE 374
Cdd:cd05969 192 -MLMKEGDelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFgvPIHD---TWWQTETGSimIANYPCMPIKPGSMGKPLP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 375 TGRLKVVDPNtGKVLGANKTGEIWAKSSY--MMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYR 452
Cdd:cd05969 268 GVKAAVVDEN-GNELPPGTKGILALKPGWpsMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 453 AIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTE---LDITDLVKQNMPwycrLHAG---VKFM 526
Cdd:cd05969 346 GHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKLG----AHVApreIEFV 421
|
490 500
....*....|....*....|
gi 1820754837 527 EKLPRTATGKIAKKQLKQIA 546
Cdd:cd05969 422 DNLPKTRSGKIMRRVLKAKE 441
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1347-1676 |
5.86e-39 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 148.71 E-value: 5.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1347 SSGTTGLPKGTEISHYSLfccLHPYK-NRTLVGHTC---IVTPTMRWHYGVLMAFRLVAANAKKLIVPDNDDAENFCQLI 1422
Cdd:cd17633 8 TSGTTGLPKAYYRSERSW---IESFVcNEDLFNISGedaILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1423 EKYQITWFGTDPFMIikfiksQLLEKYRLPTLKV--ILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVV-SAQNK 1499
Cdd:cd17633 85 NQYNATVIYLVPTML------QALARTLEPESKIksIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITyNFNQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1500 FTKLGSVGYVSSNVRIKMVDLDTeealgpNKIGELRVKAITIMQGYHKNPETTKqafdsDGWLRTGDLAYYDDNGEIYIV 1579
Cdd:cd17633 159 SRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1580 DRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVqvpNKSVTEQELISYVEKNLPDYCRLRGG 1659
Cdd:cd17633 228 GRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPKKI 304
|
330
....*....|....*..
gi 1820754837 1660 VKiVDQLPRTTTGKIAR 1676
Cdd:cd17633 305 IF-VDSLPYTSSGKIAR 320
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
65-543 |
7.27e-39 |
|
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: 151.34 E-value: 7.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 saeclaqvvkennmDTRLVVFadsagfvgraatltavlrsqdtawidefecakltspkhvaaivcSSGTSGFPKGTEISH 224
Cdd:cd05972 82 --------------DPALIYF--------------------------------------------TSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AAMINYMAHVK-VHDLKGHVSMWTPS-MRWYCGLFIVIKAILDCSKRIIVPDYD--DDEGLCRFIEKYEVSWFrcdSCFP 300
Cdd:cd05972 104 SYPLGHIPTAAyWLGLRPDDIHWNIAdPGWAKGAWSSFFGPWLLGATVFVYEGPrfDAERILELLERYGVTSF---CGPP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 301 I---RLVKFGvLSKYRLPTLKILLFGGAHFKGElqqTLVKLLPHT--DVILSYGMTDYGGLCAR-QTKYSKPGSCGFVCE 374
Cdd:cd05972 181 TayrMLIKQD-LSSYKFSHLRLVVSAGEPLNPE---VIEWWRAATglPIRDGYGQTETGLTVGNfPDMPVKPGSMGRPTP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 375 TGRLKVVDPNtGKVLGANKTGEIWAKSSY--MMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYR 452
Cdd:cd05972 257 GYDVAIIDDD-GRELPPGEEGDIAIKLPPpgLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 453 AIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTE---LDITDLVKQNMPWYCRLHAgVKFMEKL 529
Cdd:cd05972 335 GYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYPRE-IEFVEEL 413
|
490
....*....|....
gi 1820754837 530 PRTATGKIAKKQLK 543
Cdd:cd05972 414 PKTISGKIRRVELR 427
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1206-1679 |
1.09e-38 |
|
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: 152.24 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELtPMTARNFLTLTSP-KIVFTVS 1284
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEY-PEERRIYIMLDSGvRVVLTQR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1285 SSAAnlmeaakELKMNLKVVVMDKLDGYESVEENVMkghdtreiiefkcHVTNPDDVALIVPSSGTTGLPKGTEISHYSL 1364
Cdd:cd17656 94 HLKS-------KLSFNKSTILLEDPSISQEDTSNID-------------YINNSDDLLYIIYTSGTTGKPKGVQLEHKNM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1365 FCCLHPYKNRTLVGHTCIV----TPTMRWHYGVLMAFRLVAANakkLIVPDND---DAENFCQLIEKYQITWFGTdPFMI 1437
Cdd:cd17656 154 VNLLHFEREKTNINFSDKVlqfaTCSFDVCYQEIFSTLLSGGT---LYIIREEtkrDVEQLFDLVKRHNIEVVFL-PVAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1438 IKFIKSQLLEKYRLPT-LKVILSSGAHL--RKEHLEVMREKlpDVFITNHYGMTD----TACVVSAQNKFTKLGSVGYVS 1510
Cdd:cd17656 230 LKFIFSEREFINRFPTcVKHIITAGEQLviTNEFKEMLHEH--NVHLHNHYGPSEthvvTTYTINPEAEIPELPPIGKPI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1511 SNVRIKMvdLDTEEALGP-NKIGELRVKAITIMQGYHKNPETTKQAFDSDGW------LRTGDLAYYDDNGEIYIVDRIS 1583
Cdd:cd17656 308 SNTWIYI--LDQEQQLQPqGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRAD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1584 DFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVvqVPNKSVTEQELISYVEKNLPDYCRLRGGVKiV 1663
Cdd:cd17656 386 HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VMEQELNISQLREYLAKQLPEYMIPSFFVP-L 462
|
490
....*....|....*.
gi 1820754837 1664 DQLPRTTTGKIARKQL 1679
Cdd:cd17656 463 DQLPLTPNGKVDRKAL 478
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1206-1680 |
1.13e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 154.73 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGaISNTWDHELTPMTARNFLTLTSPKIVFTVSS 1285
Cdd:PRK07529 60 TYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 --------SAANLMEAAKELKMNLKVVVMDKLDGYESVEENVMKGHDTREIIEF-----KC--------HVTNPDDVALI 1344
Cdd:PRK07529 139 fpgtdiwqKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHARILDFdaelaRQpgdrlfsgRPIGPDDVAAY 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1345 VPSSGTTGLPK------GTEIS-HYS------------LFCCL---HpyknrtlVG--HTCIVTPTMRWHYGVL---MAF 1397
Cdd:PRK07529 219 FHTGGTTGMPKlaqhthGNEVAnAWLgalllglgpgdtVFCGLplfH-------VNalLVTGLAPLARGAHVVLatpQGY 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1398 RlvaanakklivpdnDDA--ENFCQLIEKYQITWFGTDPFMIikfikSQLL----EKYRLPTLKVILSSGAHLRkehLEV 1471
Cdd:PRK07529 292 R--------------GPGviANFWKIVERYRINFLSGVPTVY-----AALLqvpvDGHDISSLRYALCGAAPLP---VEV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1472 MR--EKLPDVFITNHYGMTDTACVVSAQ--NKFTKLGSVG----YvsSNVRIKMVDLD--TEEALGPNKIGELRVKAITI 1541
Cdd:PRK07529 350 FRrfEAATGVRIVEGYGLTEATCVSSVNppDGERRIGSVGlrlpY--QRVRVVILDDAgrYLRDCAVDEVGVLCIAGPNV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1542 MQGYhKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFInfrsI----NVSPAEIETVLMTHPAVLQAAVLGIP 1617
Cdd:PRK07529 428 FSGY-LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI----IrgghNIDPAAIEEALLRHPAVALAAAVGRP 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1618 N----EVdeqhPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRGGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK07529 503 DahagEL----PVAYVQLKPGASATEAELLAFARDHIAERAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1191-1681 |
1.25e-38 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 152.99 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDALtGKVqTYADMSERSIKCALWLKKQGVKPGDIIG------------LCSDNNLDVFLILLGTMYIG----- 1253
Cdd:PRK13382 57 PDRPGLIDEL-GTL-TWRELDERSDALAAALQALPIGEPRVVGimcrnhrgfveaLLAANRIGADILLLNTSFAGpalae 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1254 ------AISNTWDHELTPMTARNFLTLTSP-KIVFTVSSSAANLMEAakelkmnlkvvvmdkldgyesveenVMKGHDTR 1326
Cdd:PRK13382 135 vvtregVDTVIYDEEFSATVDRALADCPQAtRIVAWTDEDHDLTVEV-------------------------LIAAHAGQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1327 EIiefkchVTNPDDVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRTLVGH---TCIVTPTMR-WHYGVLMafrLVAA 1402
Cdd:PRK13382 190 RP------EPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAeepTVIVAPMFHaWGFSQLV---LAAS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1403 NAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMI--IKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVf 1480
Cdd:PRK13382 261 LACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFdrIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1481 ITNHYGMTDTACVVSA--QNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYhkNPETTKQAFDs 1558
Cdd:PRK13382 340 IYNNYNATEAGMIATAtpADLRAAPDTAGRPAEGTEIRILDQDFRE-VPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1559 dGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVT 1638
Cdd:PRK13382 416 -GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASAT 494
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1820754837 1639 EQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK13382 495 PETLKQHVRDNLANYKVPR-DIVVLDELPRGATGKILRRELQA 536
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1335-1681 |
1.27e-38 |
|
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: 151.76 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1335 VTNPDDVA---LIVPSSGTTGLPKGTEISH-YSLFCCLHPYKNRTLVGHTCIVT---PTMRWHYGVLMAFRLVAANAKKL 1407
Cdd:cd05929 118 ETPIEDEAagwKMLYSGGTTGRPKGIKRGLpGGPPDNDTLMAAALGFGPGADSVylsPAPLYHAAPFRWSMTALFMGGTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1408 IVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKsqLLE----KYRLPTLKVILSSGAHLRKEHLEVMREKLPDVfITN 1483
Cdd:cd05929 198 VLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLK--LPEavrnAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1484 HYGMTDT--ACVVSAQNKFTKLGSVGYVSSNvRIKMVDLDTEEaLGPNKIGELRVKAITIMQgYHKNPETTKQAFDSDGW 1561
Cdd:cd05929 275 YYGGTEGqgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNE-VPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGW 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1562 LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAfVVQ-----VPNKS 1636
Cdd:cd05929 352 STLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA-VVQpapgaDAGTA 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1820754837 1637 VTEqELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd05929 431 LAE-ELIAFLRDRLSRYKCPR-SIEFVAELPRDDTGKLYRRLLRD 473
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1191-1679 |
1.68e-38 |
|
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: 151.58 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARN 1270
Cdd:cd12117 11 PDAVAVVYG--DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 FLTLTSPKIVFTVSSSAANLMEAAkelkmnLKVVVMDKLDGYESVEENVmkghdtreiiefkchVTNPDDVALIVPSSGT 1350
Cdd:cd12117 89 MLADAGAKVLLTDRSLAGRAGGLE------VAVVIDEALDAGPAGNPAV---------------PVSPDDLAYVMYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISHYSLFcclhpyknrTLVGHTCIVTPTMrwHYGVLMA---------FRLVAA--NAKKLIVPDND---DAE 1416
Cdd:cd12117 148 TGRPKGVAVTHRGVV---------RLVKNTNYVTLGP--DDRVLQTsplafdastFEIWGAllNGARLVLAPKGtllDPD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1417 NFCQLIEKYQIT--WFGTDPFmiikfikSQLLEKY--RLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTD--- 1489
Cdd:cd12117 217 ALGALIAEEGVTvlWLTAALF-------NQLADEDpeCFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEntt 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1490 --TACVVSAQNKFTklGSV--GYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWL--- 1562
Cdd:cd12117 290 ftTSHVVTELDEVA--GSIpiGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpge 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1563 ---RTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVvqVPNKSVTE 1639
Cdd:cd12117 367 rlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV--VAEGALDA 444
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1820754837 1640 QELISYVEKNLPDYCRLRGGVKiVDQLPRTTTGKIARKQL 1679
Cdd:cd12117 445 AELRAFLRERLPAYMVPAAFVV-LDELPLTANGKVDRRAL 483
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
46-542 |
1.86e-38 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 150.86 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 46 LRSRPEFIAQVEavTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNElSPm 125
Cdd:cd05945 1 AAANPDRPAVVE--GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS-SP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 126 taryflsltkpkivfvngesAECLAQVVkennmdtrlvvfadsagfvgRAATLTAVLrsqdtawidefecaklTSPKHVA 205
Cdd:cd05945 77 --------------------AERIREIL--------------------DAAKPALLI----------------ADGDDNA 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 206 AIVCSSGTSGFPKGTEISHAAMINYMAH-VKVHDLKGH-VSMWTPS-------MRWYCGL------FIVIKAILDCSKRi 270
Cdd:cd05945 101 YIIFTSGSTGRPKGVQISHDNLVSFTNWmLSDFPLGPGdVFLNQAPfsfdlsvMDLYPALasgatlVPVPRDATADPKQ- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 271 ivpdydddegLCRFIEKYEVS-WFRCDScFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYG 349
Cdd:cd05945 180 ----------LFRFLAEHGITvWVSTPS-FAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 350 MTDYGGLC------ARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSD- 422
Cdd:cd05945 249 PTEATVAVtyievtPEVLDGYDRLPIGYAKPGAKLVILDED-GRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDe 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 423 --GWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVakVPGKEV 500
Cdd:cd05945 328 gqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFV--VPKPGA 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 501 TELDITDL---VKQNMPWYC---RLHAgvkfMEKLPRTATGKIAKKQL 542
Cdd:cd05945 406 EAGLTKAIkaeLAERLPPYMiprRFVY----LDELPLNANGKIDRKAL 449
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1191-1680 |
2.58e-38 |
|
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: 151.34 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIgqvdALT--GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTA 1268
Cdd:cd17651 9 PDAP----ALVaeGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAA-------YVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1269 RNfltlTSPKIVFTVSSSAANLMEAAKELKMNLKVVVmdkLDGYESVEENVMKGHDTREIIEfkchvTNPDDVALIVPSS 1348
Cdd:cd17651 78 AY----PAERLAFMLADAGPVLVLTHPALAGELAVEL---VAVTLLDQPGAAAGADAEPDPA-----LDADDLAYVIYTS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1349 GTTGLPKGTEISHYSL--FCCLHpykNRTLVGHtcivtPTMR--------WHYGVLMAFRLVAANAKkLIVPDND---DA 1415
Cdd:cd17651 146 GSTGRPKGVVMPHRSLanLVAWQ---ARASSLG-----PGARtlqfaglgFDVSVQEIFSTLCAGAT-LVLPPEEvrtDP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1416 ENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEH-LEVMREKLPDVFITNHYGMTDTAcVV 1494
Cdd:cd17651 217 PALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEdLREFCAGLPGLRLHNHYGPTETH-VV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1495 SA------QNKFTKLGSVGYVSSNVRIKMVDldteEALGPNKI---GELRVKAITIMQGYHKNPETTKQAFDSDGWL--- 1562
Cdd:cd17651 296 TAlslpgdPAAWPAPPPIGRPIDNTRVYVLD----AALRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPDPFVpga 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1563 ---RTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTE 1639
Cdd:cd17651 372 rmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDA 451
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1820754837 1640 QELISYVEKNLPDYCRLRGGVkIVDQLPRTTTGKIARKQLR 1680
Cdd:cd17651 452 AELRAALATHLPEYMVPSAFV-LLDALPLTPNGKLDRRALP 491
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
629-1100 |
3.28e-38 |
|
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: 151.63 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIIcpwdHVVSKlsaRYFLSLMS-------PK 701
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVL----HTINP---RLFPEQIAyiinhaeDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 702 VVFVNEEsAENLMEAAKEENLQVRVMVIGS------LPGFVSLANiLEEQVSRAEiDGFRCTKIDNpHDLAMICSSSGTT 775
Cdd:cd12119 100 VVFVDRD-FLPLLEAIAPRLPTVEHVVVMTddaampEPAGVGVLA-YEELLAAES-PEYDWPDFDE-NTAAAICYTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 776 GMPKGTELSYASL--------------------YNSITPVEEVHAkneicaW-VPtirwHGGLnqcieviMSNAKwIIFS 834
Cdd:cd12119 176 GNPKGVVYSHRSLvlhamaalltdglglsesdvVLPVVPMFHVNA------WgLP----YAAA-------MVGAK-LVLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 835 DDNIKEIALCEIIQKHGVTW-LGTDTNFAIL--YVKMNifqKYPMPSLRKMVITGAPFTKELHETVAKImpHTQILQCYG 911
Cdd:cd12119 238 GPYLDPASLAELIEREGVTFaAGVPTVWQGLldHLEAN---GRDLSSLRRVVIGGSAVPRSLIEAFEER--GVRVIHAWG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 912 LTDAGGL-CVSQAKNSKPG-----------SCGFVTKGIRIKIADEKTGIAlgP---KERGEICIKSEFMMKGYHKNPEQ 976
Cdd:cd12119 313 MTETSPLgTVARPPSEHSNlsedeqlalraKQGRPVPGVELRIVDDDGREL--PwdgKAVGELQVRGPWVTKSYYKNDEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 977 TkEAFDSDGWLHTKDIGYYDENGEIFFVNRISDfinykAIK-----LSSAEIEGVLELHPSILKAVVVPVPHETDIELPL 1051
Cdd:cd12119 391 S-EALTEDGWLRTGDVATIDEDGYLTITDRSKD-----VIKsggewISSVELENAIMAHPAVAEAAVIGVPHPKWGERPL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1052 AFVQKVVEKEVTEEE----LHDLVNKnlpWYckLQAGIKFVNDFPRISTGKID 1100
Cdd:cd12119 465 AVVVLKEGATVTAEEllefLADKVAK---WW--LPDDVVFVDEIPKTSTGKID 512
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1344-1683 |
3.81e-38 |
|
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: 153.24 E-value: 3.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1344 IVPSSGTTGLPKGTE--------ISHYSLFCCLHPYKNRT---------LVGHTCIVtptmrwhYGVLMA-FRLVAANAK 1405
Cdd:cd05967 235 ILYTSGTTGKPKGVVrdngghavALNWSMRNIYGIKPGDVwwaasdvgwVVGHSYIV-------YGPLLHgATTVLYEGK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1406 KLIVPdndDAENFCQLIEKYQITWFGTDPfMIIKFIKSQ-----LLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPdVF 1480
Cdd:cd05967 308 PVGTP---DPGAFWRVIEKYQVNALFTAP-TAIRAIRKEdpdgkYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG-VP 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1481 ITNHYGMTDTACVVSA-----QNKFTKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVK---AITIMQGYHKNPETT 1552
Cdd:cd05967 383 VIDHWWQTETGWPITAnpvglEPLPIKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKlplPPGCLLTLWKNDERF 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1553 KQAF--DSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVV 1630
Cdd:cd05967 462 KKLYlsKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVV 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1631 QVPNKSVT----EQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:cd05967 542 LKEGVKITaeelEKELVALVREQIGPVAAFR-LVIFVKRLPKTRSGKILRRTLRKIA 597
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
65-544 |
4.14e-38 |
|
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: 149.45 E-value: 4.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 saeclaqvvkennmdtrlvvfadsagfvgraatltavLRSQDTAwidefecaklTSPKHVAAIVCSSGTSGFPKGTEISH 224
Cdd:cd05903 83 -------------------------------------FRQFDPA----------AMPDAVALLLFTSGTTGEPKGVMHSH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 ----AAMINYMAHVkvhDLKGHVSMWTPS-MRWYCG-LFIVIKAILDCSKRIIVPDYDDDEGLcRFIEKYEVSWFRCDSC 298
Cdd:cd05903 116 ntlsASIRQYAERL---GLGPGDVFLVASpMAHQTGfVYGFTLPLLLGAPVVLQDIWDPDKAL-ALMREHGVTFMMGATP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 299 FPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLpHTDVILSYGMTDYGGLCARqtkySKPGSCG-FVCETGR 377
Cdd:cd05903 192 FLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTS----ITPAPEDrRLYTDGR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 378 ------LKVVDpNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDsDGWLHTGDLGYYDNDGEVFLVDRMSEFINY 451
Cdd:cd05903 267 plpgveIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDIIIR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 452 RAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPG-----KEVTE-LDITDLVKQNMPWycRLHagvkF 525
Cdd:cd05903 345 GGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGalltfDELVAyLDRQGVAKQYWPE--RLV----H 418
|
490
....*....|....*....
gi 1820754837 526 MEKLPRTATGKIAKKQLKQ 544
Cdd:cd05903 419 VDDLPRTPSGKVQKFRLRE 437
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
205-544 |
4.18e-38 |
|
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: 149.36 E-value: 4.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 205 AAIVCSSGTSGFPKGTEISHAAmINYMAHVKVHDLKghvsmWTPSMR------WYC--GLFIVIKAILDCSKRIIV-PDY 275
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHAN-LAANVRALVDAWR-----WTEDDVllhvlpLHHvhGLVNALLCPLFAGASVEFlPKF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 276 DDDEGLCRFIEKyEVSWFRCDSCFPIRLvkfgvLSKYRLPTLKILLFGGAHFKG-------------ELQQTLVKLLPHT 342
Cdd:cd05941 166 DPKEVAISRLMP-SITVFMGVPTIYTRL-----LQYYEAHFTDPQFARAAAAERlrlmvsgsaalpvPTLEEWEAITGHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 343 dVILSYGMTDYG-GLCARQTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDS 421
Cdd:cd05941 240 -LLERYGMTEIGmALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 422 DGWLHTGDLGYYDNDGEVFLVDRMS-EFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVakVPGKEV 500
Cdd:cd05941 319 DGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVV--VLRAGA 396
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1820754837 501 TELDITDL---VKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:cd05941 397 AALSLEELkewAKQRLAPYKRPRR-LILVDELPRNAMGKVNKKELRK 442
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1338-1681 |
5.58e-38 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 151.57 E-value: 5.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1338 PDDVALIVPSSGTTGLPKGTEISHYSLFCCLHPY------KNRTLVGHTCIVTPTMRWHYGVLMAFRLVAANAKKL--IV 1409
Cdd:PRK08751 207 PDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAhqwlagTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGGCnhLI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1410 PDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMReKLPDVFITNHYGMTD 1489
Cdd:PRK08751 287 SNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWK-QVTGLTLVEAYGLTE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1490 T---ACVvsaqNKFTKL---GSVGYV--SSNVRIKMvdlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGW 1561
Cdd:PRK08751 366 TspaACI----NPLTLKeynGSIGLPipSTDACIKD---DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1562 LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQvPNKSVTEQE 1641
Cdd:PRK08751 439 LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVK-KDPALTAED 517
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1820754837 1642 LISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK08751 518 VKAHARANLTGYKQPR-IIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1202-1681 |
7.60e-38 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 151.33 E-value: 7.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIG-AISNT--------WDHELTPMTAR--- 1269
Cdd:PRK07059 46 GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGyVVVNVnplytpreLEHQLKDSGAEaiv 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1270 ---NF-------LTLTSPKIVftVSSSAANLMeAAKELKMNL------KVVVMDKLDGYESVEENVMKGHDTReiieFKC 1333
Cdd:PRK07059 126 vleNFattvqqvLAKTAVKHV--VVASMGDLL-GFKGHIVNFvvrrvkKMVPAWSLPGHVRFNDALAEGARQT----FKP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1334 HVTNPDDVALIVPSSGTTGLPKGTEISHYSLFC-------CLHP-YKNRTLVGHTCIVTPTMRWHYGVL-----MAFRLV 1400
Cdd:PRK07059 199 VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVAnvlqmeaWLQPaFEKKPRPDQLNFVCALPLYHIFALtvcglLGMRTG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1401 AANakkLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVF 1480
Cdd:PRK07059 279 GRN---ILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMT-GCP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1481 ITNHYGMTDTACVVSAQ----NKFTklGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAF 1556
Cdd:PRK07059 355 ITEGYGLSETSPVATCNpvdaTEFS--GTIGLPLPSTEVSIRDDDGND-LPLGEPGEICIRGPQVMAGYWNRPDETAKVM 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1557 DSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQvPNKS 1636
Cdd:PRK07059 432 TADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVK-KDPA 510
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1820754837 1637 VTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK07059 511 LTEEDVKAFCKERLTNYKRPK-FVEFRTELPKTNVGKILRRELRD 554
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
627-1099 |
1.28e-37 |
|
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: 147.63 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 627 ECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVfvn 706
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 707 eesaenlmeaakeenlqvrvmVIGSlpgfvslanileeqvsraEIDgfrctkidnphDLAMICSSSGTTGMPKGTELSYA 786
Cdd:cd05935 78 ---------------------VVGS------------------ELD-----------DLALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 787 SLYNSItpVEEVHAKNEIC-----AWVPTIRWHGGLNQCIEVIMSNAKWIIFSDDNiKEIALcEIIQKHGVT-WLGTDTN 860
Cdd:cd05935 108 SAAANA--LQSAVWTGLTPsdvilACLPLFHVTGFVGSLNTAVYVGGTYVLMARWD-RETAL-ELIEKYKVTfWTNIPTM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 861 FAILYVKMNiFQKYPMPSLRKMVITGAPFTKELHEtvaKIMPHTQI--LQCYGLTDAgglcVSQAKNSKPG----SC-GF 933
Cdd:cd05935 184 LVDLLATPE-FKTRDLSSLKVLTGGGAPMPPAVAE---KLLKLTGLrfVEGYGLTET----MSQTHTNPPLrpklQClGI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 934 VTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDG---WLHTKDIGYYDENGEIFFVNRISDF 1010
Cdd:cd05935 256 P*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRM 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1011 INYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEElHDLVNknlpWYCKLQAGIK---- 1086
Cdd:cd05935 336 INVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTE-EDIIE----WAREQMAAYKypre 410
|
490
....*....|....*
gi 1820754837 1087 --FVNDFPRISTGKI 1099
Cdd:cd05935 411 veFVDELPRSASGKI 425
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
47-543 |
1.58e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 149.00 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMT 126
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 127 ARYFLSLTKPKIVFVNGESAECLAQVvkENNMDTRLVVFADSAGFVGRAATLTAVlrsqdtawidefeCAKLTSPKHVAA 206
Cdd:PRK13390 88 ADYIVGDSGARVLVASAALDGLAAKV--GADLPLRLSFGGEIDGFGSFEAALAGA-------------GPRLTEQPCGAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 207 IVCSSGTSGFPKGTE---------------ISHAAMINYMAHVKVHDLKGHVSMWTPsMRWyCGLFIVIKAILDCSKRIi 271
Cdd:PRK13390 153 MLYSSGTTGFPKGIQpdlpgrdvdapgdpiVAIARAFYDISESDIYYSSAPIYHAAP-LRW-CSMVHALGGTVVLAKRF- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 272 vpdydDDEGLCRFIEKYEVSWFRCDSCFPIRLVKFG--VLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTdVILSYG 349
Cdd:PRK13390 230 -----DAQATLGHVERYRITVTQMVPTMFVRLLKLDadVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 350 MTDYGGLCARQTK--YSKPGSCGFVCeTGRLKVVDpNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDG--WL 425
Cdd:PRK13390 304 STEAHGMTFIDSPdwLAHPGSVGRSV-LGDLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 426 HTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMA---FVAKVPGKEVTE 502
Cdd:PRK13390 382 TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAviqLVEGIRGSDELA 461
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1820754837 503 LDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK13390 462 RELIDYTRSRIAHY-KAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
623-1099 |
1.61e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 150.18 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:PRK06710 45 FLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNE---ESAENLMEAAKEENLQV-RVMVIGSLPGFVSLANILEEQ------VSRAE-------IDGFRCTKIDNP--- 762
Cdd:PRK06710 125 ILCLDlvfPRVTNVQSATKIEHVIVtRIADFLPFPKNLLYPFVQKKQsnlvvkVSESEtihlwnsVEKEVNTGVEVPcdp 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 763 -HDLAMICSSSGTTGMPKGTELSYASLY-NSITPVEEVHAKNE----ICAWVPTIRWHGGLNQCIEVIMSNAKWIIFSDD 836
Cdd:PRK06710 205 eNDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEgeevVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 837 NIKEIAlcEIIQKHGVTWLGTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYGLTDAG 916
Cdd:PRK06710 285 DMKMVF--EAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVT-GGKLVEGYGLTESS 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 917 GLCVSQAKNSK--PGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKeAFDSDGWLHTKDIGY 994
Cdd:PRK06710 362 PVTHSNFLWEKrvPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGY 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 995 YDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKN 1074
Cdd:PRK06710 441 MDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKY 520
|
490 500
....*....|....*....|....*
gi 1820754837 1075 LPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK06710 521 LAAY-KVPKVYEFRDELPKTTVGKI 544
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1206-1680 |
1.92e-37 |
|
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: 147.28 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMtarnFLTLTSPKIVFTVSS 1285
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAV-------YQPL----FTAFGPKAIEHRLRT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAAnlmeaakelkmnlKVVVMDKldgyesveenvmkghDTREIIEfkchvtnpDDVALIVPSSGTTGLPKGTEISHYSLF 1365
Cdd:cd05973 71 SGA-------------RLVVTDA---------------ANRHKLD--------SDPFVMMFTSGTTGLPKGVPVPLRALA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1366 CcLHPYKnRTLVGHT------CIVTPTmrWHYGVLMAFRL-VAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPfMII 1438
Cdd:cd05973 115 A-FGAYL-RDAVDLRpedsfwNAADPG--WAYGLYYAITGpLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSP-TAY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1439 KFIKSQLLEKYRLPT--LKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACVVS---AQNKFTKLGSVGYVSSNV 1513
Cdd:cd05973 190 RLLMAAGAEVPARPKgrLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLAnhhALEHPVHAGSAGRAMPGW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1514 RIKMVDLDTEEaLGPNKIGELRVKA----ITIMQGYHKNPETTKqafdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFR 1589
Cdd:cd05973 269 RVAVLDDDGDE-LGPGEPGRLAIDIanspLMWFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSFIGRADDVITMS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1590 SINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQ---ELISYVEKNLPDYCRLRgGVKIVDQL 1666
Cdd:cd05973 344 GYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPR-TIHFVDEL 422
|
490
....*....|....
gi 1820754837 1667 PRTTTGKIARKQLR 1680
Cdd:cd05973 423 PKTPSGKIQRFLLR 436
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
625-1099 |
2.24e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 149.92 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 625 GKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVF 704
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 705 VNE------------ESAENLMEAAKEENL--------QVRVMVIGSLPGFVSLANILE--EQVSRAEIDGfRCTKIDnP 762
Cdd:PRK12583 123 CADafktsdyhamlqELLPGLAEGQPGALAcerlpelrGVVSLAPAPPPGFLAWHELQArgETVSREALAE-RQASLD-R 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 763 HDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEVHAKNE---ICAWVPtirwhggLNQCIEVIMSN------AKWIIF 833
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEhdrLCVPVP-------LYHCFGMVLANlgcmtvGACLVY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 834 SDDNIKEIALCEIIQKHGVTWL-GTDTNFaILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGL 912
Cdd:PRK12583 274 PNEAFDPLATLQAVEEERCTALyGVPTMF-IAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 913 TDAGGL----CVSQAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLH 988
Cdd:PRK12583 353 TETSPVslqtTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMH 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 989 TKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELH 1068
Cdd:PRK12583 432 TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELR 511
|
490 500 510
....*....|....*....|....*....|.
gi 1820754837 1069 DLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK12583 512 EFCKARIAHF-KVPRYFRFVDEFPMTVTGKV 541
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
623-1100 |
3.06e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 149.42 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGIltenHLNTC----VPVLAILYIGGIICPwdhvVSKLSA----RYF 694
Cdd:PRK06178 54 FYGHVITYAELDELSDRFAALLRQRGVGAGDRVAV----FLPNCpqfhIVFFGILKLGAVHVP----VSPLFRehelSYE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 695 LSLMSPKVVFVNEESAEnLMEAAKEEnLQVRVMVigslpgFVSLANILEEQVSRAEIDGFR------------------C 756
Cdd:PRK06178 126 LNDAGAEVLLALDQLAP-VVEQVRAE-TSLRHVI------VTSLADVLPAEPTLPLPDSLRaprlaaagaidllpalraC 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 757 TK-----IDNPHDLAMICSSSGTTGMPKGTELSYASL-YN--SITPVEEVHAKNEI-CAWVPtIRWHGGLNQCIEVIMSN 827
Cdd:PRK06178 198 TApvplpPPALDALAALNYTGGTTGMPKGCEHTQRDMvYTaaAAYAVAVVGGEDSVfLSFLP-EFWIAGENFGLLFPLFS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 828 -------AKWiifsddniKEIALCEIIQKHGVT-WLGTDTNFAILyvkMNI--FQKYPMPSLRK-MVITgapFTKEL--- 893
Cdd:PRK06178 277 gatlvllARW--------DAVAFMAAVERYRVTrTVMLVDNAVEL---MDHprFAEYDLSSLRQvRVVS---FVKKLnpd 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 894 -----HETVAKIMPHTQilqcYGLTD---AGGLCVSQAKN-----SKPGSCGFVTKGIRIKIADEKTGIALGPKERGEIC 960
Cdd:PRK06178 343 yrqrwRALTGSVLAEAA----WGMTEthtCDTFTAGFQDDdfdllSQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 961 IKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVP 1040
Cdd:PRK06178 419 VRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVG 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 1041 VPHETDIELPLAFVQKVVEkevteeelHDLVNKNLPWYCKLQ-AG-----IKFVNDFPRISTGKID 1100
Cdd:PRK06178 498 RPDPDKGQVPVAFVQLKPG--------ADLTAAALQAWCRENmAVykvpeIRIVDALPMTATGKVR 555
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
66-544 |
3.62e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 148.31 E-value: 3.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 66 FAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGES 145
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 146 AECLAQVVKENnmdTRLVVFADSAGFVGR----AATLTAVLRSQD-TAWIDEFECAKLTSPKHVAAIVCSSGTSGFPKGT 220
Cdd:PRK12406 94 LHGLASALPAG---VTVLSVPTPPEIAAAyrisPALLTPPAGAIDwEGWLAQQEPYDGPPVPQPQSMIYTSGTTGHPKGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 221 -----EISHAAMINYMAhVKVHDLKghvsmwtPSMRWYC------------GLFivikAILDCSKRIIVPDYDDDEgLCR 283
Cdd:PRK12406 171 rraapTPEQAAAAEQMR-ALIYGLK-------PGIRALLtgplyhsapnayGLR----AGRLGGVLVLQPRFDPEE-LLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 284 FIEKYEVS-WFRCDSCFpIRLVKF--GVLSKYRLPTLKILLFGGAHFKGELQQTLVKLL-PhtdVILS-YGMTDYGG--L 356
Cdd:PRK12406 238 LIERHRIThMHMVPTMF-IRLLKLpeEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWgP---VIYEyYGSTESGAvtF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 357 CARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDND 436
Cdd:PRK12406 314 ATSEDALSHPGTVGKAAPGAELRFVDED-GRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLDAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 437 GEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWY 516
Cdd:PRK12406 393 GYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGY 472
|
490 500
....*....|....*....|....*...
gi 1820754837 517 cRLHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK12406 473 -KVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
58-542 |
3.63e-37 |
|
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: 146.90 E-value: 3.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 58 AVTGAET--TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTK 135
Cdd:cd05930 5 AVVDGDQslTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 136 PKIVfvngesaeclaqvvkennmdtrlvvfadsagfvgraatltavlrsqdtawidefecakLTSPKHVAAIVCSSGTSG 215
Cdd:cd05930 85 AKLV----------------------------------------------------------LTDPDDLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 216 FPKGTEISHAAMINYM-AHVKVHDLKGH--VSMWTPSmrwycgLFIV-IKAI---LDCSKRIIVPDYD---DDEGLCRFI 285
Cdd:cd05930 107 KPKGVMVEHRGLVNLLlWMQEAYPLTPGdrVLQFTSF------SFDVsVWEIfgaLLAGATLVVLPEEvrkDPEALADLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 286 EKYEV-------SWFRcdscfpiRLVKFGVLSkyRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDYGGlca 358
Cdd:cd05930 181 AEEGItvlhltpSLLR-------LLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATV--- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 359 rqtkyskpGSCGFVCETG----------------RLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRA---- 418
Cdd:cd05930 249 --------DATYYRVPPDdeedgrvpigrpipntRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpn 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 419 -LDSDGWLH-TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVP 496
Cdd:cd05930 320 pFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1820754837 497 GKEVTELDITDLVKQNMPWYCRLHAGVkFMEKLPRTATGKIAKKQL 542
Cdd:cd05930 400 GGELDEEELRAHLAERLPDYMVPSAFV-VLDALPLTPNGKVDRKAL 444
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1202-1683 |
4.73e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 147.92 E-value: 4.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVF 1281
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1282 tvssSAANLMEA-AKELKMNLKVVVM----DKLDGYeSVEENVMKGHDTREIIEFKCHVTNPDDvALIVP-------SSG 1349
Cdd:PRK12406 89 ----AHADLLHGlASALPAGVTVLSVptppEIAAAY-RISPALLTPPAGAIDWEGWLAQQEPYD-GPPVPqpqsmiyTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1350 TTGLPKGTEishYSLFCCLHPYKNRTLVGHTCIVTPTMR-------WH-----YGvLMAFRLvaanAKKLIVPDNDDAEN 1417
Cdd:PRK12406 163 TTGHPKGVR---RAAPTPEQAAAAEQMRALIYGLKPGIRalltgplYHsapnaYG-LRAGRL----GGVLVLQPRFDPEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1418 FCQLIEKYQITWFGTDPFMIIKFIK--SQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVfITNHYGMTDTACVV- 1494
Cdd:PRK12406 235 LLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGAVTf 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1495 -SAQNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGEL--RVKAITIMQgYHKNPETtKQAFDSDGWLRTGDLAYYD 1571
Cdd:PRK12406 314 aTSEDALSHPGTVGKAAPGAELRFVDEDGRP-LPQGEIGEIysRIAGNPDFT-YHNKPEK-RAEIDRGGFITSGDVGYLD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1572 DNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLP 1651
Cdd:PRK12406 391 ADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLA 470
|
490 500 510
....*....|....*....|....*....|..
gi 1820754837 1652 DYcRLRGGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK12406 471 GY-KVPKHIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1206-1680 |
5.35e-37 |
|
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: 146.17 E-value: 5.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTarnflTLTSPkivftvss 1285
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV-------VIPAT-----TLLTP-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 saanlmeaakelkmnlkvvvmdkldgyESVEENVMKGHDTREIIEfkcHVTNPDDVALIVPSSGTTGLPKGTEISHYSlf 1365
Cdd:cd05974 62 ---------------------------DDLRDRVDRGGAVYAAVD---ENTHADDPMLLYFTSGTTSKPKLVEHTHRS-- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1366 cclHPyknrtlVGHTCivtpTMRW--------HYGVLM------AFRLVAA--NAKKLIVPDND---DAENFCQLIEKYQ 1426
Cdd:cd05974 110 ---YP------VGHLS----TMYWiglkpgdvHWNISSpgwakhAWSCFFApwNAGATVFLFNYarfDAKRVLAALVRYG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1427 ITWFGTDPFMIIKFIKsQLLEKYRLPtLKVILSSGAHLRKEHLEVMReKLPDVFITNHYGMTDTACVVS-AQNKFTKLGS 1505
Cdd:cd05974 177 VTTLCAPPTVWRMLIQ-QDLASFDVK-LREVVGAGEPLNPEVIEQVR-RAWGLTIRDGYGQTETTALVGnSPGQPVKAGS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1506 VGYVSSNVRIKMVDLDTeealGPNKIGELRV-----KAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVD 1580
Cdd:cd05974 254 MGRPLPGYRVALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1581 RISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPN---KSVTEQELISYVEKNLPDYCRLR 1657
Cdd:cd05974 329 RADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGyepSPETALEIFRFSRERLAPYKRIR 408
|
490 500
....*....|....*....|...
gi 1820754837 1658 gGVKIVdQLPRTTTGKIARKQLR 1680
Cdd:cd05974 409 -RLEFA-ELPKTISGKIRRVELR 429
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
620-1099 |
6.28e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 147.36 E-value: 6.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 620 IDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMS 699
Cdd:PRK08276 4 IMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 700 PKVVFVNEESAENLMEAAKE--ENLQVRVMVIGSLPGFVSLAnileeqvsrAEIDGFRCTKIDNPHDLAMICSSSGTTGM 777
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAElpAGVPLLLVVAGPVPGFRSYE---------EALAAQPDTPIADETAGADMLYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 778 PKG-------------------------------TELSYASLYnsitpveevHAkneicawVPTiRWHGGLNQCIE--VI 824
Cdd:PRK08276 155 PKGikrplpgldpdeapgmmlallgfgmyggpdsVYLSPAPLY---------HT-------APL-RFGMSALALGGtvVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 825 MsnAKWiifsdDniKEIALcEIIQKHGVT---WLGTdtnfaiLYVKM-----NIFQKYPMPSLRKMVITGAPFTKE---- 892
Cdd:PRK08276 218 M--EKF-----D--AEEAL-ALIERYRVThsqLVPT------MFVRMlklpeEVRARYDVSSLRVAIHAAAPCPVEvkra 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 893 --------LHETvakimphtqilqcYGLTDAGGLCVSQAKN--SKPGSCGFVTKGiRIKIADEkTGIALGPKERGEIcik 962
Cdd:PRK08276 282 midwwgpiIHEY-------------YASSEGGGVTVITSEDwlAHPGSVGKAVLG-EVRILDE-DGNELPPGEIGTV--- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 963 sEFMMKG----YHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVV 1038
Cdd:PRK08276 344 -YFEMDGypfeYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 1039 VPVPHETDIELPLAFVQ---KVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK08276 423 FGVPDEEMGERVKAVVQpadGADAGDALAAELIAWLRGRLAHY-KCPRSIDFEDELPRTPTGKL 485
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
764-1100 |
6.61e-37 |
|
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: 145.90 E-value: 6.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 764 DLAMICSSSGTTGMPKGTELSYASLYNSITPVEEvhakneicAWvptiRW---------------HGGLNQCIEVIMSNA 828
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVD--------AW----RWteddvllhvlplhhvHGLVNALLCPLFAGA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 829 KWIIFSDDNIKEiALCEIIQKHGVTWLGTDTnfaiLYVK-----------MNIFQKYPMPSLRKMVITGAPFTKELHETV 897
Cdd:cd05941 158 SVEFLPKFDPKE-VAISRLMPSITVFMGVPT----IYTRllqyyeahftdPQFARAAAAERLRLMVSGSAALPVPTLEEW 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 898 AKIMPHTqILQCYGLTDAGGLCVSQAKNS-KPGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQ 976
Cdd:cd05941 233 EAITGHT-LLERYGMTEIGMALSNPLDGErRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 977 TKEAFDSDGWLHTKDIGYYDENGEIFFVNRIS-DFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQ 1055
Cdd:cd05941 312 TKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVV 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1820754837 1056 K-VVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd05941 392 LrAGAAALSLEELKEWAKQRLAPY-KRPRRLILVDELPRNAMGKVN 436
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1177-1684 |
6.87e-37 |
|
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: 149.18 E-value: 6.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1177 VNIAEETL----KFLKSKPDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYI 1252
Cdd:cd05968 60 MNIVEQLLdkwlADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1253 GAISNTWDHELTPMTARNFLTLTSPKIVFTVSSSA---------ANLMEAAKELKMNLKVVVMDKLD--------GYESV 1315
Cdd:cd05968 140 GGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTrrgrevnlkEEADKACAQCPTVEKVVVVRHLGndftpakgRDLSY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1316 EEnVMKGHDTReiiefkCHVTNPDDVALIVPSSGTTGLPKGTEISHyslfcCLHPYKNRTLVGHTCIVTP--------TM 1387
Cdd:cd05968 220 DE-EKETAGDG------AERTESEDPLMIIYTSGTTGKPKGTVHVH-----AGFPLKAAQDMYFQFDLKPgdlltwftDL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1388 RWHYGVLMAFRLVAANAKKLI---VPDNDDAENFCQLIEKYQITWFGTDPFMIIKFI--KSQLLEKYRLPTLKVILSSGA 1462
Cdd:cd05968 288 GWMMGPWLIFGGLILGATMVLydgAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1463 HLRKE-----HLEVMREKLPdvfITNHYGMTDTACVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVK 1537
Cdd:cd05968 368 PWNPEpwnwlFETVGKGRNP---IINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1538 A--ITIMQGYHKNP----ETTKQAFDsDGWLRtGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQA 1611
Cdd:cd05968 445 ApwPGMTRGFWRDEdrylETYWSRFD-NVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLES 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1612 AVLGIPNEVDEQHPKAFVVQVPNKSVTE---QELISYVEKNL-----PDycrlrgGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:cd05968 523 AAIGVPHPVKGEAIVCFVVLKPGVTPTEalaEELMERVADELgkplsPE------RILFVKDLPKTRNAKVMRRVIRAAY 596
|
.
gi 1820754837 1684 V 1684
Cdd:cd05968 597 L 597
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
29-543 |
9.80e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 147.05 E-value: 9.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 29 APILKKCTNVGALVLEKLRSRPEFIAQVEavTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAA 108
Cdd:PRK06188 5 ADLLHSGATYGHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 109 LYLGAISNPwdneLSPMTA----RYFLsltkpkivfvngESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRS 184
Cdd:PRK06188 83 QLAGLRRTA----LHPLGSlddhAYVL------------EDAGISTLIVDPAPFVERALALLARVPSLKHVLTLGPVPDG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 185 QD-TAWIDEFECAKLTS---PKHVAAIVCSSGTSGFPKGTEISHAAMINyMAHVKVHDLKghvsmWTPSMRWYC------ 254
Cdd:PRK06188 147 VDlLAAAAKFGPAPLVAaalPPDIAGLAYTGGTTGKPKGVMGTHRSIAT-MAQIQLAEWE-----WPADPRFLMctplsh 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 255 --GLFIViKAILDCSKRIIVPDYDDDEgLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFK-GEL 331
Cdd:PRK06188 221 agGAFFL-PTLLRGGTVIVLAKFDPAE-VLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSpVRL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 332 QQTLVKLLPhtdvILS--YGMTDYGG----LCARQTKYSKP---GSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSS 402
Cdd:PRK06188 299 AEAIERFGP----IFAqyYGQTEAPMvityLRKRDHDPDDPkrlTSCGRPTPGLRVALLDED-GREVAQGEVGEICVRGP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 403 YMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHN 482
Cdd:PRK06188 374 LVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDE 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 483 INEEHAMAFVAKVPGKEVTELDITDLVKQnmpWYCRLHA--GVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK06188 453 KWGEAVTAVVVLRPGAAVDAAELQAHVKE---RKGSVHApkQVDFVDSLPLTALGKPDKKALR 512
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
629-1100 |
1.04e-36 |
|
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: 146.74 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNEE 708
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAENLMEAAKEENLQVRVMVI----GSLPGFVSLANILeeqvsRAEIDGFRCTKIdNPHDLAMICSSSGTTGMPKGTels 784
Cdd:cd05959 111 LAPVLAAALTKSEHTLVVLIVsggaGPEAGALLLAELV-----AAEAEQLKPAAT-HADDPAFWLYSSGSTGRPKGV--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 785 yASLYNSITPVEEVHAKN-------EICAWVPTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEIALCEIIQKHGVTWL-G 856
Cdd:cd05959 182 -VHLHADIYWTAELYARNvlgiredDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAVFKRIRRYRPTVFfG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 857 TDTNFAILYVKMNIfQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTqILQCYGLTDAGGLCVSQ-AKNSKPGSCGFVT 935
Cdd:cd05959 261 VPTLYAAMLAAPNL-PSRDLSSLRLCVSAGEALPAEVGERWKARFGLD-ILDGIGSTEMLHIFLSNrPGRVRYGTTGKPV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 936 KGIRIKIADEkTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSdGWLHTKDIGYYDENGEIFFVNRISDFINYKA 1015
Cdd:cd05959 339 PGYEVELRDE-DGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLKVSG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1016 IKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV---QKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFP 1092
Cdd:cd05959 417 IWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVvlrPGYEDSEALEEELKEFVKDRLAPY-KYPRWIVFVDELP 495
|
....*...
gi 1820754837 1093 RISTGKID 1100
Cdd:cd05959 496 KTATGKIQ 503
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1203-1664 |
1.50e-36 |
|
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: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1203 KVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISntwdheltpmtarnfltltspkivfT 1282
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVD-------------------------V 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1283 VSSSAANLMEAAKELKMNLKVVVmdkldgyesVEENvmkghdtreiiefkchvtNPDDVALIVPSSGTTGLPKGTEISHY 1362
Cdd:cd17640 59 VRGSDSSVEELLYILNHSESVAL---------VVEN------------------DSDDLATIIYTSGTTGNPKGVMLTHA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1363 SLfccLHPYKNRTLVGHTCIVTPTMR----WH-YGVLMAFRLVAANAKKL---IVPDNDDaenfcqlIEKYQITWFGTDP 1434
Cdd:cd17640 112 NL---LHQIRSLSDIVPPQPGDRFLSilpiWHsYERSAEYFIFACGCSQAytsIRTLKDD-------LKRVKPHYIVSVP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1435 FM-------IIK------FIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACVVSAQN-KF 1500
Cdd:cd17640 182 RLweslysgIQKqvskssPIKQFLFLFFLSGGIFKFGISGGGALPPHVDTFFEAI-GIEVLNGYGLTETSPVVSARRlKC 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1501 TKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVD 1580
Cdd:cd17640 261 NVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1581 RISDFINFRS-INVSPAEIETVLMTHPAVLQAAVLGipnevdeQHPKAF-VVQVPNKSVTEQELISYVEKNLPDYCRLRG 1658
Cdd:cd17640 341 RAKDTIVLSNgENVEPQPIEEALMRSPFIEQIMVVG-------QDQKRLgALIVPNFEELEKWAKESGVKLANDRSQLLA 413
|
....*.
gi 1820754837 1659 GVKIVD 1664
Cdd:cd17640 414 SKKVLK 419
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1338-1680 |
1.73e-36 |
|
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: 142.62 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1338 PDDVALIVPSSGTTGLPKGTEISH----YSLFCCLHpykNRTLVGHTCIVTPTMRWH-YGVLMAFRLVAANAKKLIVP-- 1410
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHsnevYNAWMLAL---NSLFDPDDVLLCGLPLFHvNGSVVTLLTPLASGAHVVLAgp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1411 ----DNDDAENFCQLIEKYQITWFGTDPFMIIKFIksQLLEKYRLPTLKVILSSGAHLRkehLEVMR--EKLPDVFITNH 1484
Cdd:cd05944 78 agyrNPGLFDNFWKLVERYRITSLSTVPTVYAALL--QVPVNADISSLRFAMSGAAPLP---VELRArfEDATGLPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVVSAQ--NKFTKLGSVGYVSSNVRIKMVDLDTEEAL----GPNKIGELRVKAITIMQGYhKNPETTKQAFDS 1558
Cdd:cd05944 153 YGLTEATCLVAVNppDGPKRPGSVGLRLPYARVRIKVLDGVGRLlrdcAPDEVGEICVAGPGVFGGY-LYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1559 DGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVT 1638
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1820754837 1639 EQELISYVEKNLPDYCRLRGGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:cd05944 312 EEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1202-1680 |
2.20e-36 |
|
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: 144.42 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVF 1281
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1282 TvsssaanlmeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchvtnpdDVALIVPSSGTTGLPKGTEISH 1361
Cdd:cd05940 81 V---------------------------------------------------------DAALYIYTSGTTGLPKAAIISH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1362 YSLfcclhpYKNRTLVGHTCIVTPTMR-------WH-YGVLMAFRLVAANAKKLIVPDNDDAENFCQLIEKYQITWFGtd 1433
Cdd:cd05940 104 RRA------WRGGAFFAGSGGALPSDVlytclplYHsTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQ-- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1434 pfmIIKFIKSQLLEKYRLPT-----LKVILSSGahLRKEHLEVMREKLPDVFITNHYGMTDtaCVVSAQNKFTKLGSVGY 1508
Cdd:cd05940 176 ---YIGELCRYLLNQPPKPTerkhkVRMIFGNG--LRPDIWEEFKERFGVPRIAEFYAATE--GNSGFINFFGKPGAIGR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1509 VSSNVRIKM------VDLDTEEAL----------GPNKIGEL--RVKAITIMQGYHKNPETTKQ----AF-DSDGWLRTG 1565
Cdd:cd05940 249 NPSLLRKVAplalvkYDLESGEPIrdaegrcikvPRGEPGLLisRINPLEPFDGYTDPAATEKKilrdVFkKGDAWFNTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1566 DLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLG--IPNeVDEQHPKAFVVQVPNKSVTEQELI 1643
Cdd:cd05940 329 DLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGvqVPG-TDGRAGMAAIVLQPNEEFDLSALA 407
|
490 500 510
....*....|....*....|....*....|....*..
gi 1820754837 1644 SYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:cd05940 408 AHLEKNLPGYARPL-FLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1202-1681 |
2.33e-36 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 146.44 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKiVF 1281
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGAR-LL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1282 TVSSSAANLMEAAKELKMNLKVVVMdkLDGyeSVEENVMKGHDTREIIEFKCHVT----NPDDVALIVPSSGTTGLPKGT 1357
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWL--LDA--PASVSVPAGWSTAPLPPLDAPAPaaavQPGDTAAILYTSGTTGPSKGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1358 eishyslfCCLHP-------YKNRTL------VGHTCIvtPTmrWHYGVLMAFRLVAANAKKLIVPDNDDAENFCQLIEK 1424
Cdd:PRK06155 199 --------CCPHAqfywwgrNSAEDLeigaddVLYTTL--PL--FHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1425 YQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSG--AHLrkehLEVMREKLpDVFITNHYGMTDTACVVSAQNKFTK 1502
Cdd:PRK06155 267 HGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGvpAAL----HAAFRERF-GVDLLDGYGSTETNFVIAVTHGSQR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1503 LGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKA---ITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIV 1579
Cdd:PRK06155 342 PGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1580 DRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRgG 1659
Cdd:PRK06155 420 DRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPR-Y 498
|
490 500
....*....|....*....|..
gi 1820754837 1660 VKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLRE 520
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
47-543 |
2.37e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 145.33 E-value: 2.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMT 126
Cdd:PRK09088 6 RLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 127 ARYFLSLTKPKIVFVNGESAECLAQVVkennmdtrlvvfaDSAGFVGRAATLTAVlrsqDTAWIDefecakltsPKHVAA 206
Cdd:PRK09088 86 LDALLQDAEPRLLLGDDAVAAGRTDVE-------------DLAAFIASADALEPA----DTPSIP---------PERVSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 207 IVCSSGTSGFPKGTEISH----AAMINYMAHVKVhdlkGHVSMW---TPsMRWYCGLFIVIKAILDCSKRIIVPD-YDDD 278
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSErnlqQTAHNFGVLGRV----DAHSSFlcdAP-MFHIIGLITSVRPVLAVGGSILVSNgFEPK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 279 EGLCRFIE-KYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGA-HFKGELQQTLVKLLPHTDvilSYGMTDYG-- 354
Cdd:PRK09088 215 RTLGRLGDpALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGApHAAEDILGWLDDGIPMVD---GFGMSEAGtv 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 355 -GLCARQTKY-SKPGSCGFVCETGRLKVVDpNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGY 432
Cdd:PRK09088 292 fGMSVDCDVIrAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIAR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 433 YDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQN 512
Cdd:PRK09088 371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTR 450
|
490 500 510
....*....|....*....|....*....|.
gi 1820754837 513 MPWYcRLHAGVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK09088 451 LAKY-KVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1202-1679 |
2.57e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 146.72 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGL----CSDNNLDVFLIL-LGTMY--IGAISNTWD--HELTPMTARNFL 1272
Cdd:PRK06178 56 GHVITYAELDELSDRFAALLRQRGVGAGDRVAVflpnCPQFHIVFFGILkLGAVHvpVSPLFREHElsYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1273 TL-------------TSPKIVFTVSSSAANLMEAAKELKMNL---KVVVMDKLDGYESVEEnvmkghdtrEIIEFKCHVT 1336
Cdd:PRK06178 136 ALdqlapvveqvraeTSLRHVIVTSLADVLPAEPTLPLPDSLrapRLAAAGAIDLLPALRA---------CTAPVPLPPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1337 NPDDVALIVPSSGTTGLPKGteishyslfcCLHpyKNRTLVG---HTCIVTPTMRWHYGVLMAFRL--VAANAKKLIVP- 1410
Cdd:PRK06178 207 ALDALAALNYTGGTTGMPKG----------CEH--TQRDMVYtaaAAYAVAVVGGEDSVFLSFLPEfwIAGENFGLLFPl 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1411 ---------DNDDAENFCQLIEKYQITwfgtDPFMIIKFIkSQLLE-----KYRLPTLKVILSSgAHLRKEHLEVM---R 1473
Cdd:PRK06178 275 fsgatlvllARWDAVAFMAAVERYRVT----RTVMLVDNA-VELMDhprfaEYDLSSLRQVRVV-SFVKKLNPDYRqrwR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1474 EKLPDVFITNHYGMTDT-ACvvsaqNKFTK--------LGS----VGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAIT 1540
Cdd:PRK06178 349 ALTGSVLAEAAWGMTEThTC-----DTFTAgfqdddfdLLSqpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1541 IMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEV 1620
Cdd:PRK06178 424 LLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPD 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 1621 DEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRggVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK06178 503 KGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE--IRIVDALPMTATGKVRKQDL 559
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1340-1681 |
2.74e-36 |
|
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: 140.93 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1340 DVALIVPSSGTTGLPKGTEISHYSL-------------------FCCLHPYknrtLVGhtcivtptmrwhyGVLMAFRLV 1400
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLlasaaglhsrlgfgggdswLLSLPLY----HVG-------------GLAILVRSL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1401 AANAKkLIVPDNDDAenFCQLIEKYQITWFGTDPFMIIKFIKSqLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVF 1480
Cdd:cd17630 64 LAGAE-LVLLERNQA--LAEDLAPPGVTHVSLVPTQLQRLLDS-GQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1481 ITnhYGMTDTACVVSAQN-KFTKLGSVGYVSSNVRIKMVDldteealgpnkIGELRVKAITIMQGYHKNPETtkQAFDSD 1559
Cdd:cd17630 140 TT--YGMTETASQVATKRpDGFGRGGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLRGQLV--PEFNED 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1560 GWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVvqVPNKSVTE 1639
Cdd:cd17630 205 GWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI--VGRGPADP 282
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1820754837 1640 QELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd17630 283 AELRAWLKDKLARFKLPK-RIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
623-1099 |
3.95e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 144.72 E-value: 3.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:PRK03640 23 FEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNEEsaenlMEAAKEENLQVRVMVIGSLPgfvslaniLEEQVSRAEIDgfrctkIDnphDLAMICSSSGTTGMPKGTE 782
Cdd:PRK03640 103 LITDDD-----FEAKLIPGISVKFAELMNGP--------KEEAEIQEEFD------LD---EVATIMYTSGTTGKPKGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 783 LSYAS-LYNSITPVEE--VHAKNEICAWVPTirWH-GGLNqcieVIMSNakwII----------FSDDNIKEIalceiIQ 848
Cdd:PRK03640 161 QTYGNhWWSAVGSALNlgLTEDDCWLAAVPI--FHiSGLS----ILMRS---VIygmrvvlvekFDAEKINKL-----LQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 849 KHGVTwlgtdtnfaILYVKMNIFQK---------YPmPSLRKMVITGAPFTKELHET-VAKIMPhtqILQCYGLTD-AGG 917
Cdd:PRK03640 227 TGGVT---------IISVVSTMLQRllerlgegtYP-SSFRCMLLGGGPAPKPLLEQcKEKGIP---VYQSYGMTEtASQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 918 LCVSQAKNS--KPGSCGFVTKGIRIKIADEktGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDsDGWLHTKDIGYY 995
Cdd:PRK03640 294 IVTLSPEDAltKLGSAGKPLFPCELKIEKD--GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 996 DENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVqkVVEKEVTEEELHDLVNKNL 1075
Cdd:PRK03640 371 DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFV--VKSGEVTEEELRHFCEEKL 448
|
490 500
....*....|....*....|....
gi 1820754837 1076 PWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK03640 449 AKY-KVPKRFYFVEELPRNASGKL 471
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1206-1613 |
6.53e-36 |
|
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: 142.02 E-value: 6.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPM-----TAR-NF-LTLTSP 1277
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAA-------YVPLdpaypAERlAFiLEDAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1278 KIVFTVSSSAANLMEaakelkMNLKVVVMDKLDGYESVEENVMKGHDTReiiefkchvTNPDDVALIVPSSGTTGLPKGT 1357
Cdd:TIGR01733 74 RLLLTDSALASRLAG------LVLPVILLDPLELAALDDAPAPPPPDAP---------SGPDDLAYVIYTSGSTGRPKGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1358 EISHYSLfcclhpyknrtlvghtCIVTPTMRWHYG------VLMA------------FRLVAANAKKLIVPDN---DDAE 1416
Cdd:TIGR01733 139 VVTHRSL----------------VNLLAWLARRYGldpddrVLQFaslsfdasveeiFGALLAGATLVVPPEDeerDDAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1417 NFCQLIEKYQITWFGTDPFMIikfikSQLLE--KYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVV 1494
Cdd:TIGR01733 203 LLAALIAEHPVTVLNLTPSLL-----ALLAAalPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1495 SAQ------NKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAF------DSDG-- 1560
Cdd:TIGR01733 278 TATlvdpddAPRESPVPIGRPLANTRLYVLDDDLRP-VPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaGGDGar 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1561 WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAV 1613
Cdd:TIGR01733 357 LYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
46-547 |
8.89e-36 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 144.81 E-value: 8.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 46 LRSRPEFIAQVEAV--TGAETTF--AEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPW--- 118
Cdd:PRK13295 34 VASCPDKTAVTAVRlgTGAPRRFtyRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLmpi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 119 --DNELSPMtaryfLSLTKPKIVFV----NGESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTavlrsqDTAWIDE 192
Cdd:PRK13295 114 frERELSFM-----LKHAESKVLVVpktfRGFDHAAMARRLRPELPALRHVVVVGGDGADSFEALLI------TPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 193 FECAKL-----TSPKHVAAIVCSSGTSGFPKGTEISH-AAMINYMAHVKVHDLK-GHVSMWTPSMRWYCGLFIVIKAILD 265
Cdd:PRK13295 183 PDAPAIlarlrPGPDDVTQLIYTSGTTGEPKGVMHTAnTLMANIVPYAERLGLGaDDVILMASPMAHQTGFMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 266 CSKRIIVPDYDDDEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLpHTDVI 345
Cdd:PRK13295 263 LGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAAL-GAKIV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 346 LSYGMTDYGglCARQTKYSKP-----GSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRraLD 420
Cdd:PRK13295 342 SAWGMTENG--AVTLTKLDDPderasTTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--TD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 421 SDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEV 500
Cdd:PRK13295 417 ADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSL 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 501 TELDITD------LVKQNMPWycRLhagvKFMEKLPRTATGKIAKKQLKQIAK 547
Cdd:PRK13295 497 DFEEMVEflkaqkVAKQYIPE--RL----VVRDALPRTPSGKIQKFRLREMLR 543
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
640-1100 |
9.76e-36 |
|
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: 142.96 E-value: 9.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 640 CALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIIC----PWDHVVSKLSARYFLSLMSPKVVFVnEESAENLME 715
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGlvfvPLNPTLKESVLRYLVADAGGRIVLA-DAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 716 AAkeenlqvrvMVIGSLPGFVSLANILEEqvSRAEIDGFRCTkidnPHDLAMICSSSGTTGMPKGTELSYASLY---NSI 792
Cdd:cd05922 85 DA---------LPASPDPGTVLDADGIRA--ARASAPAHEVS----HEDLALLLYTSGSTGSPKLVRLSHQNLLanaRSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 793 TPVEEVHAKNEICAWVPtIRWHGGLNQCIEVIMSNAKWIIfSDDNIKEIALCEIIQKHGVTWL-GTDTNFAILyVKMnIF 871
Cdd:cd05922 150 AEYLGITADDRALTVLP-LSYDYGLSVLNTHLLRGATLVL-TNDGVLDDAFWEDLREHGATGLaGVPSTYAML-TRL-GF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 872 QKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAGG----LCVSQAKNsKPGSCGFVTKGIRIKIADEKt 947
Cdd:cd05922 226 DPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRrmtyLPPERILE-KPGSIGLAIPGGEFEILDDD- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 948 GIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVL 1027
Cdd:cd05922 304 GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAA 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1028 ELHPSILKAVVVPVPHETDIELPLAFVqkvVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd05922 384 RSIGLIIEAAAVGLPDPLGEKLALFVT---APDKIDPKDVLRSLAERLPPY-KVPATVRVVDELPLTASGKVD 452
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1206-1679 |
1.14e-35 |
|
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: 143.24 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHEltpmtarnfltltSPK--IVFTV 1283
Cdd:cd17655 24 TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD-------------YPEerIQYIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1284 SSSAANLMEAAKELKMNLK----VVVMDKLDGYESVEENVMkghdtreiiefkcHVTNPDDVALIVPSSGTTGLPKGTEI 1359
Cdd:cd17655 91 EDSGADILLTQSHLQPPIAfiglIDLLDEDTIYHEESENLE-------------PVSKSDDLAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1360 SHYSLFCCLHPYKNRTLVGHTCIVTPTMRWHY--GVLMAFRLVAANAKKLIVPDND--DAENFCQLIEKYQITwfgtdpf 1435
Cdd:cd17655 158 EHRGVVNLVEWANKVIYQGEHLRVALFASISFdaSVTEIFASLLSGNTLYIVRKETvlDGQALTQYIRQNRIT------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1436 mIIKFIKS--QLLEKYRL---PTLKVILSSGAHLRKEHLEVMREKLPD-VFITNHYGMTDTaCV------VSAQNKFTKL 1503
Cdd:cd17655 231 -IIDLTPAhlKLLDAADDsegLSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTET-TVdasiyqYEPETDQQVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1504 GSVGYVSSNVRIKMvdLDTEEALGPNKI-GELRVKAITIMQGYHKNPETTKQAFDSDGWL------RTGDLAYYDDNGEI 1576
Cdd:cd17655 309 VPIGKPLGNTRIYI--LDQYGRPQPVGVaGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1577 YIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQvpNKSVTEQELISYVEKNLPDY--- 1653
Cdd:cd17655 387 EFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVS--EKELPVAQLREFLARELPDYmip 464
|
490 500
....*....|....*....|....*..
gi 1820754837 1654 -CRLRggvkiVDQLPRTTTGKIARKQL 1679
Cdd:cd17655 465 sYFIK-----LDEIPLTPNGKVDRKAL 486
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
629-1099 |
1.17e-35 |
|
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: 141.33 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIIcpwdhvvsklsaryflslmspkvVFVNEE 708
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEA-----------------------VLLNTR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAENlmeaakeenlqvrvmvigslpgfvSLANILEEqvSRAEIDgfrctkidnphDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd05912 60 LTPN------------------------ELAFQLKD--SDVKLD-----------DIATIMYTSGTTGKPKGVQQTFGNH 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 YNSITPVEE---VHAKNEICAWVPTirWH-GGLNqcieVIMSNAKW--IIFSDDNIKEIALCEIIQKHGVTWLGTDTnfA 862
Cdd:cd05912 103 WWSAIGSALnlgLTEDDNWLCALPL--FHiSGLS----ILMRSVIYgmTVYLVDKFDAEQVLHLINSGKVTIISVVP--T 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 863 ILYVKMNIF-QKYPmPSLRKMVITGAPFTKELHET-VAKIMPhtqILQCYGLTDAgglcVSQAKN-------SKPGSCGF 933
Cdd:cd05912 175 MLQRLLEILgEGYP-NNLRCILLGGGPAPKPLLEQcKEKGIP---VYQSYGMTET----CSQIVTlspedalNKIGSAGK 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 934 VTKGIRIKIADEKTGialgPKERGEICIKSEFMMKGYHKNPEQTKEAFDsDGWLHTKDIGYYDENGEIFFVNRISDFINY 1013
Cdd:cd05912 247 PLFPVELKIEDDGQP----PYEVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLIIS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1014 KAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVqkVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPR 1093
Cdd:cd05912 322 GGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFV--VSERPISEEELIAYCSEKLAKY-KVPKKIYFVDELPR 398
|
....*.
gi 1820754837 1094 ISTGKI 1099
Cdd:cd05912 399 TASGKL 404
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
65-544 |
1.18e-35 |
|
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: 144.18 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 saeclaqvvkennmDTRLVVFADSAGFVGRAATLTAVLRSQDTAWID-EFECAKLT---SPKHVAAIVC---------SS 211
Cdd:cd05970 129 --------------DNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDfRKLIKNASpdfERPTANSYPCgedillvyfSS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 212 GTSGFPKGTE------ISHAAMINYMAHVKVHDLkgHVSM----WTPSM------RWYCGlfivikaildCSkrIIVPDY 275
Cdd:cd05970 195 GTTGMPKMVEhdftypLGHIVTAKYWQNVREGGL--HLTVadtgWGKAVwgkiygQWIAG----------AA--VFVYDY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 276 D--DDEGLCRFIEKYEVSWFrcdsCFPIRLVKFGV---LSKYRLPTLKILLFGG-----AHFKGELQQTLVKLLPhtdvi 345
Cdd:cd05970 261 DkfDPKALLEKLSKYGVTTF----CAPPTIYRFLIredLSRYDLSSLRYCTTAGealnpEVFNTFKEKTGIKLME----- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 346 lSYGMTDygglCARQTKY-----SKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSY-----MMNGYYNNPEAT 415
Cdd:cd05970 332 -GFGQTE----TTLTIATfpwmePKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 416 RRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFV--A 493
Cdd:cd05970 406 AEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIvlA 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 494 K--VPGKEVTElDITDLVKQNM-PW-YCRLhagVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:cd05970 485 KgyEPSEELKK-ELQDHVKKVTaPYkYPRI---VEFVDELPKTISGKIRRVEIRE 535
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
626-1099 |
2.19e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 142.69 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 626 KECTYAEMRERSIKCALWLRKH-GIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVF 704
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 705 VNEESAENLMEAAKEENLQvRVMVIGSLPGfvslanileeqVSRAEIDGFRCTKIDNPHdlaMICSSSGTTGMPKGTELS 784
Cdd:PRK06839 106 VEKTFQNMALSMQKVSYVQ-RVISITSLKE-----------IEDRKIDNFVEKNESASF---IICYTSGTTGKPKGAVLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 785 YASLY-NSITPVEEVHAKNEICAWVPTIRWH-GGLNQCIEVIMSNAKWIIFSD--DNIKEIALceiIQKHGVTW-LGTDT 859
Cdd:PRK06839 171 QENMFwNALNNTFAIDLTMHDRSIVLLPLFHiGGIGLFAFPTLFAGGVIIVPRkfEPTKALSM---IEKHKVTVvMGVPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 860 NFAILyVKMNIFQKYPMPSLRKMVITGAPFTKELhetvakiMPHTQ-----ILQCYGLTDAGGLCVSQAKNS---KPGSC 931
Cdd:PRK06839 248 IHQAL-INCSKFETTNLQSVRWFYNGGAPCPEEL-------MREFIdrgflFGQGFGMTETSPTVFMLSEEDarrKVGSI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 932 GFVTKGIRIKIADEKTGiALGPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFI 1011
Cdd:PRK06839 320 GKPVLFCDYELIDENKN-KVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1012 NYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDF 1091
Cdd:PRK06839 398 ISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKY-KIPKEIVFLKEL 476
|
....*...
gi 1820754837 1092 PRISTGKI 1099
Cdd:PRK06839 477 PKNATGKI 484
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1205-1685 |
2.23e-35 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 143.19 E-value: 2.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1205 QTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAI---------SNTWDHELTpmTARNFL-TL 1274
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVpapltvpptYDEPNARLR--KLRHIWqLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1275 TSPKIVfTVSSSAANLMEAAKE--LKMNLKVVVMDKLDGYESVEenvmkGHDTReiiefkchvtnPDDVALIVPSSGTTG 1352
Cdd:cd05906 118 GSPVVL-TDAELVAEFAGLETLsgLPGIRVLSIEELLDTAADHD-----LPQSR-----------PDDLALLMLTSGSTG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1353 LPKGTEISHYSLF------CCLHPYKNRTlvghtcivtPTMRW----HYGVLMAFRL--VAANAKKLIVPDND---DAEN 1417
Cdd:cd05906 181 FPKAVPLTHRNILarsagkIQHNGLTPQD---------VFLNWvpldHVGGLVELHLraVYLGCQQVHVPTEEilaDPLR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1418 FCQLIEKYQI--TWfgtDP-FMIIKFikSQLLEK-----YRLPTLKVILSSG-AHLRKEHLEVMRE----KLPDVFITNH 1484
Cdd:cd05906 252 WLDLIDRYRVtiTW---APnFAFALL--NDLLEEiedgtWDLSSLRYLVNAGeAVVAKTIRRLLRLlepyGLPPDAIRPA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVV-----------SAQNKFTKLGSV--GyvssnVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPET 1551
Cdd:cd05906 327 FGMTETCSGViysrsfptydhSQALEFVSLGRPipG-----VSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1552 TKQAFDSDGWLRTGDLAYYdDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLgipnevdeqhpkAFVVQ 1631
Cdd:cd05906 401 NAEAFTEDGWFRTGDLGFL-DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTA------------AFAVR 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1632 VPNkSVTEQELISYV-EKNLPD-----------YCRLRGGVKIV-------DQLPRTTTGKIARKQLRDMYVN 1685
Cdd:cd05906 468 DPG-AETEELAIFFVpEYDLQDalsetlrairsVVSREVGVSPAyliplpkEEIPKTSLGKIQRSKLKAAFEA 539
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1206-1680 |
2.86e-35 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 143.50 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTA-------RNFLTLTSPK 1278
Cdd:PRK04319 75 TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAI-------VGPLFEafmeeavRDRLEDSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1279 IVFTVSSSAANLMeaAKELKmNLKVVVM-----DKLDGYESVEEnVMKGHDTreiiEFKCHVTNPDDVALIVPSSGTTGL 1353
Cdd:PRK04319 148 VLITTPALLERKP--ADDLP-SLKHVLLvgedvEEGPGTLDFNA-LMEQASD----EFDIEWTDREDGAILHYTSGSTGK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1354 PKGT------EISHYS---LFCCLHP---YknrtlvghTCI-----VTPTmrwHYGVLMAFRLVAANakkLIVPDNDDAE 1416
Cdd:PRK04319 220 PKGVlhvhnaMLQHYQtgkYVLDLHEddvY--------WCTadpgwVTGT---SYGIFAPWLNGATN---VIDGGRFSPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1417 NFCQLIEKYQIT-WFgTDPFMIIKFIK--SQLLEKYRLPTLKVILSSGahlrkEHL--EVMREKLpDVF---ITNHYGMT 1488
Cdd:PRK04319 286 RWYRILEDYKVTvWY-TAPTAIRMLMGagDDLVKKYDLSSLRHILSVG-----EPLnpEVVRWGM-KVFglpIHDNWWMT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1489 DTACVVSAqNKFT---KLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKA--ITIMQGYHKNPETTKQAFdSDGWLR 1563
Cdd:PRK04319 359 ETGGIMIA-NYPAmdiKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1564 TGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQ--- 1640
Cdd:PRK04319 436 SGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElke 515
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1820754837 1641 ELISYVEKnlpdycRLRGGV-----KIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK04319 516 EIRGFVKK------GLGAHAapreiEFKDKLPKTRSGKIMRRVLK 554
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
63-543 |
4.14e-35 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 142.13 E-value: 4.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVN 142
Cdd:PRK08008 37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 143 GESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDTAWIDEfecAKLTSPKHVAAIVCSSGTSGFPKGTEI 222
Cdd:PRK08008 117 AQFYPMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPATLCY---APPLSTDDTAEILFTSGTTSRPKGVVI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 223 SHAAMInymahvkvhdLKGHVSMWTPSMRWYCGLFIVIKAI-LDCSKRIIVPDYDDDEGLCrFIEKYEVSWF---RCD-- 296
Cdd:PRK08008 194 THYNLR----------FAGYYSAWQCALRDDDVYLTVMPAFhIDCQCTAAMAAFSAGATFV-LLEKYSARAFwgqVCKyr 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 297 ----SCFP--IR-LVKFGVLSKYRLPTLKILLFGgAHFKGELQQTL-----VKLLPhtdvilSYGMTD-YGGLC----AR 359
Cdd:PRK08008 263 atitECIPmmIRtLMVQPPSANDRQHCLREVMFY-LNLSDQEKDAFeerfgVRLLT------SYGMTEtIVGIIgdrpGD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 360 QTKYSKPGSCGFVCETgrlKVVDPNtGKVLGANKTGEIWAKS---SYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDND 436
Cdd:PRK08008 336 KRRWPSIGRPGFCYEA---EIRDDH-NRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 437 GEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNM--- 513
Cdd:PRK08008 412 GFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMakf 491
|
490 500 510
....*....|....*....|....*....|..
gi 1820754837 514 --PWYcrlhagVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK08008 492 kvPSY------LEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
47-543 |
4.67e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 141.75 E-value: 4.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMT 126
Cdd:PRK13391 8 QTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 127 ARYFLSLTKPKIVFVNGESAECLAQVVKEN-NMDTRLVV--FADSAGFVGRAatlTAVLRSQDTAWIDEFECAkltspkh 203
Cdd:PRK13391 88 AAYIVDDSGARALITSAAKLDVARALLKQCpGVRHRLVLdgDGELEGFVGYA---EAVAGLPATPIADESLGT------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 204 vaAIVCSSGTSGFPKGT-------EISHAAMINYMAHvkvhdlkghvSMW--TPSMRW-------------YCGLFIVIK 261
Cdd:PRK13391 158 --DMLYSSGTTGRPKGIkrplpeqPPDTPLPLTAFLQ----------RLWgfRSDMVYlspaplyhsapqrAVMLVIRLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 262 AIldcskrIIVPDYDDDEGLCRFIEKYEVSWFRCDSCFPIRLVKF--GVLSKYRLPTLKILLFGGAHFKGELQQTLVKLL 339
Cdd:PRK13391 226 GT------VIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLpeEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWW 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 340 -PhtdVILS-YGMTDYGGLCARQTK--YSKPGSCGFVCeTGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNgYYNNPEAT 415
Cdd:PRK13391 300 gP---IIHEyYAATEGLGFTACDSEewLAHPGTVGRAM-FGDLHILDDD-GAELPPGEPGTIWFEGGRPFE-YLNDPAKT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 416 RRALDSDG-WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAK 494
Cdd:PRK13391 374 AEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQP 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 495 VPGkevteLDITDLVKQNMPWYCRLH-AGVK------FMEKLPRTATGKIAKKQLK 543
Cdd:PRK13391 454 VDG-----VDPGPALAAELIAFCRQRlSRQKcprsidFEDELPRLPTGKLYKRLLR 504
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1335-1680 |
5.00e-35 |
|
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: 140.31 E-value: 5.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1335 VTNPDDVALIVPSSGTTGLPKGTEISHYSLFCC--------LHPYKNRTLVGhtcivTPTMRWHYGV-LMAFRLVAANAK 1405
Cdd:cd05958 93 LTASDDICILAFTSGTTGAPKATMHFHRDPLASadryavnvLRLREDDRFVG-----SPPLAFTFGLgGVLLFPFGVGAS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1406 KLIVPDNDdAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEhlevMREKLPDVF---IT 1482
Cdd:cd05958 168 GVLLEEAT-PDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAA----LHRAWKEATgipII 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1483 NHYGMTDTACV-VSAQNKFTKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITimqGYHKNPETTKQAFDSDGW 1561
Cdd:cd05958 243 DGIGSTEMFHIfISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGW 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1562 LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQ- 1640
Cdd:cd05958 319 NITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVl 398
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1820754837 1641 --ELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:cd05958 399 arELQDHAKAHIAPYKYPR-AIEFVTELPRTATGKLQRFALR 439
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
61-537 |
7.12e-35 |
|
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: 140.27 E-value: 7.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVF 140
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 141 VngesaeclaqvvkennmdtrlvvfadsagfvgraatltavlrsqdtawidefecaklTSPKHVAAIVCSSGTSGFPKGT 220
Cdd:cd05914 85 V---------------------------------------------------------SDEDDVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 221 EISHAAMINYMAHVKVHDLKG------------HV--SMWTPSMRWYCGLFIVIkaiLD--CSKRIIVPDYDDDE---GL 281
Cdd:cd05914 108 MLTYRNIVSNVDGVKEVVLLGkgdkilsilplhHIypLTFTLLLPLLNGAHVVF---LDkiPSAKIIALAFAQVTptlGV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 282 CR-----------FIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLP-----TLKILLFGGAHFKGELQQTLVKL-LPhtdV 344
Cdd:cd05914 185 PVplviekifkmdIIPKLTLKKFKFKLAKKINNRKIRKLAFKKVHeafggNIKEFVIGGAKINPDVEEFLRTIgFP---Y 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 345 ILSYGMTDYGGLCArqtkYSKP-----GSCGFVcetgrLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRAL 419
Cdd:cd05914 262 TIGYGMTETAPIIS----YSPPnrirlGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 420 DSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIK-ISPAEIEALIQQHPAVFQVAVVPVPHN-INEEHAMAFVAKVPG 497
Cdd:cd05914 333 DKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINNMPFVLESLVVVQEKKlVALAYIDPDFLDVKA 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1820754837 498 KEVTELDIT------DLVKQNMPWYCRLHAGVKFMEKLPRTATGKI 537
Cdd:cd05914 413 LKQRNIIDAikwevrDKVNQKVPNYKKISKVKIVKEEFEKTPKGKI 458
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1202-1683 |
7.19e-35 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 141.17 E-value: 7.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIS---NTwdhELTPMTARNFLTLTSPK 1278
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFlplNT---AYTLAELDYFIGDAEPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1279 IVFTVSSSAANLMEAAKELKMNlKVVVMDkLDGYESVEENVMKGHDTREIIEFKchvtnPDDVALIVPSSGTTGLPKGTE 1358
Cdd:PRK07514 103 LVVCDPANFAWLSKIAAAAGAP-HVETLD-ADGTGSLLEAAAAAPDDFETVPRG-----ADDLAAILYTSGTTGRSKGAM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1359 ISHYSLfcclhpYKN-RTLVGHtcivtptmrWHYG---VLM----------AFrlVAANakklivpdnddaenfCQLIEK 1424
Cdd:PRK07514 176 LSHGNL------LSNaLTLVDY---------WRFTpddVLIhalpifhthgLF--VATN---------------VALLAG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1425 YQITWFgtdPfmiiKFIKSQLLEKYR-------LPTLKVILSSGAHLRKEHLEVMR-------EKLPDVFI-----TNH- 1484
Cdd:PRK07514 224 ASMIFL---P----KFDPDAVLALMPratvmmgVPTFYTRLLQEPRLTREAAAHMRlfisgsaPLLAETHRefqerTGHa 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 ----YGMTDTACVVSaqNKFT---KLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFD 1557
Cdd:PRK07514 297 ilerYGMTETNMNTS--NPYDgerRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1558 SDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPnevdeqHPK------AFVVQ 1631
Cdd:PRK07514 375 ADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVP------HPDfgegvtAVVVP 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1632 VPNKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK07514 449 KPGAALDEAAILAALKGRLARF-KQPKRVFFVDELPRNTMGKVQKNLLREQY 499
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
621-1099 |
8.09e-35 |
|
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: 141.48 E-value: 8.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 621 DAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSP 700
Cdd:cd05970 41 DAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 701 K-VVFVNEESAENLMEAAKEE--NLQVRVMVIGSLP-GFVSLANILEEQ---VSRAEIDGFRCTKidnphDLAMICSSSG 773
Cdd:cd05970 121 KmIVAIAEDNIPEEIEKAAPEcpSKPKLVWVGDPVPeGWIDFRKLIKNAspdFERPTANSYPCGE-----DILLVYFSSG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 774 TTGMPKGTE---------LSYASLYNSITPvEEVHAKNEICAWVPTIrWHGGLNQCIevimSNAKWIIFSDDNIKEIALC 844
Cdd:cd05970 196 TTGMPKMVEhdftyplghIVTAKYWQNVRE-GGLHLTVADTGWGKAV-WGKIYGQWI----AGAAVFVYDYDKFDPKALL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 845 EIIQKHGVTWLGTDTNFAILYVKMNIfQKYPMPSLRKMVITGAPFTKELHETVAKimpHT--QILQCYGLTDAGgLCVSQ 922
Cdd:cd05970 270 EKLSKYGVTTFCAPPTIYRFLIREDL-SRYDLSSLRYCTTAGEALNPEVFNTFKE---KTgiKLMEGFGQTETT-LTIAT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 923 AK--NSKPGSCGFVTKGIRIKIADeKTGIALGPKERGEICIKSE-----FMMKGYHKNPEQTKEAFdSDGWLHTKDIGYY 995
Cdd:cd05970 345 FPwmEPKPGSMGKPAPGYEIDLID-REGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW-HDGYYHTGDAAWM 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 996 DENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV---QKVVEKEVTEEELHDLVN 1072
Cdd:cd05970 423 DEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIvlaKGYEPSEELKKELQDHVK 502
|
490 500
....*....|....*....|....*..
gi 1820754837 1073 KNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:cd05970 503 KVTAPY-KYPRIVEFVDELPKTISGKI 528
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
65-542 |
9.82e-35 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 139.51 E-value: 9.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVnge 144
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 saeclAQVVKENNMDTrlvVFADSAGFVGRAATltavlrSQDTAWIDEfecakltspkHVAAIVCSSGTSGFPKGTEISH 224
Cdd:TIGR01923 78 -----DSLLEEKDFQA---DSLDRIEAAGRYET------SLSASFNMD----------QIATLMFTSGTTGKPKAVPHTF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AamiNYMAHVKVHDLKGHvsmWTPSMRWY--------CGLFIVIKAILDCSKRIIVpdyDDDEGLCRFIEKYEVSWFrcd 296
Cdd:TIGR01923 134 R---NHYASAVGSKENLG---FTEDDNWLlslplyhiSGLSILFRWLIEGATLRIV---DKFNQLLEMIANERVTHI--- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 297 SCFPIRLVKfgvLSKYRLP--TLKILLFGGAHFKGEL-QQTLVKLLPhtdVILSYGMTDyggLCARQTKYSKPGScgfvc 373
Cdd:TIGR01923 202 SLVPTQLNR---LLDEGGHneNLRKILLGGSAIPAPLiEEAQQYGLP---IYLSYGMTE---TCSQVTTATPEML----- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 374 eTGRLKVVDPNTG-----KVLGANKTGEIWAKSSYMMNGYYNNPEAtRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEF 448
Cdd:TIGR01923 268 -HARPDVGRPLAGreikiKVDNKEGHGEIMVKGANLMKGYLYQGEL-TPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 449 INYRAIKISPAEIEALIQQHPAVFQVAVVPVPhniNEEHAMAFVAKVPG-KEVTELDITDLVKQNMPWYcRLHAGVKFME 527
Cdd:TIGR01923 346 IISGGENIYPEEIETVLYQHPGIQEAVVVPKP---DAEWGQVPVAYIVSeSDISQAKLIAYLTEKLAKY-KVPIAFEKLD 421
|
490
....*....|....*
gi 1820754837 528 KLPRTATGKIAKKQL 542
Cdd:TIGR01923 422 ELPYNASGKILRNQL 436
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
623-1099 |
1.15e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 140.84 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:PRK08316 32 FGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNEESAENL---MEAAKEENLQVRVMVIGSLP--GFVSLANILEEQ---VSRAEIDGfrctkidnpHDLAMICSSSGT 774
Cdd:PRK08316 112 FLVDPALAPTAeaaLALLPVDTLILSLVLGGREApgGWLDFADWAEAGsvaEPDVELAD---------DDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 775 TGMPKGTELSYASL---YNS------ITP-VEEVHAkneicawVP------------TIRWHGGLNqcieVIMSNAkwii 832
Cdd:PRK08316 183 ESLPKGAMLTHRALiaeYVScivagdMSAdDIPLHA-------LPlyhcaqldvflgPYLYVGATN----VILDAP---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 833 fsddnikEIALC-EIIQKHGVTWLgtdtnFA-----ILYVKMNIFQKYPMPSLRK----MVITGAPFTKELHETvakiMP 902
Cdd:PRK08316 248 -------DPELIlRTIEAERITSF-----FApptvwISLLRHPDFDTRDLSSLRKgyygASIMPVEVLKELRER----LP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 903 HTQILQCYGLTDAGGLC-VSQAKN--SKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKE 979
Cdd:PRK08316 312 GLRFYNCYGQTEIAPLAtVLGPEEhlRRPGSAGRPVLNVETRVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 980 AFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVE 1059
Cdd:PRK08316 391 AF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG 469
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1820754837 1060 KEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK08316 470 ATVTEDELIAHCRARLAGF-KVPKRVIFVDELPRNPSGKI 508
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1340-1676 |
1.59e-34 |
|
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: 135.86 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1340 DVALIVPSSGTTGLPKGTEISHYSLFCC----LHPYKnrtLVGHTCIVTPTMRWHY-GVLMAFRLVAANAKKLIVPDNDD 1414
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAAnlqlIHAMG---LTEADVYLNMLPLFHIaGLNLALATFHAGGANVVMEKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1415 AENFcQLIEKYQITWFGTDPFMIikfikSQLLEK-----YRLPTLKVILSSGAhlrKEHLEVMREKLPDVFITNhYGMTD 1489
Cdd:cd17637 78 AEAL-ELIEEEKVTLMGSFPPIL-----SNLLDAaeksgVDLSSLRHVLGLDA---PETIQRFEETTGATFWSL-YGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1490 TACVVSAQNKFTKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDsDGWLRTGDLAY 1569
Cdd:cd17637 148 TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1570 YDDNGEIYIVDRIS--DFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVE 1647
Cdd:cd17637 226 FDEDGYLWYAGRKPekELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVG 305
|
330 340
....*....|....*....|....*....
gi 1820754837 1648 KNLPDYCRLRgGVKIVDQLPRTTTGKIAR 1676
Cdd:cd17637 306 SRIARYKKPR-YVVFVEALPKTADGSIDR 333
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1334-1680 |
1.60e-34 |
|
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: 139.11 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1334 HVTNPDDVALIVPSSGTTGLPKGTEISHYSL---------FCCLHPyKNRTLVghtciVTPtMRWHYGVLMAFRLVAANA 1404
Cdd:cd05922 112 HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLlanarsiaeYLGITA-DDRALT-----VLP-LSYDYGLSVLNTHLLRGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1405 KKLIVPDNDDAENFCQLIEKYQITWFGTDPFmIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNH 1484
Cdd:cd05922 185 TLVLTNDGVLDDAFWEDLREHGATGLAGVPS-TYAMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVM 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVVS---AQNKFTKLGSVGYVSSNVRIKMVDLDTEEAlGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGW 1561
Cdd:cd05922 264 YGQTEATRRMTylpPERILEKPGSIGLAIPGGEFEILDDDGTPT-PPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1562 LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQhPKAFVVQVPnkSVTEQE 1641
Cdd:cd05922 343 LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEK-LALFVTAPD--KIDPKD 419
|
330 340 350
....*....|....*....|....*....|....*....
gi 1820754837 1642 LISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:cd05922 420 VLRSLAERLPPY-KVPATVRVVDELPLTASGKVDYAALR 457
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
65-477 |
1.71e-34 |
|
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: 138.88 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPwdnelspmtaRYFLSltkpkivfvnge 144
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP----------IYPTS------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAECLAQVVkeNNMDTRLVvfadsagFVGraatltavlrsqdtawidefecakltSPKHVAAIVCSSGTSGFPKGTEISH 224
Cdd:cd05907 65 SAEQIAYIL--NDSEAKAL-------FVE--------------------------DPDDLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AamiNYMAHVK-----VHDLKG--HVSM----WTPSMRwyCGLFIVI------------KAILDCSKRI------IVPdy 275
Cdd:cd05907 110 R---NILSNALalaerLPATEGdrHLSFlplaHVFERR--AGLYVPLlagariyfassaETLLDDLSEVrptvflAVP-- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 276 dddeglcRFIEKY-------EVSWFRcdscfpIRLVKFGVLSKyrlptLKILLFGGAHFKGELQQTLVKL-LPhtdVILS 347
Cdd:cd05907 183 -------RVWEKVyaaikvkAVPGLK------RKLFDLAVGGR-----LRFAASGGAPLPAELLHFFRALgIP---VYEG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDYGGLCA--RQTKYsKPGSCGfvcetgrlKVVDPNTGKVlgaNKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWL 425
Cdd:cd05907 242 YGLTETSAVVTlnPPGDN-RIGTVG--------KPLPGVEVRI---ADDGEILVRGPNVMLGYYKNPEATAEALDADGWL 309
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 426 HTGDLGYYDNDGEVFLVDRMSE-FINYRAIKISPAEIEALIQQHPAVFQVAVV 477
Cdd:cd05907 310 HTGDLGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQAVVI 362
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1206-1681 |
2.37e-34 |
|
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: 144.61 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGA----IsntwDHELtPMTARNF-LTLTSPKIV 1280
Cdd:COG1020 503 TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAayvpL----DPAY-PAERLAYmLEDAGARLV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1281 FTVSSSAANLMEAAkelkmnLKVVVMDKLDGYESVEENVmkghdtreiiefKCHVTnPDDVALIVPSSGTTGLPKGTEIS 1360
Cdd:COG1020 578 LTQSALAARLPELG------VPVLALDALALAAEPATNP------------PVPVT-PDDLAYVIYTSGSTGRPKGVMVE 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1361 HYSLfcclhpykNRTLVGH--TCIVTPTMRW-----------HYGVLMAF----RLVaanakklIVPDND--DAENFCQL 1421
Cdd:COG1020 639 HRAL--------VNLLAWMqrRYGLGPGDRVlqfaslsfdasVWEIFGALlsgaTLV-------LAPPEArrDPAALAEL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1422 IEKYQITWFGTDPFMIikfikSQLLE--KYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTA-----CVV 1494
Cdd:COG1020 704 LARHRVTVLNLTPSLL-----RALLDaaPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTvdstyYEV 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1495 SAQNKFTKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAF-----DSDG--WLRTGDL 1567
Cdd:COG1020 779 TPPDADGGSVPIGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFvadpfGFPGarLYRTGDL 857
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1568 AYYDDNGEIYIVDRIsDF---IN-FRsinVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELI 1643
Cdd:COG1020 858 ARWLPDGNLEFLGRA-DDqvkIRgFR---IELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLR 933
|
490 500 510
....*....|....*....|....*....|....*...
gi 1820754837 1644 SYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:COG1020 934 LALALLLPPY-MVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1485-1680 |
2.83e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 138.58 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVVSAQ-NKFTKLGSVGYVSSNVRIKMVDLDTEE-ALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWL 1562
Cdd:PRK07787 273 YGMTETLITLSTRaDGERRPGWVGLPLAGVETRLVDEDGGPvPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1563 RTGDLAYYDDNGEIYIVDRIS-DFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVvqVPNKSVTEQE 1641
Cdd:PRK07787 353 RTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV--VGADDVAADE 430
|
170 180 190
....*....|....*....|....*....|....*....
gi 1820754837 1642 LISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK07787 431 LIDFVAQQLSVHKRPR-EVRFVDALPRNAMGKVLKKQLL 468
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
629-1054 |
4.45e-34 |
|
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: 137.51 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNEE 708
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 saenlmeaakeenlqvrvmvigslpgfvslanileeqvsraeidgFRCTKI-DNPHDLAMICSSSGTTGMPKGTELSYAS 787
Cdd:cd05903 83 ---------------------------------------------FRQFDPaAMPDAVALLLFTSGTTGEPKGVMHSHNT 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 788 LYNSITP-VEEVHAKNEICAWVPTIRWH--GGLNQCIEVIMSNAKWIIFSDDNIKEIAlcEIIQKHGVTWLGTDTNFAIL 864
Cdd:cd05903 118 LSASIRQyAERLGLGPGDVFLVASPMAHqtGFVYGFTLPLLLGAPVVLQDIWDPDKAL--ALMREHGVTFMMGATPFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 865 YVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYGLTDagglCVSQAKNSKPG-------SCGFVTKG 937
Cdd:cd05903 196 LLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTE----CPGAVTSITPApedrrlyTDGRPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 938 IRIKIADEkTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDsDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIK 1017
Cdd:cd05903 271 VEIKVVDD-TGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGEN 348
|
410 420 430
....*....|....*....|....*....|....*..
gi 1820754837 1018 LSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:cd05903 349 IPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVV 385
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
43-542 |
1.04e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 138.63 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 43 LEKLRSR-PEfiAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAI---SNPW 118
Cdd:PRK06710 30 VEQMASRyPE--KKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIvvqTNPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 119 DNE------LSPMTARYFL--SLTKPKIVFVngESAECLAQVVKennmdTRLVVFADSAG-----FVGRAATlTAVLRSQ 185
Cdd:PRK06710 108 YTEreleyqLHDSGAKVILclDLVFPRVTNV--QSATKIEHVIV-----TRIADFLPFPKnllypFVQKKQS-NLVVKVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 186 DTAWIDEFECAK---------LTSPKH-VAAIVCSSGTSGFPKGTEISHAAMINYM---AHVKVHDLKGH--VSMWTPSM 250
Cdd:PRK06710 180 ESETIHLWNSVEkevntgvevPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVSNTlmgVQWLYNCKEGEevVLGVLPFF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 251 RWYCGLFIVIKAILDCSKRIIVPDYDDdEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGE 330
Cdd:PRK06710 260 HVYGMTAVMNLSIMQGYKMVLIPKFDM-KMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 331 LQQTLvKLLPHTDVILSYGMTDYGGLCARQTKYSK--PGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGY 408
Cdd:PRK06710 339 VQEKF-ETVTGGKLVEGYGLTESSPVTHSNFLWEKrvPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGY 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 409 YNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHA 488
Cdd:PRK06710 418 WNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 489 MAFVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:PRK06710 497 KAFVVLKEGTECSEEELNQFARKYLAAY-KVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1206-1683 |
1.36e-33 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 137.71 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFTVSS 1285
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDAD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAAKELKMNLKVVVMDKLDGYESVEEnvmkghdTREIIEFKCHVTN------PDDvALIVPSSGTTGLPKGTEI 1359
Cdd:PRK05852 125 GPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSV-------HLDAATEPTPATStpeglrPDD-AMIMFTGGTTGLPKMVPW 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1360 SHYSLFCCLHPYKNRTLVG---HTCIVTPTMRWHyGVLMAFRLVAANAKKLIVPDND--DAENFCQLIEKYQITWFGTDP 1434
Cdd:PRK05852 197 THANIASSVRAIITGYRLSprdATVAVMPLYHGH-GLIAALLATLASGGAVLLPARGrfSAHTFWDDIKAVGATWYTAVP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1435 FmiikfIKSQLLEKYRL-------PTLKVILSSGAHLRKEHLEVMREKLPDVFITNhYGMTDTACVVSA---------QN 1498
Cdd:PRK05852 276 T-----IHQILLERAATepsgrkpAALRFIRSCSAPLTAETAQALQTEFAAPVVCA-FGMTEATHQVTTtqiegigqtEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1499 KFTKLGSVGYvSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYI 1578
Cdd:PRK05852 350 PVVSTGLVGR-STGAQIRIVGSDGLP-LPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1579 VDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYcRLRG 1658
Cdd:PRK05852 427 RGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAF-EIPA 505
|
490 500
....*....|....*....|....*
gi 1820754837 1659 GVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK05852 506 SFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1206-1681 |
1.49e-33 |
|
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: 137.60 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTARnfltLTSPKIVFTVS 1284
Cdd:cd05928 43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLV-------FIPGTIQ----LTAKDILYRLQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1285 SSAANLMEAAKEL------------KMNLKVVVMDK-LDGYESVEEnVMKGHDTreiiEFKCHVTNPDDVALIVPSSGTT 1351
Cdd:cd05928 112 ASKAKCIVTSDELapevdsvasecpSLKTKLLVSEKsRDGWLNFKE-LLNEAST----EHHCVETGSQEPMAIYFTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1352 GLPKGTEISHYSLfccLHPYK--NRTLVGHTcivTPTMRWH----------YGVLMAFRLVAANAKKLIVPdNDDAENFC 1419
Cdd:cd05928 187 GSPKMAEHSHSSL---GLGLKvnGRYWLDLT---ASDIMWNtsdtgwiksaWSSLFEPWIQGACVFVHHLP-RFDPLVIL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1420 QLIEKYQITWFGTDPfMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKlPDVFITNHYGMTDTA--CVVSAQ 1497
Cdd:cd05928 260 KTLSSYPITTFCGAP-TVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ-TGLDIYEGYGQTETGliCANFKG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1498 NKFtKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGE--LRVKA---ITIMQGYHKNPETTKQAFDSDGWLrTGDLAYYDD 1572
Cdd:cd05928 338 MKI-KPGSMGKASPPYDVQIID-DNGNVLPPGTEGDigIRVKPirpFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1573 NGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVP-----NKSVTEQELISYVE 1647
Cdd:cd05928 415 DGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPqflshDPEQLTKELQQHVK 494
|
490 500 510
....*....|....*....|....*....|....
gi 1820754837 1648 KNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd05928 495 SVTAPYKYPR-KVEFVQELPKTVTGKIQRNELRD 527
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
63-545 |
1.56e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 137.75 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAisnpwdnelspmtaryflsltkpKIVFVN 142
Cdd:PRK07788 74 TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGA-----------------------RIILLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 143 -GESAECLAQVVKENNMDtrlVVFADS--AGFV-------GRAATL---TAVLRSQDTAW--IDEFECAKLTSP-----K 202
Cdd:PRK07788 131 tGFSGPQLAEVAAREGVK---ALVYDDefTDLLsalppdlGRLRAWggnPDDDEPSGSTDetLDDLIAGSSTAPlpkppK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 203 HVAAIVCSSGTSGFPKGTEISH-------AAMINYMAhvkvhdLKGHVSMWTPS---MRWYCGLFIVIKAiLDCskRIIV 272
Cdd:PRK07788 208 PGGIVILTSGTTGTPKGAPRPEpsplaplAGLLSRVP------FRAGETTLLPApmfHATGWAHLTLAMA-LGS--TVVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 273 PDYDDDEGLCRFIEKYevswfRCDSCF--PI---RLVKFG--VLSKYRLPTLKILLFGGAHFKGELQQTLVKLLphTDVI 345
Cdd:PRK07788 279 RRRFDPEATLEDIAKH-----KATALVvvPVmlsRILDLGpeVLAKYDTSSLKIIFVSGSALSPELATRALEAF--GPVL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 346 LS-YGMTD--YGGLCARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYN--NPEATrrald 420
Cdd:PRK07788 352 YNlYGSTEvaFATIATPEDLAEAPGTVGRPPKGVTVKILDEN-GNEVPRGVVGRIFVGNGFPFEGYTDgrDKQII----- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 421 sDGWLHTGDLGYYDNDGEVFLVDRMSEFInyraikIS------PAEIEALIQQHPAVFQVAVVPVPhniNEEHAM---AF 491
Cdd:PRK07788 426 -DGLLSSGDVGYFDEDGLLFVDGRDDDMI------VSggenvfPAEVEDLLAGHPDVVEAAVIGVD---DEEFGQrlrAF 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 492 VAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQI 545
Cdd:PRK07788 496 VVKAPGAALDEDAIKDYVRDNLARY-KVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
764-1100 |
1.80e-33 |
|
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: 132.53 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 764 DLAMICSSSGTTGMPKGTELSYASLYNSITPVEEV-HAKNEICAWVP-TIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEi 841
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLfNISGEDAILAPgPLSHSLFLYGAISALYLGGTFIGQRKFNPKS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 842 aLCEIIQKHGVTWL-GTDTNFAILYVKMNifqkyPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAG---G 917
Cdd:cd17633 80 -WIRKINQYNATVIyLVPTMLQALARTLE-----PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSfitY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 918 LCVSQAKnsKPGSCGFVTKGIRIKIADEKTGialgpkERGEICIKSEFMMKGYHKNPEQTKeafdsDGWLHTKDIGYYDE 997
Cdd:cd17633 154 NFNQESR--PPNSVGRPFPNVEIEIRNADGG------EIGKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 998 NGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVqkvVEKEVTEEELHDLVNKNLPW 1077
Cdd:cd17633 221 EGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLTYKQLKRFLKQKLSR 297
|
330 340
....*....|....*....|...
gi 1820754837 1078 YcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd17633 298 Y-EIPKKIIFVDSLPYTSSGKIA 319
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1187-1682 |
2.22e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 137.18 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1187 LKSKPDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIS---NTW--DH 1261
Cdd:PRK06164 20 ARARPDAVALIDE--DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATViavNTRyrSH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1262 ELTPMTARNFLTLTSPKIVFTVSSSAANLMEAAKELKMNLK-VVVMDKL-----DGYESVEENVMKGHDTREIIEFKCHV 1335
Cdd:PRK06164 98 EVAHILGRGRARWLVVWPGFKGIDFAAILAAVPPDALPPLRaIAVVDDAadatpAPAPGARVQLFALPDPAPPAAAGERA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1336 TNPDDVALIVPSSGTTGLPKgteishyslfCCLHPykNRTLVGHTCIVTPTmrwhYGVLMAFRLVA-------------- 1401
Cdd:PRK06164 178 ADPDAGALLFTTSGTTSGPK----------LVLHR--QATLLRHARAIARA----YGYDPGAVLLAalpfcgvfgfstll 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1402 ---ANAKKLIVPDNDDAENFCQLIEKYQITW-FGTDPFMiiKFIKSQLLEKYRLPTLKVI----LSSGAHlrkEHLEVMR 1473
Cdd:PRK06164 242 galAGGAPLVCEPVFDAARTARALRRHRVTHtFGNDEML--RRILDTAGERADFPSARLFgfasFAPALG---ELAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1474 EKlpDVFITNHYGMTDTACVVSAQNKFTK-----LGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKN 1548
Cdd:PRK06164 317 AR--GVPLTGLYGSSEVQALVALQPATDPvsvriEGGGRPASPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1549 PETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIpnEVDEQ-HPKA 1627
Cdd:PRK06164 395 PDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1628 FVVQVPNKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTG---KIARKQLRDM 1682
Cdd:PRK06164 473 FVIPTDGASPDEAGLMAACREALAGF-KVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1191-1679 |
6.84e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 140.30 E-value: 6.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVdaLTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARN 1270
Cdd:PRK12467 526 PERPALV--FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAY 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 FLTLTSPKIVFTVSSSAAnLMEAAKELKMNLKVVVMDKLDGYesveenvmKGHDTREIIEfkchvtnPDDVALIVPSSGT 1350
Cdd:PRK12467 604 MLDDSGVRLLLTQSHLLA-QLPVPAGLRSLCLDEPADLLCGY--------SGHNPEVALD-------PDNLAYVIYTSGS 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISHYSL---FCCLHPYKNRTLVGHTCIVTpTMRWHYGVLMAFRLVAANAKKLIVPDND--DAENFCQLIEKY 1425
Cdd:PRK12467 668 TGQPKGVAISHGALanyVCVIAERLQLAADDSMLMVS-TFAFDLGVTELFGALASGATLHLLPPDCarDAEAFAALMADQ 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1426 QITWFGTDPFMIIKFIKSQLLEKYRlpTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVVSA-----QNKF 1500
Cdd:PRK12467 747 GVTVLKIVPSHLQALLQASRVALPR--PQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTyelsdEERD 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1501 TKLGSVGYVSSNVRIKMVDLDTEEALGPnKIGELRVKAITIMQGYHKNPETTKQAFDSDGW-------LRTGDLAYYDDN 1573
Cdd:PRK12467 825 FGNVPIGQPLANLGLYILDHYLNPVPVG-VVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRAD 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1574 GEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQ----ELISYVEKN 1649
Cdd:PRK12467 904 GVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQatrdELKAQLRQV 983
|
490 500 510
....*....|....*....|....*....|
gi 1820754837 1650 LPDYcRLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK12467 984 LPDY-MVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
379-548 |
7.81e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 136.09 E-value: 7.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 379 KVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFInyraIK--- 455
Cdd:PRK08315 383 KIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI----IRgge 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 456 -ISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDlvkqnmpwYCRlhaG----------VK 524
Cdd:PRK08315 459 nIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRD--------FCR---GkiahykipryIR 527
|
170 180
....*....|....*....|....
gi 1820754837 525 FMEKLPRTATGKIAKKQLKQIAKS 548
Cdd:PRK08315 528 FVDEFPMTVTGKIQKFKMREMMIE 551
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
623-1100 |
8.70e-33 |
|
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: 133.81 E-value: 8.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvvskLSARYflslmsPkv 702
Cdd:cd05930 8 DGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVP-------LDPSY------P-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 vfvneesaenlmeaakeenlQVRvmvigslpgfvsLANILEEqvSRAEIdgfrctKIDNPHDLAMICSSSGTTGMPKGTE 782
Cdd:cd05930 73 --------------------AER------------LAYILED--SGAKL------VLTDPDDLAYVIYTSGSTGKPKGVM 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 783 LSYASLYNSITPVEEVHA--KNEICAWVPTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEI-ALCEIIQKHGVTWLGTDT 859
Cdd:cd05930 113 VEHRGLVNLLLWMQEAYPltPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPeALADLLAEEGITVLHLTP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 860 NFAILYVKMNIFQKYPmpSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAGGLCVSQAKNSKPGSCGFVTKG-- 937
Cdd:cd05930 193 SLLRLLLQELELAALP--SLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGrp 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 938 ---IRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSD-----GWLH-TKDIGYYDENGEIFFVNRIs 1008
Cdd:cd05930 271 ipnTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNpfgpgERMYrTGDLVRWLPDGNLEFLGRI- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1009 DF---INYKAIKLssAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYCkLQAGI 1085
Cdd:cd05930 349 DDqvkIRGYRIEL--GEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYM-VPSAF 425
|
490
....*....|....*
gi 1820754837 1086 KFVNDFPRISTGKID 1100
Cdd:cd05930 426 VVLDALPLTPNGKVD 440
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
63-543 |
1.12e-32 |
|
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: 134.80 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVN 142
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 143 GESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDtawiDEFECAKlTSPKHVAAIVCSSGTSGFPKGTEI 222
Cdd:cd05959 109 GELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEA----EQLKPAA-THADDPAFWLYSSGSTGRPKGVVH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 223 SHAAMInYMAHVKVHDLKG----HVSMWTPSMRWYCGL-------FIVIKAILdcskriIVPDYDDDEGLCRFIEKYEVS 291
Cdd:cd05959 184 LHADIY-WTAELYARNVLGiredDVCFSAAKLFFAYGLgnsltfpLSVGATTV------LMPERPTPAAVFKRIRRYRPT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 292 WFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHtDVILSYGMTDYGGL-CARQTKYSKPGSCG 370
Cdd:cd05959 257 VFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL-DILDGIGSTEMLHIfLSNRPGRVRYGTTG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 371 FVCETGRLKVVDPNTGKVlGANKTGEIWAKSSYMMNGYYNNPEATRRALDSdGWLHTGDLGYYDNDGEVFLVDRMSEFIN 450
Cdd:cd05959 336 KPVPGYEVELRDEDGGDV-ADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 451 YRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDL---VKQNMPWYCRLHaGVKFME 527
Cdd:cd05959 414 VSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELkefVKDRLAPYKYPR-WIVFVD 492
|
490
....*....|....*.
gi 1820754837 528 KLPRTATGKIAKKQLK 543
Cdd:cd05959 493 ELPKTATGKIQRFKLR 508
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1190-1682 |
1.16e-32 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 135.70 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1190 KPDSIgqVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNlDVFL-ILLGTMYIGAISNTWDHELTPMTA 1268
Cdd:PLN02860 20 RGNAV--VTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNS-DLYLeWLLAVACAGGIVAPLNYRWSFEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1269 RNFLTLTSPKIVFT---VSSSAANLMEAA-KELKMNlkvVVMDKLDGYESVE-------ENVMKGHDTREIIEFKchvTN 1337
Cdd:PLN02860 97 KSAMLLVRPVMLVTdetCSSWYEELQNDRlPSLMWQ---VFLESPSSSVFIFlnsflttEMLKQRALGTTELDYA---WA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1338 PDDVALIVPSSGTTGLPKGTEISHYSLFccLHPYKNRTLVG--------HT---CivtptmrwHYGVLM-AFRLVAANAK 1405
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALI--VQSLAKIAIVGygeddvylHTaplC--------HIGGLSsALAMLMVGAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1406 KLIVPDNDDAENFcQLIEKYQITWFGTDPFM---IIKFIKSQLLEKYRlPTLKVILSSGAHLRKEHLEVMREKLPDVFIT 1482
Cdd:PLN02860 241 HVLLPKFDAKAAL-QAIKQHNVTSMITVPAMmadLISLTRKSMTWKVF-PSVRKILNGGGSLSSRLLPDAKKLFPNAKLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1483 NHYGMTDtAC-----------------VVSAQNKFTKLGS--------VGYVSSNVRIkMVDLDteealGPNKIGELRVK 1537
Cdd:PLN02860 319 SAYGMTE-ACssltfmtlhdptlespkQTLQTVNQTKSSSvhqpqgvcVGKPAPHVEL-KIGLD-----ESSRVGRILTR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1538 AITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIP 1617
Cdd:PLN02860 392 GPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1618 NEVDEQHPKAFV------VQVPNKSVTEQELISYVEKNLPDYCRLRG--GVKIV-------DQLPRTTTGKIARKQLRDM 1682
Cdd:PLN02860 472 DSRLTEMVVACVrlrdgwIWSDNEKENAKKNLTLSSETLRHHCREKNlsRFKIPklfvqwrKPFPLTTTGKIRRDEVRRE 551
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1188-1683 |
2.14e-32 |
|
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: 133.44 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1188 KSKPDSIGqVDALTGKVqTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMT 1267
Cdd:cd05918 10 RSQPDAPA-VCAWDGSL-TYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1268 ARNFLTLTSPKIVFTvsssaanlmeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchvTNPDDVALIVPS 1347
Cdd:cd05918 88 LQEILQDTGAKVVLT-----------------------------------------------------SSPSDAAYVIFT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1348 SGTTGLPKGTEISHYSLFCCLHPYKNRTlvghtcIVTPTMRW--------------HYGVLMAFRLVAanakklIVPDND 1413
Cdd:cd05918 115 SGSTGKPKGVVIEHRALSTSALAHGRAL------GLTSESRVlqfasytfdvsileIFTTLAAGGCLC------IPSEED 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1414 DAENFCQLIEKYQITWFGTDPFMiikfikSQLLEKYRLPTLKVILSSGahlrkehlEVMREKL-----PDVFITNHYGMT 1488
Cdd:cd05918 183 RLNDLAGFINRLRVTWAFLTPSV------ARLLDPEDVPSLRTLVLGG--------EALTQSDvdtwaDRVRLINAYGPA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1489 DTA--CVVSAQNKFTKLGSVGY-VSSNVRIkmVDLDTEEALGP-NKIGELRVKAITIMQGYHKNPETTKQAF-DSDGWL- 1562
Cdd:cd05918 249 ECTiaATVSPVVPSTDPRNIGRpLGATCWV--VDPDNHDRLVPiGAVGELLIEGPILARGYLNDPEKTAAAFiEDPAWLk 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1563 -----------RTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQ------------------AAV 1613
Cdd:cd05918 327 qegsgrgrrlyRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvvevvkpkdgssspqlVAF 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1614 LGIPNEVDEQHPKAFVVQVPNKSVTEQ--ELISYVEKNLPDYcrlrggvKI------VDQLPRTTTGKIARKQLRDMY 1683
Cdd:cd05918 407 VVLDGSSSGSGDGDSLFLEPSDEFRALvaELRSKLRQRLPSY-------MVpsvflpLSHLPLTASGKIDRRALRELA 477
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
629-1099 |
3.63e-32 |
|
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: 132.81 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENhlntcVPVLAILYI-----GGIICPwdhVVSKLSAR---YFLSLMSP 700
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPN-----TPAMYELHFgvpmaGAVLNA---LNTRLDAEeiaFILRHSEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 701 KVVFVNEESA-ENLMEAAKeenlqvrvmvigslPGFVSLanileeqvsraeidgfrctKIDNPHDLAMICSSSGTTGMPK 779
Cdd:cd12118 103 KVLFVDREFEyEDLLAEGD--------------PDFEWI-------------------PPADEWDPIALNYTSGTTGRPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 780 GTELSYASLY-NSITPVEE---------------VHAkNEIC-AWVPTIRwhGGLNQCIEVIMSNAKWiifsddnikeia 842
Cdd:cd12118 150 GVVYHHRGAYlNALANILEwemkqhpvylwtlpmFHC-NGWCfPWTVAAV--GGTNVCLRKVDAKAIY------------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 843 lcEIIQKHGVTWL-GTDTNFAILyVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHtqILQCYGLTDAGGL--- 918
Cdd:cd12118 215 --DLIEKHKVTHFcGAPTVLNML-ANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFD--VTHVYGLTETYGPatv 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 919 CVSQAK-NSKPGSCGFVTK---GIRIKIADEKTGIALGP--------KERGEICIKSEFMMKGYHKNPEQTKEAFdSDGW 986
Cdd:cd12118 290 CAWKPEwDELPTEERARLKarqGVRYVGLEEVDVLDPETmkpvprdgKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGW 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 987 LHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEE 1066
Cdd:cd12118 369 FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEE 448
|
490 500 510
....*....|....*....|....*....|...
gi 1820754837 1067 LHDLVNKNLPWYcKLQAGIKFVnDFPRISTGKI 1099
Cdd:cd12118 449 IIAFCREHLAGF-MVPKTVVFG-ELPKTSTGKI 479
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
63-544 |
4.52e-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: 341275 [Multi-domain] Cd Length: 439 Bit Score: 131.40 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVN 142
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 143 GESAEclaqvvkennmdtrlvvfadsagfvgraatltavlrsqdtawidefecakltspkhvAAIVCSSGTSGFPKGTEI 222
Cdd:cd05971 86 GSDDP---------------------------------------------------------ALIIYTSGTTGPPKGALH 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 223 SHAAMINYMAHVKV-HDL---KGHVsMWTPS-MRWYCGLFIVIKA-------ILDCSKRIIvpdydDDEGLCRFIEKYEV 290
Cdd:cd05971 109 AHRVLLGHLPGVQFpFNLfprDGDL-YWTPAdWAWIGGLLDVLLPslyfgvpVLAHRMTKF-----DPKAALDLMSRYGV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 291 SwfrcDSCFP---IRLVKF-GVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLpHTDVILSYGMTDYG---GLCARQTKy 363
Cdd:cd05971 183 T----TAFLPptaLKMMRQqGEQLKHAQVKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNlviGNCSALFP- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 364 SKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAK--SSYMMNGYYNNPEATRRALDSDgWLHTGDLGYYDNDGEVFL 441
Cdd:cd05971 257 IKPGSMGKPIPGHRVAIVDDN-GTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWY 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 442 VDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTEL---DITDLVKQnmpwycR 518
Cdd:cd05971 335 VGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKT------R 408
|
490 500 510
....*....|....*....|....*....|.
gi 1820754837 519 LHA-----GVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:cd05971 409 LAAheyprEIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
61-543 |
5.00e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 133.74 E-value: 5.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWLR-EQGVQPGDIIGICTHNHLESYVPLLAALYLGAI---SNPWDNElSPMTARYFLSLTKP 136
Cdd:PRK05677 47 GKTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIvvnTNPLYTA-REMEHQFNDSGAKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 137 KIVFVNgeSAECLAQVVKENNMDTRLVV-FADSAGFVGR---------------------AATLTAVLRSQDTAWIDEFE 194
Cdd:PRK05677 126 LVCLAN--MAHLAEKVLPKTGVKHVIVTeVADMLPPLKRllinavvkhvkkmvpayhlpqAVKFNDALAKGAGQPVTEAN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 195 CAkltsPKHVAAIVCSSGTSGFPKGTEISHAAMINYMAHVK------VHDLKGHVSMWTPSMRWYCGLFIVIKAILDCSK 268
Cdd:PRK05677 204 PQ----ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRalmgsnLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 269 RIIVPDYDDDEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAhfkgELQQTLVKL---LPHTDVI 345
Cdd:PRK05677 280 NILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGM----ALQLATAERwkeVTGCAIC 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 346 LSYGMTDYGGL-CARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGW 424
Cdd:PRK05677 356 EGYGMTETSPVvSVNPSQAIQVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 425 LHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELD 504
Cdd:PRK05677 435 LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQ 514
|
490 500 510
....*....|....*....|....*....|....*....
gi 1820754837 505 ITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK05677 515 VMEHMRANLTGYKVPKA-VEFRDELPTTNVGKILRRELR 552
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
50-542 |
5.95e-32 |
|
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: 132.25 E-value: 5.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 50 PEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARY 129
Cdd:cd05923 15 PDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 130 FLSltkpkivfvNGESAECLAQVVKEnnmdtrlvVFADSAGFVGRAATLTAVLRSQD-TAWIDEFEcAKLTSPKHVAAIV 208
Cdd:cd05923 95 LIE---------RGEMTAAVIAVDAQ--------VMDAIFQSGVRVLALSDLVGLGEpESAGPLIE-DPPREPEQPAFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 209 CSSGTSGFPKGTEISHAAM---INYMAHVkVHDLKGHVSMWTPSMRWY--CGLFIVIKAILDCSKRIIVPDYDDDEGLCR 283
Cdd:cd05923 157 YTSGTTGLPKGAVIPQRAAesrVLFMSTQ-AGLRHGRHNVVLGLMPLYhvIGFFAVLVAALALDGTYVVVEEFDPADALK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 284 FIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILsYGMTD-YGGLCARQTK 362
Cdd:cd05923 236 LIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI-YGTTEaMNSLYMRDAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 363 YSKPGSCGFVCETgRLKVVDPNTGKVLGANKTGEIWAK--SSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVF 440
Cdd:cd05923 315 TGTEMRPGFFSEV-RIVRIGGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 441 LVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKeVTElditDLVKQnmpwYCRLH 520
Cdd:cd05923 393 ILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGT-LSA----DELDQ----FCRAS 463
|
490 500 510
....*....|....*....|....*....|
gi 1820754837 521 --AGVK------FMEKLPRTATGKIAKKQL 542
Cdd:cd05923 464 elADFKrprryfFLDELPKNAMNKVLRRQL 493
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
623-1099 |
6.15e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 132.32 E-value: 6.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:PRK06145 23 YRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNEESAENLMEAAKEenlqvrvMVIGSLPgfvslanilEEQVSRAEIDGFRCTK--IDNPHDLAMICSSSGTTGMPKG 780
Cdd:PRK06145 103 LLVDEEFDAIVALETPK-------IVIDAAA---------QADSRRLAQGGLEIPPqaAVAPTDLVRLMYTSGTTDRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 781 TELSYASLYNS------------------ITPVEEVHAKNeicawVPTIR--WHGGLnQCIEvimsnakwiifsdDNIKE 840
Cdd:PRK06145 167 VMHSYGNLHWKsidhvialgltaserllvVGPLYHVGAFD-----LPGIAvlWVGGT-LRIH-------------REFDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 841 IALCEIIQKHGVT--WLGTDTNFAILYVKMNifQKYPMPSLRkMVITGAPFTKELH-ETVAKIMPHTQILQCYGLTD--A 915
Cdd:PRK06145 228 EAVLAAIERHRLTcaWMAPVMLSRVLTVPDR--DRFDLDSLA-WCIGGGEKTPESRiRDFTRVFTRARYIDAYGLTEtcS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 916 GGLCVSQAKN-SKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGY 994
Cdd:PRK06145 305 GDTLMEAGREiEKIGSTGRALAHVEIRIADGA-GRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 995 YDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKN 1074
Cdd:PRK06145 383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQR 462
|
490 500
....*....|....*....|....*
gi 1820754837 1075 LPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK06145 463 LASF-KVPRQLKVRDELPRNPSGKV 486
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1206-1683 |
7.07e-32 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 132.95 E-value: 7.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFTVSS 1285
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAAKELKMNLKVVVM--------DKLDGYESVEEnVMKGHDTreiiEFKCHVTNPDDVALIVPSSGTTGLPKGT 1357
Cdd:PRK06018 121 FVPILEKIADKLPSVERYVVLtdaahmpqTTLKNAVAYEE-WIAEADG----DFAWKTFDENTAAGMCYTSGTTGDPKGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1358 EISHYSLFccLHPY--KNRTLVGHTC--IVTPTM-RWH---YGVlmAFRLVAANAKkLIVPDND-DAENFCQLIEKYQIT 1428
Cdd:PRK06018 196 LYSHRSNV--LHALmaNNGDALGTSAadTMLPVVpLFHansWGI--AFSAPSMGTK-LVMPGAKlDGASVYELLDTEKVT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1429 WFGTDP---FMIIKFIKSqllEKYRLPTLKVILSSGAHLRKEHLEVMREKlpDVFITNHYGMTDTACV------------ 1493
Cdd:PRK06018 271 FTAGVPtvwLMLLQYMEK---EGLKLPHLKMVVCGGSAMPRSMIKAFEDM--GVEVRHAWGMTEMSPLgtlaalkppfsk 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1494 VSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEALGPNK-IGELRVKAITIMQGYHKnpeTTKQAFDSDGWLRTGDLAYYDD 1572
Cdd:PRK06018 346 LPGDARLDVLQKQGYPPFGVEMKITDDAGKELPWDGKtFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1573 NGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKN--- 1649
Cdd:PRK06018 423 YGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKiak 502
|
490 500 510
....*....|....*....|....*....|....*.
gi 1820754837 1650 --LPDycrlrgGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK06018 503 wwMPD------DVAFVDAIPHTATGKILKTALREQF 532
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
608-1099 |
1.06e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 131.74 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 608 NRLSSKPDFVGQIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVS 687
Cdd:PRK13391 5 IHAQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 688 KLSARYFLSLMSPKVVFVNEESAENLMEAAKE-ENLQVRVMVI--GSLPGFVSLANILEeQVSRAEIDgfrctkiDNPHD 764
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSAAKLDVARALLKQcPGVRHRLVLDgdGELEGFVGYAEAVA-GLPATPIA-------DESLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 765 LAMIcSSSGTTGMPKG-----------TELSYASLYNS----------ITPVEEVHAKNEicAWVPTIRWHGGlnqcIEV 823
Cdd:PRK13391 157 TDML-YSSGTTGRPKGikrplpeqppdTPLPLTAFLQRlwgfrsdmvyLSPAPLYHSAPQ--RAVMLVIRLGG----TVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 824 IMSNakwiiFSddniKEIALcEIIQKHGVT---WLGTdtnfaiLYVKM-----NIFQKYPMPSLRKMVITGAPFTKELHE 895
Cdd:PRK13391 230 VMEH-----FD----AEQYL-ALIEEYGVThtqLVPT------MFSRMlklpeEVRDKYDLSSLEVAIHAAAPCPPQVKE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 896 TVAK----ImphtqILQCYGLTDAGGLCV--SQAKNSKPGSCGFVTKGIrIKIADEKtGIALGPKERGEICIKSEFMMKg 969
Cdd:PRK13391 294 QMIDwwgpI-----IHEYYAATEGLGFTAcdSEEWLAHPGTVGRAMFGD-LHILDDD-GAELPPGEPGTIWFEGGRPFE- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 970 YHKNPEQTKEAFDSDG-WLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIE 1048
Cdd:PRK13391 366 YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGE 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 1049 LPLAFVQKVVEKEVTEEELHDL---VNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK13391 446 EVKAVVQPVDGVDPGPALAAELiafCRQRLSRQ-KCPRSIDFEDELPRLPTGKL 498
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
61-551 |
1.09e-31 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 132.19 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVF 140
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 141 VNGESAECLaQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDTAWIdefeCAKLTSPKHVAAIVCSSGTSGFPKGT 220
Cdd:PRK06155 124 VEAALLAAL-EAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPA----PAAAVQPGDTAAILYTSGTTGPSKGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 221 EISHAAMINYMAHVkVHDL---KGHVSMWTPSMRWYCGLFIVIKAILDCSKRIIVPdydddeglcRFiekyevswfrCDS 297
Cdd:PRK06155 199 CCPHAQFYWWGRNS-AEDLeigADDVLYTTLPLFHTNALNAFFQALLAGATYVLEP---------RF----------SAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 298 CFPIRLVKFGVLSKYRL-PTLKILLFGGAHFKGELQQTLVKLLPHT--------------DVILSYGMTDYGGLCARQTK 362
Cdd:PRK06155 259 GFWPAVRRHGATVTYLLgAMVSILLSQPARESDRAHRVRVALGPGVpaalhaafrerfgvDLLDGYGSTETNFVIAVTHG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 363 YSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSS---YMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEV 439
Cdd:PRK06155 339 SQRPGSMGRLAPGFEARVVDEH-DQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 440 FLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYC-- 517
Cdd:PRK06155 417 RFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAvp 496
|
490 500 510
....*....|....*....|....*....|....
gi 1820754837 518 RLhagVKFMEKLPRTATGKIAKKQLKQIAKSYAT 551
Cdd:PRK06155 497 RY---VEFVAALPKTENGKVQKFVLREQGVTADT 527
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
623-1100 |
1.21e-31 |
|
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: 130.44 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGgiicpwdHVVSKLSARyflslmSPKv 702
Cdd:cd05945 12 EGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG-------HAYVPLDAS------SPA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 vfvneESAENLMEAAKEENLqvrvmvigslpgfvslanileeqvsraeidgfrctkIDNPHDLAMICSSSGTTGMPKGTE 782
Cdd:cd05945 78 -----ERIREILDAAKPALL------------------------------------IADGDDNAYIIFTSGSTGRPKGVQ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 783 LSYASL---YNSITPVEEVHAKNEICAWVP------TIRWHGGLnqcieviMSNAKWIIFSDDNIKEI-ALCEIIQKHGV 852
Cdd:cd05945 117 ISHDNLvsfTNWMLSDFPLGPGDVFLNQAPfsfdlsVMDLYPAL-------ASGATLVPVPRDATADPkQLFRFLAEHGI 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 853 T-WLGTDTNFAILYVKMNIFQKYpMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAGGLCVS------QAKN 925
Cdd:cd05945 190 TvWVSTPSFAAMCLLSPTFTPES-LPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYievtpeVLDG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 926 SKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSD---GWLHTKDIGYYDENGEIF 1002
Cdd:cd05945 269 YDRLPIGYAKPGAKLVILDED-GRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLF 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1003 FVNRIsDF---INYKAIKLSsaEIEGVLELHPSILKAVVVPVPH-ETDIELpLAFV--QKVVEKEVTEEELHDLvNKNLP 1076
Cdd:cd05945 348 YRGRL-DFqvkLNGYRIELE--EIEAALRQVPGVKEAVVVPKYKgEKVTEL-IAFVvpKPGAEAGLTKAIKAEL-AERLP 422
|
490 500
....*....|....*....|....
gi 1820754837 1077 WYCkLQAGIKFVNDFPRISTGKID 1100
Cdd:cd05945 423 PYM-IPRRFVYLDELPLNANGKID 445
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
30-544 |
1.23e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 131.70 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 30 PILKKCTNVGALVLEKLRSRPEFIAQVEavtGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAA 108
Cdd:PRK07470 1 PMSRRVMNLAHFLRQAARRFPDRIALVW---GDRSwTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 109 LYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGESAEcLAQVVKENNMDTRLVVFADSAGF-----------VGRAAT 177
Cdd:PRK07470 78 FRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHADFPE-HAAAVRAASPDLTHVVAIGGARAgldyealvarhLGARVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 178 LTAVLRSqDTAWIdefecakltspkhvaaiVCSSGTSGFPKGTEISHAAM----INYMAHVkVHDLKGH-VSMWTPSMRW 252
Cdd:PRK07470 157 NAAVDHD-DPCWF-----------------FFTSGTTGRPKAAVLTHGQMafviTNHLADL-MPGTTEQdASLVVAPLSH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 253 YCGLFIVI------KAILDCSKRIIVPDydddegLCRFIEKYEVS-WFRCDSCFPIrLVKFGVLSKYRLPTLKILLFGGA 325
Cdd:PRK07470 218 GAGIHQLCqvargaATVLLPSERFDPAE------VWALVERHRVTnLFTVPTILKM-LVEHPAVDRYDHSSLRYVIYAGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 326 HFKGELQQT-LVKLLPhtdVILSY-GMTDYGGLCARQTKY---------SKPGSCGFVcETG-RLKVVDPNtGKVLGANK 393
Cdd:PRK07470 291 PMYRADQKRaLAKLGK---VLVQYfGLGEVTGNITVLPPAlhdaedgpdARIGTCGFE-RTGmEVQIQDDE-GRELPPGE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 394 TGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQ 473
Cdd:PRK07470 366 TGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSE 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 474 VAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK07470 445 VAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARY-KLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
60-543 |
1.72e-31 |
|
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: 131.43 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 60 TGAET--TFAEMTEKSVKCALWLREQ-GVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKP 136
Cdd:cd05928 36 KGDEVkwSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 137 KIVFVNGESAECLAQVVKE-NNMDTRLVVFADS-AGFVgraaTLTAVLRSQDtawiDEFECAKlTSPKHVAAIVCSSGTS 214
Cdd:cd05928 116 KCIVTSDELAPEVDSVASEcPSLKTKLLVSEKSrDGWL----NFKELLNEAS----TEHHCVE-TGSQEPMAIYFTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 215 GFPKGTEISHAAminYMAHVKVH-----DLKGHVSMWTPS-------------MRWYCGLFIVIKAIldcskriivPDYD 276
Cdd:cd05928 187 GSPKMAEHSHSS---LGLGLKVNgrywlDLTASDIMWNTSdtgwiksawsslfEPWIQGACVFVHHL---------PRFD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 277 DDEGLcRFIEKYEVSWFrCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLvKLLPHTDVILSYGMTDYGGL 356
Cdd:cd05928 255 PLVIL-KTLSSYPITTF-CGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKW-KAQTGLDIYEGYGQTETGLI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 357 CA-RQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSS-----YMMNGYYNNPEATRRALDSDGWLhTGDL 430
Cdd:cd05928 332 CAnFKGMKIKPGSMGKASPPYDVQIIDDN-GNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYL-TGDR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 431 GYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVP-----GKEVTELDI 505
Cdd:cd05928 410 GIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPqflshDPEQLTKEL 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1820754837 506 TDLVKQ-NMPW-YCRlhaGVKFMEKLPRTATGKIAKKQLK 543
Cdd:cd05928 490 QQHVKSvTAPYkYPR---KVEFVQELPKTVTGKIQRNELR 526
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1177-1674 |
2.06e-31 |
|
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: 131.93 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1177 VNIAEETL-KFLKSKPDSIGQV----DALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMY 1251
Cdd:cd17634 52 LNLAANALdRHLRENGDRTAIIyegdDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACAR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1252 IGAISNTWDHELTPMTARNFLTLTSPKIVFTvsssAANLMEAAKELkmNLKVVVMDKLDGYESVEENVM----------- 1320
Cdd:cd17634 132 IGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT----ADGGVRAGRSV--PLKKNVDDALNPNVTSVEHVIvlkrtgsdidw 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1321 ---KGHDTREII-----EFKCHVTNPDDVALIVPSSGTTGLPKGTEISHYSlfcclHPYKNRTLVGHTCIVTPTMRWHY- 1391
Cdd:cd17634 206 qegRDLWWRDLIakaspEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGG-----YLVYAATTMKYVFDYGPGDIYWCt 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1392 --------GVLMAFRLVAANAKKLI---VPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKS--QLLEKYRLPTLKVIL 1458
Cdd:cd17634 281 advgwvtgHSYLLYGPLACGATTLLyegVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1459 SSGAHLRKEHLE-----VMREKLPdvfITNHYGMTDT--ACVVSAQNKFT-KLGSVGYVSSNVRIKMVDLDTEEAlGPNK 1530
Cdd:cd17634 361 SVGEPINPEAYEwywkkIGKEKCP---VVDTWWQTETggFMITPLPGAIElKAGSATRPVFGVQPAVVDNEGHPQ-PGGT 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1531 IGELrvkAITI-----MQGYHKNPETTKQAFDS--DGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLM 1603
Cdd:cd17634 437 EGNL---VITDpwpgqTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLV 513
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 1604 THPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQ---ELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKI 1674
Cdd:cd17634 514 AHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPElyaELRNWVRKEIGPLATPD-VVHWVDSLPKTRSGKI 586
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
599-1100 |
2.31e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 130.88 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 599 CANVGELVLNRLSSKPDFVGQIDafTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENhlntCVPVLAIL---YI 675
Cdd:PRK06188 11 GATYGHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLN----RPEVLMAIgaaQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 676 GGIICPW--------DH--VVSKLSARyflSLMSPKVVFVneESAENLmeAAKEENLQvRVMVIGSLPGFVSLAnileeq 745
Cdd:PRK06188 85 AGLRRTAlhplgsldDHayVLEDAGIS---TLIVDPAPFV--ERALAL--LARVPSLK-HVLTLGPVPDGVDLL------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 746 vsrAEIDGF---RCTKIDNPHDLAMICSSSGTTGMPKGTELSYASLynsitpveeVHAKNEICA---WVPTIRW------ 813
Cdd:PRK06188 151 ---AAAAKFgpaPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSI---------ATMAQIQLAeweWPADPRFlmctpl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 814 -HGGLNQCIEVIMSNAKWII---FSDDnikeiALCEIIQKHGVTWlgtdTNF--AILYVKMNifqkYP------MPSLRK 881
Cdd:PRK06188 219 sHAGGAFFLPTLLRGGTVIVlakFDPA-----EVLRAIEEQRITA----TFLvpTMIYALLD----HPdlrtrdLSSLET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 882 MVITGAPFTK-ELHETVAKIMPhtqIL-QCYGLTDAGgLCVS-----QAKNSKP---GSCGFVTKGIRIKIADEKtGIAL 951
Cdd:PRK06188 286 VYYGASPMSPvRLAEAIERFGP---IFaQYYGQTEAP-MVITylrkrDHDPDDPkrlTSCGRPTPGLRVALLDED-GREV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 952 GPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHP 1031
Cdd:PRK06188 361 AQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHP 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1032 SILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVN--KNLPWYCKlqaGIKFVNDFPRISTGKID 1100
Cdd:PRK06188 440 AVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKerKGSVHAPK---QVDFVDSLPLTALGKPD 507
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
629-1099 |
2.71e-31 |
|
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: 129.16 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNEE 708
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAENLmeaakeenlqvrvmvigslpgfvslanileeqvsraeidgfrctkidNPHDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd05969 82 LYERT-----------------------------------------------DPEDPTLLHYTSGTTGTPKGVLHVHDAM 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 ---YNSITPVEEVHAKNEI-C----AWVPTIR---WHGGLNQCIEVI----MSNAKWIifsddnikeialcEIIQKHGVT 853
Cdd:cd05969 115 ifyYFTGKYVLDLHPDDIYwCtadpGWVTGTVygiWAPWLNGVTNVVyegrFDAESWY-------------GIIERVKVT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 854 -WLGTDTNFAILyVKMNIF--QKYPMPSLRKMVITGAPFTKEL----HETVAkiMPhtqILQCYGLTDAGGLCVSQ--AK 924
Cdd:cd05969 182 vWYTAPTAIRML-MKEGDElaRKYDLSSLRFIHSVGEPLNPEAirwgMEVFG--VP---IHDTWWQTETGSIMIANypCM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 925 NSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEF--MMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIF 1002
Cdd:cd05969 256 PIKPGSMGKPLPGVKAAVVDEN-GNELPPGTKGILALKPGWpsMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFW 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1003 FVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNknlpwYCKLQ 1082
Cdd:cd05969 334 FVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIIN-----FVRQK 408
|
490 500
....*....|....*....|....
gi 1820754837 1083 AG-------IKFVNDFPRISTGKI 1099
Cdd:cd05969 409 LGahvapreIEFVDNLPKTRSGKI 432
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
623-1099 |
2.84e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 131.05 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:PRK07786 38 FLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVnEESAENLMEAAKE-ENLQVRVMVIGSLPGFVSLAniLEEQVSRaeiDGFRCTKIDNPHDL-AMICSSSGTTGMPKG 780
Cdd:PRK07786 118 VVT-EAALAPVATAVRDiVPLLSTVVVAGGSSDDSVLG--YEDLLAE---AGPAHAPVDIPNDSpALIMYTSGTTGRPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 781 TELSYASLY-NSITPVEEVHA-KNEICAWVPTIRWH-GGLNQCIEVIMSNAKWIIFSDDNIKEIALCEIIQKHGVT---- 853
Cdd:PRK07786 192 AVLTHANLTgQAMTCLRTNGAdINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTgifl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 854 ----WLgtdtnfAILYVkmnifQKYPMPSLRKMVIT--GAPFTKELHETVAKIMPHTQILQCYGLTDAGGL-CVSQAKNS 926
Cdd:PRK07786 272 vpaqWQ------AVCAE-----QQARPRDLALRVLSwgAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVtCMLLGEDA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 927 --KPGSCGFVTKGIRIKIADEKTG-IALGpkERGEICIKSEFMMKGYHKNPEQTKEAFDSdGWLHTKDIGYYDENGEIFF 1003
Cdd:PRK07786 341 irKLGSVGKVIPTVAARVVDENMNdVPVG--EVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1004 VNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEV-TEEELHDLVNKNLPWYcKLQ 1082
Cdd:PRK07786 418 VDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAAlTLEDLAEFLTDRLARY-KHP 496
|
490
....*....|....*..
gi 1820754837 1083 AGIKFVNDFPRISTGKI 1099
Cdd:PRK07786 497 KALEIVDALPRNPAGKV 513
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
309-539 |
4.68e-31 |
|
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: 125.69 E-value: 4.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 309 LSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDYGglCARQTKYSKP-----GSCGFVCETGRLKVVDP 383
Cdd:cd17638 109 RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAG--VATMCRPGDDaetvaTTCGRACPGFEVRIADD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 384 ntgkvlganktGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEA 463
Cdd:cd17638 187 -----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEG 255
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 464 LIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAK 539
Cdd:cd17638 256 ALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANY-KVPRFVRFLDELPRNASGKVMK 330
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1191-1679 |
4.70e-31 |
|
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: 129.37 E-value: 4.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDaltGKVQ-TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheltPMTA- 1268
Cdd:cd05920 29 PDRIAVVD---GDRRlTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV---------PVLAl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1269 --------RNFLTLTSPKIVftvsssaanlmeaakelkmnlkvVVMDKLDGYESVEenvmkghDTREIIEfkCHvtnpDD 1340
Cdd:cd05920 97 pshrrselSAFCAHAEAVAY-----------------------IVPDRHAGFDHRA-------LARELAE--SI----PE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1341 VALIVPSSGTTGLPKGTEISH----YSL-----FCCLHPyKNRTL----VGH----TCivtPTMrwhYGVLMAfrlvaan 1403
Cdd:cd05920 141 VALFLLSGGTTGTPKLIPRTHndyaYNVrasaeVCGLDQ-DTVYLavlpAAHnfplAC---PGV---LGTLLA------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1404 AKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMRE----KLPDV 1479
Cdd:cd05920 207 GGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPvlgcTLQQV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1480 F-----ITNHYGMTDTACVVsaqnkftkLGSVGY-VSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTK 1553
Cdd:cd05920 287 FgmaegLLNYTRLDDPDEVI--------IHTQGRpMSPDDEIRVVDEEGNP-VPPGEEGELLTRGPYTIRGYYRAPEHNA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1554 QAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVV--Q 1631
Cdd:cd05920 358 RAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVlrD 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 1632 VPNKSV------TEQELISYvekNLPDycrlrgGVKIVDQLPRTTTGKIARKQL 1679
Cdd:cd05920 438 PPPSAAqlrrflRERGLAAY---KLPD------RIEFVDSLPLTAVGKIDKKAL 482
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
80-543 |
6.57e-31 |
|
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: 128.65 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 80 LREQGVQPGDIIGICTHNHLESyvpLLAALYLGAISNPwdnelspmtaryflsltKPKIVFvngESAECLAQVVKENNMD 159
Cdd:cd05929 34 AAAEGVWIADGVYIYLINSILT---VFAAAAAWKCGAC-----------------PAYKSS---RAPRAEACAIIEIKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 160 TRLVVFADSAGFVGRAATLTAVLRSQDTAWIDEfecakltspkhVAA---IVCSSGTSGFPKGTEISHAaminymaHVKV 236
Cdd:cd05929 91 ALVCGLFTGGGALDGLEDYEAAEGGSPETPIED-----------EAAgwkMLYSGGTTGRPKGIKRGLP-------GGPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 237 HDLkgHVSMWTPSMRWYCG--------------LFIVIKAILDCSKRIIVPDYDDDEGLcRFIEKYEVSWFRCDSCFPIR 302
Cdd:cd05929 153 DND--TLMAAALGFGPGADsvylspaplyhaapFRWSMTALFMGGTLVLMEKFDPEEFL-RLIERYRVTFAQFVPTMFVR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 303 LVKF--GVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTdVILSYGMTDYGGLCA--RQTKYSKPGSCGFVCEtGRL 378
Cdd:cd05929 230 LLKLpeAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGQGLTIinGEEWLTHPGSVGRAVL-GKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 379 KVVDPNtGKVLGANKTGEIWAKSSYMMNgYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISP 458
Cdd:cd05929 308 HILDED-GNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 459 AEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLV---KQNMPWYCRLHAgVKFMEKLPRTATG 535
Cdd:cd05929 386 QEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIaflRDRLSRYKCPRS-IEFVAELPRDDTG 464
|
....*...
gi 1820754837 536 KIAKKQLK 543
Cdd:cd05929 465 KLYRRLLR 472
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
57-547 |
7.25e-31 |
|
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: 129.50 E-value: 7.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 57 EAVTGAET--TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIsnpwdnelsPMTA------- 127
Cdd:COG1021 42 IAVVDGERrlSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI---------PVFAlpahrra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 128 --RYFLSLTKPK--IV--FVNGESAECLAQVVKENNMDTRLVVFADSAG-FVGraatLTAVLRSQdtawIDEFECAklTS 200
Cdd:COG1021 113 eiSHFAEQSEAVayIIpdRHRGFDYRALARELQAEVPSLRHVLVVGDAGeFTS----LDALLAAP----ADLSEPR--PD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 201 PKHVAAIVCSSGTSGFPKGTEISHAAMInYMAHVKVHdlkghVSMWTPSMRWYCGLFIVIKAILDC----------SKRI 270
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPKLIPRTHDDYL-YSVRASAE-----ICGLDADTVYLAALPAAHNFPLSSpgvlgvlyagGTVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 271 IVPDYDDDEgLCRFIEKYEVSwfrCDSCFP---IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTdVILS 347
Cdd:COG1021 257 LAPDPSPDT-AFPLIERERVT---VTALVPplaLLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCT-LQQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDygGLCarqtKYSKPG-SCGFVCET-GR-------LKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRA 418
Cdd:COG1021 332 FGMAE--GLV----NYTRLDdPEEVILTTqGRpispddeVRIVDED-GNPVPPGEVGELLTRGPYTIRGYYRAPEHNARA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 419 LDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINyRA-IKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVakVP- 496
Cdd:COG1021 405 FTPDGFYRTGDLVRRTPDGYLVVEGRAKDQIN-RGgEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFV--VPr 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 497 GKEVTELDITD-LVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQIAK 547
Cdd:COG1021 482 GEPLTLAELRRfLRERGLAAF-KLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
204-546 |
7.88e-31 |
|
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: 125.14 E-value: 7.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 204 VAAIVCSSGTSGFPKGTEISHAAMinYMAHVKVHDLKGhvsmWTPSMRWYC--------GLFIVIKAILdCSKRIIVPDY 275
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANL--LASAAGLHSRLG----FGGGDSWLLslplyhvgGLAILVRSLL-AGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 276 DDDEGlcrfiEKYEVSWFRCDSCFPIRLVKfgVL----SKYRLPTLKILLFGGAHFKGELQQTLVKLlpHTDVILSYGMT 351
Cdd:cd17630 75 NQALA-----EDLAPPGVTHVSLVPTQLQR--LLdsgqGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 352 DYGG-LCARQTKYSKPGSCGFVCETGRLKVVDPntgkvlganktGEIWAKSSYMMNGYYNNPEatRRALDSDGWLHTGDL 430
Cdd:cd17630 146 ETASqVATKRPDGFGRGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 431 GYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHninEEHAMAFVAKV-PGKEVTELDITDLV 509
Cdd:cd17630 213 GELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPD---EELGQRPVAVIvGRGPADPAELRAWL 289
|
330 340 350
....*....|....*....|....*....|....*..
gi 1820754837 510 KQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLKQIA 546
Cdd:cd17630 290 KDKLARFKLPKR-IYPVPELPRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
52-542 |
8.16e-31 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 128.62 E-value: 8.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 52 FIAQVE------AVT--GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDnels 123
Cdd:cd17651 1 FERQAArtpdapALVaeGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 124 pmtARYflsltkPkivfvngesAECLAQVVKENNMdtRLVVFADSAGFV--GRAATLTAVLRSQDTAwIDEFECAKLTSP 201
Cdd:cd17651 77 ---PAY------P---------AERLAFMLADAGP--VLVLTHPALAGElaVELVAVTLLDQPGAAA-GADAEPDPALDA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 202 KHVAAIVCSSGTSGFPKGTEISHAAMINYMA-HVKVHDLkghvsmwTPSMR--WYCGL-FIV----IKAILDCSKRIIVP 273
Cdd:cd17651 136 DDLAYVIYTSGSTGRPKGVVMPHRSLANLVAwQARASSL-------GPGARtlQFAGLgFDVsvqeIFSTLCAGATLVLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 274 DYD---DDEGLCRFIEKYEVSwfRCDSCFPI--RLVKFGVLSKYRLPTLKILLFGG-AHFKGELQQTLVKLLPHTDVILS 347
Cdd:cd17651 209 PEEvrtDPPALAAWLDEQRIS--RVFLPTVAlrALAEHGRPLGVRLAALRYLLTGGeQLVLTEDLREFCAGLPGLRLHNH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTD-----YGGLCARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSD 422
Cdd:cd17651 287 YGPTEthvvtALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 423 GWL------HTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVP 496
Cdd:cd17651 366 PFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDP 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1820754837 497 GKEVTELDITDLVKQNMPWYCrLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:cd17651 446 EAPVDAAELRAALATHLPEYM-VPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1186-1679 |
1.23e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 127.43 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1186 FLKSKPDSIGQVDAlTGKVqTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTP 1265
Cdd:cd12115 8 QAARTPDAIALVCG-DESL-TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAA-------YVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1266 MTARNfltlTSPKIVFTVSSSAANLMeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchVTNPDDVALIV 1345
Cdd:cd12115 79 LDPAY----PPERLRFILEDAQARLV-------------------------------------------LTDPDDLAYVI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1346 PSSGTTGLPKGTEISHYS----LFCCLHPYKNRTLVGhTCIVTPTMrWHYGVLMAFRLVAANAKklIVPdnddAENFCQL 1421
Cdd:cd12115 112 YTSGSTGRPKGVAIEHRNaaafLQWAAAAFSAEELAG-VLASTSIC-FDLSVFELFGPLATGGK--VVL----ADNVLAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1422 IE---KYQITWFGTDPFMIikfikSQLLEKYRLPT-LKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTD-----TAC 1492
Cdd:cd12115 184 PDlpaAAEVTLINTVPSAA-----AELLRHDALPAsVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEdttysTVA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1493 VVSAQNKFTKlgSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWL------RTGD 1566
Cdd:cd12115 259 PVPPGASGEV--SIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1567 LAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYV 1646
Cdd:cd12115 336 LVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHL 415
|
490 500 510
....*....|....*....|....*....|...
gi 1820754837 1647 EKNLPDYCrLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:cd12115 416 GTRLPAYM-VPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
36-546 |
1.62e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 128.71 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 36 TNVGALVLEKLRSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIs 115
Cdd:PRK06164 10 DTLASLLDAHARARPDAVALIDE--DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 116 npwdneLSPMTARY-------FLSLTKPKIVFVNG-----ESAECLAQVVKENNMDTRLVVFADSAgfvgrAATLTAVLR 183
Cdd:PRK06164 87 ------VIAVNTRYrshevahILGRGRARWLVVWPgfkgiDFAAILAAVPPDALPPLRAIAVVDDA-----ADATPAPAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 184 SQDTAWIDEFECAKLT------SPKHVAAIV-CSSGTSGFPK------GTEISHAAMInymAHVKVHDlKGHVSMwtpSM 250
Cdd:PRK06164 156 GARVQLFALPDPAPPAaageraADPDAGALLfTTSGTTSGPKlvlhrqATLLRHARAI---ARAYGYD-PGAVLL---AA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 251 RWYCGLF---IVIKAILDCSKRIIVPDYDDDEGLcRFIEKYEVSW-FRCDSCFpIRLVKFGVLSKyRLPTLKilLFGGAH 326
Cdd:PRK06164 229 LPFCGVFgfsTLLGALAGGAPLVCEPVFDAARTA-RALRRHRVTHtFGNDEML-RRILDTAGERA-DFPSAR--LFGFAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 327 FKGELQQtLVKLLPHTDVILS--YGMTDYGGLCARQTKySKPGSC-----GFVCET-GRLKVVDPNTGKVLGANKTGEIW 398
Cdd:PRK06164 304 FAPALGE-LAALARARGVPLTglYGSSEVQALVALQPA-TDPVSVrieggGRPASPeARVRARDPQDGALLPDGESGEIE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 399 AKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVP 478
Cdd:PRK06164 382 IRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVG 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 479 VPHNINEEhAMAFVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATG---KIAKKQLKQIA 546
Cdd:PRK06164 462 ATRDGKTV-PVAFVIPTDGASPDEAGLMAACREALAGF-KVPARVQVVEAFPVTESAngaKIQKHRLREMA 530
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
61-544 |
2.18e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 128.36 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVF 140
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 141 VNGESAEcLAQVVKENNMDTRLVVfadsagfVGRAATLTAVLRSQDTawIDEfecaklTSPKHV---------AAIVCSS 211
Cdd:PRK07786 120 TEAALAP-VATAVRDIVPLLSTVV-------VAGGSSDDSVLGYEDL--LAE------AGPAHApvdipndspALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 212 GTSGFPKGTEISHAAMI-NYMAHVKVH--DLKGHVSMWTPSMRWYCGLFIVIKAILDCSKRIIVP--DYDDDEgLCRFIE 286
Cdd:PRK07786 184 GTTGRPKGAVLTHANLTgQAMTCLRTNgaDINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPlgAFDPGQ-LLDVLE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 287 KYEVSwfrcdSCFPIRLVKFGVLS----KYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDYGGL-CARQT 361
Cdd:PRK07786 263 AEKVT-----GIFLVPAQWQAVCAeqqaRPRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVtCMLLG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 362 K--YSKPGSCGFVCETGRLKVVDPNTGKVlGANKTGEIWAKSSYMMNGYYNNPEATRRALDSdGWLHTGDLGYYDNDGEV 439
Cdd:PRK07786 338 EdaIRKLGSVGKVIPTVAARVVDENMNDV-PVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYV 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 440 FLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTEL-DITDLVKQNMPWYCR 518
Cdd:PRK07786 416 WVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLeDLAEFLTDRLARYKH 495
|
490 500
....*....|....*....|....*.
gi 1820754837 519 LHAgVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK07786 496 PKA-LEIVDALPRNPAGKVLKTELRE 520
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
76-543 |
2.50e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 126.79 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 76 CALWLREQGVQPGDIIGICTHNHLEsYVPLLAAL-----YLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGESAECLA 150
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFT-YIELSFAVayaggRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 151 QVVKENNMDTrlvVFADSAGFVGRAATLTAVLrsqdtawidefecaklTSPKHVAAIVCSSGTSGFPKGTEISHAAMI-N 229
Cdd:cd05922 85 DALPASPDPG---TVLDADGIRAARASAPAHE----------------VSHEDLALLLYTSGSTGSPKLVRLSHQNLLaN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 230 YMAHVKVHDLKGH-VSMWTPSMRWYCGLFIVIKAILDCSKRIIVPDYDDDEGLCRFIEKYevswfRCDScFPIRLVKFGV 308
Cdd:cd05922 146 ARSIAEYLGITADdRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREH-----GATG-LAGVPSTYAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 309 LS-----KYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDygglCARQTKY-------SKPGSCGFVCETG 376
Cdd:cd05922 220 LTrlgfdPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTE----ATRRMTYlpperilEKPGSIGLAIPGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 377 RLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKI 456
Cdd:cd05922 296 EFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 457 SPAEIEALIQQHPAVFQVAVVPVPHNINEEHAmAFVAKVPGKEVTelDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGK 536
Cdd:cd05922 375 SPTEIEAAARSIGLIIEAAAVGLPDPLGEKLA-LFVTAPDKIDPK--DVLRSLAERLPPY-KVPATVRVVDELPLTASGK 450
|
....*..
gi 1820754837 537 IAKKQLK 543
Cdd:cd05922 451 VDYAALR 457
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1191-1679 |
2.76e-30 |
|
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: 127.01 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDalTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARN 1270
Cdd:cd17646 12 PDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 FLTLTSPKIVFTVSSSAANLMEAAkelkmNLKVVVMDKLDGYESVEENVmkghdtreiiefkchVTNPDDVALIVPSSGT 1350
Cdd:cd17646 90 MLADAGPAVVLTTADLAARLPAGG-----DVALLGDEALAAPPATPPLV---------------PPRPDNLAYVIYTSGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISHyslfcclHPYKNRTLvghtcivtpTMRWHYG------VLM----AF---------------RLVAAnak 1405
Cdd:cd17646 150 TGRPKGVMVTH-------AGIVNRLL---------WMQDEYPlgpgdrVLQktplSFdvsvwelfwplvagaRLVVA--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1406 kliVPDND-DAENFCQLIEKYQITWFGTDPFMIIKFIksQLLEKYRLPTLKVILSSGAHLRKEHLEVMREkLPDVFITNH 1484
Cdd:cd17646 211 ---RPGGHrDPAYLAALIREHGVTTCHFVPSMLRVFL--AEPAAGSCASLRRVFCSGEALPPELAARFLA-LPGAELHNL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVVSA----QNKFTKLGSVGYVSSNVRIKMVDldteEALGP---NKIGELRVKAITIMQGYHKNPETTKQAFD 1557
Cdd:cd17646 285 YGPTEAAIDVTHwpvrGPAETPSVPIGRPVPNTRLYVLD----DALRPvpvGVPGELYLGGVQLARGYLGRPALTAERFV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1558 SDGW------LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQ 1631
Cdd:cd17646 361 PDPFgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVP 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1820754837 1632 VP-NKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:cd17646 441 AAgAAGPDTAALRAHLAERLPEY-MVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1198-1682 |
4.18e-30 |
|
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: 126.68 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1198 DALTGKVqTYADMSERSIKCALWLKKqGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSP 1277
Cdd:cd05909 2 DTLGTSL-TYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1278 KIVFTvsssAANLMEAAKELKMNL-----KVVVMDKLDGYESVEENV-----MKGHDTREIIEFKCHVTNPDDVALIVPS 1347
Cdd:cd05909 80 KTVLT----SKQFIEKLKLHHLFDveydaRIVYLEDLRAKISKADKCkaflaGKFPPKWLLRIFGVAPVQPDDPAVILFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1348 SGTTGLPKGTEISH-------YSLFCCLHPYKNRTLVG-----HT-----CIVTPtmrwhygVLMAFRLVAAnakklivP 1410
Cdd:cd05909 156 SGSEGLPKGVVLSHknllanvEQITAIFDPNPEDVVFGalpffHSfgltgCLWLP-------LLSGIKVVFH-------P 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1411 DNDDAENFCQLIEKYQIT-WFGTDPFM--IIKFIksqllEKYRLPTLKVILSsGAHLRKEHLEVMREKLPDVFITNHYGM 1487
Cdd:cd05909 222 NPLDYKKIPELIYDKKATiLLGTPTFLrgYARAA-----HPEDFSSLRLVVA-GAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1488 TDTACVVSAQNKFT--KLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTG 1565
Cdd:cd05909 296 TECSPVISVNTPQSpnKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1566 DLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTH-PAVLQAAVLGIPnevDEQHPKAFVVQVPNKSVTEQELIS 1644
Cdd:cd05909 375 DIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVP---DGRKGEKIVLLTTTTDTDPSSLND 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1820754837 1645 YVEK----NL--PDYcrlrggVKIVDQLPRTTTGKIARKQLRDM 1682
Cdd:cd05909 452 ILKNagisNLakPSY------IHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1191-1679 |
8.07e-30 |
|
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: 124.89 E-value: 8.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDALTgkVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTArn 1270
Cdd:cd17650 1 PDAIAVSDATR--QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGA-------YVPIDP-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 flTLTSPKIVFTVSSSAANLMeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchVTNPDDVALIVPSSGT 1350
Cdd:cd17650 70 --DYPAERLQYMLEDSGAKLL-------------------------------------------LTQPEDLAYVIYTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISHYSLFCCLHPYKNR-TLVGHTCIVTPTMRWHYGVLMA-FRLVAANAKKLIVPDND---DAENFCQLIEKY 1425
Cdd:cd17650 105 TGKPKGVMVEHRNVAHAAHAWRREyELDSFPVRLLQMASFSFDVFAGdFARSLLNGGTLVICPDEvklDPAALYDLILKS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1426 QITWFGTDPFMIIKFIKSQLLEKYRLPTLKV-ILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDtACVVSA--QNKFTK 1502
Cdd:cd17650 185 RITLMESTPALIRPVMAYVYRNGLDLSAMRLlIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTE-ATIDSTyyEEGRDP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1503 LGSVGYVS-----SNVRIKMVDldteEALGPNKIG---ELRVKAITIMQGYHKNPETTKQAFDSDGW------LRTGDLA 1568
Cdd:cd17650 264 LGDSANVPigrplPNTAMYVLD----ERLQPQPVGvagELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1569 YYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVlgIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEK 1648
Cdd:cd17650 340 RWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV--AVREDKGGEARLCAYVVAAATLNTAELRAFLAK 417
|
490 500 510
....*....|....*....|....*....|.
gi 1820754837 1649 NLPDYCrLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:cd17650 418 ELPSYM-IPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1331-1681 |
9.24e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 129.27 E-value: 9.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1331 FKCHVTNPDDVALIVPSSGTTGLPKGTEISHYSLFC-------CLHPYKNRTLVGhtciVTPTmrWH-YGVLMAFRLVAA 1402
Cdd:PRK08633 774 LYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSnieqisdVFNLRNDDVILS----SLPF--FHsFGLTVTLWLPLL 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1403 NAKKLI-VPDNDDAENFCQLIEKYQITW-FGTDPFMIIkFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVF 1480
Cdd:PRK08633 848 EGIKVVyHPDPTDALGIAKLVAKHRATIlLGTPTFLRL-YLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKF-GIR 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1481 ITNHYGMTDTACVVS--------AQN---KFTKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNP 1549
Cdd:PRK08633 926 ILEGYGATETSPVASvnlpdvlaADFkrqTGSKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDP 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1550 ETTKQA---FDSDGWLRTGDLAYYDDNGEIYIVDRISDF-------INFRSINvspAEIETVLMTHPAVLqaAVLGIPne 1619
Cdd:PRK08633 1006 EKTAEVikdIDGIGWYVTGDKGHLDEDGFLTITDRYSRFakiggemVPLGAVE---EELAKALGGEEVVF--AVTAVP-- 1078
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1620 vDEQHPKAFVVQVPNKSVTEQELISYV-EKNLPDYCrLRGGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK08633 1079 -DEKKGEKLVVLHTCGAEDVEELKRAIkESGLPNLW-KPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
629-1099 |
1.45e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 126.08 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGI---ICP------WDHVVSKLSARYFLSLMS 699
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIlvtINPayrlseLEYALNQSGCKALIAADG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 700 PK----VVFVNE------ESAENLMEAAKEENLQvRVMVIGS--LPGFVSLANILE--EQVSRAEIDGFRCTKidNPHDL 765
Cdd:PRK08315 125 FKdsdyVAMLYElapelaTCEPGQLQSARLPELR-RVIFLGDekHPGMLNFDELLAlgRAVDDAELAARQATL--DPDDP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 766 AMICSSSGTTGMPKGTELSYASLYN---SITPVEEVHAKNEICAWVPtirwhggLNQCIEVIMSN------AKWIIFSDD 836
Cdd:PRK08315 202 INIQYTSGTTGFPKGATLTHRNILNngyFIGEAMKLTEEDRLCIPVP-------LYHCFGMVLGNlacvthGATMVYPGE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 837 NIKEIALCEIIQKHGVTWL-GTDTNF-AILYVKMniFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTD 914
Cdd:PRK08315 275 GFDPLATLAAVEEERCTALyGVPTMFiAELDHPD--FARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 915 AGglcvsqaknskPGSC---------------GFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKE 979
Cdd:PRK08315 353 TS-----------PVSTqtrtddplekrvttvGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 980 AFDSDGWLHTKDIGYYDENGEIFFVNRISDFInykaIK----LSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQ 1055
Cdd:PRK08315 422 AIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI----IRggenIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWII 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1820754837 1056 KVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK08315 498 LRPGATLTEEDVRDFCRGKIAHY-KIPRYIRFVDEFPMTVTGKI 540
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
348-552 |
1.69e-29 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 125.94 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDYGGLCA----RQTKYSkpGSCGFVCETGRLKVVDpNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALdSDG 423
Cdd:PRK08974 357 YGLTECSPLVSvnpyDLDYYS--GSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 424 WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKvPGKEVTEl 503
Cdd:PRK08974 433 WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVK-KDPSLTE- 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 504 diTDLVKqnmpwYCRLH-AG------VKFMEKLPRTATGKIAKKQLKQIAKSYATN 552
Cdd:PRK08974 511 --EELIT-----HCRRHlTGykvpklVEFRDELPKSNVGKILRRELRDEARAKVDN 559
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
63-543 |
2.80e-29 |
|
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: 122.96 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVN 142
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 143 GESAeCLAQVVKENNMDTRLVV--FADSAGFVGRAATLTAVLRSQDTAwideFECAKLTspkhvaaivcssgtsgFPKGT 220
Cdd:cd05919 90 ADDI-AYLLYSSGTTGPPKGVMhaHRDPLLFADAMAREALGLTPGDRV----FSSAKMF----------------FGYGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 221 eishaaminymahvkvhdlkGHvSMWTPsmrWYCGlfivikaildcSKRIIVPDYDDDEGLCRFIEKYEVSWFRCDSCFP 300
Cdd:cd05919 149 --------------------GN-SLWFP---LAVG-----------ASAVLNPGWPTAERVLATLARFRPTVLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 301 IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVK--LLPHTDVIlsyGMTDYGG--LCARQTKYsKPGSCGFVCETG 376
Cdd:cd05919 194 ANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEhfGGPILDGI---GATEVGHifLSNRPGAW-RLGSTGRPVPGY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 377 RLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKI 456
Cdd:cd05919 270 EIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 457 SPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTEL---DITDLVKQNMPWYCRLHAgVKFMEKLPRTA 533
Cdd:cd05919 348 SPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRR-IAFVDELPRTA 426
|
490
....*....|
gi 1820754837 534 TGKIAKKQLK 543
Cdd:cd05919 427 TGKLQRFKLR 436
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
623-1042 |
3.56e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 124.69 E-value: 3.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWL-RKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPK 701
Cdd:PRK08314 31 FYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 702 VVFVNEESAENLMEAAkeENLQVRVMVIGSLPGF------VSLANILEEQVSRAEIDGFRCTKIDN-------------- 761
Cdd:PRK08314 111 VAIVGSELAPKVAPAV--GNLRLRHVIVAQYSDYlpaepeIAVPAWLRAEPPLQALAPGGVVAWKEalaaglappphtag 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 762 PHDLAMICSSSGTTGMPKG----------TELSyASLYNSITPvEEVHakneiCAWVPTirWH-----GGLNQCIE---- 822
Cdd:PRK08314 189 PDDLAVLPYTSGTTGVPKGcmhthrtvmaNAVG-SVLWSNSTP-ESVV-----LAVLPL--FHvtgmvHSMNAPIYagat 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 823 -VIMsnAKWiifsdDniKEIALcEIIQKHGVT-WLGTDTnfailyvkMNI-------FQKYPMPSLRKMVITGAPftkeL 893
Cdd:PRK08314 260 vVLM--PRW-----D--REAAA-RLIERYRVThWTNIPT--------MVVdflaspgLAERDLSSLRYIGGGGAA----M 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 894 HETVA-KIMPHTQI--LQCYGLTD-AGGLCVSQAKNSKPGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKG 969
Cdd:PRK08314 318 PEAVAeRLKELTGLdyVEGYGLTEtMAQTHSNPPDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKG 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 970 YHKNPEQTKEAF-DSDG--WLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVP 1042
Cdd:PRK08314 398 YWNRPEATAEAFiEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP 473
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1191-1679 |
3.69e-29 |
|
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: 122.80 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAisntwdheltpmtARN 1270
Cdd:cd17643 1 PEAVAVVDE--DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGG-------------AYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 FLTLTSP--KIVFTVSSSAANLMeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchVTNPDDVALIVPSS 1348
Cdd:cd17643 66 PIDPAYPveRIAFILADSGPSLL-------------------------------------------LTDPDDLAYVIYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1349 GTTGLPKGTEISH---YSLF-CCLHPYKnrtlvghtciVTPTMRW----HY----------GVLmafrlvaANAKKLIVP 1410
Cdd:cd17643 103 GSTGRPKGVVVSHanvLALFaATQRWFG----------FNEDDVWtlfhSYafdfsvweiwGAL-------LHGGRLVVV 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1411 DND---DAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLE--VMREKLPDVFITNHY 1485
Cdd:cd17643 166 PYEvarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRpwAGRFGLDRPQLVNMY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1486 GMTDTaCV------VSAQNKFTKLGSV-GYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAFDS 1558
Cdd:cd17643 246 GITET-TVhvtfrpLDAADLPAAAASPiGRPLPGLRVYVLDADGRP-VPPGVVGELYVSGAGVARGYLGRPELTAERFVA 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1559 DGW-------LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQ 1631
Cdd:cd17643 324 NPFggpgsrmYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVA 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 1632 VPNKSVTEQELISYVEKNLPDYCRLRGGVkIVDQLPRTTTGKIARKQL 1679
Cdd:cd17643 404 DDGAAADIAELRALLKELLPDYMVPARYV-PLDALPLTVNGKLDRAAL 450
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1340-1676 |
3.84e-29 |
|
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: 120.44 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1340 DVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRTL---VGHTCIVTPTMRWHYGVLMAFRLVAANAKKLIVPDNDDAE 1416
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLnwvVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1417 NFCQLIEKYQITWFGTDPFMIIKFI---KSQLLEkyrLPTLKVILSSGAHLRKEHLEVMrEKLPDVFITNHYGMTDT--A 1491
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVselKSANAT---VPSLRLIGYGGSRAIAADVRFI-EATGLTNTAQVYGLSETgtA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1492 CVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEalGPN-KIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYY 1570
Cdd:cd17635 158 LCLPTDDDSIEINAVGRPYPGVDVYLAATDGIA--GPSaSFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1571 DDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVV--QVPNKSVTeQELISYVEK 1648
Cdd:cd17635 235 REDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVasAELDENAI-RALKHTIRR 313
|
330 340
....*....|....*....|....*...
gi 1820754837 1649 NLPDYCRLRgGVKIVDQLPRTTTGKIAR 1676
Cdd:cd17635 314 ELEPYARPS-TIVIVTDIPRTQSGKVKR 340
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
624-1099 |
6.08e-29 |
|
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: 122.16 E-value: 6.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 624 TGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvvskLSARYflslmspkvv 703
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVP-------LFALF---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 704 fvneesaenlmeaaKEENLQVRvmvigslpgfvsLANileeqvSRAeidgfRCTKIDNPHDLAMICSSSGTTGMPKGTEL 783
Cdd:cd05971 66 --------------GPEALEYR------------LSN------SGA-----SALVTDGSDDPALIIYTSGTTGPPKGALH 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 784 SYASLYNSITPVEEVH---AKNEICAWVPT-IRWHGGLnqcIEVIMSNAKWII---------FSDDnikeiALCEIIQKH 850
Cdd:cd05971 109 AHRVLLGHLPGVQFPFnlfPRDGDLYWTPAdWAWIGGL---LDVLLPSLYFGVpvlahrmtkFDPK-----AALDLMSRY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 851 GVTwlgtdtnFAIL---YVKMNIFQKYPMP----SLRKMVITGAPFTKELhETVAKIMPHTQILQCYGLTDAGGLCVSQA 923
Cdd:cd05971 181 GVT-------TAFLpptALKMMRQQGEQLKhaqvKLRAIATGGESLGEEL-LGWAREQFGVEVNEFYGQTECNLVIGNCS 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 924 K--NSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIK--SEFMMKGYHKNPEQTKEAFDSDgWLHTKDIGYYDENG 999
Cdd:cd05971 253 AlfPIKPGSMGKPIPGHRVAIVDDN-GTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1000 EIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTeeelhDLVNKNLPWYC 1079
Cdd:cd05971 331 YFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPS-----DALAREIQELV 405
|
490 500
....*....|....*....|....*..
gi 1820754837 1080 KLQAG-------IKFVNDFPRISTGKI 1099
Cdd:cd05971 406 KTRLAaheypreIEFVNELPRTATGKI 432
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1206-1685 |
6.13e-29 |
|
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: 123.89 E-value: 6.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGvKPGDIIGLCSDNNLDVFLILLGTMYIGAI--------SNTWDHELtpmtaRNFLTLTSP 1277
Cdd:cd05931 26 TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavplppptPGRHAERL-----AAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1278 KIVFTVSSSAANL--MEAAKELKMNLKVVVMDkldgyeSVEENVMKGHDTREIiefkchvtNPDDVALIVPSSGTTGLPK 1355
Cdd:cd05931 100 RVVLTTAAALAAVraFAASRPAAGTPRLLVVD------LLPDTSAADWPPPSP--------DPDDIAYLQYTSGSTGTPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1356 GTEISHYSLF--------CCLHPYKNRT-----------LVGhtCIVTPtmrWHYG---VLM---AFrlVAANAKKLivp 1410
Cdd:cd05931 166 GVVVTHRNLLanvrqirrAYGLDPGDVVvswlplyhdmgLIG--GLLTP---LYSGgpsVLMspaAF--LRRPLRWL--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1411 dnddaenfcQLIEKYQITW-----FGTDpfMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKL------PDV 1479
Cdd:cd05931 236 ---------RLISRYRATIsaapnFAYD--LCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFapfgfrPEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1480 FiTNHYGMTDTACVVSAQNKFT---------------------------KLGSVGYVSSNVRIKMVDLDTEEALGPNKIG 1532
Cdd:cd05931 305 F-RPSYGLAEATLFVSGGPPGTgpvvlrvdrdalagravavaaddpaarELVSCGRPLPDQEVRIVDPETGRELPDGEVG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1533 ELRVKAITIMQGYHKNPETTKQAF------DSDGWLRTGDLAYYDDnGEIYIVDRISDFINFRSINVSPAEIETVLMTHP 1606
Cdd:cd05931 384 EIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEATAEEAH 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1607 AVLQ---AAVLGIPNEVDEQhpkafVVQVpnksvteQELISYVEKN-LPDYC-RLRG------GVKIVD-------QLPR 1668
Cdd:cd05931 463 PALRpgcVAAFSVPDDGEER-----LVVV-------AEVERGADPAdLAAIAaAIRAavarehGVAPADvvlvrpgSIPR 530
|
570
....*....|....*..
gi 1820754837 1669 TTTGKIARKQLRDMYVN 1685
Cdd:cd05931 531 TSSGKIQRRACRAAYLD 547
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1335-1679 |
6.88e-29 |
|
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: 122.12 E-value: 6.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1335 VTNPDDVALIVPSSGTTGLPKGTEISHYS----------LFCCLHPYKNRTLVGHTCIVTPTMRWhygvlMAFRLVaaNA 1404
Cdd:cd17648 90 ITNSTDLAYAIYTSGTTGKPKGVLVEHGSvvnlrtslseRYFGRDNGDEAVLFFSNYVFDFFVEQ-----MTLALL--NG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1405 KKLIVPDND---DAENFCQLIEKYQITWFGTDPFMIikfiksQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVfI 1481
Cdd:cd17648 163 QKLVVPPDEmrfDPDRFYAYINREKVTYLSGTPSVL------QQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGL-I 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1482 TNHYGMTDTAcvVSAQNKFTKLG-----SVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKNPETTKQAF 1556
Cdd:cd17648 236 INAYGPTETT--VTNHKRFFPGDqrfdkSLGRPVRNTKCYVLNDAMKR-VPVGAVGELYLGGDGVARGYLNRPELTAERF 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1557 -------DSDGWL-------RTGDLAYYDDNGEIYIVDRiSDF-INFRSINVSPAEIETVLMTHPAVLQAAVLG--IPNE 1619
Cdd:cd17648 313 lpnpfqtEQERARgrnarlyKTGDLVRWLPSGELEYLGR-NDFqVKIRGQRIEPGEVEAALASYPGVRECAVVAkeDASQ 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1620 VDEQHPKAFV-VQVPNK-SVTEQELISYVEKNLPDY------CRLrggvkivDQLPRTTTGKIARKQL 1679
Cdd:cd17648 392 AQSRIQKYLVgYYLPEPgHVPESDLLSFLRAKLPRYmvparlVRL-------EGIPVTINGKLDVRAL 452
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
54-543 |
7.57e-29 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 123.76 E-value: 7.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 54 AQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHlESYVP-LLAALYLGAISNPWDNELSPMTARYFLS 132
Cdd:PLN02860 23 AVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNS-DLYLEwLLAVACAGGIVAPLNYRWSFEEAKSAML 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 133 LTKPkIVFVNGESAECLAQVVKENNMDT-RLVVFADSAGFVGRAATLTAVlrSQDTAWIDEFECAKLT---SPKHVAAIV 208
Cdd:PLN02860 102 LVRP-VMLVTDETCSSWYEELQNDRLPSlMWQVFLESPSSSVFIFLNSFL--TTEMLKQRALGTTELDyawAPDDAVLIC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 209 CSSGTSGFPKGTEISHAAMI-NYMAHVKV-----HDLKGHVSmwtPsmrwYC---GLFIVIKAILDCSKRIIVPDYDDDE 279
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALIvQSLAKIAIvgygeDDVYLHTA---P----LChigGLSSALAMLMVGACHVLLPKFDAKA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 280 GLcRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYR--LPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDyggLC 357
Cdd:PLN02860 252 AL-QAIKQHNVTSMITVPAMMADLISLTRKSMTWkvFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTE---AC 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 358 ARQT-------KYSKPGSCGFVCETGRLKVVDPNTGKVLG--------------ANKTGEIWAKSSYMMNGYYNNPEATR 416
Cdd:PLN02860 328 SSLTfmtlhdpTLESPKQTLQTVNQTKSSSVHQPQGVCVGkpaphvelkigldeSSRVGRILTRGPHVMLGYWGQNSETA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 417 RALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVaKVP 496
Cdd:PLN02860 408 SVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV-RLR 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 497 GKEVTELDITDLVKQNMPW-------YCRLHAGVKFmeKLPR-----------TATGKIAKKQLK 543
Cdd:PLN02860 487 DGWIWSDNEKENAKKNLTLssetlrhHCREKNLSRF--KIPKlfvqwrkpfplTTTGKIRRDEVR 549
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
65-477 |
7.65e-29 |
|
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: 122.47 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVnge 144
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 saeclaqvvkENnmdtrlvvfadsagfvgraatltavlrsqdtawidefecakltSPKHVAAIVCSSGTSGFPKGTEISH 224
Cdd:cd17640 84 ----------EN-------------------------------------------DSDDLATIIYTSGTTGNPKGVMLTH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AAMINYMAH----VKVHDLKGHVSMWTPsmrWY------------CG---LFIVIKAILDCSKRIiVPDYDDD-----EG 280
Cdd:cd17640 111 ANLLHQIRSlsdiVPPQPGDRFLSILPI---WHsyersaeyfifaCGcsqAYTSIRTLKDDLKRV-KPHYIVSvprlwES 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 281 LCRFIEKYevswFRCDSCFPIRLVKFGVLSKyrlpTLKILLFGGahfkGELQQTLVKLLPHTDVIL--SYGMTDYGG-LC 357
Cdd:cd17640 187 LYSGIQKQ----VSKSSPIKQFLFLFFLSGG----IFKFGISGG----GALPPHVDTFFEAIGIEVlnGYGLTETSPvVS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 358 ARQTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDG 437
Cdd:cd17640 255 ARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGG 334
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1820754837 438 EVFLVDRMSEFI------NyraikISPAEIEALIQQHPAVFQVAVV 477
Cdd:cd17640 335 ELVLTGRAKDTIvlsngeN-----VEPQPIEEALMRSPFIEQIMVV 375
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1191-1679 |
8.66e-29 |
|
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: 122.38 E-value: 8.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARN 1270
Cdd:cd12114 1 PDATAVICG--DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 FLTLTSPKIVFTVSSSAANLMEAAKelkmnlkvVVMDKLDGYESVEENVMKghdtreiiefkchVTNPDDVALIVPSSGT 1350
Cdd:cd12114 79 ILADAGARLVLTDGPDAQLDVAVFD--------VLILDLDALAAPAPPPPV-------------DVAPDDLAYVIFTSGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISH---YSLFCCLhpykNRTLVghtciVTPTMRW------HY--GVLMAFRLVAANAKKLIVPDNDDAENF- 1418
Cdd:cd12114 138 TGTPKGVMISHraaLNTILDI----NRRFA-----VGPDDRVlalsslSFdlSVYDIFGALSAGATLVLPDEARRRDPAh 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1419 -CQLIEKYQITWFGTDPF---MIIKFIKSqllEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTA--- 1491
Cdd:cd12114 209 wAELIERHGVTLWNSVPAlleMLLDVLEA---AQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASiws 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1492 --CVVSAQNkfTKLGSV--GYVSSNVRIKMVDLDTEEAlgPNKI-GELRVKAITIMQGYHKNPETTKQAF--DSDG--WL 1562
Cdd:cd12114 286 iyHPIDEVP--PDWRSIpyGRPLANQRYRVLDPRGRDC--PDWVpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1563 RTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEvDEQHPKAFVVQVPNKS-VTEQE 1641
Cdd:cd12114 362 RTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTpIAPDA 440
|
490 500 510
....*....|....*....|....*....|....*...
gi 1820754837 1642 LISYVEKNLPDYCRLRGGVKIvDQLPRTTTGKIARKQL 1679
Cdd:cd12114 441 LRAFLAQTLPAYMIPSRVIAL-EALPLTANGKVDRAAL 477
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
52-548 |
1.02e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 123.13 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 52 FIAQVEAVTGAET---------TFAEMTEKSVKCALWLREQGVQPGDIIGICTHN---HLESY--VPLLaalylGAISNP 117
Cdd:PRK08162 23 FLERAAEVYPDRPavihgdrrrTWAETYARCRRLASALARRGIGRGDTVAVLLPNipaMVEAHfgVPMA-----GAVLNT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 118 WDNELSPMTARYFLSLTKPKIVFVNGESAECLAQVVKENNMDTRLVVFADSAGFVG--RAATLT--AVLRSQDT--AWI- 190
Cdd:PRK08162 98 LNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGgrFIGALDyeAFLASGDPdfAWTl 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 191 --DEFEcakltspkhvaAIVCS--SGTSGFPKGTEISH-AAMINYMAHVKVHDLKGH-VSMWTPSMrWYCG------LFI 258
Cdd:PRK08162 178 paDEWD-----------AIALNytSGTTGNPKGVVYHHrGAYLNALSNILAWGMPKHpVYLWTLPM-FHCNgwcfpwTVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 259 VIKAILDCSKRIivpdydDDEGLCRFIEKYEVSWFrCDScfPIrlvkfgVLSkyrlptlkILLFGGAHFKGELQQTLVKL 338
Cdd:PRK08162 246 ARAGTNVCLRKV------DPKLIFDLIREHGVTHY-CGA--PI------VLS--------ALINAPAEWRAGIDHPVHAM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 339 L----PHTDVILS-----------YGMTD-YG--GLCARQTKYSK-PGScgfvcETGRLK--------------VVDPNT 385
Cdd:PRK08162 303 VagaaPPAAVIAKmeeigfdlthvYGLTEtYGpaTVCAWQPEWDAlPLD-----ERAQLKarqgvryplqegvtVLDPDT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 386 GK-VLGANKT-GEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEA 463
Cdd:PRK08162 378 MQpVPADGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVED 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 464 LIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDlvkqnmpwYCRLH-AG------VKFMEkLPRTATGK 536
Cdd:PRK08162 457 VLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIA--------HCREHlAGfkvpkaVVFGE-LPKTSTGK 527
|
570
....*....|..
gi 1820754837 537 IAKKQLKQIAKS 548
Cdd:PRK08162 528 IQKFVLREQAKS 539
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1202-1683 |
1.50e-28 |
|
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: 122.19 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQ--TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKI 1279
Cdd:cd05932 2 GQVVefTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1280 VFTVSSSAANLMEAakelkmnlkvVVMDKLDGYESVEENVMKGHDTREIIeFKCH-------VTNPDDVALIVPSSGTTG 1352
Cdd:cd05932 82 LFVGKLDDWKAMAP----------GVPEGLISISLPPPSAANCQYQWDDL-IAQHppleerpTRFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1353 LPKGTEISHYSL-FCC--------------------LHPYKNRTLVGHTCIVTptmrwhyGVLMAFrlvaanAKKLivpd 1411
Cdd:cd05932 151 QPKGVMLTFGSFaWAAqagiehigteendrmlsylpLAHVTERVFVEGGSLYG-------GVLVAF------AESL---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1412 nddaENFCQLIEKYQITWFGTDPFMIIKF-------------------------IKSQLLEKYRLPTLKVILSSGAHLRK 1466
Cdd:cd05932 214 ----DTFVEDVQRARPTLFFSVPRLWTKFqqgvqdkipqqklnlllkipvvnslVKRKVLKGLGLDQCRLAGCGSAPVPP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1467 EHLEVMRE-KLPdvfITNHYGMTDTaCVVSAQNK--FTKLGSVGYVSSNVRIKMVDldteealgpnkIGELRVKAITIMQ 1543
Cdd:cd05932 290 ALLEWYRSlGLN---ILEAYGMTEN-FAYSHLNYpgRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1544 GYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDfiNFRSIN---VSPAEIETVLMTHPAVLQAAVLG----- 1615
Cdd:cd05932 355 GYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKD--IFKTSKgkyVAPAPIENKLAEHDRVEMVCVIGsglpa 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1616 -----IPNEvdEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRGGVKI-----VDQLPRTTTGKIARKQLRDMY 1683
Cdd:cd05932 433 plalvVLSE--EARLRADAFARAELEASLRAHLARVNSTLDSHEQLAGIVVVkdpwsIDNGILTPTLKIKRNVLEKAY 508
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1169-1682 |
1.53e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 122.75 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1169 ELSIPKRPVN-IAEETLKFLKSKPDSIGQVDALT-GKV-QTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLI 1245
Cdd:PRK08162 5 EQGLDRNAANyVPLTPLSFLERAAEVYPDRPAVIhGDRrRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1246 LLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFtVSSSAANLMEAAKELKMNLKVVVMDKLDG-YESVEEnvmKGHd 1324
Cdd:PRK08162 85 HFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLI-VDTEFAEVAREALALLPGPKPLVIDVDDPeYPGGRF---IGA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1325 treiIEFKCHVTNPD-DVALIVP-----------SSGTTGLPKGTEISHYSLFccLHPYKNrtlvghtcIVTPTMRWH-- 1390
Cdd:PRK08162 160 ----LDYEAFLASGDpDFAWTLPadewdaialnyTSGTTGNPKGVVYHHRGAY--LNALSN--------ILAWGMPKHpv 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1391 Y-GVLMAFRL--------VAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSG 1461
Cdd:PRK08162 226 YlWTLPMFHCngwcfpwtVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1462 AHLRKEHLEVMREKLPDVfiTNHYGMTDT---ACVVSAQNKFTKLGSVGYVSSNVR----------IKMVDLDTEEALgP 1528
Cdd:PRK08162 306 AAPPAAVIAKMEEIGFDL--THVYGLTETygpATVCAWQPEWDALPLDERAQLKARqgvryplqegVTVLDPDTMQPV-P 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1529 N---KIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTH 1605
Cdd:PRK08162 383 AdgeTIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRH 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1606 PAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRggvKIV-DQLPRTTTGKIARKQLRDM 1682
Cdd:PRK08162 462 PAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPK---AVVfGELPKTSTGKIQKFVLREQ 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1206-1679 |
1.98e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.84 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELtPMTARNFLtLTSPKIVFTVSS 1285
Cdd:PRK12316 538 DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY-PAERLAYM-LEDSGVQLLLSQ 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAAnlmeaAKELKMNLKVVVMDkLDGYESVEENVMKGHDTREIiefkchvtNPDDVALIVPSSGTTGLPKGTEISHYSL- 1364
Cdd:PRK12316 616 SHL-----GRKLPLAAGVQVLD-LDRPAAWLEGYSEENPGTEL--------NPENLAYVIYTSGSTGKPKGAGNRHRALs 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1365 -FCCLHPYKNRTLVGHTCIVTPTMRWHYGVLMAFRLVAANAKKLIVPDND--DAENFCQLIEKYQITWFGTDPFMIIKFI 1441
Cdd:PRK12316 682 nRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrDPAKLVELINREGVDTLHFVPSMLQAFL 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1442 KSQLLEKyrLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVVSAQNKFTKLG---SVGYVSSNVRIKMV 1518
Cdd:PRK12316 762 QDEDVAS--CTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGdsvPIGRPIANLACYIL 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1519 DLDteeaLGPNKI---GELRVKAITIMQGYHKNPETTKQAF------DSDGWLRTGDLAYYDDNGEIYIVDRISDFINFR 1589
Cdd:PRK12316 840 DAN----LEPVPVgvlGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1590 SINVSPAEIETVLMTHPAVLQAAVLGipneVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRT 1669
Cdd:PRK12316 916 GLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGDWREALKAHLAASLPEY-MVPAQWLALERLPLT 990
|
490
....*....|
gi 1820754837 1670 TTGKIARKQL 1679
Cdd:PRK12316 991 PNGKLDRKAL 1000
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1191-1681 |
3.67e-28 |
|
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: 119.72 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGqVDALTGKVqTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheLTPMTArn 1270
Cdd:cd17653 11 PDAVA-VESLGGSL-TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAA-------YVPLDA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 flTLTSPKIVFTVSSSAANLMEAAkelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchvTNPDDVALIVPSSGT 1350
Cdd:cd17653 80 --KLPSARIQAILRTSGATLLLTT-----------------------------------------DSPDDLAYIIFTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISHYSLfccLHPYKNrtlVGHTCIVTPTMR--------WHYGVLMAFRLVAaNAKKLIVpdNDDAENFCQLI 1422
Cdd:cd17653 117 TGIPKGVMVPHRGV---LNYVSQ---PPARLDVGPGSRvaqvlsiaFDACIGEIFSTLC-NGGTLVL--ADPSDPFAHVA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1423 EKyqitwfgTDPFMIIKFIKSqLLEKYRLPTLKVILSSGAHLRKEhleVMREKLPDVFITNHYGMTDTACVVSaqnkFTK 1502
Cdd:cd17653 188 RT-------VDALMSTPSILS-TLSPQDFPNLKTIFLGGEAVPPS---LLDRWSPGRRLYNAYGPTECTISST----MTE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1503 LG-----SVGYVSSNVRIKMVDLDTEEALGPnKIGELRVKAITIMQGYHKNPETTKQAFDSDGW------LRTGDLAYYD 1571
Cdd:cd17653 253 LLpgqpvTIGKPIPNSTCYILDADLQPVPEG-VVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWT 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1572 DNGEIYIVDRISDFINFRSINVSPAEIETVLMT-HPAVLQAAVLgipneVDEQHPKAFVvqVPnKSVTEQELISYVEKNL 1650
Cdd:cd17653 332 EDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAI-----VVNGRLVAFV--TP-ETVDVDGLRSELAKHL 403
|
490 500 510
....*....|....*....|....*....|.
gi 1820754837 1651 PDYCRLRGGVKiVDQLPRTTTGKIARKQLRD 1681
Cdd:cd17653 404 PSYAVPDRIIA-LDSFPLTANGKVDRKALRE 433
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
59-536 |
4.50e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 121.15 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 59 VTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIS-----NPWDNELspmtaRYFLS 132
Cdd:PRK07798 23 VCGDRRlTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPvnvnyRYVEDEL-----RYLLD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 133 LTKPKIVFVNGESAECLAQVVKEN-NMDTRLVVFADSAG-FVGRAATLTAVLRSQDTAwiDEFECaklTSPKHVAaIVCS 210
Cdd:PRK07798 98 DSDAVALVYEREFAPRVAEVLPRLpKLRTLVVVEDGSGNdLLPGAVDYEDALAAGSPE--RDFGE---RSPDDLY-LLYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 211 SGTSGFPKGT-----EISHAAM--INYMAHVKVHDLKGHVSMWT--PSMRWYC--------GLFIVIKAILDCSKRIIVP 273
Cdd:PRK07798 172 GGTTGMPKGVmwrqeDIFRVLLggRDFATGEPIEDEEELAKRAAagPGMRRFPapplmhgaGQWAAFAALFSGQTVVLLP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 274 D--YDDDEgLCRFIEKYEVSwfrcdscfpiRLVKFG------------VLSKYRLPTLKILLFGGAHFKGELQQTLVKLL 339
Cdd:PRK07798 252 DvrFDADE-VWRTIEREKVN----------VITIVGdamarplldaleARGPYDLSSLFAIASGGALFSPSVKEALLELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 340 PHTDVILSYGMTDYG-GLCARQTKYSKPGSCGFVCETGRLKVVDPNTGKVL-GANKTGEIwAKSSYMMNGYYNNPEATRR 417
Cdd:PRK07798 321 PNVVLTDSIGSSETGfGGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEpGSGEIGWI-ARRGHIPLGYYKDPEKTAE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 418 ALDS-DG--WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAK 494
Cdd:PRK07798 400 TFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQL 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1820754837 495 VPGKEVTELDITDlvkqnmpwYCRLH-AGVK------FMEKLPRTATGK 536
Cdd:PRK07798 480 REGARPDLAELRA--------HCRSSlAGYKvpraiwFVDEVQRSPAGK 520
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
764-1099 |
5.11e-28 |
|
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: 117.36 E-value: 5.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 764 DLAMICSSSGTTGMPKGTELSYASLYnSITPVEEVHAKNEI----------------CAWVPTIRWHGGLnqcievimsn 827
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFF-AVPDILQKEGLNWVvgdvtylplpathiggLWWILTCLIHGGL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 828 akwIIFSDDNIKEIALCEIIQKHGVTWLG---TDTNFAILYVKMNIfqKYpMPSLRkMVITGAPFTKELHETVAKIMPHT 904
Cdd:cd17635 71 ---CVTGGENTTYKSLFKILTTNAVTTTClvpTLLSKLVSELKSAN--AT-VPSLR-LIGYGGSRAIAADVRFIEATGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 905 QILQCYGLTDAGGLCVSQAKNSKP--GSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFd 982
Cdd:cd17635 144 NTAQVYGLSETGTALCLPTDDDSIeiNAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 983 SDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIEL-PLAFVQKVVEKE 1061
Cdd:cd17635 222 IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELvGLAVVASAELDE 301
|
330 340 350
....*....|....*....|....*....|....*...
gi 1820754837 1062 VTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:cd17635 302 NAIRALKHTIRRELEPY-ARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
56-544 |
5.15e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 120.37 E-value: 5.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 56 VEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTK 135
Cdd:PRK07514 21 IETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 136 PKIVFVNGESAECLAQVVKENNmdTRLVVFADSAGfvgrAATLTAVLRSQDtawiDEFECAKlTSPKHVAAIVCSSGTSG 215
Cdd:PRK07514 101 PALVVCDPANFAWLSKIAAAAG--APHVETLDADG----TGSLLEAAAAAP----DDFETVP-RGADDLAAILYTSGTTG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 216 FPKGTEISH-------AAMINYMA----HVKVHDLK-GHVSmwtpsmrwycGLFIVIK-AILDCSKRIIVPDYDDDEGLC 282
Cdd:PRK07514 170 RSKGAMLSHgnllsnaLTLVDYWRftpdDVLIHALPiFHTH----------GLFVATNvALLAGASMIFLPKFDPDAVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 283 RFiekyevswfrcdscfPIRLVKFGVlskyrlPTLKILLFGGAHFKGELQQTL-------VKLLPHTDV---------IL 346
Cdd:PRK07514 240 LM---------------PRATVMMGV------PTFYTRLLQEPRLTREAAAHMrlfisgsAPLLAETHRefqertghaIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 347 S-YGMTD--------YGGlcARqtkysKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRR 417
Cdd:PRK07514 299 ErYGMTEtnmntsnpYDG--ER-----RAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 418 ALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFInyraikIS------PAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAF 491
Cdd:PRK07514 372 EFRADGFFITGDLGKIDERGYVHIVGRGKDLI------ISggynvyPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAV 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 492 VAKVPGKEVTELDITDLVKQnmpwycRLhAGVK------FMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK07514 446 VVPKPGAALDEAAILAALKG------RL-ARFKqpkrvfFVDELPRNTMGKVQKNLLRE 497
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1162-1682 |
5.53e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 121.28 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1162 DNILIGKELSIPKRPVNiaeetlkFLKSKPDSI-GQVDALTGKVQ-TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNN 1239
Cdd:PLN03102 2 DNLALCEANNVPLTPIT-------FLKRASECYpNRTSIIYGKTRfTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1240 LDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFTVSSSAANLME-----AAKELKMNLKVVVMDKLDGYES 1314
Cdd:PLN03102 75 PAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREvlhllSSEDSNLNLPVIFIHEIDFPKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1315 V-------EENVMKGHDTREIIEFKCHVTNPDDVALIVPSSGTTGLPKGTEISHYSLFCClhpyKNRTLVGHTCIVTPTM 1387
Cdd:PLN03102 155 PsseeldyECLIQRGEPTPSLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLS----TLSAIIGWEMGTCPVY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1388 RWhygVLMAFRL--------VAANAKKLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIK-SQLLEKYRLPTLKVIl 1458
Cdd:PLN03102 231 LW---TLPMFHCngwtftwgTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgNSLDLSPRSGPVHVL- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1459 sSGAHLRKEHLEVMREKLPdvFITNH-YGMTDTACVV---SAQNKFTKLGSVGYVS-------SNVRIKMVDLDTEEALG 1527
Cdd:PLN03102 307 -TGGSPPPAALVKKVQRLG--FQVMHaYGLTEATGPVlfcEWQDEWNRLPENQQMElkarqgvSILGLADVDVKNKETQE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1528 P-----NKIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVL 1602
Cdd:PLN03102 384 SvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1603 MTHPAVLQAAVLGIPNEVDEQHPKAFVV---------QVPNKSVT-EQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTG 1672
Cdd:PLN03102 463 YKYPKVLETAVVAMPHPTWGETPCAFVVlekgettkeDRVDKLVTrERDLIEYCRENLPHFMCPR-KVVFLQELPKNGNG 541
|
570
....*....|
gi 1820754837 1673 KIARKQLRDM 1682
Cdd:PLN03102 542 KILKPKLRDI 551
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
623-1044 |
5.79e-28 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 120.63 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:PRK06155 42 FGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNEESAENLmEAAKEENLQV-RVMVIGSLPGFVSLANI-------LEEQVSRAEIdgfrctkidNPHDLAMICSSSGT 774
Cdd:PRK06155 122 LVVEAALLAAL-EAADPGDLPLpAVWLLDAPASVSVPAGWstaplppLDAPAPAAAV---------QPGDTAAILYTSGT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 775 TGMPKGTELSYASLY----NSiTPVEEVHAKNEICAWVPTirWH-GGLNQCIEVIMSNAKWII--------FSDDnikei 841
Cdd:PRK06155 192 TGPSKGVCCPHAQFYwwgrNS-AEDLEIGADDVLYTTLPL--FHtNALNAFFQALLAGATYVLeprfsasgFWPA----- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 842 alceiIQKHGVTWlgtdtnFAILYVKMNIFQKYPMP------SLRKMVITGAP--FTKELHETVAkimphTQILQCYGLT 913
Cdd:PRK06155 264 -----VRRHGATV------TYLLGAMVSILLSQPAResdrahRVRVALGPGVPaaLHAAFRERFG-----VDLLDGYGST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 914 DAGGLCVSQAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSE---FMMKGYHKNPEQTKEAFdSDGWLHTK 990
Cdd:PRK06155 328 ETNFVIAVTHGSQRPGSMGRLAPGFEARVVDEH-DQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAW-RNLWFHTG 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 991 DIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHE 1044
Cdd:PRK06155 406 DRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSE 459
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1181-1679 |
6.53e-28 |
|
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: 119.20 E-value: 6.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1181 EETLKFLkskPDSIGQVDalTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWD 1260
Cdd:cd17645 5 EEQVERT---PDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1261 HELTPMTARNFLTLTSPKIVftvsssaanlmeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchVTNPDD 1340
Cdd:cd17645 80 PDYPGERIAYMLADSSAKIL------------------------------------------------------LTNPDD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1341 VALIVPSSGTTGLPKGTEISHYSL--FCCLH-PYKNRTLVGHTCIVTpTMRWHYGVLMAFRLVAANAKKLIVPDND--DA 1415
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLvnLCEWHrPYFGVTPADKSLVYA-SFSFDASAWEIFPHLTAGAALHVVPSERrlDL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1416 ENFCQLIEKYQITwfgtdpfmiIKFIKSQLLEKYRL---PTLKVILSSGahlrkEHLEVMREKlpDVFITNHYGMTDTAC 1492
Cdd:cd17645 185 DALNDYFNQEGIT---------ISFLPTGAAEQFMQldnQSLRVLLTGG-----DKLKKIERK--GYKLVNNYGPTENTV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1493 VVSAQNKFTKLGS--VGYVSSNVRIKMvdLDTEEALGPNKI-GELRVKAITIMQGYHKNPETTKQAFDSDGWL------R 1563
Cdd:cd17645 249 VATSFEIDKPYANipIGKPIDNTRVYI--LDEALQLQPIGVaGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1564 TGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPnevDEQHPKAFVVQV-PNKSVTEQEL 1642
Cdd:cd17645 327 TGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKE---DADGRKYLVAYVtAPEEIPHEEL 403
|
490 500 510
....*....|....*....|....*....|....*..
gi 1820754837 1643 ISYVEKNLPDYCRLRGGVKIvDQLPRTTTGKIARKQL 1679
Cdd:cd17645 404 REWLKNDLPDYMIPTYFVHL-KALPLTANGKVDRKAL 439
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1179-1682 |
9.08e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 119.50 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1179 IAEETLKFLKSKPDSIGQVDalTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSdnNLDVFLILlgtmYIGAISNT 1258
Cdd:PRK07638 3 ITKEYKKHASLQPNKIAIKE--NDRVLTYKDWFESVCKVANWLNEKESKNKTIAILLE--NRIEFLQL----FAGAAMAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1259 WdheltpmTArnfltltspkIVFTVSSSAANLMEAAKELKMNLKVVVMDKLDGYESVEENVMKGHDTREIIEFKCHVTNP 1338
Cdd:PRK07638 75 W-------TC----------VPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEWKRMIEKYLPTYAP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1339 DDVALIVP-----SSGTTGLPKGTEISH----YSLFCCLHPY----KNRTLVGHTCIVTPTMrwhYGVLMAFRLVAAN-- 1403
Cdd:PRK07638 138 IENVQNAPfymgfTSGSTGKPKAFLRAQqswlHSFDCNVHDFhmkrEDSVLIAGTLVHSLFL---YGAISTLYVGQTVhl 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1404 AKKLIVPDNDDAenfcqlIEKYQITWFGTDPFMIIKFIKsqlLEKYRLPTLKVIlSSGAHLRKEHLEVMREKLPDVFITN 1483
Cdd:PRK07638 215 MRKFIPNQVLDK------LETENISVMYTVPTMLESLYK---ENRVIENKMKII-SSGAKWEAEAKEKIKNIFPYAKLYE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1484 HYGMTDTACV---VSAQNKfTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYhKNPETTKQAFDSDG 1560
Cdd:PRK07638 285 FYGASELSFVtalVDEESE-RRPNSVGRPFHNVQVRICNEAGEE-VQKGEIGTVYVKSPQFFMGY-IIGGVLARELNADG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1561 WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQvpnkSVTEQ 1640
Cdd:PRK07638 362 WMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKG----SATKQ 437
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1820754837 1641 ELISYVEKNLPDYCRLRGGVkIVDQLPRTTTGKIARKQLRDM 1682
Cdd:PRK07638 438 QLKSFCLQRLSSFKIPKEWH-FVDEIPYTNSGKIARMEAKSW 478
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
65-548 |
9.19e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 120.51 E-value: 9.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAECLAQVVK-----ENNMDTRlVVFADSAGFVGRAAtltavlrSQDTawidEFEC---AKLTSPKHVAAIVC------- 209
Cdd:PLN03102 121 FEPLAREVLHllsseDSNLNLP-VIFIHEIDFPKRPS-------SEEL----DYECliqRGEPTPSLVARMFRiqdehdp 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 210 -----SSGTSGFPKGTEISH--------AAMINY-MAHVKVHdlkghvsMWTPSMrWYCGLFIVIKAILD------CSKR 269
Cdd:PLN03102 189 islnyTSGTTADPKGVVISHrgaylstlSAIIGWeMGTCPVY-------LWTLPM-FHCNGWTFTWGTAArggtsvCMRH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 270 IIVPDydddegLCRFIEKYEVSWFRC-DSCFPIRLVKFGVLSKYRLPTLKILLfGGAHFKGELQQTLVKLLPHtdVILSY 348
Cdd:PLN03102 261 VTAPE------IYKNIEMHNVTHMCCvPTVFNILLKGNSLDLSPRSGPVHVLT-GGSPPPAALVKKVQRLGFQ--VMHAY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 349 GMTDYGG---LCARQTKYSK-PGSCGF-----------------VCETGRLKVVdPNTGKVLGanktgEIWAKSSYMMNG 407
Cdd:PLN03102 332 GLTEATGpvlFCEWQDEWNRlPENQQMelkarqgvsilgladvdVKNKETQESV-PRDGKTMG-----EIVIKGSSIMKG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 408 YYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEH 487
Cdd:PLN03102 406 YLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGET 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 488 AMAFVAKVPGKEVTELDITDLV--KQNMPWYCRLHA-------GVKFMEKLPRTATGKIAKKQLKQIAKS 548
Cdd:PLN03102 485 PCAFVVLEKGETTKEDRVDKLVtrERDLIEYCRENLphfmcprKVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
629-1099 |
9.27e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 120.51 E-value: 9.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENhlntcVPVL-----AILYIGGIICPWDHVVSKLSARYFLSLMSPKVV 703
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPN-----TPAMyemhfAVPMAGAVLNPINTRLDATSIAAILRHAKPKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 704 FVNEESAENLME-----AAKEENLQVRVMVIGSL--PGFVSLANI-LEEQVSRAEIDGF---RCTKIDNPHDLAMICSSS 772
Cdd:PLN03102 116 FVDRSFEPLAREvlhllSSEDSNLNLPVIFIHEIdfPKRPSSEELdYECLIQRGEPTPSlvaRMFRIQDEHDPISLNYTS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 773 GTTGMPKGTELSYASLYNS-----------ITPV-----EEVHAKNEICAWVPTIRwhGGLNQCIevimsnakwiifsdd 836
Cdd:PLN03102 196 GTTADPKGVVISHRGAYLStlsaiigwemgTCPVylwtlPMFHCNGWTFTWGTAAR--GGTSVCM--------------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 837 niKEIALCEI---IQKHGVTWLG-TDTNFAILyVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKImpHTQILQCYGL 912
Cdd:PLN03102 259 --RHVTAPEIyknIEMHNVTHMCcVPTVFNIL-LKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 913 TDAGG---LCVSQAK-NSKPGSCGFVTK---GIRI------KIADEKT--GIALGPKERGEICIKSEFMMKGYHKNPEQT 977
Cdd:PLN03102 334 TEATGpvlFCEWQDEwNRLPENQQMELKarqGVSIlgladvDVKNKETqeSVPRDGKTMGEIVIKGSSIMKGYLKNPKAT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 978 KEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKV 1057
Cdd:PLN03102 414 SEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLE 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1058 VEKEVTEEELHDLVNK--NLPWYCK-------LQAGIKFVNDFPRISTGKI 1099
Cdd:PLN03102 493 KGETTKEDRVDKLVTRerDLIEYCRenlphfmCPRKVVFLQELPKNGNGKI 543
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
204-539 |
9.43e-28 |
|
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: 116.59 E-value: 9.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 204 VAAIVCSSGTSGFPKGTEISHAAMINYMAHVKVHDLKGHVS--MWTPSMRWYCGLFIVIKAILDCS-KRIIVPDYDDDEG 280
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGdvTYLPLPATHIGGLWWILTCLIHGgLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 281 LCRFIEKYEVSwfrcDSCF-PIRLVKFGVLSKYRL---PTLKILLFGGAhFKGELQQTLVKLLPHTDVILSYGMTDYGGL 356
Cdd:cd17635 83 LFKILTTNAVT----TTCLvPTLLSKLVSELKSANatvPSLRLIGYGGS-RAIAADVRFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 357 CARQT--KYSKPGSCGFVCETGRLKVVDpNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYD 434
Cdd:cd17635 158 LCLPTddDSIEINAVGRPYPGVDVYLAA-TDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 435 NDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKvpGKEVTELDITDL---VKQ 511
Cdd:cd17635 236 EDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA--SAELDENAIRALkhtIRR 313
|
330 340
....*....|....*....|....*...
gi 1820754837 512 NMPWYCRlHAGVKFMEKLPRTATGKIAK 539
Cdd:cd17635 314 ELEPYAR-PSTIVIVTDIPRTQSGKVKR 340
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1171-1681 |
1.55e-27 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 119.95 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1171 SIPKRPVNIAEET-LKFL-KSKPDSIGQVDALTGKVQ-TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILL 1247
Cdd:PLN02479 9 DLPKNAANYTALTpLWFLeRAAVVHPTRKSVVHGSVRyTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1248 GTMYIGAISNTWDHELTPMTARNFLTLTSPKIV------FTVSSSAANLMEAAKE--LKMNLKVVVMDKLDGYESVEENV 1319
Cdd:PLN02479 89 GVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVmvdqefFTLAEEALKILAEKKKssFKPPLLIVIGDPTCDPKSLQYAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1320 MKGhdtreIIEFKCHVTN---------PDD----VALIVpSSGTTGLPKGTEISH-----YSLFCCLHPYKNR------T 1375
Cdd:PLN02479 169 GKG-----AIEYEKFLETgdpefawkpPADewqsIALGY-TSGTTASPKGVVLHHrgaylMALSNALIWGMNEgavylwT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1376 LVGHTC---IVTPTMRWHYGVLMAFRLVAANAkklivpdnddaenFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYR-L 1451
Cdd:PLN02479 243 LPMFHCngwCFTWTLAALCGTNICLRQVTAKA-------------IYSAIANYGVTHFCAAPVVLNTIVNAPKSETILpL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1452 PTLKVILSSGAHLRKEHLEVMREKlpDVFITNHYGMTDT-----ACV---------VSAQNKFTKLGSVGYVSSNvRIKM 1517
Cdd:PLN02479 310 PRVVHVMTAGAAPPPSVLFAMSEK--GFRVTHTYGLSETygpstVCAwkpewdslpPEEQARLNARQGVRYIGLE-GLDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1518 VDLDTEEALGPN--KIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSP 1595
Cdd:PLN02479 387 VDTKTMKPVPADgkTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1596 AEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFV-----VQVPNKSVTEQELISYVEKNLPDYCRLRGGVkiVDQLPRTT 1670
Cdd:PLN02479 466 LEVENVVYTHPAVLEASVVARPDERWGESPCAFVtlkpgVDKSDEAALAEDIMKFCRERLPAYWVPKSVV--FGPLPKTA 543
|
570
....*....|.
gi 1820754837 1671 TGKIARKQLRD 1681
Cdd:PLN02479 544 TGKIQKHVLRA 554
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
59-542 |
1.58e-27 |
|
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: 118.53 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 59 VTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPK 137
Cdd:cd12114 7 ICGDGTlTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 138 IVFVNGESAEclaqvvkeNNMDTRLVVFADSAGFVGRAATLTAVLRSQDTAWIdefecakltspkhvaaiVCSSGTSGFP 217
Cdd:cd12114 87 LVLTDGPDAQ--------LDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYV-----------------IFTSGSTGTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 218 KGTEISHAAMINYMAhvkvhDLKGHVSMwTPSMRWYC-----------GLFivikAILDCSKRIIVPDYDDDEG---LCR 283
Cdd:cd12114 142 KGVMISHRAALNTIL-----DINRRFAV-GPDDRVLAlsslsfdlsvyDIF----GALSAGATLVLPDEARRRDpahWAE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 284 FIEKYEVS-WfrcdSCFPIR---LVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTD------- 352
Cdd:cd12114 212 LIERHGVTlW----NSVPALlemLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEasiwsiy 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 353 --------------YGGLCARQtkyskpgscgfvcetgRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPE--ATR 416
Cdd:cd12114 288 hpidevppdwrsipYGRPLANQ----------------RYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPEltAAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 417 RALDSDG--WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAK 494
Cdd:cd12114 351 FVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPD 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 495 VPGKEVTELDITDLVKQNMPWYCRLHAGVkFMEKLPRTATGKIAKKQL 542
Cdd:cd12114 431 NDGTPIAPDALRAFLAQTLPAYMIPSRVI-ALEALPLTANGKVDRAAL 477
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
629-1039 |
1.72e-27 |
|
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: 118.23 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVnee 708
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 saenlmeaakeENlqvrvmvigslpgfvslanileeqvsraeidgfrctkidNPHDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd17640 84 -----------EN---------------------------------------DSDDLATIIYTSGTTGNPKGVMLTHANL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 Y---NSITPVEEVHAKNEICAWVPTirWHGGLNQCIEVIMSNAKWIIFSddNIKeiALCEIIQKHGVTWL-GTDTNFAIL 864
Cdd:cd17640 114 LhqiRSLSDIVPPQPGDRFLSILPI--WHSYERSAEYFIFACGCSQAYT--SIR--TLKDDLKRVKPHYIvSVPRLWESL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 865 YVKMnIFQKYPMPSLRKMVITGAPFTKELHETVA---KIMPHTQ---------ILQCYGLTD-AGGLCVSQAKNSKPGSC 931
Cdd:cd17640 188 YSGI-QKQVSKSSPIKQFLFLFFLSGGIFKFGISgggALPPHVDtffeaigieVLNGYGLTEtSPVVSARRLKCNVRGSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 932 GFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDfi 1011
Cdd:cd17640 267 GRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKD-- 344
|
410 420 430
....*....|....*....|....*....|....
gi 1820754837 1012 nykAIKLSSAE------IEGVLELHPSILKAVVV 1039
Cdd:cd17640 345 ---TIVLSNGEnvepqpIEEALMRSPFIEQIMVV 375
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
316-539 |
2.95e-27 |
|
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: 114.42 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 316 TLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDYGGLCARQTKYS-KPGSCGFVCETGRLKVVDPNTGKVlgankt 394
Cdd:cd17633 111 KIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESrPPNSVGRPFPNVEIEIRNADGGEI------ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 395 GEIWAKSSYMMNGYYNNpeatrRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQV 474
Cdd:cd17633 185 GKIFVKSEMVFSGYVRG-----GFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEA 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 475 AVVPVPHNINEEHAmafVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAK 539
Cdd:cd17633 260 IVVGIPDARFGEIA---VALYSGDKLTYKQLKRFLKQKLSRY-EIPKKIIFVDSLPYTSSGKIAR 320
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
626-1100 |
4.34e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 117.86 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 626 KECTYAEMRERSIKCALWLRKHGIQKGDNIGIltenHLNTCVPVLAILY----IGGIICPwdhvvskLSARYflslmspk 701
Cdd:PRK08008 36 RRYSYLELNEEINRTANLFYSLGIRKGDKVAL----HLDNCPEFIFCWFglakIGAIMVP-------INARL-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 702 vvfVNEESAENLmeaakeENLQVRVMVIGS--LPGF--------VSLANILEEQVSRAEIDG---FRCTKIDNP------ 762
Cdd:PRK08008 97 ---LREESAWIL------QNSQASLLVTSAqfYPMYrqiqqedaTPLRHICLTRVALPADDGvssFTQLKAQQPatlcya 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 763 -----HDLAMICSSSGTTGMPKGTELS-----YASLYNS-----------ITPVEEVHAKNEICAWVPTIRwHGGLNQCI 821
Cdd:PRK08008 168 pplstDDTAEILFTSGTTSRPKGVVIThynlrFAGYYSAwqcalrdddvyLTVMPAFHIDCQCTAAMAAFS-AGATFVLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 822 EVIMSNAKWiifsddnikeialcEIIQKHGVTwlgtdtnfailyvkmnIFQKYPMPSLRKMVITGAPFTKE--------- 892
Cdd:PRK08008 247 EKYSARAFW--------------GQVCKYRAT----------------ITECIPMMIRTLMVQPPSANDRQhclrevmfy 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 893 LHETVAKIMPHTQ-----ILQCYGLTDA-GGLCvsqakNSKPG------SCGFVTKGIRIKIADEkTGIALGPKERGEIC 960
Cdd:PRK08008 297 LNLSDQEKDAFEErfgvrLLTSYGMTETiVGII-----GDRPGdkrrwpSIGRPGFCYEAEIRDD-HNRPLPAGEIGEIC 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 961 IKSE---FMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAV 1037
Cdd:PRK08008 371 IKGVpgkTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1038 VVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:PRK08008 451 VVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKF-KVPSYLEIRKDLPRNCSGKII 512
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
762-1043 |
5.19e-27 |
|
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: 117.70 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 762 PHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEVHAKNEIC-------AWVPtirwhggLNQCIE------VIMSNA 828
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKInptdvyiSYLP-------LAHIFErvvealFLYHGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 829 KwIIFSDDNIKEI----------ALC---------------EIIQKHGVT-WLgtdTNFA----ILYVKMN--------- 869
Cdd:cd05927 186 K-IGFYSGDIRLLlddikalkptVFPgvprvlnriydkifnKVQAKGPLKrKL---FNFAlnykLAELRSGvvraspfwd 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 870 --IFQKYPM---PSLRKMVITGAPFTKELhETVAKIMPHTQILQCYGLTD-AGGLCVSQAKNSKPGSCGFVTKGIRIKIA 943
Cdd:cd05927 262 klVFNKIKQalgGNVRLMLTGSAPLSPEV-LEFLRVALGCPVLEGYGQTEcTAGATLTLPGDTSVGHVGGPLPCAEVKLV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 944 D--EKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFinykaIKLSSA 1021
Cdd:cd05927 341 DvpEMNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNI-----FKLSQG 415
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1820754837 1022 E------IEGVLELHPSI-------------LKAVVVPVPH 1043
Cdd:cd05927 416 EyvapekIENIYARSPFVaqifvygdslksfLVAIVVPDPD 456
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1202-1681 |
7.71e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 120.27 E-value: 7.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELtPMTARNFLTLTSP-KIV 1280
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEY-PRERLAYMIEDSGvKLL 3196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1281 FTVSSSAANLMEAAkelkmNLKVVVMDKLDGYESVEENVMKghdtreiiefkchVTNPDDVALIVPSSGTTGLPKGTEIS 1360
Cdd:PRK12467 3197 LTQAHLLEQLPAPA-----GDTALTLDRLDLNGYSENNPST-------------RVMGENLAYVIYTSGSTGKPKGVGVR 3258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1361 HYSLFCCLHPYKN-RTLVGHTCIVTPTM--------RWhYGVLMAfrlvaanAKKLIVPDND--DAENFCQLIEKYQITW 1429
Cdd:PRK12467 3259 HGALANHLCWIAEaYELDANDRVLLFMSfsfdgaqeRF-LWTLIC-------GGCLVVRDNDlwDPEELWQAIHAHRISI 3330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1430 FGTDPFMIIKFIksQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTA-------CVVSAQNKFTK 1502
Cdd:PRK12467 3331 ACFPPAYLQQFA--EDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVvtvtlwkCGGDAVCEAPY 3408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1503 LgSVGYVSSNVRIKMVDldteEALGP---NKIGELRVKAITIMQGYHKNPETTKQAF------DSDGWL-RTGDLAYYDD 1572
Cdd:PRK12467 3409 A-PIGRPVAGRSIYVLD----GQLNPvpvGVAGELYIGGVGLARGYHQRPSLTAERFvadpfsGSGGRLyRTGDLARYRA 3483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1573 NGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQeLISYVEKNLPD 1652
Cdd:PRK12467 3484 DGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRET-LRDHLAASLPD 3562
|
490 500
....*....|....*....|....*....
gi 1820754837 1653 YcRLRGGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK12467 3563 Y-MVPAQLLVLAAMPLGPNGKVDRKALPD 3590
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
63-483 |
9.17e-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: 116.80 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVN 142
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 143 G-ESAECLAQVVKEnnmdtrlvvfadsaGFVGRAATLTAVLRSQDTaWIDEFECAK------LTSPKHVAAIVCSSGTSG 215
Cdd:cd05932 86 KlDDWKAMAPGVPE--------------GLISISLPPPSAANCQYQ-WDDLIAQHPpleerpTRFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 216 FPKGTEISHAA-------------------MINYM--AHVKVHDLKGHVSMWTPSMRWYCglfivikaildcskriivpd 274
Cdd:cd05932 151 QPKGVMLTFGSfawaaqagiehigteendrMLSYLplAHVTERVFVEGGSLYGGVLVAFA-------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 275 ydddEGLCRFIEkyEVSWFRCDSCFPI-RL-VKF--GVLSKYRLPTLKILL---FGGAHFKGELQQTL----VKLL---- 339
Cdd:cd05932 211 ----ESLDTFVE--DVQRARPTLFFSVpRLwTKFqqGVQDKIPQQKLNLLLkipVVNSLVKRKVLKGLgldqCRLAgcgs 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 340 -PHTDVILS------------YGMTDygglcarqtkyskpgSCGF--VCETGRLK---VVDPNTGKVLGANKTGEIWAKS 401
Cdd:cd05932 285 aPVPPALLEwyrslglnileaYGMTE---------------NFAYshLNYPGRDKigtVGNAGPGVEVRISEDGEILVRS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 402 SYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSE-FINYRAIKISPAEIEALIQQHPAVFQVAVV--- 477
Cdd:cd05932 350 PALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDiFKTSKGKYVAPAPIENKLAEHDRVEMVCVIgsg 429
|
....*..
gi 1820754837 478 -PVPHNI 483
Cdd:cd05932 430 lPAPLAL 436
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
42-546 |
9.72e-27 |
|
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: 117.80 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 42 VLEKLRSRPEFIAqVEAVTGAET--TFAEMTEKSVKCALWLREQGVQPGDIIGIcthnhlesYVPL--------LAALYL 111
Cdd:cd05967 60 VEAGRGDQIALIY-DSPVTGTERtyTYAELLDEVSRLAGVLRKLGVVKGDRVII--------YMPMipeaaiamLACARI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 112 GAISNP-----WDNELSpmtARyfLSLTKPKIVFvngeSAEC-------------LAQVVKENNMDTR--LVVFADSAgf 171
Cdd:cd05967 131 GAIHSVvfggfAAKELA---SR--IDDAKPKLIV----TASCgiepgkvvpykplLDKALELSGHKPHhvLVLNRPQV-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 172 vgrAATLTAVLRSQDtaWIDEFECAKLTSPKHVAA-----IVCSSGTSGFPKG---TEISHAAMINY-MAHVkvHDLK-G 241
Cdd:cd05967 200 ---PADLTKPGRDLD--WSELLAKAEPVDCVPVAAtdplyILYTSGTTGKPKGvvrDNGGHAVALNWsMRNI--YGIKpG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 242 HVsMWTPS-MRWYCG-LFIVIKAILDCSKRIIV---PDYDDDEG-LCRFIEKYEVSwfrCDSCFP--IRLVK-----FGV 308
Cdd:cd05967 273 DV-WWAASdVGWVVGhSYIVYGPLLHGATTVLYegkPVGTPDPGaFWRVIEKYQVN---ALFTAPtaIRAIRkedpdGKY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 309 LSKYRLPTLKILLFGGAHFKGELQQTLVKLLpHTDVILSYGMTDYG--------GLcarQTKYSKPGSCGFVCETGRLKV 380
Cdd:cd05967 349 IKKYDLSSLRTLFLAGERLDPPTLEWAENTL-GVPVIDHWWQTETGwpitanpvGL---EPLPIKAGSPGKPVPGYQVQV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 381 VDPNtGKVLGANKTGEIWAKSSY---MMNGYYNNPEATRRAL--DSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIK 455
Cdd:cd05967 425 LDED-GEPVGPNELGNIVIKLPLppgCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHR 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 456 ISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELD----ITDLVKQNM-PWYCRLHagVKFMEKLP 530
Cdd:cd05967 504 LSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEElekeLVALVREQIgPVAAFRL--VIFVKRLP 581
|
570
....*....|....*.
gi 1820754837 531 RTATGKIAKKQLKQIA 546
Cdd:cd05967 582 KTRSGKILRRTLRKIA 597
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
608-1099 |
1.05e-26 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 116.48 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 608 NRLSSKPDFVGQIDafTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVS 687
Cdd:TIGR02262 13 NVVEGRGGKTAFID--DISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 688 KLSARYFLSLMSPKVVFVNEESAENLMEA-AKEENLQVRVMVIGSLPGFVSLANILEeqvsrAEIDGFRcTKIDNPHDLA 766
Cdd:TIGR02262 91 ADDYAYMLEDSRARVVFVSGALLPVIKAAlGKSPHLEHRVVVGRPEAGEVQLAELLA-----TESEQFK-PAATQADDPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 767 MICSSSGTTGMPKGTELSYASLYNSitpvEEVHAKN-------EICAWVPTIRWHGGLNQCIEVIMSNAKWIIFSDDNIK 839
Cdd:TIGR02262 165 FWLYSSGSTGMPKGVVHTHSNPYWT----AELYARNtlgiredDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 840 EIALCEIIQKHGVTWL-GTDTNFAILYVKMNIFQKYPMpSLRKMVITGAPFTKELHETVAKIMPHtQILQCYGLTDAGGL 918
Cdd:TIGR02262 241 PDAVFDRLRRHQPTIFyGVPTLYAAMLADPNLPSEDQV-RLRLCTSAGEALPAEVGQRWQARFGV-DIVDGIGSTEMLHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 919 CVSQAKNS-KPGSCGFVTKGIRIKIADEKTGIaLGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSdGWLHTKDIGYYDE 997
Cdd:TIGR02262 319 FLSNLPGDvRYGTSGKPVPGYRLRLVGDGGQD-VADGEPGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGDKYVRND 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 998 NGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNL-P 1076
Cdd:TIGR02262 397 DGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLaP 476
|
490 500
....*....|....*....|...
gi 1820754837 1077 WycKLQAGIKFVNDFPRISTGKI 1099
Cdd:TIGR02262 477 Y--KYPRWIVFVDDLPKTATGKI 497
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
732-1054 |
1.59e-26 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 116.69 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 732 LPGFVSLANILEE----QVSRAEIDGfrctkidnpHDLAMICSSSGTTGMPKGTELSYAslyNSITPVEEVHAkneicAW 807
Cdd:PRK08974 180 LPDAISFRSALHKgrrmQYVKPELVP---------EDLAFLQYTGGTTGVAKGAMLTHR---NMLANLEQAKA-----AY 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 808 VPTIR------------WH--------------GGLNqcieVIMSNAKWIifsDDNIKEIalceiiQKHGVTWL-GTDTN 860
Cdd:PRK08974 243 GPLLHpgkelvvtalplYHifaltvncllfielGGQN----LLITNPRDI---PGFVKEL------KKYPFTAItGVNTL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 861 FAILyVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYGLTDAGGLCVSQAKNSK--PGSCGFVTKGI 938
Cdd:PRK08974 310 FNAL-LNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLT-GQYLLEGYGLTECSPLVSVNPYDLDyySGSIGLPVPST 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 939 RIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKL 1018
Cdd:PRK08974 388 EIKLVDDD-GNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNV 465
|
330 340 350
....*....|....*....|....*....|....*.
gi 1820754837 1019 SSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:PRK08974 466 YPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV 501
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1206-1679 |
1.76e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 119.11 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPmtarnfltltsPKIVFTVSS 1285
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPR-----------ERLAYMIED 1669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAAKELKMNLKVVvmdklDGYESV----EENVMKGHDTREIIEfkchVTNPDDVALIVPSSGTTGLPKGTEISH 1361
Cdd:PRK12467 1670 SGIELLLTQSHLQARLPLP-----DGLRSLvldqEDDWLEGYSDSNPAV----NLAPQNLAYVIYTSGSTGRPKGAGNRH 1740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1362 YSLFCCLHPYKNRTLVGHTCIVTPTMRWHY--GVLMAFRLVAANAKKLIVPD--NDDAENFCQLIEKYQITWFGTDPFMI 1437
Cdd:PRK12467 1741 GALVNRLCATQEAYQLSAADVVLQFTSFAFdvSVWELFWPLINGARLVIAPPgaHRDPEQLIQLIERQQVTTLHFVPSML 1820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1438 IKFIksQLLEKYRLPT-LKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVVSAQnKFTKLGSVGYVSSNVRIK 1516
Cdd:PRK12467 1821 QQLL--QMDEQVEHPLsLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHW-TCRRKDLEGRDSVPIGQP 1897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1517 MVDLDT---EEALGPNKI---GELRVKAITIMQGYHKNPETTKQAF------DSDGWL-RTGDLAYYDDNGEIYIVDRIS 1583
Cdd:PRK12467 1898 IANLSTyilDASLNPVPIgvaGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLyRTGDLARYRADGVIEYLGRID 1977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1584 DFINFRSINVSPAEIETVLMTHPAVLQAAVlgIPNE-VDEQHPKAFVV----QVPNKSVTEQ----ELISYVEKNLPDYc 1654
Cdd:PRK12467 1978 HQVKIRGFRIELGEIEARLREQGGVREAVV--IAQDgANGKQLVAYVVptdpGLVDDDEAQValraILKNHLKASLPEY- 2054
|
490 500
....*....|....*....|....*
gi 1820754837 1655 RLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK12467 2055 MVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
623-1044 |
2.19e-26 |
|
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: 115.12 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQkGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFvneeSAENLMEAAKEENLqvrvMVIGSLPGFVSLANILEeQVSRAE-IDGFRCTKI-------------DNPHDLAMI 768
Cdd:cd05909 82 VL----TSKQFIEKLKLHHL----FDVEYDARIVYLEDLRA-KISKADkCKAFLAGKFppkwllrifgvapVQPDDPAVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 769 CSSSGTTGMPKGTELSYASLYNS---ITPVEEVHAKNEICAWVPTirWHG-GLNQCIEVIMSNAKWIIFSDD--NIKEIA 842
Cdd:cd05909 153 LFTSGSEGLPKGVVLSHKNLLANveqITAIFDPNPEDVVFGALPF--FHSfGLTGCLWLPLLSGIKVVFHPNplDYKKIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 843 lcEIIQKHGVTWL-GTDTnFAILYVKMniFQKYPMPSLRkMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAGGLCVS 921
Cdd:cd05909 231 --ELIYDKKATILlGTPT-FLRGYARA--AHPEDFSSLR-LVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 922 QAKNS--KPGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENG 999
Cdd:cd05909 305 NTPQSpnKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEG 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1820754837 1000 EIFFVNRISDF--INYKAIKLSSAEiEGVLELHPSILKAVVVPVPHE 1044
Cdd:cd05909 384 FLTITGRLSRFakIAGEMVSLEAIE-DILSEILPEDNEVAVVSVPDG 429
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
629-1045 |
2.65e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 115.52 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHvvsklsaryflSLMSPKVVFVNEE 708
Cdd:PRK07470 34 TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNF-----------RQTPDEVAYLAEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAENLM----------EAAKEENLQVR-VMVIGSLPGFVSLANILEE----QVSRAEIDGfrctkiDNPhdlAMICSSSG 773
Cdd:PRK07470 103 SGARAMichadfpehaAAVRAASPDLThVVAIGGARAGLDYEALVARhlgaRVANAAVDH------DDP---CWFFFTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 774 TTGMPKGTELSYASLYNSITpveevhakNEICAWVPTIRW-----------HG-GLNQCIEViMSNAKWIIFSDDNIKEI 841
Cdd:PRK07470 174 TTGRPKAAVLTHGQMAFVIT--------NHLADLMPGTTEqdaslvvaplsHGaGIHQLCQV-ARGAATVLLPSERFDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 842 ALCEIIQKHGVTWLGTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHET-VAKIMPhtQILQCYGLTDAGGlCV 920
Cdd:PRK07470 245 EVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRaLAKLGK--VLVQYFGLGEVTG-NI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 921 S----------QAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTK 990
Cdd:PRK07470 322 TvlppalhdaeDGPDARIGTCGFERTGMEVQIQDDE-GRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 991 DIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHET 1045
Cdd:PRK07470 400 DLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPV 454
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
609-1099 |
2.81e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 115.62 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 609 RLSSKPDFVGQIDAfTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSK 688
Cdd:PRK06087 32 TARAMPDKIAVVDN-HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 689 LSARYFLSLMSPKVVF----VNEESAENLMEAAKEE--NLQVRVMVIGSLPGF--VSLANILEEQVSRAEidgFRCTKID 760
Cdd:PRK06087 111 AELVWVLNKCQAKMFFaptlFKQTRPVDLILPLQNQlpQLQQIVGVDKLAPATssLSLSQIIADYEPLTT---AITTHGD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 761 nphDLAMICSSSGTTGMPKGTELSYaslyNSITPVEEVHAK------NEIcAWVPTIRWH--GGLNQCIEVIMSNAKWII 832
Cdd:PRK06087 188 ---ELAAVLFTSGTEGLPKGVMLTH----NNILASERAYCArlnltwQDV-FMMPAPLGHatGFLHGVTAPFLIGARSVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 833 fsDDNIKEIALCEIIQKHGVTWLGTDTNFaiLYVKMNIFQKYP--MPSLRKMVITGAPFTKELHETVAKimPHTQILQCY 910
Cdd:PRK06087 260 --LDIFTPDACLALLEQQRCTCMLGATPF--IYDLLNLLEKQPadLSALRFFLCGGTTIPKKVARECQQ--RGIKLLSVY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 911 GLTDAgglcvSQAKNSKPGSC--------GFVTKGIRIKIADE--KTgiaLGPKERGEICIKSEFMMKGYHKNPEQTKEA 980
Cdd:PRK06087 334 GSTES-----SPHAVVNLDDPlsrfmhtdGYAAAGVEIKVVDEarKT---LPPGCEGEEASRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 981 FDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVqkVVEK 1060
Cdd:PRK06087 406 LDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYV--VLKA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1820754837 1061 EVTEEELHDLV----NKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK06087 484 PHHSLTLEEVVaffsRKRVAKY-KYPEHIVVIDKLPRTASGKI 525
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
41-548 |
2.86e-26 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 114.56 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 41 LVLEKLRSRPEFIAqVEAVTGaETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDN 120
Cdd:cd05918 4 LIEERARSQPDAPA-VCAWDG-SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 121 ELSPMTARYFLSLTKPKIVFVngesaeclaqvvkennmdtrlvvfadsagfvgraatltavlrsqdtawidefecaklTS 200
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVLT---------------------------------------------------------SS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 201 PKHVAAIVCSSGTSGFPKGTEISHAAMI-NYMAHVKVHDLkghvsmwTPSMRW-----YCglFIVikAILD--------- 265
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALStSALAHGRALGL-------TSESRVlqfasYT--FDV--SILEifttlaagg 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 266 CskrIIVP-DYDDDEGLCRFIEKYEVSWfrcdsCF--P--IRLvkfgvLSKYRLPTLKILLFGGahfkgE-LQQTLV-KL 338
Cdd:cd05918 174 C---LCIPsEEDRLNDLAGFINRLRVTW-----AFltPsvARL-----LDPEDVPSLRTLVLGG-----EaLTQSDVdTW 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 339 LPHTDVILSYGMTDYGGLCARQ--TKYSKPGSCGFVCeTGRLKVVDPNTGKVL---GAnkTGEIWAKSSYMMNGYYNNPE 413
Cdd:cd05918 236 ADRVRLINAYGPAECTIAATVSpvVPSTDPRNIGRPL-GATCWVVDPDNHDRLvpiGA--VGELLIEGPILARGYLNDPE 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 414 ATRRA-LDSDGWLH------------TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQH-PAVFQVAVVPV 479
Cdd:cd05918 313 KTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 480 PHNINEEHAM--AFVAkVPGKEVTELDITDLVKQNMPWYCRLHAGVK-----------------FMEKLPRTATGKIAKK 540
Cdd:cd05918 393 KPKDGSSSPQlvAFVV-LDGSSSGSGDGDSLFLEPSDEFRALVAELRsklrqrlpsymvpsvflPLSHLPLTASGKIDRR 471
|
....*...
gi 1820754837 541 QLKQIAKS 548
Cdd:cd05918 472 ALRELAES 479
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
627-1043 |
3.13e-26 |
|
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: 114.87 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 627 ECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVN 706
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 707 EESAENLMEAAKEENLQVRVMVIGSLPGF-------VSLANILEEQVSRAeidgfrctkidnPHDLAMICSSSGTTGMPK 779
Cdd:cd05932 86 KLDDWKAMAPGVPEGLISISLPPPSAANCqyqwddlIAQHPPLEERPTRF------------PEQLATLIYTSGTTGQPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 780 GTELSYASLynsitpveevhakneicAWvptirwhgGLNQCIEVIMSNAKWIIFSddnikEIALCEIIQK----HGVTWL 855
Cdd:cd05932 154 GVMLTFGSF-----------------AW--------AAQAGIEHIGTEENDRMLS-----YLPLAHVTERvfveGGSLYG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 856 GTDTNFA----------------------ILYVK--MNIFQKYPMPSLR---KMVITGAPFTKELHETV----------- 897
Cdd:cd05932 204 GVLVAFAesldtfvedvqrarptlffsvpRLWTKfqQGVQDKIPQQKLNlllKIPVVNSLVKRKVLKGLgldqcrlagcg 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 898 AKIMPHT----------QILQCYGLTDAGGLC-VSQAKNSKPGSCGFVTKGIRIKIADEktgialgpkerGEICIKSEFM 966
Cdd:cd05932 284 SAPVPPAllewyrslglNILEAYGMTENFAYShLNYPGRDKIGTVGNAGPGVEVRISED-----------GEILVRSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 967 MKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISD-FINYKAIKLSSAEIEGVLELHPSILKAVVV----PV 1041
Cdd:cd05932 353 MMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDiFKTSKGKYVAPAPIENKLAEHDRVEMVCVIgsglPA 432
|
..
gi 1820754837 1042 PH 1043
Cdd:cd05932 433 PL 434
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1206-1681 |
3.58e-26 |
|
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: 115.74 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLcsdnNLDVFLILLGTMY----IGAIsntwdHEL-----TPMTARNFLTLTS 1276
Cdd:cd05966 86 TYRELLREVCRFANVLKSLGVKKGDRVAI----YMPMIPELVIAMLacarIGAV-----HSVvfagfSAESLADRINDAQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1277 PKIVFTVSSS---------AANLMEAAKELKMNLKVVVMDKLDGYESVEE-------NVMKGHDTreiiEFKCHVTNPDD 1340
Cdd:cd05966 157 CKLVITADGGyrggkviplKEIVDEALEKCPSVEKVLVVKRTGGEVPMTEgrdlwwhDLMAKQSP----ECEPEWMDSED 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1341 VALIVPSSGTTGLPKGteISH----YSLFCC--------LHPyknrTLV-----------GHTCIVtptmrwhYGVLmaf 1397
Cdd:cd05966 233 PLFILYTSGSTGKPKG--VVHttggYLLYAAttfkyvfdYHP----DDIywctadigwitGHSYIV-------YGPL--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1398 rlvAANAKKLI---VPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIK--SQLLEKYRLPTLKVILSSGAHLRKE----- 1467
Cdd:cd05966 297 ---ANGATTVMfegTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVLGSVGEPINPEawmwy 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1468 HLEVMREKLPdvfITNHYGMTDT-----ACVVSAQNkfTKLGSVGYVSSNVRIKMVDLDTEEALGPNKiGELRVKAI--T 1540
Cdd:cd05966 374 YEVIGKERCP---IVDTWWQTETggimiTPLPGATP--LKPGSATRPFFGIEPAILDEEGNEVEGEVE-GYLVIKRPwpG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1541 IMQGYHKNPETTKQAFDSD--GWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPN 1618
Cdd:cd05966 448 MARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPH 527
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1619 EVDEQHPKAFVV---QVPNKSVTEQELISYVEKNL-----PDYcrlrggVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd05966 528 DIKGEAIYAFVTlkdGEEPSDELRKELRKHVRKEIgpiatPDK------IQFVPGLPKTRSGKIMRRILRK 592
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
40-542 |
4.20e-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: 114.22 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 40 ALVLEKLRSRPEFIAqveAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPW 118
Cdd:cd12117 1 ELFEEQAARTPDAVA---VVYGDRSlTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 119 DNELSPMTARYFLSLTKPKIVFVNGESAECLAQVVkennmdTRLVVFADSAGFVGRAATLTAvlrsqdtawidefecakl 198
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLE------VAVVIDEALDAGPAGNPAVPV------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 199 tSPKHVAAIVCSSGTSGFPKGTEISHAAMI------NYmahvkVHDLKGHVSMWTPSMRWYCGLFIVIKAILDCSKRIIV 272
Cdd:cd12117 134 -SPDDLAYVMYTSGSTGRPKGVAVTHRGVVrlvkntNY-----VTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 273 PDYD--DDEGLCRFIEKYEVS--W-----FRcdscfpiRLVKFGVLSkyrLPTLKILLFGG-----AHFKGELQQtlvkl 338
Cdd:cd12117 208 PKGTllDPDALGALIAEEGVTvlWltaalFN-------QLADEDPEC---FAGLRELLTGGevvspPHVRRVLAA----- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 339 LPHTDVILSYGMTDygglcarQTKYSkpgsCGFVCETG----------------RLKVVDPNtGKVLGANKTGEIWAKSS 402
Cdd:cd12117 273 CPGLRLVNGYGPTE-------NTTFT----TSHVVTELdevagsipigrpiantRVYVLDED-GRPVPPGVPGELYVGGD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 403 YMMNGYYNNPEATRRALDSDGWL------HTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAV 476
Cdd:cd12117 341 GLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 477 VPVPHNINEEHAMAFVakVPGKEVTELDITDLVKQNMPWYCRLHAGVkFMEKLPRTATGKIAKKQL 542
Cdd:cd12117 421 VVREDAGGDKRLVAYV--VAEGALDAAELRAFLRERLPAYMVPAAFV-VLDELPLTANGKVDRRAL 483
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
629-1100 |
4.25e-26 |
|
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: 114.86 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIicPwdhvVSKLSA------RYFLSLMSPKV 702
Cdd:COG1021 52 SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--P----VFALPAhrraeiSHFAEQSEAVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNEESA----ENLMEAAKEENLQVR-VMVIGSLPGFVSLANILEEQVSRAEIDgfrctkIDnPHDLAMICSSSGTTGM 777
Cdd:COG1021 126 YIIPDRHRgfdyRALARELQAEVPSLRhVLVVGDAGEFTSLDALLAAPADLSEPR------PD-PDDVAFFQLSGGTTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 778 PKG---TELSYasLYNsitpveeVHAKNEICAWVPTIR----------------------WHGGLnqcieVIMSNAkwii 832
Cdd:COG1021 199 PKLiprTHDDY--LYS-------VRASAEICGLDADTVylaalpaahnfplsspgvlgvlYAGGT-----VVLAPD---- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 833 FSDDNIkeialCEIIQKHGVTWLGTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHT-QilQCYG 911
Cdd:COG1021 261 PSPDTA-----FPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTlQ--QVFG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 912 LtdAGGLCvsqaknskpgsCG----------FVTKGiR-------IKIADEkTGIALGPKERGEICIKSEFMMKGYHKNP 974
Cdd:COG1021 334 M--AEGLV-----------NYtrlddpeeviLTTQG-RpispddeVRIVDE-DGNPVPPGEVGELLTRGPYTIRGYYRAP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 975 EQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:COG1021 399 EHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFV 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1820754837 1055 QKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:COG1021 479 VPRGEPLTLAELRRFLRERGLAAF-KLPDRLEFVDALPLTAVGKID 523
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
623-1044 |
5.30e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 115.10 E-value: 5.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTEN---HLntcVPVLAILYIGGIIC---P--------------- 681
Cdd:PRK05605 53 FFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNcpqHI---VAFYAVLRLGAVVVehnPlytahelehpfedhg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 682 ------WDHVVS---KLSARYFLslmsPKVVFVNEESAenlMEAAKEENLQV--------RVMVIGSLPGFVSLanileE 744
Cdd:PRK05605 130 arvaivWDKVAPtveRLRRTTPL----ETIVSVNMIAA---MPLLQRLALRLpipalrkaRAALTGPAPGTVPW-----E 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 745 QVSRAEIDGfRCTKIDNP----HDLAMICSSSGTTGMPKGTELSYASLYNSItpveeVHAKneicAWVPTIR-------- 812
Cdd:PRK05605 198 TLVDAAIGG-DGSDVSHPrptpDDVALILYTSGTTGKPKGAQLTHRNLFANA-----AQGK----AWVPGLGdgpervla 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 813 ----WHG-GLNQCIEVIMS-NAKWIIFSDDNIKEIAlcEIIQKHGVTWL-GTDTnfaiLYVKM-------NIfqkyPMPS 878
Cdd:PRK05605 268 alpmFHAyGLTLCLTLAVSiGGELVLLPAPDIDLIL--DAMKKHPPTWLpGVPP----LYEKIaeaaeerGV----DLSG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 879 LRKmVITGA----PFTKELHETVAKIMphtqILQCYGLTDAGGLCVSQAKNS--KPGSCGFVTKGIRIKIAD-EKTGIAL 951
Cdd:PRK05605 338 VRN-AFSGAmalpVSTVELWEKLTGGL----LVEGYGLTETSPIIVGNPMSDdrRPGYVGVPFPDTEVRIVDpEDPDETM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 952 GPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHP 1031
Cdd:PRK05605 413 PDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHP 491
|
490
....*....|...
gi 1820754837 1032 SILKAVVVPVPHE 1044
Cdd:PRK05605 492 GVEDAAVVGLPRE 504
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
624-1054 |
9.17e-26 |
|
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: 114.51 E-value: 9.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 624 TGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVV 703
Cdd:cd05968 88 TSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 704 FVNE---------ESAENLMEAAkEENLQVRVMVI---GSLPGFVSLANIL--EEQVSRAEiDGFRCTKIDNPhdlAMIC 769
Cdd:cd05968 168 ITADgftrrgrevNLKEEADKAC-AQCPTVEKVVVvrhLGNDFTPAKGRDLsyDEEKETAG-DGAERTESEDP---LMII 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 770 SSSGTTGMPKGTELSYASLynsitPVEEVH--------AKNEICAWVPTIRWHGGlnqcievimsnaKWIIF-------- 833
Cdd:cd05968 243 YTSGTTGKPKGTVHVHAGF-----PLKAAQdmyfqfdlKPGDLLTWFTDLGWMMG------------PWLIFgglilgat 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 834 ------SDDNIKEIALCEIIQKHGVTWLGTDTNF--AILYVKMNIFQKYPMPSLRKMVITGAPFTKE----LHETVAKim 901
Cdd:cd05968 306 mvlydgAPDHPKADRLWRMVEDHEITHLGLSPTLirALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEpwnwLFETVGK-- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 902 PHTQILQCYGLTD-AGG-LCVSQAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKErGEICIKSEF--MMKGYHKNPEQT 977
Cdd:cd05968 384 GRNPIINYSGGTEiSGGiLGNVLIKPIKPSSFNGPVPGMKADVLDES-GKPARPEV-GELVLLAPWpgMTRGFWRDEDRY 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 978 KEAFDS---DGWLHtKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:cd05968 462 LETYWSrfdNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFV 540
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
626-1099 |
9.25e-26 |
|
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: 112.56 E-value: 9.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 626 KECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIicpwdhvvsklsaryflslmspkVVFV 705
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAI-----------------------AVVI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 706 NEESAENLMEAAKEeNLQVRVMVIgslpgfvslanileeqvsraeidgfrctkidNPHDLAMICSSSGTTGMPKGTELSY 785
Cdd:cd05919 66 NPLLHPDDYAYIAR-DCEARLVVT-------------------------------SADDIAYLLYSSGTTGPPKGVMHAH 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 786 ASLYN----------SITPVEEVHAkneicawVPTIRWHGGL-NQCIEVIMSNAKWIIFSDDNIKEIALcEIIQKHGVTW 854
Cdd:cd05919 114 RDPLLfadamarealGLTPGDRVFS-------SAKMFFGYGLgNSLWFPLAVGASAVLNPGWPTAERVL-ATLARFRPTV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 855 L-GTDTNFAILYVKMNiFQKYPMPSLRKMVITGAPFTKELHEtvaKIMPHT--QILQCYGLTDAGGLCVS-QAKNSKPGS 930
Cdd:cd05919 186 LyGVPTFYANLLDSCA-GSPDALRSLRLCVSAGEALPRGLGE---RWMEHFggPILDGIGATEVGHIFLSnRPGAWRLGS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 931 CGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDF 1010
Cdd:cd05919 262 TGRPVPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDM 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1011 INYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV---QKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKF 1087
Cdd:cd05919 340 LKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVvlkSPAAPQESLARDIHRHLLERLSAH-KVPRRIAF 418
|
490
....*....|..
gi 1820754837 1088 VNDFPRISTGKI 1099
Cdd:cd05919 419 VDELPRTATGKL 430
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
65-476 |
1.06e-25 |
|
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: 111.97 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQ-GVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNG 143
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 144 ESAECLAQVVKENNMDTRLVVFADSAGFVgraatltavlrsqdtawidEFECAKLTSPKHVAAIVCSSGTSGFPKGTEIS 223
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPA-------------------PPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 224 HAAMINYMA-HVKVHDLKG-----HVS----------MWTPsmrWYCG--LFIVIKAILDcskriivpdyDDDEGLCRFI 285
Cdd:TIGR01733 142 HRSLVNLLAwLARRYGLDPddrvlQFAslsfdasveeIFGA---LLAGatLVVPPEDEER----------DDAALLAALI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 286 EKYEVSWFrcdSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYG---------MTDYGGL 356
Cdd:TIGR01733 209 AEHPVTVL---NLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGptettvwstATLVDPD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 357 CARQTK-----YSKPGScgfvcetgRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEAT-RRALDSDGWL----- 425
Cdd:TIGR01733 286 DAPRESpvpigRPLANT--------RLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNRPELTaERFVPDPFAGgdgar 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 426 --HTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAV 476
Cdd:TIGR01733 357 lyRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
38-542 |
1.07e-25 |
|
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: 113.19 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 38 VGALVLEKLRSRPEFIAqveaVTGAET--TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIs 115
Cdd:cd05920 17 LGDLLARSAARHPDRIA----VVDGDRrlTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 116 npwdnelsPMTA---------RYFLSLTKPKivfvngesaeclaqvvkennmdtrLVVFADSAGFVGRAATLTAVLRSQD 186
Cdd:cd05920 92 --------PVLAlpshrrselSAFCAHAEAV------------------------AYIVPDRHAGFDHRALARELAESIP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 187 TawidefecakltspkhVAAIVCSSGTSGFPKGTEISHAAMInYMAHVKVHdlkghVSMWTPSMRWYCGLFIVIKAILDC 266
Cdd:cd05920 140 E----------------VALFLLSGGTTGTPKLIPRTHNDYA-YNVRASAE-----VCGLDQDTVYLAVLPAAHNFPLAC 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 267 ----------SKRIIVPDYDDDEGLcRFIEKYEVSwfrCDSCFP---IRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQ 333
Cdd:cd05920 198 pgvlgtllagGRVVLAPDPSPDAAF-PLIEREGVT---VTALVPalvSLWLDAAASRRADLSSLRLLQVGGARLSPALAR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 334 TLVKLLPHTdVILSYGMTDyGGLCarQTKYSKPGScgFVCET-GR-------LKVVDPNtGKVLGANKTGEIWAKSSYMM 405
Cdd:cd05920 274 RVPPVLGCT-LQQVFGMAE-GLLN--YTRLDDPDE--VIIHTqGRpmspddeIRVVDEE-GNPVPPGEEGELLTRGPYTI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 406 NGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINE 485
Cdd:cd05920 347 RGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLG 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 486 EHAMAFVakVP-GKEVTELDITDLVKQNMPWYCRLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:cd05920 427 ERSCAFV--VLrDPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
61-543 |
1.23e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 113.06 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVF 140
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 141 VNGESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDtawidefecakltspkhVAAIVCSSGTSGFPKGT 220
Cdd:PRK06145 105 VDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTD-----------------LVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 221 ----------EISHAAMINYMA-----------HVKVHDLKGHVSMWTpsmrwycGLFIVIKAildcskriivpDYDDDE 279
Cdd:PRK06145 168 mhsygnlhwkSIDHVIALGLTAserllvvgplyHVGAFDLPGIAVLWV-------GGTLRIHR-----------EFDPEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 280 GLCRfIEKYEVS--WFRcdscfPIRLVKFGVL---SKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDYG 354
Cdd:PRK06145 230 VLAA-IERHRLTcaWMA-----PVMLSRVLTVpdrDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 355 G---LCARQTKYSKPGSCGFVCETGRLKVVDpNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLG 431
Cdd:PRK06145 304 SgdtLMEAGREIEKIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 432 YYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQ 511
Cdd:PRK06145 382 YLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQ 461
|
490 500 510
....*....|....*....|....*....|..
gi 1820754837 512 NMPWYcRLHAGVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK06145 462 RLASF-KVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
609-1099 |
1.46e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 113.70 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 609 RLSSKPdfvgqidAFT--GKECTYAEMRERSIKCALWLRKH-GIQKGDNIGILTENHLNTCVPVLAILYIGGIIC----- 680
Cdd:PRK05677 36 RFADKP-------AFSnlGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 681 ----PWDHVVSKLSARYFLSLMS---------PKV----VFVNEES------AENLMEAAKEenlQVRVMVIG-SLPGFV 736
Cdd:PRK05677 109 ytarEMEHQFNDSGAKALVCLANmahlaekvlPKTgvkhVIVTEVAdmlpplKRLLINAVVK---HVKKMVPAyHLPQAV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 737 SLANILeeqvSRAEIDGFRCTKIdNPHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEVHAKN--EIC----AWVPT 810
Cdd:PRK05677 186 KFNDAL----AKGAGQPVTEANP-QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNlnEGCeiliAPLPL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 811 IRWHGGLNQCIEVIMSNAKWIIFSddNIKEI-ALCEIIQKHGVT-WLGTDTNFAILyVKMNIFQKYPMPSLRKMVITGAP 888
Cdd:PRK05677 261 YHIYAFTFHCMAMMLIGNHNILIS--NPRDLpAMVKELGKWKFSgFVGLNTLFVAL-CNNEAFRKLDFSALKLTLSGGMA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 889 FTKELHETvAKIMPHTQILQCYGLTDAGGL-CVSQAKNSKPGSCGFVTKGIRIK-IADEKTGIALGpkERGEICIKSEFM 966
Cdd:PRK05677 338 LQLATAER-WKEVTGCAICEGYGMTETSPVvSVNPSQAIQVGTIGIPVPSTLCKvIDDDGNELPLG--EVGELCVKGPQV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 967 MKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETD 1046
Cdd:PRK05677 415 MKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKS 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1047 IELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK05677 495 GEAIKVFVVVKPGETLTKEQVMEHMRANLTGY-KVPKAVEFRDELPTTNVGKI 546
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
344-544 |
1.89e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.01 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 344 VILSYGMTD-YGGLCARQTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKT-GEIWAKSSYMMNGYYNNPEATRRALDS 421
Cdd:PRK07787 269 PVERYGMTEtLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETvGELQVRGPTLFDGYLNRPDATAAAFTA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 422 DGWLHTGDLGYYDNDGEVFLVDRMS-EFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVakVPGKEV 500
Cdd:PRK07787 349 DGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV--VGADDV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1820754837 501 TELDITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK07787 427 AADELIDFVAQQLSVHKRPRE-VRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
629-1054 |
2.65e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.45 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFV--- 705
Cdd:PRK13295 57 TYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpkt 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 706 -----NEESAENLMEAAKEenLQvRVMVIGSlPGFVSLANIL------EEQVSRAEIDGFRctkiDNPHDLAMICSSSGT 774
Cdd:PRK13295 137 frgfdHAAMARRLRPELPA--LR-HVVVVGG-DGADSFEALLitpaweQEPDAPAILARLR----PGPDDVTQLIYTSGT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 775 TGMPKGTELSYASLYNSITP-VEEVHAKNEICAWVPTIRWH--GGLNQCIEVIMSNAKwIIFSD--DNIKEIALceiIQK 849
Cdd:PRK13295 209 TGEPKGVMHTANTLMANIVPyAERLGLGADDVILMASPMAHqtGFMYGLMMPVMLGAT-AVLQDiwDPARAAEL---IRT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 850 HGVTWLGTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYGLTDAG---GLCVSQAKNS 926
Cdd:PRK13295 285 EGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAAL-GAKIVSAWGMTENGavtLTKLDDPDER 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 927 KPGSCGFVTKGIRIKIADEkTGIALGPKERGEICIKSEFMMKGYHKNPEQTkeAFDSDGWLHTKDIGYYDENGEIFFVNR 1006
Cdd:PRK13295 364 ASTTDGCPLPGVEVRVVDA-DGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGR 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1820754837 1007 ISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:PRK13295 441 SKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFV 488
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1206-1680 |
2.66e-25 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 111.31 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheltpmtarnFLTL--TSP--KIVF 1281
Cdd:cd17649 14 SYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGA---------------YVPLdpEYPaeRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1282 TVSSSAANLMEAAkelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchvtNPDDVALIVPSSGTTGLPKGTEISH 1361
Cdd:cd17649 79 MLEDSGAGLLLTH------------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1362 YSL--FCC-------LHPyKNRTL--------VGHTCIVTPtmrwhygvlmafrlVAANAKKLIVPDN--DDAENFCQLI 1422
Cdd:cd17649 117 GPLaaHCQataerygLTP-GDRELqfasfnfdGAHEQLLPP--------------LICGACVVLRPDElwASADELAEMV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1423 EKYQITWFGTDPFMIikfikSQLLEKY------RLPTLKVILSSGAHLRKEHLEvmREKLPDVFITNHYG-----MTDTA 1491
Cdd:cd17649 182 RELGVTVLDLPPAYL-----QQLAEEAdrtgdgRPPSLRLYIFGGEALSPELLR--RWLKAPVRLFNAYGpteatVTPLV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1492 CVVSAQNKFtkLGS---VGYVSSNVRIKMVDldteEALGP---NKIGELRVKAITIMQGYHKNPETTKQAF--DSDG--- 1560
Cdd:cd17649 255 WKCEAGAAR--AGAsmpIGRPLGGRSAYILD----ADLNPvpvGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapg 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1561 --WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHpKAFVVQVPNKSVT 1638
Cdd:cd17649 329 srLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL-VAYVVLRAAAAQP 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1820754837 1639 E--QELISYVEKNLPDY---CRLrggvKIVDQLPRTTTGKIARKQLR 1680
Cdd:cd17649 408 ElrAQLRTALRASLPDYmvpAHL----VFLARLPLTPNGKLDRKALP 450
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
764-1100 |
3.28e-25 |
|
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: 108.57 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 764 DLAMICSSSGTTGMPKGTELSYASLYNSITPVEEVHAKNEICAW---VPTIRWhGGLNQCIEVIMSNAKWIIFSddniKE 840
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWllsLPLYHV-GGLAILVRSLLAGAELVLLE----RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 841 IALCEIIQKHGVTWLG-TDTnfAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKImpHTQILQCYGLTD-AGGL 918
Cdd:cd17630 76 QALAEDLAPPGVTHVSlVPT--QLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTEtASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 919 CVSQAKNSKPGSCGFVTKGIRIKIADektgialgpkeRGEICIKSEFMMKGYHKNPEQtkEAFDSDGWLHTKDIGYYDEN 998
Cdd:cd17630 152 ATKRPDGFGRGGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 999 GEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVqkVVEKEVTEEELHDLVNKNLPWY 1078
Cdd:cd17630 219 GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI--VGRGPADPAELRAWLKDKLARF 296
|
330 340
....*....|....*....|..
gi 1820754837 1079 cKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd17630 297 -KLPKRIYPVPELPRTGGGKVD 317
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1390-1672 |
4.16e-25 |
|
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: 108.54 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1390 HYGVLM-AFRLVAANAKKLIVPdNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKvilsSGAHLRKEH 1468
Cdd:cd17636 52 HIGTLMfTLATFHAGGTNVFVR-RVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLR----SSPAAPEWN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1469 LEVMREKLPDVFITNHYGMTD-TACVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHK 1547
Cdd:cd17636 127 DMATVDTSPWGRKPGGYGQTEvMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGRE-VPDGEVGEIVARGPTVMAGYWN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1548 NPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKA 1627
Cdd:cd17636 206 RPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKA 284
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1820754837 1628 FVVQVPNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTG 1672
Cdd:cd17636 285 IVVLKPGASVTEAELIEHCRARIASYKKPK-SVEFADALPRTAGG 328
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-544 |
4.52e-25 |
|
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: 110.30 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNge 144
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 saeclaqvvkennMDTRlvvfadsagfvgraatltavlrsqdtawidefecAKLTSPKHVaaIVCSSGTSGFPKGTEISH 224
Cdd:cd05973 80 -------------AANR----------------------------------HKLDSDPFV--MMFTSGTTGLPKGVPVPL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AAMINYMAHVKVH-DLKGHVSMWT---PSmrWYCGLFIVIKAILDCSKRIIVpdydddeglcrfiekYEVSwFRCDSCFP 300
Cdd:cd05973 111 RALAAFGAYLRDAvDLRPEDSFWNaadPG--WAYGLYYAITGPLALGHPTIL---------------LEGG-FSVESTWR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 301 IrLVKFGVLSKYRLPTL-KILLFGG----AHFKGELQQTLVKLLPHTDVILS-------------YGMTDYGGLCARQTK 362
Cdd:cd05973 173 V-IERLGVTNLAGSPTAyRLLMAAGaevpARPKGRLRRVSSAGEPLTPEVIRwfdaalgvpihdhYGQTELGMVLANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 363 YSKP---GSCGFVCETGRLKVVDPNtGKVLGANKTG--EIWAKSSYMM--NGYYNNPEATRraldSDGWLHTGDLGYYDN 435
Cdd:cd05973 252 LEHPvhaGSAGRAMPGWRVAVLDDD-GDELGPGEPGrlAIDIANSPLMwfRGYQLPDTPAI----DGGYYLTGDTVEFDP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 436 DGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTElDITDLVKQNMPW 515
Cdd:cd05973 327 DGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTP-ALADELQLHVKK 405
|
490 500 510
....*....|....*....|....*....|..
gi 1820754837 516 YCRLHA---GVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:cd05973 406 RLSAHAyprTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
602-1100 |
4.64e-25 |
|
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: 110.88 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 602 VGELVLNRLSSKPDFVGQIDAftGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGG--II 679
Cdd:cd05920 17 LGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAvpVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 680 CPWDHVVSKLSarYFLSLMSPKVVFVNEESAenlmeaakeenlqvrvmvigslpGFVSLANILEEQVSRAEIdgfrctki 759
Cdd:cd05920 95 ALPSHRRSELS--AFCAHAEAVAYIVPDRHA-----------------------GFDHRALARELAESIPEV-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 760 dnphdlAMICSSSGTTGMPK---GTELSYAslYNsitpveeVHAKNEICAWVPTIRW-------HGGLNQC---IEVIMS 826
Cdd:cd05920 142 ------ALFLLSGGTTGTPKlipRTHNDYA--YN-------VRASAEVCGLDQDTVYlavlpaaHNFPLACpgvLGTLLA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 827 NAKwIIFSDDNIKEIALcEIIQKHGVTWLGTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQI 906
Cdd:cd05920 207 GGR-VVLAPDPSPDAAF-PLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 907 LQCYGLtdAGGLcVSQAKNSKPGSCGFVTKGiR-------IKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKE 979
Cdd:cd05920 284 QQVFGM--AEGL-LNYTRLDDPDEVIIHTQG-RpmspddeIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYRAPEHNAR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 980 AFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVE 1059
Cdd:cd05920 359 AFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDP 438
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1820754837 1060 KEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd05920 439 PPSAAQLRRFLRERGLAAY-KLPDRIEFVDSLPLTAVGKID 478
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
65-543 |
5.76e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 111.91 E-value: 5.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVnge 144
Cdd:PRK04319 75 TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAECLAQVVKEN--NMDTRLVVFADS---AGFVGRAATLTAVLRSQDTAWIDEFECAKLtspkHVaaivcSSGTSGFPKG 219
Cdd:PRK04319 152 TPALLERKPADDlpSLKHVLLVGEDVeegPGTLDFNALMEQASDEFDIEWTDREDGAIL----HY-----TSGSTGKPKG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 220 TEISHAAMINYMAHVK-VHDLKGHVSMW-TPSMRWYCGLFIVIKAILDCSKRIIVpdyddDEGlcRF--------IEKYE 289
Cdd:PRK04319 223 VLHVHNAMLQHYQTGKyVLDLHEDDVYWcTADPGWVTGTSYGIFAPWLNGATNVI-----DGG--RFsperwyriLEDYK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 290 VS-WFRCDSCFPiRLVKFG--VLSKYRLPTLKILLFGGAHFKGEL----QQTLVklLPHTDvilSYGMTDYGG--LCARQ 360
Cdd:PRK04319 296 VTvWYTAPTAIR-MLMGAGddLVKKYDLSSLRHILSVGEPLNPEVvrwgMKVFG--LPIHD---NWWMTETGGimIANYP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 361 TKYSKPGSCGFV---CETGrlkVVDpNTGKVLGANKTGEIWAKSSY--MMNGYYNNPEATRRALdSDGWLHTGDLGYYDN 435
Cdd:PRK04319 370 AMDIKPGSMGKPlpgIEAA---IVD-DQGNELPPNRMGNLAIKKGWpsMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 436 DGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTE---LDITDLVKQn 512
Cdd:PRK04319 445 DGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEelkEEIRGFVKK- 523
|
490 500 510
....*....|....*....|....*....|....*.
gi 1820754837 513 mpwycRLHAGV-----KFMEKLPRTATGKIAKKQLK 543
Cdd:PRK04319 524 -----GLGAHAapreiEFKDKLPKTRSGKIMRRVLK 554
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
37-537 |
5.87e-25 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 111.90 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 37 NVGALVLEK-LRSRPEFIAQV---EAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYL 111
Cdd:cd17634 53 NLAANALDRhLRENGDRTAIIyegDDTSQSRTiSYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 112 GAISNPWDNELSPMTARYFLSLTKPKIVFVNGESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDTAWID 191
Cdd:cd17634 133 GAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLW 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 192 EFECAKLTSPKHVAA---------IVCSSGTSGFPKGTEISHAAMINY----MAHV-KVHdlKGHVSMWTPSMRWYCGLF 257
Cdd:cd17634 213 WRDLIAKASPEHQPEamnaedplfILYTSGTTGKPKGVLHTTGGYLVYaattMKYVfDYG--PGDIYWCTADVGWVTGHS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 258 IVIKAILDCSKRII----VPDYDDDEGLCRFIEKYEVSWFRCdSCFPIR-LVKFG--VLSKYRLPTLKILLFGGAHFKGE 330
Cdd:cd17634 291 YLLYGPLACGATTLlyegVPNWPTPARMWQVVDKHGVNILYT-APTAIRaLMAAGddAIEGTDRSSLRILGSVGEPINPE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 331 LQQTLVKLLPHTD--VILSYGMTDYGGLCA--RQTKYSKPGSCGFVCETG-RLKVVDpNTGKVLGANKTGEIWAKSSY-- 403
Cdd:cd17634 370 AYEWYWKKIGKEKcpVVDTWWQTETGGFMItpLPGAIELKAGSATRPVFGvQPAVVD-NEGHPQPGGTEGNLVITDPWpg 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 404 MMNGYYNNPEatrRALDS-----DGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVP 478
Cdd:cd17634 449 QTRTLFGDHE---RFEQTyfstfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVG 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 479 VPHNINEEHAMAFVAKVPGKEVT-EL--DITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKI 537
Cdd:cd17634 526 IPHAIKGQAPYAYVVLNHGVEPSpELyaELRNWVRKEIGPLATPDV-VHWVDSLPKTRSGKI 586
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1202-1680 |
6.70e-25 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 111.89 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVF 1281
Cdd:PRK08279 60 DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1282 TVSSSAANLMEAAKELKMNLKVVVMDKLDGYESVE-ENVMKGHDTreiiefkCHVTNP--------DDVALIVPSSGTTG 1352
Cdd:PRK08279 140 VGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGyEDLAAAAAG-------APTTNPasrsgvtaKDTAFYIYTSGTTG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1353 LPKGTEISHYSLFCCLHPYknrtlvGHTCIVTPTMR-------WH-YGVLMAFRLVAANAKKLIVPDNDDAENFCQLIEK 1424
Cdd:PRK08279 213 LPKAAVMSHMRWLKAMGGF------GGLLRLTPDDVlycclplYHnTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1425 YQITwfgtdPFMIIKFIKSQLL-----EKYRLPTLKVILssGAHLRKEHLEVM--REKLPDVFitNHYGMTDtaCVVSAQ 1497
Cdd:PRK08279 287 YRAT-----AFQYIGELCRYLLnqppkPTDRDHRLRLMI--GNGLRPDIWDEFqqRFGIPRIL--EFYAASE--GNVGFI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1498 NKFTKLGSVGYV----SSNVRIKMVDLDTEEAL----------GPNKIGEL--RVKAITIMQGYhKNPETTKQ-----AF 1556
Cdd:PRK08279 356 NVFNFDGTVGRVplwlAHPYAIVKYDVDTGEPVrdadgrcikvKPGEVGLLigRITDRGPFDGY-TDPEASEKkilrdVF 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1557 -DSDGWLRTGDLAYYDDNGEIYIVDRISDfiNFR--SINVSPAEIETVLMTHPAVLQAAVLGipnevdeqhpkafvVQVP 1633
Cdd:PRK08279 435 kKGDAWFNTGDLMRDDGFGHAQFVDRLGD--TFRwkGENVATTEVENALSGFPGVEEAVVYG--------------VEVP 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1634 NksvTE------------------QELISYVEKNLPDYCR---LRggvkIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK08279 499 G---TDgragmaaivladgaefdlAALAAHLYERLPAYAVplfVR----LVPELETTGTFKYRKVDLR 559
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
764-1099 |
6.80e-25 |
|
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: 107.59 E-value: 6.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 764 DLAMICSSSGTTGMPKGTELSY---ASLYNSITPVEEVHAKNEICAWVPTIRWHGGLNQCIEVIMSNAKWI---IFSDDn 837
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrqtLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVpvaVFDVD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 838 ikeiALCEIIQKHGVTWL-GTDTNF-AILYVKMNifQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDA 915
Cdd:cd17638 80 ----AILEAIERERITVLpGPPTLFqSLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 916 GglCVSQAKNSKP-----GSCGFVTKGIRIKIADEktgialgpkerGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTK 990
Cdd:cd17638 154 G--VATMCRPGDDaetvaTTCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 991 DIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDL 1070
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAW 300
|
330 340
....*....|....*....|....*....
gi 1820754837 1071 VNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:cd17638 301 CRERLANY-KVPRFVRFLDELPRNASGKV 328
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
607-1054 |
7.52e-25 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 111.43 E-value: 7.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 607 LNRLSS-KPDFVgqIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHV 685
Cdd:PLN02860 13 LTRLATlRGNAV--VTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 686 VSKLSARYFLSLMSPkVVFVNEESAEN---LMEAAKEENLQVRV-MVIGSLPGFVSLANILEEQVSRAEidGFRCTKID- 760
Cdd:PLN02860 91 WSFEEAKSAMLLVRP-VMLVTDETCSSwyeELQNDRLPSLMWQVfLESPSSSVFIFLNSFLTTEMLKQR--ALGTTELDy 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 761 --NPHDLAMICSSSGTTGMPKGTELSYASLynsitpVEEVHAKNEICAWVPT-IRWH-------GGLNQCIEVIMSNAKW 830
Cdd:PLN02860 168 awAPDDAVLICFTSGTTGRPKGVTISHSAL------IVQSLAKIAIVGYGEDdVYLHtaplchiGGLSSALAMLMVGACH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 831 IIFSDDNIKeiALCEIIQKHGVTWLGTDTnfAIL-----YVKMNIFQKyPMPSLRKMVITGAPFTKELHETVAKIMPHTQ 905
Cdd:PLN02860 242 VLLPKFDAK--AALQAIKQHNVTSMITVP--AMMadlisLTRKSMTWK-VFPSVRKILNGGGSLSSRLLPDAKKLFPNAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 906 ILQCYGLTDA-----------------------GGLCVSQAKNSKPGSC-GFVTKGIRIKIADEktgialGPKERGEICI 961
Cdd:PLN02860 317 LFSAYGMTEAcssltfmtlhdptlespkqtlqtVNQTKSSSVHQPQGVCvGKPAPHVELKIGLD------ESSRVGRILT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 962 KSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPV 1041
Cdd:PLN02860 391 RGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
490
....*....|...
gi 1820754837 1042 PHETDIELPLAFV 1054
Cdd:PLN02860 471 PDSRLTEMVVACV 483
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
45-543 |
9.30e-25 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 110.88 E-value: 9.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 45 KLRSRPEFIAQveavtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLG-AISNPwdNEL- 122
Cdd:PRK07059 35 QYADRPAFICM-----GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGyVVVNV--NPLy 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 123 SPMTARYFLSLTKPKIVFVNGESAECLAQVVkeNNMDTRLVVFA---DSAGFVGRAATLtaVLRSQDT---AW-IDEF-- 193
Cdd:PRK07059 108 TPRELEHQLKDSGAEAIVVLENFATTVQQVL--AKTAVKHVVVAsmgDLLGFKGHIVNF--VVRRVKKmvpAWsLPGHvr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 194 ------ECAKLT------SPKHVAAIVCSSGTSGFPKGTEISHAamiNYMAHV--------KVHDLKGHVSMwtpsmrwy 253
Cdd:PRK07059 184 fndalaEGARQTfkpvklGPDDVAFLQYTGGTTGVSKGATLLHR---NIVANVlqmeawlqPAFEKKPRPDQ-------- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 254 cgLFIV-------IKAILDCS--------KRIIVPDYDDDEGLCRFIEKYEVSwfrcdsCFPIRLVKFGVL------SKY 312
Cdd:PRK07059 253 --LNFVcalplyhIFALTVCGllgmrtggRNILIPNPRDIPGFIKELKKYQVH------IFPAVNTLYNALlnnpdfDKL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 313 RLPTLKILLFGGAHFKGELQQTLVKLLpHTDVILSYGM--TDYGGLCARQTKYSKPGSCGFVCETGRLKVVDpNTGKVLG 390
Cdd:PRK07059 325 DFSKLIVANGGGMAVQRPVAERWLEMT-GCPITEGYGLseTSPVATCNPVDATEFSGTIGLPLPSTEVSIRD-DDGNDLP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 391 ANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPA 470
Cdd:PRK07059 403 LGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 471 VFQVAVVPVPHNINEEHAMAFVAKvPGKEVTELDITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK07059 483 VLEVAAVGVPDEHSGEAVKLFVVK-KDPALTEEDVKAFCKERLTNYKRPKF-VEFRTELPKTNVGKILRRELR 553
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1206-1679 |
1.38e-24 |
|
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: 109.30 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELtPmTARN---------FLTLTS 1276
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-P-ADRLryiledaepALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1277 PKIVFTVSSSAanlmeaakelkmnlkVVVMDKLDGYESVEENVMKGhdtreiiefkchvTNPDDVALIVPSSGTTGLPKG 1356
Cdd:cd12116 92 DALPDRLPAGL---------------PVLLLALAAAAAAPAAPRTP-------------VSPDDLAYVIYTSGSTGRPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1357 TEISHYSLFCCLHPYKNRTLVGHTC----IVTPTmrWHYGVLMAFRLVAANAKKLIVPDND--DAENFCQLIEKYQITWF 1430
Cdd:cd12116 144 VVVSHRNLVNFLHSMRERLGLGPGDrllaVTTYA--FDISLLELLLPLLAGARVVIAPRETqrDPEALARLIEAHSITVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1431 GTDPfmiikfiksqllekyrlPTLKVILSSG----AHLRkehLEVMREKLPDVF----------ITNHYGMTDTACVVSA 1496
Cdd:cd12116 222 QATP-----------------ATWRMLLDAGwqgrAGLT---ALCGGEALPPDLaarllsrvgsLWNLYGPTETTIWSTA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1497 QNKFTKLGSV--GYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDG-------WLRTGDL 1567
Cdd:cd12116 282 ARVTAAAGPIpiGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPfagpgsrLYRTGDL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1568 AYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEvDEQHPKAFVVQVPNKSVTEQELISYVE 1647
Cdd:cd12116 361 VRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDAAALRAHLR 439
|
490 500 510
....*....|....*....|....*....|..
gi 1820754837 1648 KNLPDYCrLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:cd12116 440 ATLPAYM-VPSAFVRLDALPLTANGKLDRKAL 470
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1190-1682 |
1.65e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 110.08 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1190 KPDSIGQVDaltGKVQ-TYADMSERSIKCALWLKKQGVKPGDIiGLCSDNNLD----VFLILL--GTMYIGAISNTWDHE 1262
Cdd:PRK10946 36 ASDAIAVIC---GERQfSYRELNQASDNLACSLRRQGIKPGDT-ALVQLGNVAefyiTFFALLklGVAPVNALFSHQRSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1263 LTPmtarnFLTLTSPKIVftVSSSAANL------MEAAKELKMNLKVVVMDKLDGYESVEENVMKGHDTreiieFKCHVT 1336
Cdd:PRK10946 112 LNA-----YASQIEPALL--IADRQHALfsdddfLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPAED-----FTATPS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1337 NPDDVALIVPSSGTTGLPKGTEISHYSLFcclhpYKNRTLVgHTCIVTPTMRW-------H---------YGVLMAFRLV 1400
Cdd:PRK10946 180 PADEVAFFQLSGGSTGTPKLIPRTHNDYY-----YSVRRSV-EICGFTPQTRYlcalpaaHnypmsspgaLGVFLAGGTV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1401 aanakklIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYR--LPTLKVILSSGAHLrKEHL-----EVMR 1473
Cdd:PRK10946 254 -------VLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRaqLASLKLLQVGGARL-SETLarripAELG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1474 EKLPDVFitnhyGMTD-----TACVVSAQNKFTKLGSVgyVSSNVRIKMVDLDTEEaLGPNKIGELRVKAITIMQGYHKN 1548
Cdd:PRK10946 326 CQLQQVF-----GMAEglvnyTRLDDSDERIFTTQGRP--MSPDDEVWVADADGNP-LPQGEVGRLMTRGPYTFRGYYKS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1549 PETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAF 1628
Cdd:PRK10946 398 PQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAF 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1629 -VVQVPNKSVT------EQELISYvekNLPDYcrlrggVKIVDQLPRTTTGKIARKQLRDM 1682
Cdd:PRK10946 478 lVVKEPLKAVQlrrflrEQGIAEF---KLPDR------VECVDSLPLTAVGKVDKKQLRQW 529
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1195-1679 |
1.74e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 112.57 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1195 GQVDALT--GKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELtPMTARNFL 1272
Cdd:PRK05691 2202 PQAPALTfaGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY-PLERLHYM 2280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1273 TLTSpKIVFTVSSSAanLMEAAKELKMNLKVVVMDK----LDGYESVEENVMKGhdtreiiefkchvtnPDDVALIVPSS 1348
Cdd:PRK05691 2281 IEDS-GIGLLLSDRA--LFEALGELPAGVARWCLEDdaaaLAAYSDAPLPFLSL---------------PQHQAYLIYTS 2342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1349 GTTGLPKGTEISHYSL----------F------CCLHPYKNRTLVGHTCIVTPtmrwhygVLMAFRLVaanakkLIVPDN 1412
Cdd:PRK05691 2343 GSTGKPKGVVVSHGEIamhcqavierFgmraddCELHFYSINFDAASERLLVP-------LLCGARVV------LRAQGQ 2409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1413 DDAENFCQLIEKYQITWFGTDPFMiikfiKSQLL-----EKYRLPtLKVILSSGAHLRKEHLEVMREKL-PDVFItNHYG 1486
Cdd:PRK05691 2410 WGAEEICQLIREQQVSILGFTPSY-----GSQLAqwlagQGEQLP-VRMCITGGEALTGEHLQRIRQAFaPQLFF-NAYG 2482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1487 MTDT-----ACVVSAQNKfTKLGSV--GYVSSNvRIKMVdLDTEEALGPN-KIGELRVKAITIMQGYHKNPETTKQ---- 1554
Cdd:PRK05691 2483 PTETvvmplACLAPEQLE-EGAASVpiGRVVGA-RVAYI-LDADLALVPQgATGELYVGGAGLAQGYHDRPGLTAErfva 2559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1555 -AFDSDG--WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQ 1631
Cdd:PRK05691 2560 dPFAADGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSA 2639
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1632 VPNKSVTEQE-----LISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK05691 2640 VAGQDDEAQAalreaLKAHLKQQLPDY-MVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
201-546 |
1.93e-24 |
|
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: 107.18 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 201 PKHVAAIVCSSGTSGFPKGTEISHAAMInYMAHVKvhdlkGHVSMWTPSMRWYCGL--------FIVIKAILDCSKRIIV 272
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEV-YNAWML-----ALNSLFDPDDVLLCGLplfhvngsVVTLLTPLASGAHVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 273 PD---------YDDdegLCRFIEKYEVSWFrcdSCFPIRL-VKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHT 342
Cdd:cd05944 75 AGpagyrnpglFDN---FWKLVERYRITSL---STVPTVYaALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 343 dVILSYGMTDygGLCARQTKY----SKPGSCGF---VCETgRLKVVDPNTGKVL--GANKTGEIWAKSSYMMNGYYNNpE 413
Cdd:cd05944 149 -VVEGYGLTE--ATCLVAVNPpdgpKRPGSVGLrlpYARV-RIKVLDGVGRLLRdcAPDEVGEICVAGPGVFGGYLYT-E 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 414 ATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVA 493
Cdd:cd05944 224 GNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQ 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 494 KVPGKEVTELDITDLVKQNMPWYCRLHAGVKFMEKLPRTATGKIAKKQLKQIA 546
Cdd:cd05944 304 LKPGAVVEEEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
847-1100 |
2.03e-24 |
|
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: 109.00 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 847 IQKHGVTWLGT-DTNFA-ILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPhTQILQCYGLTDAGGLCVSQAK 924
Cdd:cd05929 212 IERYRVTFAQFvPTMFVrLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGG-PIIWEYYGGTEGQGLTIINGE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 925 N--SKPGSCGFVTKGiRIKIADEKtGIALGPKERGEIcikseFMMKG----YHKNPEQTKEAFDSDGWLHTKDIGYYDEN 998
Cdd:cd05929 291 EwlTHPGSVGRAVLG-KVHILDED-GNEVPPGEIGEV-----YFANGpgfeYTNDPEKTAAARNEGGWSTLGDVGYLDED 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 999 GEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEE---LHDLVNKNL 1075
Cdd:cd05929 364 GYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALaeeLIAFLRDRL 443
|
250 260
....*....|....*....|....*
gi 1820754837 1076 PWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd05929 444 SRY-KCPRSIEFVAELPRDDTGKLY 467
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1177-1679 |
2.56e-24 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 111.67 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1177 VNIAEETLKFLKSK-----PDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMY 1251
Cdd:PRK10252 453 VEIPETTLSALVAQqaaktPDAPALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1252 IGAISNTWDHELTPMTARNFLTLTSPKIVFTVSSSAANLMEAAKelkmnLKVVVMDKLDGYESVEENVMkghdtreiief 1331
Cdd:PRK10252 531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPD-----LTSLCYNAPLAPQGAAPLQL----------- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1332 kchvTNPDDVALIVPSSGTTGLPKGTeishyslfcclhpyknrtLVGHTCIVTPT--MRWHYGV---------------- 1393
Cdd:PRK10252 595 ----SQPHHTAYIIFTSGSTGRPKGV------------------MVGQTAIVNRLlwMQNHYPLtaddvvlqktpcsfdv 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1394 --------LMA-FRLVAANakklivPD-NDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLP--TLKVILSSG 1461
Cdd:PRK10252 653 svweffwpFIAgAKLVMAE------PEaHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQScaSLRQVFCSG 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1462 ----AHLRKEHlevmrEKLPDVFITNHYGMTDTACVVS-----AQNKFTKLGS---VGYVSSNVRIKMVDlDTEEALGPN 1529
Cdd:PRK10252 727 ealpADLCREW-----QQLTGAPLHNLYGPTEAAVDVSwypafGEELAAVRGSsvpIGYPVWNTGLRILD-ARMRPVPPG 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1530 KIGELRVKAITIMQGYHKNPETTKQAFDSDGWL------RTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLM 1603
Cdd:PRK10252 801 VAGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQ 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1604 THPAVLQAAVL------GIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCrlrggVKIV----DQLPRTTTGK 1673
Cdd:PRK10252 881 ALPDVEQAVTHacvinqAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHM-----VPVVllqlDQLPLSANGK 955
|
....*.
gi 1820754837 1674 IARKQL 1679
Cdd:PRK10252 956 LDRKAL 961
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
344-546 |
3.47e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 109.14 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 344 VILSYGMTD---------YGGLcarqtkySKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEA 414
Cdd:PRK12492 361 IVEGYGLTEtspvastnpYGEL-------ARLGTVGIPVPGTALKVIDDD-GNELPLGERGELCIKGPQVMKGYWQQPEA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 415 TRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAF-VA 493
Cdd:PRK12492 433 TAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFvVA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 494 KVPGKEVTELDItdLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQIA 546
Cdd:PRK12492 513 RDPGLSVEELKA--YCKENFTGY-KVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
44-542 |
3.70e-24 |
|
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: 108.57 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 44 EKLRSRPEFIAqveAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNEL 122
Cdd:cd17655 5 EQAEKTPDHTA---VVFEDQTlTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 123 SPMTARYFLSLTKPKIVFVNGESAECLAQVVKENNMDtrlvvfaDSAGFVGRAATLTAVLRSQDTAWidefecakltspk 202
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLD-------EDTIYHEESENLEPVSKSDDLAY------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 203 hvaaIVCSSGTSGFPKGTEISHAAMINY---MAHVKVHDLKGHVSMWTPsmrWYCGLFIV-IKAILDCSKRI-IVPDYDD 277
Cdd:cd17655 142 ----VIYTSGSTGKPKGVMIEHRGVVNLvewANKVIYQGEHLRVALFAS---ISFDASVTeIFASLLSGNTLyIVRKETV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 278 DEG--LCRFIEKYEVSwfrCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHT-DVILSYGMTD-- 352
Cdd:cd17655 215 LDGqaLTQYIRQNRIT---IIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTEtt 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 353 -------YGGLCARQTKYS--KPGScgfvceTGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDG 423
Cdd:cd17655 292 vdasiyqYEPETDQQVSVPigKPLG------NTRIYILDQY-GRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 424 WL------HTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVakVPG 497
Cdd:cd17655 365 FVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYI--VSE 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1820754837 498 KEVTELDITDLVKQNMPWYCRLHAGVKfMEKLPRTATGKIAKKQL 542
Cdd:cd17655 443 KELPVAQLREFLARELPDYMIPSYFIK-LDEIPLTPNGKVDRKAL 486
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
377-547 |
3.86e-24 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 109.16 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 377 RLKVVDPNTGKVLGANKT--GEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAI 454
Cdd:PLN02479 383 GLDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 455 KISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKE-----VTELDITDLVKQNMPWYCrLHAGVKFmEKL 529
Cdd:PLN02479 462 NISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDksdeaALAEDIMKFCRERLPAYW-VPKSVVF-GPL 539
|
170
....*....|....*...
gi 1820754837 530 PRTATGKIAKKQLKQIAK 547
Cdd:PLN02479 540 PKTATGKIQKHVLRAKAK 557
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1337-1683 |
5.17e-24 |
|
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: 107.96 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1337 NPDDVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRTlvgHTCIVTPTMRW----HYGVLMAFRLVA--ANAKKLIVP 1410
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST---EWKTKDRILSWmpltHDMGLIAFHLAPliAGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1411 DND---DAENFCQLIEKYQITWFGTDPF---MIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMRE-----KLPDV 1479
Cdd:cd05908 181 TRLfirRPILWLKKASEHKATIVSSPNFgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDhmskyGLKRN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1480 FITNHYGMTDT---ACVVSAQNKFT--------------------------KLGSVGYVSSNVRIKMVDLDTEEaLGPNK 1530
Cdd:cd05908 261 AILPVYGLAEAsvgASLPKAQSPFKtitlgrrhvthgepepevdkkdseclTFVEVGKPIDETDIRICDEDNKI-LPDGY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1531 IGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYdDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVL- 1609
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVEl 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1610 -QAAVLGIPNEVDEQHpKAFVVQVPNKSvtEQELISYVEKnLPDYCRLRGGVKI-----VDQLPRTTTGKIARKQLRDMY 1683
Cdd:cd05908 419 gRVVACGVNNSNTRNE-EIFCFIEHRKS--EDDFYPLGKK-IKKHLNKRGGWQInevlpIRRIPKTTSGKVKRYELAQRY 494
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
348-537 |
5.35e-24 |
|
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: 105.04 E-value: 5.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDYGGLCARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDsDGWLHT 427
Cdd:cd17637 143 YGQTETSGLVTLSPYRERPGSAGRPGPLVRVRIVDDN-DRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHT 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 428 GDLGYYDNDGEVFLVDRMSEfinYRAIK-----ISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTE 502
Cdd:cd17637 221 GDLGRFDEDGYLWYAGRKPE---KELIKpggenVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTA 297
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1820754837 503 LDITDLVKQNM-----PWYcrlhagVKFMEKLPRTATGKI 537
Cdd:cd17637 298 DELIEFVGSRIarykkPRY------VVFVEALPKTADGSI 331
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1202-1681 |
5.39e-24 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 107.52 E-value: 5.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAISntwdheltpmTARNFlTLTSPKIV 1280
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAP----------AFINY-NLSGDPLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1281 FTVSSSAAnlmeaakelkmnlKVVVMDkldgyesveenvmkghdtreiiefkchvtnPDDVALIVPSSGTTGLPKGTEIS 1360
Cdd:cd05937 72 HCLKLSGS-------------RFVIVD------------------------------PDDPAILIYTSGTTGLPKAAAIS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1361 HYSLfcclhpYKNRTLVGHTCIVTPTMRWHY--------GVLMAFRLVAANAKKLIVPDNDDAENFCQLIEKYQITwfgt 1432
Cdd:cd05937 109 WRRT------LVTSNLLSHDLNLKNGDRTYTcmplyhgtAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGAT---- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1433 dpfmIIKFIKSqlLEKYRLPT--------LKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVVSAQNK--FTk 1502
Cdd:cd05937 179 ----IIQYVGE--LCRYLLSTppspydrdHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVgdFG- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1503 LGSVGYVSSNVRIKM--------VDLDTEEALGPNK---------------IGELRVKAITIMQGYHKNPETTKQAF--- 1556
Cdd:cd05937 252 AGAIGHHGLIRRWKFenqvvlvkMDPETDDPIRDPKtgfcvrapvgepgemLGRVPFKNREAFQGYLHNEDATESKLvrd 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1557 ---DSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVP 1633
Cdd:cd05937 332 vfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLE 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1634 NKSV-----TEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:cd05937 412 ESSAvptefTKSLLASLARKNLPSYAVPL-FLRLTEEVATTDNHKQQKGVLRD 463
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1206-1679 |
6.02e-24 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 107.52 E-value: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAisntwdheltpmtARNFLTLTSPKIVFTVss 1285
Cdd:cd17644 27 TYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGG-------------AYVPLDPNYPQERLTY-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 saanLMEAAKelkmnlkVVVMdkldgyesveenvmkghdtreiiefkchVTNPDDVALIVPSSGTTGLPKGTEISHYSLF 1365
Cdd:cd17644 92 ----ILEDAQ-------ISVL----------------------------LTQPENLAYVIYTSGSTGKPKGVMIEHQSLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1366 cclhpykNRTLVGHTCI-VTPTMRWHYGVLMAFRLVA--------ANAKKLIVPDN--DDAENFCQLIEKYQITWFGTDP 1434
Cdd:cd17644 133 -------NLSHGLIKEYgITSSDRVLQFASIAFDVAAeeiyvtllSGATLVLRPEEmrSSLEDFVQYIQQWQLTVLSLPP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1435 FMIIKFIKSQLLEKYRLP-TLKVILSSGAHLRKEHLEVMREKL-PDVFITNHYGMT----DTACVVSAQNKFTKLGSV-- 1506
Cdd:cd17644 206 AYWHLLVLELLLSTIDLPsSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTeatiAATVCRLTQLTERNITSVpi 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1507 GYVSSNVRIKMVDldteEALGPNKI---GELRVKAITIMQGYHKNPETTKQAFDSDGWL--------RTGDLAYYDDNGE 1575
Cdd:cd17644 286 GRPIANTQVYILD----ENLQPVPVgvpGELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlyKTGDLARYLPDGN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1576 IYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCR 1655
Cdd:cd17644 362 IEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMI 441
|
490 500
....*....|....*....|....
gi 1820754837 1656 LRGGVkIVDQLPRTTTGKIARKQL 1679
Cdd:cd17644 442 PSAFV-VLEELPLTPNGKIDRRAL 464
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1338-1673 |
9.47e-24 |
|
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: 105.16 E-value: 9.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1338 PDDVaLIVPSSGTTGLPKGTEISHYSLFCCL--------HPYKNRTLVGHTCIVTPTMRW-------H-YGVLMAFRLVA 1401
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQEDIFRMLmggadfgtGEFTPSEDAHKAAAAAAGTVMfpapplmHgTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1402 ANAKKLIVPDNDDAENFCQLIEKYQIT--WFGTDPFM--IIKFIKSQllEKYRLPTLKVILSSGAHLRKEHLEVMREKLP 1477
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTsmTIVGDAMArpLIDALRDA--GPYDLSSLFAISSGGALLSPEVKQGLLELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1478 DVFITNHYGMTDTACVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAF- 1556
Cdd:cd05924 160 NITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGHIPLGYYGDEAKTAETFp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1557 DSDG--WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAfVVQV-P 1633
Cdd:cd05924 240 EVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVA-VVQLrE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1820754837 1634 NKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGK 1673
Cdd:cd05924 319 GAGVDLEELREHCRTRIARY-KLPKQVVFVDEIERSPAGK 357
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
61-544 |
9.69e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 108.16 E-value: 9.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAI---SNP-------------------- 117
Cdd:PRK05605 55 GATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPlytahelehpfedhgarvai 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 118 -WDNeLSPMTARYFLSLTKPKIVFVNGESAECLAQVVKennmdTRLVVFADSAGfvgRAAtLTA----------VLRSQD 186
Cdd:PRK05605 135 vWDK-VAPTVERLRRTTPLETIVSVNMIAAMPLLQRLA-----LRLPIPALRKA---RAA-LTGpapgtvpwetLVDAAI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 187 TAWIDEFECAKLTsPKHVAAIVCSSGTSGFPKGTEISHAamiNYMAHVkvhdLKGHVsmWTPSM-----RWYC------- 254
Cdd:PRK05605 205 GGDGSDVSHPRPT-PDDVALILYTSGTTGKPKGAQLTHR---NLFANA----AQGKA--WVPGLgdgpeRVLAalpmfha 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 255 -GLFIVIK-AILDCSKRIIVPDYDDDEGLcRFIEKYEVSWFrcdscfPirlvkfGVlskyrlPTL--KILLFGGAH---- 326
Cdd:PRK05605 275 yGLTLCLTlAVSIGGELVLLPAPDIDLIL-DAMKKHPPTWL------P------GV------PPLyeKIAEAAEERgvdl 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 327 ------FKGEL---QQTLVKLLPHTD--VILSYGMTDYG--GLCARQTKYSKPGSCGFVCETGRLKVVDP-NTGKVLGAN 392
Cdd:PRK05605 336 sgvrnaFSGAMalpVSTVELWEKLTGglLVEGYGLTETSpiIVGNPMSDDRRPGYVGVPFPDTEVRIVDPeDPDETMPDG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 393 KTGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVF 472
Cdd:PRK05605 416 EEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVE 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 473 QVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDlvkqnmpwYCRLH-AGVKF------MEKLPRTATGKIAKKQLKQ 544
Cdd:PRK05605 495 DAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRA--------YCREHlTRYKVprrfyhVDELPRDQLGKVRRREVRE 565
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
622-1100 |
1.37e-23 |
|
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: 106.64 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 622 AFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLslmspk 701
Cdd:cd17655 17 VFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYIL------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 702 vvfvnEESAENLMEAAKEenLQVRVMVIGSLpGFVSLANILEEQVSRAEIDGfrctkidNPHDLAMICSSSGTTGMPKGT 781
Cdd:cd17655 91 -----EDSGADILLTQSH--LQPPIAFIGLI-DLLDEDTIYHEESENLEPVS-------KSDDLAYVIYTSGSTGKPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 782 ELSYASLYNSITPVEEVHAKNEI--CAWVPTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEI-ALCEIIQKHGVTWL-GT 857
Cdd:cd17655 156 MIEHRGVVNLVEWANKVIYQGEHlrVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGqALTQYIRQNRITIIdLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 858 DTNFAILyVKMNIFqkyPMPSLRKMVITGAPFTKELHETVAKIMPHT-QILQCYGLTDAG-----GLCVSQAKNSKPGSC 931
Cdd:cd17655 236 PAHLKLL-DAADDS---EGLSLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTvdasiYQYEPETDQQVSVPI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 932 GFVTKGIRIKIADEK-----TGIAlgpkerGEICIKSEFMMKGYHKNPEQTKEAFDSDGWL------HTKDIGYYDENGE 1000
Cdd:cd17655 312 GKPLGNTRIYILDQYgrpqpVGVA------GELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1001 IFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHE-----------TDIELPLAfvqkvvekevteeELHD 1069
Cdd:cd17655 386 IEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEqgqnylcayivSEKELPVA-------------QLRE 452
|
490 500 510
....*....|....*....|....*....|.
gi 1820754837 1070 LVNKNLPWYCKLQAGIKfVNDFPRISTGKID 1100
Cdd:cd17655 453 FLARELPDYMIPSYFIK-LDEIPLTPNGKVD 482
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
62-546 |
1.42e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 107.73 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 62 AET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGaISNPWDNELSPMTARYFLSLTKPKIV- 139
Cdd:PRK07529 56 PETwTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLv 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 140 ----FVNGESAECLAQVVKE-NNMDTRLVVfaDSAGFVGRAATLT----------------AVLRSQDTawiDEFECAKL 198
Cdd:PRK07529 135 tlgpFPGTDIWQKVAEVLAAlPELRTVVEV--DLARYLPGPKRLAvplirrkaharildfdAELARQPG---DRLFSGRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 199 TSPKHVAAIVCSSGTSGFPKGTEISHAAMInYMAHvkvhdLKGHVSMWTPSMRWYCGL-----FIVIKAILDCSKR---I 270
Cdd:PRK07529 210 IGPDDVAAYFHTGGTTGMPKLAQHTHGNEV-ANAW-----LGALLLGLGPGDTVFCGLplfhvNALLVTGLAPLARgahV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 271 IVPD---YDDDEGLCRF---IEKYEVSWFrcdSCFPirlVKFGVLSK-----YRLPTLKILLFGGAHFKGEL-----QQT 334
Cdd:PRK07529 284 VLATpqgYRGPGVIANFwkiVERYRINFL---SGVP---TVYAALLQvpvdgHDISSLRYALCGAAPLPVEVfrrfeAAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 335 LVKLLPhtdvilSYGMTDYGGLCARQTKY--SKPGSCGFVCETGRLKVV--DPNTGKV--LGANKTGEIWAKSSYMMNGY 408
Cdd:PRK07529 358 GVRIVE------GYGLTEATCVSSVNPPDgeRRIGSVGLRLPYQRVRVVilDDAGRYLrdCAVDEVGVLCIAGPNVFSGY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 409 YNnPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFInyraIK----ISPAEIEALIQQHPAVFQVAVVPVPhnin 484
Cdd:PRK07529 432 LE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI----IRgghnIDPAAIEEALLRHPAVALAAAVGRP---- 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 485 EEHA----MAFVAKVPGKEVTELDITDLVKQNMPWYCRLHAGVKFMEKLPRTATGKIAKKQLKQIA 546
Cdd:PRK07529 503 DAHAgelpVAYVQLKPGASATEAELLAFARDHIAERAAVPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
629-1054 |
1.89e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 105.34 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvvsklsaryflslmspkvvfvnee 708
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 sAENLMEAAKeenlqvrvmvigslpgfvslaniLEEQVSRAEidGFRCTKIDNPH--DLAMICSSSGTTGMPK---GTEL 783
Cdd:cd05974 55 -ATTLLTPDD-----------------------LRDRVDRGG--AVYAAVDENTHadDPMLLYFTSGTTSKPKlveHTHR 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 784 SY-----ASLY-----------NSITPVEEVHAKNeiCAWVPtirWHGGlnqcievimsnAKWIIFSDDNIKEIALCEII 847
Cdd:cd05974 109 SYpvghlSTMYwiglkpgdvhwNISSPGWAKHAWS--CFFAP---WNAG-----------ATVFLFNYARFDAKRVLAAL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 848 QKHGVTWLGTDTNFAILYVKMNIfQKYPMPsLRKMVITGAPFTKELHETVAKIMPHTqILQCYGLTDAGGLCV-SQAKNS 926
Cdd:cd05974 173 VRYGVTTLCAPPTVWRMLIQQDL-ASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETTALVGnSPGQPV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 927 KPGSCGFVTKGIRIKIADEKTGialgPKERGEICI-----KSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEI 1001
Cdd:cd05974 250 KAGSMGRPLPGYRVALLDPDGA----PATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYL 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1002 FFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:cd05974 325 TYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFI 377
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
47-545 |
2.11e-23 |
|
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: 107.19 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMT 126
Cdd:cd05968 75 RTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 127 ARYFLSLTKPKIVFV------NGESAECLAQVVKENNMD--TRLVVFADSAGFVGRAATltavlrSQDTAWIDE----FE 194
Cdd:cd05968 155 AATRLQDAEAKALITadgftrRGREVNLKEEADKACAQCptVEKVVVVRHLGNDFTPAK------GRDLSYDEEketaGD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 195 CAKLTSPKHVAAIVCSSGTSGFPKGTEISHAAMINYMAHVKVH--DLK-GHVSMWTPSMRWYCGLFIVIKAILDCSKRII 271
Cdd:cd05968 229 GAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFqfDLKpGDLLTWFTDLGWMMGPWLIFGGLILGATMVL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 272 ---VPDYDDDEGLCRFIEKYEVSWFRCDSCFPIRLVKFGV--LSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDV-I 345
Cdd:cd05968 309 ydgAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDapVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNpI 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 346 LSY-GMTDYGG--LCARQTKYSKPGSCGFVCETGRLKVVDPNTGKVLGanKTGEIWAKSSY--MMNGYYNNPEatrRALD 420
Cdd:cd05968 389 INYsGGTEISGgiLGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP--EVGELVLLAPWpgMTRGFWRDED---RYLE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 421 S------DGWLHtGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAK 494
Cdd:cd05968 464 TywsrfdNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVL 542
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 495 VPG--------KEVTELDITDLVKQNMPwycrlhAGVKFMEKLPRTATGKIAKKQLKQI 545
Cdd:cd05968 543 KPGvtptealaEELMERVADELGKPLSP------ERILFVKDLPKTRNAKVMRRVIRAA 595
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
207-536 |
2.25e-23 |
|
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: 104.00 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 207 IVCSSGTSGFPKGTEISH-------AAMINYMAHVKVHD-LKGHVSMWTPSMRWY--CGLF-----IVIKAILDCSKRII 271
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQedifrmlMGGADFGTGEFTPSeDAHKAAAAAAGTVMFpaPPLMhgtgsWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 272 VPD--YDDDEGLcRFIEKYEV-SWFRCDSCFPIRLVK-FGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILS 347
Cdd:cd05924 88 LPDdrFDPEEVW-RTIEKHKVtSMTIVGDAMARPLIDaLRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLVDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDYGGLCARQTKYSKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRA---LDSDGW 424
Cdd:cd05924 167 FGSSETGFTGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGHIPLGYYGDEAKTAETfpeVDGVRY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 425 LHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELD 504
Cdd:cd05924 247 AVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDLEE 326
|
330 340 350
....*....|....*....|....*....|..
gi 1820754837 505 ITDLVKQNMPWYcRLHAGVKFMEKLPRTATGK 536
Cdd:cd05924 327 LREHCRTRIARY-KLPKQVVFVDEIERSPAGK 357
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
602-1054 |
2.30e-23 |
|
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: 106.05 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 602 VGELVLNRLSSKPDFVGQIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICP 681
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 682 WDHVVSKLSARYFLSL--MSPKVVFVNEESAENLMEAAkeenlqVRVMVIGSLPGFVSLAN---ILEEQVSRAEIDGFrc 756
Cdd:cd05923 83 INPRLKAAELAELIERgeMTAAVIAVDAQVMDAIFQSG------VRVLALSDLVGLGEPESagpLIEDPPREPEQPAF-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 757 tkidnphdlamICSSSGTTGMPKGTELSYASLYNSI----TPVEEVH-AKNEICAWVPTIRWHGGLNQCIEVIMSNAKWI 831
Cdd:cd05923 155 -----------VFYTSGTTGLPKGAVIPQRAAESRVlfmsTQAGLRHgRHNVVLGLMPLYHVIGFFAVLVAALALDGTYV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 832 IFSDDNIKEIAlcEIIQKHGVTWL-GTDTNFAILyVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPhTQILQCY 910
Cdd:cd05923 224 VVEEFDPADAL--KLIEQERVTSLfATPTHLDAL-AAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLP-GEKVNIY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 911 GLTDA-GGLCVSQAKNSKPGSCGFVTKgIRIKIADEKTGIALGPKERGEICIK--SEFMMKGYHKNPEQTKEAFdSDGWL 987
Cdd:cd05923 300 GTTEAmNSLYMRDARTGTEMRPGFFSE-VRIVRIGGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWY 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 988 HTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:cd05923 378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACV 444
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
621-1054 |
2.74e-23 |
|
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: 106.51 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 621 DAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhVVSKLSARYFLSLM-- 698
Cdd:cd17634 78 DTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV---IFGGFAPEAVAGRIid 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 699 -SPKVVFvneeSAENLMEAAKEENLqvRVMVIGSL-PGFVSLANILEEQVSRAEIDGFRCTKID---------------- 760
Cdd:cd17634 155 sSSRLLI----TADGGVRAGRSVPL--KKNVDDALnPNVTSVEHVIVLKRTGSDIDWQEGRDLWwrdliakaspehqpea 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 761 -NPHDLAMICSSSGTTGMPKG---TELSYA-SLYNSITPVEEVHAkNEICAWVPTIRW--------HGGLNQCIEVIMSN 827
Cdd:cd17634 229 mNAEDPLFILYTSGTTGKPKGvlhTTGGYLvYAATTMKYVFDYGP-GDIYWCTADVGWvtghsyllYGPLACGATTLLYE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 828 AKwiifsDDNIKEIALCEIIQKHGVTWLGTDTNF--AILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQ 905
Cdd:cd17634 308 GV-----PNWPTPARMWQVVDKHGVNILYTAPTAirALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEK 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 906 --ILQCYGLTDAGGLCVSQAKNSKPGSCGFVTK---GIRIKIADEKtGIALGPKERGEICIKSEF--MMKGYHKNPEQTK 978
Cdd:cd17634 383 cpVVDTWWQTETGGFMITPLPGAIELKAGSATRpvfGVQPAVVDNE-GHPQPGGTEGNLVITDPWpgQTRTLFGDHERFE 461
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 979 EAFDS--DGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:cd17634 462 QTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYV 539
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
761-1027 |
3.66e-23 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 106.05 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 761 NPHDLAMICSSSGTTGMPKGTELSYASL-------YNSITPVEEvhakNEICAWVPTIRWHGgLNQCIEVIMSNAKWIIF 833
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLlanqracLKFFSPKED----DVMMSFLPPFHAYG-FNSCTLFPLLSGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 834 SDDNIKEIALCEIIQKHGVTWLGTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLT 913
Cdd:PRK06334 256 AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 914 DAGGLCVSQAKNS-KPGSC-GFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKN-PEQTKEAFDSDGWLHTK 990
Cdd:PRK06334 336 ECSPVITINTVNSpKHESCvGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEdFGQGFVELGGETWYVTG 415
|
250 260 270
....*....|....*....|....*....|....*..
gi 1820754837 991 DIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVL 1027
Cdd:PRK06334 416 DLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-1679 |
4.00e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.12 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 38 VGALVLEKLRSRPEFIAQVeaVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNP 117
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVV--FGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 118 WDNELSPMTARYFLsltkpkivfvnGESAecLAQVVKENNMDTRLVVfadsagfvgrAATLTAVLRSQDTAWIDEFECAK 197
Cdd:PRK12316 2083 LDPNYPAERLAYML-----------EDSG--AALLLTQRHLLERLPL----------PAGVARLPLDRDAEWADYPDTAP 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 198 L--TSPKHVAAIVCSSGTSGFPKGTEISHAAMINYMA---------------HVKVHDLKGHVSMWTPSmrwycglfivi 260
Cdd:PRK12316 2140 AvqLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQaageryelspadcelQFMSFSFDGAHEQWFHP----------- 2208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 261 kaiLDCSKRIIVPDYD--DDEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRlPTLKILLFGGAHFKGELQQTLVKL 338
Cdd:PRK12316 2209 ---LLNGARVLIRDDElwDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRP-PAVRVYCFGGEAVPAASLRLAWEA 2284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 339 LPHTDVILSYGMTDYGGLCARQTKYSKPGSCGFVCETGRLkvVDPNTGKVLGAN-------KTGEIWAKSSYMMNGYYNN 411
Cdd:PRK12316 2285 LRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRA--LGNRRAYILDADlnllapgMAGELYLGGEGLARGYLNR 2362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 412 PEATRRALDSDGWLH-------TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVpvphNIN 484
Cdd:PRK12316 2363 PGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVV----AQD 2438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 485 EEHAMAFVAKVPGKEVTELDITDL---VKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQL-----KQIAKSYATNCCRE 556
Cdd:PRK12316 2439 GASGKQLVAYVVPDDAAEDLLAELrawLAARLPAY-MVPAHWVVLERLPLNPNGKLDRKALpkpdvSQLRQAYVAPQEGL 2517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 557 RRIERETFTDIMTSSGEKANEYVpsFRIEENVLIGTGETHPVCANVG-ELVLNRLSSKPDFVGQIDAFTGKECTYAEMRE 635
Cdd:PRK12316 2518 EQRLAAIWQAVLKVEQVGLDDHF--FELGGHSLLATQVVSRVRQDLGlEVPLRILFERPTLAAFAASLESGQTSRAPVLQ 2595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 636 RSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMS--------PKVVFVNE 707
Cdd:PRK12316 2596 KVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRfvevgeqtRQVILPNM 2675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 708 ESAENLMEAAKEENLQVRVMVIGSLPGFVSLANILEEQVSRAEIDGFRCTKIDNPHDLAmicsSSGTTGMPKGTELsyAS 787
Cdd:PRK12316 2676 SLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIV----SDGWSMQVMVDEL--VQ 2749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 788 LYNSITPVEEVHAKNEICAWVPTIRWH--------------------GGLNQCIEVIMSNAKWIIFSD---------DNI 838
Cdd:PRK12316 2750 AYAGARRGEQPTLPPLPLQYADYAAWQrawmdsgegarqldywrerlGGEQPVLELPLDRPRPALQSHrgarldvalDVA 2829
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 839 KEIALCEIIQKHGVTwlgtdTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQC-YGLTDAGG 917
Cdd:PRK12316 2830 LSRELLALARREGVT-----LFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAqVDAQLAFR 2904
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 918 LCVSQAKNSKPGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGwlHTKDIGYYDE 997
Cdd:PRK12316 2905 DLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDG--AATQFDLALD 2982
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 998 NGEIffVNRISDFINYKAIKLSSAEIEGvLELHPSILKAVVVPVPHETDIELPLAFVQKvvekevteeelhdlvnknlpW 1077
Cdd:PRK12316 2983 TWES--AEGLGASLTYATDLFDARTVER-LARHWQNLLRGMVENPQRSVDELAMLDAEE--------------------R 3039
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1078 YCKLQAGIKFVNDFPRistgkidkkklkllaksyanvsiriscqcafgcyknkrdsncykidinmcnleinnkchndsrd 1157
Cdd:PRK12316 3040 GQLLEAWNATAAEYPL---------------------------------------------------------------- 3055
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1158 friEDNILIGKELSIPKRPVNIAeetLKFlkskpdsigqvdalTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSD 1237
Cdd:PRK12316 3056 ---ERGVHRLFEEQVERTPDAVA---LAF--------------GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVE 3115
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1238 NNLDVFLILLGTMYIGAISNTWDHELTpmtarnfltltSPKIVFTVSSSAANLMEAAKELKMNLK--VVVMDKLDGYESV 1315
Cdd:PRK12316 3116 RSLEMVVGLLAILKAGGAYVPLDPEYP-----------EERLAYMLEDSGAQLLLSQSHLRLPLAqgVQVLDLDRGDENY 3184
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1316 EENVMKGHdtreiiefkchvTNPDDVALIVPSSGTTGLPKGTEISHYSL--FCCLHPYKNRTLVGHTCIVTPTMRWHYGV 1393
Cdd:PRK12316 3185 AEANPAIR------------TMPENLAYVIYTSGSTGKPKGVGIRHSALsnHLCWMQQAYGLGVGDRVLQFTTFSFDVFV 3252
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1394 LMAFRLVAANAKKLI--VPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRlpTLKVILSSGAHLRKEHLEV 1471
Cdd:PRK12316 3253 EELFWPLMSGARVVLagPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCT--SLKRIVCGGEALPADLQQQ 3330
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1472 MREKLPdvfITNHYGMTDTACVVSA---QNKFTKLGSVGYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKN 1548
Cdd:PRK12316 3331 VFAGLP---LYNLYGPTEATITVTHwqcVEEGKDAVPIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNR 3406
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1549 PETTKQAFDSDGW------LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLgipnEVDE 1622
Cdd:PRK12316 3407 PGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDG 3482
|
1690 1700 1710 1720 1730
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1623 QHPKAFVVQVPNKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK12316 3483 RQLVAYVVPEDEAGDLREALKAHLKASLPEY-MVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1330-1642 |
4.68e-23 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 105.75 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1330 EFKCHVTNPDDVALIVPSSGTTGLPKGTEISHyslfcclhpyknrtlvGHTCIVTPTMRWHYGV------LMAFRLVAAN 1403
Cdd:PRK09274 165 PFPMADLAPDDMAAILFTSGSTGTPKGVVYTH----------------GMFEAQIEALREDYGIepgeidLPTFPLFALF 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1404 AKKL----IVPDND-------DAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVM 1472
Cdd:PRK09274 229 GPALgmtsVIPDMDptrpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERF 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1473 REKLP-DVFITNHYGMTDT--ACVVSAQNKFTKLGS---------VGYVSSNVRIKMVDLDTE--------EALGPNKIG 1532
Cdd:PRK09274 309 RAMLPpDAEILTPYGATEAlpISSIESREILFATRAatdngagicVGRPVDGVEVRIIAISDApipewddaLRLATGEIG 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1533 ELRVKAITIMQGYHKNPETTKQA--FDSDG--WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAV 1608
Cdd:PRK09274 389 EIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
|
330 340 350
....*....|....*....|....*....|....*....
gi 1820754837 1609 LQAAVLGIPnEVDEQHPkAFVVQV-----PNKSVTEQEL 1642
Cdd:PRK09274 469 KRSALVGVG-VPGAQRP-VLCVELepgvaCSKSALYQEL 505
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1347-1683 |
5.54e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 105.17 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1347 SSGTTGLPKGTEISHYSlfCCLHPYKNrTLVGHTCI--------VTPTmrWH---YGVLMAFRLVAAnakKLIVPDND-D 1414
Cdd:PRK07008 184 TSGTTGNPKGALYSHRS--TVLHAYGA-ALPDAMGLsardavlpVVPM--FHvnaWGLPYSAPLTGA---KLVLPGPDlD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1415 AENFCQLIEKYQITWFGTDP---FMIIKFIKSqllEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTD-- 1489
Cdd:PRK07008 256 GKSLYELIEAERVTFSAGVPtvwLGLLNHMRE---AGLRFSTLRRTVIGGSACPPAMIRTFEDEY-GVEVIHAWGMTEms 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1490 ---TACVVS---------AQNKF-TKLGSVGYvssNVRIKMVDLDTEEALGPNK-IGELRVKAITIMQGYHKNPETTKqa 1555
Cdd:PRK07008 332 plgTLCKLKwkhsqlpldEQRKLlEKQGRVIY---GVDMKIVGDDGRELPWDGKaFGDLQVRGPWVIDRYFRGDASPL-- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1556 fdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNK 1635
Cdd:PRK07008 407 --VDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1636 SVTEQELISYVEKN-----LPDycrlrgGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK07008 485 EVTREELLAFYEGKvakwwIPD------DVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
39-542 |
5.76e-23 |
|
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: 104.66 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 39 GALVLEKLRSRPEFIAQVEavTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPW 118
Cdd:cd17646 1 HALVAEQAARTPDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 119 DNELSPMTARYFLSLTKPKIVFVNGESAECLAQVVkennmdtrLVVFADSAGFVGRAATLTAVlrsqdtawidefecakL 198
Cdd:cd17646 79 DPGYPADRLAYMLADAGPAVVLTTADLAARLPAGG--------DVALLGDEALAAPPATPPLV----------------P 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 199 TSPKHVAAIVCSSGTSGFPKGTEISHAAMINYMAHVKVHDLKGH-------------VSMWTpsmrwycgLFivikAILD 265
Cdd:cd17646 135 PRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPgdrvlqktplsfdVSVWE--------LF----WPLV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 266 CSKRIIVPDYD---DDEGLCRFIEKYEVSwfrcdSCF--PIRLVKF-GVLSKYRLPTLKILLFGGAHFKGELQQTLVKlL 339
Cdd:cd17646 203 AGARLVVARPGghrDPAYLAALIREHGVT-----TCHfvPSMLRVFlAEPAAGSCASLRRVFCSGEALPPELAARFLA-L 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 340 PHTDVILSYGMT----DYGGLCARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPE-- 413
Cdd:cd17646 277 PGAELHNLYGPTeaaiDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQLARGYLGRPAlt 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 414 ATRRALDSDG----WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAM 489
Cdd:cd17646 356 AERFVPDPFGpgsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLV 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 490 AFVAKVPGKEVTELD-ITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:cd17646 436 GYVVPAAGAAGPDTAaLRAHLAERLPEY-MVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1313-1679 |
6.84e-23 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 104.59 E-value: 6.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1313 ESVEENVMKGhdtrEIIEFKCHVTNpDDVALIVPSSGTTGLPKGTEISHYSL--F----CCLHPYKNrtlvGHTCIVTPT 1386
Cdd:PRK04813 122 DELKDIFATG----NPYDFDHAVKG-DDNYYIIFTSGTTGKPKGVQISHDNLvsFtnwmLEDFALPE----GPQFLNQAP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1387 MRWHYGVlMAFRLVAANAKKLIVPDNDDAENFCQL---IEKYQI-TWFGTDPFMIIKFIKSQLLEKyRLPTLKVILSSGA 1462
Cdd:PRK04813 193 YSFDLSV-MDLYPTLASGGTLVALPKDMTANFKQLfetLPQLPInVWVSTPSFADMCLLDPSFNEE-HLPNLTHFLFCGE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1463 HLRKEHLEVMREKLPDVFITNHYGMTDTACVVSA-------QNKFTKLgSVGYVSSNVRIKMVDLDTEEALGPNKiGELR 1535
Cdd:PRK04813 271 ELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSieitdemLDQYKRL-PIGYAKPDSPLLIIDEEGTKLPDGEQ-GEIV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1536 VKAITIMQGYHKNPETTKQAF-DSDGW--LRTGDLAYYDDnGEIYIVDRIsDF-INFRSINVSPAEIETVLMTHPAVLQA 1611
Cdd:PRK04813 349 ISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLED-GLLFYQGRI-DFqIKLNGYRIELEEIEQNLRQSSYVESA 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 1612 AVlgIPNEVDE--QHPKAFVVQVPNKSVTEQELISYV----EKNLPDYCRLRggvKIV--DQLPRTTTGKIARKQL 1679
Cdd:PRK04813 427 VV--VPYNKDHkvQYLIAYVVPKEEDFEREFELTKAIkkelKERLMEYMIPR---KFIyrDSLPLTPNGKIDRKAL 497
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1206-1673 |
7.45e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 104.97 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFTVSS 1285
Cdd:PRK07798 30 TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYERE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAAKELKmNLKVVVM-------DKLDGYESVEENVMKGHDTREIIEfkchvTNPDDVALIVpSSGTTGLPKGTE 1358
Cdd:PRK07798 110 FAPRVAEVLPRLP-KLRTLVVvedgsgnDLLPGAVDYEDALAAGSPERDFGE-----RSPDDLYLLY-TGGTTGMPKGVM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1359 ISHYSLFcclhpyknRTLVGHTCIVT-----------------PTMRW-------H----YGVLMAFrlvaANAKKLIVP 1410
Cdd:PRK07798 183 WRQEDIF--------RVLLGGRDFATgepiedeeelakraaagPGMRRfpapplmHgagqWAAFAAL----FSGQTVVLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1411 DND--DAENFCQLIEKYQ---ITWFGtDPF---MIIKFIKSqllEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFIT 1482
Cdd:PRK07798 251 PDVrfDADEVWRTIEREKvnvITIVG-DAMarpLLDALEAR---GPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1483 NHYG----------MTDTACVVSAQNKFTklgsvgyvsSNVRIKMVDLDTEEAL-GPNKIGELrvkAIT--IMQGYHKNP 1549
Cdd:PRK07798 327 DSIGssetgfggsgTVAKGAVHTGGPRFT---------IGPRTVVLDEDGNPVEpGSGEIGWI---ARRghIPLGYYKDP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1550 ETTKQAFDS-DG--WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPK 1626
Cdd:PRK07798 395 EKTAETFPTiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVV 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1820754837 1627 AFVVQVPNKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGK 1673
Cdd:PRK07798 475 AVVQLREGARPDLAELRAHCRSSLAGY-KVPRAIWFVDEVQRSPAGK 520
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
597-1045 |
9.87e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 104.58 E-value: 9.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 597 PVCANVGELVLNRLSSKPDFVGQIDAFTgkeCTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIG 676
Cdd:PRK05852 16 PRIADLVEVAATRLPEAPALVVTADRIA---ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 677 GIICPWDHVVSKLSARYFLSLMSPKVVFVNEES-AENLMEAAKEENLQVRV-MVIGSLPGFVS--LANILEEQVSRAEID 752
Cdd:PRK05852 93 LVVVPLDPALPIAEQRVRSQAAGARVVLIDADGpHDRAEPTTRWWPLTVNVgGDSGPSGGTLSvhLDAATEPTPATSTPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 753 GFRctkidnpHDLAMICSSSGTTGMPK---GTELSYASLYNSITPVEEVHAKNEICAWVPTIRWHGGLNQCIEVIMSNAK 829
Cdd:PRK05852 173 GLR-------PDDAMIMFTGGTTGLPKmvpWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 830 WIIFSDDNIKEIALCEIIQKHGVTWL-GTDTNFAILY--VKMNIFQKYPmPSLRKMVITGAPFTKE----LHETVAKIMp 902
Cdd:PRK05852 246 VLLPARGRFSAHTFWDDIKAVGATWYtAVPTIHQILLerAATEPSGRKP-AALRFIRSCSAPLTAEtaqaLQTEFAAPV- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 903 htqiLQCYGLTDAGGLCVSQA-----KNSKPG-SCGFVTK--GIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNP 974
Cdd:PRK05852 324 ----VCAFGMTEATHQVTTTQiegigQTENPVvSTGLVGRstGAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDP 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 975 EQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHET 1045
Cdd:PRK05852 399 TITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
41-544 |
1.00e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 104.58 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 41 LVLEKLRSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDN 120
Cdd:PRK05852 21 LVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 121 ELSPMTARYFLSLTKPKIVFVNGE--------SAECLAQVVK----ENNMDTRLVVFADSAGFVGRAATLTAVLRSQDta 188
Cdd:PRK05852 101 ALPIAEQRVRSQAAGARVVLIDADgphdraepTTRWWPLTVNvggdSGPSGGTLSVHLDAATEPTPATSTPEGLRPDD-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 189 widefecakltspkhvAAIVCSSGTSGFPKGTEISH---AAMINYM----------AHVKVHDL-KGHvsmwtpsmrwyc 254
Cdd:PRK05852 179 ----------------AMIMFTGGTTGLPKMVPWTHaniASSVRAIitgyrlsprdATVAVMPLyHGH------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 255 GLFIVIKAILDCSKRIIVPD---------YDDdeglcrfIEKYEVSWFRC-DSCFPIRLVKFGVLSKYRL-PTLKILLFG 323
Cdd:PRK05852 231 GLIAALLATLASGGAVLLPArgrfsahtfWDD-------IKAVGATWYTAvPTIHQILLERAATEPSGRKpAALRFIRSC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 324 GAHFKGELQQTLVK--LLPhtdVILSYGMTDYGGLCA-RQTKYS----KPG-SCGFVCETG--RLKVVDPNtGKVLGANK 393
Cdd:PRK05852 304 SAPLTAETAQALQTefAAP---VVCAFGMTEATHQVTtTQIEGIgqteNPVvSTGLVGRSTgaQIRIVGSD-GLPLPAGA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 394 TGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQ 473
Cdd:PRK05852 380 VGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVME 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 474 VAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK05852 459 AAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAF-EIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
64-549 |
1.07e-22 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 104.45 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 64 TTFAEMTEKSVKCALWLREQGVQPGDIIGICTHN---HLESYvplLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVF 140
Cdd:PRK06018 40 TTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNtwrHLEAW---YGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 141 VNGESAECLAQVVKENNMDTRLVVFADSAgfVGRAATLTAVLRSQDtaWIDEF--ECAKLTSPKHVAAIVC-SSGTSGFP 217
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTDAA--HMPQTTLKNAVAYEE--WIAEAdgDFAWKTFDENTAAGMCyTSGTTGDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 218 KGTEISHAAMINYMAHVKVHDLKG--------------HVSMW-----TPSMrwycglfivikaildcSKRIIVPDYD-D 277
Cdd:PRK06018 193 KGVLYSHRSNVLHALMANNGDALGtsaadtmlpvvplfHANSWgiafsAPSM----------------GTKLVMPGAKlD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 278 DEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLlpHTDVILSYGMTDY---G 354
Cdd:PRK06018 257 GASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM--GVEVRHAWGMTEMsplG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 355 GLCARQTKYSK-PGSC--------GFVCETGRLKVVD------PNTGKVLGANKT-GEIWAKSSYMMNGyynnpeatrRA 418
Cdd:PRK06018 335 TLAALKPPFSKlPGDArldvlqkqGYPPFGVEMKITDdagkelPWDGKTFGRLKVrGPAVAAAYYRVDG---------EI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 419 LDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGK 498
Cdd:PRK06018 406 LDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGE 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 499 EVTELDITD-----LVKQNMPwycrlhAGVKFMEKLPRTATGKIAKKQLKQIAKSY 549
Cdd:PRK06018 486 TATREEILKymdgkIAKWWMP------DDVAFVDAIPHTATGKILKTALREQFKDY 535
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
348-535 |
1.11e-22 |
|
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: 101.22 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDYGGLcARQTKYSKPGSCGFvcetGR------LKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPE--ATRRAl 419
Cdd:cd17636 143 YGQTEVMGL-ATFAALGGGAIGGA----GRpsplvqVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEvnARRTR- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 420 dsDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKE 499
Cdd:cd17636 216 --GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS 293
|
170 180 190
....*....|....*....|....*....|....*.
gi 1820754837 500 VTELDITDLVKQNMPWYCRLHAgVKFMEKLPRTATG 535
Cdd:cd17636 294 VTEAELIEHCRARIASYKKPKS-VEFADALPRTAGG 328
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
613-1099 |
1.36e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 103.73 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 613 KPDFVGQIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICP--WDHVVSKLS 690
Cdd:PRK09088 8 QPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPlnWRLSASELD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 691 AryFLSLMSPKVVFvneesAENLMEAAKEENLqvrvmvigSLPGFVSLANILEEqVSRAEIDgfrctkidnPHDLAMICS 770
Cdd:PRK09088 88 A--LLQDAEPRLLL-----GDDAVAAGRTDVE--------DLAAFIASADALEP-ADTPSIP---------PERVSLILF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 771 SSGTTGMPKGTELSYASLYNS---ITPVEEVHAKNEICAWVPTirWHG-GLNQCIEVIMSNAKWIIFSDDnikeialceI 846
Cdd:PRK09088 143 TSGTSGQPKGVMLSERNLQQTahnFGVLGRVDAHSSFLCDAPM--FHIiGLITSVRPVLAVGGSILVSNG---------F 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 847 IQKHGVTWLGtDTNFAIL-YV----KMNIFQKYP------MPSLRKMVITGAPFTKE-LHETVAKIMPhtqILQCYGLTD 914
Cdd:PRK09088 212 EPKRTLGRLG-DPALGIThYFcvpqMAQAFRAQPgfdaaaLRHLTALFTGGAPHAAEdILGWLDDGIP---MVDGFGMSE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 915 AG---GLCVSQAK-NSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTK 990
Cdd:PRK09088 288 AGtvfGMSVDCDViRAKAGAAGIPTPTVQTRVVDDQ-GNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 991 DIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDL 1070
Cdd:PRK09088 367 DIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSH 446
|
490 500
....*....|....*....|....*....
gi 1820754837 1071 VNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK09088 447 LSTRLAKY-KVPKHLRLVDALPRTASGKL 474
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
602-1100 |
1.76e-22 |
|
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: 103.01 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 602 VGELVLNRLSSKPDFVGqIDAFTGkECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICP 681
Cdd:cd05918 1 VHDLIEERARSQPDAPA-VCAWDG-SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 682 WD--HVVSKLsaRYFLSLMSPKVVFVneesaenlmeaakeenlqvrvmvigslpgfvslanileeqvsraeidgfrctki 759
Cdd:cd05918 79 LDpsHPLQRL--QEILQDTGAKVVLT------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 760 DNPHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEVHAKNeicawvPTIRW--------------------HGGlnq 819
Cdd:cd05918 103 SSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT------SESRVlqfasytfdvsileifttlaAGG--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 820 CIevimsnakwIIFSDDNIKEiALCEIIQKHGVTWLG-TDTNFAILyvkmnifQKYPMPSLRKMVITGAPFTKELhetVA 898
Cdd:cd05918 174 CL---------CIPSEEDRLN-DLAGFINRLRVTWAFlTPSVARLL-------DPEDVPSLRTLVLGGEALTQSD---VD 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 899 KIMPHTQILQCYGLTDAGGLCVSQA--KNSKPGSCGFVTkGIRIKIADEKTGIALGPK-ERGEICIKSEFMMKGYHKNPE 975
Cdd:cd05918 234 TWADRVRLINAYGPAECTIAATVSPvvPSTDPRNIGRPL-GATCWVVDPDNHDRLVPIgAVGELLIEGPILARGYLNDPE 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 976 QTKEAF-DSDGWLH------------TKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELH-PSILKAVVVPV 1041
Cdd:cd05918 313 KTAAAFiEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVV 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1042 PHETDIELPL--AFVQKVVEKEVTEEELHDLVNKNLPWY---CKLQAGIK-------------FVNDFPRISTGKID 1100
Cdd:cd05918 393 KPKDGSSSPQlvAFVVLDGSSSGSGDGDSLFLEPSDEFRalvAELRSKLRqrlpsymvpsvflPLSHLPLTASGKID 469
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
622-1054 |
2.01e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 103.75 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 622 AFT--GKECTYAEMRERSIKCALWLRKH-GIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARY----- 693
Cdd:PRK12492 42 AFSnlGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHqfkds 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 694 ------FLSLMSPKVVFVNEESA-ENLMEAAKEENL-------------QVRVMVIG-SLPGFVSLANILEE------QV 746
Cdd:PRK12492 122 garalvYLNMFGKLVQEVLPDTGiEYLIEAKMGDLLpaakgwlvntvvdKVKKMVPAyHLPQAVPFKQALRQgrglslKP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 747 SRAEIDgfrctkidnphDLAMICSSSGTTGMPKGTELSYASLynsITPVEEVHA----------------KNEICAWVPT 810
Cdd:PRK12492 202 VPVGLD-----------DIAVLQYTGGTTGLAKGAMLTHGNL---VANMLQVRAclsqlgpdgqplmkegQEVMIAPLPL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 811 IRWHGGLNQCIEVIMSNAKWIIFSddNIKEIA--LCEIIQKHGVTWLGTDTNFAILyvkMNI--FQKYPMPSLRKMVITG 886
Cdd:PRK12492 268 YHIYAFTANCMCMMVSGNHNVLIT--NPRDIPgfIKELGKWRFSALLGLNTLFVAL---MDHpgFKDLDFSALKLTNSGG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 887 APFTKELHETVAKIMPHTqILQCYGLTDAGGLCVSQ--AKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSE 964
Cdd:PRK12492 343 TALVKATAERWEQLTGCT-IVEGYGLTETSPVASTNpyGELARLGTVGIPVPGTALKVIDDD-GNELPLGERGELCIKGP 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 965 FMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHE 1044
Cdd:PRK12492 421 QVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDE 500
|
490
....*....|
gi 1820754837 1045 TDIELPLAFV 1054
Cdd:PRK12492 501 RSGEAVKLFV 510
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1191-1679 |
2.13e-22 |
|
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: 102.33 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1191 PDSIGQVDAltGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdheltpmtarn 1270
Cdd:cd17652 1 PDAPAVVFG--DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAA--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1271 FLTLT----SPKIVFTVSSSAANLMeaakelkmnlkvvvmdkldgyesveenvmkghdtreiiefkchVTNPDDVALIVP 1346
Cdd:cd17652 64 YLPLDpaypAERIAYMLADARPALL-------------------------------------------LTTPDNLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1347 SSGTTGLPKGTEISHYSLFCCLhpyknRTLVGHtCIVTPTMRW-----------HYGVLMAF----RLVAANAKKLIVPd 1411
Cdd:cd17652 101 TSGSTGRPKGVVVTHRGLANLA-----AAQIAA-FDVGPGSRVlqfaspsfdasVWELLMALlagaTLVLAPAEELLPG- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1412 nddaENFCQLIEKYQITwfgtdpFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRkehLEVMREKLPDVFITNHYGMTDTA 1491
Cdd:cd17652 174 ----EPLADLLREHRIT------HVTLPPAALAALPPDDLPDLRTLVVAGEACP---AELVDRWAPGRRMINAYGPTETT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1492 CVVSAQNKFTKLGSV--GYVSSNVRIKMVDlDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGW-------L 1562
Cdd:cd17652 241 VCATMAGPLPGGGVPpiGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmY 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1563 RTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLgipneVDEQHPK-----AFVVQVPNKSV 1637
Cdd:cd17652 320 RTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV-----VRDDRPGdkrlvAYVVPAPGAAP 394
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1820754837 1638 TEQELISYVEKNLPDYCrLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:cd17652 395 TAAELRAHLAERLPGYM-VPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-546 |
2.17e-22 |
|
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: 102.26 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLtkpkivfvnGE 144
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDR---------GG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAECLAQVVKENNmDTRLVVFadsagfvgraatltavlrsqdtawidefecakltspkhvaaivcSSGTSGFPKGTEISH 224
Cdd:cd05974 73 AVYAAVDENTHAD-DPMLLYF--------------------------------------------TSGTTSKPKLVEHTH 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AAM-INYMAHVKVHDLK-GHVSMWTPSMRWYCGLFIVIKAILDCSKRIIVPDYD--DDEGLCRFIEKYEVSWFrcdsCFP 300
Cdd:cd05974 108 RSYpVGHLSTMYWIGLKpGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYArfDAKRVLAALVRYGVTTL----CAP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 301 ---IRLVKFGVLSKYRLPtLKILLFGGAHFKGELQQTLVKLLPHTdVILSYGMTDYGGLCARQT-KYSKPGSCGFVCETG 376
Cdd:cd05974 184 ptvWRMLIQQDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETTALVGNSPgQPVKAGSMGRPLPGY 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 377 RLKVVDPNTGKVlganKTGEIW-----AKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINY 451
Cdd:cd05974 262 RVALLDPDGAPA----TEGEVAldlgdTRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 452 RAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKE---VTELDITDLVKQNMPWYCRLHAgVKFMEk 528
Cdd:cd05974 337 SDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEpspETALEIFRFSRERLAPYKRIRR-LEFAE- 414
|
490
....*....|....*...
gi 1820754837 529 LPRTATGKIAKKQLKQIA 546
Cdd:cd05974 415 LPKTISGKIRRVELRRRE 432
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
629-1054 |
2.39e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 103.44 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWdhvvskLSA------RYFLSLMSPKV 702
Cdd:PRK04319 75 TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPL------FEAfmeeavRDRLEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNEESAENLMeAAKEENLQvRVMVIG----SLPGFVSLANILEeQVSraeiDGFRCTKIDnPHDLAMICSSSGTTGMP 778
Cdd:PRK04319 149 LITTPALLERKP-ADDLPSLK-HVLLVGedveEGPGTLDFNALME-QAS----DEFDIEWTD-REDGAILHYTSGSTGKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 779 KGT-ELSYASLYNSITP--VEEVHAkNEI--C----AWV---------PtirWHGGLNQCI-EVIMSNAKWIifsddnik 839
Cdd:PRK04319 221 KGVlHVHNAMLQHYQTGkyVLDLHE-DDVywCtadpGWVtgtsygifaP---WLNGATNVIdGGRFSPERWY-------- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 840 eialcEIIQKHGVT-WLGTDTNFAILyvkM----NIFQKYPMPSLRKMVITGAP------------FTKELHETvakimp 902
Cdd:PRK04319 289 -----RILEDYKVTvWYTAPTAIRML---MgagdDLVKKYDLSSLRHILSVGEPlnpevvrwgmkvFGLPIHDN------ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 903 htqilqcYGLTDAGG--LCVSQAKNSKPGSCGFVTKGIRIKIADeKTGIALGPKERGEICIKSEF--MMKGYHKNPEQTK 978
Cdd:PRK04319 355 -------WWMTETGGimIANYPAMDIKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKGWpsMMRGIWNNPEKYE 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 979 EAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:PRK04319 427 SYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFV 501
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
629-1054 |
2.39e-22 |
|
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: 103.52 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICP---------WDHVVSKLsaRYFLSLMS 699
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPltvpptydePNARLRKL--RHIWQLLG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 700 PKVVFVNEESAENLMEAAKEENLQVRvmvigslpgfvSLANILEEQVSRAEIDGFRCTkidnPHDLAMICSSSGTTGMPK 779
Cdd:cd05906 119 SPVVLTDAELVAEFAGLETLSGLPGI-----------RVLSIEELLDTAADHDLPQSR----PDDLALLMLTSGSTGFPK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 780 GTELSYASLYNSITPVEEVH---AKNEICAWVPTIrwH-GGLNQC---------------IEVIMSN-AKWIifsddnik 839
Cdd:cd05906 184 AVPLTHRNILARSAGKIQHNgltPQDVFLNWVPLD--HvGGLVELhlravylgcqqvhvpTEEILADpLRWL-------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 840 eialcEIIQKHGV--TWLgtdTNFAilYVKMNIF------QKYPMPSLRKMV--------ITGAPFTKELHETVAkimPH 903
Cdd:cd05906 254 -----DLIDRYRVtiTWA---PNFA--FALLNDLleeiedGTWDLSSLRYLVnageavvaKTIRRLLRLLEPYGL---PP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 904 TQILQCYGLTDAGGLCVSQAKNSKPG--------SCGFVTKGIRIKIADEkTGIALGPKERGEICIKSEFMMKGYHKNPE 975
Cdd:cd05906 321 DAIRPAFGMTETCSGVIYSRSFPTYDhsqalefvSLGRPIPGVSMRIVDD-EGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 976 QTKEAFDSDGWLHTKDIGYYDeNGEIFFVNRISDFINYKAIKLSSAEIEGVLE----LHPSILKAVVV-PVPHETDiELP 1050
Cdd:cd05906 400 ANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEevpgVEPSFTAAFAVrDPGAETE-ELA 477
|
....
gi 1820754837 1051 LAFV 1054
Cdd:cd05906 478 IFFV 481
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
52-543 |
3.12e-22 |
|
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: 104.94 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 52 FIAQVE------AVTGAET--TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGA------ISNP 117
Cdd:COG1020 482 FEAQAArtpdavAVVFGDQslTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAayvpldPAYP 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 118 wdnelspmTAR--YFLSLTKPKIVFVNGESAECLAQvvkennmDTRLVVFADSAGFVGRAATLTAVLRSqdtawidefec 195
Cdd:COG1020 562 --------AERlaYMLEDAGARLVLTQSALAARLPE-------LGVPVLALDALALAAEPATNPPVPVT----------- 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 196 akltsPKHVAAIVCSSGTSGFPKGTEISHAAMINYM-AHVKVHDLKGH------------VSMWTPSMRWYCGlfivika 262
Cdd:COG1020 616 -----PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLaWMQRRYGLGPGdrvlqfaslsfdASVWEIFGALLSG------- 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 263 ildcsKRIIVPDYD---DDEGLCRFIEKYEV-------SWFR--CDSCFPirlvkfgvlskyRLPTLKILLFGGAHFKGE 330
Cdd:COG1020 684 -----ATLVLAPPEarrDPAALAELLARHRVtvlnltpSLLRalLDAAPE------------ALPSLRLVLVGGEALPPE 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 331 LQQTLVKLLPHTDVILSYGMT----DygglcarqtkyskpgSCGFVCETG----------------RLKVVDPNtGKVLG 390
Cdd:COG1020 747 LVRRWRARLPGARLVNLYGPTettvD---------------STYYEVTPPdadggsvpigrpiantRVYVLDAH-LQPVP 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 391 ANKTGEIW------AKssymmnGYYNNPEATRRA-----LDSDG--WLHTGDLGYYDNDGEVflvdrmsEFINyRA---I 454
Cdd:COG1020 811 VGVPGELYiggaglAR------GYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL-------EFLG-RAddqV 876
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 455 KIS-----PAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKL 529
Cdd:COG1020 877 KIRgfrieLGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPY-MVPAAVVLLLPL 955
|
570
....*....|....
gi 1820754837 530 PRTATGKIAKKQLK 543
Cdd:COG1020 956 PLTGNGKLDRLALP 969
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
368-538 |
3.64e-22 |
|
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: 102.70 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 368 SCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRR------ALDSDGWLHTGDLGYYdNDGEVFL 441
Cdd:cd05931 356 SCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGFL-HDGELYI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 442 VDRMSEFINYRAIKISPAEIEALIQQHPAVFQ---VAVVPVPHNINEEhaMAFVAKVpGKEVTELDITDLVKQNMPWYCR 518
Cdd:cd05931 435 TGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEER--LVVVAEV-ERGADPADLAAIAAAIRAAVAR 511
|
170 180
....*....|....*....|....*.
gi 1820754837 519 LH----AGVKFME--KLPRTATGKIA 538
Cdd:cd05931 512 EHgvapADVVLVRpgSIPRTSSGKIQ 537
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
384-547 |
4.07e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 102.65 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 384 NTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEA 463
Cdd:PRK08751 398 DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIED 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 464 LIQQHPAVFQVAVVPVPHNINEEHAMAFVAKvPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK08751 478 VIAMMPGVLEVAAVGVPDEKSGEIVKVVIVK-KDPALTAEDVKAHARANLTGY-KQPRIIEFRKELPKTNVGKILRRELR 555
|
....
gi 1820754837 544 QIAK 547
Cdd:PRK08751 556 DAAK 559
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1337-1654 |
6.03e-22 |
|
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: 101.91 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1337 NPDDVALIVPSSGTTGLPKGTEISHYSLFCCL---------HPYKNRTLVG------------------HTCIV---TP- 1385
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIaglgdrvpeLLGPDDRYLAylplahifelaaenvclyRGGTIgygSPr 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1386 -----TMRWHYGVLMAFR---LVAANA-----KKLI---VPDNDdaenfcqLIEKyQITWFG--TDPFMIIKFIKSQLLE 1447
Cdd:cd17639 166 tltdkSKRGCKGDLTEFKptlMVGVPAiwdtiRKGVlakLNPMG-------GLKR-TLFWTAyqSKLKALKEGPGTPLLD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1448 -----KYRLPT---LKVILSSGAHLRKEHLEVMREKLPDVFITnhYGMTDTACVVSAQNKF-TKLGSVGYVSSNVRIKMV 1518
Cdd:cd17639 238 elvfkKVRAALggrLRYMLSGGAPLSADTQEFLNIVLCPVIQG--YGLTETCAGGTVQDPGdLETGRVGPPLPCCEIKLV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1519 DldTEEA----LGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFInfRSIN-- 1592
Cdd:cd17639 316 D--WEEGgystDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLV--KLQNge 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 1593 -VSPAEIETVLMTHPAVLQAAVLgipneVDEQHPKAFVVQVPNKSVTEQELISY--VEKNLPDYC 1654
Cdd:cd17639 392 yIALEKLESIYRSNPLVNNICVY-----ADPDKSYPVAIVVPNEKHLTKLAEKHgvINSEWEELC 451
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
60-543 |
6.06e-22 |
|
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: 101.98 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 60 TGAET--TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPwdnelspmtaryflsLTKPK 137
Cdd:cd05906 34 DGSEEfqSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAP---------------LTVPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 138 IvfvngeSAECLAQVVKENNMDTRL---VVFADSAGF--VGRAATLTAVLRSQDTAWIDEFECAKLT-----SPKHVAAI 207
Cdd:cd05906 99 T------YDEPNARLRKLRHIWQLLgspVVLTDAELVaeFAGLETLSGLPGIRVLSIEELLDTAADHdlpqsRPDDLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 208 VCSSGTSGFPKGTEISHAAMINYMAHVKVHDLKGHVsmwTPSMRW----------YCGLFIVIkaiLDCSKRIIVPDY-- 275
Cdd:cd05906 173 MLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ---DVFLNWvpldhvgglvELHLRAVY---LGCQQVHVPTEEil 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 276 DDDEGLCRFIEKYEVS--W---FRCDSCfpIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLL-PH---TDVIL 346
Cdd:cd05906 247 ADPLRWLDLIDRYRVTitWapnFAFALL--NDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLePYglpPDAIR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 347 -SYGMTDYGGLC---ARQTKYSKPGSCGFVCeTGR------LKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATR 416
Cdd:cd05906 325 pAFGMTETCSGViysRSFPTYDHSQALEFVS-LGRpipgvsMRIVDDE-GQLLPEGEVGRLQVRGPVVTKGYYNNPEANA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 417 RALDSDGWLHTGDLGYYDNdGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAV---FqVAVVPV--PHNINEEHAMAF 491
Cdd:cd05906 403 EAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsF-TAAFAVrdPGAETEELAIFF 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 492 V--AKVPGKEVTELD-ITDLVKQNMpwycrlhaGVKF-------MEKLPRTATGKIAKKQLK 543
Cdd:cd05906 481 VpeYDLQDALSETLRaIRSVVSREV--------GVSPayliplpKEEIPKTSLGKIQRSKLK 534
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1336-1679 |
8.17e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.88 E-value: 8.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1336 TNPDDVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRTLVGHTCIVTPTMRWHY-GVLMAFRLVAANAKKLIVPDND- 1413
Cdd:PRK12316 4691 LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFdGSHEGLYHPLINGASVVIRDDSl 4770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1414 -DAENFCQLIEKYQITWFGTDPFMIikfikSQLLEKYR----LPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMT 1488
Cdd:PRK12316 4771 wDPERLYAEIHEHRVTVLVFPPVYL-----QQLAEHAErdgePPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPT 4845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1489 DTACVVSAQN--KFTKLGS----VGYVSSNVRIKMvdLDTEEALGP-NKIGELRVKAITIMQGYHKNPETTKQAFDSDGW 1561
Cdd:PRK12316 4846 ETTVTVLLWKarDGDACGAaympIGTPLGNRSGYV--LDGQLNPLPvGVAGELYLGGEGVARGYLERPALTAERFVPDPF 4923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1562 -------LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVP- 1633
Cdd:PRK12316 4924 gapggrlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPa 5003
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1634 ------NKSVTEQELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK12316 5004 ladadeAQAELRDELKAALRERLPEY-MVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
629-1099 |
9.45e-22 |
|
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: 100.29 E-value: 9.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvvsklsaryFLSLMSPKVVfvnee 708
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQP------------LFTAFGPKAI----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 saenlmeaakeenlQVRVMVIGSLPGFVSLANileeqvsRAEIDgfrctkidnpHDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd05973 65 --------------EHRLRTSGARLVVTDAAN-------RHKLD----------SDPFVMMFTSGTTGLPKGVPVPLRAL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 YNSITPVEE-VHAKNEICAW----------------------VPTIRWHGGlnqcievimsnakwiiFSDDNIkeialCE 845
Cdd:cd05973 114 AAFGAYLRDaVDLRPEDSFWnaadpgwayglyyaitgplalgHPTILLEGG----------------FSVEST-----WR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 846 IIQKHGVTWL-GTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYGLTDAGGLCVSQAK 924
Cdd:cd05973 173 VIERLGVTNLaGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 925 NSKP---GSCGFVTKGIRIKIADEkTGIALGPKERGEICI---KSEFMMKGYHKNPEQTkeAFDSdGWLHTKDIGYYDEN 998
Cdd:cd05973 252 LEHPvhaGSAGRAMPGWRVAVLDD-DGDELGPGEPGRLAIdiaNSPLMWFRGYQLPDTP--AIDG-GYYLTGDTVEFDPD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 999 GEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV---QKVVEKEVTEEELHDLVNKNL 1075
Cdd:cd05973 328 GSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVvlrGGHEGTPALADELQLHVKKRL 407
|
490 500
....*....|....*....|....
gi 1820754837 1076 PWYCKLQAgIKFVNDFPRISTGKI 1099
Cdd:cd05973 408 SAHAYPRT-IHFVDELPKTPSGKI 430
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
344-543 |
1.12e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 101.30 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 344 VILSYGMTDyGGLCARQTKYSKPGSCGFVceTGRLKVVDPNTGK------------VLGANKTGEIW-AKSSYMMNGYYN 410
Cdd:PRK07867 293 VVDGFGSTE-GGVAITRTPDTPPGALGPL--PPGVAIVDPDTGTecppaedadgrlLNADEAIGELVnTAGPGGFEGYYN 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 411 NPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMA 490
Cdd:PRK07867 370 DPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMA 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 491 FVAKVPGkevTELDI----------TDLVKQNMPWYcrlhagVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK07867 449 ALVLAPG---AKFDPdafaeflaaqPDLGPKQWPSY------VRVCAELPRTATFKVLKRQLS 502
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
762-1099 |
1.46e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.11 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 762 PHDLAMICSSSGTTGMPKGTELSYASLynsITPVEEVHAkneicaWVPTIrwhGGLNQCIEVIMS----------NAKWI 831
Cdd:PRK08751 207 PDDIAFLQYTGGTTGVAKGAMLTHRNL---VANMQQAHQ------WLAGT---GKLEEGCEVVITalplyhifalTANGL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 832 IFSD--------DNIKEIA--LCEIIQKHGVTWLGTDTNFAILyvkMNI--FQKYPMPSLRKMVITGAPFTKELHETVAK 899
Cdd:PRK08751 275 VFMKiggcnhliSNPRDMPgfVKELKKTRFTAFTGVNTLFNGL---LNTpgFDQIDFSSLKMTLGGGMAVQRSVAERWKQ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 900 IMpHTQILQCYGLTDAG-GLCVSQAK-NSKPGSCGFVTKGIRIKIADEkTGIALGPKERGEICIKSEFMMKGYHKNPEQT 977
Cdd:PRK08751 352 VT-GLTLVEAYGLTETSpAACINPLTlKEYNGSIGLPIPSTDACIKDD-AGTVLAIGEIGELCIKGPQVMKGYWKRPEET 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 978 KEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIEL-PLAFVQK 1056
Cdd:PRK08751 430 AKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIvKVVIVKK 509
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1820754837 1057 VVEKEVTEEELHdlVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK08751 510 DPALTAEDVKAH--ARANLTGY-KQPRIIEFRKELPKTNVGKI 549
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
50-542 |
1.89e-21 |
|
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: 99.46 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 50 PEFIAQVEAVTgaETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELspmtary 129
Cdd:cd17650 1 PDAIAVSDATR--QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 130 flsltkPKivfvngesaeclaqvvkennmdTRLVVFADSAGfvgraATLTavlrsqdtawidefecakLTSPKHVAAIVC 209
Cdd:cd17650 72 ------PA----------------------ERLQYMLEDSG-----AKLL------------------LTQPEDLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 210 SSGTSGFPKGTEISHAAMIN-YMAHVKVHDLKG----HVSMWTPSMRWYCGLFIviKAILDCSKRIIVPD--YDDDEGLC 282
Cdd:cd17650 101 TSGTTGKPKGVMVEHRNVAHaAHAWRREYELDSfpvrLLQMASFSFDVFAGDFA--RSLLNGGTLVICPDevKLDPAALY 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 283 RFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLV-KLLPHTDVILSYGMT---------- 351
Cdd:cd17650 179 DLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAaRFGQGMRIINSYGVTeatidstyye 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 352 -DYGGLC-ARQTKYSKPgscgfvCETGRLKVVDPnTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGW----- 424
Cdd:cd17650 259 eGRDPLGdSANVPIGRP------LPNTAMYVLDE-RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapger 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 425 -LHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQvAVVPVPHNINEEHAM-AFVakVPGKEVTE 502
Cdd:cd17650 332 mYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGGEARLcAYV--VAAATLNT 408
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1820754837 503 LDITDLVKQNMPWYCrLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:cd17650 409 AELRAFLAKELPSYM-IPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1338-1615 |
2.60e-21 |
|
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: 99.98 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1338 PDDVALIVPSSGTTGLPKGTEISH---YSLFCCLhpykNRTLVGHTCIvTPTmrwhyGVLMAF--------RLVAA---- 1402
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHgniVSNVAGV----FKILEILNKI-NPT-----DVYISYlplahifeRVVEAlfly 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1403 ----------NAKKLI-------------VP-----------DNDDAENFCQ-----LIEKYQITWF-----GTDPF--- 1435
Cdd:cd05927 183 hgakigfysgDIRLLLddikalkptvfpgVPrvlnriydkifNKVQAKGPLKrklfnFALNYKLAELrsgvvRASPFwdk 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1436 MIIKFIKSQLLEKYRLptlkvILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACVVSAQNKF-TKLGSVGYVSSNVR 1514
Cdd:cd05927 263 LVFNKIKQALGGNVRL-----MLTGSAPLSPEVLEFLRVAL-GCPVLEGYGQTECTAGATLTLPGdTSVGHVGGPLPCAE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1515 IKMVDLDTEE--ALGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFinFRSIN 1592
Cdd:cd05927 337 VKLVDVPEMNydAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNI--FKLSQ 414
|
330 340
....*....|....*....|....*.
gi 1820754837 1593 ---VSPAEIETVLMTHPAVLQAAVLG 1615
Cdd:cd05927 415 geyVAPEKIENIYARSPFVAQIFVYG 440
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1485-1682 |
3.36e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 99.72 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVVSAQNKfTKLGSVGYVSSNVRIkmVDLDT------------------EEAlgpnkIGELRVKAITIM-QGY 1545
Cdd:PRK13388 295 YGSSEGAVIVVREPG-TPPGSIGRGAPGVAI--YNPETltecavarfdahgallnaDEA-----IGELVNTAGAGFfEGY 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1546 HKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNE-VDEQH 1624
Cdd:PRK13388 367 YNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDErVGDQV 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 1625 PKAFVVQvPNKSVTEQELISYVE-------KNLPDYcrlrggVKIVDQLPRTTTGKIARKQLRDM 1682
Cdd:PRK13388 446 MAALVLR-DGATFDPDAFAAFLAaqpdlgtKAWPRY------VRIAADLPSTATNKVLKRELIAQ 503
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1344-1676 |
3.90e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 100.20 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1344 IVPSSGTTGLPKGTEISH--------YSLFCCLHPYKNRTLVGHTCIVTPTMrwhYGVLMAFrLVAANAKKL----IVPD 1411
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNgphlvglkYYWRSIIEKDIPTVVFSHSSIGWVSF---HGFLYGS-LSLGNTFVMfeggIIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1412 NDDAENFCQLIEKYQITWFGTDPFMIIKFIK-----SQLLEKYRLPTLKVILSSGahlrkehlEVMREKLPD-------V 1479
Cdd:PTZ00237 335 KHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYDLSNLKEIWCGG--------EVIEESIPEyienklkI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1480 FITNHYGMTDTAC--VVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELRVK-------AITimqgYHKNPE 1550
Cdd:PTZ00237 407 KSSRGYGQTEIGItyLYCYGHINIPYNATGVPSIFIKPSILSEDGKE-LNVNEIGEVAFKlpmppsfATT----FYKNDE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1551 TTKQAFDS-DGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFV 1629
Cdd:PTZ00237 482 KFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLL 561
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1630 VQVPNKSVTEQEL------ISYVEKNLPDYCRLRGGVKIVDQLPRTTTGKIAR 1676
Cdd:PTZ00237 562 VLKQDQSNQSIDLnklkneINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
629-1099 |
6.43e-21 |
|
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: 99.31 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIicpwdHVV-------SKLSARyfLSLMSPK 701
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAI-----HSVvfggfaaKELASR--IDDAKPK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 702 VVFVNEESAEN---------LMEAAKEENLQ-VRVMVI--GSLPG--FVSLANIL-EEQVSRAE-IDgfrCTKIDNPHDL 765
Cdd:cd05967 157 LIVTASCGIEPgkvvpykplLDKALELSGHKpHHVLVLnrPQVPAdlTKPGRDLDwSELLAKAEpVD---CVPVAATDPL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 766 aMICSSSGTTGMPKG---------TELSYA--SLYNsITPVEEVHAKNEIcAWV--PTIRWHGGLNQCIEVIMSNAKWII 832
Cdd:cd05967 234 -YILYTSGTTGKPKGvvrdngghaVALNWSmrNIYG-IKPGDVWWAASDV-GWVvgHSYIVYGPLLHGATTVLYEGKPVG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 833 FSDDNikeiALCEIIQKHGVTWLGT-----------DTNFAILyvkmnifQKYPMPSLRKMVITGAPFTKELHETVAKIM 901
Cdd:cd05967 311 TPDPG----AFWRVIEKYQVNALFTaptairairkeDPDGKYI-------KKYDLSSLRTLFLAGERLDPPTLEWAENTL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 902 pHTQILQCYGLTDAG----GLCVSQAKNS-KPGSCGFVTKGIRIKIADEkTGIALGPKERGEICIKSEF---MMKGYHKN 973
Cdd:cd05967 380 -GVPVIDHWWQTETGwpitANPVGLEPLPiKAGSPGKPVPGYQVQVLDE-DGEPVGPNELGNIVIKLPLppgCLLTLWKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 974 PEQTKEAF--DSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPL 1051
Cdd:cd05967 458 DERFKKLYlsKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPL 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1052 AFVQKVVEKEVTEEELHD----LVNKNLPWYCKLQAGIkFVNDFPRISTGKI 1099
Cdd:cd05967 538 GLVVLKEGVKITAEELEKelvaLVREQIGPVAAFRLVI-FVKRLPKTRSGKI 588
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
629-1038 |
6.44e-21 |
|
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: 97.34 E-value: 6.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRK-HGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWD--HVVSKLsaRYFLSLMSPKVVFV 705
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDpaYPAERL--AFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 706 NEESAENLMEAAKEenlqvrvmvigslpgfVSLANILEEQVSRAEIDGFRCTKIDNPHDLAMICSSSGTTGMPKGTELSY 785
Cdd:TIGR01733 79 DSALASRLAGLVLP----------------VILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 786 ASLYNSITPVEEVHAKNE---------------ICAWVPTIRwHGGlnqCIEVIMSnakwiifSDDNIKEIALCEIIQKH 850
Cdd:TIGR01733 143 RSLVNLLAWLARRYGLDPddrvlqfaslsfdasVEEIFGALL-AGA---TLVVPPE-------DEERDDAALLAALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 851 GVTWLGTDTNFAILYVKMnifQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAgglCVSQAKNSKPGS 930
Cdd:TIGR01733 212 PVTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTET---TVWSTATLVDPD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 931 C--GFVTKGI-------RIKIADEKTGIaLGPKERGEICIKSEFMMKGYHKNPEQTKEAF------DSDG--WLHTKDIG 993
Cdd:TIGR01733 286 DapRESPVPIgrplantRLYVLDDDLRP-VPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaGGDGarLYRTGDLV 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1820754837 994 YYDENGEIFFVNRIsDF---INYKAIKLssAEIEGVLELHPSILKAVV 1038
Cdd:TIGR01733 365 RYLPDGNLEFLGRI-DDqvkIRGYRIEL--GEIEAALLRHPGVREAVV 409
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
624-1044 |
7.22e-21 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 100.38 E-value: 7.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 624 TGKECTYAEMRERSIKCALWLRKHgIQKGDNIGILtenhLNTCVPV----LAILYIGGII------------------CP 681
Cdd:PRK08633 638 TGGELSYGKALTGALALARLLKRE-LKDEENVGIL----LPPSVAGalanLALLLAGKVPvnlnytaseaalksaieqAQ 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 682 WDHVVS------KLSARYFL--SLMSPKVVFVneesaENLMEAakeenlqvrvmvIGSLPGFVSLANIleeQVSRAEIDG 753
Cdd:PRK08633 713 IKTVITsrkfleKLKNKGFDleLPENVKVIYL-----EDLKAK------------ISKVDKLTALLAA---RLLPARLLK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 754 FRCTKIDNPHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEV-HAKNE--ICA--------------WVPTIrwhgg 816
Cdd:PRK08633 773 RLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVfNLRNDdvILSslpffhsfgltvtlWLPLL----- 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 817 lnqcievimSNAKWIIFSDD-NIKEIAlcEIIQKHGVTWL-GTDTnFAILYVKMNIFQKYPMPSLRkMVITGApftKELH 894
Cdd:PRK08633 848 ---------EGIKVVYHPDPtDALGIA--KLVAKHRATILlGTPT-FLRLYLRNKKLHPLMFASLR-LVVAGA---EKLK 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 895 ETVA---KIMPHTQILQCYGLTD-------------AGGlcVSQAKNSKPGSCGFVTKGIRIKIADEKTGIALGPKERGE 958
Cdd:PRK08633 912 PEVAdafEEKFGIRILEGYGATEtspvasvnlpdvlAAD--FKRQTGSKEGSVGMPLPGVAVRIVDPETFEELPPGEDGL 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 959 ICIKSEFMMKGYHKNPEQTKEA---FDSDGWLHTKDIGYYDENGEIFFVNRISDF--INYKAIKLSSAEIEGVLELHPSI 1033
Cdd:PRK08633 990 ILIGGPQVMKGYLGDPEKTAEVikdIDGIGWYVTGDKGHLDEDGFLTITDRYSRFakIGGEMVPLGAVEEELAKALGGEE 1069
|
490
....*....|.
gi 1820754837 1034 LKAVVVPVPHE 1044
Cdd:PRK08633 1070 VVFAVTAVPDE 1080
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
614-1099 |
7.85e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 98.16 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 614 PDFVGQIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARY 693
Cdd:PRK13390 11 PDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 694 FLSLMSPKVVFVNeeSAENLMEAAKEENLQVRVMVIGSLPGFVSLANILEEQvsraeidGFRCTkiDNPHDLAMIcSSSG 773
Cdd:PRK13390 91 IVGDSGARVLVAS--AALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGA-------GPRLT--EQPCGAVML-YSSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 774 TTGMPKGTE---------------LSYASLYNSITPVEEVHAKNEICAWVPtIRWHGGLNQCIEVIMSNAKWiifsddni 838
Cdd:PRK13390 159 TTGFPKGIQpdlpgrdvdapgdpiVAIARAFYDISESDIYYSSAPIYHAAP-LRWCSMVHALGGTVVLAKRF-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 839 KEIALCEIIQKHGVTWLGTDTNFAILYVKMN--IFQKYPMPSLRKMVITGAPFTKEL-HETVAKIMPhtQILQCYGLTDA 915
Cdd:PRK13390 230 DAQATLGHVERYRITVTQMVPTMFVRLLKLDadVRTRYDVSSLRAVIHAAAPCPVDVkHAMIDWLGP--IVYEYYSSTEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 916 GGLCVSQAKN--SKPGSCGFVTKGiRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDG--WLHTKD 991
Cdd:PRK13390 308 HGMTFIDSPDwlAHPGSVGRSVLG-DLHICDDD-GNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 992 IGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLV 1071
Cdd:PRK13390 386 LGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELI 465
|
490 500 510
....*....|....*....|....*....|
gi 1820754837 1072 NKNLPWYCKLQA--GIKFVNDFPRISTGKI 1099
Cdd:PRK13390 466 DYTRSRIAHYKAprSVEFVDELPRTPTGKL 495
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1343-1679 |
1.04e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 98.14 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1343 LIVPSSGTTGLPKGT----EISHYSLFCCLHPYKNRTLVGHTCIVTPTMrWH---YGVLMafrLVAANAKKLIVPDNDDA 1415
Cdd:PRK13383 178 IVLLTSGTTGKPKGVprapQLRSAVGVWVTILDRTRLRTGSRISVAMPM-FHglgLGMLM---LTIALGGTVLTHRHFDA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1416 ENFCQLIEKYQITWFGTDPFMIIKFIK--SQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVfITNHYGMTDTAcv 1493
Cdd:PRK13383 254 EAALAQASLHRADAFTAVPVVLARILElpPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVG-- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1494 VSAQNKFTKL----GSVGYVSSNVRIKMVDLDTeEALGPNKIGELRVKAITIMQGYHKNPETTKqafdSDGWLRTGDLAY 1569
Cdd:PRK13383 331 IGALATPADLrdapETVGKPVAGCPVRILDRNN-RPVGPRVTGRIFVGGELAGTRYTDGGGKAV----VDGMTSTGDMGY 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1570 YDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKN 1649
Cdd:PRK13383 406 LDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDR 485
|
330 340 350
....*....|....*....|....*....|
gi 1820754837 1650 LPDYCRLRgGVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK13383 486 VSRFEQPR-DINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
629-1100 |
1.05e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 98.03 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIicP----WDHVVSKLsaRYFLSLMSPKVVF 704
Cdd:PRK07798 30 TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV--PvnvnYRYVEDEL--RYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 705 VNEESAENLMEA-AKEENLQVRVMV-----IGSLPGFVSLANILEEQvSRAEIDGFRCtkidnPHDLAMICSSsGTTGMP 778
Cdd:PRK07798 106 YEREFAPRVAEVlPRLPKLRTLVVVedgsgNDLLPGAVDYEDALAAG-SPERDFGERS-----PDDLYLLYTG-GTTGMP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 779 KG----TELSYASLYNSI-----TPVEEVHAKNEICAWVPTIRW-------HG-GLNQCIEVIMSNAKWIIFSDDNIKEI 841
Cdd:PRK07798 179 KGvmwrQEDIFRVLLGGRdfatgEPIEDEEELAKRAAAGPGMRRfpapplmHGaGQWAAFAALFSGQTVVLLPDVRFDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 842 ALCEIIQKHGVTWLgTDTNFAI---LYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAG-G 917
Cdd:PRK07798 259 EVWRTIEREKVNVI-TIVGDAMarpLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIGSSETGfG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 918 LCVSQAKNSKPGSCGFVTKGIRIKIADEKTGIAL-GPKERGEICiKSEFMMKGYHKNPEQTKEAFDS-DG--WLHTKDIG 993
Cdd:PRK07798 338 GSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEpGSGEIGWIA-RRGHIPLGYYKDPEKTAETFPTiDGvrYAIPGDRA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 994 YYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNK 1073
Cdd:PRK07798 417 RVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRS 496
|
490 500
....*....|....*....|....*..
gi 1820754837 1074 NLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:PRK07798 497 SLAGY-KVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
629-1043 |
1.06e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 98.02 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNEE 708
Cdd:PRK07514 30 TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAENLMEAAKEENLQvRVMVI-----GSLPGFVSLANILEEQVSRAeidgfrctkidnPHDLAMICSSSGTTGMPKGTEL 783
Cdd:PRK07514 110 NFAWLSKIAAAAGAP-HVETLdadgtGSLLEAAAAAPDDFETVPRG------------ADDLAAILYTSGTTGRSKGAML 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 784 SYASLY-NSITPVEE---------VHAkneicawVPTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEIalceiiqkhgVT 853
Cdd:PRK07514 177 SHGNLLsNALTLVDYwrftpddvlIHA-------LPIFHTHGLFVATNVALLAGASMIFLPKFDPDAV----------LA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 854 WLGTDTNF---AILYVKM---NIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTqILQCYGLTDAGGLcvsqakNSK 927
Cdd:PRK07514 240 LMPRATVMmgvPTFYTRLlqePRLTREAAAHMRLFISGSAPLLAETHREFQERTGHA-ILERYGMTETNMN------TSN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 928 P-------GSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGE 1000
Cdd:PRK07514 313 PydgerraGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGY 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1820754837 1001 IFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPH 1043
Cdd:PRK07514 393 VHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPH 435
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1339-1683 |
1.22e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 95.50 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1339 DDVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRtLVGhtcivtpTMRW------HY--GVLMAFRLVAANAKKLI-- 1408
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDR-LGG-------PGQWllalpaHHiaGLQVLVRSVIAGSEPVEld 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1409 VPDNDDAENFCQLIEKYqitwfgTDPFMIIKFIKSQLLEKYR-------LPTLKVILSSGAHLRKEHLEvmREKLPDVFI 1481
Cdd:PRK07824 107 VSAGFDPTALPRAVAEL------GGGRRYTSLVPMQLAKALDdpaataaLAELDAVLVGGGPAPAPVLD--AAAAAGINV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1482 TNHYGMTDTA--CVVSaqnkftklgsvGYVSSNVRIKMVDldteealgpnkiGELRVKAITIMQGYhKNPETTKqAFDSD 1559
Cdd:PRK07824 179 VRTYGMSETSggCVYD-----------GVPLDGVRVRVED------------GRIALGGPTLAKGY-RNPVDPD-PFAEP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1560 GWLRTGDLAYYDDnGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTE 1639
Cdd:PRK07824 234 GWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1820754837 1640 QELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PRK07824 313 EALRAHVARTLDRTAAPR-ELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
614-1099 |
1.28e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 98.08 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 614 PDFVGQIDAFtgKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGgiicpwdhvvsklsARy 693
Cdd:PRK07788 63 PDRAALIDER--GTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG--------------AR- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 694 fLSLMSpkvvfvNEESAENLMEAAKEENlqVRVMVIGSlpGFVSLANILEEQVSRAEIDGFRCTKIDNPH-------DLA 766
Cdd:PRK07788 126 -IILLN------TGFSGPQLAEVAAREG--VKALVYDD--EFTDLLSALPPDLGRLRAWGGNPDDDEPSGstdetldDLI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 767 ----------------MICSSSGTTGMPKGTELSYASlynSITPVEEvhakneICAWVPTIR----------WHG-GLNQ 819
Cdd:PRK07788 195 agsstaplpkppkpggIVILTSGTTGTPKGAPRPEPS---PLAPLAG------LLSRVPFRAgettllpapmFHAtGWAH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 820 CIeVIMSNAKWIIFSDDNIKEIALcEIIQKHGVTWLGTDTNF--AILYVKMNIFQKYPMPSLRKMVITGAPFTKEL---- 893
Cdd:PRK07788 266 LT-LAMALGSTVVLRRRFDPEATL-EDIAKHKATALVVVPVMlsRILDLGPEVLAKYDTSSLKIIFVSGSALSPELatra 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 894 HETVAKImphtqILQCYGLTDAGGLCVSQ----AKNskPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKG 969
Cdd:PRK07788 344 LEAFGPV-----LYNLYGSTEVAFATIATpedlAEA--PGTVGRPPKGVTVKILDEN-GNEVPRGVVGRIFVGNGFPFEG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 970 Y-HKNPEQTKeafdsDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIE 1048
Cdd:PRK07788 416 YtDGRDKQII-----DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1049 LPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK07788 491 RLRAFVVKAPGAALDEDAIKDYVRDNLARY-KVPRDVVFLDELPRNPTGKV 540
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
44-542 |
1.48e-20 |
|
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: 97.12 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 44 EKLRSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELS 123
Cdd:cd17644 8 EQVERTPDAVAVVFE--DQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 124 PMTARYFLSltkpkivfvngesaeclaqvvkennmDTRLVVFadsagfvgraatltavlrsqdtawidefecakLTSPKH 203
Cdd:cd17644 86 QERLTYILE--------------------------DAQISVL--------------------------------LTQPEN 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 204 VAAIVCSSGTSGFPKGTEISHAAMINYmAH--VKVHDLkghvsmwTPSMRwyCGLFI----------VIKAILDCSKRII 271
Cdd:cd17644 108 LAYVIYTSGSTGKPKGVMIEHQSLVNL-SHglIKEYGI-------TSSDR--VLQFAsiafdvaaeeIYVTLLSGATLVL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 272 VPD--YDDDEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLP-TLKILLFGGAHFKGELQQTLVKLL-PHTDVILS 347
Cdd:cd17644 178 RPEemRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPsSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTD--YGGLCARQTKYSKPgscgfvcetgrlKVVDPNTGKVLGANKT---------------GEIWAKSSYMMNGYYN 410
Cdd:cd17644 258 YGPTEatIAATVCRLTQLTER------------NITSVPIGRPIANTQVyildenlqpvpvgvpGELHIGGVGLARGYLN 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 411 NPEATRRALDSDGWLH--------TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHN 482
Cdd:cd17644 326 RPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQ 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 483 INEEHAMAFVakVPGKEVTeLDITDL---VKQNMPWYCRLHAGVkFMEKLPRTATGKIAKKQL 542
Cdd:cd17644 406 PGNKRLVAYI--VPHYEES-PSTVELrqfLKAKLPDYMIPSAFV-VLEELPLTPNGKIDRRAL 464
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
762-1100 |
1.52e-20 |
|
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: 95.53 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 762 PHDLAMICSSsGTTGMPKG----TELSYASLYNSITPVEEVHAKNEICAWV----PTIRW-------HG-GLNQCIEVIM 825
Cdd:cd05924 3 ADDLYILYTG-GTTGMPKGvmwrQEDIFRMLMGGADFGTGEFTPSEDAHKAaaaaAGTVMfpapplmHGtGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 826 SNAKwIIFSDDNIKEIALCEIIQKHGVTWLgTDTNFAILYVKMNIFQK---YPMPSLRKMVITGAPFTKELHETVAKIMP 902
Cdd:cd05924 82 GGQT-VVLPDDRFDPEEVWRTIEKHKVTSM-TIVGDAMARPLIDALRDagpYDLSSLFAISSGGALLSPEVKQGLLELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 903 HTQILQCYGLTDAGGLCVSQAKNSKPGSCGFVTKGIRIKIADEKTG-IALGPKERGEICiKSEFMMKGYHKNPEQTKEAF 981
Cdd:cd05924 160 NITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVVLDDDGRvVPPGSGGVGWIA-RRGHIPLGYYGDEAKTAETF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 982 -DSDG--WLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVV 1058
Cdd:cd05924 239 pEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLRE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1820754837 1059 EKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd05924 319 GAGVDLEELREHCRTRIARY-KLPKQVVFVDEIERSPAGKAD 359
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
378-552 |
1.72e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 97.37 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 378 LKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKIS 457
Cdd:PRK10946 365 VWVADAD-GNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 458 PAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAF-VAKVPGKEVT------ELDITDLvkqnmpwycRLHAGVKFMEKLP 530
Cdd:PRK10946 444 AEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFlVVKEPLKAVQlrrflrEQGIAEF---------KLPDRVECVDSLP 514
|
170 180
....*....|....*....|..
gi 1820754837 531 RTATGKIAKKQLKQIAKSYATN 552
Cdd:PRK10946 515 LTAVGKVDKKQLRQWLASRASA 536
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
65-544 |
1.79e-20 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 97.52 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAECLAQVVKENNMDTRLVVFADSAGfvgraATLTAVLrsqdtawIDEFECAK-LTSPKHVAAIVCSSGTSGFPKGTeiS 223
Cdd:PRK13382 150 FSATVDRALADCPQATRIVAWTDEDH-----DLTVEVL-------IAAHAGQRpEPTGRKGRVILLTSGTTGTPKGA--R 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 224 HAAMINYMAHVKVHD---LKGH--VSMWTPSMRWYCGLFIVIKAILDCSkrIIVPDYDDDEGLCRFIEKYEVSWFrcdSC 298
Cdd:PRK13382 216 RSGPGGIGTLKAILDrtpWRAEepTVIVAPMFHAWGFSQLVLAASLACT--IVTRRRFDPEATLDLIDRHRATGL---AV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 299 FPI---RLVKF--GVLSKYRLPTLKILLFGGAHFKgelQQTLVKLLPH-TDVILS-YGMTDyGGLCARQTK---YSKPGS 368
Cdd:PRK13382 291 VPVmfdRIMDLpaEVRNRYSGRSLRFAAASGSRMR---PDVVIAFMDQfGDVIYNnYNATE-AGMIATATPadlRAAPDT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 369 CGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYynNPEATRRAldSDGWLHTGDLGYYDNDGEVFLVDRMSEF 448
Cdd:PRK13382 367 AGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEM 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 449 INYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEK 528
Cdd:PRK13382 442 IVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANY-KVPRDIVVLDE 520
|
490
....*....|....*.
gi 1820754837 529 LPRTATGKIAKKQLKQ 544
Cdd:PRK13382 521 LPRGATGKILRRELQA 536
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
629-1100 |
2.82e-20 |
|
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: 96.19 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDhvVSKLSAR--YFLSLMSPKVVFVN 706
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVD--IDQPAARreAILADAGARLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 707 EESAENLMEAAKEENLqvrvmvigslpgfVSLANILEEQVSRAEIDgfrctkidnPHDLAMICSSSGTTGMPKGTELSYA 786
Cdd:cd12114 92 GPDAQLDVAVFDVLIL-------------DLDALAAPAPPPPVDVA---------PDDLAYVIFTSGSTGTPKGVMISHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 787 SLYNSITPVEEVHAKNeicawvPTIRWHG--GLNQCIEV------IMSNAKWIIFSDDNIKE-IALCEIIQKHGVT-Wlg 856
Cdd:cd12114 150 AALNTILDINRRFAVG------PDDRVLAlsSLSFDLSVydifgaLSAGATLVLPDEARRRDpAHWAELIERHGVTlW-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 857 tdtNF--AILYVKMNIFQKYPM--PSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAG---GLCVSQAKNSKPG 929
Cdd:cd12114 222 ---NSvpALLEMLLDVLEAAQAllPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASiwsIYHPIDEVPPDWR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 930 SC--GFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAF--DSDG--WLHTKDIGYYDENGEIFF 1003
Cdd:cd12114 299 SIpyGRPLANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1004 VNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYCKLQA 1083
Cdd:cd12114 378 LGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSR 457
|
490
....*....|....*..
gi 1820754837 1084 GIkFVNDFPRISTGKID 1100
Cdd:cd12114 458 VI-ALEALPLTANGKVD 473
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1597-1673 |
2.89e-20 |
|
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: 86.44 E-value: 2.89e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1597 EIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGK 1673
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPK-EVVFVDELPKTRSGK 76
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
622-1099 |
3.23e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 96.63 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 622 AFT--GKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGgiicpwdHVVSKLSARYF----- 694
Cdd:PRK07059 41 AFIcmGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAG-------YVVVNVNPLYTprele 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 695 --LSLMSPKVVFVNEESAENLMEAAKEENLQ------------------------VRVMVIG-SLPGFVSLANILEEQVS 747
Cdd:PRK07059 114 hqLKDSGAEAIVVLENFATTVQQVLAKTAVKhvvvasmgdllgfkghivnfvvrrVKKMVPAwSLPGHVRFNDALAEGAR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 748 RAeidgFRCTKIdNPHDLAMICSSSGTTGMPKGTELSYASL--------------YNSITPVEEVhakNEICAwVP---- 809
Cdd:PRK07059 194 QT----FKPVKL-GPDDVAFLQYTGGTTGVSKGATLLHRNIvanvlqmeawlqpaFEKKPRPDQL---NFVCA-LPlyhi 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 810 ---------TIRwHGGLNqcieVIMSNAKWIifsDDNIKEIalceiiQKHGV-TWLGTDTNFAILyvkMNI--FQKYPMP 877
Cdd:PRK07059 265 faltvcgllGMR-TGGRN----ILIPNPRDI---PGFIKEL------KKYQVhIFPAVNTLYNAL---LNNpdFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 878 SLRkMVITGApftKELHETVAK---IMPHTQILQCYGLTDAGGLCVSQAKNSK--PGSCGFVTKGIRIKIADEKtGIALG 952
Cdd:PRK07059 328 KLI-VANGGG---MAVQRPVAErwlEMTGCPITEGYGLSETSPVATCNPVDATefSGTIGLPLPSTEVSIRDDD-GNDLP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 953 PKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPS 1032
Cdd:PRK07059 403 LGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 1033 ILKAVVVPVPHETDIELPLAFVQKVVEkevteeelhDLVNKNLPWYCKLQAG-------IKFVNDFPRISTGKI 1099
Cdd:PRK07059 483 VLEVAAVGVPDEHSGEAVKLFVVKKDP---------ALTEEDVKAFCKERLTnykrpkfVEFRTELPKTNVGKI 547
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1335-1681 |
3.73e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 96.29 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1335 VTNPDDVALIVPSSGTTGLPKGTEISHYSLfcclhPYKNRTLVGH-------TCIVTPTMrWHYGVLMAFRLVAANAKKL 1407
Cdd:PRK07867 148 VADPDDLFMLIFTSGTSGDPKAVRCTHRKV-----ASAGVMLAQRfglgpddVCYVSMPL-FHSNAVMAGWAVALAAGAS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1408 IV-PDNDDAENFCQLIEKYQITWFG--TDPFmiikfikSQLLEKYRLP-----TLKVILSSGAHLRKehLEVMREKLpDV 1479
Cdd:PRK07867 222 IAlRRKFSASGFLPDVRRYGATYANyvGKPL-------SYVLATPERPddadnPLRIVYGNEGAPGD--IARFARRF-GC 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1480 FITNHYGMTDTAcVVSAQNKFTKLGSVGYVSSNVRIkmVDLDTEEALGP------------NKIGEL-RVKAITIMQGYH 1546
Cdd:PRK07867 292 VVVDGFGSTEGG-VAITRTPDTPPGALGPLPPGVAI--VDPDTGTECPPaedadgrllnadEAIGELvNTAGPGGFEGYY 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1547 KNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPK 1626
Cdd:PRK07867 369 NDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVM 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1627 AFVVQVPNKSVTEQELISYVE-------KNLPDYcrlrggVKIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK07867 448 AALVLAPGAKFDPDAFAEFLAaqpdlgpKQWPSY------VRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
610-1092 |
3.86e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 96.35 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 610 LSSKPDFVGQIDAftGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWD-----H 684
Cdd:PRK06164 20 ARARPDAVALIDE--DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNtryrsH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 685 VVSKLSARYFLSLMSPKVVFVNEESAENLMEAAKEENLQVR-VMVIGS----LPGFVSLANI-LEEQVSRAEIDGFrCTK 758
Cdd:PRK06164 98 EVAHILGRGRARWLVVWPGFKGIDFAAILAAVPPDALPPLRaIAVVDDaadaTPAPAPGARVqLFALPDPAPPAAA-GER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 759 IDNPHDLAMICSSSGTTGMPKgtelsyASLYNSITPVEEVHAKNEICAWVPTIR------WHG--GLNQCIEVIMSNAKw 830
Cdd:PRK06164 177 AADPDAGALLFTTSGTTSGPK------LVLHRQATLLRHARAIARAYGYDPGAVllaalpFCGvfGFSTLLGALAGGAP- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 831 iIFSDDNIKEIALCEIIQKHGVTW-LGTDTNFAILYVKMNifQKYPMPSLRKMVItgAPFTKELHETVAKI----MPHTQ 905
Cdd:PRK06164 250 -LVCEPVFDAARTARALRRHRVTHtFGNDEMLRRILDTAG--ERADFPSARLFGF--ASFAPALGELAALArargVPLTG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 906 IlqcYGLTDAGGLcVSQAKNSKPGSCGFVTKG------IRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKE 979
Cdd:PRK06164 325 L---YGSSEVQAL-VALQPATDPVSVRIEGGGrpaspeARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 980 AFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIElPLAFVQKVVE 1059
Cdd:PRK06164 401 ALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTV-PVAFVIPTDG 479
|
490 500 510
....*....|....*....|....*....|...
gi 1820754837 1060 KEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFP 1092
Cdd:PRK06164 480 ASPDEAGLMAACREALAGF-KVPARVQVVEAFP 511
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
41-542 |
4.39e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.11 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 41 LVLEKLRSRPEFIAqveAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWD 119
Cdd:PRK12316 516 LFEEQVERTPEAPA---LAFGEETlDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 120 NElspmtaryflsltkpkivfvngESAECLAQVVKENNMdtrLVVFADS--AGFVGRAATLTAVLRSQDTAWIDEFECAK 197
Cdd:PRK12316 593 PE----------------------YPAERLAYMLEDSGV---QLLLSQShlGRKLPLAAGVQVLDLDRPAAWLEGYSEEN 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 198 LTS---PKHVAAIVCSSGTSGFPKGTEISHAAMINY---MAHVKVHDLKGHVSMWTPSmRWYCGLFIVIKAILDCSKRII 271
Cdd:PRK12316 648 PGTelnPENLAYVIYTSGSTGKPKGAGNRHRALSNRlcwMQQAYGLGVGDTVLQKTPF-SFDVSVWEFFWPLMSGARLVV 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 272 VP--DYDDDEGLCRFIEKYEVSWFRcdscFPIRLVKfGVLSKYRLP---TLKILLFGGAHFKGELQQTLVKLLPHTDVIL 346
Cdd:PRK12316 727 AApgDHRDPAKLVELINREGVDTLH----FVPSMLQ-AFLQDEDVAsctSLRRIVCSGEALPADAQEQVFAKLPQAGLYN 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 347 SYGMTDYG-----GLCARQTKYSKPgsCGFVCETGRLKVVDPNTGKV-LGAnkTGEIWAKSSYMMNGYYNNPEATRRAL- 419
Cdd:PRK12316 802 LYGPTEAAidvthWTCVEEGGDSVP--IGRPIANLACYILDANLEPVpVGV--LGELYLAGRGLARGYHGRPGLTAERFv 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 420 -----DSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVphniNEEHAMAFVAK 494
Cdd:PRK12316 878 pspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVVL 953
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 495 VPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:PRK12316 954 ESEGGDWREALKAHLAASLPEY-MVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
59-546 |
4.41e-20 |
|
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: 95.86 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 59 VTGAETTFAEMTEKSVKCALWLREqGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKI 138
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 139 VFVNGESAECLAQV-VKENNMDTRLVVFADSAGFVGRAATLTAVLRSQ--DTAWIDEFECAKlTSPKHVAAIVCSSGTSG 215
Cdd:cd05909 82 VLTSKQFIEKLKLHhLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKfpPKWLLRIFGVAP-VQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 216 FPKGTEISHAAMI-NYMAHVKVHDLKGHVSMWTPSMRWYC-GLFI-VIKAILDCSKRIIVPDYDDDEGLCRFIEKYEVSW 292
Cdd:cd05909 161 LPKGVVLSHKNLLaNVEQITAIFDPNPEDVVFGALPFFHSfGLTGcLWLPLLSGIKVVFHPNPLDYKKIPELIYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 293 FRCDSCFPIRLVKFgvLSKYRLPTLKILLFGGAHFKGELQQTLVKLLpHTDVILSYGMTDYGGLCARQTKYS--KPGSCG 370
Cdd:cd05909 241 LLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECSPVISVNTPQSpnKEGTVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 371 FVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFIN 450
Cdd:cd05909 318 RPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 451 YRAIKISPAEIEALIQQH-PAVFQVAVVPVPHNINEEHAMAFVAkvpGKEVTELDITDLVKqnmpwycrlHAGVK----- 524
Cdd:cd05909 397 IAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT---TTDTDPSSLNDILK---------NAGISnlakp 464
|
490 500
....*....|....*....|....*.
gi 1820754837 525 ----FMEKLPRTATGKIAKKQLKQIA 546
Cdd:cd05909 465 syihQVEEIPLLGTGKPDYVTLKALA 490
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1335-1679 |
4.45e-20 |
|
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: 95.61 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1335 VTNPDDVALIVPSSGTTGLPKGTEISHyslfcclhpyknRTLVGHtcivTPTMRWHYGV------LMAFRLVAANAKKL- 1407
Cdd:cd05910 81 IPKADEPAAILFTSGSTGTPKGVVYRH------------GTFAAQ----IDALRQLYGIrpgevdLATFPLFALFGPALg 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1408 ---IVPDND-------DAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLP 1477
Cdd:cd05910 145 ltsVIPDMDptrparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1478 D-VFITNHYGMTDT--ACVVSAQNKFTKLGS---------VGYVSSNVRIKMVDLDTEE--------ALGPNKIGELRVK 1537
Cdd:cd05910 225 DeAEILTPYGATEAlpVSSIGSRELLATTTAatsggagtcVGRPIPGVRVRIIEIDDEPiaewddtlELPRGEIGEITVT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1538 AITIMQGYHKNPETTKQAFDSDG----WLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAV 1613
Cdd:cd05910 305 GPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1614 LGIPNEVdEQHPKAFVVQVPNKSVT----EQELISYVEKNlPDYCRLRgGVKIVDQLPRTT--TGKIARKQL 1679
Cdd:cd05910 385 VGVGKPG-CQLPVLCVEPLPGTITPrarlEQELRALAKDY-PHTQRIG-RFLIHPSFPVDIrhNAKIFREKL 453
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
324-547 |
5.16e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 95.62 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 324 GAHFKGELQQTLVKLLPHTDVILSYGMTDYGGLCARQTKYS--KPGSCGFVCETGRLKVVDPnTGKVLGANKTGEIWAKS 401
Cdd:PRK07638 262 GAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVDEESerRPNSVGRPFHNVQVRICNE-AGEEVQKGEIGTVYVKS 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 402 SYMMNGYYNNpEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPH 481
Cdd:PRK07638 341 PQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPD 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 482 NINEEHAmafVAKVPGKEvTELDITDLVKQNMP-------WYcrlhagvkFMEKLPRTATGKIAKKQLKQIAK 547
Cdd:PRK07638 420 SYWGEKP---VAIIKGSA-TKQQLKSFCLQRLSsfkipkeWH--------FVDEIPYTNSGKIARMEAKSWIE 480
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
43-550 |
5.20e-20 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 96.48 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 43 LEKLRSRPEFIAQVEAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNpwdne 121
Cdd:cd05966 63 LKERGDKVAIIWEGDEPDQSRTiTYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHS----- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 122 lspmtaryflsltkpkIVFvNGESAECLAQVVkeNNMDTRLVVFADsAGF---------------------------VGR 174
Cdd:cd05966 138 ----------------VVF-AGFSAESLADRI--NDAQCKLVITAD-GGYrggkviplkeivdealekcpsvekvlvVKR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 175 AATLTAVLRSQDTAWIDEF-----EC-AKLTSPKHVAAIVCSSGTSGFPKGTEISHAAminYMAHVK-----VHDLKGHV 243
Cdd:cd05966 198 TGGEVPMTEGRDLWWHDLMakqspECePEWMDSEDPLFILYTSGSTGKPKGVVHTTGG---YLLYAAttfkyVFDYHPDD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 244 SMW-TPSMRWYCG-LFIVIKAILDCSKRII---VPDYDDDEGLCRFIEKYEVSWFRCDscfP--IR-LVKFG--VLSKYR 313
Cdd:cd05966 275 IYWcTADIGWITGhSYIVYGPLANGATTVMfegTPTYPDPGRYWDIVEKHKVTIFYTA---PtaIRaLMKFGdeWVKKHD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 314 LPTLKILlfggaHFKGElqqtlvkllP----------------HTDVILSYGMTDYGGLC------ARQTKyskPGSCGF 371
Cdd:cd05966 352 LSSLRVL-----GSVGE---------PinpeawmwyyevigkeRCPIVDTWWQTETGGIMitplpgATPLK---PGSATR 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 372 VCETGRLKVVDPNTGKVlGANKTGEIWAKSSY--MMNGYYNNPEATRRALDSD--GWLHTGDLGYYDNDGEVFLVDRMSE 447
Cdd:cd05966 415 PFFGIEPAILDEEGNEV-EGEVEGYLVIKRPWpgMARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDD 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 448 FINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQnmpwyCRLHAG----- 522
Cdd:cd05966 494 VINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKH-----VRKEIGpiatp 568
|
570 580 590
....*....|....*....|....*....|
gi 1820754837 523 --VKFMEKLPRTATGKIAKKQLKQIAKSYA 550
Cdd:cd05966 569 dkIQFVPGLPKTRSGKIMRRILRKIAAGEE 598
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
365-543 |
5.65e-20 |
|
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: 94.85 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 365 KPGSCGFVCETGRLKVVDpNTGKVLGANKTGEIWAKSSymmNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDR 444
Cdd:cd05958 263 RPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 445 MSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTEL---DITDLVKQNMPWYCRLHA 521
Cdd:cd05958 339 SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRA 418
|
170 180
....*....|....*....|..
gi 1820754837 522 gVKFMEKLPRTATGKIAKKQLK 543
Cdd:cd05958 419 -IEFVTELPRTATGKLQRFALR 439
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
629-1100 |
5.94e-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: 94.68 E-value: 5.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDhvvsklsaryflslmspkvvfvnee 708
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLD------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 saenlmeaakeenlqvrvmviGSLPGfVSLANILEEqvSRAEIdgfrCTKIDNPHDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd17653 79 ---------------------AKLPS-ARIQAILRT--SGATL----LLTTDSPDDLAYIIFTSGSTGIPKGVMVPHRGV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 YNSitpVEEVHAkneicawvptiRWHGGLNQCIEVIMSNAkwiiFsDDNIKEI--ALCeiiqkHGVTWL--GTDTNFAIL 864
Cdd:cd17653 131 LNY---VSQPPA-----------RLDVGPGSRVAQVLSIA----F-DACIGEIfsTLC-----NGGTLVlaDPSDPFAHV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 865 YVKMNIFQKYP----------MPSLRKMVITGAPFTKELhetVAKIMPHTQILQCYGLTDAGglCVSQAKNSKPGScgFV 934
Cdd:cd17653 187 ARTVDALMSTPsilstlspqdFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTECT--ISSTMTELLPGQ--PV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 935 TKG-----IRIKIADEKTGIALGPkERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLH------TKDIGYYDENGEIFF 1003
Cdd:cd17653 260 TIGkpipnSTCYILDADLQPVPEG-VVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1004 VNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIelplAFVqkvVEKEVTEEELHDLVNKNLPWYCKLQA 1083
Cdd:cd17653 339 LGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNGRLV----AFV---TPETVDVDGLRSELAKHLPSYAVPDR 411
|
490
....*....|....*..
gi 1820754837 1084 GIKfVNDFPRISTGKID 1100
Cdd:cd17653 412 IIA-LDSFPLTANGKVD 427
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1202-1680 |
6.48e-20 |
|
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: 95.58 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQ-TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAI----SNTWDHELTPMTarnfLTLTS 1276
Cdd:cd05915 21 EVHRtTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVlhtaNPRLSPKEIAYI----LNHAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1277 PKIVFtVSSSAANLMEAAKELKMNLKVVVMDKlDGYESVEENVMKGHDTREIIEfkcHVTNPDDVALIVpSSGTTGLPKG 1356
Cdd:cd05915 97 DKVLL-FDPNLLPLVEAIRGELKTVQHFVVMD-EKAPEGYLAYEEALGEEADPV---RVPERAACGMAY-TTGTTGLPKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1357 TEISHYSlfcclhPYKNRTLVG------------HTCIVtPTMR---WHY--------GVLMAFRLVAanakklivpdND 1413
Cdd:cd05915 171 VVYSHRA------LVLHSLAASlvdgtalsekdvVLPVV-PMFHvnaWCLpyaatlvgAKQVLPGPRL----------DP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1414 daENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVmrEKLPDVFITNHYGMTD---- 1489
Cdd:cd05915 234 --ASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIAR--FERMGVEVRQGYGLTEtspv 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1490 -TACVVSAQnkFTKLGSvgyvSSNVRIKMVD-----------LDTEEALGPNKIGELRVKAI---TIMQGYHKNPETTKQ 1554
Cdd:cd05915 310 vVQNFVKSH--LESLSE----EEKLTLKAKTglpiplvrlrvADEEGRPVPKDGKALGEVQLkgpWITGGYYGNEEATRS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1555 AFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFvVQVPN 1634
Cdd:cd05915 384 ALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV-VVPRG 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1820754837 1635 KSVTEQELISYVEKNLPDYCRLRGGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:cd05915 463 EKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
625-1100 |
6.79e-20 |
|
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: 94.96 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 625 GKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVF 704
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 705 VNEESAENLMEaakeenLQVRVMVIGSLPGFvslanilEEQVSRAEIDgfrctkidnPHDLAMICSSSGTTGMPKGTELS 784
Cdd:cd12117 100 TDRSLAGRAGG------LEVAVVIDEALDAG-------PAGNPAVPVS---------PDDLAYVMYTSGSTGRPKGVAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 785 YASL--------YNSITPVEEV-HAKN--------EIcaWVPtirwhgglnqcievIMSNAKWIIFSDDNIKEI-ALCEI 846
Cdd:cd12117 158 HRGVvrlvkntnYVTLGPDDRVlQTSPlafdastfEI--WGA--------------LLNGARLVLAPKGTLLDPdALGAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 847 IQKHGVT--WLgTDTNFAILYvkmnifQKYP--MPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDagglcvsq 922
Cdd:cd12117 222 IAEEGVTvlWL-TAALFNQLA------DEDPecFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTE-------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 923 akNSKPGSCGFVTK---------------GIRIKIADEkTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWL 987
Cdd:cd12117 287 --NTTFTTSHVVTEldevagsipigrpiaNTRVYVLDE-DGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 988 ------HTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVqkVVEKE 1061
Cdd:cd12117 364 pgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV--VAEGA 441
|
490 500 510
....*....|....*....|....*....|....*....
gi 1820754837 1062 VTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd12117 442 LDAAELRAFLRERLPAY-MVPAAFVVLDELPLTANGKVD 479
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
38-544 |
1.41e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.38 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 38 VGALVLEKLRSRPEFIAqveAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISN 116
Cdd:PRK12467 514 VHQLIEAQARQHPERPA---LVFGEQVlSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYV 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 117 PWDNELSPMTARYFLSLTKPKIVFVNGESAECLAqvvkennmdtrlvvfadsagfvgRAATLTAVLRSQDTAWIDEFECA 196
Cdd:PRK12467 591 PLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLP-----------------------VPAGLRSLCLDEPADLLCGYSGH 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 197 KLT---SPKHVAAIVCSSGTSGFPKGTEISHAAMINY-----------------MAHVKVHDLkGHVSMWTPSMRwycgl 256
Cdd:PRK12467 648 NPEvalDPDNLAYVIYTSGSTGQPKGVAISHGALANYvcviaerlqlaaddsmlMVSTFAFDL-GVTELFGALAS----- 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 257 fivikaildcSKRIIVPDYD---DDEGLCRFIEKYEVSWFRCdscFPIRLVKFGVLSKYRLPT-LKILLFGGAHFKGELQ 332
Cdd:PRK12467 722 ----------GATLHLLPPDcarDAEAFAALMADQGVTVLKI---VPSHLQALLQASRVALPRpQRALVCGGEALQVDLL 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 333 QTLVKLLPHTDVILSYGMTDYG-----GLCARQTKYSKPGSCGFVCETGRLKVVDpNTGKVLGANKTGEIWAKSSYMMNG 407
Cdd:PRK12467 789 ARVRALGPGARLINHYGPTETTvgvstYELSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARG 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 408 YYNNP--EATRRALDSDG-----WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVP 480
Cdd:PRK12467 868 YHRRPalTAERFVPDPFGadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP 947
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 481 hninEEHAMAFVAK-VPG-------KEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK12467 948 ----GDAGLQLVAYlVPAavadgaeHQATRDELKAQLRQVLPDY-MVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1176-1679 |
1.61e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 94.30 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1176 PVNIAEETLKFLKSKPDSIGQVDALTGKVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAI 1255
Cdd:PRK05857 13 PSTVLDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1256 SNTWDHELTPMTARNFLTLTSPKIVFTVSSSAANlmeaAKELKMNLKVVVMDKLDGYESVEENVMKGHDTREiiefkchV 1335
Cdd:PRK05857 93 AVMADGNLPIAAIERFCQITDPAAALVAPGSKMA----SSAVPEALHSIPVIAVDIAAVTRESEHSLDAASL-------A 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1336 TNP----DDVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRTL------VGHTcIVTPTMRWHYGVLMaFRLVAANAK 1405
Cdd:PRK05857 162 GNAdqgsEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGLnwvtwvVGET-TYSPLPATHIGGLW-WILTCLMHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1406 KLIVPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAhlRKEHLEVMREKLPDVFITNHY 1485
Cdd:PRK05857 240 GLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGS--RAIAADVRFIEATGVRTAQVY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1486 GMTDTACVV----SAQNKFTKL--GSVGYVSSNVRIKMVDldtEEALGPN--------KIGELRVKAITIMQGYHKNPET 1551
Cdd:PRK05857 318 GLSETGCTAlclpTDDGSIVKIeaGAVGRPYPGVDVYLAA---TDGIGPTapgagpsaSFGTLWIKSPANMLGYWNNPER 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1552 TKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEvdeqHPKAFV-- 1629
Cdd:PRK05857 395 TAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDE----EFGALVgl 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 1630 VQVPNKSVTEQELISYVEKNLPDYCRLRGGVK------IVDQLPRTTTGKIARKQL 1679
Cdd:PRK05857 470 AVVASAELDESAARALKHTIAARFRRESEPMArpstivIVTDIPRTQSGKVMRASL 525
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
624-1099 |
1.66e-19 |
|
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: 94.45 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 624 TGKEC--TYAEMRERSIKCALWLRKH-GIQKGDNIGILTENhlntcVP-----VLAILYIGGIICPWDHVVSKLSARYFL 695
Cdd:cd05928 36 KGDEVkwSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPR-----VPewwlvNVACIRTGLVFIPGTIQLTAKDILYRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 696 SLMSPKVVFVNEESAENLMEAAKE-ENLQVRVMVI-GSLPGFVSLANILeeqvsRAEIDGFRCTKIDNPHDLAmICSSSG 773
Cdd:cd05928 111 QASKAKCIVTSDELAPEVDSVASEcPSLKTKLLVSeKSRDGWLNFKELL-----NEASTEHHCVETGSQEPMA-IYFTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 774 TTGMPKGTELSYASLYNSITPVEEvhakneicawvptiRWHGGLNQCIEVIMSNAKWIIFSDDNIKEIALC-------EI 846
Cdd:cd05928 185 TTGSPKMAEHSHSSLGLGLKVNGR--------------YWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQgacvfvhHL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 847 IQKHGVTWLGTDTNFAI-----------LYVKMNiFQKYPMPSLRKMVITGAPFTKELHETvAKIMPHTQILQCYGLTDA 915
Cdd:cd05928 251 PRFDPLVILKTLSSYPIttfcgaptvyrMLVQQD-LSSYKFPSLQHCVTGGEPLNPEVLEK-WKAQTGLDIYEGYGQTET 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 916 GGLC-VSQAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIK-------SEFMmkGYHKNPEQTKEAFDSDGWL 987
Cdd:cd05928 329 GLICaNFKGMKIKPGSMGKASPPYDVQIIDDN-GNVLPPGTEGDIGIRvkpirpfGLFS--GYVDNPEKTAATIRGDFYL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 988 hTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQ-----KVVEKEV 1062
Cdd:cd05928 406 -TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqfLSHDPEQ 484
|
490 500 510
....*....|....*....|....*....|....*..
gi 1820754837 1063 TEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:cd05928 485 LTKELQQHVKSVTAPY-KYPRKVEFVQELPKTVTGKI 520
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
42-542 |
2.02e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 94.30 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 42 VLEKLRSRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNE 121
Cdd:PRK05857 20 VFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 122 LSPMTARYFLSLTKPKIVFVNGES---AECLAQVVKennmdtrlvvfADSAGFVGRAATLTAVLRSQDTAWIDefecakl 198
Cdd:PRK05857 100 LPIAAIERFCQITDPAAALVAPGSkmaSSAVPEALH-----------SIPVIAVDIAAVTRESEHSLDAASLA------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 199 TSPKHVA----AIVCSSGTSGFPKGT-----------EISHAAMINYMAHVKVHDLKGHVSMWTPSMRWYcglfivikaI 263
Cdd:PRK05857 162 GNADQGSedplAMIFTSGTTGEPKAVllanrtffavpDILQKEGLNWVTWVVGETTYSPLPATHIGGLWW---------I 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 264 LDCSKR--IIVPDYDDDEGLCRFIEKYEVSwfrcDSCF-PI---RLVKFGVLSKYRLPTLKILLFGGAhfkgELQQTLVK 337
Cdd:PRK05857 233 LTCLMHggLCVTGGENTTSLLEILTTNAVA----TTCLvPTllsKLVSELKSANATVPSLRLVGYGGS----RAIAADVR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 338 LLPHTDVILS--YGMTDYG--GLC------------ARQTKYSKPGSCGFVCETGRlkvVDPNTGKVLGANKTGEIWAKS 401
Cdd:PRK05857 305 FIEATGVRTAqvYGLSETGctALClptddgsivkieAGAVGRPYPGVDVYLAATDG---IGPTAPGAGPSASFGTLWIKS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 402 SYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPh 481
Cdd:PRK05857 382 PANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIP- 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 482 ninEEHAMAFV--AKVPGKEVTELDITDLVKQNMPWYCRLHAGVK------FMEKLPRTATGKIAKKQL 542
Cdd:PRK05857 460 ---DEEFGALVglAVVASAELDESAARALKHTIAARFRRESEPMArpstivIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
629-1100 |
2.22e-19 |
|
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: 93.56 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNEE 708
Cdd:cd17651 22 TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAEnlmEAAKEENLQVRVMVigslpgfvslanilEEQVSRAEIDGFRCTkidNPHDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd17651 102 LAG---ELAVELVAVTLLDQ--------------PGAAAGADAEPDPAL---DADDLAYVIYTSGSTGRPKGVVMPHRSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 YNsitpveevhakneicawvpTIRWH---GGLNQCIEVI-MSN-----AKWIIFSddnikeiALCeiiqkHGVT-WLGTD 858
Cdd:cd17651 162 AN-------------------LVAWQaraSSLGPGARTLqFAGlgfdvSVQEIFS-------TLC-----AGATlVLPPE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 859 ------TNFAILYVKMNI---FQKYPM---------------PSLRKMVITG--APFTKELHETVAKiMPHTQILQCYGL 912
Cdd:cd17651 211 evrtdpPALAAWLDEQRIsrvFLPTVAlralaehgrplgvrlAALRYLLTGGeqLVLTEDLREFCAG-LPGLRLHNHYGP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 913 TD-----AGGLCVSQAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWL 987
Cdd:cd17651 290 TEthvvtALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 988 ------HTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKE 1061
Cdd:cd17651 369 pgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAP 448
|
490 500 510
....*....|....*....|....*....|....*....
gi 1820754837 1062 VTEEELHDLVNKNLPWYCkLQAGIKFVNDFPRISTGKID 1100
Cdd:cd17651 449 VDAAELRAALATHLPEYM-VPSAFVLLDALPLTPNGKLD 486
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
815-1042 |
2.30e-19 |
|
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: 91.18 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 815 GGLNQCIEVIMSNAKWIIFSDDNIKEIAlcEIIQKHGVTWLGTdtnFA-ILYVKMNIFQKYP--MPSLRkmVITG--APf 889
Cdd:cd17637 54 AGLNLALATFHAGGANVVMEKFDPAEAL--ELIEEEKVTLMGS---FPpILSNLLDAAEKSGvdLSSLR--HVLGldAP- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 890 tkelhETVAKIMPHT--QILQCYGLTDAGGLCVSQAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMM 967
Cdd:cd17637 126 -----ETIQRFEETTgaTFWSLYGQTETSGLVTLSPYRERPGSAGRPGPLVRVRIVDDN-DRPVPAGETGEIVVRGPLVF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 968 KGYHKNPEQTKEAFDsDGWLHTKDIGYYDENGEIFFVNRisdfinyKA----IK-----LSSAEIEGVLELHPSILKAVV 1038
Cdd:cd17637 200 QGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGR-------KPekelIKpggenVYPAEVEKVILEHPAIAEVCV 271
|
....
gi 1820754837 1039 VPVP 1042
Cdd:cd17637 272 IGVP 275
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
188-548 |
2.33e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 95.38 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 188 AWIDEFECAKLTSPKHVAAIVCSSGTSGFPKGTEISHAamiNYMAHVK--------------------VHDLKGHVSMWT 247
Cdd:PRK08633 768 ARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHH---NILSNIEqisdvfnlrnddvilsslpfFHSFGLTVTLWL 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 248 PsmrwycgLFIVIKAILdcskriiVPDYDDDEGLCRFIEKYEVSWFRCDSCFpIRL-VKFGVLSKYRLPTLKILLFGGAH 326
Cdd:PRK08633 845 P-------LLEGIKVVY-------HPDPTDALGIAKLVAKHRATILLGTPTF-LRLyLRNKKLHPLMFASLRLVVAGAEK 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 327 FKGELQQTLvKLLPHTDVILSYGMTDYGGLCA------------RQTkYSKPGSCGFVCETGRLKVVDPNTGKVLGANKT 394
Cdd:PRK08633 910 LKPEVADAF-EEKFGIRILEGYGATETSPVASvnlpdvlaadfkRQT-GSKEGSVGMPLPGVAVRIVDPETFEELPPGED 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 395 GEIWAKSSYMMNGYYNNPEATRRAL---DSDGWLHTGDLGYYDNDGEVFLVDRMSEF-------INYRAIKispAEIEAL 464
Cdd:PRK08633 988 GLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFakiggemVPLGAVE---EELAKA 1064
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 465 IQQHPAVFQVAVVP---------VPHNINEEhamaFVAKVPgKEVTELDITDLVKqnmPWYCrlhagvKFMEKLPRTATG 535
Cdd:PRK08633 1065 LGGEEVVFAVTAVPdekkgeklvVLHTCGAE----DVEELK-RAIKESGLPNLWK---PSRY------FKVEALPLLGSG 1130
|
410
....*....|...
gi 1820754837 536 KIAKKQLKQIAKS 548
Cdd:PRK08633 1131 KLDLKGLKELALA 1143
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
50-542 |
3.35e-19 |
|
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: 92.76 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 50 PEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARY 129
Cdd:cd17643 1 PEAVAVVDE--DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 130 FLsltkpkivfvngesaeclaqvvkennmdtrlvvfADSagfvgRAATLtavlrsqdtawidefecakLTSPKHVAAIVC 209
Cdd:cd17643 79 IL----------------------------------ADS-----GPSLL-------------------LTDPDDLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 210 SSGTSGFPKGTEISHAAMINYMAHVkvhdlkGHVSMWTPSMRW-----YCGLFIV--IKAILDCSKRIIVPDYD---DDE 279
Cdd:cd17643 101 TSGSTGRPKGVVVSHANVLALFAAT------QRWFGFNEDDVWtlfhsYAFDFSVweIWGALLHGGRLVVVPYEvarSPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 280 GLCRFIEKYEV-------SWFRcdscfpiRLVKFGVLSKYRLPTLKILLFGG-AHFKGELQQTLVKL-LPHTDVILSYGM 350
Cdd:cd17643 175 DFARLLRDEGVtvlnqtpSAFY-------QLVEAADRDGRDPLALRYVIFGGeALEAAMLRPWAGRFgLDRPQLVNMYGI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 351 TD------YGGLCARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPE--ATRRALDSD 422
Cdd:cd17643 248 TEttvhvtFRPLDAADLPAAAASPIGRPLPGLRVYVLDAD-GRPVPPGVVGELYVSGAGVARGYLGRPEltAERFVANPF 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 423 G-----WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVpVPHNINEEHAMafVAKVPG 497
Cdd:cd17643 327 GgpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVI-VREDEPGDTRL--VAYVVA 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1820754837 498 KEVTELDITDL---VKQNMPWYCRLHAGVkFMEKLPRTATGKIAKKQL 542
Cdd:cd17643 404 DDGAAADIAELralLKELLPDYMVPARYV-PLDALPLTVNGKLDRAAL 450
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
761-1009 |
4.53e-19 |
|
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: 92.66 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 761 NPHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEE-----VHAKNEICAWVP-------------------------- 809
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrvpelLGPDDRYLAYLPlahifelaaenvclyrggtigygspr 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 810 ------TIRWHGGLNQCIEVIMSN--AKWiifsdDNIKEIALCEIIQKHGVT----WLGTDT-NFAIL------YVKMNI 870
Cdd:cd17639 166 tltdksKRGCKGDLTEFKPTLMVGvpAIW-----DTIRKGVLAKLNPMGGLKrtlfWTAYQSkLKALKegpgtpLLDELV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 871 FQKYPMPS---LRKMVITGAPFTKELHETVaKIM--PhtqILQCYGLTDA-GGLCVSQAKNSKPGSCGFVTKGIRIKIAD 944
Cdd:cd17639 241 FKKVRAALggrLRYMLSGGAPLSADTQEFL-NIVlcP---VIQGYGLTETcAGGTVQDPGDLETGRVGPPLPCCEIKLVD 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 945 EKTG--IALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISD 1009
Cdd:cd17639 317 WEEGgySTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKD 383
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
52-544 |
4.74e-19 |
|
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: 92.88 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 52 FIAQVEAVTGAET------TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNhlesyVPLLAALYLGA---------ISN 116
Cdd:cd05915 7 LFGRKEVVSRLHTgevhrtTYAEVYQRARRLMGGLRALGVGVGDRVATLGFN-----HFRHLEAYFAVpgmgavlhtANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 117 PWDNELSPMTaryfLSLTKPKIVFVNGE----SAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDtawide 192
Cdd:cd05915 82 RLSPKEIAYI----LNHAEDKVLLFDPNllplVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVP------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 193 fECAKLtspkhvaAIVCSSGTSGFPKGTEISH-AAMIN-----------------YMAHVKVHDLKGHVSMWTPSMrwYC 254
Cdd:cd05915 152 -ERAAC-------GMAYTTGTTGLPKGVVYSHrALVLHslaaslvdgtalsekdvVLPVVPMFHVNAWCLPYAATL--VG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 255 GLFIVIKAIldcskriivpdyDDDEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAhfkgELQQT 334
Cdd:cd05915 222 AKQVLPGPR------------LDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGS----AAPRS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 335 LVKL--LPHTDVILSYGMTDYGGL---CARQTKYSK-PGScgfvcETGRLK-------------VVDPNTGKVLGANKTG 395
Cdd:cd05915 286 LIARfeRMGVEVRQGYGLTETSPVvvqNFVKSHLESlSEE-----EKLTLKaktglpiplvrlrVADEEGRPVPKDGKAL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 396 EIWA-KSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQV 474
Cdd:cd05915 361 GEVQlKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEA 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 475 AVVPVPHNINEEHAMAFVaKVPGKEVTELDITDLVKQNMPWYCRLHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:cd05915 441 AVVAIPHPKWQERPLAVV-VPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
62-544 |
4.80e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 93.31 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 62 AETTFAEMTEKSVKCALWLREQ-GVQPGDIIGICTHN---HLESyvpLLAALYLGAISNPWDNELSPMTARYFLSLTKPK 137
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNcaeHLEV---LFAVACMGAVFNPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 138 IVFVNGESAECLAQVVKENNmDTRLVVFAdSAGFVGRAAT----------LTAVL--RSQDTAWIDEfecakltsPKHVA 205
Cdd:PRK05620 114 VIVADPRLAEQLGEILKECP-CVRAVVFI-GPSDADSAAAhmpegikvysYEALLdgRSTVYDWPEL--------DETTA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 206 AIVC-SSGTSGFPKGTEISHAAMINYMAHVKVHDLKG--------------HVSMW-TPSMRWYCGLFIVIkaildcskr 269
Cdd:PRK05620 184 AAICySTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAvthgesflccvpiyHVLSWgVPLAAFMSGTPLVF--------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 270 iivPDYD-DDEGLCRFIEkyevswfrcdSCFPirLVKFGVlskyrlPTLKILLFggAHF------KGELQQ--------- 333
Cdd:PRK05620 255 ---PGPDlSAPTLAKIIA----------TAMP--RVAHGV------PTLWIQLM--VHYlknppeRMSLQEiyvggsavp 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 334 -TLVKLLPH---TDVILSYGMTDYG--GLCAR-------QTKYSKPGSCGFVCETGRLKVVdpNTGKVLGAN--KTGEIW 398
Cdd:PRK05620 312 pILIKAWEErygVDVVHVWGMTETSpvGTVARppsgvsgEARWAYRVSQGRFPASLEYRIV--NDGQVMESTdrNEGEIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 399 AKSSYMMNGYYNNP----------------EATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIE 462
Cdd:PRK05620 390 VRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 463 ALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMP----WYcrLHAGVKFMEKLPRTATGKIA 538
Cdd:PRK05620 470 NYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDrlpnWM--LPEYWTFVDEIDKTSVGKFD 547
|
....*.
gi 1820754837 539 KKQLKQ 544
Cdd:PRK05620 548 KKDLRQ 553
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
50-543 |
5.81e-19 |
|
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: 92.05 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 50 PEFIAQVeaVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARY 129
Cdd:cd17649 1 PDAVALV--FGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 130 FLSltkpkivfvngesaeclaqvvkennmdtrlvvfaDSAgfvgraatlTAVLRSQDtawidefecakltsPKHVAAIVC 209
Cdd:cd17649 79 MLE----------------------------------DSG---------AGLLLTHH--------------PRQLAYVIY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 210 SSGTSGFPKGTEISHAAMINYM-AHVKVHDLK-GHVSMWTPSM-------RWYCGLFivikaildCSKRIIVPD---YDD 277
Cdd:cd17649 102 TSGSTGTPKGVAVSHGPLAAHCqATAERYGLTpGDRELQFASFnfdgaheQLLPPLI--------CGACVVLRPdelWAS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 278 DEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLP-TLKILLFGGAHFKGE-LQQTLVkllphTDVIL--SYGMTDy 353
Cdd:cd17649 174 ADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPpSLRLYIFGGEALSPElLRRWLK-----APVRLfnAYGPTE- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 354 gglcARQTKYSKPGSCGFVCETGRL---KVVDPNTGKVLGAN-------KTGEIWAKSSYMMNGYYNNPEAT--RRALDS 421
Cdd:cd17649 248 ----ATVTPLVWKCEAGAARAGASMpigRPLGGRSAYILDADlnpvpvgVTGELYIGGEGLARGYLGRPELTaeRFVPDP 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 422 DG-----WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNiNEEHAMAFVAKVP 496
Cdd:cd17649 324 FGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRA 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1820754837 497 GKEVTELDI---TDLVKQnMPWYCRLHAGVkFMEKLPRTATGKIAKKQLK 543
Cdd:cd17649 403 AAAQPELRAqlrTALRAS-LPDYMVPAHLV-FLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
41-542 |
6.14e-19 |
|
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: 91.61 E-value: 6.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 41 LVLEKLRSRPEFIAqveAVTGAE-TTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWD 119
Cdd:cd12115 4 LVEAQAARTPDAIA---LVCGDEsLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 120 NELSPMTARYFLsltkpkivfvngESAEClaqvvkennmdtRLVvfadsagfvgraatltavlrsqdtawidefecakLT 199
Cdd:cd12115 81 PAYPPERLRFIL------------EDAQA------------RLV----------------------------------LT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 200 SPKHVAAIVCSSGTSGFPKGTEISH---AAMIN-YMAHVKVHDLKGHVSmwTPSMRWYCGLFIVIkAILDCSKRII---- 271
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHrnaAAFLQwAAAAFSAEELAGVLA--STSICFDLSVFELF-GPLATGGKVVladn 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 272 VPDYDDDEGLCrfiekyEVSWFRCDSCFPIRLVKFGVLSkyrlPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYG-- 349
Cdd:cd12115 180 VLALPDLPAAA------EVTLINTVPSAAAELLRHDALP----ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGps 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 350 -MTDYGGLCARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWL--- 425
Cdd:cd12115 250 eDTTYSTVAPVPPGASGEVSIGRPLANTQAYVLDRA-LQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpga 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 426 ---HTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTE 502
Cdd:cd12115 329 rlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLV 408
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1820754837 503 LDITDLVKQNMPWYCrLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:cd12115 409 EDLRRHLGTRLPAYM-VPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1203-1615 |
6.23e-19 |
|
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: 92.87 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1203 KVQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFT 1282
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1283 VSSSAAN-LMEAAKELKMNLKVVVMDK--LDGYE-----SVEENVMKG--HDTREIIEFKCHV--TNPDDVALIVPSSGT 1350
Cdd:cd17641 90 EDEEQVDkLLEIADRIPSVRYVIYCDPrgMRKYDdprliSFEDVVALGraLDRRDPGLYEREVaaGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISHyslfcclhpyknRTLVGHTCI---VTPTMR--WHYGVL-----MAFRLVAANA--KKLIVPDNDDAENF 1418
Cdd:cd17641 170 TGKPKLAMLSH------------GNFLGHCAAylaADPLGPgdEYVSVLplpwiGEQMYSVGQAlvCGFIVNFPEEPETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1419 CQLIEKYQITWFGTDPFM---IIKFIKSQLLEKYR----------------LPTLKVILSSGAHLRKEH-------LEVM 1472
Cdd:cd17641 238 MEDLREIGPTFVLLPPRVwegIAADVRARMMDATPfkrfmfelgmklglraLDRGKRGRPVSLWLRLASwladallFRPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1473 REKL----------------PDVFITNH---------YGMTDTACVVSAQNKF-TKLGSVGYVSSNVRIKMVDldteeal 1526
Cdd:cd17641 318 RDRLgfsrlrsaatggaalgPDTFRFFHaigvplkqlYGQTELAGAYTVHRDGdVDPDTVGVPFPGTEVRIDE------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1527 gpnkIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINF-RSINVSPAEIETVLMTH 1605
Cdd:cd17641 391 ----VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFS 466
|
490
....*....|
gi 1820754837 1606 PAVLQAAVLG 1615
Cdd:cd17641 467 PYIAEAVVLG 476
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
65-480 |
7.00e-19 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 91.86 E-value: 7.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPwdneLSPMtaryflsLTKPKivfvnge 144
Cdd:PRK09029 30 TWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLP----LNPQ-------LPQPL------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 saecLAQVVKENNMDTRLVvFADSAGFVG-RAATLTAVLRSQDTAWidefecakltSPKHVAAIVCSSGTSGFPKgteis 223
Cdd:PRK09029 92 ----LEELLPSLTLDFALV-LEGENTFSAlTSLHLQLVEGAHAVAW----------QPQRLATMTLTSGSTGLPK----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 224 hAAMINYMAHVkvHDLKG--------------------HVS----MWtpsmRW-YCGLFIVIK-------AILDCSKRII 271
Cdd:PRK09029 152 -AAVHTAQAHL--ASAEGvlslmpftaqdswllslplfHVSgqgiVW----RWlYAGATLVVRdkqpleqALAGCTHASL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 272 VPDYdddegLcrfiekyevsWfrcdscfpiRLvkfgvLSKYRLP-TLKILLFGGAHFKGELQQTLVKLLPHTdvILSYGM 350
Cdd:PRK09029 225 VPTQ-----L----------W---------RL-----LDNRSEPlSLKAVLLGGAAIPVELTEQAEQQGIRC--WCGYGL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 351 TDYGG-LCARQTKySKPGsCGFVCEtGR-LKVVDpntgkvlganktGEIWAKSSYMMNGYYNNPEATRrALDSDGWLHTG 428
Cdd:PRK09029 274 TEMAStVCAKRAD-GLAG-VGSPLP-GReVKLVD------------GEIWLRGASLALGYWRQGQLVP-LVNDEGWFATR 337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 429 DLGYYdNDGEVFLVDRM-SEFI----NyraikISPAEIEALIQQHPAVFQVAVVPVP 480
Cdd:PRK09029 338 DRGEW-QNGELTILGRLdNLFFsggeG-----IQPEEIERVINQHPLVQQVFVVPVA 388
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
626-1039 |
7.55e-19 |
|
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: 92.49 E-value: 7.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 626 KECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFV 705
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 706 -NEESAENLMEAAKEENL--QV-----RVMVIGSLPGFVSLANILEE-QVSRAEIDGFRCTKID--NPHDLAMICSSSGT 774
Cdd:cd17641 90 eDEEQVDKLLEIADRIPSvrYViycdpRGMRKYDDPRLISFEDVVALgRALDRRDPGLYEREVAagKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 775 TGMPKGTELSYASLYNSIT---PVEEVHAKNEICAWVPtIRWHGglnqciEVIMSNAKWII------FSDD------NIK 839
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAaylAADPLGPGDEYVSVLP-LPWIG------EQMYSVGQALVcgfivnFPEEpetmmeDLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 840 EIA---------LCEIIQ------------------KHG--VTWLGTDTNFAILYVKMNIFQKYPM-------------- 876
Cdd:cd17641 243 EIGptfvllpprVWEGIAadvrarmmdatpfkrfmfELGmkLGLRALDRGKRGRPVSLWLRLASWLadallfrplrdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 877 -PSLRKMVITGAPFTKELHETVAKImpHTQILQCYGLTD-AGGLCVSQAKNSKPGSCGFVTKGIRIKIAdektgialgpk 954
Cdd:cd17641 323 fSRLRSAATGGAALGPDTFRFFHAI--GVPLKQLYGQTElAGAYTVHRDGDVDPDTVGVPFPGTEVRID----------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 955 ERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFIN-YKAIKLSSAEIEGVLELHPSI 1033
Cdd:cd17641 390 EVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKLKFSPYI 469
|
....*.
gi 1820754837 1034 LKAVVV 1039
Cdd:cd17641 470 AEAVVL 475
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1348-1681 |
8.00e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 92.90 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1348 SGTTGLPKGteISH----YSLFCCL-HPYknrtlV-------------------GHTCIVtptmrwhYGVLmafrlvAAN 1403
Cdd:PRK00174 254 SGSTGKPKG--VLHttggYLVYAAMtMKY-----VfdykdgdvywctadvgwvtGHSYIV-------YGPL------ANG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1404 AKKLI---VPDNDDAENFCQLIEKYQITWFGTDPFMIIKFIK--SQLLEKYRLPTLKVILSSGAHLRKE-----HLEVMR 1473
Cdd:PRK00174 314 ATTLMfegVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKKYDLSSLRLLGSVGEPINPEawewyYKVVGG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1474 EKLPdvfITNHYGMTDT-ACVVS----AQNkfTKLGSVGYVSSNVRIKMVDLDTEEaLGPNKIGELrvkAIT-----IMQ 1543
Cdd:PRK00174 394 ERCP---IVDTWWQTETgGIMITplpgATP--LKPGSATRPLPGIQPAVVDEEGNP-LEGGEGGNL---VIKdpwpgMMR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1544 GYHKNPETTKQAFDSD--GWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVD 1621
Cdd:PRK00174 465 TIYGDHERFVKTYFSTfkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIK 544
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1622 EQHPKAFVVQVPNKSVTE---QELISYVEKNL-----PDYCRlrggvkIVDQLPRTTTGKIARKQLRD 1681
Cdd:PRK00174 545 GQGIYAFVTLKGGEEPSDelrKELRNWVRKEIgpiakPDVIQ------FAPGLPKTRSGKIMRRILRK 606
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
63-465 |
9.07e-19 |
|
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: 92.10 E-value: 9.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVN 142
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 143 GESaeclaQVVKENNMDTRL-----VVFADSAGF-------VGRAATLTAVLRSQDTAWIDEFECAKL-TSPKHVAAIVC 209
Cdd:cd17641 91 DEE-----QVDKLLEIADRIpsvryVIYCDPRGMrkyddprLISFEDVVALGRALDRRDPGLYEREVAaGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 210 SSGTSGFPKGTEISHAAMINYMAHVKVHDLKG----HVSM----WTPSMRWYCGLFIVIKAILDCSK---------RIIV 272
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGpgdeYVSVlplpWIGEQMYSVGQALVCGFIVNFPEepetmmedlREIG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 273 PDY-------------------DDDEGLCRFIEK------YEV-----------SWFRCDSCFPIRLVkFGVLsKYRL-- 314
Cdd:cd17641 246 PTFvllpprvwegiaadvrarmMDATPFKRFMFElgmklgLRAldrgkrgrpvsLWLRLASWLADALL-FRPL-RDRLgf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 315 PTLKILLFGGAHFKGELQQTLVKL-LPHTDVilsYGMTDYGGL-CARQTKYSKPGSCGFvcetgrlkvvdPNTGKVLGAN 392
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFFHAIgVPLKQL---YGQTELAGAyTVHRDGDVDPDTVGV-----------PFPGTEVRID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 393 KTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSE-------------FINYRaIKISPA 459
Cdd:cd17641 390 EVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDvgttsdgtrfspqFIENK-LKFSPY 468
|
....*.
gi 1820754837 460 EIEALI 465
Cdd:cd17641 469 IAEAVV 474
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1204-1680 |
9.89e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 92.15 E-value: 9.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1204 VQTYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFT 1282
Cdd:PRK05620 38 QTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1283 VSSSAANLMEAAKELKMNLKVVVMDKLDGyeSVEENVMKGH----------DTREIIeFKCHVTNPDDVALIVPSSGTTG 1352
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPSDA--DSAAAHMPEGikvysyeallDGRSTV-YDWPELDETTAAAICYSTGTTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1353 LPKGTEISHYSLFccLHPYKNRTL----VGH----TCIVTPTMRWHYGVLMAFRLVAAnakKLIVPDND-DAENFCQLIE 1423
Cdd:PRK05620 195 APKGVVYSHRSLY--LQSLSLRTTdslaVTHgesfLCCVPIYHVLSWGVPLAAFMSGT---PLVFPGPDlSAPTLAKIIA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1424 KYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACV---------V 1494
Cdd:PRK05620 270 TAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTETSPVgtvarppsgV 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1495 SAQNKFTKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNP----------------ETTKQAFDS 1558
Cdd:PRK05620 349 SGEARWAYRVSQGRFPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1559 DGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVT 1638
Cdd:PRK05620 429 DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPT 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1820754837 1639 E---QELISYVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK05620 509 RetaERLRDQLRDRLPNW-MLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
592-1100 |
1.09e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 592 TGETHPVCANVGELVLNRLSSKPDFVGQIdaFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLA 671
Cdd:PRK12316 1995 TPEAYPRGPGVHQRIAEQAARAPEAIAVV--FGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLA 2072
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 672 ILYIGGIICPWDHVVSKLSARYFLslmspkvvfvnEESAENLMeaAKEENLQVRvmvigsLPGFVSLANILEEqvSRAEI 751
Cdd:PRK12316 2073 VLKAGGAYVPLDPNYPAERLAYML-----------EDSGAALL--LTQRHLLER------LPLPAGVARLPLD--RDAEW 2131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 752 DGFRCTKIDN---PHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEVH----AKNEIcaWVPTIRWHGGLNQCIEVI 824
Cdd:PRK12316 2132 ADYPDTAPAVqlaGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYelspADCEL--QFMSFSFDGAHEQWFHPL 2209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 825 MSNAKWIIFSDDNIKEIALCEIIQKHGVTWLGTDTNFAILYVKMNIFQKYPmPSLRKMVITGAPFTKELHETVAKIMPHT 904
Cdd:PRK12316 2210 LNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRP-PAVRVYCFGGEAVPAASLRLAWEALRPV 2288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 905 QILQCYGLTDAgGLCVSQAKNSKPGSCGFVTKGIRIKIADEKTGI------ALGPKERGEICIKSEFMMKGYHKNPEQTK 978
Cdd:PRK12316 2289 YLFNGYGPTEA-VVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYIldadlnLLAPGMAGELYLGGEGLARGYLNRPGLTA 2367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 979 EAFDSDGWLH-------TKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELpL 1051
Cdd:PRK12316 2368 ERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQL-V 2446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1820754837 1052 AFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:PRK12316 2447 AYVVPDDAAEDLLAELRAWLAARLPAY-MVPAHWVVLERLPLNPNGKLD 2494
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
344-581 |
1.16e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 91.63 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 344 VILSYGMTDYGGLCARQTKySKPGSCGFVCETgrLKVVDPNT------------GKVLGANKT-GEIWAKS-SYMMNGYY 409
Cdd:PRK13388 291 VEDGYGSSEGAVIVVREPG-TPPGSIGRGAPG--VAIYNPETltecavarfdahGALLNADEAiGELVNTAgAGFFEGYY 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 410 NNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAM 489
Cdd:PRK13388 368 NNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVM 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 490 AFVAKVPGKEVTELDIT-------DLVKQNMPWYCRLhagvkfMEKLPRTATGKIAKKQLKQIAKSYATNCCRERRIERE 562
Cdd:PRK13388 447 AALVLRDGATFDPDAFAaflaaqpDLGTKAWPRYVRI------AADLPSTATNKVLKRELIAQGWATGDPVTLWVRRGGP 520
|
250
....*....|....*....
gi 1820754837 563 TFTDiMTSSGEKANEYVPS 581
Cdd:PRK13388 521 AYRL-MSEPAKAALAAEFA 538
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-544 |
1.35e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 38 VGALVLEKLRSRPEFIAqveAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISN 116
Cdd:PRK12316 4553 VHQLVAERARMTPDAVA---VVFDEEKlTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 117 PWDNELSpmtaryflsltKPKIVFVNGESAECLaqVVKENNMDTRLVVfadsagfvgrAATLTAVLRSQDTAWID--EFE 194
Cdd:PRK12316 4630 PLDPEYP-----------RERLAYMMEDSGAAL--LLTQSHLLQRLPI----------PDGLASLALDRDEDWEGfpAHD 4686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 195 CAKLTSPKHVAAIVCSSGTSGFPKGTEISHAAMINYMA---------------HVKVHDLKGHVSMWTPSMrwYCGLFIV 259
Cdd:PRK12316 4687 PAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHatgeryeltpddrvlQFMSFSFDGSHEGLYHPL--INGASVV 4764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 260 IKAildcskriivPDYDDDEGLCRFIEKYEVSWFRCDSCFPIRLVKfGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLL 339
Cdd:PRK12316 4765 IRD----------DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE-HAERDGEPPSLRVYCFGGEAVAQASYDLAWRAL 4833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 340 PHTDVILSYGMTDYG--GLCARQTKYSKPGS----CGFVCETGRLKVVDpNTGKVLGANKTGEIWAKSSYMMNGYYNNPE 413
Cdd:PRK12316 4834 KPVYLFNGYGPTETTvtVLLWKARDGDACGAaympIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPA 4912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 414 ATRRALDSD------GWLH-TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEE 486
Cdd:PRK12316 4913 LTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQ 4992
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 487 HAMAFV----AKVPGKEV-TEL--DITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:PRK12316 4993 LVGYVVpqdpALADADEAqAELrdELKAALRERLPEY-MVPAHLVFLARMPLTPNGKLDRKALPQ 5056
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
65-542 |
1.46e-18 |
|
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: 90.81 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAECLAQVVkennMDTRLVVFADSAGFVGRAATltavlrsqdtawidefecaklTSPKHVAAIVCSSGTSGFPKGTEISH 224
Cdd:cd12116 94 LPDRLPAGL----PVLLLALAAAAAAPAAPRTP---------------------VSPDDLAYVIYTSGSTGRPKGVVVSH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AAMINYMahvkvHDLKGHVSMwTPSMRW-----YC----GLFIVIKaiLDCSKRIIVPDYD---DDEGLCRFIEKYEVSW 292
Cdd:cd12116 149 RNLVNFL-----HSMRERLGL-GPGDRLlavttYAfdisLLELLLP--LLAGARVVIAPREtqrDPEALARLIEAHSITV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 293 FRCDscfpirlvkfgvlskyrlPTL-KILLFGG----AHFK----GE-LQQTLVKLL--PHTDVILSYGMTDygglcarQ 360
Cdd:cd12116 221 MQAT------------------PATwRMLLDAGwqgrAGLTalcgGEaLPPDLAARLlsRVGSLWNLYGPTE-------T 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 361 TKYSkpgSCGFVCETG------------RLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLH-- 426
Cdd:cd12116 276 TIWS---TAARVTAAAgpipigrplantQVYVLDAA-LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpg 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 427 -----TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPhninEEHAMAFVAKVPGKEVT 501
Cdd:cd12116 352 srlyrTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRE----DGGDRRLVAYVVLKAGA 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1820754837 502 ELDITDL---VKQNMPWY---CRLHAgvkfMEKLPRTATGKIAKKQL 542
Cdd:cd12116 428 APDAAALrahLRATLPAYmvpSAFVR----LDALPLTANGKLDRKAL 470
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1338-1615 |
1.56e-18 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 91.70 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1338 PDDVALIVPSSGTTGLPKGTEISHYSLFCCLHPYKNRTLVGHTCI-------------VTPTMRWHYGVLMAFrlVAANA 1404
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVhisylplahiyerVNQIVMLHYGVAVGF--YQGDN 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1405 KKLIvpdnDDAEN-----FCQLIEKYQITWFGTDP------------FMIIKFIKSQLLEKYRLPT-------------- 1453
Cdd:PLN02736 298 LKLM----DDLAAlrptiFCSVPRLYNRIYDGITNavkesgglkerlFNAAYNAKKQALENGKNPSpmwdrlvfnkikak 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1454 ----LKVILSSGAHLRKEHLEVMREKLpDVFITNHYGMTDTACVVSAQNKFTKL-GSVGYVSSNVRIKMVDL-----DTE 1523
Cdd:PLN02736 374 lggrVRFMSSGASPLSPDVMEFLRICF-GGRVLEGYGMTETSCVISGMDEGDNLsGHVGSPNPACEVKLVDVpemnyTSE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1524 EAlgPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISD-FINFRSINVSPAEIETVL 1602
Cdd:PLN02736 453 DQ--PYPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNiFKLAQGEYIAPEKIENVY 530
|
330
....*....|...
gi 1820754837 1603 MTHPAVLQAAVLG 1615
Cdd:PLN02736 531 AKCKFVAQCFVYG 543
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
622-1100 |
2.26e-18 |
|
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: 90.12 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 622 AFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWD--HVVSKLsaRYFLslms 699
Cdd:cd17649 7 VFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDpeYPAERL--RYML---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 700 pkvvfvnEESAENLMEAAKEENLqvrvmvigslpgfvslanileeqvsraeidgfrctkidnphdlAMICSSSGTTGMPK 779
Cdd:cd17649 81 -------EDSGAGLLLTHHPRQL-------------------------------------------AYVIYTSGSTGTPK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 780 GTELSYASLYN---SITPVEEVHAKNEICAWVPtIRWHGGLNQCIEVIMSNAKWIIFSDDN-IKEIALCEIIQKHGVTWL 855
Cdd:cd17649 111 GVAVSHGPLAAhcqATAERYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPDELwASADELAEMVRELGVTVL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 856 GTDTNFAILYVK-MNIFQKYPMPSLRKMVITGAPFTKELHETVAKImpHTQILQCYGLTDA---GGLCVSQAKNSKPGS- 930
Cdd:cd17649 190 DLPPAYLQQLAEeADRTGDGRPPSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEAtvtPLVWKCEAGAARAGAs 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 931 --CGFVTKGIRIKIADEKTGiALGPKERGEICIKSEFMMKGYHKNPEQTKEAF--DSDG-----WLHTKDIGYYDENGEI 1001
Cdd:cd17649 268 mpIGRPLGGRSAYILDADLN-PVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1002 FFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELpLAFV--QKVVEKEVTEEELHDLVNKNLPWYc 1079
Cdd:cd17649 347 EYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL-VAYVvlRAAAAQPELRAQLRTALRASLPDY- 424
|
490 500
....*....|....*....|.
gi 1820754837 1080 KLQAGIKFVNDFPRISTGKID 1100
Cdd:cd17649 425 MVPAHLVFLARLPLTPNGKLD 445
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
629-1099 |
2.82e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 90.39 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGD-------NIGILTENH------------LNTCVPVLAILYIggiicpWDHVVSKl 689
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDtvavllpNIPAMVEAHfgvpmagavlntLNTRLDAASIAFM------LRHGEAK- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 690 saryflslmspkVVFVNEESAEnLMEAAKEENLQVRVMVI----GSLPGFVSLANILEEQVSRAEIDGFRCTKIDNPHDL 765
Cdd:PRK08162 118 ------------VLIVDTEFAE-VAREALALLPGPKPLVIdvddPEYPGGRFIGALDYEAFLASGDPDFAWTLPADEWDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 766 AMICSSSGTTGMPKGTELSYASLY-NSITPVEEV----HAK----------NEIC-AWvpTIRWHGGLNQCIevimsnaK 829
Cdd:PRK08162 185 IALNYTSGTTGNPKGVVYHHRGAYlNALSNILAWgmpkHPVylwtlpmfhcNGWCfPW--TVAARAGTNVCL-------R 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 830 WI----IFsddnikeialcEIIQKHGVTWLGtdtNFAILYVKMNIFQKYPMPSLRKMV---ITGAPFTKELHETVAKImp 902
Cdd:PRK08162 256 KVdpklIF-----------DLIREHGVTHYC---GAPIVLSALINAPAEWRAGIDHPVhamVAGAAPPAAVIAKMEEI-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 903 HTQILQCYGLTDAGG---LCVSQA------------KNSKPGSCGFVTKGIRIkiADEKTGIALgPKE---RGEICIKSE 964
Cdd:PRK08162 320 GFDLTHVYGLTETYGpatVCAWQPewdalplderaqLKARQGVRYPLQEGVTV--LDPDTMQPV-PADgetIGEIMFRGN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 965 FMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHE 1044
Cdd:PRK08162 397 IVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDP 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 1045 TDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFvNDFPRISTGKI 1099
Cdd:PRK08162 476 KWGEVPCAFVELKDGASATEEEIIAHCREHLAGF-KVPKAVVF-GELPKTSTGKI 528
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
629-1054 |
2.91e-18 |
|
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: 90.70 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIicpwdH--VVSKLSARyflSLMS------P 700
Cdd:cd05966 86 TYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAV-----HsvVFAGFSAE---SLADrindaqC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 701 KVVFVNEES---------AENLMEAAKEENLQVRVMVIGSLPGFVSLAN----ILEEQVSRAEIDgFRCTKIDNPHDLaM 767
Cdd:cd05966 158 KLVITADGGyrggkviplKEIVDEALEKCPSVEKVLVVKRTGGEVPMTEgrdlWWHDLMAKQSPE-CEPEWMDSEDPL-F 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 768 ICSSSGTTGMPKGTELSYAS--LYNSITP--VEEVHAkNEICAWVPTIRW---H-----GGLNQCIEVIM--------SN 827
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGGylLYAATTFkyVFDYHP-DDIYWCTADIGWitgHsyivyGPLANGATTVMfegtptypDP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 828 AKWiifsddnikeialCEIIQKHGVTWLGTD-TnfAI-LYVKM--NIFQKYPMPSLRKMVITGAPFTKE----LHETVAK 899
Cdd:cd05966 315 GRY-------------WDIVEKHKVTIFYTApT--AIrALMKFgdEWVKKHDLSSLRVLGSVGEPINPEawmwYYEVIGK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 900 imPHTQILQCYGLTDAGGLCVSQ---AKNSKPGSCGFVTKGIRIKIADEKTGIALGPKErGEICIKSEF--MMKGYHKNP 974
Cdd:cd05966 380 --ERCPIVDTWWQTETGGIMITPlpgATPLKPGSATRPFFGIEPAILDEEGNEVEGEVE-GYLVIKRPWpgMARTIYGDH 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 975 EQTKEAFDSD--GWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLA 1052
Cdd:cd05966 457 ERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYA 536
|
..
gi 1820754837 1053 FV 1054
Cdd:cd05966 537 FV 538
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
866-1100 |
3.29e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 89.84 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 866 VKMNIFQKYPMpslrKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAGGLCVSQAKNS--KPGSCGFVTKGIRIKIA 943
Cdd:PRK07638 246 YKENRVIENKM----KIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVDEESerRPNSVGRPFHNVQVRIC 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 944 DEkTGIALGPKERGEICIKSEFMMKGYhKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEI 1023
Cdd:PRK07638 322 NE-AGEEVQKGEIGTVYVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEI 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1024 EGVLELHPSILKAVVVPVPHETDIELPLAFVQkvveKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:PRK07638 400 ESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIK----GSATKQQLKSFCLQRLSSF-KIPKEWHFVDEIPYTNSGKIA 471
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
50-544 |
3.91e-18 |
|
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: 89.29 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 50 PEFIAqVEAVTGaETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSpmtary 129
Cdd:cd17653 11 PDAVA-VESLGG-SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 130 flsltkpkivfvngesaeclaqvvkennmdtrlvvfadsagfvgrAATLTAVLRSQDTAWidefeCAKLTSPKHVAAIVC 209
Cdd:cd17653 83 ---------------------------------------------SARIQAILRTSGATL-----LLTTDSPDDLAYIIF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 210 SSGTSGFPKGTEISHAAMINYMA------HVKVHDLKGHvsMWTPSMrWYCGLfiVIKAILdCSKRIIVPDyDDDEGLCR 283
Cdd:cd17653 113 TSGSTGIPKGVMVPHRGVLNYVSqpparlDVGPGSRVAQ--VLSIAF-DACIG--EIFSTL-CNGGTLVLA-DPSDPFAH 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 284 FIEKyevswfrCDScFPIRLVKFGVLSKYRLPTLKILLFGGAhfkgELQQTLVKLLPHTDVIL-SYGMTDYGGLCA-RQT 361
Cdd:cd17653 186 VART-------VDA-LMSTPSILSTLSPQDFPNLKTIFLGGE----AVPPSLLDRWSPGRRLYnAYGPTECTISSTmTEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 362 KYSKPGSCGFVCETGRLKVVDPNTGKVLgANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLH------TGDLGYYDN 435
Cdd:cd17653 254 LPGQPVTIGKPIPNSTCYILDADLQPVP-EGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 436 DGEVFLVDRMSEFINYRAIKISPAEIEA-LIQQHPAVFQVAVVPVPHNIneehaMAFVAkvPgKEVTELDITDLVKQNMP 514
Cdd:cd17653 333 DGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVVNGRL-----VAFVT--P-ETVDVDGLRSELAKHLP 404
|
490 500 510
....*....|....*....|....*....|
gi 1820754837 515 WYCRLHAGVKfMEKLPRTATGKIAKKQLKQ 544
Cdd:cd17653 405 SYAVPDRIIA-LDSFPLTANGKVDRKALRE 433
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1521-1683 |
5.00e-18 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 90.06 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1521 DTEEALGPNKIGELRVKAITIMQGYHKNPETTKqAFDSDGWLRTGDLAYYDDnGEIYIVDRISDFINFRSINVSPAEIET 1600
Cdd:PRK09192 401 EAGMPLPERVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIEW 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1601 VLMTHPAVLQ--AAVLGIPNEVDEqhpkAFVVQVPNKSVTEQELISYVEKnLPDYCRLRGGVKIVDQL------PRTTTG 1672
Cdd:PRK09192 479 IAEQEPELRSgdAAAFSIAQENGE----KIVLLVQCRISDEERRGQLIHA-LAALVRSEFGVEAAVELvpphslPRTSSG 553
|
170
....*....|.
gi 1820754837 1673 KIARKQLRDMY 1683
Cdd:PRK09192 554 KLSRAKAKKRY 564
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
629-1007 |
8.34e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 89.65 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTEnhlnTCVPVLAILYigGIicpWDH--VVSKLSA-------RYFLSLMS 699
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEE----TRWEWLASIY--GI---WSQsmVAATVYAnlgedalAYALRETE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 700 PKVVFVNEESAENLMEAAKEENL-QVRVMVIGSLPGFVSLAN---ILEEQV---SRAEIDGFRCTKIDNPHDLAMICSSS 772
Cdd:PTZ00216 194 CKAIVCNGKNVPNLLRLMKSGGMpNTTIIYLDSLPASVDTEGcrlVAWTDVvakGHSAGSHHPLNIPENNDDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 773 GTTGMPKGTELSYASLYNSITPVEE-------VHAKNEI-CAWVPTIrwHgglnqcievIMsnakwiifsddnikEIALC 844
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALEDrlndligPPEEDETyCSYLPLA--H---------IM--------------EFGVT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 845 EIIQKHGVtWLG-------TDTnFAILY--------------------VKMNIFQKYPMP-SLRKMVITGA--------- 887
Cdd:PTZ00216 329 NIFLARGA-LIGfgsprtlTDT-FARPHgdltefrpvfligvprifdtIKKAVEAKLPPVgSLKRRVFDHAyqsrlralk 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 888 -----PFTKELHETVAKIM----------------PHTQ---------ILQCYGLTDA---GGlcVSQAKNSKPGSCGFV 934
Cdd:PTZ00216 407 egkdtPYWNEKVFSAPRAVlggrvramlsgggplsAATQefvnvvfgmVIQGWGLTETvccGG--IQRTGDLEPNAVGQL 484
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 935 TKGIRIKIAD-EKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRI 1007
Cdd:PTZ00216 485 LKGVEMKLLDtEEYKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRV 558
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
629-1006 |
8.98e-18 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 89.39 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNEE 708
Cdd:PLN02736 80 TYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAENLMEAAKEENLQVRVMVIG-------SLPG-----FVSLANILEEqvSRAEIDGFRCTKidnPHDLAMICSSSGTTG 776
Cdd:PLN02736 160 TLNTLLSCLSEIPSVRLIVVVGgadeplpSLPSgtgveIVTYSKLLAQ--GRSSPQPFRPPK---PEDVATICYTSGTTG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 777 MPKGTELSYASL----------------------------YNSITPVEEVHA---------------------KNEICAW 807
Cdd:PLN02736 235 TPKGVVLTHGNLianvagsslstkfypsdvhisylplahiYERVNQIVMLHYgvavgfyqgdnlklmddlaalRPTIFCS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 808 VP------------TIRWHGGLNQCIEVIMSNAKwiifsddnikeialceiiqKHGvtwLGTDTNFAILYVKMnIFQKYP 875
Cdd:PLN02736 315 VPrlynriydgitnAVKESGGLKERLFNAAYNAK-------------------KQA---LENGKNPSPMWDRL-VFNKIK 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 876 MP---SLRKMVITGAPFTKELHETVaKIMPHTQILQCYGLTDAGglCVSQAKNSKPGSCGFV---TKGIRIKIAD----E 945
Cdd:PLN02736 372 AKlggRVRFMSSGASPLSPDVMEFL-RICFGGRVLEGYGMTETS--CVISGMDEGDNLSGHVgspNPACEVKLVDvpemN 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 946 KTGiALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNR 1006
Cdd:PLN02736 449 YTS-EDQPYPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
38-542 |
1.02e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.22 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 38 VGALVLEKLRSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNP 117
Cdd:PRK12467 1576 VHQLIEDQAAATPEAVALVFG--EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 118 WDNELSPMTARYFLSLTKPKIVFVNGESAECLAQvvkennmdtrlvvfadsagfvgrAATLTAVLRSQDTAWID---EFE 194
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLTQSHLQARLPL-----------------------PDGLRSLVLDQEDDWLEgysDSN 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 195 CAKLTSPKHVAAIVCSSGTSGFPKGTEISHAAMIN---YMAH----------VKVHDLKGHVSMWtpsmrwycGLFiviK 261
Cdd:PRK12467 1711 PAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNrlcATQEayqlsaadvvLQFTSFAFDVSVW--------ELF---W 1779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 262 AILDCSKRIIVPD--YDDDEGLCRFIEKYEVSWFrcdSCFPIRLVKF--GVLSKYRLPTLKILLFGGAHFKGELQQTLVK 337
Cdd:PRK12467 1780 PLINGARLVIAPPgaHRDPEQLIQLIERQQVTTL---HFVPSMLQQLlqMDEQVEHPLSLRRVVCGGEALEVEALRPWLE 1856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 338 LLPHTDVILSYGMTDygglCARQTKYSKpgsCGFVCETGRLKV-----VDPNTGKVLGANKT-------GEIWAKSSYMM 405
Cdd:PRK12467 1857 RLPDTGLFNLYGPTE----TAVDVTHWT---CRRKDLEGRDSVpigqpIANLSTYILDASLNpvpigvaGELYLGGVGLA 1929
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 406 NGYYNNPE--ATRRALDSDGWL-----HTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVP 478
Cdd:PRK12467 1930 RGYLNRPAltAERFVADPFGTVgsrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA 2009
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 479 VpHNINEEHAMAFVakVP-GKEVTELD---------ITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:PRK12467 2010 Q-DGANGKQLVAYV--VPtDPGLVDDDeaqvalraiLKNHLKASLPEY-MVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1485-1685 |
1.06e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 88.13 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVVSA--QNKFTKLG-SVGYVSSNVRIKmvdldteeaLGPNKIGELRVKAITIMQGYHknPettkQAFDSDGW 1561
Cdd:PRK07445 261 YGMTETASQIATlkPDDFLAGNnSSGQVLPHAQIT---------IPANQTGNITIQAQSLALGYY--P----QILDSQGI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1562 LRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPnevDEQHPKAFV-VQVPNKSVTEQ 1640
Cdd:PRK07445 326 FETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLP---DPHWGEVVTaIYVPKDPSISL 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1641 ELI-SYVEKNLPDYcrlrggvKI------VDQLPRTTTGKIARKQLRDMYVN 1685
Cdd:PRK07445 403 EELkTAIKDQLSPF-------KQpkhwipVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
629-1054 |
1.97e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 87.74 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGgiICP----WDHVVSKLSAryFLSLMSPKVVF 704
Cdd:PRK10946 50 SYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPvnalFSHQRSELNA--YASQIEPALLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 705 VNEESA----ENLMEAAKEENLQVRVMVIGSLPGFVSLANILEEqvsraEIDGFRCTKidNPHD-LAMICSSSGTTGMPK 779
Cdd:PRK10946 126 ADRQHAlfsdDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINH-----PAEDFTATP--SPADeVAFFQLSGGSTGTPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 780 GTELSYASLYNSitpveeVHAKNEICAWVPTIRW-------H-------GGLNqcieVIMSNAKWIIFSDdniKEIALC- 844
Cdd:PRK10946 199 LIPRTHNDYYYS------VRRSVEICGFTPQTRYlcalpaaHnypmsspGALG----VFLAGGTVVLAPD---PSATLCf 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 845 EIIQKHGVT-----------WLGTDTNFAilyvkmnifQKYPMPSLRKMVITGAPFTkelhETVAKIMPHT---QILQCY 910
Cdd:PRK10946 266 PLIEKHQVNvtalvppavslWLQAIAEGG---------SRAQLASLKLLQVGGARLS----ETLARRIPAElgcQLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 911 GLtdAGGLcVSQAKNSKPGSCGFVTKGI------RIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSD 984
Cdd:PRK10946 333 GM--AEGL-VNYTRLDDSDERIFTTQGRpmspddEVWVADAD-GNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 985 GWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFL 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1184-1680 |
2.16e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.46 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1184 LKFLKSKPDSigqvdaltGKVQTYADMSERSIKCALWLKKQGVkPGDIIGLCSDNNLDVFLILLGTMYIGAI-------- 1255
Cdd:PRK05691 28 LRFLADDPGE--------GVVLSYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVAAFFGCLYAGVIavpayppe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1256 SNTWDHEltpmtaRNFLTLTS---PKIVFTVSSSAANLMEAAKELKMNL-KVVVMDKLDgyeSVEENVMKGHDTReiief 1331
Cdd:PRK05691 99 SARRHHQ------ERLLSIIAdaePRLLLTVADLRDSLLQMEELAAANApELLCVDTLD---PALAEAWQEPALQ----- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1332 kchvtnPDDVALIVPSSGTTGLPKGTEISHYSLFC-----------CLHP----------YKNRTLVGHtcIVTPTMRWH 1390
Cdd:PRK05691 165 ------PDDIAFLQYTSGSTALPKGVQVSHGNLVAneqlirhgfgiDLNPddvivswlplYHDMGLIGG--LLQPIFSGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1391 YGVLMAFRLVAANAKKLIvpdnddaenfcQLIEKYQITWFGTDPF---MIIKFIKSQLLEKYRLPTLKVILSSGAHLRKE 1467
Cdd:PRK05691 237 PCVLMSPAYFLERPLRWL-----------EAISEYGGTISGGPDFayrLCSERVSESALERLDLSRWRVAYSGSEPIRQD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1468 HLEVMREKL------PDVFITNhYGMTDTACVVS------------------AQNKF-----TKLGSVGYVSSNVRIKMV 1518
Cdd:PRK05691 306 SLERFAEKFaacgfdPDSFFAS-YGLAEATLFVSggrrgqgipaleldaealARNRAepgtgSVLMSCGRSQPGHAVLIV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1519 DLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAF---DSDGWLRTGDLAYYDDnGEIYIVDRISDFINFRSINVSP 1595
Cdd:PRK05691 385 DPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1596 AEIETVLMTHPAVLQA------AV-------LGIPNEVDEQhpkafvVQvpnKSVTEQELISYVEKNLPDYCRLRGGVKI 1662
Cdd:PRK05691 464 QDIEKTVEREVEVVRKgrvaafAVnhqgeegIGIAAEISRS------VQ---KILPPQALIKSIRQAVAEACQEAPSVVL 534
|
570 580
....*....|....*....|.
gi 1820754837 1663 V---DQLPRTTTGKIARKQLR 1680
Cdd:PRK05691 535 LlnpGALPKTSSGKLQRSACR 555
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
627-1054 |
3.06e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 87.53 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 627 ECTYAEMRERSIKCALWLRKH-GIQKGDNIGILTEN---HLNTcvpVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:PRK05620 38 QTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNcaeHLEV---LFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNEESAENLMEAAKEENLQVRVMVIGSLPgFVSLANILEEQVS----RAEIDGfRCTKIDNP----HDLAMICSSSGT 774
Cdd:PRK05620 115 IVADPRLAEQLGEILKECPCVRAVVFIGPSD-ADSAAAHMPEGIKvysyEALLDG-RSTVYDWPeldeTTAAAICYSTGT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 775 TGMPKGTELSYASLY------NSITPVEEVHAKNEICAwVPTirWHGgLNQCIEV--IMSNAKwIIFSDDNIKEIALCEI 846
Cdd:PRK05620 193 TGAPKGVVYSHRSLYlqslslRTTDSLAVTHGESFLCC-VPI--YHV-LSWGVPLaaFMSGTP-LVFPGPDLSAPTLAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 847 I------QKHGVT--WLGtdtnfaiLYVkmNIFQKYP--MpSLRKMVITGAPFTKELhETVAKIMPHTQILQCYGLTDAG 916
Cdd:PRK05620 268 IatamprVAHGVPtlWIQ-------LMV--HYLKNPPerM-SLQEIYVGGSAVPPIL-IKAWEERYGVDVVHVWGMTETS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 917 GL-CVS--------QAKNSKPGSCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQT---------- 977
Cdd:PRK05620 337 PVgTVArppsgvsgEARWAYRVSQGRFPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrg 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 978 ------KEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPL 1051
Cdd:PRK05620 417 edvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPL 496
|
...
gi 1820754837 1052 AFV 1054
Cdd:PRK05620 497 AVT 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
368-537 |
3.23e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 88.69 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 368 SCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRA---LDSDGWLHTGDLGYYdNDGEVFLVDR 444
Cdd:PRK05691 371 SCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLGFL-RDGELFVTGR 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 445 MSEFINYRAIKISPAEIEALIQQHPAVF---QVAVVPVPHNINEEHAMAF-VAKVPGKEVTELDITDLVKQNMPWYCR-- 518
Cdd:PRK05691 450 LKDMLIVRGHNLYPQDIEKTVEREVEVVrkgRVAAFAVNHQGEEGIGIAAeISRSVQKILPPQALIKSIRQAVAEACQea 529
|
170 180
....*....|....*....|....*
gi 1820754837 519 ------LHAGVkfmekLPRTATGKI 537
Cdd:PRK05691 530 psvvllLNPGA-----LPKTSSGKL 549
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
172-480 |
4.15e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 86.88 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 172 VGR-----AATLTAVLRSQDTAwidEFECAKLTsPKHVAAIVCSSGTSGFPKGTEISH---AAMInymAHVKVH--DLKG 241
Cdd:PRK09274 143 VGGrllwgGTTLATLLRDGAAA---PFPMADLA-PDDMAAILFTSGSTGTPKGVVYTHgmfEAQI---EALREDygIEPG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 242 HVSMWT-PSMrwycGLFIvikaiLDCSKRIIVPDYD-------DDEGLCRFIEKYEVSwfrCDSCFPI---RLVKFGVLS 310
Cdd:PRK09274 216 EIDLPTfPLF----ALFG-----PALGMTSVIPDMDptrpatvDPAKLFAAIERYGVT---NLFGSPAlleRLGRYGEAN 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 311 KYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVIL-SYG---------------------MTDYGGlcarqtkyskpGS 368
Cdd:PRK09274 284 GIKLPSLRRVISAGAPVPIAVIERFRAMLPPDAEILtPYGatealpissiesreilfatraATDNGA-----------GI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 369 C-GFVCETGRLKVVDPNTG--------KVLGANKTGEIWAKSSYMMNGYYNNPEATRRA--LDSDG--WLHTGDLGYYDN 435
Cdd:PRK09274 353 CvGRPVDGVEVRIIAISDApipewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDA 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1820754837 436 DGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVP 480
Cdd:PRK09274 433 QGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
886-1011 |
5.64e-17 |
|
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: 86.64 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 886 GAPFTKELHETVAKImpHTQILQCYGLTDAGGL-CVSQAKNSKPGSCGFVTKGIRIKIADE-KTGIalgpkerGEICIKS 963
Cdd:cd05933 329 AAPISRETLEFFLSL--NIPIMELYGMSETSGPhTISNPQAYRLLSCGKALPGCKTKIHNPdADGI-------GEICFWG 399
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1820754837 964 EFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFI 1011
Cdd:cd05933 400 RHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELI 447
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
878-1100 |
5.71e-17 |
|
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: 84.45 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 878 SLRKMVITGAPFTKELhetVAKIMPHT--QILQCYGLTDAGGL--CVSQAKNSKPGSCG--FVTKGIRIKIADEKTGIAL 951
Cdd:cd05944 122 SLRFAMSGAAPLPVEL---RARFEDATglPVVEGYGLTEATCLvaVNPPDGPKRPGSVGlrLPYARVRIKVLDGVGRLLR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 952 --GPKERGEICIKSEFMMKGYhKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLEL 1029
Cdd:cd05944 199 dcAPDEVGEICVAGPGVFGGY-LYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLR 277
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1030 HPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYCKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd05944 278 HPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARDHVPERAAVPKHIEVLEELPVTAVGKVF 348
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
614-1099 |
6.81e-17 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 85.97 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 614 PDFVGQIDAFtgKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARY 693
Cdd:PRK13382 57 PDRPGLIDEL--GTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 694 FLSLMSPKVVFVNEESAENLMEAAKEENLQVRVMVIGSLPGFVSLANILEEQVSRAEIDGFRCTKIdnphdlamICSSSG 773
Cdd:PRK13382 135 VVTREGVDTVIYDEEFSATVDRALADCPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRV--------ILLTSG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 774 TTGMPKGTELSYASlynSITPVEEVHAKNEICAWVPTI----RWHG-GLNQcIEVIMSNAKWIIFSDDNIKEIALcEIIQ 848
Cdd:PRK13382 207 TTGTPKGARRSGPG---GIGTLKAILDRTPWRAEEPTVivapMFHAwGFSQ-LVLAASLACTIVTRRRFDPEATL-DLID 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 849 KHGVTWLG-TDTNF-AILYVKMNIFQKYPMPSLRKMVITGAPFTKELhetVAKIMPH--TQILQCYGLTDAGGLCVSQAK 924
Cdd:PRK13382 282 RHRATGLAvVPVMFdRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDV---VIAFMDQfgDVIYNNYNATEAGMIATATPA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 925 N--SKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYhkNPEQTKEAFDsdGWLHTKDIGYYDENGEIF 1002
Cdd:PRK13382 359 DlrAAPDTAGRPAEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVGYLDENGRLF 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1003 FVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQ 1082
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANY-KVP 512
|
490
....*....|....*..
gi 1820754837 1083 AGIKFVNDFPRISTGKI 1099
Cdd:PRK13382 513 RDIVVLDELPRGATGKI 529
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
201-468 |
6.83e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 86.02 E-value: 6.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 201 PKHVAAIVCSSGTSGFPKGTEISHAAMI-NYMAHVKVHDLKGHVSM--WTPSMRWY----CGLFIVIKAILdcskriIVP 273
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLaNQRACLKFFSPKEDDVMmsFLPPFHAYgfnsCTLFPLLSGVP------VVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 274 DYD--DDEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMT 351
Cdd:PRK06334 256 AYNplYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 352 DYGGLCARQTKYS-KPGSC-GFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYY-NNPEATRRALDSDGWLHTG 428
Cdd:PRK06334 336 ECSPVITINTVNSpKHESCvGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTG 415
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1820754837 429 DLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQH 468
Cdd:PRK06334 416 DLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1337-1619 |
6.95e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 86.02 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1337 NPDDVALIVPSSGTTGLPKGTEISHYSL-------FCCLHPYKNRTLVG----------HTCIVTPTMRwhyGVLMAFRL 1399
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLlanqracLKFFSPKEDDVMMSflppfhaygfNSCTLFPLLS---GVPVVFAY 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1400 VAANAKKLIvpdnddaenfcQLIEKYQITWFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDV 1479
Cdd:PRK06334 258 NPLYPKKIV-----------EMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1480 FITNHYGMTDTACVVSAQNKFT--KLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETtkQAF- 1556
Cdd:PRK06334 327 QLRQGYGTTECSPVITINTVNSpkHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFG--QGFv 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1557 --DSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTH------PAVLQAAVLGIPNE 1619
Cdd:PRK06334 405 elGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqnaaDHAGPLVVCGLPGE 475
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1195-1599 |
7.26e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 86.20 E-value: 7.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1195 GQVDALTGkvQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAiSNTWDHELTPM-------- 1266
Cdd:PRK07768 22 GEPDAPVR--HTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGA-SLTMLHQPTPRtdlavwae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1267 -TARNFLTLTSPKIVFtvsssAANLMEAAKEL-KMNLKVVVMDKLDGYESVEenvmkghdtreIIEfkchvTNPDDVALI 1344
Cdd:PRK07768 99 dTLRVIGMIGAKAVVV-----GEPFLAAAPVLeEKGIRVLTVADLLAADPID-----------PVE-----TGEDDLALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1345 VPSSGTTGLPKGTEISHYSLFCCLHPYKNRtlVGHTCIVTPTMRW----HYGVLMAFrlvaanakkLIVPDNDDAENFC- 1419
Cdd:PRK07768 158 QLTSGSTGSPKAVQITHGNLYANAEAMFVA--AEFDVETDVMVSWlplfHDMGMVGF---------LTVPMYFGAELVKv 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1420 -------------QLIEKYQITWFGTDPF---MIIKFIKSQLLEK-YRLPTLKVILSSGAHLRKEHLEVM-----REKLP 1477
Cdd:PRK07768 227 tpmdflrdpllwaELISKYRGTMTAAPNFayaLLARRLRRQAKPGaFDLSSLRFALNGAEPIDPADVEDLldagaRFGLR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1478 DVFITNHYGMTDTACVVS-------------------AQNKFT--------KLGSVGYVSSNVRIKMVDLDTEeALGPNK 1530
Cdd:PRK07768 307 PEAILPAYGMAEATLAVSfspcgaglvvdevdadllaALRRAVpatkgntrRLATLGPPLPGLEVRVVDEDGQ-VLPPRG 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 1531 IGELRVKAITIMQGYhKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIE 1599
Cdd:PRK07768 386 VGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
629-1055 |
9.00e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 86.16 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENhlntcVPVLAILYIG----GIICPwdhVVSKLSARYFLSLM---SPK 701
Cdd:PRK07529 60 TYAELLADVTRTANLLHSLGVGPGDVVAFLLPN-----LPETHFALWGgeaaGIANP---INPLLEPEQIAELLraaGAK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 702 VV-----FVNEESAENLMEAAKE-ENLQ--VRVMVIGSLPGFVSLANILEEQVSR-------AEIDGFRCTKID-----N 761
Cdd:PRK07529 132 VLvtlgpFPGTDIWQKVAEVLAAlPELRtvVEVDLARYLPGPKRLAVPLIRRKAHarildfdAELARQPGDRLFsgrpiG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 762 PHDLAMICSSSGTTGMPKGTELSYASL-YN---SITPVEEVHAKNEICAwVPTIRWHGGLNQCIEVIMSNAKWII----- 832
Cdd:PRK07529 212 PDDVAAYFHTGGTTGMPKLAQHTHGNEvANawlGALLLGLGPGDTVFCG-LPLFHVNALLVTGLAPLARGAHVVLatpqg 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 833 FSDDN-IKEIalCEIIQKHGVTWLGT-DTNFAILyvkMNIfqkypmP-------SLRkMVITG-APFTKELHEtvaKIMP 902
Cdd:PRK07529 291 YRGPGvIANF--WKIVERYRINFLSGvPTVYAAL---LQV------PvdghdisSLR-YALCGaAPLPVEVFR---RFEA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 903 HT--QILQCYGLTDAGglCVSqAKN-----SKPGSCG--FVTKGIRIKIADEKTGIA--LGPKERGEICIKSEFMMKGYh 971
Cdd:PRK07529 356 ATgvRIVEGYGLTEAT--CVS-SVNppdgeRRIGSVGlrLPYQRVRVVILDDAGRYLrdCAVDEVGVLCIAGPNVFSGY- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 972 KNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFInykaIK----LSSAEIEGVLELHPSILKAVVVPVPHETDI 1047
Cdd:PRK07529 432 LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI----IRgghnIDPAAIEEALLRHPAVALAAAVGRPDAHAG 507
|
....*...
gi 1820754837 1048 ELPLAFVQ 1055
Cdd:PRK07529 508 ELPVAYVQ 515
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1206-1679 |
1.03e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.15 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELtPMTARNFLTLTSPKIVFTVSS 1285
Cdd:PRK05691 1158 DYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDY-PAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAANLMEAAKelkmNLKVVVMD--KLDGYESvEENVMKGHDtreiiefkchvtnpDDVALIVPSSGTTGLPKGTEISHYS 1363
Cdd:PRK05691 1237 HLLERLPQAE----GVSAIALDslHLDSWPS-QAPGLHLHG--------------DNLAYVIYTSGSTGQPKGVGNTHAA 1297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1364 LFCCLH----PYK---NRTLVGHTCIVTPTMRWH--YGVLMAFRLVAANakkliVPDNDDAENFCQLIEKYQITWFGTDP 1434
Cdd:PRK05691 1298 LAERLQwmqaTYAlddSDVLMQKAPISFDVSVWEcfWPLITGCRLVLAG-----PGEHRDPQRIAELVQQYGVTTLHFVP 1372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1435 FMIIKFIKSQLLEKYRlpTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVVS---AQNKFTKLGSVGYVSS 1511
Cdd:PRK05691 1373 PLLQLFIDEPLAAACT--SLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVThwqCQAEDGERSPIGRPLG 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1512 NVRIKMvdLDTEEALGPNKI-GELRVKAITIMQGYHKNPETTKQAF--DSDG-----WLRTGDLAYYDDNGEIYIVDRIS 1583
Cdd:PRK05691 1451 NVLCRV--LDAELNLLPPGVaGELCIGGAGLARGYLGRPALTAERFvpDPLGedgarLYRTGDRARWNADGALEYLGRLD 1528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1584 DFINFRSINVSPAEIETVLMTHPAVLQAAVLgIPNEVDEQHPKAFVVQVPNKSVTEQELISYVEKNLPDY------CRLr 1657
Cdd:PRK05691 1529 QQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYmvpaqlIRL- 1606
|
490 500
....*....|....*....|..
gi 1820754837 1658 ggvkivDQLPRTTTGKIARKQL 1679
Cdd:PRK05691 1607 ------DQMPLGPSGKLDRRAL 1622
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
65-542 |
1.04e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 85.43 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAisnpwdnelspmtaryflsltkpKIVFVNGE 144
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGA-----------------------DVVPISTE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 -SAECLAQVVKENNMDTrlvVFADSAgFVGRAATLTAVLRSQDTAWIDEFECA---KLTSPKHVaaIVCSSGTSGFPKGt 220
Cdd:PRK13383 119 fRSDALAAALRAHHIST---VVADNE-FAERIAGADDAVAVIDPATAGAEESGgrpAVAAPGRI--VLLTSGTTGKPKG- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 221 eISHAAMINYMAHVKVHDLK-------GHVSMWTPsMRWYCGLFIVIKAILDCSKRIIVPDYDDDEGLCrfiekyEVSWF 293
Cdd:PRK13383 192 -VPRAPQLRSAVGVWVTILDrtrlrtgSRISVAMP-MFHGLGLGMLMLTIALGGTVLTHRHFDAEAALA------QASLH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 294 RCD--SCFPIRLVKF-----GVLSKYRLPTLKILLFGGAHFKGELQQTLVKllPHTDVILS-YGMTDYG--GLCARQTKY 363
Cdd:PRK13383 264 RADafTAVPVVLARIlelppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMD--TYGDILYNgYGSTEVGigALATPADLR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 364 SKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYynnPEATRRALdSDGWLHTGDLGYYDNDGEVFLVD 443
Cdd:PRK13383 342 DAPETVGKPVAGCPVRILDRN-NRPVGPRVTGRIFVGGELAGTRY---TDGGGKAV-VDGMTSTGDMGYLDNAGRLFIVG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 444 RMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYCRLHaGV 523
Cdd:PRK13383 417 REDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPR-DI 495
|
490
....*....|....*....
gi 1820754837 524 KFMEKLPRTATGKIAKKQL 542
Cdd:PRK13383 496 NIVSSIPRNPTGKVLRKEL 514
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
358-544 |
1.26e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.44 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 358 ARQTKYSKPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNNPEATRrALDSDGWLHTGDLGYYdNDG 437
Cdd:PRK09192 376 AETRRVRTFVNCGKALPGHEIEIRNEA-GMPLPERVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLGYL-LDG 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 438 EVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQ--VAVVPVPhNINEEHAMAFVAKVPGKEVTELDITDLVKQnmpw 515
Cdd:PRK09192 453 YLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdAAAFSIA-QENGEKIVLLVQCRISDEERRGQLIHALAA---- 527
|
170 180 190
....*....|....*....|....*....|....*
gi 1820754837 516 YCRLHAGVKFMEKL------PRTATGKIAKKQLKQ 544
Cdd:PRK09192 528 LVRSEFGVEAAVELvpphslPRTSSGKLSRAKAKK 562
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
198-542 |
1.49e-16 |
|
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: 84.37 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 198 LTSPKHVAAIVCSSGTSGFPKGTEISHAAMINYMAHV-KVHDLKGHVSMWTPSMRWYCGLFIV---IKAILDCSKRIIVP 273
Cdd:cd17648 90 ITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLsERYFGRDNGDEAVLFFSNYVFDFFVeqmTLALLNGQKLVVPP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 274 DYD--DDEGLCRFIEKYEVSWFrcdSCFPirlvkfGVLSKY---RLPTLKILLFGG-----AHFKgELQQTLVKLlphtd 343
Cdd:cd17648 170 DEMrfDPDRFYAYINREKVTYL---SGTP------SVLQQYdlaRLPHLKRVDAAGeeftaPVFE-KLRSRFAGL----- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 344 VILSYGMTDyGGLCARQTKYSKPG----SCGFVCETGRLKVVDPNTgKVLGANKTGEIWAKSSYMMNGYYNNPEATR--- 416
Cdd:cd17648 235 IINAYGPTE-TTVTNHKRFFPGDQrfdkSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTAerf 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 417 ----------RALDSDGWLH-TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNIN- 484
Cdd:cd17648 313 lpnpfqteqeRARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQa 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 485 ----EEHAMAFVAKVPGkEVTELDITDLVKQNMPWY---CRLHAgvkfMEKLPRTATGKIAKKQL 542
Cdd:cd17648 393 qsriQKYLVGYYLPEPG-HVPESDLLSFLRAKLPRYmvpARLVR----LEGIPVTINGKLDVRAL 452
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
628-1055 |
2.14e-16 |
|
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: 84.60 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 628 CTYAEMRERSIKCALWLRKHGiQKGDNIGILTENHLNTCVPVLAILYIGGIICP------------WDHVVSKLSARyfl 695
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPlppptpgrhaerLAAILADAGPR--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 696 slmspkVVFVNEESAENLMEAAKeenlqvrvmvigSLPGFVSLANILEEQVSRAEIDGFRCTKIDnPHDLAMICSSSGTT 775
Cdd:cd05931 101 ------VVLTTAAALAAVRAFAA------------SRPAAGTPRLLVVDLLPDTSAADWPPPSPD-PDDIAYLQYTSGST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 776 GMPKGTELSYASLYN---SITPVEEVHAKNEICAWVPTirWH-----GGL-----NQCIEVIMSNA-------KWIifsd 835
Cdd:cd05931 162 GTPKGVVVTHRNLLAnvrQIRRAYGLDPGDVVVSWLPL--YHdmgliGGLltplySGGPSVLMSPAaflrrplRWL---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 836 dnikeialcEIIQKHGVTWLGTdTNFAILYV--KMNIFQKYP-----------------MPSLRKMVITGAPFTkelhet 896
Cdd:cd05931 236 ---------RLISRYRATISAA-PNFAYDLCvrRVRDEDLEGldlsswrvalngaepvrPATLRRFAEAFAPFG------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 897 vakiMPHTQILQCYGL----------TDAGGLCVSQ-------------AKNSKPG----SCGFVTKGIRIKIADEKTGI 949
Cdd:cd05931 300 ----FRPEAFRPSYGLaeatlfvsggPPGTGPVVLRvdrdalagravavAADDPAArelvSCGRPLPDQEVRIVDPETGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 950 ALGPKERGEICIKSEFMMKGYHKNPEQTKEAF------DSDGWLHTKDIGYYDEnGEIFFVNRISDFI-----NYkaikl 1018
Cdd:cd05931 376 ELPDGEVGEIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRTGDLGFLHD-GELYITGRLKDLIivrgrNH----- 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 1820754837 1019 SSAEIE-GVLELHPSILKAVVVPVPHETDIELPLAFVQ 1055
Cdd:cd05931 450 YPQDIEaTAEEAHPALRPGCVAAFSVPDDGEERLVVVA 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
622-1049 |
2.22e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.98 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 622 AFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPK 701
Cdd:PRK12467 532 VFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVR 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 702 VVFVNEESAENLMEAAKeenlqVRVMVIgslpgfvslaNILEEQVS-RAEIdgFRCTKIDnPHDLAMICSSSGTTGMPKG 780
Cdd:PRK12467 612 LLLTQSHLLAQLPVPAG-----LRSLCL----------DEPADLLCgYSGH--NPEVALD-PDNLAYVIYTSGSTGQPKG 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 781 TELSYASLYNSITPVEEVH--AKNEICAWVPTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEI-ALCEIIQKHGVTWLGT 857
Cdd:PRK12467 674 VAISHGALANYVCVIAERLqlAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAeAFAALMADQGVTVLKI 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 858 DTnfAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAG-----GLCVSQAKNSKPGSCG 932
Cdd:PRK12467 754 VP--SHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTvgvstYELSDEERDFGNVPIG 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 933 FVTKGIRIKIADEKTGIALGPKeRGEICIKSEFMMKGYHKNPEQTKEAFDSD------GWLH-TKDIGYYDENGEIFFVN 1005
Cdd:PRK12467 832 QPLANLGLYILDHYLNPVPVGV-VGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLG 910
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1820754837 1006 RISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIEL 1049
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQL 954
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
939-1054 |
2.23e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 84.51 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 939 RIKIADEKTG--IALGPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAI 1016
Cdd:PLN02479 383 GLDVVDTKTMkpVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGE 461
|
90 100 110
....*....|....*....|....*....|....*...
gi 1820754837 1017 KLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:PLN02479 462 NISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFV 499
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
546-1041 |
2.33e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.78 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 546 AKSYATNCCRERRIER-----ETFTDIMTSSGEKANEYVPSFRIEENVLI-----GTGETHPVCANVGELVLNRLSSKPD 615
Cdd:PRK12316 447 ALTYATDLFEARTVERmarhwQNLLRGMVENPQARVDELPMLDAEERGQLvegwnATAAEYPLQRGVHRLFEEQVERTPE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 616 fvGQIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDhvvsklsaryfl 695
Cdd:PRK12316 527 --APALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD------------ 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 696 slmspkvvfvNEESAENLMEAAKEENLQVRV---MVIGSLPGFVSLANILEEQVSrAEIDGFRCTKID---NPHDLAMIC 769
Cdd:PRK12316 593 ----------PEYPAERLAYMLEDSGVQLLLsqsHLGRKLPLAAGVQVLDLDRPA-AWLEGYSEENPGtelNPENLAYVI 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 770 SSSGTTGMPKGTELSYASLYNSITPVEE---------VHAKNEICAWVPTIRWHGGLnqcieviMSNAKWIIFSDDNIKE 840
Cdd:PRK12316 662 YTSGSTGKPKGAGNRHRALSNRLCWMQQayglgvgdtVLQKTPFSFDVSVWEFFWPL-------MSGARLVVAAPGDHRD 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 841 IA-LCEIIQKHGVTWLGTDTNFailyvkMNIFQKYPMP----SLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDA 915
Cdd:PRK12316 735 PAkLVELINREGVDTLHFVPSM------LQAFLQDEDVasctSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEA 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 916 G-----GLCVSQAKNSKPgsCGFVTKGIRIKIADEktgiALGP---KERGEICIKSEFMMKGYHKNPEQTKEAF------ 981
Cdd:PRK12316 809 AidvthWTCVEEGGDSVP--IGRPIANLACYILDA----NLEPvpvGVLGELYLAGRGLARGYHGRPGLTAERFvpspfv 882
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 982 DSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPV 1041
Cdd:PRK12316 883 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 942
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
65-542 |
2.59e-16 |
|
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: 84.06 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAECLAQvvkennmDTRLVVFADSAGFVGRAATLTAVLRSQdtawidefecakltspkHVAAIVCSSGTSGFPKGTEISH 224
Cdd:cd17656 95 LKSKLSF-------NKSTILLEDPSISQEDTSNIDYINNSD-----------------DLLYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 225 AAMINYMAHVKVH---DLKGHVSMWTpSMRWYCGLFIVIKAILDCSKRIIVPD--YDDDEGLCRFIEKYEVSwfrcDSCF 299
Cdd:cd17656 151 KNMVNLLHFEREKtniNFSDKVLQFA-TCSFDVCYQEIFSTLLSGGTLYIIREetKRDVEQLFDLVKRHNIE----VVFL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 300 PIRLVKFgVLSKY----RLPT-LKILLFGGAH------FKGELQQTLVKLLPH-----TDVILSYGMtDYGGLCARQTKY 363
Cdd:cd17656 226 PVAFLKF-IFSERefinRFPTcVKHIITAGEQlvitneFKEMLHEHNVHLHNHygpseTHVVTTYTI-NPEAEIPELPPI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 364 SKPGSCGFVCETGRLKVVDPntgkvLGAnkTGEIWAKSSYMMNGYYNNPEATRRALDSDGW------LHTGDLGYYDNDG 437
Cdd:cd17656 304 GKPISNTWIYILDQEQQLQP-----QGI--VGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 438 EVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQvAVVPVPHNINEEHAM-AFVakVPGKEVTELDITDLVKQNMPWY 516
Cdd:cd17656 377 NIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE-AVVLDKADDKGEKYLcAYF--VMEQELNISQLREYLAKQLPEY 453
|
490 500
....*....|....*....|....*.
gi 1820754837 517 cRLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:cd17656 454 -MIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
623-1078 |
3.21e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.16 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:PRK08279 58 FEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VFVNEESAENLMEAAKEENLQVRVMVIG-----SLPGFVSLAnileeqvsrAEIDGFRctkIDNPH--------DLAMIC 769
Cdd:PRK08279 138 LIVGEELVEAFEEARADLARPPRLWVAGgdtldDPEGYEDLA---------AAAAGAP---TTNPAsrsgvtakDTAFYI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 770 SSSGTTGMPKgtelsyASLYNsitpveevHAKneicaWVPTIRWHGGLNQCIE----------------------VIMSN 827
Cdd:PRK08279 206 YTSGTTGLPK------AAVMS--------HMR-----WLKAMGGFGGLLRLTPddvlycclplyhntggtvawssVLAAG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 828 AKWII---FS-----DDnikeialceiIQKHGVTwlgtdtnfAILYVK------MNifqkYPmPS-------LRKMVITG 886
Cdd:PRK08279 267 ATLALrrkFSasrfwDD----------VRRYRAT--------AFQYIGelcrylLN----QP-PKptdrdhrLRLMIGNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 887 ------APFTKELhetvaKIMphtQILQCYGLTDA-GGLCvsqakN--SKPGSCGFVTKGIRIKIA----DEKTG----- 948
Cdd:PRK08279 324 lrpdiwDEFQQRF-----GIP---RILEFYAASEGnVGFI-----NvfNFDGTVGRVPLWLAHPYAivkyDVDTGepvrd 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 949 -----IALGPKERGE----ICIKSEFmmKGYhKNPEQTK-----EAF-DSDGWLHTKDIGYYDENGEIFFVNRISDFINY 1013
Cdd:PRK08279 391 adgrcIKVKPGEVGLligrITDRGPF--DGY-TDPEASEkkilrDVFkKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRW 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1014 KAIKLSSAEIEGVLELHPSILKAVV--VPVPhETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWY 1078
Cdd:PRK08279 468 KGENVATTEVENALSGFPGVEEAVVygVEVP-GTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAY 533
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
614-1039 |
3.86e-16 |
|
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: 83.29 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 614 PDFVGQIDAFTgkECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARY 693
Cdd:cd17650 1 PDAIAVSDATR--QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 694 FLslmspkvvfvnEESAENLMeaakeenlqvrvmvigslpgfvslanileeqvsraeidgfrctkIDNPHDLAMICSSSG 773
Cdd:cd17650 79 ML-----------EDSGAKLL--------------------------------------------LTQPEDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 774 TTGMPKG---TELSYASLYNSITPVEEVHAKNEICAWVPTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEIA-LCEIIQK 849
Cdd:cd17650 104 TTGKPKGvmvEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAaLYDLILK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 850 HGVTWLGTDTNFAILYVKMNIFQKYPMPSLRkMVITGA--PFTKELHETVAKIMPHTQILQCYGLTDAgglCVS----QA 923
Cdd:cd17650 184 SRITLMESTPALIRPVMAYVYRNGLDLSAMR-LLIVGSdgCKAQDFKTLAARFGQGMRIINSYGVTEA---TIDstyyEE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 924 KNSKPGSCGFVTKG-----IRIKIADEK-----TGIAlgpkerGEICIKSEFMMKGYHKNPEQTKEAFDSDGW------L 987
Cdd:cd17650 260 GRDPLGDSANVPIGrplpnTAMYVLDERlqpqpVGVA------GELYIGGAGVARGYLNRPELTAERFVENPFapgermY 333
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 988 HTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVV 1039
Cdd:cd17650 334 RTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA 385
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1204-1680 |
4.09e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 84.31 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1204 VQTYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHEL----TPMTARNfltlTSPKI 1279
Cdd:PRK06060 30 VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELhrddHALAARN----TEPAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1280 VFTVSS-----SAANLMEAAKELKMNLKVVVMDkldgYESVeenvmkghdtreiiefkchvtNPDDVALIVPSSGTTGLP 1354
Cdd:PRK06060 106 VVTSDAlrdrfQPSRVAEAAELMSEAARVAPGG----YEPM---------------------GGDALAYATYTSGTTGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1355 KGTEISHYSLF------CC----LHPYKnrtlVGhtcIVTPTMRWHYGV--LMAFRLvAANAKKLIVPDNDDAENFCQLI 1422
Cdd:PRK06060 161 KAAIHRHADPLtfvdamCRkalrLTPED----TG---LCSARMYFAYGLgnSVWFPL-ATGGSAVINSAPVTPEAAAILS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1423 EKYQITWFGTDPFMIIKFIKSQLLEKYRlpTLKVILSSGahlrkEHLEV-MREKLPDVF----ITNHYGMTDTA-CVVSA 1496
Cdd:PRK06060 233 ARFGPSVLYGVPNFFARVIDSCSPDSFR--SLRCVVSAG-----EALELgLAERLMEFFggipILDGIGSTEVGqTFVSN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1497 QNKFTKLGSVGYVSSNVRIKMVDLDTEEAlGPNKIGELRVKAITIMQGYHKNPETTkqaFDSDGWLRTGDLAYYDDNGEI 1576
Cdd:PRK06060 306 RVDEWRLGTLGRVLPPYEIRVVAPDGTTA-GPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1577 YIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTEQeLISYVEKNLpdYCRL 1656
Cdd:PRK06060 382 TYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGS-VMRDLHRGL--LNRL 458
|
490 500
....*....|....*....|....*....
gi 1820754837 1657 RG-----GVKIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK06060 459 SAfkvphRFAVVDRLPRTPNGKLVRGALR 487
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1348-1680 |
4.16e-16 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 83.84 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1348 SGTTGLPKG-------------TEISHysLFCClHPykNRTL---------VGHTCIVtptmrwhYGVLMAfrlvaanAK 1405
Cdd:PRK10524 242 SGTTGKPKGvqrdtggyavalaTSMDT--IFGG-KA--GETFfcasdigwvVGHSYIV-------YAPLLA-------GM 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1406 KLIV----PDNDDAENFCQLIEKYQITWFGTDPfMIIKFIKSQ---LLEKYRLPTLKVILSSGAHLRKEHLEVMREKLpD 1478
Cdd:PRK10524 303 ATIMyeglPTRPDAGIWWRIVEKYKVNRMFSAP-TAIRVLKKQdpaLLRKHDLSSLRALFLAGEPLDEPTASWISEAL-G 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1479 VFITNHYGMTDTAC-VVSAQNKF----TKLGSVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAIT---IMQGYHKNPE 1550
Cdd:PRK10524 381 VPVIDNYWQTETGWpILAIARGVedrpTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLppgCMQTVWGDDD 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1551 TtkqaFDSDGWLRTGDLAY-------YDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQ 1623
Cdd:PRK10524 461 R----FVKTYWSLFGRQVYstfdwgiRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQ 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 1624 HPKAFVVQVPNKSVT--------EQELISYVEKNLPDYCRlRGGVKIVDQLPRTTTGKIARKQLR 1680
Cdd:PRK10524 537 VAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVAR-PARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
602-1042 |
5.05e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 85.01 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 602 VGELVLNRLSSKPDFVGQIdaFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICP 681
Cdd:PRK12316 4553 VHQLVAERARMTPDAVAVV--FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 682 WDHVVSKLSARYFLslmspkvvfvnEESAENLMeaAKEENLQVRvmvigsLP---GFVSLAnileeqVSRAEI-DGFRCT 757
Cdd:PRK12316 4631 LDPEYPRERLAYMM-----------EDSGAALL--LTQSHLLQR------LPipdGLASLA------LDRDEDwEGFPAH 4685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 758 ----KIDnPHDLAMICSSSGTTGMPKGTELSYASLYNSItpveevHAKNEICAWVP--------TIRWHGGLNQCIEVIM 825
Cdd:PRK12316 4686 dpavRLH-PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHL------HATGERYELTPddrvlqfmSFSFDGSHEGLYHPLI 4758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 826 SNAKWIIFSDDNIKEIALCEIIQKHGVTWLgtdtNFAILYVKMnIFQKYP----MPSLRKMVITGAPFTKELHETVAKIM 901
Cdd:PRK12316 4759 NGASVVIRDDSLWDPERLYAEIHEHRVTVL----VFPPVYLQQ-LAEHAErdgePPSLRVYCFGGEAVAQASYDLAWRAL 4833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 902 PHTQILQCYGLTDAgGLCVSQAKNSKPGSCGFVTKGIRIKIADEKTGI---ALGPK---ERGEICIKSEFMMKGYHKNPE 975
Cdd:PRK12316 4834 KPVYLFNGYGPTET-TVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVldgQLNPLpvgVAGELYLGGEGVARGYLERPA 4912
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 976 QTKEAFDSD------GWLH-TKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVP 1042
Cdd:PRK12316 4913 LTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQE 4986
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
302-467 |
6.85e-16 |
|
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: 83.18 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 302 RLVKFGVLSKYR----LPTLKILLFGGAHFKGELQQTLVKL-LPHTDVilsYGMTDYGGLCARQTKYS-KPGSCGFVCET 375
Cdd:cd05933 303 RLAKKLVFKKVRkalgLDRCQKFFTGAAPISRETLEFFLSLnIPIMEL---YGMSETSGPHTISNPQAyRLLSCGKALPG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 376 GRLKVVDPNtgkvlgANKTGEI--WAKSSYMmnGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFI---- 449
Cdd:cd05933 380 CKTKIHNPD------ADGIGEIcfWGRHVFM--GYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIitag 451
|
170 180
....*....|....*....|
gi 1820754837 450 --NyraikISPAEIEALIQQ 467
Cdd:cd05933 452 geN-----VPPVPIEDAVKK 466
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
27-542 |
9.83e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.67 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 27 EKAPILKKCtnVGALVLEKLRSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLL 106
Cdd:PRK12467 3088 AAAYPSERL--VHQLIEAQVARTPEAPALVFG--DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALL 3163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 107 AALYLGAISNPWDNELSpmtaryflsltkpkivfvngesAECLAQVVKENNMDTrLVVFADSAGFVGRAATLTAVLRSQD 186
Cdd:PRK12467 3164 AVLKAGGAYVPLDPEYP----------------------RERLAYMIEDSGVKL-LLTQAHLLEQLPAPAGDTALTLDRL 3220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 187 TAWIDEFEC-AKLTSPKHVAAIVCSSGTSGFPKGTEISHAAMIN---YMAHVKVHDLKGHVSMWTP------SMRWYCGL 256
Cdd:PRK12467 3221 DLNGYSENNpSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANhlcWIAEAYELDANDRVLLFMSfsfdgaQERFLWTL 3300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 257 FivikaildCSKRIIVPDYD--DDEGLCRFIEKYEVSwfrcDSCF-PIRLVKFGVLSKYR-LPTLKILLFGGAHFKGELQ 332
Cdd:PRK12467 3301 I--------CGGCLVVRDNDlwDPEELWQAIHAHRIS----IACFpPAYLQQFAEDAGGAdCASLDIYVFGGEAVPPAAF 3368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 333 QTLVKLLPHTDVILSYGMTDygglCARQTKYSKPGSCGfVCET-----GR------LKVVDPNTGKV-LGAnkTGEIWAK 400
Cdd:PRK12467 3369 EQVKRKLKPRGLTNGYGPTE----AVVTVTLWKCGGDA-VCEApyapiGRpvagrsIYVLDGQLNPVpVGV--AGELYIG 3441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 401 SSYMMNGYYNNPEAT-RRAL-----DSDGWLH-TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQ 473
Cdd:PRK12467 3442 GVGLARGYHQRPSLTaERFVadpfsGSGGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVRE 3521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 474 VAVVPVPHNINEEHAMAFVAKVPGKEVTElDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:PRK12467 3522 AVVLARDGAGGKQLVAYVVPADPQGDWRE-TLRDHLAASLPDY-MVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
873-1099 |
1.08e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 82.05 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 873 KYPMPSLRKMVITGAPFTKElhetVAKIM-----PhtQILQCYGLTDAGG--LCVSQAKNSKPGSCGFVTKGIRIKIADE 945
Cdd:PRK12406 267 KYDVSSLRHVIHAAAPCPAD----VKRAMiewwgP--VIYEYYGSTESGAvtFATSEDALSHPGTVGKAAPGAELRFVDE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 946 KtGIALGPKERGEICIKSEFMMK-GYHKNPEQTKEAfDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIE 1024
Cdd:PRK12406 341 D-GRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIE 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 1025 GVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK12406 419 AVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGY-KVPKHIEIMAELPREDSGKI 492
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
629-1045 |
1.50e-15 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 82.17 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTEN-------------HLNTCVPVLAILYIGGIICPWDHVvsklsaryfl 695
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNcpqwivameacaaHSLICVPLYDTLGPGAVDYIVDHA---------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 696 slmSPKVVFVNEESAENLMEA----AKEenlqvrvmvigsLPGFVSLANILEEQVSRAEIDG--------FRCTKIDNPH 763
Cdd:PLN02430 148 ---EIDFVFVQDKKIKELLEPdcksAKR------------LKAIVSFTSVTEEESDKASQIGvktyswidFLHMGKENPS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 764 --------DLAMICSSSGTTGMPKGTELSYAS-----------------------LYNSITPV---------EEVHAKNE 803
Cdd:PLN02430 213 etnppkplDICTIMYTSGTSGDPKGVVLTHEAvatfvrgvdlfmeqfedkmthddVYLSFLPLahildrmieEYFFRKGA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 804 ICAWvptirWHGGLNQCIEVIMSnAKWIIFSD---------DNIKEiALCEI----------IQKHGVTWL--GTDTNFA 862
Cdd:PLN02430 293 SVGY-----YHGDLNALRDDLME-LKPTLLAGvprvferihEGIQK-ALQELnprrrlifnaLYKYKLAWMnrGYSHKKA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 863 ILYVKMNIFQKYPMP---SLRKMVITGAPFTKELHETVaKIMPHTQILQCYGLTDAGGLCVSQAKN--SKPGSCGFVT-- 935
Cdd:PLN02430 366 SPMADFLAFRKVKAKlggRLRLLISGGAPLSTEIEEFL-RVTSCAFVVQGYGLTETLGPTTLGFPDemCMLGTVGAPAvy 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 936 KGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFinyka 1015
Cdd:PLN02430 445 NELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNL----- 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1820754837 1016 IKLSSAE------IEGVLELHP-------------SILKAVVVPVPHET 1045
Cdd:PLN02430 519 IKLSQGEyvaleyLENVYGQNPivediwvygdsfkSMLVAVVVPNEENT 567
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
629-1100 |
1.85e-15 |
|
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: 80.82 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvvskLSARYflslmsPkvvfvnee 708
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP-------LDPAY------P-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 saenlmeaakeenlQVRvmvigslpgfvsLANILEEqvSRAEIdgfrctKIDNPHDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd12115 85 --------------PER------------LRFILED--AQARL------VLTDPDDLAYVIYTSGSTGRPKGVAIEHRNA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 YNSIT------PVEE---VHAKNEIC-------AWVPTIrwHGGlnqciEVIMSNAKWIIFSddnikEIALCEiiqkhgV 852
Cdd:cd12115 131 AAFLQwaaaafSAEElagVLASTSICfdlsvfeLFGPLA--TGG-----KVVLADNVLALPD-----LPAAAE------V 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 853 TWLGTDTNFAILYVKMNIFqkyPmPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDA---GGLCVSQAKNSKPG 929
Cdd:cd12115 193 TLINTVPSAAAELLRHDAL---P-ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDttySTVAPVPPGASGEV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 930 SCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWL------HTKDIGYYDENGEIFF 1003
Cdd:cd12115 269 SIGRPLANTQAYVLDRA-LQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEF 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1004 VNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYCkLQA 1083
Cdd:cd12115 348 LGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYM-VPS 426
|
490
....*....|....*..
gi 1820754837 1084 GIKFVNDFPRISTGKID 1100
Cdd:cd12115 427 RFVRLDALPLTPNGKID 443
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
629-1099 |
2.34e-15 |
|
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: 80.94 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENhlntcVPVLAILYIGG-----IICPWDHVVSKLSARYFLSLMSPKVV 703
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFN-----HFRHLEAYFAVpgmgaVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 704 FVNEEsaenlMEAAKEENLQVrvmvigslpgfvsLANILE---EQVSRAEIDGFRCTkiDNPH----------DLAMICS 770
Cdd:cd05915 101 LFDPN-----LLPLVEAIRGE-------------LKTVQHfvvMDEKAPEGYLAYEE--ALGEeadpvrvperAACGMAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 771 SSGTTGMPKGTELSYASLYNSITPV---EEVHAKNE---ICA----------WVPTIRWHGGLNQCIEVIMSNAkwIIFS 834
Cdd:cd05915 161 TTGTTGLPKGVVYSHRALVLHSLAAslvDGTALSEKdvvLPVvpmfhvnawcLPYAATLVGAKQVLPGPRLDPA--SLVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 835 DdnikeialceiIQKHGVTWLGTDTNF--AILYVKMNIFQKYPMPSlrkMVITGAPFTKELHETVAKIMPHtQILQCYGL 912
Cdd:cd05915 239 L-----------FDGEGVTFTAGVPTVwlALADYLESTGHRLKTLR---RLVVGGSAAPRSLIARFERMGV-EVRQGYGL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 913 TDAGGL---CVSQAK-NSKPGScgfvtKGIRIKIADEKTGIA-----LGP---------KERGEICIKSEFMMKGYHKNP 974
Cdd:cd05915 304 TETSPVvvqNFVKSHlESLSEE-----EKLTLKAKTGLPIPLvrlrvADEegrpvpkdgKALGEVQLKGPWITGGYYGNE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 975 EQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:cd05915 379 EATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1055 QKVVEKEVTEEELHdlvnknlpwYCKLQAG--------IKFVNDFPRISTGKI 1099
Cdd:cd05915 459 VPRGEKPTPEELNE---------HLLKAGFakwqlpdaYVFAEEIPRTSAGKF 502
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1206-1616 |
2.83e-15 |
|
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: 80.94 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIG----AIS---NTWDHELTPMtaRNFLTLTSPK 1278
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGvpaaPVSpaySLMSQDLAKL--KHLFELLKPG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1279 IVFtvSSSAANLMEAAKELKMNLK--VVVMDKLDGYESVE-ENVMKGHDTREIIEFKCHVTnPDDVALIVPSSGTTGLPK 1355
Cdd:cd05921 105 LVF--AQDAAPFARALAAIFPLGTplVVSRNAVAGRGAISfAELAATPPTAAVDAAFAAVG-PDTVAKFLFTSGSTGLPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1356 GTeISHYSLFCCLHPYKNRTLV---GHTCIVTPTMRWHY--GVLMAFRLVAANAKKLIVpdnDDAENFCQLIEK-----Y 1425
Cdd:cd05921 182 AV-INTQRMLCANQAMLEQTYPffgEEPPVLVDWLPWNHtfGGNHNFNLVLYNGGTLYI---DDGKPMPGGFEEtlrnlR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1426 QI--TWFGTDPF---MIIKFI-KSQLLEKYRLPTLKVILSSGAHL------RKEHLEVmREKLPDVFITNHYGMTDTA-- 1491
Cdd:cd05921 258 EIspTVYFNVPAgweMLVAALeKDEALRRRFFKRLKLMFYAGAGLsqdvwdRLQALAV-ATVGERIPMMAGLGATETApt 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1492 CVVSaQNKFTKLGSVGYVSSNVRIKMVDLDTEEalgpnkigELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGD---LA 1568
Cdd:cd05921 337 ATFT-HWPTERSGLIGLPAPGTELKLVPSGGKY--------EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDaakLA 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1569 YYDDNGEIYIVD-RISDFINFRS---INVSPAEIETVLMTHPAVLQAAVLGI 1616
Cdd:cd05921 408 DPDDPAKGLVFDgRVAEDFKLASgtwVSVGPLRARAVAACAPLVHDAVVAGE 459
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
629-1039 |
4.56e-15 |
|
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: 80.22 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIgILTENHLNTCVPVLAILYIGGIICpwdhvvsklsaryflslmSPKVVFVNEE 708
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEV-VFQITHNNKFLYLFWACLLGGMIA------------------VPVSIGSNEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAENLMeaakeenlqvRVMVIGSLPGFVSLANILEEqvsraeidgfrctkidNPHDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd05908 78 HKLKLN----------KVWNTLKNPYLITEEEVLCE----------------LADELAFIQFSSGSTGDPKGVMLTHENL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 -YN--SITPVEEVHAKNEICAWVP------TIRWH-----GGLNQcieVIMSNAKWIIFSDDNIKEIalceiiQKHGVTW 854
Cdd:cd05908 132 vHNmfAILNSTEWKTKDRILSWMPlthdmgLIAFHlapliAGMNQ---YLMPTRLFIRRPILWLKKA------SEHKATI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 855 LGTdTNFAILYV----KMNIFQKYPMPSLRkMVITGA-PFTKEL-HETVAKIMPH----TQILQCYGLTDAG-GLCVSQA 923
Cdd:cd05908 203 VSS-PNFGYKYFlktlKPEKANDWDLSSIR-MILNGAePIDYELcHEFLDHMSKYglkrNAILPVYGLAEASvGASLPKA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 924 -KNSKPGSCG--FVTKGIRIKIADEKTGIALGPKERG--------EIC----------------IKSEFMMKGYHKNPEQ 976
Cdd:cd05908 281 qSPFKTITLGrrHVTHGEPEPEVDKKDSECLTFVEVGkpidetdiRICdednkilpdgyighiqIRGKNVTPGYYNNPEA 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 977 TKEAFDSDGWLHTKDIGYYdENGEIFFVNRISDFINYKAIKLSSAEIEGV-LELHPSILKAVVV 1039
Cdd:cd05908 361 TAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIaEELEGVELGRVVA 423
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1485-1615 |
5.02e-15 |
|
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: 80.48 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTAC--VVSAQNKFTkLGSVGYVSSNVRIKMVDLDTeealgpNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWL 1562
Cdd:cd05933 351 YGMSETSGphTISNPQAYR-LLSCGKALPGCKTKIHNPDA------DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWL 423
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 1563 RTGDLAYYDDNGEIYIVDRISDFInfrsI-----NVSPAEIE-TVLMTHPAVLQAAVLG 1615
Cdd:cd05933 424 HSGDLGKLDEDGFLYITGRIKELI----ItaggeNVPPVPIEdAVKKELPIISNAMLIG 478
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
348-476 |
5.41e-15 |
|
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: 79.95 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDYGGLCARQTKYSK-PGSCG--FVCETGRLKVVdPNTG-KVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDG 423
Cdd:cd05927 306 YGQTECTAGATLTLPGDTsVGHVGgpLPCAEVKLVDV-PEMNyDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDG 384
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 424 WLHTGDLGYYDNDGEVFLVDRMSEFI-----NYraikISPAEIEALIQQHPAVFQVAV 476
Cdd:cd05927 385 WLHTGDIGEWLPNGTLKIIDRKKNIFklsqgEY----VAPEKIENIYARSPFVAQIFV 438
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
629-1026 |
5.66e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 80.45 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNEE 708
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAENLMEAAKEENLQVRVMVigslpgfvSLANILEEQVSRAEIDGFRCTK----------------IDNPHDLAMICSSS 772
Cdd:PLN02614 161 KISELFKTCPNSTEYMKTVV--------SFGGVSREQKEEAETFGLVIYAwdeflklgegkqydlpIKKKSDICTIMYTS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 773 GTTGMPKGTELSYASLYNSITPV--------EEVHAKNEICAWVP-----------TIRWHGGlnqCIEVIMSNAKWIIF 833
Cdd:PLN02614 233 GTTGDPKGVMISNESIVTLIAGVirllksanAALTVKDVYLSYLPlahifdrvieeCFIQHGA---AIGFWRGDVKLLIE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 834 SDDNIKEIALCEIIQKHGVTWLGT---------------DTNFAILYVKMNIFQKY--PMPSLRKMVIT----------- 885
Cdd:PLN02614 310 DLGELKPTIFCAVPRVLDRVYSGLqkklsdggflkkfvfDSAFSYKFGNMKKGQSHveASPLCDKLVFNkvkqglggnvr 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 886 -----GAPFTKELhETVAKIMPHTQILQCYGLTD--AGGLCVSQAKNSKPGSCG--FVTKGIRIKIADEKTGIALGPKER 956
Cdd:PLN02614 390 iilsgAAPLASHV-ESFLRVVACCHVLQGYGLTEscAGTFVSLPDELDMLGTVGppVPNVDIRLESVPEMEYDALASTPR 468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 957 GEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFinykaIKLSSAEIEGV 1026
Cdd:PLN02614 469 GEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNI-----FKLSQGEYVAV 532
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
309-546 |
5.98e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 79.27 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 309 LSKYRLptlkILLFGGAHFKGELQQTLVKLLPhtdVILSYGMTDygglCARQTKYSKPG-------SCGFVCETGRLKVV 381
Cdd:PRK07445 229 LAQFRT----ILLGGAPAWPSLLEQARQLQLR---LAPTYGMTE----TASQIATLKPDdflagnnSSGQVLPHAQITIP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 382 DPNTGKVlganktgEIWAKSSYMmnGYYnnPEAtrraLDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEI 461
Cdd:PRK07445 298 ANQTGNI-------TIQAQSLAL--GYY--PQI----LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEV 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 462 EALIQQHPAVFQVAVVPVPHNINEEHAMAFVakVPGKEVTELDI------TDLVKQNMP--WYCrlhagvkfMEKLPRTA 533
Cdd:PRK07445 363 EAAILATGLVQDVCVLGLPDPHWGEVVTAIY--VPKDPSISLEElktaikDQLSPFKQPkhWIP--------VPQLPRNP 432
|
250
....*....|...
gi 1820754837 534 TGKIAKKQLKQIA 546
Cdd:PRK07445 433 QGKINRQQLQQIA 445
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
629-1040 |
7.60e-15 |
|
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: 80.67 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvvskL-----SARyfLSLM----S 699
Cdd:COG1020 503 TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP-------LdpaypAER--LAYMledaG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 700 PKVVFVNEESAENLMEaakeenLQVRVMVIGSLpgfvslaNILEEQVSRAEIDGfrctkidNPHDLAMICSSSGTTGMPK 779
Cdd:COG1020 574 ARLVLTQSALAARLPE------LGVPVLALDAL-------ALAAEPATNPPVPV-------TPDDLAYVIYTSGSTGRPK 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 780 GTELSYASLYNSitpveeVHAKNEICAWVPTIRW--------------------HGG-LnqcievimsnakwIIFSDDNI 838
Cdd:COG1020 634 GVMVEHRALVNL------LAWMQRRYGLGPGDRVlqfaslsfdasvweifgallSGAtL-------------VLAPPEAR 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 839 KEIA-LCEIIQKHGVTWLgtdtNF--AILYVkMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDA 915
Cdd:COG1020 695 RDPAaLAELLARHRVTVL----NLtpSLLRA-LLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTET 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 916 GGLCVSQAKNSKPGSCGFVT-----KGIRIKIADEK-----TGIAlgpkerGEICIKSEFMMKGYHKNPEQTKEAF---- 981
Cdd:COG1020 770 TVDSTYYEVTPPDADGGSVPigrpiANTRVYVLDAHlqpvpVGVP------GELYIGGAGLARGYLNRPELTAERFvadp 843
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 982 -DSDG--WLHTKDIGYYDENGEIFFVNRIsDF---IN-YKaIKLssAEIEGVLELHPSILKAVVVP 1040
Cdd:COG1020 844 fGFPGarLYRTGDLARWLPDGNLEFLGRA-DDqvkIRgFR-IEL--GEIEAALLQHPGVREAVVVA 905
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
623-1100 |
9.16e-15 |
|
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: 79.02 E-value: 9.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLslmspkv 702
Cdd:cd17644 21 FEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYIL------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 vfvneesaenlmeaakeENLQVRVMVIgslpgfvslanileeqvsraeidgfrctkidNPHDLAMICSSSGTTGMPKGTE 782
Cdd:cd17644 94 -----------------EDAQISVLLT-------------------------------QPENLAYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 783 LSYASLYN-SITPVEEVHAKNE--ICAWVpTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEIA-LCEIIQKHGVTWLGTD 858
Cdd:cd17644 126 IEHQSLVNlSHGLIKEYGITSSdrVLQFA-SIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEdFVQYIQQWQLTVLSLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 859 TNFAILYVKMNIFQKYPMP-SLRKMVITGAPFTKELHETVAKIM-PHTQILQCYGLTDAGgLCVSQAKNSKPGSCGFVTK 936
Cdd:cd17644 205 PAYWHLLVLELLLSTIDLPsSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTEAT-IAATVCRLTQLTERNITSV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 937 GIRIKIADEKTGI------ALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLH--------TKDIGYYDENGEIF 1002
Cdd:cd17644 284 PIGRPIANTQVYIldenlqPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1003 FVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYCKLQ 1082
Cdd:cd17644 364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPS 443
|
490
....*....|....*...
gi 1820754837 1083 AGIkFVNDFPRISTGKID 1100
Cdd:cd17644 444 AFV-VLEELPLTPNGKID 460
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
316-543 |
1.17e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 79.31 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 316 TLKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDYGglcarQTKYS------KPGSCGFVCETGRLKVVDPNtGKVL 389
Cdd:PRK06060 261 SLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVG-----QTFVSnrvdewRLGTLGRVLPPYEIRVVAPD-GTTA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 390 GANKTGEIWAKSSYMMNGYYNNPEATrraLDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHP 469
Cdd:PRK06060 335 GPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDE 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 470 AVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYCRLHAGVKF--MEKLPRTATGKIAKKQLK 543
Cdd:PRK06060 412 AVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFavVDRLPRTPNGKLVRGALR 487
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
1206-1680 |
1.20e-14 |
|
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: 78.62 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAIsntwdhelTPMTARNfltLTSPKIVFTVSS 1285
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVE--------TALINSN---LRLESLLHCITV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 SAAnlmeaaKELKMNLKvvvmDKLDGYESVEENvmkghdtreiiefKCHVTNPDDVALIVPSSGTTGLPKGTEISHYS-L 1364
Cdd:cd05939 74 SKA------KALIFNLL----DPLLTQSSTEPP-------------SQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRyY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1365 FCCLHPYKNRTLVGHTCIVTPTMRWH-------YGVLMAFRLVAANAKKLivpdndDAENFCQLIEKYQITwfgtdpfmI 1437
Cdd:cd05939 131 RIAAGAYYAFGMRPEDVVYDCLPLYHsaggimgVGQALLHGSTVVIRKKF------SASNFWDDCVKYNCT--------I 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1438 IKFIKS---QLLEKYRLPTLK---VILSSGAHLRKEHLE--VMREKLPDvfITNHYGMTDTACvvSAQNKFTKLGSVGYV 1509
Cdd:cd05939 197 VQYIGEicrYLLAQPPSEEEQkhnVRLAVGNGLRPQIWEqfVRRFGIPQ--IGEFYGATEGNS--SLVNIDNHVGACGFN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1510 SSN------VRIKMVDLDTEEAL----------GPNKIGEL--RVKAITIM---QGYHKNPETTKQ----AFDS-DGWLR 1563
Cdd:cd05939 273 SRIlpsvypIRLIKVDEDTGELIrdsdglcipcQPGEPGLLvgKIIQNDPLrrfDGYVNEGATNKKiardVFKKgDSAFL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1564 TGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIpnEVDEQHPKAFV--VQVPNKSVTEQE 1641
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV--EVPGVEGRAGMaaIVDPERKVDLDR 430
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1820754837 1642 LISYVEKNLPDYCR---LRggvkIVDQLPRTTTGKIARKQLR 1680
Cdd:cd05939 431 FSAVLAKSLPPYARpqfIR----LLPEVDKTGTFKLQKTDLQ 468
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
460-536 |
1.57e-14 |
|
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: 69.88 E-value: 1.57e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 460 EIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYCRLHAgVKFMEKLPRTATGK 536
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKE-VVFVDELPKTRSGK 76
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
58-542 |
1.69e-14 |
|
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: 77.98 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 58 AVT--GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTK 135
Cdd:cd17645 16 AVVdrGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 136 PKIVfvngesaeclaqvvkennmdtrlvvfadsagfvgraatltavlrsqdtawidefecakLTSPKHVAAIVCSSGTSG 215
Cdd:cd17645 96 AKIL----------------------------------------------------------LTNPDDLAYVIYTSGSTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 216 FPKGTEISHAAMINYMA-------------HVKVHDLKGHVSMWTPSMRWYCG--LFIVIKAI-LDCSKriiVPDYDDDE 279
Cdd:cd17645 118 LPKGVMIEHHNLVNLCEwhrpyfgvtpadkSLVYASFSFDASAWEIFPHLTAGaaLHVVPSERrLDLDA---LNDYFNQE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 280 GLCrfiekyeVSWFRCDSCfpirlVKFGVLSKYrlpTLKILLFGGAHFKgelqqtLVKLLPHTdVILSYGMTDyGGLCAR 359
Cdd:cd17645 195 GIT-------ISFLPTGAA-----EQFMQLDNQ---SLRVLLTGGDKLK------KIERKGYK-LVNNYGPTE-NTVVAT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 360 QTKYSKPG---SCGFVCETGRLKVVDP-NTGKVLGAnkTGEIWAKSSYMMNGYYNNPEATRRALDSDGWL------HTGD 429
Cdd:cd17645 252 SFEIDKPYaniPIGKPIDNTRVYILDEaLQLQPIGV--AGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 430 LGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVakVPGKEVTELDITDLV 509
Cdd:cd17645 330 LAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYV--TAPEEIPHEELREWL 407
|
490 500 510
....*....|....*....|....*....|...
gi 1820754837 510 KQNMPWYCRLHAGVKfMEKLPRTATGKIAKKQL 542
Cdd:cd17645 408 KNDLPDYMIPTYFVH-LKALPLTANGKVDRKAL 439
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
764-1100 |
2.09e-14 |
|
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: 77.52 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 764 DLAMICSSSGTTGMPKGTE------LSYASLY--NSITPVEevhaKNEICAwVPTIRWHGGLNQCIEVIMS-NAKWIIFS 834
Cdd:cd05958 98 DICILAFTSGTTGAPKATMhfhrdpLASADRYavNVLRLRE----DDRFVG-SPPLAFTFGLGGVLLFPFGvGASGVLLE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 835 DDNIKEIAlcEIIQKHGVTWLGT-DTNFAILYVKMNiFQKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYGLT 913
Cdd:cd05958 173 EATPDLLL--SAIARYKPTVLFTaPTAYRAMLAHPD-AAGPDLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGST 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 914 DAGGLCVSQAK-NSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEfmmKGYHKNPEQTKEAFDSDGWLHTKDI 992
Cdd:cd05958 249 EMFHIFISARPgDARPGATGKPVPGYEAKVVDDE-GNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDT 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 993 GYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV---QKVVEKEVTEEELHD 1069
Cdd:cd05958 325 YSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVvlrPGVIPGPVLARELQD 404
|
330 340 350
....*....|....*....|....*....|.
gi 1820754837 1070 LVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd05958 405 HAKAHIAPY-KYPRAIEFVTELPRTATGKLQ 434
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
614-1039 |
2.25e-14 |
|
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: 77.90 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 614 PDFVGQIdaFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARY 693
Cdd:cd17656 2 PDAVAVV--FENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 694 FLSLMSPKVVFVNEESAENLmeaakEENLQVRVmvigslpgfvsLANILEEQVSRAEIDgfrctKIDNPHDLAMICSSSG 773
Cdd:cd17656 80 IMLDSGVRVVLTQRHLKSKL-----SFNKSTIL-----------LEDPSISQEDTSNID-----YINNSDDLLYIIYTSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 774 TTGMPKGTELSYASLYNsITPVEEVHAKNEICAWV---PTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEI-ALCEIIQK 849
Cdd:cd17656 139 TTGKPKGVQLEHKNMVN-LLHFEREKTNINFSDKVlqfATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVeQLFDLVKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 850 HGVTWLGTDTNFailyVKMnIFQKY----PMPSLRKMVITGA-------PFTKELHETVAKIMPH-----TQILQCYGLt 913
Cdd:cd17656 218 HNIEVVFLPVAF----LKF-IFSERefinRFPTCVKHIITAGeqlvitnEFKEMLHEHNVHLHNHygpseTHVVTTYTI- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 914 DAGGLCVSQAKNSKPGSCgfvtkgIRIKIADE-KTGIALGPKerGEICIKSEFMMKGYHKNPEQTKEAFDSDGW------ 986
Cdd:cd17656 292 NPEAEIPELPPIGKPISN------TWIYILDQeQQLQPQGIV--GELYISGASVARGYLNRQELTAEKFFPDPFdpnerm 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 987 LHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVV 1039
Cdd:cd17656 364 YRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVL 416
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
36-542 |
2.32e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 78.93 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 36 TNVGALVLEKLRSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIS 115
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 116 NPWDNELSPMTARYFLSLTKPKIVFVngeSAECLAQvvkennmdtrlvvFADSAGfvgraatlTAVLRSQDTAWIDEFEC 195
Cdd:PRK10252 536 LPLDTGYPDDRLKMMLEDARPSLLIT---TADQLPR-------------FADVPD--------LTSLCYNAPLAPQGAAP 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 196 AKLTSPKHVAAIVCSSGTSGFPKGTEISHAAMINYMAHVKVH-----------------DlkghVSMWT---PSMrwyCG 255
Cdd:PRK10252 592 LQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHypltaddvvlqktpcsfD----VSVWEffwPFI---AG 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 256 LFIVIKAildcskriivPD-YDDDEGLCRFIEKYEVS--WFrcdscFPIRLVKF-GVLSKYRLP----TLKILLFGGAHF 327
Cdd:PRK10252 665 AKLVMAE----------PEaHRDPLAMQQFFAEYGVTttHF-----VPSMLAAFvASLTPEGARqscaSLRQVFCSGEAL 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 328 KGELQ---QTLVKLLPHTdvilSYGMTD----------YGGLCARQTKYSKPgsCGF-VCETG------RLKVVDPNTgk 387
Cdd:PRK10252 730 PADLCrewQQLTGAPLHN----LYGPTEaavdvswypaFGEELAAVRGSSVP--IGYpVWNTGlrildaRMRPVPPGV-- 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 388 vlgankTGEIWAKSSYMMNGYYNNPEATRRALDSDGWL------HTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEI 461
Cdd:PRK10252 802 ------AGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEI 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 462 EALIQQHPAVFQVAVVPVPHNINEEH---AMAFVAKVPGKEVTELDITDL---VKQNMPWYCRLHAGVKfMEKLPRTATG 535
Cdd:PRK10252 876 DRAMQALPDVEQAVTHACVINQAAATggdARQLVGYLVSQSGLPLDTSALqaqLRERLPPHMVPVVLLQ-LDQLPLSANG 954
|
....*..
gi 1820754837 536 KIAKKQL 542
Cdd:PRK10252 955 KLDRKAL 961
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1206-1582 |
2.75e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 78.09 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDvfliLLGTMYigaisNTWDHELTPMTA---------RNFLTLTS 1276
Cdd:PTZ00216 123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWE----WLASIY-----GIWSQSMVAATVyanlgedalAYALRETE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1277 PKIVFTVSSSAANLMEAAKELKM-NLKVVVMDKL------DGYESV--EENVMKGHDTREiiEFKCHV-TNPDDVALIVP 1346
Cdd:PTZ00216 194 CKAIVCNGKNVPNLLRLMKSGGMpNTTIIYLDSLpasvdtEGCRLVawTDVVAKGHSAGS--HHPLNIpENNDDLALIMY 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1347 SSGTTGLPKGTEISHYSLFCCLHPYKNR--TLVGH-------------------TCIVTPTMRwhyGVLMAF----RLVA 1401
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLTAGILALEDRlnDLIGPpeedetycsylplahimefGVTNIFLAR---GALIGFgsprTLTD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1402 ANAKklivPDNDDAEnfcqliekYQitwfgtdPFMII----------KFIKSQL-----LEK------Y--RLPTLK--- 1455
Cdd:PTZ00216 349 TFAR----PHGDLTE--------FR-------PVFLIgvprifdtikKAVEAKLppvgsLKRrvfdhaYqsRLRALKegk 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1456 ----------------------VILSSGAHLRKEHLEVMREklpdVF--ITNHYGMTDTACVVSAQnkFT---KLGSVGY 1508
Cdd:PTZ00216 410 dtpywnekvfsapravlggrvrAMLSGGGPLSAATQEFVNV----VFgmVIQGWGLTETVCCGGIQ--RTgdlEPNAVGQ 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 1509 VSSNVRIKMVDLD----TEEalgPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRI 1582
Cdd:PTZ00216 484 LLKGVEMKLLDTEeykhTDT---PEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRV 558
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1206-1652 |
4.22e-14 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 77.17 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKivftvss 1285
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPR------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 saanlmeaakelkmnlKVVVMDKLDgyesveenVMKGHDTREIIEFkchvtnpddvalivpSSGTTGLPKGTEISHYSL- 1364
Cdd:cd17647 95 ----------------GLIVIRAAG--------VVVGPDSNPTLSF---------------TSGSEGIPKGVLGRHFSLa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1365 ---------FCCLHPYKNRTLVG--HTcivtPTMRWHYGVLMAfrlvaanAKKLIVPDNDDA---ENFCQLIEKYQITWF 1430
Cdd:cd17647 136 yyfpwmakrFNLSENDKFTMLSGiaHD----PIQRDMFTPLFL-------GAQLLVPTQDDIgtpGRLAEWMAKYGATVT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1431 GTDPFMiikfikSQLL---EKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTACVVS---------AQN 1498
Cdd:cd17647 205 HLTPAM------GQLLtaqATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSyfevpsrssDPT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1499 KFTKLGSV---GYVSSNVRIKMVD-LDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAF------DSDGWL------ 1562
Cdd:cd17647 279 FLKNLKDVmpaGRGMLNVQLLVVNrNDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFvnnwfvEPDHWNyldkdn 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1563 ----------------RTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPK 1626
Cdd:cd17647 359 nepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLV 438
|
490 500
....*....|....*....|....*.
gi 1820754837 1627 AFVVQVPNKSVTEQELISYVEKNLPD 1652
Cdd:cd17647 439 SYIVPRFDKPDDESFAQEDVPKEVST 464
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
317-503 |
5.44e-14 |
|
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: 76.87 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 317 LKILLFGGAHFKGELQQTL-VKLLPhtdVILSYGMTDY--GGLCARQTKYSkPGSCGFVCETGRLKVVDPNTGKVLGANK 393
Cdd:cd17639 252 LRYMLSGGAPLSADTQEFLnIVLCP---VIQGYGLTETcaGGTVQDPGDLE-TGRVGPPLPCCEIKLVDWEEGGYSTDKP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 394 T--GEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFIN-----YraikISPAEIEALIQ 466
Cdd:cd17639 328 PprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKlqngeY----IALEKLESIYR 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1820754837 467 QHPAVFQVAVVPVPHNI--------NEEHAMAFVAK--VPGKEVTEL 503
Cdd:cd17639 404 SNPLVNNICVYADPDKSypvaivvpNEKHLTKLAEKhgVINSEWEEL 450
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1177-1679 |
6.55e-14 |
|
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: 76.93 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1177 VNIAEeTLKFLKSKPDSIGQVDALTGKVQ--TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGA 1254
Cdd:cd05943 70 LNYAE-NLLRHADADDPAAIYAAEDGERTevTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1255 IsntWDHELTPMTARNFLTLTS---PKIVFTVSSS---------AANLMEAAKELKMNLKVVVMDKLDGYESVE----EN 1318
Cdd:cd05943 149 I---WSSCSPDFGVPGVLDRFGqiePKVLFAVDAYtyngkrhdvREKVAELVKGLPSLLAVVVVPYTVAAGQPDlskiAK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1319 VM-----KGHDTREIIEFkCHVtNPDDVALIVPSSGTTGLPK-------GTEISH---YSLFCCLHPyknrtlvGHT-CI 1382
Cdd:cd05943 226 ALtledfLATGAAGELEF-EPL-PFDHPLYILYSSGTTGLPKcivhgagGTLLQHlkeHILHCDLRP-------GDRlFY 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1383 VTPT--MRWHYgvLMAFRLVAANakklIV-----PDNDDAENFCQLIEKYQITWFGTDPfmiiKFIkSQLLEK------- 1448
Cdd:cd05943 297 YTTCgwMMWNW--LVSGLAVGAT----IVlydgsPFYPDTNALWDLADEEGITVFGTSA----KYL-DALEKAglkpaet 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1449 YRLPTLKVILSSGAHLRKEHLEVMREKL-PDVFITNHYGMTDTACVVSAQNK---FTKlGSVGYVSSNVRIKMVDLDTEE 1524
Cdd:cd05943 366 HDLSSLRTILSTGSPLKPESFDYVYDHIkPDVLLASISGGTDIISCFVGGNPllpVYR-GEIQCRGLGMAVEAFDEEGKP 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1525 ALGPnkIGELR-VKAITIMQ-GYHKNPETTK--QA-FDS-DGWLRTGDLAYYDDNGEIYIVDRiSD-FINFRSINVSPAE 1597
Cdd:cd05943 445 VWGE--KGELVcTKPFPSMPvGFWNDPDGSRyrAAyFAKyPGVWAHGDWIEITPRGGVVILGR-SDgTLNPGGVRIGTAE 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1598 IETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQVPNKSVTE---QELISYVEKNL-----PDycrlrggvKI--VDQLP 1667
Cdd:cd05943 522 IYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDelrKRIRSTIRSALsprhvPA--------KIiaVPDIP 593
|
570
....*....|....*
gi 1820754837 1668 RTTTGK---IARKQL 1679
Cdd:cd05943 594 RTLSGKkveVAVKKI 608
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
763-1100 |
7.87e-14 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 76.09 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 763 HDLAMICSSSGTTGMPKGTELSYASLyNSITP-VEEVHAKNE---------------ICAWVPTIRWHGGLNqCIEvims 826
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHDNL-VSFTNwMLEDFALPEgpqflnqapysfdlsVMDLYPTLASGGTLV-ALP---- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 827 naKWIIfsdDNIKEiaLCEIIQKHGV-TWLGTDTnFAILYVKMNIFQKYPMPSLRKMVITGapftKEL-HETVAKIM--- 901
Cdd:PRK04813 217 --KDMT---ANFKQ--LFETLPQLPInVWVSTPS-FADMCLLDPSFNEEHLPNLTHFLFCG----EELpHKTAKKLLerf 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 902 PHTQILQCYGLTDAGGlCVSQAK-------NSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNP 974
Cdd:PRK04813 285 PSATIYNTYGPTEATV-AVTSIEitdemldQYKRLPIGYAKPDSPLLIIDEE-GTKLPDGEQGEIVISGPSVSKGYLNNP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 975 EQTKEAF-DSDGW--LHTKDIGYYDeNGEIFFVNRIsDFinykAIKLSS-----AEIEGVLELHPSILKAVVVP------ 1040
Cdd:PRK04813 363 EKTAEAFfTFDGQpaYHTGDAGYLE-DGLLFYQGRI-DF----QIKLNGyrielEEIEQNLRQSSYVESAVVVPynkdhk 436
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1041 --------VPHETDIELPLAFVQkvvekevteeELHDLVNKNLPWYCKLQagiKFV--NDFPRISTGKID 1100
Cdd:PRK04813 437 vqyliayvVPKEEDFEREFELTK----------AIKKELKERLMEYMIPR---KFIyrDSLPLTPNGKID 493
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
879-1040 |
8.22e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 76.80 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 879 LRKMVITGAPFTKELHETVaKIMPHTQILQCYGLTDAGGLCVSQAKNSKP--GSCG--FVTKGIRIKIADEKTGIALGPK 954
Cdd:PLN02861 385 VRLLLSGAAPLPRHVEEFL-RVTSCSVLSQGYGLTESCGGCFTSIANVFSmvGTVGvpMTTIEARLESVPEMGYDALSDV 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 955 ERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFinykaIKLSSAEIEGVLELH---- 1030
Cdd:PLN02861 464 PRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNI-----FKLSQGEYVAVENLEntys 537
|
170 180
....*....|....*....|....*
gi 1820754837 1031 ---------------PSILKAVVVP 1040
Cdd:PLN02861 538 rcpliasiwvygnsfESFLVAVVVP 562
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
927-1099 |
9.80e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 75.80 E-value: 9.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 927 KPGSCGFVTKGIRIKIADEK-TGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVN 1005
Cdd:PRK07787 291 RPGWVGLPLAGVETRLVDEDgGPVPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1006 RIS-DFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVqkVVEKEVTEEELHDLVNKNLPWYcKLQAG 1084
Cdd:PRK07787 371 REStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV--VGADDVAADELIDFVAQQLSVH-KRPRE 447
|
170
....*....|....*
gi 1820754837 1085 IKFVNDFPRISTGKI 1099
Cdd:PRK07787 448 VRFVDALPRNAMGKV 462
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1206-1680 |
1.36e-13 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 76.09 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVFTVSS 1285
Cdd:PLN02654 122 TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1286 saanLMEAAKELkmNLKVVVMDKLDgyESVEENV-------------MKGHDTR-----------EIIEF--KCHV--TN 1337
Cdd:PLN02654 202 ----VKRGPKTI--NLKDIVDAALD--ESAKNGVsvgicltyenqlaMKREDTKwqegrdvwwqdVVPNYptKCEVewVD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1338 PDDVALIVPSSGTTGLPKGT-------EISHYSLFCCLHPYKNRT----------LVGHTCIVtptmrwhYGVLMafrlv 1400
Cdd:PLN02654 274 AEDPLFLLYTSGSTGKPKGVlhttggyMVYTATTFKYAFDYKPTDvywctadcgwITGHSYVT-------YGPML----- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1401 aaNAKKLIV----PDNDDAENFCQLIEKYQITWFGTDPFMIIKFIKS--QLLEKYRLPTLKVILSSGAHLRKEHLEVMRE 1474
Cdd:PLN02654 342 --NGATVLVfegaPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDgdEYVTRHSRKSLRVLGSVGEPINPSAWRWFFN 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1475 KLPD--VFITNHYGMTDTACVVsaqnkFTKL--------GSVGYVSSNVRIKMVDLDTEEALGPNKiGELRVK-----AI 1539
Cdd:PLN02654 420 VVGDsrCPISDTWWQTETGGFM-----ITPLpgawpqkpGSATFPFFGVQPVIVDEKGKEIEGECS-GYLCVKkswpgAF 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1540 TIMQGYHKNPETTK-QAFDsdGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPN 1618
Cdd:PLN02654 494 RTLYGDHERYETTYfKPFA--GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEH 571
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1619 EVDEQHPKAFVVQVPNKSVTEQ---ELISYVEKNL-----PDYCRLRGGvkivdqLPRTTTGKIARKQLR 1680
Cdd:PLN02654 572 EVKGQGIYAFVTLVEGVPYSEElrkSLILTVRNQIgafaaPDKIHWAPG------LPKTRSGKIMRRILR 635
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
629-1100 |
1.40e-13 |
|
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: 75.41 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWD--HVVSKLsaRYFLSLMSPKVVFVN 706
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDpdYPADRL--RYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 707 EESAENLmeaakeeNLQVRVMVIGSLPGFVSLANILEEQVsraeidgfrctkidnPHDLAMICSSSGTTGMPKGTELSYA 786
Cdd:cd12116 92 DALPDRL-------PAGLPVLLLALAAAAAAPAAPRTPVS---------------PDDLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 787 SLYNSITPVEEVHAKNEICAW--VPTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKE-IALCEIIQKHGVTWL-GTDTNFA 862
Cdd:cd12116 150 NLVNFLHSMRERLGLGPGDRLlaVTTYAFDISLLELLLPLLAGARVVIAPRETQRDpEALARLIEAHSITVMqATPATWR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 863 ILyvKMNIFQkyPMPSLRkMVITGAPFTKELHETVAKimPHTQILQCYGLTDAGGLCVSQAKNskpGSCGFVTKG----- 937
Cdd:cd12116 230 ML--LDAGWQ--GRAGLT-ALCGGEALPPDLAARLLS--RVGSLWNLYGPTETTIWSTAARVT---AAAGPIPIGrplan 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 938 IRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLH-------TKDIGYYDENGEIFFVNRISDF 1010
Cdd:cd12116 300 TQVYVLDAA-LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1011 INYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELpLAFVQKVVEKEVTEEELHDLVNKNLPWYCKLQAGIKfVND 1090
Cdd:cd12116 379 VKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVR-LDA 456
|
490
....*....|
gi 1820754837 1091 FPRISTGKID 1100
Cdd:cd12116 457 LPLTANGKLD 466
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
623-1100 |
1.86e-13 |
|
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: 74.51 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKV 702
Cdd:cd17645 19 DRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 VfvneesaenlmeaakeenlqvrvmvigslpgfvslanileeqvsraeidgfrctkIDNPHDLAMICSSSGTTGMPKGTE 782
Cdd:cd17645 99 L-------------------------------------------------------LTNPDDLAYVIYTSGSTGLPKGVM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 783 LSYASLYN---------SITPVEE--VHAKNEICAWVPTIRWHGGLNQCIEVIMSNAKWIIfsddnikeIALCEIIQKHG 851
Cdd:cd17645 124 IEHHNLVNlcewhrpyfGVTPADKslVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDL--------DALNDYFNQEG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 852 VTWLGTDTNFAILYVKMNifqkypMPSLRkMVITGAPFTKelhetVAKIMPHtQILQCYGLTDaGGLCVSQAKNSKPGSC 931
Cdd:cd17645 196 ITISFLPTGAAEQFMQLD------NQSLR-VLLTGGDKLK-----KIERKGY-KLVNNYGPTE-NTVVATSFEIDKPYAN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 932 GFVTKGI---RIKIADEktGIALGPK-ERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWL------HTKDIGYYDENGEI 1001
Cdd:cd17645 262 IPIGKPIdntRVYILDE--ALQLQPIgVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1002 FFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVqkVVEKEVTEEELHDLVNKNLPWYCKL 1081
Cdd:cd17645 340 EFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYV--TAPEEIPHEELREWLKNDLPDYMIP 417
|
490
....*....|....*....
gi 1820754837 1082 QAGIKfVNDFPRISTGKID 1100
Cdd:cd17645 418 TYFVH-LKALPLTANGKVD 435
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
845-1054 |
2.02e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 75.18 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 845 EIIQKHGVTwlgtdtnfaILY---------VKM--NIFQKYPMPSLRKMVITGAPFTKE----LHETVAKimPHTQILQC 909
Cdd:PRK00174 333 EVIDKHKVT---------IFYtaptairalMKEgdEHPKKYDLSSLRLLGSVGEPINPEawewYYKVVGG--ERCPIVDT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 910 YGLTDAGGLCVSQ---AKNSKPGSCGFVTKGIRIKIADEkTGIALGPKERGEICIKSEF--MMKGYHKNPEQTKEAFDSD 984
Cdd:PRK00174 402 WWQTETGGIMITPlpgATPLKPGSATRPLPGIQPAVVDE-EGNPLEGGEGGNLVIKDPWpgMMRTIYGDHERFVKTYFST 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 985 --GWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:PRK00174 481 fkGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFV 552
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
343-549 |
2.04e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.13 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 343 DVILSYGMTD---YGGLC---ARQTKYSKPGSCGFVCETGR------LKVVDPNTGKVLGANKT-GEIWAKSSYMMNGYY 409
Cdd:PRK07008 320 EVIHAWGMTEmspLGTLCklkWKHSQLPLDEQRKLLEKQGRviygvdMKIVGDDGRELPWDGKAfGDLQVRGPWVIDRYF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 410 NNPEATRraldSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAM 489
Cdd:PRK07008 400 RGDASPL----VDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 490 AFVAKVPGKEVTELDITDLVKQNMP-WYcrLHAGVKFMEKLPRTATGKIAKKQLKQIAKSY 549
Cdd:PRK07008 476 LVVVKRPGAEVTREELLAFYEGKVAkWW--IPDDVVFVDAIPHTATGKLQKLKLREQFRDY 534
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1342-1679 |
2.25e-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: 74.43 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1342 ALIVPSSGTTGLPKGTEISHYSL------FCCL-HPYKNRTLVGhtcivTPTMRWHYGVLMAFRLVAANAKKLIVPDNDD 1414
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCIlpniqhFRSLfNITSEDILFL-----TSPLTFDPSVVEIFLSLSSGATLLIVPTSVK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1415 AENFC---QLIEKYQITWFGTDPFMIIKF----IKSQLLEkyRLPTLKVILSSGAHLRKEH-LEVMREKLPDVFITNHYG 1486
Cdd:cd17654 196 VLPSKladILFKRHRITVLQATPTLFRRFgsqsIKSTVLS--ATSSLRVLALGGEPFPSLViLSSWRGKGNRTRIFNIYG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1487 MTDTACVVSAqNKFTKLGS---VGYVSSNVRIKMVDLDTEEALGPNKIGELrvKAITIMQGYHKNPETTkqafdsdgWLR 1563
Cdd:cd17654 274 ITEVSCWALA-YKVPEEDSpvqLGSPLLGTVIEVRDQNGSEGTGQVFLGGL--NRVCILDDEVTVPKGT--------MRA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1564 TGDLAYYDDnGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVlgipNEVDEQHPKAFVVQVPNKSVTEQELI 1643
Cdd:cd17654 343 TGDFVTVKD-GELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV----TLSDQQRLIAFIVGESSSSRIHKELQ 417
|
330 340 350
....*....|....*....|....*....|....*...
gi 1820754837 1644 SYVEK--NLPDYcrlrggVKIVDQLPRTTTGKIARKQL 1679
Cdd:cd17654 418 LTLLSshAIPDT------FVQIDKLPLTSHGKVDKSEL 449
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
65-464 |
2.53e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 75.24 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFV--- 141
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqdk 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 142 --------NGESAECLAQVVKENNMDTRLVVFADSAGFvgraatltavlrsQDTAWIDEF----ECAKLTSPKH---VAA 206
Cdd:PLN02430 158 kikellepDCKSAKRLKAIVSFTSVTEEESDKASQIGV-------------KTYSWIDFLhmgkENPSETNPPKpldICT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 207 IVCSSGTSGFPKGTEISHAAMINYMAHVKVHDLKGHVSMWTPSMrwYCGlFIVIKAILDcskRII----------VPDYD 276
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFEDKMTHDDV--YLS-FLPLAHILD---RMIeeyffrkgasVGYYH 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 277 DD----------------EGLCRFIEK-YEVSWFRCDSCFPIRLVKFGVLSKYRLP------------------------ 315
Cdd:PLN02430 299 GDlnalrddlmelkptllAGVPRVFERiHEGIQKALQELNPRRRLIFNALYKYKLAwmnrgyshkkaspmadflafrkvk 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 316 -----TLKILLFGGAHFKGELQQTLvKLLPHTDVILSYGMTDYGGLCAR--QTKYSKPGSCGFVCETGRLKVVD-PNTG- 386
Cdd:PLN02430 379 aklggRLRLLISGGAPLSTEIEEFL-RVTSCAFVVQGYGLTETLGPTTLgfPDEMCMLGTVGAPAVYNELRLEEvPEMGy 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 387 KVLGANKTGEIWAKSSYMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDRMSEFinyraIKISPAEIEAL 464
Cdd:PLN02430 458 DPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNL-----IKLSQGEYVAL 529
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1435-1640 |
3.38e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 74.47 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1435 FMIIKFIKSQLLEKYRLptlkvILSSGAHLRKEHLEVMREKlPDVFITNHYGMTDT--ACVVSAQNKFTKLGSVGYVS-- 1510
Cdd:PLN02430 371 FLAFRKVKAKLGGRLRL-----LISGGAPLSTEIEEFLRVT-SCAFVVQGYGLTETlgPTTLGFPDEMCMLGTVGAPAvy 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1511 SNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDRISDFINF-R 1589
Cdd:PLN02430 445 NELRLEEVPEMGYDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQ 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1590 SINVSPAEIETVLMTHPAVLQAAVLGipnevDEQHPKAFVVQVPNKSVTEQ 1640
Cdd:PLN02430 524 GEYVALEYLENVYGQNPIVEDIWVYG-----DSFKSMLVAVVVPNEENTNK 569
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
629-1020 |
3.40e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 74.53 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPwdhvVS-----------KLsaRYFLSL 697
Cdd:PRK08180 71 TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAP----VSpayslvsqdfgKL--RHVLEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 698 MSPKVVFVNEESA-ENLMEAAKEENLQVrVMVIGSLPG--FVSLANILEEQVSRAEIDGFRCTkidNPHDLAMICSSSGT 774
Cdd:PRK08180 145 LTPGLVFADDGAAfARALAAVVPADVEV-VAVRGAVPGraATPFAALLATPPTAAVDAAHAAV---GPDTIAKFLFTSGS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 775 TGMPKGTELSYASLYNSITPVEEVHA--KNE---ICAWVPtirWH---GGlNQCIEVIMSN--AKWIifsDD-------- 836
Cdd:PRK08180 221 TGLPKAVINTHRMLCANQQMLAQTFPflAEEppvLVDWLP---WNhtfGG-NHNLGIVLYNggTLYI---DDgkptpggf 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 837 -----NIKEIA-------------LceiiqkhgVTWLGTDTNFA-ILYVKMNIFQkYPMPSLrkmvitGAPFTKELHE-T 896
Cdd:PRK08180 294 detlrNLREISptvyfnvpkgwemL--------VPALERDAALRrRFFSRLKLLF-YAGAAL------SQDVWDRLDRvA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 897 VAKIMPHTQILQCYGLTDAGGLCVSQA-KNSKPGSCGFVTKGIRIKI--ADEKTgialgpkergEICIKSEFMMKGYHKN 973
Cdd:PRK08180 359 EATCGERIRMMTGLGMTETAPSATFTTgPLSRAGNIGLPAPGCEVKLvpVGGKL----------EVRVKGPNVTPGYWRA 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 974 PEQTKEAFDSDGWLHTKDIG-YYDEN----GeIFFVNRIS-DFinykaiKLSS 1020
Cdd:PRK08180 429 PELTAEAFDEEGYYRSGDAVrFVDPAdperG-LMFDGRIAeDF------KLSS 474
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
364-546 |
5.14e-13 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 73.83 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 364 SKPGSCGFVCETGRLKVVDPNTGKVLGANKTG--------------EIWAKSSYMMNGYYnnpEATRRALDSdgwlhTGD 429
Cdd:PRK10524 408 TRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGvlviegplppgcmqTVWGDDDRFVKTYW---SLFGRQVYS-----TFD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 430 LGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFV-----AKVPGKEVT--- 501
Cdd:PRK10524 480 WGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVvpkdsDSLADREARlal 559
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1820754837 502 ELDITDLVKQNMPWYCRlHAGVKFMEKLPRTATGKIAKKQLKQIA 546
Cdd:PRK10524 560 EKEIMALVDSQLGAVAR-PARVWFVSALPKTRSGKLLRRAIQAIA 603
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
207-544 |
6.98e-13 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 73.01 E-value: 6.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 207 IVCSSGTSGFPKGTEISHAAMI---NYMahVKVHDLKGHVSMWTPS--------MRWYCGL------FIVIKAILDCSKR 269
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNLVsftNWM--LEDFALPEGPQFLNQApysfdlsvMDLYPTLasggtlVALPKDMTANFKQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 270 iivpdydddegLCRFIEKYEVS-W-----FrCDSCFpirlvkfgvLSKY----RLPTLKILLFGGAHFKGELQQTLVKLL 339
Cdd:PRK04813 226 -----------LFETLPQLPINvWvstpsF-ADMCL---------LDPSfneeHLPNLTHFLFCGEELPHKTAKKLLERF 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 340 PHTDVILSYGMTDYGG----------LCARQTK----YSKPGScgfvcetgRLKVVDPNtGKVLGANKTGEIWAKSSYMM 405
Cdd:PRK04813 285 PSATIYNTYGPTEATVavtsieitdeMLDQYKRlpigYAKPDS--------PLLIIDEE-GTKLPDGEQGEIVISGPSVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 406 NGYYNNPEATRRAL-DSDGW--LHTGDLGYYDnDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHN 482
Cdd:PRK04813 356 KGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKD 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 483 INEEHAMAFVAKVPGKEVTELDITDLVKQ----NMPWYC--RlhagvKF--MEKLPRTATGKIAKKQLKQ 544
Cdd:PRK04813 435 HKVQYLIAYVVPKEEDFEREFELTKAIKKelkeRLMEYMipR-----KFiyRDSLPLTPNGKIDRKALIE 499
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
365-547 |
1.77e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 72.10 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 365 KPGSC-----GFVCEtgrlkVVDpNTGKVLGANKTGEIWAKSSY--MMNGYYNNPEatrRALDS-----DGWLHTGDLGY 432
Cdd:PRK00174 422 KPGSAtrplpGIQPA-----VVD-EEGNPLEGGEGGNLVIKDPWpgMMRTIYGDHE---RFVKTyfstfKGMYFTGDGAR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 433 YDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKqn 512
Cdd:PRK00174 493 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRN-- 570
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1820754837 513 mpWyCRLHAG-------VKFMEKLPRTATGKIAKKQLKQIAK 547
Cdd:PRK00174 571 --W-VRKEIGpiakpdvIQFAPGLPKTRSGKIMRRILRKIAE 609
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
875-1041 |
1.81e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 71.72 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 875 PMPSLRKMVITGAPFTKELHETVAKIM-PHTQILQCYGLTDAGGLCV----------SQAKNSKPGSC-GFVTKGIRIKI 942
Cdd:cd05910 197 TLPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEALPVSSigsrellattTAATSGGAGTCvGRPIPGVRVRI 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 943 -ADEKTGIA-------LGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDG----WLHTKDIGYYDENGEIFFVNRISDF 1010
Cdd:cd05910 277 iEIDDEPIAewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
170 180 190
....*....|....*....|....*....|.
gi 1820754837 1011 INYKAIKLSSAEIEGVLELHPSILKAVVVPV 1041
Cdd:cd05910 357 VITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1343-1679 |
1.83e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 71.22 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1343 LIVPSSGTTGLPK---------GTEISHY-SLFCClhPYKNRTLVghTCIVTPTMRWHYGVLMAFR-------LVAANAK 1405
Cdd:PRK08308 105 LLQYSSGTTGEPKlirrswteiDREIEAYnEALNC--EQDETPIV--ACPVTHSYGLICGVLAALTrgskpviITNKNPK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1406 KLIVpdnddaenfcQLIEKYQITWFGTDPFMIIkfIKSQLLEKYRLptlKVILSSGAHLRKEHLEVMREKLPDVFitNHY 1485
Cdd:PRK08308 181 FALN----------ILRNTPQHILYAVPLMLHI--LGRLLPGTFQF---HAVMTSGTPLPEAWFYKLRERTTYMM--QQY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1486 GMTDTACV-VSAQNKFTklGSVGYVSSNVRIKMvdldteeALGPNKIGELRVKAitimqgyhknpettkqafdSDGWLRT 1564
Cdd:PRK08308 244 GCSEAGCVsICPDMKSH--LDLGNPLPHVSVSA-------GSDENAPEEIVVKM-------------------GDKEIFT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1565 GDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVVQvpNKSVTEQELIS 1644
Cdd:PRK08308 296 KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVIS--HEEIDPVQLRE 373
|
330 340 350
....*....|....*....|....*....|....*
gi 1820754837 1645 YVEKNLPDYcRLRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK08308 374 WCIQHLAPY-QVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1505-1685 |
1.98e-12 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 72.08 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1505 SVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAF------------------DSDGWLRTGD 1566
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGD 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1567 LAYYDDnGEIYIVDRISDFINFRSINVSPAEIE-TVLMTHPAVLQ--AAVLGIPNEVDEQhpkafVVQVPNKSV--TEQE 1641
Cdd:PRK12476 483 LGVYLD-GELYITGRIADLIVIDGRNHYPQDIEaTVAEASPMVRRgyVTAFTVPAEDNER-----LVIVAERAAgtSRAD 556
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 1642 LISYVEKNLPDYCRlRGGVKIVD-------QLPRTTTGKIARKQLRDMYVN 1685
Cdd:PRK12476 557 PAPAIDAIRAAVSR-RHGLAVADvrlvpagAIPRTTSGKLARRACRAQYLD 606
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
204-479 |
2.28e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 71.34 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 204 VAAIVCSSGTSGFPKGTEISHAaminyMAHVKVHDLK-------GHVSMWT-PsmrwycgLFIVIKAILDCSKriIVPDY 275
Cdd:cd05910 87 PAAILFTSGSTGTPKGVVYRHG-----TFAAQIDALRqlygirpGEVDLATfP-------LFALFGPALGLTS--VIPDM 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 276 D-------DDEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPTLKILLFGGAHFKGELQQTLVKLL-PHTDVILS 347
Cdd:cd05910 153 DptrparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDYGGLC--------ARQTKYSKP--GSC-GFVCETGRLKVVDPNTG--------KVLGANKTGEIWAKSSYMMNGY 408
Cdd:cd05910 233 YGATEALPVSsigsrellATTTAATSGgaGTCvGRPIPGVRVRIIEIDDEpiaewddtLELPRGEIGEITVTGPTVTPTY 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 409 YNNPEATRRALDSDG----WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPV 479
Cdd:cd05910 313 VNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1164-1615 |
2.41e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 72.00 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1164 ILIGKELSIPKRPVNIAEETLKFLKSKPDS--IGQVDALTG---KVqTYADMSERSIKCALWLKKQGVKPGDIIGLCSDN 1238
Cdd:PRK12582 36 IVIKSRHPLGPYPRSIPHLLAKWAAEAPDRpwLAQREPGHGqwrKV-TYGEAKRAVDALAQALLDLGLDPGRPVMILSGN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1239 NLDVFLILLGTMYIGA-----------ISNtwDHEltpmTARNFLTLTSPKIVFTVSSSA-ANLMEAAKELKMNLkVVVM 1306
Cdd:PRK12582 115 SIEHALMTLAAMQAGVpaapvspayslMSH--DHA----KLKHLFDLVKPRVVFAQSGAPfARALAALDLLDVTV-VHVT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1307 DKLDGYESVEENVMKGHDTREIIEFKCHVTNPDDVALIVPSSGTTGLPKGTeISHYSLFCclhpyKNRTLVGHTCIVTPT 1386
Cdd:PRK12582 188 GPGEGIASIAFADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAV-INTQRMMC-----ANIAMQEQLRPREPD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1387 ---------MRWHY--GVLMAFRLVAANAKKLIVpdnDDAENFCQLIEK-----YQI--TWFGTDPF---MIIKFI-KSQ 1444
Cdd:PRK12582 262 ppppvsldwMPWNHtmGGNANFNGLLWGGGTLYI---DDGKPLPGMFEEtirnlREIspTVYGNVPAgyaMLAEAMeKDD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1445 LLEKYRLPTLKVILSSGAHLRKEHLEVMR--------EKLPdvfITNHYGMTDTACVVSAQNKFT-KLGSVGYVSSNVRI 1515
Cdd:PRK12582 339 ALRRSFFKNLRLMAYGGATLSDDLYERMQalavrttgHRIP---FYTGYGATETAPTTTGTHWDTeRVGLIGLPLPGVEL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1516 KMVdldteealgPN--KIgELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYY---DDNGEIYIVD-RISDfiNFR 1589
Cdd:PRK12582 416 KLA---------PVgdKY-EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFvdpDDPEKGLIFDgRVAE--DFK 483
|
490 500 510
....*....|....*....|....*....|.
gi 1820754837 1590 S-----INVSPAEIETVLMTHPAVLQAAVLG 1615
Cdd:PRK12582 484 LstgtwVSVGTLRPDAVAACSPVIHDAVVAG 514
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
602-1100 |
3.08e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.12 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 602 VGELVLNRLSSKPDFVGQIdaFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICP 681
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALV--FGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVP 3174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 682 WDHVVSKLSARYFLslmspkvvfvnEESAENLMEAAKEenlqvrvmVIGSLPGFVSLANILEEQVS-RAEIDGFRCTKID 760
Cdd:PRK12467 3175 LDPEYPRERLAYMI-----------EDSGVKLLLTQAH--------LLEQLPAPAGDTALTLDRLDlNGYSENNPSTRVM 3235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 761 nPHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEVH---AKNEICAWVPtIRWHGGLNQCIEVIMSNAKWIIFSDDN 837
Cdd:PRK12467 3236 -GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYeldANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRDNDL 3313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 838 IKEIALCEIIQKHGVTWLgtdtNFAILYVKMNIFQKYP--MPSLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDA 915
Cdd:PRK12467 3314 WDPEELWQAIHAHRISIA----CFPPAYLQQFAEDAGGadCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEA 3389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 916 GgLCVSQAKNSKPGSCGFVTKGIRIKIADEKTGI---ALGPKERG---EICIKSEFMMKGYHKNPEQTKEAF------DS 983
Cdd:PRK12467 3390 V-VTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVldgQLNPVPVGvagELYIGGVGLARGYHQRPSLTAERFvadpfsGS 3468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 984 DGWLH-TKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELpLAFVQKVVEKEV 1062
Cdd:PRK12467 3469 GGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQL-VAYVVPADPQGD 3547
|
490 500 510
....*....|....*....|....*....|....*...
gi 1820754837 1063 TEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:PRK12467 3548 WRETLRDHLAASLPDY-MVPAQLLVLAAMPLGPNGKVD 3584
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
623-1041 |
3.88e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.12 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLslmspkv 702
Cdd:PRK05691 2209 FAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMI------- 2281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 703 vfvnEESAENLMeaakeenLQVRVM--VIGSLPGFVSLANILEEQVSRAEIDGFRCTKIDNPHDLAMICSSSGTTGMPKG 780
Cdd:PRK05691 2282 ----EDSGIGLL-------LSDRALfeALGELPAGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKG 2350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 781 TELSYASLYNSITPV-EEVHAKNEICAW-VPTIRWHGGLNQCIEVIMSNAKWIIFSDDNIKEIALCEIIQKHGVTWLGTD 858
Cdd:PRK05691 2351 VVVSHGEIAMHCQAViERFGMRADDCELhFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFT 2430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 859 TNFAILYVKMNIFQKYPMPSlrKMVITGA-PFTKELHETVAKIMPHTQILQCYGLTDAGGL-CVSQAKNSKPGSCGFVTK 936
Cdd:PRK05691 2431 PSYGSQLAQWLAGQGEQLPV--RMCITGGeALTGEHLQRIRQAFAPQLFFNAYGPTETVVMpLACLAPEQLEEGAASVPI 2508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 937 GIRIK-----IADEKtgIALGPK-ERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLH-------TKDIGYYDENGEIFF 1003
Cdd:PRK05691 2509 GRVVGarvayILDAD--LALVPQgATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEY 2586
|
410 420 430
....*....|....*....|....*....|....*...
gi 1820754837 1004 VNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPV 1041
Cdd:PRK05691 2587 VGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL 2624
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1202-1679 |
3.93e-12 |
|
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: 70.78 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1202 GKVQTYADMSERSIKCALWLKKQ-GVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIV 1280
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1281 FTvsssAANLMEAAKEL-----KMNLKVVVMDK---LDGYESVEENVMKGHDTREIIEFKCHVTnPDDVALIVPSSGTTG 1352
Cdd:cd05938 83 VV----APELQEAVEEVlpalrADGVSVWYLSHtsnTEGVISLLDKVDAASDEPVPASLRAHVT-IKSPALYIYTSGTTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1353 LPKGTEISHYSLFCCLHPYKNRTLVGHTCIVTPTMRWHY-GVLMAFRLVAANAKKLIVPDNDDAENF---CQlieKYQIT 1428
Cdd:cd05938 158 LPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSsGFLLGIGGCIELGATCVLKPKFSASQFwddCR---KHNVT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1429 wfgtdpfmIIKFIKSQLLEKYRLP------TLKVILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDTAcvVSAQNKFTK 1502
Cdd:cd05938 235 --------VIQYIGELLRYLCNQPqspndrDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGN--IGFFNYTGK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1503 LGSVGYVSSNVR-------IKMvDLDTEEAL----------GPNKIGeLRVKAITIMQ---GYHKNPETTKQ-----AFD 1557
Cdd:cd05938 305 IGAVGRVSYLYKllfpfelIKF-DVEKEEPVrdaqgfcipvAKGEPG-LLVAKITQQSpflGYAGDKEQTEKkllrdVFK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1558 S-DGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGIPNEVDE-QHPKAFVVQVPNK 1635
Cdd:cd05938 383 KgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEgRIGMAAVKLKPGH 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1820754837 1636 SVTEQELISYVEKNLPDYCRLRgGVKIVDQLPRTTTGKIARKQL 1679
Cdd:cd05938 463 EFDGKKLYQHVREYLPAYARPR-FLRIQDSLEITGTFKQQKVRL 505
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
41-542 |
6.16e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.35 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 41 LVLEKLRSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDN 120
Cdd:PRK05691 2193 LFAAQAARTPQAPALTFA--GQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 121 ELSPMTARYFLSLTKPKIVFVNGESAECLAQVVKENNmdtRLVVFADSAGfvgraatltavLRSQDTAwidefECAKLTS 200
Cdd:PRK05691 2271 EYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVA---RWCLEDDAAA-----------LAAYSDA-----PLPFLSL 2331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 201 PKHVAAIVCSSGTSGFPKGTEISHAAMINYMAHV------KVHDLKGHV----------SMWTPSMrwyCGLFIVIKAil 264
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVierfgmRADDCELHFysinfdaaseRLLVPLL---CGARVVLRA-- 2406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 265 dcskriivPDYDDDEGLCRFIEKYEVSWFRCDSCFPIRLVKFGVLSKYRLPtLKILLFGGAHFKGELQQTLVKLLPHTDV 344
Cdd:PRK05691 2407 --------QGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLP-VRMCITGGEALTGEHLQRIRQAFAPQLF 2477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 345 ILSYGMTDygglcarqtKYSKPGSC--GFVCETGRL-----KVVDPNTGKVLGAN-------KTGEIWAKSSYMMNGYYN 410
Cdd:PRK05691 2478 FNAYGPTE---------TVVMPLAClaPEQLEEGAAsvpigRVVGARVAYILDADlalvpqgATGELYVGGAGLAQGYHD 2548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 411 NPEATRRALDSDGWLH-------TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNI 483
Cdd:PRK05691 2549 RPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPS 2628
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 484 NEEHAMAFVAKVPGKEVTELD-----ITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:PRK05691 2629 GKQLAGYLVSAVAGQDDEAQAalreaLKAHLKQQLPDY-MVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
603-1040 |
6.43e-12 |
|
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: 70.00 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 603 GELVLNRLSSKPDFVGQIdaFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPW 682
Cdd:cd17646 1 HALVAEQAARTPDAPAVV--DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 683 D--HVVSKLSarYFLSLMSPKVVFVNEESAENLMEAAkeenlqvrVMVIGSLPGFVSLANILEEQVSRaeidgfrctkid 760
Cdd:cd17646 79 DpgYPADRLA--YMLADAGPAVVLTTADLAARLPAGG--------DVALLGDEALAAPPATPPLVPPR------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 761 nPHDLAMICSSSGTTGMPKGTELSYASLYN---------SITPVEEVHAK---------NEIcaWVPtirwhgglnqcie 822
Cdd:cd17646 137 -PDNLAYVIYTSGSTGRPKGVMVTHAGIVNrllwmqdeyPLGPGDRVLQKtplsfdvsvWEL--FWP------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 823 vIMSNAKWIIFSDDNIKEIA-LCEIIQKHGVTwlgtdtnfAILYVK--MNIFQKYP----MPSLRKMVITGAPFTKELHE 895
Cdd:cd17646 201 -LVAGARLVVARPGGHRDPAyLAALIREHGVT--------TCHFVPsmLRVFLAEPaagsCASLRRVFCSGEALPPELAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 896 TVAKiMPHTQILQCYGLTDAGgLCVSQAKNSKPGSCGFVTKG-----IRIKIADEktgiALGPKERG---EICIKSEFMM 967
Cdd:cd17646 272 RFLA-LPGAELHNLYGPTEAA-IDVTHWPVRGPAETPSVPIGrpvpnTRLYVLDD----ALRPVPVGvpgELYLGGVQLA 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 968 KGYHKNPEQTKEAFDSDGWLH------TKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVP 1040
Cdd:cd17646 346 RGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVA 424
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
50-542 |
7.25e-12 |
|
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: 69.59 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 50 PEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARY 129
Cdd:cd17652 1 PDAPAVVFG--DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 130 FLSLTKPKIVfvngesaeclaqvvkennmdtrlvvfadsagfvgraatltavlrsqdtawidefecakLTSPKHVAAIVC 209
Cdd:cd17652 79 MLADARPALL----------------------------------------------------------LTTPDNLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 210 SSGTSGFPKGTEISHAAMINYMA-HVKVHDLkghvsmwTPSMRW-------YCGLFIVIKAILDCSKRIIVPDYDD---D 278
Cdd:cd17652 101 TSGSTGRPKGVVVTHRGLANLAAaQIAAFDV-------GPGSRVlqfaspsFDASVWELLMALLAGATLVLAPAEEllpG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 279 EGLCRFIEKYEVSWFrcdSCFPIRLvkfGVLSKYRLPTLKILLFGGAHFKGELQQTLVkllPHTDVILSYGMTDyGGLCA 358
Cdd:cd17652 174 EPLADLLREHRITHV---TLPPAAL---AALPPDDLPDLRTLVVAGEACPAELVDRWA---PGRRMINAYGPTE-TTVCA 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 359 rqtKYSKPGSCGFVCETGRlkvVDPNT-GKVLGAN-------KTGEIWAKSSYMMNGYYNNPEATR-RAL-----DSDGW 424
Cdd:cd17652 244 ---TMAGPLPGGGVPPIGR---PVPGTrVYVLDARlrpvppgVPGELYIAGAGLARGYLNRPGLTAeRFVadpfgAPGSR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 425 LH-TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTEL 503
Cdd:cd17652 318 MYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAA 397
|
490 500 510
....*....|....*....|....*....|....*....
gi 1820754837 504 DITDLVKQNMPWYCrLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:cd17652 398 ELRAHLAERLPGYM-VPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
378-486 |
8.91e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 69.97 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 378 LKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALD------SDG-----WLHTGDLGYYDnDGEVFLVDRMS 446
Cdd:PRK05850 381 VRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpSPGtpegpWLRTGDLGFIS-EGELFIVGRIK 459
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1820754837 447 EFINYRAIKISPAEIEALIQQhpavF---QVAVVPVPHNINEE 486
Cdd:PRK05850 460 DLLIVDGRNHYPDDIEATIQE----ItggRVAAISVPDDGTEK 498
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
381-544 |
9.77e-12 |
|
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: 69.38 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 381 VDPNTGKVLGANKTG---------------EIWAKSSYMMNGYYNNPEATRRAL------DSDGWLHTGDLGYYDNDGEV 439
Cdd:cd05937 275 MDPETDDPIRDPKTGfcvrapvgepgemlgRVPFKNREAFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRW 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 440 FLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAV--VPVPHNINEEHAMAFVAKVPGKEVTELD---ITDLVKQNMP 514
Cdd:cd05937 355 YFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITLEESSAVPTEFTkslLASLARKNLP 434
|
170 180 190
....*....|....*....|....*....|
gi 1820754837 515 WYCrLHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:cd05937 435 SYA-VPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
600-1044 |
9.79e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 69.65 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 600 ANVGELVLNRLSSKPDFVGQIDAFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGII 679
Cdd:PRK05857 14 STVLDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 680 CPWDHVVSKLSARYFLSLMSPKVVFVNEESAENlMEAAKEENLQVRVMVIGSLPGFVSLANILEEQVSRAEIDgfrcTKI 759
Cdd:PRK05857 94 VMADGNLPIAAIERFCQITDPAAALVAPGSKMA-SSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNAD----QGS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 760 DNPhdLAMIcSSSGTTGMPKGTELSYASLYnSITPVeevhAKNEICAWV----------PTIRWH-GGLNQCIEVIMSNA 828
Cdd:PRK05857 169 EDP--LAMI-FTSGTTGEPKAVLLANRTFF-AVPDI----LQKEGLNWVtwvvgettysPLPATHiGGLWWILTCLMHGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 829 KWIIFSDDNIkeiALCEIIQKHGV-TWLGTDTNFAILYVKMNiFQKYPMPSLRKMVITGapfTKELHETVAKI-MPHTQI 906
Cdd:PRK05857 241 LCVTGGENTT---SLLEILTTNAVaTTCLVPTLLSKLVSELK-SANATVPSLRLVGYGG---SRAIAADVRFIeATGVRT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 907 LQCYGLTDAG--GLCVSQAKNS----KPGSCGFVTKGIRIKIADEKTGialGPKER--------GEICIKSEFMMKGYHK 972
Cdd:PRK05857 314 AQVYGLSETGctALCLPTDDGSivkiEAGAVGRPYPGVDVYLAATDGI---GPTAPgagpsasfGTLWIKSPANMLGYWN 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 973 NPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHE 1044
Cdd:PRK05857 391 NPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDE 461
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
368-540 |
1.15e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 69.77 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 368 SCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRR------------------ALDSDGWLHTGD 429
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERtfgaklqsrlaegshadgAADDGTWLRTGD 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 430 LGYYdNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQ-HPAVFQ--VAVVPVPHNINEEhaMAFVA-KVPGKEVTE-LD 504
Cdd:PRK12476 483 LGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRRgyVTAFTVPAEDNER--LVIVAeRAAGTSRADpAP 559
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1820754837 505 ITDLVKQNMpwyCRLH----AGVKFMEK--LPRTATGKIAKK 540
Cdd:PRK12476 560 AIDAIRAAV---SRRHglavADVRLVPAgaIPRTTSGKLARR 598
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
47-429 |
1.15e-11 |
|
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: 69.38 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPE--FIAQVEAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELS 123
Cdd:cd05921 6 RQAPDrtWLAEREGNGGWRRvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 124 PMTA-----RYFLSLTKPKIVFVngESAECLAQVVKENNMDTRLVVFADSAGFVGRAATLTAVLRSQDTAWIDEFECAkl 198
Cdd:cd05921 86 LMSQdlaklKHLFELLKPGLVFA--QDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAAFAA-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 199 TSPKHVAAIVCSSGTSGFPKGTEISHAAM---INYMAHVKVhDLKGHVSMWTPSMRW--YCGLFIVIKAIL--------D 265
Cdd:cd05921 162 VGPDTVAKFLFTSGSTGLPKAVINTQRMLcanQAMLEQTYP-FFGEEPPVLVDWLPWnhTFGGNHNFNLVLynggtlyiD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 266 CSK-------------RIIVPDY---------------DDDEGLCRfiekyevSWFRcdscfpirlvkfgvlskyrlpTL 317
Cdd:cd05921 241 DGKpmpggfeetlrnlREISPTVyfnvpagwemlvaalEKDEALRR-------RFFK---------------------RL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 318 KILLFGGA----HFKGELQQTLVKLLPHTDVILS-YGMTDYGGLCARQTK-YSKPGSCGFVCETGRLKVVdPNTGKVlga 391
Cdd:cd05921 293 KLMFYAGAglsqDVWDRLQALAVATVGERIPMMAgLGATETAPTATFTHWpTERSGLIGLPAPGTELKLV-PSGGKY--- 368
|
410 420 430
....*....|....*....|....*....|....*...
gi 1820754837 392 nktgEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGD 429
Cdd:cd05921 369 ----EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGD 402
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
625-1042 |
1.27e-11 |
|
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: 68.92 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 625 GKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVF 704
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 705 VneesaenlmeaakeenlqvrvmvigslpgfvslanileeqvsraeidgfrctkidnphDLAMICSSSGTTGMPKGTELS 784
Cdd:cd05940 81 V----------------------------------------------------------DAALYIYTSGTTGLPKAAIIS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 785 YASLYNSITPV--------EEV--------HAKNEICAWVptirwhgglnqciEVIMSNAKWII--------FSDDNIKE 840
Cdd:cd05940 103 HRRAWRGGAFFagsggalpSDVlytclplyHSTALIVGWS-------------ACLASGATLVIrkkfsasnFWDDIRKY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 841 iaLCEIIQKHGvtwlgtdtnfAILYVKMNIFQKypmPSLRK---MVITGAPFTKELHETVAKIMPHTQILQCYGLTDagG 917
Cdd:cd05940 170 --QATIFQYIG----------ELCRYLLNQPPK---PTERKhkvRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATE--G 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 918 LCVSQAKNSKPGSCGF----VTKGIRIKIA--DEKTG----------IALGPKERGE----ICIKSEFmmKGYHKNPEQT 977
Cdd:cd05940 233 NSGFINFFGKPGAIGRnpslLRKVAPLALVkyDLESGepirdaegrcIKVPRGEPGLlisrINPLEPF--DGYTDPAATE 310
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 978 K----EAF-DSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVV--VPVP 1042
Cdd:cd05940 311 KkilrDVFkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVP 382
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1510-1601 |
1.28e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 69.20 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1510 SSNVRIkmVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAFD------SDG-----WLRTGDLAYYDDnGEIYI 1578
Cdd:PRK05850 378 SPTVRI--VDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpSPGtpegpWLRTGDLGFISE-GELFI 454
|
90 100
....*....|....*....|....
gi 1820754837 1579 VDRISDFINFRSINVSPAEIE-TV 1601
Cdd:PRK05850 455 VGRIKDLLIVDGRNHYPDDIEaTI 478
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
730-1009 |
1.38e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 69.16 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 730 GSLPGFVSLANIleEQVSRAEidGFRCTKIDnPHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEV--HAKNEI--- 804
Cdd:PRK09274 146 RLLWGGTTLATL--LRDGAAA--PFPMADLA-PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDygIEPGEIdlp 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 805 --------------CAWVPTI---RwhgglnqcieVIMSNAKWIIfsddnikeialcEIIQKHGVTWLgtdtnFA--ILY 865
Cdd:PRK09274 221 tfplfalfgpalgmTSVIPDMdptR----------PATVDPAKLF------------AAIERYGVTNL-----FGspALL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 866 VKMNIF---QKYPMPSLRKMVITGAPFTKELHETVAKIMPH-TQILQCYGLTDAGGLCV----------SQAKNSKPGSC 931
Cdd:PRK09274 274 ERLGRYgeaNGIKLPSLRRVISAGAPVPIAVIERFRAMLPPdAEILTPYGATEALPISSiesreilfatRAATDNGAGIC 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 932 -GFVTKGIRIKIADEKTG-IA-------LGPKERGEICIKSEFMMKGYHKNPEQTKEA--FDSDG--WLHTKDIGYYDEN 998
Cdd:PRK09274 354 vGRPVDGVEVRIIAISDApIPewddalrLATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQ 433
|
330
....*....|.
gi 1820754837 999 GEIFFVNRISD 1009
Cdd:PRK09274 434 GRLWFCGRKAH 444
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
910-1099 |
1.40e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 68.94 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 910 YGLTDaGGLCVSQAKNSKPGSCGFVTKGIriKIADEKTGIALGPKER------------GEIC-IKSEFMMKGYHKNPEQ 976
Cdd:PRK07867 297 FGSTE-GGVAITRTPDTPPGALGPLPPGV--AIVDPDTGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 977 TKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHET----------- 1045
Cdd:PRK07867 374 DAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVvgdqvmaalvl 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1046 --DIEL-PLAFVQkvvekevteeELH---DLVNKNLPWYcklqagIKFVNDFPRISTGKI 1099
Cdd:PRK07867 453 apGAKFdPDAFAE----------FLAaqpDLGPKQWPSY------VRVCAELPRTATFKV 496
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
629-1100 |
1.41e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.01 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGIL---TENHLNTCVPVLAIlyigGIICpwdHVVSklsARYF-------LSLM 698
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI----GAIC---HTVN---PRLFpeqiawiINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 699 SPKVVFVNEESAEnLMEAAKEENLQVRVMVI---------GSLPGFVSLANILEEQvsraeiDG-FRCTKIDNPHDLAMi 768
Cdd:PRK06018 111 EDRVVITDLTFVP-ILEKIADKLPSVERYVVltdaahmpqTTLKNAVAYEEWIAEA------DGdFAWKTFDENTAAGM- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 769 CSSSGTTGMPKGTELSYAS--LYNSITPVEEV---HAKNEICAWVPTIR---WhgGLNQC-----IEVIMSNAKwiifsd 835
Cdd:PRK06018 183 CYTSGTTGDPKGVLYSHRSnvLHALMANNGDAlgtSAADTMLPVVPLFHansW--GIAFSapsmgTKLVMPGAK------ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 836 dnIKEIALCEIIQKHGVTW-LGTDTNFAILYVKMNIfQKYPMPSLRKMVITGAPFTKELHETVAKImpHTQILQCYGLTD 914
Cdd:PRK06018 255 --LDGASVYELLDTEKVTFtAGVPTVWLMLLQYMEK-EGLKLPHLKMVVCGGSAMPRSMIKAFEDM--GVEVRHAWGMTE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 915 A---GGLCVSQAKNSK-PGSC--------GFVTKGIRIKIAD-EKTGIALGPKERGEICIKSEFMMKGYHKnpeQTKEAF 981
Cdd:PRK06018 330 MsplGTLAALKPPFSKlPGDArldvlqkqGYPPFGVEMKITDdAGKELPWDGKTFGRLKVRGPAVAAAYYR---VDGEIL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 982 DSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKE 1061
Cdd:PRK06018 407 DDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGET 486
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1820754837 1062 VTEEELHDLVN-KNLPWYckLQAGIKFVNDFPRISTGKID 1100
Cdd:PRK06018 487 ATREEILKYMDgKIAKWW--MPDDVAFVDAIPHTATGKIL 524
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1206-1679 |
2.36e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.43 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLT-SPKIVFTvs 1284
Cdd:PRK05691 3747 SYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSrTPVLVCS-- 3824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1285 ssaANLMEAAKELKMNLKVVVMDKLDGYESVEENVMKGHDTREiiefkchVTNPDDVALIVPSSGTTGLPKGTEISHYSL 1364
Cdd:PRK05691 3825 ---AACREQARALLDELGCANRPRLLVWEEVQAGEVASHNPGI-------YSGPDNLAYVIYTSGSTGLPKGVMVEQRGM 3894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1365 F---CCLHPYKNrtLVGHTCIV-TPTMRWHYGVlmaFRLVAA---NAKKLIVPdNDDAENFCQLIEKYQ---ITWFGTDP 1434
Cdd:PRK05691 3895 LnnqLSKVPYLA--LSEADVIAqTASQSFDISV---WQFLAAplfGARVEIVP-NAIAHDPQGLLAHVQaqgITVLESVP 3968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1435 FMIIKFIKSqllEKYRLPTLKVILSSGAHLRKEHLEVMREKLPDVFITNHYG---MTDTACVVSAQNKFTKlGS---VGY 1508
Cdd:PRK05691 3969 SLIQGMLAE---DRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGpaeCSDDVAFFRVDLASTR-GSylpIGS 4044
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1509 VSSNVRIKMvdLDTEEALGP-NKIGELRVKAITIMQGYHKNPETTKQAF-------DSDGWLRTGDLAYYDDNGEIYIVD 1580
Cdd:PRK05691 4045 PTDNNRLYL--LDEALELVPlGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVG 4122
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1581 RISDFINFRSINVSPAEIETVLMTHPAVLQAAVlGIPNEVDEQHPKAFVvqVPNKSVTEQ-ELISYVEK----NLPDYcR 1655
Cdd:PRK05691 4123 RIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYL--VPHQTVLAQgALLERIKQrlraELPDY-M 4198
|
490 500
....*....|....*....|....
gi 1820754837 1656 LRGGVKIVDQLPRTTTGKIARKQL 1679
Cdd:PRK05691 4199 VPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
614-1036 |
2.91e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 68.15 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 614 PD--FVGQIDAFTG--KECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKL 689
Cdd:PRK12582 63 PDrpWLAQREPGHGqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLM 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 690 SA-----RYFLSLMSPKVVFVNEESA-ENLMEAAKEENLQVrVMVIGSLPGFVSLAniLEEQVSRAEIDGFRcTKID--N 761
Cdd:PRK12582 143 SHdhaklKHLFDLVKPRVVFAQSGAPfARALAALDLLDVTV-VHVTGPGEGIASIA--FADLAATPPTAAVA-AAIAaiT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 762 PHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEVHAKNEICA------WVPtirWH---GGlNQCIEVIMSNAK--W 830
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPppvsldWMP---WNhtmGG-NANFNGLLWGGGtlY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 831 IifsDD-------------NIKEIAlceiiqkhGVTWLGTDTNFAILYVKM--------NIFQKypmpsLRKMVITGAPF 889
Cdd:PRK12582 295 I---DDgkplpgmfeetirNLREIS--------PTVYGNVPAGYAMLAEAMekddalrrSFFKN-----LRLMAYGGATL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 890 TKELHE-----TVAKIMPHTQILQCYGLTDAGGLCVSQAKNS-KPGSCGFVTKGIRIKIAdektgiALGPKErgEICIKS 963
Cdd:PRK12582 359 SDDLYErmqalAVRTTGHRIPFYTGYGATETAPTTTGTHWDTeRVGLIGLPLPGVELKLA------PVGDKY--EVRVKG 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 964 EFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYY----DENGEIFFVNRIS-DFinykaiKLSSAEIEGVLELHPSILKA 1036
Cdd:PRK12582 431 PNVTPGYHKDPELTAAAFDEEGFYRLGDAARFvdpdDPEKGLIFDGRVAeDF------KLSTGTWVSVGTLRPDAVAA 502
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
771-1099 |
3.41e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 67.37 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 771 SSGTTGMPKGTELSYASL------YNSITPVEEV----------HAKNEICawvptirwhgGLNQCIEvimSNAKWIIFS 834
Cdd:PRK08308 109 SSGTTGEPKLIRRSWTEIdreieaYNEALNCEQDetpivacpvtHSYGLIC----------GVLAALT---RGSKPVIIT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 835 DDNIKEIalceiIQKHgvtwlgTDTNFAILYvkmnifqkyPMPSLRKMVITGAPFTKELHE--TVAKIMPH--------- 903
Cdd:PRK08308 176 NKNPKFA-----LNIL------RNTPQHILY---------AVPLMLHILGRLLPGTFQFHAvmTSGTPLPEawfyklrer 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 904 -TQILQCYGLTDAGglCVSQAKN-SKPGSCGFVTKGIRIKIADektgialGPKERGEICIKsefmmkgyhkNPEQTkeaf 981
Cdd:PRK08308 236 tTYMMQQYGCSEAG--CVSICPDmKSHLDLGNPLPHVSVSAGS-------DENAPEEIVVK----------MGDKE---- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 982 dsdgwLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHetdielPLA----FVQKV 1057
Cdd:PRK08308 293 -----IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKD------PVAgervKAKVI 361
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1820754837 1058 VEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKI 1099
Cdd:PRK08308 362 SHEEIDPVQLREWCIQHLAPY-QVPHEIESVTEIPKNANGKV 402
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
627-1054 |
3.98e-11 |
|
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: 68.07 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 627 ECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGI--ICPWDHVVSKLSARyfLSLMSPKVVF 704
Cdd:cd05943 98 EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIwsSCSPDFGVPGVLDR--FGQIEPKVLF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 705 VNEESAENLMEAAKEENLQVrvmVIGSLPGFVSLAnILEEQVSRAEIDGfrcTKIDNPHDLA------------------ 766
Cdd:cd05943 176 AVDAYTYNGKRHDVREKVAE---LVKGLPSLLAVV-VVPYTVAAGQPDL---SKIAKALTLEdflatgaagelefeplpf 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 767 ----MICSSSGTTGMPK-------GTELSYAS---LYNSITPVEEVHakneicaWVPTIRWhgglnqcievIMSNakWII 832
Cdd:cd05943 249 dhplYILYSSGTTGLPKcivhgagGTLLQHLKehiLHCDLRPGDRLF-------YYTTCGW----------MMWN--WLV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 833 -----------------FSDDNikeiALCEIIQKHGVTWLGTDTNFAILYVKMNIFQK--YPMPSLRKMVITGAPFTKEL 893
Cdd:cd05943 310 sglavgativlydgspfYPDTN----ALWDLADEEGITVFGTSAKYLDALEKAGLKPAetHDLSSLRTILSTGSPLKPES 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 894 HETV-AKIMPHTQILQCYGLTDAGGLCVSQAKNSK--PGSCGFVTKGIRIKIADEKTGIALGPKerGEICIKSEF--MMK 968
Cdd:cd05943 386 FDYVyDHIKPDVLLASISGGTDIISCFVGGNPLLPvyRGEIQCRGLGMAVEAFDEEGKPVWGEK--GELVCTKPFpsMPV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 969 GYHKNPEQTK--EA-FDS-DG-WLHtKDIGYYDENGEIFFVNRiSD-FINYKAIKLSSAEIEGVLELHPSILKAVVVPVP 1042
Cdd:cd05943 464 GFWNDPDGSRyrAAyFAKyPGvWAH-GDWIEITPRGGVVILGR-SDgTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQE 541
|
490
....*....|...
gi 1820754837 1043 HE-TDIELPLaFV 1054
Cdd:cd05943 542 WKdGDERVIL-FV 553
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
629-1038 |
4.96e-11 |
|
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: 67.46 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSA-----RYFLSLMSPKVV 703
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQdlaklKHLFELLKPGLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 704 FVneESAENLMEAAKE-ENLQVRVMVIGSLP---GFVSLANILEEQVSRAEIDGFRCTkidNPHDLAMICSSSGTTGMPK 779
Cdd:cd05921 107 FA--QDAAPFARALAAiFPLGTPLVVSRNAVagrGAISFAELAATPPTAAVDAAFAAV---GPDTVAKFLFTSGSTGLPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 780 GTELSYASLYNSITPVEEVHA--KNE---ICAWVPTIRWHGGlNQCIEVIMSNAKWIIFSD------------DNIKEIA 842
Cdd:cd05921 182 AVINTQRMLCANQAMLEQTYPffGEEppvLVDWLPWNHTFGG-NHNFNLVLYNGGTLYIDDgkpmpggfeetlRNLREIS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 843 lceiiqkhgVTWLGT-DTNFAILYVKM--------NIFQKypmpsLRKMVITGAPFTKELHETVAKI-MPHT----QILQ 908
Cdd:cd05921 261 ---------PTVYFNvPAGWEMLVAALekdealrrRFFKR-----LKLMFYAGAGLSQDVWDRLQALaVATVgeriPMMA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 909 CYGLTDAGGLC-VSQAKNSKPGSCGFVTKGIRIKI--ADEKTgialgpkergEICIKSEFMMKGYHKNPEQTKEAFDSDG 985
Cdd:cd05921 327 GLGATETAPTAtFTHWPTERSGLIGLPAPGTELKLvpSGGKY----------EVRVKGPNVTPGYWRQPELTAQAFDEEG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 986 WLHTKDIGYY----DENGEIFFVNRIS-DFinykaiKLSSA--------EIEGVLELHPSILKAVV 1038
Cdd:cd05921 397 FYCLGDAAKLadpdDPAKGLVFDGRVAeDF------KLASGtwvsvgplRARAVAACAPLVHDAVV 456
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
629-1042 |
5.42e-11 |
|
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: 67.48 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLR-KHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDHVVSKLSARYFLSLMSPKVVFVNE 707
Cdd:cd17632 69 TYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 708 ESAENLMEAAKEENLQVRVMVIG-----------------SLPGFVSLANILEEQVSRAE--IDGFRCTKIDNPHDLAMI 768
Cdd:cd17632 149 EHLDLAVEAVLEGGTPPRLVVFDhrpevdahraalesareRLAAVGIPVTTLTLIAVRGRdlPPAPLFRPEPDDDPLALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 769 CSSSGTTGMPKG---TELSYASLYNSITPVEEVHAKNEICAWVPTIRWHGGLNQCIEVIMSN--AKWIIFSD-----DNI 838
Cdd:cd17632 229 IYTSGSTGTPKGamyTERLVATFWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGgtAYFAAASDmstlfDDL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 839 -----KEIAL----CEII-QKHG--VTWL---GTDTNFAILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMpH 903
Cdd:cd17632 309 alvrpTELFLvprvCDMLfQRYQaeLDRRsvaGADAETLAERVKAELRERVLGGRLLAAVCGSAPLSAEMKAFMESLL-D 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 904 TQILQCYGLTDAGGLCVSQAKNSKPgscgfVTKGIRIKIADektgiaLG------PKERGEICIKSEFMMKGYHKNPEQT 977
Cdd:cd17632 388 LDLHDGYGSTEAGAVILDGVIVRPP-----VLDYKLVDVPE------LGyfrtdrPHPRGELLVKTDTLFPGYYKRPEVT 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 978 KEAFDSDGWLHTKDIGYYDENGEIFFVNRISDfinykAIKLSSAE------IEGVLELHP-------------SILKAVV 1038
Cdd:cd17632 457 AEVFDEDGFYRTGDVMAELGPDRLVYVDRRNN-----VLKLSQGEfvtvarLEAVFAASPlvrqifvygnserAYLLAVV 531
|
....
gi 1820754837 1039 VPVP 1042
Cdd:cd17632 532 VPTQ 535
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
905-1044 |
5.85e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 66.97 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 905 QILQCYGLTDaGGLCVSQAKNSKPGSCGFVTKGIRIKIADEKT----------GIALGPKER-GEICIKS-EFMMKGYHK 972
Cdd:PRK13388 290 QVEDGYGSSE-GAVIVVREPGTPPGSIGRGAPGVAIYNPETLTecavarfdahGALLNADEAiGELVNTAgAGFFEGYYN 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 973 NPEQTKEAFdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHE 1044
Cdd:PRK13388 369 NPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
378-544 |
5.95e-11 |
|
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: 67.13 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 378 LKVVDpNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNdGEVFLVDRMSEFINYRAIKIS 457
Cdd:cd05908 325 IRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRN-GRLVITGREKDIIFVNGQNVY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 458 PAEIEALIQQHPAVF--QVAVVPVpHNIN--EEHAMAFVAKvpGKEVTEL-----DITDLVKQNMPWycRLHAgVKFMEK 528
Cdd:cd05908 403 PHDIERIAEELEGVElgRVVACGV-NNSNtrNEEIFCFIEH--RKSEDDFyplgkKIKKHLNKRGGW--QINE-VLPIRR 476
|
170
....*....|....*.
gi 1820754837 529 LPRTATGKIAKKQLKQ 544
Cdd:cd05908 477 IPKTTSGKVKRYELAQ 492
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1454-1581 |
9.45e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 66.58 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1454 LKVILSSGAHLrKEHLEVMREKLPDVFITNHYGMTDT--ACVVSAQNKFTKLGSVGYVSSNVRIKMVDLDTEE--ALGPN 1529
Cdd:PLN02614 388 VRIILSGAAPL-ASHVESFLRVVACCHVLQGYGLTEScaGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEydALAST 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 1530 KIGELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDR 1581
Cdd:PLN02614 467 PRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDR 517
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1457-1581 |
9.51e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 66.79 E-value: 9.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1457 ILSSGAHLRKEHLEVMREKLPDVFITNHYGMTDT--ACVVSAQNKFTKLGSVG--YVSSNVRIKMVDLDTEEALGPNKIG 1532
Cdd:PLN02861 387 LLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEScgGCFTSIANVFSMVGTVGvpMTTIEARLESVPEMGYDALSDVPRG 466
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1820754837 1533 ELRVKAITIMQGYHKNPETTKQAFdSDGWLRTGDLAYYDDNGEIYIVDR 1581
Cdd:PLN02861 467 EICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDR 514
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
759-1046 |
9.79e-11 |
|
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: 66.27 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 759 IDNPHDLAMICSSSGTTGMPKGTELSYASLYNSITPVEEV--------HAKNEICAWV--PTIRwhgglnQCIEVIMSNA 828
Cdd:cd17648 90 ITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERyfgrdngdEAVLFFSNYVfdFFVE------QMTLALLNGQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 829 KWIIFSD-DNIKEIALCEIIQKHGVTWL-GTDTnfailyvkmnIFQKYPM---PSLRKMVITGAPFTKELHETVAKIMPh 903
Cdd:cd17648 164 KLVVPPDeMRFDPDRFYAYINREKVTYLsGTPS----------VLQQYDLarlPHLKRVDAAGEEFTAPVFEKLRSRFA- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 904 TQILQCYGLTDAGglcVSQAKNSKPGSCGFvTKGIRIKIADEKTGIaLGPKER-------GEICIKSEFMMKGYHKNPEQ 976
Cdd:cd17648 233 GLIINAYGPTETT---VTNHKRFFPGDQRF-DKSLGRPVRNTKCYV-LNDAMKrvpvgavGELYLGGDGVARGYLNRPEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 977 TKEAF-------DSDGWL-------HTKDIGYYDENGEIFFVNRiSDF-INYKAIKLSSAEIEGVLELHPSILKAVVVPV 1041
Cdd:cd17648 308 TAERFlpnpfqtEQERARgrnarlyKTGDLVRWLPSGELEYLGR-NDFqVKIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
....*
gi 1820754837 1042 PHETD 1046
Cdd:cd17648 387 EDASQ 391
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
931-1011 |
1.38e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 66.18 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 931 CGFVTKGIRIKIADEkTGIALGPKERGEICIKSEFMMKGYHKNPEQTKeAFDSDGWLHTKDIGYYdENGEIFFVNRISDF 1010
Cdd:PRK09192 387 CGKALPGHEIEIRNE-AGMPLPERVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLGYL-LDGYLYITGRAKDL 463
|
.
gi 1820754837 1011 I 1011
Cdd:PRK09192 464 I 464
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1206-1615 |
1.50e-10 |
|
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: 65.94 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLK-KQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPKIVftvS 1284
Cdd:cd17632 69 TYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL---A 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1285 SSAANL---MEAAKELKMNLKVVVMD---KLD------------------GYESVEENVMKGHDTREIIEFkCHVTNPDD 1340
Cdd:cd17632 146 VSAEHLdlaVEAVLEGGTPPRLVVFDhrpEVDahraalesarerlaavgiPVTTLTLIAVRGRDLPPAPLF-RPEPDDDP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1341 VALIVPSSGTTGLPKG---TE--ISHYSLfcclhpyKNRTLVGHTCIVTPTMR-----------WHYGVLM----AFRLV 1400
Cdd:cd17632 225 LALLIYTSGSTGTPKGamyTErlVATFWL-------KVSSIQDIRPPASITLNfmpmshiagriSLYGTLArggtAYFAA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1401 AANAKKL-------------IVPdnddaeNFCQLI-EKYQIT-----WFGTDPFMIIKFIKSQLLEKYRLPTLKVILSSG 1461
Cdd:cd17632 298 ASDMSTLfddlalvrptelfLVP------RVCDMLfQRYQAEldrrsVAGADAETLAERVKAELRERVLGGRLLAAVCGS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1462 AHLRKEhLEVMREKLPDVFITNHYGMTDtACVVSAQNKFTKLGSVGYvssnvriKMVDLdteEALG------PNKIGELR 1535
Cdd:cd17632 372 APLSAE-MKAFMESLLDLDLHDGYGSTE-AGAVILDGVIVRPPVLDY-------KLVDV---PELGyfrtdrPHPRGELL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1536 VKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDRISDFIN-----FrsinVSPAEIETVLMTHPAVLQ 1610
Cdd:cd17632 440 VKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKlsqgeF----VTVARLEAVFAASPLVRQ 515
|
....*
gi 1820754837 1611 AAVLG 1615
Cdd:cd17632 516 IFVYG 520
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
64-542 |
2.64e-10 |
|
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: 64.80 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 64 TTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNG 143
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 144 EsaeclaqvvkennmdtrlvvfadsagfvgraatltavLRSQDTAWIDEFECAKLTSPKHVAAIVCSSGTSGFPKGTEIS 223
Cdd:cd17654 97 E-------------------------------------LDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 224 HAAMINYMAHVKVhdlkghVSMWTPSMRWYCGLFI--------VIKAILDCSKRIIVPDYDDDEGLCrfIEKYEVSWFRC 295
Cdd:cd17654 140 HKCILPNIQHFRS------LFNITSEDILFLTSPLtfdpsvveIFLSLSSGATLLIVPTSVKVLPSK--LADILFKRHRI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 296 DSC---------FPIRLVKFGVLSkyRLPTLKILLFGGAHFKGE-LQQTLVKLLPHTDVILSYGMTDYG--GLCARQTKY 363
Cdd:cd17654 212 TVLqatptlfrrFGSQSIKSTVLS--ATSSLRVLALGGEPFPSLvILSSWRGKGNRTRIFNIYGITEVScwALAYKVPEE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 364 SKPGSCGFVCETGRLKVVDPNTGKVLGANKTGEIwaKSSYMMNGYYNNPEATRRAldsdgwlhTGDLgYYDNDGEVFLVD 443
Cdd:cd17654 290 DSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGL--NRVCILDDEVTVPKGTMRA--------TGDF-VTVKDGELFFLG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 444 RMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPvphnINEEHAMAFVAKVPGKEVT--ELDITDLVKQNMPWYcrlha 521
Cdd:cd17654 359 RKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTL----SDQQRLIAFIVGESSSSRIhkELQLTLLSSHAIPDT----- 429
|
490 500
....*....|....*....|.
gi 1820754837 522 gVKFMEKLPRTATGKIAKKQL 542
Cdd:cd17654 430 -FVQIDKLPLTSHGKVDKSEL 449
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
395-494 |
3.04e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 65.00 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 395 GEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDR--------MSEFINYRAikispaeIEALIQ 466
Cdd:PTZ00216 508 GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRvkalakncLGEYIALEA-------LEALYG 580
|
90 100 110
....*....|....*....|....*....|....*...
gi 1820754837 467 QHPAVFQ--VAVVPVPHN--------INEEHAMAFVAK 494
Cdd:PTZ00216 581 QNELVVPngVCVLVHPARsyicalvlTDEAKAMAFAKE 618
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
425-543 |
3.09e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 64.29 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 425 LHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNI-NEEHAMAFVAKvpgKEVTEL 503
Cdd:PRK08308 293 IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVaGERVKAKVISH---EEIDPV 369
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1820754837 504 DITDLVKQNMPWYCRLHAgVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK08308 370 QLREWCIQHLAPYQVPHE-IESVTEIPKNANGKVSRKLLE 408
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
8-431 |
4.16e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 64.68 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 8 DITDKGDLTFKIEDDILIGEKAPilkkctNVGALVLEKLRSRPE--FIAQVEAVTGA--ETTFAEMTEKSVKCALWLREQ 83
Cdd:PRK12582 27 SVERRADGSIVIKSRHPLGPYPR------SIPHLLAKWAAEAPDrpWLAQREPGHGQwrKVTYGEAKRAVDALAQALLDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 84 GVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTA-----RYFLSLTKPKIVFVngESAECLAQVVKENNM 158
Cdd:PRK12582 101 GLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHdhaklKHLFDLVKPRVVFA--QSGAPFARALAALDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 159 DTRLVVFADSAGfVGRAATLTAVLRSqdTAWIDEFECA-KLTSPKHVAAIVCSSGTSGFPKG---TEISHAAMINYMAHV 234
Cdd:PRK12582 179 LDVTVVHVTGPG-EGIASIAFADLAA--TPPTAAVAAAiAAITPDTVAKYLFTSGSTGMPKAvinTQRMMCANIAMQEQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 235 KVHDLKGHVSMWTPSMRW--------------YCG--LFI------------VIKAILDCSKRI----------IVPDYD 276
Cdd:PRK12582 256 RPREPDPPPPVSLDWMPWnhtmggnanfngllWGGgtLYIddgkplpgmfeeTIRNLREISPTVygnvpagyamLAEAME 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 277 DDEGLCRfiekyevSWFRcdscfpirlvkfgvlskyrlpTLKILLFGGAHFKGEL----QQTLVKLLPHTDVILS-YGMT 351
Cdd:PRK12582 336 KDDALRR-------SFFK---------------------NLRLMAYGGATLSDDLyermQALAVRTTGHRIPFYTgYGAT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 352 DygglcarqtkySKPGSCGFVCETGRLKVVD-PNTG---KVLGANKTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHT 427
Cdd:PRK12582 388 E-----------TAPTTTGTHWDTERVGLIGlPLPGvelKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRL 456
|
....
gi 1820754837 428 GDLG 431
Cdd:PRK12582 457 GDAA 460
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
910-1045 |
4.70e-10 |
|
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: 63.09 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 910 YGLTDAGGL-CVSQAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFdSDGWLH 988
Cdd:cd17636 143 YGQTEVMGLaTFAALGGGAIGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHH 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 989 TKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHET 1045
Cdd:cd17636 221 TNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPR 277
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
629-1099 |
4.78e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 64.25 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAIlyiggiicpwdhvvsklsaryflSLMSPKVVFVNEE 708
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAV-----------------------GLLGADVVPISTE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 SAENLMEAAKEENlQVRVMV-----IGSLPGFVSLANILEEQVSRAEIDGFRcTKIDNPHDLAMIcsSSGTTGMPKGT-- 781
Cdd:PRK13383 119 FRSDALAAALRAH-HISTVVadnefAERIAGADDAVAVIDPATAGAEESGGR-PAVAAPGRIVLL--TSGTTGKPKGVpr 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 782 --ELSyASLYNSITPVEEVHAKNEICAWVPTIRWHG-GLNQCIEVImSNAKWIIFSDDNIKEIALCEIIQKHGVTWLGTD 858
Cdd:PRK13383 195 apQLR-SAVGVWVTILDRTRLRTGSRISVAMPMFHGlGLGMLMLTI-ALGGTVLTHRHFDAEAALAQASLHRADAFTAVP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 859 TNFA-ILYVKMNIFQKYPMPSLRKMVITG----APFTKELHETVAKIMphtqiLQCYGLTDAG--GLCVSQAKNSKPGSC 931
Cdd:PRK13383 273 VVLArILELPPRVRARNPLPQLRVVMSSGdrldPTLGQRFMDTYGDIL-----YNGYGSTEVGigALATPADLRDAPETV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 932 GFVTKGIRIKIADeKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKeafdSDGWLHTKDIGYYDENGEIFFVNRISDFI 1011
Cdd:PRK13383 348 GKPVAGCPVRILD-RNNRPVGPRVTGRIFVGGELAGTRYTDGGGKAV----VDGMTSTGDMGYLDNAGRLFIVGREDDMI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1012 NYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDF 1091
Cdd:PRK13383 423 ISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRF-EQPRDINIVSSI 501
|
....*...
gi 1820754837 1092 PRISTGKI 1099
Cdd:PRK13383 502 PRNPTGKV 509
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
1452-1581 |
5.85e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 64.35 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1452 PTLKVILSSGAHLRKEhleVMRE--KLPDVFITNHYGMTDTACVVSAQNK----FTKLGsvGYVSSNVRIKMVDLDTEEA 1525
Cdd:PTZ00342 461 PNLEVILNGGGKLSPK---IAEElsVLLNVNYYQGYGLTETTGPIFVQHAddnnTESIG--GPISPNTKYKVRTWETYKA 535
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 1526 LGPNKIGELRVKAITIMQGYHKNPETTKQAFDSDGWLRTGDLAYYDDNGEIYIVDR 1581
Cdd:PTZ00342 536 TDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDR 591
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
760-1024 |
7.75e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 63.97 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 760 DNPHDLAMICSSSGTTGMPKGTELSYASLYNSITPV------EEVHAKNEIcAWVPtirwhggLNQCIE------VIMSN 827
Cdd:PTZ00342 301 EDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLckhsifKKYNPKTHL-SYLP-------ISHIYErviaylSFMLG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 828 AKWIIFSddniKEIALC--EIIQKHGVTWLGTDTNFAILYVK-MNIFQKYPMP---------SLRKMVITGaPFTKELHE 895
Cdd:PTZ00342 373 GTINIWS----KDINYFskDIYNSKGNILAGVPKVFNRIYTNiMTEINNLPPLkrflvkkilSLRKSNNNG-GFSKFLEG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 896 TV-------AKIMPHTQIL------------------------QCYGLTDAGG-LCVSQAKNSKPGSCGF-VTKGIRIKI 942
Cdd:PTZ00342 448 IThisskikDKVNPNLEVIlngggklspkiaeelsvllnvnyyQGYGLTETTGpIFVQHADDNNTESIGGpISPNTKYKV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 943 ADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFinykaIKLSSAE 1022
Cdd:PTZ00342 528 RTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGL-----VKLSQGE 602
|
...
gi 1820754837 1023 -IE 1024
Cdd:PTZ00342 603 yIE 605
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1206-1608 |
9.99e-10 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 63.93 E-value: 9.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTWDHELTPMTARNFLTLTSPK--IVFTV 1283
Cdd:TIGR03443 272 TYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRalIVIEK 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1284 SSSAANLMEA--AKELKMNLKV----------VVMDKLDGYES-VEENVMKGHDTREIIefkchVTNPDDVALIVPSSGT 1350
Cdd:TIGR03443 352 AGTLDQLVRDyiDKELELRTEIpalalqddgsLVGGSLEGGETdVLAPYQALKDTPTGV-----VVGPDSNPTLSFTSGS 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1351 TGLPKGTEISHYSLFcclhpyknrtlvghtcivtptmrwHYGVLMA--FRLvAANAK----------------------- 1405
Cdd:TIGR03443 427 EGIPKGVLGRHFSLA------------------------YYFPWMAkrFGL-SENDKftmlsgiahdpiqrdmftplflg 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1406 -KLIVPDNDDAENFCQLIE---KYQITWFGTDPFMiikfikSQLLEKY---RLPTLKVILSSGAHLRKEHLEVMREKLPD 1478
Cdd:TIGR03443 482 aQLLVPTADDIGTPGRLAEwmaKYGATVTHLTPAM------GQLLSAQattPIPSLHHAFFVGDILTKRDCLRLQTLAEN 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1479 VFITNHYGMTDTACVVS--------AQNKFTK-LGSV---GYVSSNVRIKMVD-LDTEEALGPNKIGELRVKAITIMQGY 1545
Cdd:TIGR03443 556 VCIVNMYGTTETQRAVSyfeipsrsSDSTFLKnLKDVmpaGKGMKNVQLLVVNrNDRTQTCGVGEVGEIYVRAGGLAEGY 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1546 HKNPETTKQAF------DSDGWL----------------------RTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAE 1597
Cdd:TIGR03443 636 LGLPELNAEKFvnnwfvDPSHWIdldkennkperefwlgprdrlyRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGE 715
|
490
....*....|.
gi 1820754837 1598 IETVLMTHPAV 1608
Cdd:TIGR03443 716 IDTHLSQHPLV 726
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
82-476 |
1.18e-09 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 62.86 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 82 EQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGESAECLAQVVKENNMDTR 161
Cdd:cd17632 87 EQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEGGTPPR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 162 LVVF----------------ADSAGFVGRAATLTAVLRSQDTAWIDEFECAKLTSPKHVAAIVCSSGTSGFPKG---TE- 221
Cdd:cd17632 167 LVVFdhrpevdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGamyTEr 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 222 ----------------ISHAAMINY--MAHVkvhdlKGHVSMWTPSMRWYCGLFIvikAILDCSKRIivpdydDDEGLCR 283
Cdd:cd17632 247 lvatfwlkvssiqdirPPASITLNFmpMSHI-----AGRISLYGTLARGGTAYFA---AASDMSTLF------DDLALVR 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 284 -------------FIEKY--EVSWFRCDSCFPIRL---VKFGVLSKYRLPTLKILLFGGAHFKGELqQTLVKLLPHTDVI 345
Cdd:cd17632 313 ptelflvprvcdmLFQRYqaELDRRSVAGADAETLaerVKAELRERVLGGRLLAAVCGSAPLSAEM-KAFMESLLDLDLH 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 346 LSYGMTDYGGLcARQTKYSKPGSCGFvcetgrlKVVD-PNtgkvLGANKT------GEIWAKSSYMMNGYYNNPEATRRA 418
Cdd:cd17632 392 DGYGSTEAGAV-ILDGVIVRPPVLDY-------KLVDvPE----LGYFRTdrphprGELLVKTDTLFPGYYKRPEVTAEV 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 419 LDSDGWLHTGDLGYYDNDGEVFLVDRMSEfinyrAIKISPAE------IEALIQQHPAVFQVAV 476
Cdd:cd17632 460 FDEDGFYRTGDVMAELGPDRLVYVDRRNN-----VLKLSQGEfvtvarLEAVFAASPLVRQIFV 518
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1206-1566 |
1.19e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.97 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCALWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIG----AISntwdheltP---MTARNF------L 1272
Cdd:PRK08180 71 TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGvpyaPVS--------PaysLVSQDFgklrhvL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1273 TLTSPKIVFtVSSSA--ANLMEAAKELkmNLKVVV------MDKLDGYESVEE-----NVMKGHDTreiiefkchvTNPD 1339
Cdd:PRK08180 143 ELLTPGLVF-ADDGAafARALAAVVPA--DVEVVAvrgavpGRAATPFAALLAtpptaAVDAAHAA----------VGPD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1340 DVALIVPSSGTTGLPKGTeISHYSLFC--------CLHPYKNRTLVghtcIVT--PtmrWH--YGVLMAFRLVAANAKKL 1407
Cdd:PRK08180 210 TIAKFLFTSGSTGLPKAV-INTHRMLCanqqmlaqTFPFLAEEPPV----LVDwlP---WNhtFGGNHNLGIVLYNGGTL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1408 IVpdnDDAENFCQLIEK-------YQITWFGTDP--F-MIIKFIK--SQLLEKYrLPTLKVILSSGAHLRK---EHLEVM 1472
Cdd:PRK08180 282 YI---DDGKPTPGGFDEtlrnlreISPTVYFNVPkgWeMLVPALErdAALRRRF-FSRLKLLFYAGAALSQdvwDRLDRV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1473 REKLPD--VFITNHYGMTDTA-CVVSAQNKFTKLGSVGYVSSNVRIKMVDLDteealgpNKIgELRVKAITIMQGYHKNP 1549
Cdd:PRK08180 358 AEATCGerIRMMTGLGMTETApSATFTTGPLSRAGNIGLPAPGCEVKLVPVG-------GKL-EVRVKGPNVTPGYWRAP 429
|
410
....*....|....*..
gi 1820754837 1550 ETTKQAFDSDGWLRTGD 1566
Cdd:PRK08180 430 ELTAEAFDEEGYYRSGD 446
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
62-546 |
1.21e-09 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 62.99 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 62 AETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFV 141
Cdd:PLN02654 119 ASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 142 NGESAECLAQVVKENNMDTRLVVFADSAGFVGRAATL--TAVLRSQDTAWID-----------------EFECAKLTSPK 202
Cdd:PLN02654 199 CNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYenQLAMKREDTKWQEgrdvwwqdvvpnyptkcEVEWVDAEDPL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 203 HvaaIVCSSGTSGFPKGTEISHAAMINYMAHVKVH--DLKGHVSMW-TPSMRWYCG-LFIVIKAILDCSKRII---VPDY 275
Cdd:PLN02654 279 F---LLYTSGSTGKPKGVLHTTGGYMVYTATTFKYafDYKPTDVYWcTADCGWITGhSYVTYGPMLNGATVLVfegAPNY 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 276 DDdEGLC-RFIEKYEVSWFRCDSCFPIRLVKFGV--LSKYRLPTLKILLFGGAHFKGELQQTLVKLL-----PHTDvilS 347
Cdd:PLN02654 356 PD-SGRCwDIVDKYKVTIFYTAPTLVRSLMRDGDeyVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVgdsrcPISD---T 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDYGGLCARQTKYS---KPGSCGFVCETGRLKVVDPNtGKVLGANKTGEIWAKSSY-----MMNGYYNNPEATRRAl 419
Cdd:PLN02654 432 WWQTETGGFMITPLPGAwpqKPGSATFPFFGVQPVIVDEK-GKEIEGECSGYLCVKKSWpgafrTLYGDHERYETTYFK- 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 420 DSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKE 499
Cdd:PLN02654 510 PFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVP 589
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 500 VTELDITDLVkqnMPWYCRLHA-----GVKFMEKLPRTATGKIAKKQLKQIA 546
Cdd:PLN02654 590 YSEELRKSLI---LTVRNQIGAfaapdKIHWAPGLPKTRSGKIMRRILRKIA 638
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
759-1099 |
1.26e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 63.22 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 759 IDNPHDLAMIcSSSGTTGMPKG---------TELSYASLYNSITPVEEVHAKNEICAWVptiRWHGGLNQCIEVimsNAK 829
Cdd:PTZ00237 251 VESSHPLYIL-YTSGTTGNSKAvvrsngphlVGLKYYWRSIIEKDIPTVVFSHSSIGWV---SFHGFLYGSLSL---GNT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 830 WIIFSDDNIK----EIALCEIIQKHGVTWLGTDTNFAILYVKM-----NIFQKYPMPSLRKMVITGAPFTKELHETVAKI 900
Cdd:PTZ00237 324 FVMFEGGIIKnkhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeatIIRSKYDLSNLKEIWCGGEVIEESIPEYIENK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 901 MpHTQILQCYGLTDAGG---LCVSqAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEF---MMKGYHKNP 974
Cdd:PTZ00237 404 L-KIKSSRGYGQTEIGItylYCYG-HINIPYNATGVPSIFIKPSILSED-GKELNVNEIGEVAFKLPMppsFATTFYKND 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 975 EQTKEAFDS-DGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAF 1053
Cdd:PTZ00237 481 EKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGL 560
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1054 VQKVVEKEVTEEELHDL-------VNKNLPWYCKLQAgIKFVNDFPRISTGKI 1099
Cdd:PTZ00237 561 LVLKQDQSNQSIDLNKLkneinniITQDIESLAVLRK-IIIVNQLPKTKTGKI 612
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1505-1684 |
1.41e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 62.82 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1505 SVGYVSSNVRIKMVDLDTEEALGPNKIGELRVKAITIMQGYHKNPETTKQAF-----------------DSDGWLRTGDL 1567
Cdd:PRK07769 392 SAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRTGDY 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1568 AYYDDnGEIYIVDRISDFINFRSINVSPAEIE-TVLMTHPAVLQAAVLG-------IPNEVDEQhPKAFVVQVPNKSvTE 1639
Cdd:PRK07769 472 GVYFD-GELYITGRVKDLVIIDGRNHYPQDLEyTAQEATKALRTGYVAAfsvpanqLPQVVFDD-SHAGLKFDPEDT-SE 548
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1640 QELIsyVEKNLPDYCRL---------------RGGVKIVDQL-------PRTTTGKIARKQLRDMYV 1684
Cdd:PRK07769 549 QLVI--VAERAPGAHKLdpqpiaddiraaiavRHGVTVRDVLlvpagsiPRTSSGKIARRACRAAYL 613
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
174-542 |
1.42e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 61.98 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 174 RAATLTAVLRSQDTawIDEfecakltspkHVAAIVCSSGTSGFPKGTEISHAAMINyMAHVkVHDLKGHVSMWTPSMRWY 253
Cdd:PRK07824 19 RAALLRDALRVGEP--IDD----------DVALVVATSGTTGTPKGAMLTAAALTA-SADA-THDRLGGPGQWLLALPAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 254 --CGLFIVIKAILDCSKRII--VPDYDDDEGLCRFIEKYEvSWFRCDSCFPIRLVK-FGVLSKYR-LPTLKILLFGGAHF 327
Cdd:PRK07824 85 hiAGLQVLVRSVIAGSEPVEldVSAGFDPTALPRAVAELG-GGRRYTSLVPMQLAKaLDDPAATAaLAELDAVLVGGGPA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 328 KGELQQTLVKLlpHTDVILSYGMTDYGGLCArqtkYSkpgscGFVCETGRLKVVDpntGKV-LGanktGEIWAKssymmn 406
Cdd:PRK07824 164 PAPVLDAAAAA--GINVVRTYGMSETSGGCV----YD-----GVPLDGVRVRVED---GRIaLG----GPTLAK------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 407 GYYNNPEATrrALDSDGWLHTGDLGYYDnDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPHNINEE 486
Cdd:PRK07824 220 GYRNPVDPD--PFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQ 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 487 HAMAFVAKVPGKEVTELDITDLVKQNMPwycRLHA--GVKFMEKLPRTATGKIAKKQL 542
Cdd:PRK07824 297 RVVAAVVGDGGPAPTLEALRAHVARTLD---RTAAprELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1485-1681 |
1.61e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 62.20 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTACVVSAQnKFTKLGSVGYVSSNVRIKMVDldteealgpnkiGELRVKAITIMQGYHKN----PETtkqafDSDG 1560
Cdd:PRK09029 271 YGLTEMASTVCAK-RADGLAGVGSPLPGREVKLVD------------GEIWLRGASLALGYWRQgqlvPLV-----NDEG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1561 WLRTGDLAYYDDnGEIYIVDRISD-FInfrS--INVSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAfVVQVPNKSV 1637
Cdd:PRK09029 333 WFATRDRGEWQN-GELTILGRLDNlFF---SggEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA-VVESDSEAA 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 1638 TEQeLISYVEKNL-----P-DYCRL-----RGGVkivdqlprtttgKIARKQLRD 1681
Cdd:PRK09029 408 VVN-LAEWLQDKLarfqqPvAYYLLppelkNGGI------------KISRQALKE 449
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
1339-1676 |
2.17e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 61.70 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1339 DDVALIVPSSGTTGLPKG-----------TEISHYSLFCC-LHPyknrtlvGHTCIVTPTmrwhYGVLMAFRLVAANAKK 1406
Cdd:COG1541 83 EEIVRIHASSGTTGKPTVvgytrkdldrwAELFARSLRAAgVRP-------GDRVQNAFG----YGLFTGGLGLHYGAER 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1407 L---IVP-DNDDAENFCQLIEKYQIT-WFGTDPFM--IIKFIKSQLLEKYRLPtLKVILSSGAHLRkehlEVMREKLPDV 1479
Cdd:COG1541 152 LgatVIPaGGGNTERQLRLMQDFGPTvLVGTPSYLlyLAEVAEEEGIDPRDLS-LKKGIFGGEPWS----EEMRKEIEER 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1480 F---ITNHYGMTDTACVVS----AQNkftklgsvGY-VSSNVRIKM-VDLDTEEALGPNKIGELrVkaITImqgyhknpe 1550
Cdd:COG1541 227 WgikAYDIYGLTEVGPGVAyeceAQD--------GLhIWEDHFLVEiIDPETGEPVPEGEEGEL-V--VTT--------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1551 TTKQA-----FdsdgwlRTGDLAYYDD--------NGEI-YIVDRISDFINFRSINVSPAEIETVLMTHPAVLQAAVLGI 1616
Cdd:COG1541 287 LTKEAmplirY------RTGDLTRLLPepcpcgrtHPRIgRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVV 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 1617 --PNEVDEqhpkaFVVQV-PNKSVTEQELISYVEKNLPDYCRLRGGVKIV--DQLPRtTTGKIAR 1676
Cdd:COG1541 361 drEGGLDE-----LTVRVeLAPGASLEALAEAIAAALKAVLGLRAEVELVepGSLPR-SEGKAKR 419
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
368-544 |
2.51e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 62.05 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 368 SCGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRR-----------------ALDSDGWLHTGDL 430
Cdd:PRK07769 392 SAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlseshaegAPDDALWVRTGDY 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 431 GYYdNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQ-HPAVFQ--VAVVPVPHN------INEEHA------------M 489
Cdd:PRK07769 472 GVY-FDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEaTKALRTgyVAAFSVPANqlpqvvFDDSHAglkfdpedtseqL 550
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 490 AFVA-KVPGKEVTELD-ITDLVKQNMPwycrLHAGVKFMEKL-------PRTATGKIAKKQLKQ 544
Cdd:PRK07769 551 VIVAeRAPGAHKLDPQpIADDIRAAIA----VRHGVTVRDVLlvpagsiPRTSSGKIARRACRA 610
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
30-444 |
2.52e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 61.96 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 30 PI--LKKCTNVGALVLEKLRSRPeFIAQVEAVTGAE-----TTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESY 102
Cdd:PLN02614 40 PIegMDSCWDVFRMSVEKYPNNP-MLGRREIVDGKPgkyvwQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 103 VPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGESAECLAQVVKENNMDTRLVVfadSAGFVGR-----AAT 177
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVV---SFGGVSReqkeeAET 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 178 LTAVLRSqdtaWiDEF----ECAK----LTSPKHVAAIVCSSGTSGFPKGTEISHAAMINYMAHVkVHDLK--------- 240
Cdd:PLN02614 196 FGLVIYA----W-DEFlklgEGKQydlpIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGV-IRLLKsanaaltvk 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 241 -------------------------GHVSMWTPSMRWYCGLFIVIKAILDCSkriiVPDYDDD--EGLCR------FIEK 287
Cdd:PLN02614 270 dvylsylplahifdrvieecfiqhgAAIGFWRGDVKLLIEDLGELKPTIFCA----VPRVLDRvySGLQKklsdggFLKK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 288 yevswFRCDSCFPirlVKFG------------------VLSKYRLP---TLKILLFGGAHFKGELQqTLVKLLPHTDVIL 346
Cdd:PLN02614 346 -----FVFDSAFS---YKFGnmkkgqshveasplcdklVFNKVKQGlggNVRIILSGAAPLASHVE-SFLRVVACCHVLQ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 347 SYGMTDYgglCArQTKYSKPGSCGFVCETG--------RLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYYNNPEATRRA 418
Cdd:PLN02614 417 GYGLTES---CA-GTFVSLPDELDMLGTVGppvpnvdiRLESVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEV 492
|
490 500
....*....|....*....|....*.
gi 1820754837 419 LdSDGWLHTGDLGYYDNDGEVFLVDR 444
Cdd:PLN02614 493 L-IDGWLHTGDVGEWQPNGSMKIIDR 517
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
623-1043 |
3.46e-09 |
|
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: 61.29 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 623 FTGKECTYAEMRERSIKCALWLRK-HGIQKGDNIGILTENHLNTCVPVLAILYIGGIicpwdhvvsklsaryflslmspk 701
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 702 VVFVNEesaeNLMEAAkeenlqvrvmVIGSLpgfvslanileeQVSRAEIdgfrctKIDNPHDLAMICSSSGTTGMPKGT 781
Cdd:cd05937 58 PAFINY----NLSGDP----------LIHCL------------KLSGSRF------VIVDPDDPAILIYTSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 782 ELSYASLYNSITPVEEV-HAKNEICAWVPTIRWHG--GLNQCIEVIMSNAKWII---FSDDNI-KEIALCE--IIQKHGv 852
Cdd:cd05937 106 AISWRRTLVTSNLLSHDlNLKNGDRTYTCMPLYHGtaAFLGACNCLMSGGTLALsrkFSASQFwKDVRDSGatIIQYVG- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 853 twlgtDTNFAILYVKMNIFQKypMPSLRkmVITGAPFTKELHETVAKIMPHTQILQCYGLTDagGLCVSQAKNSKP---G 929
Cdd:cd05937 185 -----ELCRYLLSTPPSPYDR--DHKVR--VAWGNGLRPDIWERFRERFNVPEIGEFYAATE--GVFALTNHNVGDfgaG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 930 SCGFVTKGIRIK-----------------IADEKTGIALGPK--ERGEICI----KSEFMMKGYHKNPEQTKEAF----- 981
Cdd:cd05937 254 AIGHHGLIRRWKfenqvvlvkmdpetddpIRDPKTGFCVRAPvgEPGEMLGrvpfKNREAFQGYLHNEDATESKLvrdvf 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 982 -DSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVV--VPVPH 1043
Cdd:cd05937 334 rKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPG 398
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
764-1026 |
3.94e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.17 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 764 DLAMICSSSGTTGMPKGTELSYASLY-NSITPVEEVHAKNE---ICAWVPTirWHG-GLNQCIEVIMSNAKWIIFS--DD 836
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAVQITHGNLYaNAEAMFVAAEFDVEtdvMVSWLPL--FHDmGMVGFLTVPMYFGAELVKVtpMD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 837 NIKEIAL-CEIIQKHGvtwlGTDT---NFA--ILYVKMNIFQK---YPMPSLRKMVITGAPFTkelHETVAKI------- 900
Cdd:PRK07768 231 FLRDPLLwAELISKYR----GTMTaapNFAyaLLARRLRRQAKpgaFDLSSLRFALNGAEPID---PADVEDLldagarf 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 901 -MPHTQILQCYGLTDA----------GGLCV--------SQAKNSKPGSCG----FVT-----KGIRIKIADEkTGIALG 952
Cdd:PRK07768 304 gLRPEAILPAYGMAEAtlavsfspcgAGLVVdevdadllAALRRAVPATKGntrrLATlgpplPGLEVRVVDE-DGQVLP 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 953 PKERGEICIKSEFMMKGYhKNPEQTKEAFDSDGWLHTKDIGYYDENGEIFFVNRISDFI-----N-YKA-IKLSSAEIEG 1025
Cdd:PRK07768 383 PRGVGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIimagrNiYPTdIERAAARVEG 461
|
.
gi 1820754837 1026 V 1026
Cdd:PRK07768 462 V 462
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
629-1054 |
5.62e-09 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 61.07 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIicpwdH--VVSKLSARYFLSLM---SPKVV 703
Cdd:PLN02654 122 TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAV-----HsvVFAGFSAESLAQRIvdcKPKVV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 704 FVNEE--------SAENLMEAAKEENLQVRVMVIGSLPGFVSLANILEEQVSRAEIDGF-------RCTKID----NPHD 764
Cdd:PLN02654 197 ITCNAvkrgpktiNLKDIVDAALDESAKNGVSVGICLTYENQLAMKREDTKWQEGRDVWwqdvvpnYPTKCEvewvDAED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 765 LAMICSSSGTTGMPKG-------------TELSYASLYNSitpvEEVHAKNEICAWV---PTIRWHGGLNQCIEVIMSNA 828
Cdd:PLN02654 277 PLFLLYTSGSTGKPKGvlhttggymvytaTTFKYAFDYKP----TDVYWCTADCGWItghSYVTYGPMLNGATVLVFEGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 829 KwiifsddNIKEIALC-EIIQKHGVTWLGTDTNF--AILYVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIMPHTQ 905
Cdd:PLN02654 353 P-------NYPDSGRCwDIVDKYKVTIFYTAPTLvrSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSR 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 906 --ILQCYGLTDAGGLCVSQ---AKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEF-----MMKGYHKNPE 975
Cdd:PLN02654 426 cpISDTWWQTETGGFMITPlpgAWPQKPGSATFPFFGVQPVIVDEK-GKEIEGECSGYLCVKKSWpgafrTLYGDHERYE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 976 QTKEA------FDSDGWLHTKDiGYYdengeiFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIEL 1049
Cdd:PLN02654 505 TTYFKpfagyyFSGDGCSRDKD-GYY------WLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQG 577
|
....*
gi 1820754837 1050 PLAFV 1054
Cdd:PLN02654 578 IYAFV 582
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
872-1054 |
5.86e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 60.73 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 872 QKYPMPSLRKMVITGAPftkeLHETVAK-IMPHTQ--ILQCYGLTDAG--------GLcvsQAKNSKPGSCGFVTKGIRI 940
Cdd:PRK10524 350 RKHDLSSLRALFLAGEP----LDEPTASwISEALGvpVIDNYWQTETGwpilaiarGV---EDRPTRLGSPGVPMYGYNV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 941 KIADEKTGIALGPKERGEICIKSE----FMmkgyhknpeQT----KEAFDSDGWLH-------TKDIGYYDENGEIFFVN 1005
Cdd:PRK10524 423 KLLNEVTGEPCGPNEKGVLVIEGPlppgCM---------QTvwgdDDRFVKTYWSLfgrqvysTFDWGIRDADGYYFILG 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1820754837 1006 RISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:PRK10524 494 RTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFV 542
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
625-1100 |
9.00e-09 |
|
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: 60.01 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 625 GKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDhvvsklsaryflslmspkvvf 704
Cdd:cd17643 10 DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPID--------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 705 vneesaenlmEAAKEEnlQVRVMVIGSLPGFVslanileeqvsraeidgfrctkIDNPHDLAMICSSSGTTGMPKGTELS 784
Cdd:cd17643 69 ----------PAYPVE--RIAFILADSGPSLL----------------------LTDPDDLAYVIYTSGSTGRPKGVVVS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 785 YAS---LYNSITPVEEVHAKN---------------EIcaWVPTIrwHGG-LnqcieVIMSNakWIIFSDDnikeiALCE 845
Cdd:cd17643 115 HANvlaLFAATQRWFGFNEDDvwtlfhsyafdfsvwEI--WGALL--HGGrL-----VVVPY--EVARSPE-----DFAR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 846 IIQKHGVTWLG-TDTNFAILyVKMNIFQKYPMPSLRKMVITGAPFTKELHETVAKIM--PHTQILQCYGLTDAgglCV-- 920
Cdd:cd17643 179 LLRDEGVTVLNqTPSAFYQL-VEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFglDRPQLVNMYGITET---TVhv 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 921 -------SQAKNSKPGSCGFVTKGIRIKIADEKtGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFDSDGW------- 986
Cdd:cd17643 255 tfrpldaADLPAAAASPIGRPLPGLRVYVLDAD-GRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrm 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 987 LHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEE 1066
Cdd:cd17643 334 YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAE 413
|
490 500 510
....*....|....*....|....*....|....
gi 1820754837 1067 LHDLVNKNLPWYcKLQAGIKFVNDFPRISTGKID 1100
Cdd:cd17643 414 LRALLKELLPDY-MVPARYVPLDALPLTVNGKLD 446
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
201-444 |
1.00e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 60.12 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 201 PKHVAAIVCSSGTSGFPKGTEISHAAMINYMAHVKVH------DLKGHVSMWTPS---------MRWYCGLFIVI----- 260
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHsifkkyNPKTHLSYLPIShiyerviayLSFMLGGTINIwskdi 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 261 ----KAILDCSKRII--VP------------DYDDDEGLCRFIEKYEVSWFRCDSCfpIRLVKF-----GVLSKYRL--- 314
Cdd:PTZ00342 383 nyfsKDIYNSKGNILagVPkvfnriytnimtEINNLPPLKRFLVKKILSLRKSNNN--GGFSKFlegitHISSKIKDkvn 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 315 PTLKILLFGGAHFKGELQQTLVKLLpHTDVILSYGMTDYGG-LCARQTKYSKPGSCGF-VCETGRLKVVDPNTGKVLGAN 392
Cdd:PTZ00342 461 PNLEVILNGGGKLSPKIAEELSVLL-NVNYYQGYGLTETTGpIFVQHADDNNTESIGGpISPNTKYKVRTWETYKATDTL 539
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 393 KTGEIWAKSSYMMNGYYNNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDR 444
Cdd:PTZ00342 540 PKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDR 591
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1513-1682 |
1.05e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.78 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1513 VRIKMVDLDTEeaLGPNKIGELRVKAITIMQGYhknpeTTKQAFDSDGWLRTGDLAYYDDnGEIYIVDRISDFINFRSIN 1592
Cdd:PRK05851 356 VRISPGDGAAG--VAGREIGEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGYLVD-GGLVVCGRAKELITVAGRN 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1593 VSPAEIETVLMTHPAVLQAAVLGIPNEVDEQHPKAFVV---QVPNKSVTEQELISYVEKN---LP-DYCRLRGGvkivdQ 1665
Cdd:PRK05851 428 IFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAaefRGPDEAGARSEVVQRVASEcgvVPsDVVFVAPG-----S 502
|
170
....*....|....*..
gi 1820754837 1666 LPRTTTGKIARKQLRDM 1682
Cdd:PRK05851 503 LPRTSSGKLRRLAVKRS 519
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
629-1100 |
1.23e-08 |
|
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: 59.41 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 629 TYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWDhvvsklsaryflsLMSPkvvfvnee 708
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPID-------------PASP-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 709 saenlmeaakeENLQVRVMviGSLPGFVSLANILEEQVSRAEIDGFRCTKIDNPHDLAMICSSSGTTGMPKGTELSYASL 788
Cdd:cd17654 77 -----------EQRSLTVM--KKCHVSYLLQNKELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 789 YNSITPV--------EEVHAKNEICAWVPTIrwhgglnqcIEVIMS--NAKWIIFSDDNIKEIALC---EIIQKHGVTWL 855
Cdd:cd17654 144 LPNIQHFrslfnitsEDILFLTSPLTFDPSV---------VEIFLSlsSGATLLIVPTSVKVLPSKladILFKRHRITVL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 856 G-TDTNFAILYVK-MNIFQKYPMPSLRKMVITGAPF-TKELHETVAKIMPHTQILQCYGLTDAGglCVSQAKNSK----P 928
Cdd:cd17654 215 QaTPTLFRRFGSQsIKSTVLSATSSLRVLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITEVS--CWALAYKVPeedsP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 929 GSCGFVTKGIRIKIADEKTG-----IALGPKERGeiCIksefmMKGYHKNPEQTkeafdsdgWLHTKDIgYYDENGEIFF 1003
Cdd:cd17654 293 VQLGSPLLGTVIEVRDQNGSegtgqVFLGGLNRV--CI-----LDDEVTVPKGT--------MRATGDF-VTVKDGELFF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1004 VNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVpvphETDIELPLAFVqkvvEKEVTEEELHDLVNKNLPWYCKLQA 1083
Cdd:cd17654 357 LGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT----LSDQQRLIAFI----VGESSSSRIHKELQLTLLSSHAIPD 428
|
490
....*....|....*..
gi 1820754837 1084 GIKFVNDFPRISTGKID 1100
Cdd:cd17654 429 TFVQIDKLPLTSHGKVD 445
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
395-544 |
1.36e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.39 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 395 GEIWAKSSYMMNGYYNNPeatrrALDSDGWLHTGDLGYYdNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQV 474
Cdd:PRK05851 373 GEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREG 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 475 AVVPVPHNINE-EHAMAFVAKVPGKEvtELDITDLVKQNMPWYCRL-HAGVKFME--KLPRTATGKIAKKQLKQ 544
Cdd:PRK05851 447 AVVAVGTGEGSaRPGLVIAAEFRGPD--EAGARSEVVQRVASECGVvPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1206-1685 |
1.52e-08 |
|
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: 59.28 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1206 TYADMSERSIKCA-LWLKKQGVKPGDIIGLCSDNNLDVFLILLGTMYIGAISNTwdheLTPMTARNFLTLTSPKIVFTVS 1284
Cdd:cd05905 16 TWGKLLSRAEKIAaVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIP----IEPPDISQQLGFLLGTCKVRVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1285 -SSAANLMEAAKELKMNLKVVVMDKLDGY----ESVEENVMKGHDTREIIefKCHVTNPDDVALIVPSSGTTGLPKGTEI 1359
Cdd:cd05905 92 lTVEACLKGLPKKLLKSKTAAEIAKKKGWpkilDFVKIPKSKRSKLKKWG--PHPPTRDGDTAYIEYSFSSDGSLSGVAV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1360 SHYSL--FC-----CLHPYKNRTLVghtCIVTPTMR---WHyGVLMAfrlVAANAKKLIVPDNDDAEN---FCQLIEKYQ 1426
Cdd:cd05905 170 SHSSLlaHCralkeACELYESRPLV---TVLDFKSGlglWH-GCLLS---VYSGHHTILIPPELMKTNpllWLQTLSQYK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1427 ITwfgtdpfmiIKFIKSQLLEKY------RLPTLK---VILSSGAHLRKEHLEVMREKLPDVFI---TNHyGMTDTACVV 1494
Cdd:cd05905 243 VR---------DAYVKLRTLHWClkdlssTLASLKnrdVNLSSLRMCMVPCENRPRISSCDSFLklfQTL-GLSPRAVST 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1495 SAQNKFTKLGSV----------GYVSSN-----------------------------VRIKMVDLDTEEALGPNKIGELR 1535
Cdd:cd05905 313 EFGTRVNPFICWqgtsgpepsrVYLDMRalrhgvvrlderdkpnslplqdsgkvlpgAQVAIVNPETKGLCKDGEIGEIW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1536 VKAITIMQGY-----------HKNPETTKQAFDSD-GWLRTGDLAY------YDDNGE----IYIVDRISDFINFRSINV 1593
Cdd:cd05905 393 VNSPANASGYflldgetndtfKVFPSTRLSTGITNnSYARTGLLGFlrptkcTDLNVEehdlLFVVGSIDETLEVRGLRH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1594 SPAEIE-TVLMTHPAVLQAAVLGIPNE---VDEQHP----KAF--VVQVPNKSVTEQELISYVeknlpdycrlrggVKIV 1663
Cdd:cd05905 473 HPSDIEaTVMRVHPYRGRCAVFSITGLvvvVAEQPPgseeEALdlVPLVLNAILEEHQVIVDC-------------VALV 539
|
570 580
....*....|....*....|....
gi 1820754837 1664 D--QLPRTTTGKIARKQLRDMYVN 1685
Cdd:cd05905 540 PpgSLPKNPLGEKQRMEIRQAFLA 563
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1022-1098 |
1.60e-08 |
|
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: 52.93 E-value: 1.60e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 1022 EIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYcKLQAGIKFVNDFPRISTGK 1098
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPY-AVPKEVVFVDELPKTRSGK 76
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
61-543 |
2.81e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 58.73 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 61 GAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVF 140
Cdd:PRK08279 60 DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 141 VNGESAECLAQvVKENNMDTRLVVFADSAGF--VGRAATLTAVLRSQDTAwiDEFECAKLTSpKHVAAIVCSSGTSGFPK 218
Cdd:PRK08279 140 VGEELVEAFEE-ARADLARPPRLWVAGGDTLddPEGYEDLAAAAAGAPTT--NPASRSGVTA-KDTAFYIYTSGTTGLPK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 219 GTEISHAAMINYMAHVkvhdlkGHVSMWTPSMRWYC--------GLFIVIKAILDCSKRIIVpdydddeglcRfiEKYEV 290
Cdd:PRK08279 216 AAVMSHMRWLKAMGGF------GGLLRLTPDDVLYCclplyhntGGTVAWSSVLAAGATLAL----------R--RKFSA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 291 S--W-----FRCdSCFpirlVKFGVLSKYRL-----PT---LKILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTD-YG 354
Cdd:PRK08279 278 SrfWddvrrYRA-TAF----QYIGELCRYLLnqppkPTdrdHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEgNV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 355 GLCarqTKYSKPGSCGFVceTGRLK----VV--DPNTGKVL-GAN------KTGE-------IWAKSSYmmNGyYNNPEA 414
Cdd:PRK08279 353 GFI---NVFNFDGTVGRV--PLWLAhpyaIVkyDVDTGEPVrDADgrcikvKPGEvglligrITDRGPF--DG-YTDPEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 415 TRRAL------DSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAV--VPVPhNINEE 486
Cdd:PRK08279 425 SEKKIlrdvfkKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVP-GTDGR 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820754837 487 HAMAfvAKVPGkEVTELDITDL---VKQNMPWYCR-LHagVKFMEKLPRTATGKIAKKQLK 543
Cdd:PRK08279 504 AGMA--AIVLA-DGAEFDLAALaahLYERLPAYAVpLF--VRLVPELETTGTFKYRKVDLR 559
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
762-1028 |
5.18e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.26 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 762 PHDLAMICSSSGTTGMPKGTELSYASLYNSITPVE-----EVHAKNEICAWVPTirWH-----GGLNQCIE-----VIMS 826
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRhgfgiDLNPDDVIVSWLPL--YHdmgliGGLLQPIFsgvpcVLMS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 827 NA-------KWIifsddnikeialcEIIQKHGVTWLGtDTNFAilyvkmnifqkYPMPSLR--------------KMVIT 885
Cdd:PRK05691 243 PAyflerplRWL-------------EAISEYGGTISG-GPDFA-----------YRLCSERvsesalerldlsrwRVAYS 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 886 GA-PFTKELHETVA-KIMP----HTQILQCYGLTDAGgLCVSQAKNSK------------------PG------SCGFVT 935
Cdd:PRK05691 298 GSePIRQDSLERFAeKFAAcgfdPDSFFASYGLAEAT-LFVSGGRRGQgipaleldaealarnraePGtgsvlmSCGRSQ 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 936 KGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAF---DSDGWLHTKDIGYYDEnGEIFFVNRISDFIN 1012
Cdd:PRK05691 377 PGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLGFLRD-GELFVTGRLKDMLI 455
|
330
....*....|....*.
gi 1820754837 1013 YKAIKLSSAEIEGVLE 1028
Cdd:PRK05691 456 VRGHNLYPQDIEKTVE 471
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
910-1055 |
5.92e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 57.19 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 910 YGLTDAGG-LCVSQAkNSKPGsCGFVTKGIRIKIADektgialgpkerGEICIKSEFMMKGYHKNpEQTKEAFDSDGWLH 988
Cdd:PRK09029 271 YGLTEMAStVCAKRA-DGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFA 335
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 989 TKDIGYYDeNGEIFFVNRISD-FInykaiklsSA-------EIEGVLELHPSILKAVVVPVPhetDIEL---PLAFVQ 1055
Cdd:PRK09029 336 TRDRGEWQ-NGELTILGRLDNlFF--------SGgegiqpeEIERVINQHPLVQQVFVVPVA---DAEFgqrPVAVVE 401
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
65-444 |
7.18e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 57.54 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELSPMTARYFLSLTKPKIVFVNGE 144
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 SAECLAQVVKENNMDTRLVV-FADSAGFVGRAATLTAV--LRSQDTAWIDEFECAklTSPKH---VAAIVCSSGTSGFPK 218
Cdd:PLN02861 159 KISSILSCLPKCSSNLKTIVsFGDVSSEQKEEAEELGVscFSWEEFSLMGSLDCE--LPPKQktdICTIMYTSGTTGEPK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 219 GTEISHAAMI------------------------NYMAHVKVHD--------LKG-HVSMWTPSMRW------------Y 253
Cdd:PLN02861 237 GVILTNRAIIaevlstdhllkvtdrvateedsyfSYLPLAHVYDqvietyciSKGaSIGFWQGDIRYlmedvqalkptiF 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 254 CGLFIVIKAILDCSKRIIVPDYDDDEGLCRFIEKYEVSW----FRCDSCFPI--RLVkFGVLSKYRLPTLKILLFGGAHF 327
Cdd:PLN02861 317 CGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNlrkgLKQEEASPRldRLV-FDKIKEGLGGRVRLLLSGAAPL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 328 KGELQQTLvKLLPHTDVILSYGMTDYGGLC--ARQTKYSKPGSCGFVCET--GRLKVVdPNTG-KVLGANKTGEIWAKSS 402
Cdd:PLN02861 396 PRHVEEFL-RVTSCSVLSQGYGLTESCGGCftSIANVFSMVGTVGVPMTTieARLESV-PEMGyDALSDVPRGEICLRGN 473
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1820754837 403 YMMNGYYNNPEATRRALdSDGWLHTGDLGYYDNDGEVFLVDR 444
Cdd:PLN02861 474 TLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDR 514
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1337-1674 |
7.68e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 57.67 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1337 NPDDVALIVPSSGTTGLPKGTEISHYSL-------------------FCCLHPYKNRTLVGHTCIVT----PTMRW---- 1389
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLlanraqvaaridfspedkvFNALPVFHSFGLTGGLVLPLlsgvKVFLYpspl 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1390 HYgvlmafRlvaanakklIVPdnddaenfcQLIekYQIT---WFGTDPFMIiKFIKSQllEKYRLPTLKVILSSGAHLRK 1466
Cdd:PRK06814 871 HY------R---------IIP---------ELI--YDTNatiLFGTDTFLN-GYARYA--HPYDFRSLRYVFAGAEKVKE 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1467 EHLEVMREKLpDVFITNHYGMTDTACVVSAQNK-FTKLGSVGYVSSNVRIKMvdldtEEALGPNKIGELRVKAITIMQGY 1545
Cdd:PRK06814 922 ETRQTWMEKF-GIRILEGYGVTETAPVIALNTPmHNKAGTVGRLLPGIEYRL-----EPVPGIDEGGRLFVRGPNVMLGY 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1546 HK--NPETTKQAfdSDGWLRTGDLAYYDDNGEIYIVDRISDFINFRSINVSPAEIETVLMT-HPAVLQAAVlGIPnevDE 1622
Cdd:PRK06814 996 LRaeNPGVLEPP--ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAV-SIP---DA 1069
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 1623 QHPKAFVVQVPNKSVTEQELISYVEKN-LPDYcRLRGGVKIVDQLPRTTTGKI 1674
Cdd:PRK06814 1070 RKGERIILLTTASDATRAAFLAHAKAAgASEL-MVPAEIITIDEIPLLGTGKI 1121
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
63-255 |
1.15e-07 |
|
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: 56.51 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 63 ETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIsnpWdNELSP-MTARYFL---SLTKPKI 138
Cdd:cd05943 98 EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAI---W-SSCSPdFGVPGVLdrfGQIEPKV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 139 VFV------NGES---AECLAQVVKENNMDTRLVVFADS-------AGFVGRAATLTAVLRsQDTAWIDEFEcakLTSPK 202
Cdd:cd05943 174 LFAvdaytyNGKRhdvREKVAELVKGLPSLLAVVVVPYTvaagqpdLSKIAKALTLEDFLA-TGAAGELEFE---PLPFD 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 203 HVAAIVCSSGTSGFPKGteISHAAMINYMAHVKVHDLkgHVSMwTPSMR--WY--CG 255
Cdd:cd05943 250 HPLYILYSSGTTGLPKC--IVHGAGGTLLQHLKEHIL--HCDL-RPGDRlfYYttCG 301
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
622-1041 |
1.58e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 56.59 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 622 AFTGKECTYAEMRERSIKCALWLRKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICPWD--HVVSKLsaRYFLSLMS 699
Cdd:PRK10252 478 ADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDtgYPDDRL--KMMLEDAR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 700 PKVVFVNEESAENLMEAAKEENLQVRVMvigsLPGfvslanileeqvsraeiDGFRCTKIDNPHDLAMICSSSGTTGMPK 779
Cdd:PRK10252 556 PSLLITTADQLPRFADVPDLTSLCYNAP----LAP-----------------QGAAPLQLSQPHHTAYIIFTSGSTGRPK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 780 GTELSYASLYN---------SITPVEEVHAKN----EICAW---VPtirwhgglnqcievIMSNAKWIIFSDDNIKE-IA 842
Cdd:PRK10252 615 GVMVGQTAIVNrllwmqnhyPLTADDVVLQKTpcsfDVSVWeffWP--------------FIAGAKLVMAEPEAHRDpLA 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 843 LCEIIQKHGVtwlgTDTNF------AILYVKMNIFQKYPMPSLRKMVITGAPFTKEL----HETVakimpHTQILQCYGL 912
Cdd:PRK10252 681 MQQFFAEYGV----TTTHFvpsmlaAFVASLTPEGARQSCASLRQVFCSGEALPADLcrewQQLT-----GAPLHNLYGP 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 913 TDAgGLCVS---------QAKNSKPGSCGFVTKGIRIKIADEKT-----GIAlgpkerGEICIKSEFMMKGYHKNPEQTK 978
Cdd:PRK10252 752 TEA-AVDVSwypafgeelAAVRGSSVPIGYPVWNTGLRILDARMrpvppGVA------GDLYLTGIQLAQGYLGRPDLTA 824
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820754837 979 EAFDSDGWL------HTKDIGYYDENGEIFFVNRiSDF---INYKAIKLSsaEIEGVLELHPSILKAVVVPV 1041
Cdd:PRK10252 825 SRFIADPFApgermyRTGDVARWLDDGAVEYLGR-SDDqlkIRGQRIELG--EIDRAMQALPDVEQAVTHAC 893
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
768-1054 |
2.09e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 55.48 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 768 ICSSSGTTGMPKGTELSYASL----YNSITP-VEEVHAKNEICAWVPTIR---WhgGLNQciEVIMSNAKwIIFSDDNIK 839
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHRSTvlhaYGAALPdAMGLSARDAVLPVVPMFHvnaW--GLPY--SAPLTGAK-LVLPGPDLD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 840 EIALCEIIQKHGVT--------WLGTdtnfaILYVKMNifqKYPMPSLRKMVITGAPFTKELHETVAKIMpHTQILQCYG 911
Cdd:PRK07008 256 GKSLYELIEAERVTfsagvptvWLGL-----LNHMREA---GLRFSTLRRTVIGGSACPPAMIRTFEDEY-GVEVIHAWG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 912 LTDA---GGLCVSQAKNSK-PGSC--------GFVTKGIRIKIADEKtGIALgP---KERGEICIKSEFMMKGYHKNPEQ 976
Cdd:PRK07008 327 MTEMsplGTLCKLKWKHSQlPLDEqrkllekqGRVIYGVDMKIVGDD-GREL-PwdgKAFGDLQVRGPWVIDRYFRGDAS 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 977 TKeafdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFV 1054
Cdd:PRK07008 405 PL----VDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVV 478
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
344-444 |
2.57e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 55.49 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 344 VILSYGMTDYGglCARQTKYSKPGSCGFV------CEtgrLKVVDpntgkVLGANKT--------GEIWAKSSYMMNGYY 409
Cdd:PLN02736 404 VLEGYGMTETS--CVISGMDEGDNLSGHVgspnpaCE---VKLVD-----VPEMNYTsedqpyprGEICVRGPIIFKGYY 473
|
90 100 110
....*....|....*....|....*....|....*
gi 1820754837 410 NNPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDR 444
Cdd:PLN02736 474 KDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
759-1100 |
3.58e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 54.28 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 759 IDNphDLAMICSSSGTTGMPKGTELSYASLYNSitpVEEVHAK-NEICAWVPTIRWH--GGLNQCIEVIMSNAKWIIFSD 835
Cdd:PRK07824 33 IDD--DVALVVATSGTTGTPKGAMLTAAALTAS---ADATHDRlGGPGQWLLALPAHhiAGLQVLVRSVIAGSEPVELDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 836 DNIKEI-ALCEIIQKhgvtwLGTDTNFAILyVKMNIFQKYPMP-------SLRKMVITGAPFTKELHETVAK--IMphtq 905
Cdd:PRK07824 108 SAGFDPtALPRAVAE-----LGGGRRYTSL-VPMQLAKALDDPaataalaELDAVLVGGGPAPAPVLDAAAAagIN---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 906 ILQCYGLTDAGGLCVSQaknskpgscGFVTKGIRIKIADEKtgIALGpkergeicikSEFMMKGYhKNPEQTKeAFDSDG 985
Cdd:PRK07824 178 VVRTYGMSETSGGCVYD---------GVPLDGVRVRVEDGR--IALG----------GPTLAKGY-RNPVDPD-PFAEPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 986 WLHTKDIGYYDeNGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVVPVPHETDIELPLAFVQKVVEKEVTEE 1065
Cdd:PRK07824 235 WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 1820754837 1066 ELHDLVNKNLP-WYCKLQagIKFVNDFPRISTGKID 1100
Cdd:PRK07824 314 ALRAHVARTLDrTAAPRE--LHVVDELPRRGIGKVD 347
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
65-543 |
6.70e-07 |
|
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: 53.90 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 65 TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIsnpwdnelspmtaryflsltkpkivfvnge 144
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV------------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 145 saeclaqvvkennmdtrlvvfadsagfvgrAATLTAVLRSQDTAwidefECAKLTSPKHVAAIVC----SSGTSGFPKGT 220
Cdd:cd05940 55 ------------------------------AALINYNLRGESLA-----HCLNVSSAKHLVVDAAlyiyTSGTTGLPKAA 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 221 EISHAAMINYMAHVkvhdlkGHVSMWTPSMRWY-C-------GLFIVIKAILDCSKRIIVPD-------YDDdeglcrfI 285
Cdd:cd05940 100 IISHRRAWRGGAFF------AGSGGALPSDVLYtClplyhstALIVGWSACLASGATLVIRKkfsasnfWDD-------I 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 286 EKYEVSWFrcdscfpirlVKFGVLSKYRLPTL--------KILLFGGAHFKGELQQTLVKLLPHTDVILSYGMTDygGLC 357
Cdd:cd05940 167 RKYQATIF----------QYIGELCRYLLNQPpkpterkhKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATE--GNS 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 358 ARQTKYSKPGSCGF----VCETGRLKVV--DPNTGKVL----------GANKTGEIWAKSSYMMN--GYYNNPEATRRAL 419
Cdd:cd05940 235 GFINFFGKPGAIGRnpslLRKVAPLALVkyDLESGEPIrdaegrcikvPRGEPGLLISRINPLEPfdGYTDPAATEKKIL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 420 -----DSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAV--VPVPhNINEEHAMAFV 492
Cdd:cd05940 315 rdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVP-GTDGRAGMAAI 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 493 AKVPGkevTELDITDL---VKQNMPWYCRlHAGVKFMEKLPRTATGKIAKKQLK 543
Cdd:cd05940 394 VLQPN---EEFDLSALaahLEKNLPGYAR-PLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
48-293 |
1.05e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 53.65 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 48 SRPEFIAQVEAVTGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAIsnpW-----DNEL 122
Cdd:PRK03584 99 DRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAI---WsscspDFGV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 123 SPMTARyfLSLTKPKIVF-VNG--------ESAECLAQVVKENNMDTRLVV-----FADSAGFVGRAATLTAVLRSQDTA 188
Cdd:PRK03584 176 QGVLDR--FGQIEPKVLIaVDGyryggkafDRRAKVAELRAALPSLEHVVVvpylgPAAAAAALPGALLWEDFLAPAEAA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 189 widEFECAKLtsP-KHVAAIVCSSGTSGFPKGTEISHAAMInyMAHVKVH----DLK-GHVSMW--TPS-MRW---YCGL 256
Cdd:PRK03584 254 ---ELEFEPV--PfDHPLWILYSSGTTGLPKCIVHGHGGIL--LEHLKELglhcDLGpGDRFFWytTCGwMMWnwlVSGL 326
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1820754837 257 F----IVikaILDCSkriivPDYDDDEGLCRFIEKYEVSWF 293
Cdd:PRK03584 327 LvgatLV---LYDGS-----PFYPDPNVLWDLAAEEGVTVF 359
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
379-462 |
1.20e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.08 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 379 KVVDPNtGKVLGANKTGEIWAKSSYMMNGYYNnPEATRRALDSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISP 458
Cdd:PRK07768 372 RVVDED-GQVLPPRGVGVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYP 449
|
....
gi 1820754837 459 AEIE 462
Cdd:PRK07768 450 TDIE 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
35-542 |
2.12e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.86 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 35 CTNVGALVLEKL----RSRPEFIAQVEAvtGAETTFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALY 110
Cdd:PRK05691 1126 CAPAQAWLPELLneqaRQTPERIALVWD--GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILK 1203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 111 LGAISNPWDNELSPMTARYFLSLTKPKIVFVNGESAECLAQV--VKENNMDTrlvVFADSagfvgraatltavlrsqdta 188
Cdd:PRK05691 1204 AGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAegVSAIALDS---LHLDS-------------------- 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 189 WIDEFECAKLtSPKHVAAIVCSSGTSGFPKGTEISHAAM---INYMAHVKVHD----------LKGHVSMWTPSMRWYCG 255
Cdd:PRK05691 1261 WPSQAPGLHL-HGDNLAYVIYTSGSTGQPKGVGNTHAALaerLQWMQATYALDdsdvlmqkapISFDVSVWECFWPLITG 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 256 LFIVIKAildcskriiVPDYDDDEGLCRFIEKYEVSwfrCDSCFPIRLVKFgvlskYRLP------TLKILLFGGAHFKG 329
Cdd:PRK05691 1340 CRLVLAG---------PGEHRDPQRIAELVQQYGVT---TLHFVPPLLQLF-----IDEPlaaactSLRRLFSGGEALPA 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 330 ELQQTLVKLLPHTDVILSYGMTDYGglcARQTKYSKPGSCGFVCETGR------LKVVDPNTgKVLGANKTGEIWAKSSY 403
Cdd:PRK05691 1403 ELRNRVLQRLPQVQLHNRYGPTETA---INVTHWQCQAEDGERSPIGRplgnvlCRVLDAEL-NLLPPGVAGELCIGGAG 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 404 MMNGYYNNP--EATRRALDSDG-----WLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQvAV 476
Cdd:PRK05691 1479 LARGYLGRPalTAERFVPDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQ-AA 1557
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820754837 477 VPVPHNINEEHAMAFVAKVPGKEVTELDITDLVKQNMPWYcRLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:PRK05691 1558 VLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEY-MVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
878-1099 |
4.35e-06 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 51.57 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 878 SLRKMVITGAPFTKELHETVAKIMPHTQILQCYGLTDAGGLCVSQAKNS-KPGSCGFVTKGIRIKIAdEKTGIALGPKER 956
Cdd:PRK06060 261 SLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVDEwRLGTLGRVLPPYEIRVV-APDGTTAGPGVE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 957 GEICIKSEFMMKGYHKNPEQTKEafdSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKA 1036
Cdd:PRK06060 340 GDLWVRGPAIAKGYWNRPDSPVA---NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 1037 VVVPVPHETDIELPLAFVQKVVEKEVTEEELHDLVNKNLPWYCKLQAGIKF--VNDFPRISTGKI 1099
Cdd:PRK06060 417 AVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFavVDRLPRTPNGKL 481
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
762-1039 |
4.44e-06 |
|
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: 51.10 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 762 PHDLAMICSSSGTTGMPKGTELSYASLYNSITpveevhAKNEICAWVPTIRWHgglnQCI---------EVIM---SNAK 829
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA------AQIAAFDVGPGSRVL----QFAspsfdasvwELLMallAGAT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 830 WIIFSDDNIKEIA-LCEIIQKHGVT----------WLGTDTnfailyvkmnifqkypMPSLRKMVITGAPFTKELhetVA 898
Cdd:cd17652 162 LVLAPAEELLPGEpLADLLREHRIThvtlppaalaALPPDD----------------LPDLRTLVVAGEACPAEL---VD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 899 KIMPHTQILQCYGLTDAGgLCVSQAKNSKPGS---CGFVTKGIRIKIADEktgiALGP---KERGEICIKSEFMMKGYHK 972
Cdd:cd17652 223 RWAPGRRMINAYGPTETT-VCATMAGPLPGGGvppIGRPVPGTRVYVLDA----RLRPvppGVPGELYIAGAGLARGYLN 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 973 NPEQTKEAFDSD------GWLH-TKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVLELHPSILKAVVV 1039
Cdd:cd17652 298 RPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV 371
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
49-542 |
4.52e-06 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 51.36 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 49 RPEFIAQVEAVTGAETTFAEMTEKSVKCAL-----WLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPWDNELS 123
Cdd:cd17647 1 FPERTCVVETPSLNSSKTRSFTYRDINEASnivahYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 124 PMTARYFLSLTKPKivfvngesaeclaqvvkennmdtRLVVFADSAGFVGraatltavlrsqdtawidefecakltsPKH 203
Cdd:cd17647 81 PARQNIYLGVAKPR-----------------------GLIVIRAAGVVVG---------------------------PDS 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 204 VAAIVCSSGTSGFPKGTEISH---AAMINYMAHV-------KVHDLKG------HVSMWTPsmrwycgLFIvikaildcS 267
Cdd:cd17647 111 NPTLSFTSGSEGIPKGVLGRHfslAYYFPWMAKRfnlsendKFTMLSGiahdpiQRDMFTP-------LFL--------G 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 268 KRIIVPDYDD---DEGLCRFIEKYevswfrcdscfpirlvkfGVLSKYRLPTLKILLFGG----------AHFKGELQQ- 333
Cdd:cd17647 176 AQLLVPTQDDigtPGRLAEWMAKY------------------GATVTHLTPAMGQLLTAQattpfpklhhAFFVGDILTk 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 334 ----TLVKLLPHTDVILSYGMTDygglCARQTKYSKPGSC----GF------VCETGR------LKVVDPN-TGKVLGAN 392
Cdd:cd17647 238 rdclRLQTLAENVRIVNMYGTTE----TQRAVSYFEVPSRssdpTFlknlkdVMPAGRgmlnvqLLVVNRNdRTQICGIG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 393 KTGEIWAKSSYMMNGYYNNPEATRRA--------------LDSDG-------WL-------HTGDLGYYDNDGEVFLVDR 444
Cdd:cd17647 314 EVGEIYVRAGGLAEGYRGLPELNKEKfvnnwfvepdhwnyLDKDNnepwrqfWLgprdrlyRTGDLGRYLPNGDCECCGR 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 445 MSEFINYRAIKISPAEIEALIQQHPAVFQvAVVPVPHNINEEHAM-AFVAKVPGKEVTEL-------------------- 503
Cdd:cd17647 394 ADDQVKIRGFRIELGEIDTHISQHPLVRE-NITLVRRDKDEEPTLvSYIVPRFDKPDDESfaqedvpkevstdpivkgli 472
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1820754837 504 -------DITDLVKQNMPWYCrLHAGVKFMEKLPRTATGKIAKKQL 542
Cdd:cd17647 473 gyrklikDIREFLKKRLASYA-IPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
47-219 |
6.20e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 51.03 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 47 RSRPE--FIAQVEAVTGAET-TFAEMTEKSVKCALWLREQGVQPGDIIGICTHNHLESYVPLLAALYLGAISNPwdneLS 123
Cdd:PRK08180 50 QEAPDrvFLAERGADGGWRRlTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAP----VS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 124 PMTA---------RYFLSLTKPKIVFVN--GESAECLAQVVkennmDTRLVVFADSAGFVGRAAT-LTAVLRSQDTAWID 191
Cdd:PRK08180 126 PAYSlvsqdfgklRHVLELLTPGLVFADdgAAFARALAAVV-----PADVEVVAVRGAVPGRAATpFAALLATPPTAAVD 200
|
170 180
....*....|....*....|....*...
gi 1820754837 192 EFECAklTSPKHVAAIVCSSGTSGFPKG 219
Cdd:PRK08180 201 AAHAA--VGPDTIAKFLFTSGSTGLPKA 226
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
386-537 |
1.06e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 50.13 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 386 GKVLGANKTGEIWAK----SSYMMNgYYNNPEATRRALDS-DGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAE 460
Cdd:PTZ00237 451 GKELNVNEIGEVAFKlpmpPSFATT-FYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNT 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 461 IEALIQQHPAVFQVAVVPVPHNINEEHAMAFVAKVPGKEVTELDITDL-------VKQNMPWYCRLhAGVKFMEKLPRTA 533
Cdd:PTZ00237 530 IETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLkneinniITQDIESLAVL-RKIIIVNQLPKTK 608
|
....
gi 1820754837 534 TGKI 537
Cdd:PTZ00237 609 TGKI 612
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
878-1011 |
1.32e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 50.12 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 878 SLRKMVITGAPFTKELHETVaKIMPHTQILQCYGLTD--AGGlCVSQAKNSKPGSCGFVTKGIRIKIADEKTG---IALG 952
Cdd:PLN02387 421 RIRFMLSGGAPLSGDTQRFI-NICLGAPIGQGYGLTEtcAGA-TFSEWDDTSVGRVGPPLPCCYVKLVSWEEGgylISDK 498
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820754837 953 PKERGEICIKSEFMMKGYHKNPEQTKEAFDSDG----WLHTKDIGYYDENGEIFFVNRISDFI 1011
Cdd:PLN02387 499 PMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIV 561
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
914-1011 |
2.07e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 49.17 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 914 DAGGLCVSQAKNSKPG------SCGFVTKGIrIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAFD----- 982
Cdd:PRK05850 350 DYEKLSAGHAKRCETGggtplvSYGSPRSPT-VRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvd 428
|
90 100 110
....*....|....*....|....*....|....*
gi 1820754837 983 -SDG-----WLHTKDIGYYDEnGEIFFVNRISDFI 1011
Cdd:PRK05850 429 pSPGtpegpWLRTGDLGFISE-GELFIVGRIKDLL 462
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
930-1011 |
2.50e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 48.97 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 930 SCGFVTKGIRIKIADEKTGIALGPKERGEICIKSEFMMKGYHKNPEQTKEAF------------------DSDGWLHTKD 991
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGD 482
|
90 100
....*....|....*....|
gi 1820754837 992 IGYYdENGEIFFVNRISDFI 1011
Cdd:PRK12476 483 LGVY-LDGELYITGRIADLI 501
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1485-1608 |
1.06e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.03 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1485 YGMTDTaCVVSAQNKF--TKLGSVGYVSSNVRIKMVDLDTEEAL---GPNKIGELRVKAITIMQGYHKNPETTKQAFDSD 1559
Cdd:PLN02387 452 YGLTET-CAGATFSEWddTSVGRVGPPLPCCYVKLVSWEEGGYLisdKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVD 530
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1820754837 1560 G----WLRTGDLAYYDDNGEIYIVDRISDFINFRSIN-VSPAEIETVLMTHPAV 1608
Cdd:PLN02387 531 ErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEyVSLGKVEAALSVSPYV 584
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
627-1011 |
1.17e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 47.03 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 627 ECTYAEM--RERSIKCALwlrKHGIQKGDNIGILTENHLNTCVPVLAILYIGGIICP-WD-----HVvSKLSAryFLSLM 698
Cdd:PRK07769 55 DLTWSQFgaRNRAVGARL---QQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPlFDpaepgHV-GRLHA--VLDDC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 699 SPKVVFVNEESAENLME-----AAKEenlQVRVMVIGSLPGFVSlanileEQVSRAEIDgfrctkidnPHDLAMICSSSG 773
Cdd:PRK07769 129 TPSAILTTTDSAEGVRKffrarPAKE---RPRVIAVDAVPDEVG------ATWVPPEAN---------EDTIAYLQYTSG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 774 TTGMPKGTELSYASL-YNSITPVEEVHAKNEI--CAWVP--------TIRWHGGLNQCIEvIMSNAKWIIFSDDNIKEIA 842
Cdd:PRK07769 191 STRIPAGVQITHLNLpTNVLQVIDALEGQEGDrgVSWLPffhdmgliTVLLPALLGHYIT-FMSPAAFVRRPGRWIRELA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 843 lceiiQKHGVTWlGTDT---NFAILYVKMNIFQKYPMPSLR----KMVITGA-PFT----KELHETVAKI-MPHTQILQC 909
Cdd:PRK07769 270 -----RKPGGTG-GTFSaapNFAFEHAAARGLPKDGEPPLDlsnvKGLLNGSePVSpasmRKFNEAFAPYgLPPTAIKPS 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 910 YGLTDAGgLCVS----------------------------QAKNSKPG-SCGFVTKGIRIKIADEKTGIALGPKERGEIC 960
Cdd:PRK07769 344 YGMAEAT-LFVSttpmdeeptviyvdrdelnagrfvevpaDAPNAVAQvSAGKVGVSEWAVIVDPETASELPDGQIGEIW 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820754837 961 IKSEFMMKGYHKNPEQTKEAF-----------------DSDGWLHTKDIGYYdENGEIFFVNRISDFI 1011
Cdd:PRK07769 423 LHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRTGDYGVY-FDGELYITGRVKDLV 489
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
1563-1683 |
1.55e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 46.61 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 1563 RTGDL------AYYDDNGeiyivdRISDFINFRSINVSPAEIETVLMT-HPAVLQAAVLGIP--NEVDEQHPKAFVVQVP 1633
Cdd:PLN03052 592 RHGDIfertsgGYYRAHG------RADDTMNLGGIKVSSVEIERVCNAaDESVLETAAIGVPppGGGPEQLVIAAVLKDP 665
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1820754837 1634 NKSVTEQELI-----SYVEKNLPDYCRLRGgVKIVDQLPRTTTGKIARKQLRDMY 1683
Cdd:PLN03052 666 PGSNPDLNELkkifnSAIQKKLNPLFKVSA-VVIVPSFPRTASNKVMRRVLRQQL 719
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
348-544 |
1.98e-04 |
|
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: 45.88 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDygGLCARQTKYSKPGSCGFVCETG------RLKVVDPNTGKVL----------GANKTGEIWAK-----SSYMMN 406
Cdd:cd05939 250 YGATE--GNSSLVNIDNHVGACGFNSRILpsvypiRLIKVDEDTGELIrdsdglcipcQPGEPGLLVGKiiqndPLRRFD 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 407 GYYNNpEATRRALDSDGWLH------TGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAV--VP 478
Cdd:cd05939 328 GYVNE-GATNKKIARDVFKKgdsaflSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVE 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820754837 479 VPHniNEEHA-MAFVAKVPGKEVTELDITDLVKQnMPWYCRlHAGVKFMEKLPRTATGKIAKKQLKQ 544
Cdd:cd05939 407 VPG--VEGRAgMAAIVDPERKVDLDRFSAVLAKS-LPPYAR-PQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
389-545 |
5.94e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 389 LGAnkTGEIWAKSSYMMNGYYNNPEATRRAL-------DSDGWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEI 461
Cdd:PRK05691 4063 LGA--VGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEI 4140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 462 EALIQQHPAVfQVAVVPVPHNINEEHAMAFVakVPGKEVTELD-ITDLVKQ----NMPWY-CRLHAGVkfMEKLPRTATG 535
Cdd:PRK05691 4141 EARLHEQAEV-REAAVAVQEGVNGKHLVGYL--VPHQTVLAQGaLLERIKQrlraELPDYmVPLHWLW--LDRLPLNANG 4215
|
170
....*....|
gi 1820754837 536 KIAKKQLKQI 545
Cdd:PRK05691 4216 KLDRKALPAL 4225
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
369-479 |
1.44e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 43.11 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 369 CGFVCETGRLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYY-----------NNPEATRRALDSD-GWLHTGDLGY---- 432
Cdd:cd05905 363 SGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPANASGYFlldgetndtfkVFPSTRLSTGITNnSYARTGLLGFlrpt 442
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820754837 433 ------YDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQ-HP-----AVFQVAVVPV 479
Cdd:cd05905 443 kctdlnVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRvHPyrgrcAVFSITGLVV 501
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
909-1027 |
6.01e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 41.13 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 909 CYGLTDAGglcvSQAKNSKPG-------SCGFVTKGIRIKIADEKTGIalgpkergeICIKSEFMMKGYHKNpeqtkeAF 981
Cdd:PRK07445 260 TYGMTETA----SQIATLKPDdflagnnSSGQVLPHAQITIPANQTGN---------ITIQAQSLALGYYPQ------IL 320
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1820754837 982 DSDGWLHTKDIGYYDENGEIFFVNRISDFINYKAIKLSSAEIEGVL 1027
Cdd:PRK07445 321 DSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAI 366
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
348-551 |
7.17e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 41.10 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 348 YGMTDYGGLCARQTK-YSKPGSCGFVcetgrLKVVDPNTGKVLGANKTGEIWAKSSYMMNGYY--NNPeatrRALD--SD 422
Cdd:PRK06814 939 YGVTETAPVIALNTPmHNKAGTVGRL-----LPGIEYRLEPVPGIDEGGRLFVRGPNVMLGYLraENP----GVLEppAD 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820754837 423 GWLHTGDLGYYDNDGEVFLVDRMSEFINYRAIKISPAEIEALIQQHPAVFQVAVVPVPhniNEEHAMAFVAKVPGKEVTE 502
Cdd:PRK06814 1010 GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIP---DARKGERIILLTTASDATR 1086
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1820754837 503 LDITDLVKQNMPWYCRLHAGVKFMEKLPRTATGKIAKKQLKQIAKSYAT 551
Cdd:PRK06814 1087 AAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAA 1135
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