|
Name |
Accession |
Description |
Interval |
E-value |
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
38-623 |
1.03e-147 |
|
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: 440.52 E-value: 1.03e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 38 AFATKPAFIWADDDAASTRTaLTYAQLDAAAGRMARNLLGtvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVP 117
Cdd:cd05931 5 ARPDRPAYTFLDDEGGREET-LTYAELDRRARAIAARLQA---VGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 118 PDPARfdgpAHAHLLRAVSQTRPTAAVADAGYIDSVaktvsssvaaaggdnaRARLAATAMLGSLRWLAVDELEREREGG 197
Cdd:cd05931 81 PTPGR----HAERLAAILADAGPRVVLTTAAALAAV----------------RAFAASRPAAGTPRLLVVDLLPDTSAAD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 198 GDGpgpeapyVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLV-FLLLTV 276
Cdd:cd05931 141 WPP-------PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIgGLLTPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 277 VAGATCVLAAPGVFLRRPRLWLELVSEFGATCTPVPSFALPLVlrrGRGHRRDRRRLLELGSLRNLILINEPIYESSVDE 356
Cdd:cd05931 214 YSGGPSVLMSPAAFLRRPLRWLRLISRYRATISAAPNFAYDLC---VRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 357 FVEAFCSHGLRATSVSPSYGLAENCTFVSTAWRTSESSSGHIPsYMKLLPSARLSPPPSSAANE-------VPEIEIAVV 429
Cdd:cd05931 291 FAEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLRVD-RDALAGRAVAVAADDPAARElvscgrpLPDQEVRIV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 430 DEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCARVPGRAGaCFVRTGDRGVVRgpERYLYVVGRSADVITLDd 509
Cdd:cd05931 370 DPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG-GWLRTGDLGFLH--DGELYITGRLKDLIIVR- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 510 gvggGRRRvHAHYVETAAFgSAPDRLRGGCVAAFATsstlwSRSQTGVVAVVAELQKViAGVGDHRGLCDGIRAAVWRDE 589
Cdd:cd05931 446 ----GRNH-YPQDIEATAE-EAHPALRPGCVAAFSV-----PDDGEERLVVVAEVERG-ADPADLAAIAAAIRAAVAREH 513
|
570 580 590
....*....|....*....|....*....|....
gi 1205983844 590 GVMVGLAVLVDGGVVPKTTSGKLRRGAAREMLAA 623
Cdd:cd05931 514 GVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
59-505 |
4.53e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 218.34 E-value: 4.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNL--LGtvgsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppDPaRFDGPAHAHLLRavs 136
Cdd:pfam00501 22 LTYRELDERANRLAAGLraLG----VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPL---NP-RLPAEELAYILE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 QTRPTAAVADagyidsvaktvsSSVAAAGGDNARARLAATAMLGSLRWLAVDELEREREGGGDGPGPEAPYVGCGPDDVY 216
Cdd:pfam00501 91 DSGAKVLITD------------DALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 217 LIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYD----LHPGSVIVSWLPQYHDCGLV-FLLLTVVAGATCVLAAPGVFL 291
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 292 RrPRLWLELVSEFGATCTP-VPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPIYESSVDEFVEAFCSHglrats 370
Cdd:pfam00501 239 D-PAALLELIERYKVTVLYgVPTLLNMLLEAGAPKRALLS-------SLRLVLSGGAPLPPELARRFRELFGGA------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 371 VSPSYGLAENCTFVSTAWRTSESSSGhIPSYMKLLPSArlspppssaanevpeiEIAVVDEDTGEPVEDGVEGEIWVSSP 450
Cdd:pfam00501 305 LVNGYGLTETTGVVTTPLPLDEDLRS-LGSVGRPLPGT----------------EVKIVDDETGEPVPPGEPGELCVRGP 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1205983844 451 SNASGYLGHPSATREVFcarVPGRagacFVRTGDRGVVRgPERYLYVVGRSADVI 505
Cdd:pfam00501 368 GVMKGYLNDPELTAEAF---DEDG----WYRTGDLGRRD-EDGYLEIVGRKKDQI 414
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
83-629 |
1.87e-62 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 219.23 E-value: 1.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 83 RRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDParfdgPAHAHLLRAV-SQTRPTaavadagyidsvakTVSSSV 161
Cdd:PRK12476 90 GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPEL-----PGHAERLDTAlRDAEPT--------------VVLTTT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 162 AAAggDNARARLAATAMLGSLRWLAVDELEreregggDGPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHN 241
Cdd:PRK12476 151 AAA--EAVEGFLRNLPRLRRPRVIAIDAIP-------DSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 242 VRAARKAYD-LHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLRRPRLWLELVSE---FGATCTPVPSFALP 317
Cdd:PRK12476 222 LVQMILSIDlLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRRPQRWIKALSEgsrTGRVVTAAPNFAYE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 318 LvlrrgrGHRRDRRRLLELGSLRNLILIN--EPIYESSVDEFVEAFCSHGLRATSVSPSYGLAENCTFVSTAWRTSESSS 395
Cdd:PRK12476 302 W------AAQRGLPAEGDDIDLSNVVLIIgsEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPSV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 396 GHIPSymKLLPSARLSPPPSSAANEVPEIEI---------AVVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREV 466
Cdd:PRK12476 376 VYLDR--EQLGAGRAVRVAADAPNAVAHVSCgqvarsqwaVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERT 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 467 FCARVPGR-----------AGACFVRTGDRGVVRGPEryLYVVGRSADVITLDdgvggGRrrvhAHY---VETAAFGSAP 532
Cdd:PRK12476 454 FGAKLQSRlaegshadgaaDDGTWLRTGDLGVYLDGE--LYITGRIADLIVID-----GR----NHYpqdIEATVAEASP 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 533 dRLRGGCVAAFATSStlwsrSQTGVVAVVAElQKVIAGVGDHRGLCDGIRAAVWRDEGVMVGLAVLVDGGVVPKTTSGKL 612
Cdd:PRK12476 523 -MVRRGYVTAFTVPA-----EDNERLVIVAE-RAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKL 595
|
570
....*....|....*..
gi 1205983844 613 RRGAAREMLAAGKLPVV 629
Cdd:PRK12476 596 ARRACRAQYLDGRLGVH 612
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
51-659 |
4.90e-59 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 216.57 E-value: 4.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 51 DAASTRTALTYAQLDAAAGRMARNLLGTVGSlrrGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPARfdgPAH-A 129
Cdd:PRK05691 33 DDPGEGVVLSYRDLDLRARTIAAALQARASF---GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESAR---RHHqE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 130 HLLRAVSQTRPTAAVADAGYIDSVAKtvsssvaaaggdnararLAATAMLGSLRWLAVDELEREREGGGDGPGPEapyvg 209
Cdd:PRK05691 107 RLLSIIADAEPRLLLTVADLRDSLLQ-----------------MEELAAANAPELLCVDTLDPALAEAWQEPALQ----- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 210 cgPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAY--DLHPGSVIVSWLPQYHDCGLV-FLLLTVVAGATCVLAA 286
Cdd:PRK05691 165 --PDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPLYHDMGLIgGLLQPIFSGVPCVLMS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 287 PGVFLRRPRLWLELVSEFGATCTPVPSFALPLVlrrgrghrrdrRRLLELGSLRNLILIN--------EPIYESSVDEFV 358
Cdd:PRK05691 243 PAYFLERPLRWLEAISEYGGTISGGPDFAYRLC-----------SERVSESALERLDLSRwrvaysgsEPIRQDSLERFA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 359 EAFCSHGLRATSVSPSYGLAENCTFVSTAWRtsesssGHIPSYMKL----LPSARLSP----PPSSAANEVPEIEIAVVD 430
Cdd:PRK05691 312 EKFAACGFDPDSFFASYGLAEATLFVSGGRR------GQGIPALELdaeaLARNRAEPgtgsVLMSCGRSQPGHAVLIVD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 431 EDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCArvpgRAGACFVRTGDRGVVRGPEryLYVVGRSADVITLddg 510
Cdd:PRK05691 386 PQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE----HDGRTWLRTGDLGFLRDGE--LFVTGRLKDMLIV--- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 511 vgggrrRVHAHYVE--TAAFGSAPDRLRGGCVAAFATSstlwSRSQTGvVAVVAELQKVIAGVGDHRGLCDGIRAAVWRD 588
Cdd:PRK05691 457 ------RGHNLYPQdiEKTVEREVEVVRKGRVAAFAVN----HQGEEG-IGIAAEISRSVQKILPPQALIKSIRQAVAEA 525
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205983844 589 EGVMVGLAVLVDGGVVPKTTSGKLRRGAAREMLAAGKLpvVFEARYDDGNGPVAALRTAE-EEMAGKSAASW 659
Cdd:PRK05691 526 CQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL--DSYALFPALQAVEAAQTAASgDELQARIAAIW 595
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
83-626 |
9.53e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 206.50 E-value: 9.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 83 RRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDParfdgPAHAHLLRAV-SQTRPTAAVADAGYIDSVAKTVSSSV 161
Cdd:PRK07769 77 KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPAE-----PGHVGRLHAVlDDCTPSAILTTTDSAEGVRKFFRARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 162 AaaggdNARARLaatamlgslrwLAVDELEREREGGGDGPGPEApyvgcgpDDVYLIQYTSGATGVPRPVVVTAGSAAHN 241
Cdd:PRK07769 152 A-----KERPRV-----------IAVDAVPDEVGATWVPPEANE-------DTIAYLQYTSGSTRIPAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 242 VRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLRRPRLWLELVS----EFGATCTPVPSFALP 317
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRPGRWIRELArkpgGTGGTFSAAPNFAFE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 318 LvlrrgRGHRRDRRRLLELGSLRNLI-LIN--EPIYESSVDEFVEAFCSHGLRATSVSPSYGLAENCTFVSTAWRTSESS 394
Cdd:PRK07769 289 H-----AAARGLPKDGEPPLDLSNVKgLLNgsEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 395 SGHIPSYMklLPSARLSPPPSSAANEVPEI--------EIAV-VDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATRE 465
Cdd:PRK07769 364 VIYVDRDE--LNAGRFVEVPADAPNAVAQVsagkvgvsEWAViVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 466 VFCARVPGR----------AGACFVRTGDRGVVRGPEryLYVVGRSADVITLDdgvggGRRrvhaHY---VETAAFGSAP 532
Cdd:PRK07769 442 TFQNILKSRlseshaegapDDALWVRTGDYGVYFDGE--LYITGRVKDLVIID-----GRN----HYpqdLEYTAQEATK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 533 dRLRGGCVAAFAT-----SSTLWSRSQTGV----------VAVVAElQKVIAGVGDHRGLCDGIRAAVWRDEGVMVGLAV 597
Cdd:PRK07769 511 -ALRTGYVAAFSVpanqlPQVVFDDSHAGLkfdpedtseqLVIVAE-RAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVL 588
|
570 580
....*....|....*....|....*....
gi 1205983844 598 LVDGGVVPKTTSGKLRRGAAREMLAAGKL 626
Cdd:PRK07769 589 LVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
58-624 |
1.99e-55 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 199.08 E-value: 1.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 58 ALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvpPDPARFDGPAH--AHLLRAV 135
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLAL--GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL--PLPMGFGGRESyiAQLRGML 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 136 SQTRPTAAVADAGYIDSVAktvsssvAAAGGDNARARLAATAMLgsLRWLAVDELERERegggdgpgpeapyvgcgPDDV 215
Cdd:PRK09192 125 ASAQPAAIITPDELLPWVN-------EATHGNPLLHVLSHAWFK--ALPEADVALPRPT-----------------PDDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 216 YLIQYTSGATGVPRPVVVTAGSAAHNVRA-ARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCV-LAAPGVFLRR 293
Cdd:PRK09192 179 AYLQYSSGSTRFPRGVIITHRALMANLRAiSHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVdYLPTRDFARR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 294 PRLWLELVSEFGATCTPVPSFALPLVlrrgrghrrdrRRLLELGSLRNLILIN--------EPIYESSVDEFVEAFCSHG 365
Cdd:PRK09192 259 PLQWLDLISRNRGTISYSPPFGYELC-----------ARRVNSKDLAELDLSCwrvagigaDMIRPDVLHQFAEAFAPAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 366 LRATSVSPSYGLAENCTFVS-----------TAWRTSESSSGHipsymkllpsARLSPPPSSAANE-------VPEIEIA 427
Cdd:PRK09192 328 FDDKAFMPSYGLAEATLAVSfsplgsgivveEVDRDRLEYQGK----------AVAPGAETRRVRTfvncgkaLPGHEIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 428 VVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVfcaRVPGragacFVRTGDRGVVRgpERYLYVVGRSADVITL 507
Cdd:PRK09192 398 IRNEA-GMPLPERVVGHICVRGPSLMSGYFRDEESQDVL---AADG-----WLDTGDLGYLL--DGYLYITGRAKDLIII 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 508 DDgvgggrRRVHAHYVETAAfgSAPDRLRGGCVAAFATsstlwsrSQTGVVAVVAELQKVIAGVGDHRGLCDGIRAAVWR 587
Cdd:PRK09192 467 NG------RNIWPQDIEWIA--EQEPELRSGDAAAFSI-------AQENGEKIVLLVQCRISDEERRGQLIHALAALVRS 531
|
570 580 590
....*....|....*....|....*....|....*..
gi 1205983844 588 DEGVMVgLAVLVDGGVVPKTTSGKLRRGAAREMLAAG 624
Cdd:PRK09192 532 EFGVEA-AVELVPPHSLPRTSSGKLSRAKAKKRYLSG 567
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
38-627 |
2.65e-54 |
|
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: 192.72 E-value: 2.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 38 AFATKPAFIWADddaastrTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVP 117
Cdd:COG0318 11 RHPDRPALVFGG-------RRLTYAELDARARRLAAALRAL--GVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 118 PDPARfdgpAHAHLLRavsqtrptaavadagyidsvaktvsssvaaaggdNARARLAATAmlgslrwlavdelereregg 197
Cdd:COG0318 82 RLTAE----ELAYILE----------------------------------DSGARALVTA-------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 198 gdgpgpeapyvgcgpddvyLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGL-VFLLLTV 276
Cdd:COG0318 104 -------------------LILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 277 VAGATCVLAAPgvflRRPRLWLELVSEFGATCTP-VPSFALPLVlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVD 355
Cdd:COG0318 165 LAGATLVLLPR----FDPERVLELIERERVTVLFgVPTMLARLL-------RHPEFARYDLSSLRLVVSGGAPLPPELLE 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 356 EFVEAFcshGLRatsVSPSYGLAENCTFVSTAwrtsesssghipsymkllPSARLSPPPSSAANEVPEIEIAVVDEDtGE 435
Cdd:COG0318 234 RFEERF---GVR---IVEGYGLTETSPVVTVN------------------PEDPGERRPGSVGRPLPGVEVRIVDED-GR 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 436 PVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVRgPERYLYVVGRSADVItlddgVGGGR 515
Cdd:COG0318 289 ELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF------RDG--WLRTGDLGRLD-EDGYLYIVGRKKDMI-----ISGGE 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 516 R--------RVHAHY--VETAAFGsAPDRLRGGCVAAFAtssTLWSRSQTGVVAVVAELQKVIAGVGdhrglcdGIRAAV 585
Cdd:COG0318 355 NvypaeveeVLAAHPgvAEAAVVG-VPDEKWGERVVAFV---VLRPGAELDAEELRAFLRERLARYK-------VPRRVE 423
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1205983844 586 WRDEgvmvglavlvdggvVPKTTSGKLRRGAAREMLAAGKLP 627
Cdd:COG0318 424 FVDE--------------LPRTASGKIDRRALRERYAAGALE 451
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
45-616 |
9.66e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 177.44 E-value: 9.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 45 FIWADDDAASTRTALTYAQLDAAAGRMARNLLgTVGSLrrGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPdparfd 124
Cdd:PRK05850 22 FIDYEQDPAGVAETLTWSQLYRRTLNVAEELR-RHGST--GDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 125 gpahahlLRAVSQTRPTAAVADAGyiDSVAKTVSSSVAAAGGDNARARLAATAMLgslrwLAVDELEREREGGGDGPGPE 204
Cdd:PRK05850 93 -------QGGAHDERVSAVLRDTS--PSVVLTTSAVVDDVTEYVAPQPGQSAPPV-----IEVDLLDLDSPRGSDARPRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 205 ApyvgcgPDDVYLiQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSV------IVSWLPQYHDCGLVF-LLLTVV 277
Cdd:PRK05850 159 L------PSTAYL-QYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFGDTGGVpppdttVVSWLPFYHDMGLVLgVCAPIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 278 AGATCVLAAPGVFLRRPRLWLELVSEFGATCTPVPSFALPLvlrrgrGHRRDRRRLLELGSLRN-LILIN--EPIYESSV 354
Cdd:PRK05850 232 GGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFEL------AVRKTSDDDMAGLDLGGvLGIISgsERVHPATL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 355 DEFVEAFCSHGLRATSVSPSYGLAENCTFVSTawrtseSSSGHIPSYMKL----LPSARLSPPPSSAANE-----VPEIE 425
Cdd:PRK05850 306 KRFADRFAPFNLRETAIRPSYGLAEATVYVAT------REPGQPPESVRFdyekLSAGHAKRCETGGGTPlvsygSPRSP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 426 IA-VVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCARV----PGRAGACFVRTGDRGVVRGPEryLYVVGR 500
Cdd:PRK05850 380 TVrIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLvdpsPGTPEGPWLRTGDLGFISEGE--LFIVGR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 501 SADVITLDdgvggGRRrvhaHYvetaafgsaPD-------RLRGGCVAAFATSStlwsrSQTGVVAVVAELQKVIAGVGD 573
Cdd:PRK05850 458 IKDLLIVD-----GRN----HY---------PDdieatiqEITGGRVAAISVPD-----DGTEKLVAIIELKKRGDSDEE 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1205983844 574 HRGLCDGIR----AAVWRDEGVMVGLAVLVDGGVVPKTTSGKLRRGA 616
Cdd:PRK05850 515 AMDRLRTVKrevtSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAA 561
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
50-627 |
1.96e-43 |
|
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: 164.83 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 50 DDAASTRTALTYAQLDAAAGRMARNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPARfdgpaha 129
Cdd:cd05905 6 DSKGKEATTLTWGKLLSRAEKIAAVLQKKVG-LKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQ------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 130 hllrAVSQTRPTAAVAdagyidsVAKTVSSSVAAAGGDNARARLAATAMLgSLRWLAVDELEREREGGGDGPGPEAPYVG 209
Cdd:cd05905 78 ----QLGFLLGTCKVR-------VALTVEACLKGLPKKLLKSKTAAEIAK-KKGWPKILDFVKIPKSKRSKLKKWGPHPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 210 CGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVF-LLLTVVAGATCVLAAPG 288
Cdd:cd05905 146 TRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHgCLLSVYSGHHTILIPPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 289 VFLRRPRLWLELVSEFGATCTPVPSFALPL-VLRRGRGHRRDRRRLLELGSLRNLILINE-PIYESSVDEFVEAFCSHGL 366
Cdd:cd05905 226 LMKTNPLLWLQTLSQYKVRDAYVKLRTLHWcLKDLSSTLASLKNRDVNLSSLRMCMVPCEnRPRISSCDSFLKLFQTLGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 367 RATSVSPSYGLAENcTFVSTAwRTSESSSGHIPSYMKLLPSARLSPPPSSAANEV---------PEIEIAVVDEDTGEPV 437
Cdd:cd05905 306 SPRAVSTEFGTRVN-PFICWQ-GTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLplqdsgkvlPGAQVAIVNPETKGLC 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 438 EDGVEGEIWVSSPSNASGYLGHPSATREVFCARVPGRAGAC-----FVRTGDRGVVRGPERY---------LYVVGRSAD 503
Cdd:cd05905 384 KDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGitnnsYARTGLLGFLRPTKCTdlnveehdlLFVVGSIDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 504 VITLDdgvggGRRRvHAHYVETAAFGSAPDrlRGGCvAAFatsstlwsrSQTGVVAVVAELQKVI-AGVGDhrgLCDGIR 582
Cdd:cd05905 464 TLEVR-----GLRH-HPSDIEATVMRVHPY--RGRC-AVF---------SITGLVVVVAEQPPGSeEEALD---LVPLVL 522
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1205983844 583 AAVWRDEGVMVGLAVLVDGGVVPKTTSGKLRRGAAREMLAAGKLP 627
Cdd:cd05905 523 NAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLH 567
|
|
| FAAL_FadD21 |
NF038337 |
fatty-acid--AMP ligase FAAL21/FadD21; |
44-619 |
1.46e-40 |
|
fatty-acid--AMP ligase FAAL21/FadD21;
Pssm-ID: 439631 [Multi-domain] Cd Length: 579 Bit Score: 156.96 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 44 AFIWAD--DDAASTRTALTYAQLdaaagrmARNLLGTVGSLRR----GDAVLVLASPGLRLVKLLFACQRAGLTAVPVVP 117
Cdd:NF038337 22 AFRYTDyeQDWAGVTETLTWAQL-------YRRTLNVAHEVRRhgttGDRAVILAPQGLPYIVAFLGAMQAGLIAVPLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 118 PDPARFDgpahahllravsqTRPTAAVADAGyiDSVAKTVSssvAAAGGDNARARLAATAMLGSLrwLAVDELEreregg 197
Cdd:NF038337 95 PQPGSHD-------------ERVSAVLADTS--PSVVLTTS---AAAAAVAEYLHRPDTGAVPAV--IEIDSLD------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 198 GDGPGPEAPYVGCGPDDVYLiQYTSGATGVPRPVVVTAGSAAHNVRAARKAY--DLH----PGSVIVSWLPQYHDCGLVF 271
Cdd:NF038337 149 LDGPNSPSIRISDAPSIAYL-QYTSGSTRLPAGVMVSHRNLQVNFQQLMAAYfpDTNgvapRDTTIVSWLPFYHDMGLVL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 272 -LLLTVVAGATCVLAAPGVFLRRPRLWLELVSEFGATCTPVPSFALPLvlrrgrGHRRDRRRLLELGSLRNLILI---NE 347
Cdd:NF038337 228 gVIAPILGGYRSELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFEL------AVRKTTDADLAGLDLGNVIGIvsgAE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 348 PIYESSVDEFVEAFCSHGLRATSVSPSYGLAENCTFVSTAWRTSESSSGHI-PSYM-----KLLPSARLSPPPSSAANEV 421
Cdd:NF038337 302 RIHPATLDRFCKRFAPYNFREDMMQPSYGLAEATVYVASRAEGGAPEVVHFePEKLsegsaQRCEARTGSPLLSYGTPTS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 422 PEIEIavVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCARV----PGRAGACFVRTGDRGVVRGPEryLYV 497
Cdd:NF038337 382 PTVRI--VDPDTCIECPAGTVGEIWVHGDNVAEGYWQKPEETRRTFGGVLanpsPGTPEGPWLRTGDLGFISEDE--MFI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 498 VGRSADVITLddgvgGGRRrvhaHYVETAAfgSAPDRLRGGCVAAFATSStlwsrSQTGVVAVVAELQKVIAGVGDHRGL 577
Cdd:NF038337 458 VGRMKDLLIV-----YGRN----HYPEDIE--STVQEITGGRVAAISVPV-----DETEKLVTIIELKKRGDSDEEAMRK 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1205983844 578 CDGIR----AAVWRDEGVMVGLAVLVDGGVVPKTTSGKLRRGAARE 619
Cdd:NF038337 522 LDAVKnnvtAAISRSHGLNVADLVLVPPGSIPTTTSGKIRRAACVE 567
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
211-622 |
1.99e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 155.92 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 211 GPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGS-VIVSWLPQYHDCGLV-FLLLTVVAGATCVLAAPG 288
Cdd:PRK07768 150 GEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETdVMVSWLPLFHDMGMVgFLTVPMYFGAELVKVTPM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 289 VFLRRPRLWLELVSEFGATCTPVPSFALPLVlrRGRGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFCSHGLRA 368
Cdd:PRK07768 230 DFLRDPLLWAELISKYRGTMTAAPNFAYALL--ARRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRP 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 369 TSVSPSYGLAENCTFVS-----TAWRTSESSSGHIPSYMKLLPS--------ARLSPPpssaaneVPEIEIAVVDEDtGE 435
Cdd:PRK07768 308 EAILPAYGMAEATLAVSfspcgAGLVVDEVDADLLAALRRAVPAtkgntrrlATLGPP-------LPGLEVRVVDED-GQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 436 PVEDGVEGEIWVSSPSNASGYLghpsaTREVFcarVPGRAGACFVRTGDRGVVRGPERyLYVVGRSADVITLddgvggGR 515
Cdd:PRK07768 380 VLPPRGVGVIELRGESVTPGYL-----TMDGF---IPAQDADGWLDTGDLGYLTEEGE-VVVCGRVKDVIIM------AG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 516 RRVHAHYVETAAfgSAPDRLRGGCVAAFATssTLWSRSQTGVVAVVAELQKVIAGVgdhRGLCDGIRAAVWRDEGVMVGL 595
Cdd:PRK07768 445 RNIYPTDIERAA--ARVEGVRPGNAVAVRL--DAGHSREGFAVAVESNAFEDPAEV---RRIRHQVAHEVVAEVGVRPRN 517
|
410 420
....*....|....*....|....*..
gi 1205983844 596 AVLVDGGVVPKTTSGKLRRGAAREMLA 622
Cdd:PRK07768 518 VVVLGPGSIPKTPSGKLRRANAAELVT 544
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
51-624 |
1.05e-39 |
|
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: 153.59 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 51 DAASTRTALTYAQLDAAAGRMARnLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPARFDGPAHAH 130
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAA-GLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 131 LLRAVSQTRPTAAVADAGYIDSVAKtvsssvaaaggdnararLAATAMLGSLRWLAVDELEREREGGGDGPgpeapyvgC 210
Cdd:cd05906 110 LRHIWQLLGSPVVLTDAELVAEFAG-----------------LETLSGLPGIRVLSIEELLDTAADHDLPQ--------S 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 211 GPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFL-LLTVVAGATCVLAAPGV 289
Cdd:cd05906 165 RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 290 FLRRPRLWLELVSEFGATCTPVPSFALPLVlrrGRGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFCSHGLRAT 369
Cdd:cd05906 245 ILADPLRWLDLIDRYRVTITWAPNFAFALL---NDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 370 SVSPSYGLAENCtfvstawrtsessSGHIpsYmkllpSARLSPPPSSAANE-------VPEIEIAVVDEDtGEPVEDGVE 442
Cdd:cd05906 322 AIRPAFGMTETC-------------SGVI--Y-----SRSFPTYDHSQALEfvslgrpIPGVSMRIVDDE-GQLLPEGEV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 443 GEIWVSSPSNASGYLGHPSATREVFcarvpgRAGACFvRTGDRGVVRGPEryLYVVGRSADVITLdDGVgggrrRVHAHY 522
Cdd:cd05906 381 GRLQVRGPVVTKGYYNNPEANAEAF------TEDGWF-RTGDLGFLDNGN--LTITGRTKDTIIV-NGV-----NYYSHE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 523 VETAAfgsapDRLRG---GCVAAFATsstlwsRSQTGVVAVVAELQKVIAGVGDHRG-LCDGIRAAVWRDEGVMVGLAVL 598
Cdd:cd05906 446 IEAAV-----EEVPGvepSFTAAFAV------RDPGAETEELAIFFVPEYDLQDALSeTLRAIRSVVSREVGVSPAYLIP 514
|
570 580
....*....|....*....|....*.
gi 1205983844 599 VDGGVVPKTTSGKLRRGAAREMLAAG 624
Cdd:cd05906 515 LPKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
214-543 |
2.03e-37 |
|
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: 142.42 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 214 DVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPgvflRR 293
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK----FD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 294 PRLWLELVSEFGATCTP-VPSFALPLVlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcshGLRATSVs 372
Cdd:cd04433 77 PEAALELIEREKVTILLgVPTLLARLL-------KAPESAGYDLSSLRALVSGGAPLPPELLERFEEAP---GIKLVNG- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 373 psYGLAENCTFVSTAWRTSESSsghipsymkllpsarlspPPSSAANEVPEIEIAVVDEDTGEpVEDGVEGEIWVSSPSN 452
Cdd:cd04433 146 --YGLTETGGTVATGPPDDDAR------------------KPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 453 ASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVRgPERYLYVVGRSADVITlddgVGGgrRRVHAHYVET------- 525
Cdd:cd04433 205 MKGYWNNPEATAAVD------EDG--WYRTGDLGRLD-EDGYLYIVGRLKDMIK----SGG--ENVYPAEVEAvllghpg 269
|
330 340
....*....|....*....|..
gi 1205983844 526 ----AAFGsAPDRLRGGCVAAF 543
Cdd:cd04433 270 vaeaAVVG-VPDPEWGERVVAV 290
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
25-622 |
1.41e-33 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 136.01 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 25 VVDRYLPvwaklpAFATKPAFIWADDDAASTRtaLTYAQLDAAAGRMArNLLGTVGsLRRGDAVLVLASPGLRLVKLLFA 104
Cdd:COG0365 14 CLDRHAE------GRGDKVALIWEGEDGEERT--LTYAELRREVNRFA-NALRALG-VKKGDRVAIYLPNIPEAVIAMLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 105 CQRAGLTAVPVVPpdpaRFdgPAHAHLLRaVSQTRPTAAVADAGYIDsVAKTVSSSVAAaggDNARARL----------- 173
Cdd:COG0365 84 CARIGAVHSPVFP----GF--GAEALADR-IEDAEAKVLITADGGLR-GGKVIDLKEKV---DEALEELpslehvivvgr 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 174 --AATAMLGSLRWlavDELerereggGDGPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVV-VTAGSAAHNVRAARKAYD 250
Cdd:COG0365 153 tgADVPMEGDLDW---DEL-------LAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVhTHGGYLVHAATTAKYVLD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 251 LHPGSVIVSwlpqYHDCGLVFLLLTVV-----AGATCVLAAPGVFLRRPRLWLELVSEFGAT--CT-------------- 309
Cdd:COG0365 223 LKPGDVFWC----TADIGWATGHSYIVygpllNGATVVLYEGRPDFPDPGRLWELIEKYGVTvfFTaptairalmkagde 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 310 PVPSFALPlvlrrgrghrrdrrrllelgSLRNLILINEPIYESSVDEFVEAFcshglratsvspsyglaeNCTFVSTAWR 389
Cdd:COG0365 299 PLKKYDLS--------------------SLRLLGSAGEPLNPEVWEWWYEAV------------------GVPIVDGWGQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 390 TsESssGHIpsyMkLLPSARLSPPPSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWV--SSPSNASGYLGHPSATREVF 467
Cdd:COG0365 341 T-ET--GGI---F-ISNLPGLPVKPGSMGKPVPGYDVAVVDED-GNPVPPGEEGELVIkgPWPGMFRGYWNDPERYRETY 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 468 CARVPGragacFVRTGDrGVVRGPERYLYVVGRSADVITlddgVGGgrRRV-----------HAHYVETAAFGsAPDRLR 536
Cdd:COG0365 413 FGRFPG-----WYRTGD-GARRDEDGYFWILGRSDDVIN----VSG--HRIgtaeiesalvsHPAVAEAAVVG-VPDEIR 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 537 GGCVAAFatsstlwsrsqtgvvaVVAElqkviAGVGDHRGLCDGIRAAVwRDEgvmvgLA--------VLVDGgvVPKTT 608
Cdd:COG0365 480 GQVVKAF----------------VVLK-----PGVEPSDELAKELQAHV-REE-----LGpyaypreiEFVDE--LPKTR 530
|
650
....*....|....
gi 1205983844 609 SGKLRRGAAREMLA 622
Cdd:COG0365 531 SGKIMRRLLRKIAE 544
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
60-500 |
9.30e-33 |
|
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: 130.85 E-value: 9.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 60 TYAQLDAAAGRMARNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPA-RFdgpahAHLLRAvsqT 138
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG-VGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAeRL-----AFILED---A 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 139 RPTAAVADAGYIDSVAktvsssvaaaggdnaraRLAATAMLGSLRWLAVDELEREREGGGdgpgpeapyVGCGPDDVYLI 218
Cdd:TIGR01733 72 GARLLLTDSALASRLA-----------------GLVLPVILLDPLELAALDDAPAPPPPD---------APSGPDDLAYV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 219 QYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLRRPRLWL 298
Cdd:TIGR01733 126 IYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 299 ELVSEFGATC-TPVPSFALPLVlrrgrghrrdRRRLLELGSLRNLILINEPIYESSVDEFVEAFCSHGLRATsvspsYGL 377
Cdd:TIGR01733 206 ALIAEHPVTVlNLTPSLLALLA----------AALPPALASLRLVILGGEALTPALVDRWRARGPGARLINL-----YGP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 378 AEnCTFVSTAWRTsessSGHIPSYMKLLPSARlspppssaanEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYL 457
Cdd:TIGR01733 271 TE-TTVWSTATLV----DPDDAPRESPVPIGR----------PLANTRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYL 334
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1205983844 458 GHPSATREVFCAR-VPGRAGACFVRTGDRGVVRgPERYLYVVGR 500
Cdd:TIGR01733 335 NRPELTAERFVPDpFAGGDGARLYRTGDLVRYL-PDGNLEFLGR 377
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
212-625 |
1.65e-32 |
|
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: 131.84 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLV-FLLLTVVAGATCVLAAPGVF 290
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIaFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 291 LRRPRLWLELVSEFGATCTPVPSFALPLVlrrGRGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFCSHGLRATS 370
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSPNFGYKYF---LKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 371 VSPSYGLAENCTFVSTAWRTSESSSGHIPSYMKLL--PSARLSPPPSSAANEV------PEIEIAVVDEDTgEPVEDGVE 442
Cdd:cd05908 262 ILPVYGLAEASVGASLPKAQSPFKTITLGRRHVTHgePEPEVDKKDSECLTFVevgkpiDETDIRICDEDN-KILPDGYI 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 443 GEIWVSSPSNASGYLGHPSATREVFCARvpgragaCFVRTGDRGVVRGPEryLYVVGRSADVITlddgVGGgrRRVHAHY 522
Cdd:cd05908 341 GHIQIRGKNVTPGYYNNPEATAKVFTDD-------GWLKTGDLGFIRNGR--LVITGREKDIIF----VNG--QNVYPHD 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 523 VETAAFGSAPDRLrgGCVAAFATSSTlwSRSQTGVVAVVAELQKviagVGDHRGLCDGIRAAVWRDEGVMVGLAVLVDgg 602
Cdd:cd05908 406 IERIAEELEGVEL--GRVVACGVNNS--NTRNEEIFCFIEHRKS----EDDFYPLGKKIKKHLNKRGGWQINEVLPIR-- 475
|
410 420
....*....|....*....|...
gi 1205983844 603 VVPKTTSGKLRRGAAREMLAAGK 625
Cdd:cd05908 476 RIPKTTSGKVKRYELAQRYQSGE 498
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
56-500 |
1.23e-30 |
|
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: 125.33 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 56 RTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPArfdgpahAHLLRAV 135
Cdd:cd05930 10 DQSLTYAELDARANRLARYLRER--GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPA-------ERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 136 SQTRPTAAVADAGyidsvaktvsssvaaaggdnararlaatamlgslrwlavdelereregggdgpgpeapyvgcgpDDV 215
Cdd:cd05930 81 EDSGAKLVLTDPD----------------------------------------------------------------DLA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 216 YLIqYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVfLRRPR 295
Cdd:cd05930 97 YVI-YTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEV-RKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 296 LWLELVSEFGATCT-PVPSFALPLVlrrgrghrrDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcsHGLRATSVsps 374
Cdd:cd05930 175 ALADLLAEEGITVLhLTPSLLRLLL---------QELELAALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNL--- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 375 YGLAEnCTFVSTAWRTSEsssghipsymkllPSARLSPPP--SSAANevpeIEIAVVDEDtGEPVEDGVEGEIWVSSPSN 452
Cdd:cd05930 241 YGPTE-ATVDATYYRVPP-------------DDEEDGRVPigRPIPN----TRVYVLDEN-LRPVPPGVPGELYIGGAGL 301
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1205983844 453 ASGYLGHPSATREVFCArVPGRAGACFVRTGDRGVVRgPERYLYVVGR 500
Cdd:cd05930 302 ARGYLNRPELTAERFVP-NPFGPGERMYRTGDLVRWL-PDGNLEFLGR 347
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
212-625 |
1.56e-29 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 123.34 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGS-VIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVF 290
Cdd:PRK05851 151 SGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATdVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAF 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 291 LRRPRLWLELVSEFGATCTPVPSFALPLVlrrgrGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFCSHGLRATS 370
Cdd:PRK05851 231 SASPFRWLSWLSDSRATLTAAPNFAYNLI-----GKYARRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 371 VSPSYGLAENCTFVStawrTSESSSGhipsymklLPSARLSPPPSSAA-------NEVPEIEIAVVDEDTGEPVEDGVEG 443
Cdd:PRK05851 306 AAPSYGLAESTCAVT----VPVPGIG--------LRVDEVTTDDGSGArrhavlgNPIPGMEVRISPGDGAAGVAGREIG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 444 EIWVSSPSNASGYLGHPsatrevfcarvPGRAGACFvRTGDRGVVRGPEryLYVVGRSADVITlddgVGGgrRRVHAHYV 523
Cdd:PRK05851 374 EIEIRGASMMSGYLGQA-----------PIDPDDWF-PTGDLGYLVDGG--LVVCGRAKELIT----VAG--RNIFPTEI 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 524 ETAAfgSAPDRLRGGCVAAFATSstlwSRSQTGVVAVVAELqkviagVGDHRglcDGIRAAVWR----DEGVMVGLAVLV 599
Cdd:PRK05851 434 ERVA--AQVRGVREGAVVAVGTG----EGSARPGLVIAAEF------RGPDE---AGARSEVVQrvasECGVVPSDVVFV 498
|
410 420
....*....|....*....|....*.
gi 1205983844 600 DGGVVPKTTSGKLRRGAAREMLAAGK 625
Cdd:PRK05851 499 APGSLPRTSSGKLRRLAVKRSLEAAD 524
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
53-505 |
2.27e-27 |
|
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: 116.16 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 53 ASTRTALTYAQLDAAAGRMARNL--LGtvgsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppDPArFDGPAHAH 130
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLrkLG----LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAA---NPI-YTADELAH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 131 LLRavsQTRPTAAVADAGYIDsvakTVSSSVAAAGG-------DNARARLAATAMLGSLRWLAVDELEreregggdgpgp 203
Cdd:cd05911 77 QLK---ISKPKVIFTDPDGLE----KVKEAAKELGPkdkiivlDDKPDGVLSIEDLLSPTLGEEDEDL------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 204 eAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLH--PGSVIVSWLPQYHDCGLVFLLLTVVAGAT 281
Cdd:cd05911 138 -PPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLFTTLASLLNGAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 282 cvlaapGVFLRR--PRLWLELVSEFGATCTPVPSfalPLVlrrgrghrrdrrrllelgslrnLILINEPIYE----SSVD 355
Cdd:cd05911 217 ------VIIMPKfdSELFLDLIEKYKITFLYLVP---PIA----------------------AALAKSPLLDkydlSSLR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 356 EF----------VEAFCSHGLRATSVSPSYGLAENC--TFVSTAWRTSESSSGHIpsymkllpsarlspppssaaneVPE 423
Cdd:cd05911 266 VIlsggaplskeLQELLAKRFPNATIKQGYGMTETGgiLTVNPDGDDKPGSVGRL----------------------LPN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 424 IEIAVVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpGRAGacFVRTGDRGVVRgPERYLYVVGRSAD 503
Cdd:cd05911 324 VEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETF-----DEDG--WLHTGDIGYFD-EDGYLYIVDRKKE 395
|
..
gi 1205983844 504 VI 505
Cdd:cd05911 396 LI 397
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
39-543 |
2.22e-26 |
|
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: 113.04 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 39 FATKPAFIWADddaastrTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPp 118
Cdd:cd05936 12 FPDKTALIFMG-------RKLTYRELDALAEAFAAGLQNL--GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 119 dpaRFDGPAHAHLLRavsqtrptaavadagyiDSVAKTVSSSVAaaggdnaRARLAATAMLGSLRwlavdelerereggg 198
Cdd:cd05936 82 ---LYTPRELEHILN-----------------DSGAKALIVAVS-------FTDLLAAGAPLGER--------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 199 dgpgpeapyVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAY--DLHPGSVIVSWLPQYHDCGL-VFLLLT 275
Cdd:cd05936 120 ---------VALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLtVALLLP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 276 VVAGATCVLaapgvFLR-RPRLWLELVSEFGATCTP-VPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPIYESS 353
Cdd:cd05936 191 LALGATIVL-----IPRfRPIGVLKEIRKHRVTIFPgVPTMYIALLNAPEFKKRDFS-------SLRLCISGGAPLPVEV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 354 VDEFVEAFcshGLRatsVSPSYGLaenctfvstawrtSESSsghipsymkllPSARLSPP-----PSSAANEVPEIEIAV 428
Cdd:cd05936 259 AERFEELT---GVP---IVEGYGL-------------TETS-----------PVVAVNPLdgprkPGSIGIPLPGTEVKI 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 429 VDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGvVRGPERYLYVVGRSADVITld 508
Cdd:cd05936 309 VDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF------VDG--WLRTGDIG-YMDEDGYFFIVDRKKDMII-- 376
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1205983844 509 dgVGGGR---RRV----HAH-YVETAAFGSAPDRLRGGCVAAF 543
Cdd:cd05936 377 --VGGFNvypREVeevlYEHpAVAEAAVVGVPDPYSGEAVKAF 417
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
57-486 |
8.62e-25 |
|
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: 108.59 E-value: 8.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 57 TALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPARfdgpahaHLLRAVS 136
Cdd:cd17651 19 RRLTYAELDRRANRLAHRLRAR--GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE-------RLAFMLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 QTRPTAAVADAGYIDSVAktvsssvaaaggdnarARLAATAMLGSLRWLAVDELEREregggdgpgpeapyVGCGPDDVY 216
Cdd:cd17651 90 DAGPVLVLTHPALAGELA----------------VELVAVTLLDQPGAAAGADAEPD--------------PALDADDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 217 LIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLRRPRL 296
Cdd:cd17651 140 YVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 297 WlELVSEFGATCTPVPSFALPLVlrrgrgHRRDRRRLLELGSLRNLILINEPIyesSVDEFVEAFCShGLRATSVSPSYG 376
Cdd:cd17651 220 A-AWLDEQRISRVFLPTVALRAL------AEHGRPLGVRLAALRYLLTGGEQL---VLTEDLREFCA-GLPGLRLHNHYG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 377 LAENcTFVstawrTSESSSGhipsymklLPSARLSPPPSSAAneVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGY 456
Cdd:cd17651 289 PTET-HVV-----TALSLPG--------DPAAWPAPPPIGRP--IDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGY 351
|
410 420 430
....*....|....*....|....*....|
gi 1205983844 457 LGHPSATREVFCARvPGRAGACFVRTGDRG 486
Cdd:cd17651 352 LNRPELTAERFVPD-PFVPGARMYRTGDLA 380
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
59-486 |
1.97e-24 |
|
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: 109.56 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNL--LGtvgsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPArfdgpahAHLLRAVS 136
Cdd:COG1020 502 LTYAELNARANRLAHHLraLG----VGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPA-------ERLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 QTRPTAAVADAGYidsvaktvsssvaaaggdnaRARLAATAmlgsLRWLAVDELEREREGGGDGPgpeapyVGCGPDDV- 215
Cdd:COG1020 571 DAGARLVLTQSAL--------------------AARLPELG----VPVLALDALALAAEPATNPP------VPVTPDDLa 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 216 YLIqYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVfLRRPR 295
Cdd:COG1020 621 YVI-YTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEA-RRDPA 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 296 LWLELVSEFGATC-TPVPSFALPLVLRRGRGHRrdrrrllelgSLRNLILINEPIYESSVDEFVEAFcsHGLRATSVsps 374
Cdd:COG1020 699 ALAELLARHRVTVlNLTPSLLRALLDAAPEALP----------SLRLVLVGGEALPPELVRRWRARL--PGARLVNL--- 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 375 YGLAEnCTFVSTAWRTSESssghipsymkllPSARLSPP---PssaaneVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPS 451
Cdd:COG1020 764 YGPTE-TTVDSTYYEVTPP------------DADGGSVPigrP------IANTRVYVLDAH-LQPVPVGVPGELYIGGAG 823
|
410 420 430
....*....|....*....|....*....|....*
gi 1205983844 452 NASGYLGHPSATREVFCARVPGRAGACFVRTGDRG 486
Cdd:COG1020 824 LARGYLNRPELTAERFVADPFGFPGARLYRTGDLA 858
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
40-500 |
8.27e-24 |
|
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: 105.02 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 40 ATKPAFIWADDDaastrtaLTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPD 119
Cdd:cd05945 5 PDRPAVVEGGRT-------LTYRELKERADALAAALASL--GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 120 PArfdgpahAHLLRAVSQTRPTAAVADagyidsvaktvsssvaaaggdnararlaatamlgslrwlavdelereregggd 199
Cdd:cd05945 76 PA-------ERIREILDAAKPALLIAD----------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 200 gpgpeapyvgcgPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAG 279
Cdd:cd05945 96 ------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASG 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 280 ATCVLAAPGVfLRRPRLWLELVSEFGATC-TPVPSFALPLvlrrgrgHRRDRRRLLELGSLRNLILINEPIYESSVDEFV 358
Cdd:cd05945 164 ATLVPVPRDA-TADPKQLFRFLAEHGITVwVSTPSFAAMC-------LLSPTFTPESLPSLRHFLFCGEVLPHKTARALQ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 359 EAFcshglRATSVSPSYGLAEnCTFVSTAWRTSEsssgHIPSYMKLLPSARLspppssaaneVPEIEIAVVDEDtGEPVE 438
Cdd:cd05945 236 QRF-----PDARIYNTYGPTE-ATVAVTYIEVTP----EVLDGYDRLPIGYA----------KPGAKLVILDED-GRPVP 294
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205983844 439 DGVEGEIWVSSPSNASGYLGHPSATREVFcarVPGRAGACFvRTGDRGvVRGPERYLYVVGR 500
Cdd:cd05945 295 PGEKGELVISGPSVSKGYLNNPEKTAAAF---FPDEGQRAY-RTGDLV-RLEADGLLFYRGR 351
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
42-505 |
8.28e-24 |
|
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: 104.61 E-value: 8.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 42 KPAFIWADddaastrTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdPA 121
Cdd:cd17631 11 RTALVFGG-------RSLTYAELDERVNRLAHALRAL--GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL----NF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 122 RFDGPAHAHLLRavsqtrptaavadagyiDSVAKTVSssvaaaggdnararlaatamlgslrwlavdelereregggdgp 201
Cdd:cd17631 78 RLTPPEVAYILA-----------------DSGAKVLF------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 202 gpeapyvgcgpDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGL-VFLLLTVVAGA 280
Cdd:cd17631 98 -----------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 281 TCVLAA---PGVFLRrprlwleLVSEFGATCTpvpsFALPLVLRRGRGHRRDRRRLLElgSLRNLILINEPIYESSVDEF 357
Cdd:cd17631 167 TVVILRkfdPETVLD-------LIERHRVTSF----FLVPTMIQALLQHPRFATTDLS--SLRAVIYGGAPMPERLLRAL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 358 VEafcshglRATSVSPSYGLAENCTFVStawrtsesssghipsymkLLPSARLSPPPSSAANEVPEIEIAVVDEDtGEPV 437
Cdd:cd17631 234 QA-------RGVKFVQGYGMTETSPGVT------------------FLSPEDHRRKLGSAGRPVFFVEVRIVDPD-GREV 287
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205983844 438 EDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVRGpERYLYVVGRSADVI 505
Cdd:cd17631 288 PPGEVGEIVVRGPHVMAGYWNRPEATAAAF------RDG--WFHTGDLGRLDE-DGYLYIVDRKKDMI 346
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
42-505 |
2.52e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 95.00 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 42 KPAFIWADddaastrTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdPA 121
Cdd:PRK08316 27 KTALVFGD-------RSWTYAELDAAVNRVAAALLDL--GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV----NF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 122 RFDGPAHAHLLRavsQTRPTAAVADAGyidsVAKTVSSSVAAAGGDNARARLAATAMLGSLRWLAVDELEREREGGGDGP 201
Cdd:PRK08316 94 MLTGEELAYILD---HSGARAFLVDPA----LAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 202 GPEApyvgcgpDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGL-VFLLLTVVAGA 280
Cdd:PRK08316 167 ELAD-------DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLdVFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 281 TCVL-AAPgvflrRPRLWLELVSEFGATCTpvpsFALPLVLRRgrghrrdrrrllelgslrnliLINEPiyessvdefve 359
Cdd:PRK08316 240 TNVIlDAP-----DPELILRTIEAERITSF----FAPPTVWIS---------------------LLRHP----------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 360 AFCSHGLRA-------TSVSPSYGLAEnctfvstawrtsesssghipsYMKLLPSAR----------------LSPP--- 413
Cdd:PRK08316 279 DFDTRDLSSlrkgyygASIMPVEVLKE---------------------LRERLPGLRfyncygqteiaplatvLGPEehl 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 414 --PSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgrAGACFvRTGDRGvVRGP 491
Cdd:PRK08316 338 rrPGSAGRPVLNVETRVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-------RGGWF-HSGDLG-VMDE 407
|
490
....*....|....
gi 1205983844 492 ERYLYVVGRSADVI 505
Cdd:PRK08316 408 EGYITVVDRKKDMI 421
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
21-505 |
6.90e-20 |
|
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: 93.45 E-value: 6.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 21 PDQPVVDRYLPVWAklPAFATKPAFIwaddDAASTRtALTYAQLDAAAGRMARNLLGTVGslRRGDAVLVLASPGLRLVK 100
Cdd:cd05904 2 PTDLPLDSVSFLFA--SAHPSRPALI----DAATGR-ALTYAELERRVRRLAAGLAKRGG--RKGDVVLLLSPNSIEFPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 101 LLFACQRAGLTAVPVVPPDPArfdgpahAHLLRAVSQTRPTAAVADAGYIDSVAKTVSSSVAaagGDNARARLAAtamlG 180
Cdd:cd05904 73 AFLAVLSLGAVVTTANPLSTP-------AEIAKQVKDSGAKLAFTTAELAEKLASLALPVVL---LDSAEFDSLS----F 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 181 SLRWLAVDELERERegggdgpgpeapyVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRA--ARKAYDLHPGSVIV 258
Cdd:cd05904 139 SDLLFEADEAEPPV-------------VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQfvAGEGSNSDSEDVFL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 259 SWLPQYHDCGLVFLLLTVVA-GATcVLAAPGVFLRrprLWLELVSEFGATCTP-VPSFALPLVLRRGRGHRRDRrrllel 336
Cdd:cd05904 206 CVLPMFHIYGLSSFALGLLRlGAT-VVVMPRFDLE---ELLAAIERYKVTHLPvVPPIVLALVKSPIVDKYDLS------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 337 gSLRNLILINEPIYESSVDEFVEAFCShglraTSVSPSYGLAENCTFVSTAwrtsesssghipsymklLPSARLSPPPSS 416
Cdd:cd05904 276 -SLRQIMSGAAPLGKELIEAFRAKFPN-----VDLGQGYGMTESTGVVAMC-----------------FAPEKDRAKYGS 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 417 AANEVPEIEIAVVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcaRVPGragacFVRTGDRGVVRGpERYLY 496
Cdd:cd05904 333 VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI--DKEG-----WLHTGDLCYIDE-DGYLF 404
|
....*....
gi 1205983844 497 VVGRSADVI 505
Cdd:cd05904 405 IVDRLKELI 413
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
40-505 |
7.65e-20 |
|
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: 93.15 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 40 ATKPAFIwadddAASTRTALTYAQLDAAAGRMARNL--LGtvgsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVP 117
Cdd:cd05926 1 PDAPALV-----VPGSTPALTYADLAELVDDLARQLaaLG----IKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 118 P-DPARFDgpahahllRAVSQTRPTAAVADAGYIDSV---AKTVSSSVAAAGGDNARARLAATAmlGSLRWLAVDELERE 193
Cdd:cd05926 72 AyKKAEFE--------FYLADLGSKLVLTPKGELGPAsraASKLGLAILELALDVGVLIRAPSA--ESLSNLLADKKNAK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 194 REGGGDgpgpeapyvgcgPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPG--SVIVswLPQYHDCGLVF 271
Cdd:cd05926 142 SEGVPL------------PDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDdrTLVV--MPLFHVHGLVA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 272 LLLTVVAGATCVLAAPGvFlrRPRLWLELVSEFGAT-CTPVPsfalplvlrrgrghrrdrrrllelgSLRNLILINEPIY 350
Cdd:cd05926 208 SLLSTLAAGGSVVLPPR-F--SASTFWPDVRDYNATwYTAVP-------------------------TIHQILLNRPEPN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 351 ESSVD---EFVEAfCS--------HGLRAT---SVSPSYGLAENCtfvstawrtSESSSGHIPSYMKLLPSArlsPPPSS 416
Cdd:cd05926 260 PESPPpklRFIRS-CSaslppavlEALEATfgaPVLEAYGMTEAA---------HQMTSNPLPPGPRKPGSV---GKPVG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 417 AanevpeiEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcaRVPGragacFVRTGDRGvVRGPERYLY 496
Cdd:cd05926 327 V-------EVRILDED-GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA--FKDG-----WFRTGDLG-YLDADGYLF 390
|
....*....
gi 1205983844 497 VVGRSADVI 505
Cdd:cd05926 391 LTGRIKELI 399
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
55-486 |
1.95e-19 |
|
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: 91.95 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 55 TRTALTYAQLDAAAGRMARNLlgTVGSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPArfdgPAHAHLLRa 134
Cdd:cd17646 20 EGRTLTYRELDERANRLAHLL--RARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPA----DRLAYMLA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 135 vsqtrptaavadagyiDSVAKTVSSSVAAAGgdnARARLAATAMLGSLRWLAVDELEREregggdgpgpeapyVGCGPDD 214
Cdd:cd17646 93 ----------------DAGPAVVLTTADLAA---RLPAGGDVALLGDEALAAPPATPPL--------------VPPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 215 -VYLIqYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVfLRR 293
Cdd:cd17646 140 lAYVI-YTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGG-HRD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 294 PRLWLELVSEFGATCTP-VPSFALPLVLRRGRGHRRdrrrllelgSLRNLILINEPIYESSVDEFVEAFcshglrATSVS 372
Cdd:cd17646 218 PAYLAALIREHGVTTCHfVPSMLRVFLAEPAAGSCA---------SLRRVFCSGEALPPELAARFLALP------GAELH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 373 PSYGLAEnCTFVSTAWRTSesssghipsymkllpsARLSPPPSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSN 452
Cdd:cd17646 283 NLYGPTE-AAIDVTHWPVR----------------GPAETPSVPIGRPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQL 344
|
410 420 430
....*....|....*....|....*....|....
gi 1205983844 453 ASGYLGHPSATREVFCARvPGRAGACFVRTGDRG 486
Cdd:cd17646 345 ARGYLGRPALTAERFVPD-PFGPGSRMYRTGDLA 377
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
8-505 |
2.14e-19 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 92.04 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 8 RAAMSTENYdacYPDQPVVDRYLPVWAKLPafaTKPAFIWADDDAASTRTaLTYAQLDAAAGRMARNL--LGTvgslRRG 85
Cdd:PRK13295 12 RAASIAAGH---WHDRTINDDLDACVASCP---DKTAVTAVRLGTGAPRR-FTYRELAALVDRVAVGLarLGV----GRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 86 DAVLVLASPGLRLVKLLFACQRAGLTAVPVVP-------------------PDPARFDGPAHAHLLRAVsqtRPTAAvad 146
Cdd:PRK13295 81 DVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPifrerelsfmlkhaeskvlVVPKTFRGFDHAAMARRL---RPELP--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 147 agyidSVAKTVsssVAAAGGDNARARLAATAmlgslRWlavdELEREREGGGDGPGPeapyvgcGPDDVYLIQYTSGATG 226
Cdd:PRK13295 155 -----ALRHVV---VVGGDGADSFEALLITP-----AW----EQEPDAPAILARLRP-------GPDDVTQLIYTSGTTG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 227 VPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVF-LLLTVVAGATCVLAApgvfLRRPRLWLELVSEFG 305
Cdd:PRK13295 211 EPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYgLMMPVMLGATAVLQD----IWDPARAAELIRTEG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 306 ATCTPVPS-FALPLVlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcshglrATSVSPSYGLAENCTFV 384
Cdd:PRK13295 287 VTFTMASTpFLTDLT-------RAVKESGRPVSSLRTFLCAGAPIPGALVERARAAL------GAKIVSAWGMTENGAVT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 385 STawrtsesssghipsymkllpsaRLSPPPSSAANE----VPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHP 460
Cdd:PRK13295 354 LT----------------------KLDDPDERASTTdgcpLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRP 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1205983844 461 SATREvfcarvpgRAGACFvRTGDRGVVrGPERYLYVVGRSADVI 505
Cdd:PRK13295 411 QLNGT--------DADGWF-DTGDLARI-DADGYIRISGRSKDVI 445
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
208-505 |
7.25e-18 |
|
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: 86.76 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 208 VGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLT-VVAGATCVLAA 286
Cdd:cd05935 79 VGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTaVYVGGTYVLMA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 287 pgvflRRPR-LWLELVSEFGAT-CTPVPSFALPLVlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcsh 364
Cdd:cd05935 159 -----RWDReTALELIEKYKVTfWTNIPTMLVDLL-------ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT--- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 365 GLRATSVspsYGLAENCtfvstawrtsesssghipsymkllPSARLSPP--PSSAANEVP--EIEIAVVDEDTGEPVEDG 440
Cdd:cd05935 224 GLRFVEG---YGLTETM------------------------SQTHTNPPlrPKLQCLGIP*fGVDARVIDIETGRELPPN 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205983844 441 VEGEIWVSSPSNASGYLGHPSATREVFcARVPGRAgacFVRTGDRGvVRGPERYLYVVGRSADVI 505
Cdd:cd05935 277 EVGEIVVRGPQIFKGYWNRPEETEESF-IEIKGRR---FFRTGDLG-YMDEEGYFFFVDRVKRMI 336
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
210-618 |
2.70e-17 |
|
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: 84.70 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 210 CGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSV---IVSWLPQYHDCGLVFLLLTVvaGATCVLAA 286
Cdd:cd05972 78 TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIhwnIADPGWAKGAWSSFFGPWLL--GATVFVYE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 287 PGVFlrRPRLWLELVSEFGAT--CTPVPSFALplvlrrgrgHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcsh 364
Cdd:cd05972 156 GPRF--DAERILELLERYGVTsfCGPPTAYRM---------LIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAAT--- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 365 glrATSVSPSYGLAENCTFVSTawrtsesssghipsymkllpSARLSPPPSSAANEVPEIEIAVVDEDtGEPVEDGVEGE 444
Cdd:cd05972 222 ---GLPIRDGYGQTETGLTVGN--------------------FPDMPVKPGSMGRPTPGYDVAIIDDD-GRELPPGEEGD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 445 IWV--SSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGvVRGPERYLYVVGRSADVITLDDgvgggrRRV---- 518
Cdd:cd05972 278 IAIklPPPGLFLGYVGDPEKTEASI------RGD--YYLTGDRA-YRDEDGYFWFVGRADDIIKSSG------YRIgpfe 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 519 -------HAHYVETAAFGSaPDRLRGGCVAAFATSSTLWSRSqtgvVAVVAELQkviagvgDHRGLCDGIRAAVWRDEGV 591
Cdd:cd05972 343 vesalleHPAVAEAAVVGS-PDPVRGEVVKAFVVLTSGYEPS----EELAEELQ-------GHVKKVLAPYKYPREIEFV 410
|
410 420
....*....|....*....|....*..
gi 1205983844 592 MvglavlvdggVVPKTTSGKLRRGAAR 618
Cdd:cd05972 411 E----------ELPKTISGKIRRVELR 427
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-543 |
3.66e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 84.27 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 60 TYAQLDAAAGRMArNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPpdpaRFDGPAHAHLLRavsQTR 139
Cdd:cd05934 5 TYAELLRESARIA-AALAALG-IRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT----ALRGDELAYIID---HSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 140 PTAAVADagyidsvaktvsssvaaaggdnararlaaTAMlgslrwlavdelereregggdgpgpeapyvgcgpddvylIQ 219
Cdd:cd05934 76 AQLVVVD-----------------------------PAS---------------------------------------IL 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 220 YTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYH-DCGLVFLLLTVVAGATCVLaapgvfLRR--PRL 296
Cdd:cd05934 88 YTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHiNAQAVSVLAALSVGATLVL------LPRfsASR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 297 WLELVSEFGATCTPVPSFALPLVLRRGRGHRRDRRRllelgsLRnLILINePIYESSVDEFVEAFcshGLRatsVSPSYG 376
Cdd:cd05934 162 FWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHR------LR-AAYGA-PNPPELHEEFEERF---GVR---LLEGYG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 377 LAENCTFVSTAwrtsesssghipsymklLPSARlspPPSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSS---PSNA 453
Cdd:cd05934 228 MTETIVGVIGP-----------------RDEPR---RPGSIGRPAPGYEVRIVDDD-GQELPAGEPGELVIRGlrgWGFF 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 454 SGYLGHPSATREVFcarvpgRAGacFVRTGDRGvVRGPERYLYVVGRSADVItlddgvgggRRR--------------VH 519
Cdd:cd05934 287 KGYYNMPEATAEAM------RNG--WFHTGDLG-YRDADGFFYFVDRKKDMI---------RRRgenissaeverailRH 348
|
490 500
....*....|....*....|....
gi 1205983844 520 AHYVETAAFGsAPDRLRGGCVAAF 543
Cdd:cd05934 349 PAVREAAVVA-VPDEVGEDEVKAV 371
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
76-547 |
4.47e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 84.41 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 76 LGTVGSLRRGDAVLVLASPGLRLVKLLFACQRAG-LTAVPVVPPDPARfdGPAHAHLLRAVSQTRptAAVADAGYIDsva 154
Cdd:cd05922 9 ALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgRLGLVFVPLNPTL--KESVLRYLVADAGGR--IVLADAGAAD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 155 ktvsssvaaaggdnaRARLAATAMLGSLRWLAVDELEREREGGGDGPGPeapyvgcgPDDVYLIQYTSGATGVPRPVVVT 234
Cdd:cd05922 82 ---------------RLRDALPASPDPGTVLDADGIRAARASAPAHEVS--------HEDLALLLYTSGSTGSPKLVRLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 235 AGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFlrrPRLWLELVSEFGATCTP-VPS 313
Cdd:cd05922 139 HQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL---DDAFWEDLREHGATGLAgVPS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 314 FALPLvlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcshglRATSVSPSYGLAEnCTfvstawrtses 393
Cdd:cd05922 216 TYAML--------TRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELL-----PGAQVYVMYGQTE-AT----------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 394 ssghipSYMKLLPSARLSPPPSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREvfcarvpG 473
Cdd:cd05922 271 ------RRMTYLPPERILEKPGSIGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRK-------E 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 474 RAGACFVRTGDRGvVRGPERYLYVVGRSADVITLddgvgGGRR----------RVHAHYVETAAFGSAPDRLRGgcVAAF 543
Cdd:cd05922 337 GRGGGVLHTGDLA-RRDEDGFLFIVGRRDRMIKL-----FGNRispteieaaaRSIGLIIEAAAVGLPDPLGEK--LALF 408
|
....
gi 1205983844 544 ATSS 547
Cdd:cd05922 409 VTAP 412
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
58-505 |
4.48e-17 |
|
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: 84.35 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 58 ALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPdparFDGPAHAHLLRavsq 137
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL--GVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPF----FREHELAFILR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 138 trptaavadagyidsvaktvsssvaaaggdNARAR-LAATAMLGSLRWLAVdelereregggdgpgpeapyvgcgPDDVY 216
Cdd:cd05903 71 ------------------------------RAKAKvFVVPERFRQFDPAAM------------------------PDAVA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 217 LIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVagatcVLAAPGVFLRR--P 294
Cdd:cd05903 97 LLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPL-----LLGAPVVLQDIwdP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 295 RLWLELVSEFGATCT-PVPSFALPLVlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcshglrATSVSP 373
Cdd:cd05903 172 DKALALMREHGVTFMmGATPFLTDLL-------NAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL------GAKVCS 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 374 SYGLAENCTFVStawrtsesssghipsymkllpsaRLSPPPSSAA-----NEVPEIEIAVVDeDTGEPVEDGVEGEIWVS 448
Cdd:cd05903 239 AYGSTECPGAVT-----------------------SITPAPEDRRlytdgRPLPGVEIKVVD-DTGATLAPGVEGELLSR 294
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205983844 449 SPSNASGYLGHPSATREVFcarvpgraGACFVRTGDRGVVrGPERYLYVVGRSADVI 505
Cdd:cd05903 295 GPSVFLGYLDRPDLTADAA--------PEGWFRTGDLARL-DEDGYLRITGRSKDII 342
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
43-542 |
5.16e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 84.55 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 43 PAFIWADDdaastRTALTYAQLdaaaGRMARNLLG--TVGSLRRGDAVLVLASPGLRLVKLLFACQRAGLTavpVVPPDP 120
Cdd:PRK05852 33 PALVVTAD-----RIAISYRDL----ARLVDDLAGqlTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV---VVPLDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 121 ArfdgpahahLLRAVSQTRPTAAVADAGYIDSVAKtvsssvaaagGDNARARL---AATAMLGSLRWLAVDELEREREGG 197
Cdd:PRK05852 101 A---------LPIAEQRVRSQAAGARVVLIDADGP----------HDRAEPTTrwwPLTVNVGGDSGPSGGTLSVHLDAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 198 GDGPGPEAPYVGCGPDDVyLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLL-TV 276
Cdd:PRK05852 162 TEPTPATSTPEGLRPDDA-MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLaTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 277 VAGATCVLAAPGVFLRRPrLWLELVSEFGATCTPVPSFALPLVlrrgrGHRRDRRRLLELGSLRNLILINEPIYESSVDE 356
Cdd:PRK05852 241 ASGGAVLLPARGRFSAHT-FWDDIKAVGATWYTAVPTIHQILL-----ERAATEPSGRKPAALRFIRSCSAPLTAETAQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 357 FVEAFcshglrATSVSPSYGLAENCTFVSTAwRTSESSSGHIPsymkllpsaRLSPPPSSAANEvPEIEIAVVDedtGEP 436
Cdd:PRK05852 315 LQTEF------AAPVVCAFGMTEATHQVTTT-QIEGIGQTENP---------VVSTGLVGRSTG-AQIRIVGSD---GLP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 437 VEDGVEGEIWVSSPSNASGYLGHPSATREVFCARvpgragacFVRTGDRG--------VVRGpeRYLYVVGRSADVITLD 508
Cdd:PRK05852 375 LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG--------WLRTGDLGslsaagdlSIRG--RIKELINRGGEKISPE 444
|
490 500 510
....*....|....*....|....*....|....*.
gi 1205983844 509 --DGVGGGrrrvHAHYVETAAFGsAPDRLRGGCVAA 542
Cdd:PRK05852 445 rvEGVLAS----HPNVMEAAVFG-VPDQLYGEAVAA 475
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
59-484 |
5.43e-17 |
|
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: 83.90 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPARfdgpahahllravsqt 138
Cdd:cd17643 13 LTYGELDARANRLARTLRAE--GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE---------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 139 RPTAAVADAGyidsvaktvsssvaaaggdnararlaatamlgsLRWLAVDelereregggdgpgpeapyvgcgPDDVYLI 218
Cdd:cd17643 75 RIAFILADSG---------------------------------PSLLLTD-----------------------PDDLAYV 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 219 QYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVivsWLpQYHDCGLVF----LLLTVVAGATCVLAAPGVfLRRP 294
Cdd:cd17643 99 IYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDV---WT-LFHSYAFDFsvweIWGALLHGGRLVVVPYEV-ARSP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 295 RLWLELVSEFGATC-TPVPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPIYESSVDEFVEAfcsHGLRATSVSP 373
Cdd:cd17643 174 EDFARLLRDEGVTVlNQTPSAFYQLVEAADRDGRDPL-------ALRYVIFGGEALEAAMLRPWAGR---FGLDRPQLVN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 374 SYGLAENCTFVStawrtsesssghipsYMKLLPSARLSPPPSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNA 453
Cdd:cd17643 244 MYGITETTVHVT---------------FRPLDAADLPAAAASPIGRPLPGLRVYVLDAD-GRPVPPGVVGELYVSGAGVA 307
|
410 420 430
....*....|....*....|....*....|.
gi 1205983844 454 SGYLGHPSATREVFCARVPGRAGACFVRTGD 484
Cdd:cd17643 308 RGYLGRPELTAERFVANPFGGPGSRMYRTGD 338
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
60-505 |
9.14e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 83.70 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 60 TYAQLDAAAGRMARNLLGtVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPV---VPP-----------DPARFDG 125
Cdd:PRK06187 33 TYAELDERVNRLANALRA-LG-VKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPInirLKPeeiayilndaeDRVVLVD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 126 PAHAHLLRAVsqtrptaavadAGYIDSVAKTVSSSVAAAGGDNARAR-----LAATAmlGSLRWLAVDElereregggdg 200
Cdd:PRK06187 111 SEFVPLLAAI-----------LPQLPTVRTVIVEGDGPAAPLAPEVGeyeelLAAAS--DTFDFPDIDE----------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 201 pgpeapyvgcgpDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGA 280
Cdd:PRK06187 167 ------------NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 281 TcvlaapGVFLRR--PRLWLELVSEFGATCtpvpSFALP-----LVLRRGRGHRRDRrrllelgSLRNLILINEPIYESS 353
Cdd:PRK06187 235 K------QVIPRRfdPENLLDLIETERVTF----FFAVPtiwqmLLKAPRAYFVDFS-------SLRLVIYGGAALPPAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 354 VDEFVEAFcshGLRATSVspsYGLAENCTFVSTAWrtsesssghipsymkllPSARLSPP---PSSAANEVPEIEIAVVD 430
Cdd:PRK06187 298 LREFKEKF---GIDLVQG---YGMTETSPVVSVLP-----------------PEDQLPGQwtkRRSAGRPLPGVEARIVD 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205983844 431 EDtGEPVE-DGVE-GEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVrGPERYLYVVGRSADVI 505
Cdd:PRK06187 355 DD-GDELPpDGGEvGEIIVRGPWLMQGYWNRPEATAETI------DGG--WLHTGDVGYI-DEDGYLYITDRIKDVI 421
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
44-612 |
1.05e-16 |
|
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: 83.78 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 44 AFIWADDDAASTRTaLTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdparF 123
Cdd:cd17634 71 AIIYEGDDTSQSRT-ISYRELHREVCRFAGTLLDL--GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVI-------F 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 124 DGPAHAHLLRAVSQTRPTAAV-ADAGY--------IDSVAKTVSSSVAAAGGDNARARLAATAMLGSLRWLAVDELerer 194
Cdd:cd17634 141 GGFAPEAVAGRIIDSSSRLLItADGGVragrsvplKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDL---- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 195 eggGDGPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGsaAHNVRAA---RKAYDLHPGSVI-----VSWLpqyhd 266
Cdd:cd17634 217 ---IAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTG--GYLVYAAttmKYVFDYGPGDIYwctadVGWV----- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 267 CGLVFLLL-TVVAGATCVL-------AAPGvflrrpRLWlELVSEFGATCTpvpsFALPLVLRRGRGHRRDRRRLLELGS 338
Cdd:cd17634 287 TGHSYLLYgPLACGATTLLyegvpnwPTPA------RMW-QVVDKHGVNIL----YTAPTAIRALMAAGDDAIEGTDRSS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 339 LRNLILINEPIYESSVDEFVEAFCSHGlratsvspsyglaenCTFVSTAWRTsESSSGHIPSYMKLLPsarlsPPPSSAA 418
Cdd:cd17634 356 LRILGSVGEPINPEAYEWYWKKIGKEK---------------CPVVDTWWQT-ETGGFMITPLPGAIE-----LKAGSAT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 419 NEVPEIEIAVVDEDtGEPVEDGVEGEIWVSS--PSNASGYLGHPSATREVFCARVPGragacFVRTGDrGVVRGPERYLY 496
Cdd:cd17634 415 RPVFGVQPAVVDNE-GHPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFSTFKG-----MYFSGD-GARRDEDGYYW 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 497 VVGRSADVITLddgvgGGRRRVHAHY---------VETAAFGSAPDRLRGGCVAAFATsstlwsrsqtgvvavvaelqkV 567
Cdd:cd17634 488 ITGRSDDVINV-----AGHRLGTAEIesvlvahpkVAEAAVVGIPHAIKGQAPYAYVV---------------------L 541
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1205983844 568 IAGVGDHRGLCDGIRAAVWRDEGVMVGLAVLVDGGVVPKTTSGKL 612
Cdd:cd17634 542 NHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
59-505 |
1.16e-16 |
|
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: 83.66 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGtVGsLRRGDAVLVLASPGLRLVKLLFACQRAGltAVPVvppdparFDGPAH-AHLLRA-VS 136
Cdd:COG1021 51 LSYAELDRRADRLAAGLLA-LG-LRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPV-------FALPAHrRAEISHfAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 QTRPTAAVADAGY--------IDSVAKTVSSsvaaaggdnararLAATAMLGSLR-WLAVDELEREREGGGDGpgpeapy 207
Cdd:COG1021 120 QSEAVAYIIPDRHrgfdyralARELQAEVPS-------------LRHVLVVGDAGeFTSLDALLAAPADLSEP------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 208 vGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVF--LLLTVVAGATCVLA 285
Cdd:COG1021 180 -RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpgVLGVLYAGGTVVLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 286 APGvflrRPRLWLELVSEFGATCTP-VPSFALPLVlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcsh 364
Cdd:COG1021 259 PDP----SPDTAFPLIERERVTVTAlVPPLALLWL-------DAAERSRYDLSSLRVLQVGGAKLSPELARRVRPAL--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 365 GLRATSVspsYGLAE---NCTfvstawrtsesssghipsymkllpsaRLSPPPSSAANEV-----PEIEIAVVDEDtGEP 436
Cdd:COG1021 325 GCTLQQV---FGMAEglvNYT--------------------------RLDDPEEVILTTQgrpisPDDEVRIVDED-GNP 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205983844 437 VEDGVEGEIWVSSPSNASGYLGHPSATREVFCARvpGragacFVRTGDRgVVRGPERYLYVVGRSADVI 505
Cdd:COG1021 375 VPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPD--G-----FYRTGDL-VRRTPDGYLVVEGRAKDQI 435
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
211-510 |
2.55e-16 |
|
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: 82.02 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 211 GPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAA---- 286
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSirtl 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 287 --------PGVFLRRPRLWLELVSEFGATCTPVPSFALPLvlrrgrghrrdrrrllelgsLRNLILINE----------- 347
Cdd:cd17640 166 kddlkrvkPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFL--------------------FLFFLSGGIfkfgisgggal 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 348 PIYessVDEFVEAFcshGLRatsVSPSYGLAENcTFVSTAWRTSES---SSGHIpsymkllpsarlspppssaaneVPEI 424
Cdd:cd17640 226 PPH---VDTFFEAI---GIE---VLNGYGLTET-SPVVSARRLKCNvrgSVGRP----------------------LPGT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 425 EIAVVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpGRAGacFVRTGDRG-VVRGPEryLYVVGRSAD 503
Cdd:cd17640 274 EIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVL-----DSDG--WFNTGDLGwLTCGGE--LVLTGRAKD 344
|
....*..
gi 1205983844 504 VITLDDG 510
Cdd:cd17640 345 TIVLSNG 351
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
59-500 |
4.73e-16 |
|
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: 81.18 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLG-TVGSlrrGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPArfdgPAHAHLLRavsQ 137
Cdd:cd12116 13 LSYAELDERANRLAARLRArGVGP---GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPA----DRLRYILE---D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 138 TRPTAAVADAGYIDSvaktvsssvAAAGGDNARARLAATAMLGSLRWLAVDelereregggdgpgpeapyvgcGPDDVYL 217
Cdd:cd12116 83 AEPALVLTDDALPDR---------LPAGLPVLLLALAAAAAAPAAPRTPVS----------------------PDDLAYV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 218 IqYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVfLRRPRLW 297
Cdd:cd12116 132 I-YTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRET-QRDPEAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 298 LELVSEFGAT---CTPVPSFALplvlrrgrghrrDRRRLLELGSLRNLILinepiYESSVDEFVEAFCSHGLRATSVsps 374
Cdd:cd12116 210 ARLIEAHSITvmqATPATWRML------------LDAGWQGRAGLTALCG-----GEALPPDLAARLLSRVGSLWNL--- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 375 YGLAENcTFVSTAWRTSEsSSGHIPsymkllpsarLSPPpssaaneVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNAS 454
Cdd:cd12116 270 YGPTET-TIWSTAARVTA-AAGPIP----------IGRP-------LANTQVYVLDAA-LRPVPPGVPGELYIGGDGVAQ 329
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1205983844 455 GYLGHPSATREVFCARVPGRAGACFVRTGDRGVVRGPERYLYvVGR 500
Cdd:cd12116 330 GYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEY-LGR 374
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
57-503 |
5.93e-16 |
|
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: 81.09 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 57 TALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPArfdgpahAHLLRAVS 136
Cdd:cd12117 21 RSLTYAELNERANRLARRLRAA--GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA-------ERLAFMLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 QTRPTAAVADAGYIDSVAKTVSSSVAAAGGDNARARLAATAmlgslrwlavdelereregggdgpgpeapyvgCGPDDVY 216
Cdd:cd12117 92 DAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVP--------------------------------VSPDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 217 LIQYTSGATGVPRPVVVTAGSAAHNVRAARKAyDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLRRPRL 296
Cdd:cd12117 140 YVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 297 wLELVSEFGATCTPVPSFALPLVlrrgrghrrDRRRLLELGSLRNLILINEPIYESSVDEFVEAFCshGLRATSVspsYG 376
Cdd:cd12117 219 -GALIAEEGVTVLWLTAALFNQL---------ADEDPECFAGLRELLTGGEVVSPPHVRRVLAACP--GLRLVNG---YG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 377 LAENCTFvSTAWRTSEsssghipsymklLPSARLSPPPSSAaneVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGY 456
Cdd:cd12117 284 PTENTTF-TTSHVVTE------------LDEVAGSIPIGRP---IANTRVYVLDED-GRPVPPGVPGELYVGGDGLALGY 346
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1205983844 457 LGHPSATREVFcARVPGRAGACFVRTGDRgVVRGPERYLYVVGRSAD 503
Cdd:cd12117 347 LNRPALTAERF-VADPFGPGERLYRTGDL-ARWLPDGRLEFLGRIDD 391
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
57-486 |
1.09e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 80.39 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 57 TALTYAQLDAAAGRMARNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPARfdgpAHAHLLRAvS 136
Cdd:PRK08314 34 RAISYRELLEEAERLAGYLQQECG-VRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE----ELAHYVTD-S 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 QTRptAAVADAGYIDSVAKTVSSS-------------VAAAGGDNARARLAATAMLGSLRWLAVDELEREREGGGDGPGP 203
Cdd:PRK08314 108 GAR--VAIVGSELAPKVAPAVGNLrlrhvivaqysdyLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAPPPH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 204 EApyvgcGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLT-VVAGATC 282
Cdd:PRK08314 186 TA-----GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNApIYAGATV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 283 VL------AAPGVFLRRPRlwlelVSEFGATCTPV------PSFAlplvlrrgrghrrdrrrLLELGSLRNLILINEPIY 350
Cdd:PRK08314 261 VLmprwdrEAAARLIERYR-----VTHWTNIPTMVvdflasPGLA-----------------ERDLSSLRYIGGGGAAMP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 351 ESSVDEFVEAFcshGLRATSvspSYGLAEnctfvsTAwrtsesssghipsymkllpSARLSPPPSSAANE---VP--EIE 425
Cdd:PRK08314 319 EAVAERLKELT---GLDYVE---GYGLTE------TM-------------------AQTHSNPPDRPKLQclgIPtfGVD 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205983844 426 IAVVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCArvpgRAGACFVRTGDRG 486
Cdd:PRK08314 368 ARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE----IDGKRFFRTGDLG 424
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
59-505 |
1.45e-15 |
|
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: 79.64 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGTvGSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDParfdgpaHAHLLRAVSQT 138
Cdd:cd05941 12 ITYADLVARAARLANRLLAL-GKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYP-------LAELEYVITDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 139 RPTAAVADAgyidsvaktvsssvaaaggdnararlaatamlgslrwlavdelereregggdgpgpeapyvgcgpddvyLI 218
Cdd:cd05941 84 EPSLVLDPA---------------------------------------------------------------------LI 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 219 QYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVF-LLLTVVAGATCVlaapgvFLRR--PR 295
Cdd:cd05941 95 LYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNaLLCPLFAGASVE------FLPKfdPK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 296 LWLELVSEFGATC-TPVPSFALPLvlrrgrghrrdrrrllelgslrnlilINEPIYESSVDEFVEAFCSHGLRATsVSPS 374
Cdd:cd05941 169 EVAISRLMPSITVfMGVPTIYTRL--------------------------LQYYEAHFTDPQFARAAAAERLRLM-VSGS 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 375 YGLAENctfVSTAWrtsESSSGHIP--------SYMKLlpSARLSPP--PSSAANEVPEIEIAVVDEDTGEPVEDGVEGE 444
Cdd:cd05941 222 AALPVP---TLEEW---EAITGHTLlerygmteIGMAL--SNPLDGErrPGTVGMPLPGVQARIVDEETGEPLPRGEVGE 293
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205983844 445 IWVSSPSNASGYLGHPSATREVFcarvpgRAGACFvRTGDRGVVRgPERYLYVVGRSADVI 505
Cdd:cd05941 294 IQVRGPSVFKEYWNKPEATKEEF------TDDGWF-KTGDLGVVD-EDGYYWILGRSSVDI 346
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
42-505 |
1.53e-15 |
|
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: 79.72 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 42 KPAFIwadDDAAStrtaLTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPV---VPP 118
Cdd:cd05959 20 KTAFI---DDAGS----LTYAELEAEARRVAGALRAL--GVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVntlLTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 119 DPARFdGPAHAHLLRAVSQTRPTAAVADAGYIDSVAKTVSSSVAAAGGDNARARLAATamlgslrwlaVDELEREREGGG 198
Cdd:cd05959 91 DDYAY-YLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAEL----------VAAEAEQLKPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 199 DgpgpeapyvgcGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRA-ARKAYDLHPGSVIVSWLPQYHDCGL---VFLLL 274
Cdd:cd05959 160 T-----------HADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELyARNVLGIREDDVCFSAAKLFFAYGLgnsLTFPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 275 TVvaGATCVL----AAPGVFLRRPRLWlelvsefgatcTPVPSFALPlvLRRGRGHRRDRRRLLELGSLRNLILINEPIY 350
Cdd:cd05959 229 SV--GATTVLmperPTPAAVFKRIRRY-----------RPTVFFGVP--TLYAAMLAAPNLPSRDLSSLRLCVSAGEALP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 351 ESSVDEFVEAF---CSHGLRATSVspsyglaenctfvstawrtsesssGHIpsYMKLLPSARlspPPSSAANEVPEIEIA 427
Cdd:cd05959 294 AEVGERWKARFgldILDGIGSTEM------------------------LHI--FLSNRPGRV---RYGTTGKPVPGYEVE 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205983844 428 VVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCARvpgragacFVRTGDRgVVRGPERYLYVVGRSADVI 505
Cdd:cd05959 345 LRDED-GGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE--------WTRTGDK-YVRDDDGFYTYAGRADDML 412
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
212-543 |
3.23e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 77.70 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVF-LLLTVVAGATCVLAAPGVf 290
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLgVLACLTHGATMVFPSPSF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 291 lrRPRLWLELVSEFgaTCTP---VPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPIYESSVDEFVEAfcshgLR 367
Cdd:cd05917 80 --DPLAVLEAIEKE--KCTAlhgVPTMFIAELEHPDFDKFDLS-------SLRTGIMAGAPCPPELMKRVIEV-----MN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 368 ATSVSPSYGLAEnCTFVSTAWRTSESSSGHIPSYMKLLPsarlspppssaanevpEIEIAVVDEDTGEPVEDGVEGEIWV 447
Cdd:cd05917 144 MKDVTIAYGMTE-TSPVSTQTRTDDSIEKRVNTVGRIMP----------------HTEAKIVDPEGGIVPPVGVPGELCI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 448 SSPSNASGYLGHPSATREVFcarvpgrAGACFVRTGDRGVVRgPERYLYVVGRSADVItlddgVGGG--------RRRVH 519
Cdd:cd05917 207 RGYSVMKGYWNDPEKTAEAI-------DGDGWLHTGDLAVMD-EDGYCRIVGRIKDMI-----IRGGeniypreiEEFLH 273
|
330 340
....*....|....*....|....*
gi 1205983844 520 AH-YVETAAFGSAPDRLRGGCVAAF 543
Cdd:cd05917 274 THpKVSDVQVVGVPDERYGEEVCAW 298
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
216-484 |
7.09e-15 |
|
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: 77.41 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 216 YLIqYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLrRPR 295
Cdd:cd17649 98 YVI-YTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWA-SAD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 296 LWLELVSEFGATCTpvpsfALPLVLRRGRGHRRDRRRLLELGSLRNLILINepiyessvdefvEAFCSHGLRATSVSP-- 373
Cdd:cd17649 176 ELAEMVRELGVTVL-----DLPPAYLQQLAEEADRTGDGRPPSLRLYIFGG------------EALSPELLRRWLKAPvr 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 374 ---SYGLAEnCTFVSTAWrtsesssgHIPSYMKLLPSarlSPPPSSAaneVPEIEIAVVDEDTGePVEDGVEGEIWVSSP 450
Cdd:cd17649 239 lfnAYGPTE-ATVTPLVW--------KCEAGAARAGA---SMPIGRP---LGGRSAYILDADLN-PVPVGVTGELYIGGE 302
|
250 260 270
....*....|....*....|....*....|....
gi 1205983844 451 SNASGYLGHPSATREVFCARVPGRAGACFVRTGD 484
Cdd:cd17649 303 GLARGYLGRPELTAERFVPDPFGAPGSRLYRTGD 336
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
59-505 |
2.06e-14 |
|
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: 75.81 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGTVgsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDP-ARFDgpahaHLLRavsq 137
Cdd:cd17653 23 LTYGELDAASNALANRLLQLG--VVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPsARIQ-----AILR---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 138 trptaavadagyidsvaktvsssvaaaggdNARARLAATAMlgslrwlavdelereregggdgpgpeapyvgcGPDDVYL 217
Cdd:cd17653 92 ------------------------------TSGATLLLTTD--------------------------------SPDDLAY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 218 IQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPgvflrrPRLW 297
Cdd:cd17653 110 IIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADP------SDPF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 298 LELVSEFGAT-CTPvpSFALPLvlrrgrghrrdrrRLLELGSLRNLILINEPIYESSVDEFveafcSHGLRatsVSPSYG 376
Cdd:cd17653 184 AHVARTVDALmSTP--SILSTL-------------SPQDFPNLKTIFLGGEAVPPSLLDRW-----SPGRR---LYNAYG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 377 LAEnCTFVSTawrtsesssghipsYMKLLPSArlsppPSSAANEVPEIEIAVVDEDTgEPVEDGVEGEIWVSSPSNASGY 456
Cdd:cd17653 241 PTE-CTISST--------------MTELLPGQ-----PVTIGKPIPNSTCYILDADL-QPVPEGVVGEICISGVQVARGY 299
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1205983844 457 LGHPSATREVFcARVPGRAGACFVRTGDRGvVRGPERYLYVVGRSADVI 505
Cdd:cd17653 300 LGNPALTASKF-VPDPFWPGSRMYRTGDYG-RWTEDGGLEFLGREDNQV 346
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
48-507 |
2.17e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 76.32 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 48 ADDDAASTR---TALTYAQLDAAAGRMARnLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdPARFD 124
Cdd:PRK06164 22 ARPDAVALIdedRPLSRAELRALVDRLAA-WLAAQG-VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV----NTRYR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 125 GPAHAHLLRavsQTRPTAAVADAGY--IDSVAktvsssVAAAGGDNARARLAATAMLGSLRWLAVDEL---EREREGGGD 199
Cdd:PRK06164 96 SHEVAHILG---RGRARWLVVWPGFkgIDFAA------ILAAVPPDALPPLRAIAVVDDAADATPAPApgaRVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 200 GPGPEAPYVGCGPDDVYLIQYT-SGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVA 278
Cdd:PRK06164 167 PAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 279 GATCVLaapgvflrrprlwlELVSEFGATCTPVPSFALPLVLRRGRGHRRDRRRLLELGSLRNLILINEPIYESSVDEFV 358
Cdd:PRK06164 247 GAPLVC--------------EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPALGELA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 359 EAFCSHGLRATSVspsYGLAENCTFVStAWRTSEsssghiPSYMKLLPSARLSPPpssaanevpEIEIAVVDEDTGEPVE 438
Cdd:PRK06164 313 ALARARGVPLTGL---YGSSEVQALVA-LQPATD------PVSVRIEGGGRPASP---------EARVRARDPQDGALLP 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205983844 439 DGVEGEIWVSSPSNASGYLGHPSATREVFCARvpgragaCFVRTGDRGVVRGPERYLYvVGRSADVITL 507
Cdd:PRK06164 374 DGESGEIEIRAPSLMRGYLDNPDATARALTDD-------GYFRTGDLGYTRGDGQFVY-QTRMGDSLRL 434
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
37-510 |
2.31e-14 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 76.29 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 37 PAFATKPAFIWADddaastrtaLTYAQLDAAAGRMARNL--LGtvgsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVP 114
Cdd:COG1022 28 VALREKEDGIWQS---------LTWAEFAERVRALAAGLlaLG----VKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 115 VVPpdparfdgpahahllravsqtrpTAAVADAGYI--DSVAKtvsssVAAAGGDNARARLAA----------------T 176
Cdd:COG1022 95 IYP-----------------------TSSAEEVAYIlnDSGAK-----VLFVEDQEQLDKLLEvrdelpslrhivvldpR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 177 AMLGSLRWLAVDELEREREGGGDGPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSV 256
Cdd:COG1022 147 GLRDDPRLLSLDELLALGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 257 IVSWLPQYHDCGLVFLLLTVVAGATCVLA-------------APGVFLRRPRLW---LELVSEFGATCTPVP----SFAL 316
Cdd:COG1022 227 TLSFLPLAHVFERTVSYYALAAGATVAFAespdtlaedlrevKPTFMLAVPRVWekvYAGIQAKAEEAGGLKrklfRWAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 317 PLVLRRGRGHRRDRRRLLELGSLRNL--ILINEPIYE-----------------SSVDEFveaFCSHGLRatsVSPSYGL 377
Cdd:COG1022 307 AVGRRYARARLAGKSPSLLLRLKHALadKLVFSKLREalggrlrfavsggaalgPELARF---FRALGIP---VLEGYGL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 378 AENCTfVSTAWRTSES---SSGhipsymkllpsarlsPPpssaaneVPEIEIAvVDEDtgepvedgveGEIWVSSPSNAS 454
Cdd:COG1022 381 TETSP-VITVNRPGDNrigTVG---------------PP-------LPGVEVK-IAED----------GEILVRGPNVMK 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1205983844 455 GYLGHPSATREVFCArvPGragacFVRTGDRGVVRgPERYLYVVGRSADVITLDDG 510
Cdd:COG1022 427 GYYKNPEATAEAFDA--DG-----WLHTGDIGELD-EDGFLRITGRKKDLIVTSGG 474
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
214-505 |
2.69e-14 |
|
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: 74.60 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 214 DVYLIQYTSGATGVPRPVVV---TAGSAAHNVRAARKayDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAapGVF 290
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLankTFFAVPDILQKEGL--NWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG--GEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 291 LRRPRLWLELVSEFGATCTPVPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPIYESSVdEFVEAFcshglRATS 370
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVP-------SLRLIGYGGSRAIAADV-RFIEAT-----GLTN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 371 VSPSYGLAEnctfVSTAwrtsesssghipsymKLLPSARLSPPPSSAANEVPEIEIAVVDEDTGEPVEDGvEGEIWVSSP 450
Cdd:cd17635 145 TAQVYGLSE----TGTA---------------LCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSAS-FGTIWIKSP 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1205983844 451 SNASGYLGHPSATREVFcarVPGragacFVRTGDRGVVRgPERYLYVVGRSADVI 505
Cdd:cd17635 205 ANMLGYWNNPERTAEVL---IDG-----WVNTGDLGERR-EDGFLFITGRSSESI 250
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
59-505 |
1.12e-13 |
|
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: 73.90 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGltAVPVvppdparFDGPAHAHL-LRA-VS 136
Cdd:cd05920 41 LTYRELDRRADRLAAGLRGL--GIRPGDRVVVQLPNVAEFVVLFFALLRLG--AVPV-------LALPSHRRSeLSAfCA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 QTRPTAAVADAgyidsvaktvsssvaAAGGDNARArlaatamlgslrwLAVDELEreregggdgpgpeapyvgCGPDdVY 216
Cdd:cd05920 110 HAEAVAYIVPD---------------RHAGFDHRA-------------LARELAE------------------SIPE-VA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 217 LIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVF--LLLTVVAGATCVLAAPGvflrRP 294
Cdd:cd05920 143 LFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPDP----SP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 295 RLWLELVSEFGATCTP-VPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPIYESSVDEFVEAFcshGLRATSVsp 373
Cdd:cd05920 219 DAAFPLIEREGVTVTAlVPALVSLWLDAAASRRADLS-------SLRLLQVGGARLSPALARRVPPVL---GCTLQQV-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 374 sYGLAENctfvstawrtsesssghipsymkLLPSARLSPPPSSAANE-----VPEIEIAVVDEDtGEPVEDGVEGEIWVS 448
Cdd:cd05920 287 -FGMAEG-----------------------LLNYTRLDDPDEVIIHTqgrpmSPDDEIRVVDEE-GNPVPPGEEGELLTR 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205983844 449 SPSNASGYLGHPSATREVFCARvpgragaCFVRTGDRgVVRGPERYLYVVGRSADVI 505
Cdd:cd05920 342 GPYTIRGYYRAPEHNARAFTPD-------GFYRTGDL-VRRTPDGYLVVEGRIKDQI 390
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
57-629 |
1.44e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 73.89 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 57 TALTYAQLDAAAGRMARNLlgTVGSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPArfdgpahAHLLRAVS 136
Cdd:PRK05857 40 SALRYRELVAEVGGLAADL--RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPI-------AAIERFCQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 QTRPTAA-VADAGYIDSVAKTVSSSVAAAGGDNARARLAATAMLGSLRWLAVDelereregggdgpgpeapyVGCGPDDV 215
Cdd:PRK05857 111 ITDPAAAlVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGN-------------------ADQGSEDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 216 YLIQYTSGATGVPRPVVV---TAGSAAHNVRAARKAY-DLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAP-GVF 290
Cdd:PRK05857 172 LAMIFTSGTTGEPKAVLLanrTFFAVPDILQKEGLNWvTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGEnTTS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 291 LRR-------------PRLWLELVSEFGATCTPVPsfalplvlrrgrghrrdrrrllelgSLRNLILINEPIYESSVdEF 357
Cdd:PRK05857 252 LLEilttnavattclvPTLLSKLVSELKSANATVP-------------------------SLRLVGYGGSRAIAADV-RF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 358 VEAfcsHGLRATSVspsYGLAEN-CTfvSTAWRTSESSSGHIPSymkllpsarlspppSSAANEVPEIEIAVVDEDTGEP 436
Cdd:PRK05857 306 IEA---TGVRTAQV---YGLSETgCT--ALCLPTDDGSIVKIEA--------------GAVGRPYPGVDVYLAATDGIGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 437 -VEDGVE----GEIWVSSPSNASGYLGHPSATREVFcarVPGragacFVRTGDRgVVRGPERYLYVVGRSADVItlddgV 511
Cdd:PRK05857 364 tAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVL---IDG-----WVNTGDL-LERREDGFFYIKGRSSEMI-----I 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 512 GGG---------RRRVHAHYVETAAFGSAPDRLRGGCVAAFATSSTLWSRSQTgvvavvAELQKVIAgvgdhrglcdgir 582
Cdd:PRK05857 430 CGGvniapdevdRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAA------RALKHTIA------------- 490
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1205983844 583 AAVWRDEGVMVGLAVLVDGGVVPKTTSGKLRRGAAREMLAAGKLPVV 629
Cdd:PRK05857 491 ARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVV 537
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
24-549 |
1.74e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 73.64 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 24 PVVDRYLPVWAKLPA--FATKPAFIWADddaastrTALTYAQLDAAAGRMARNLlgTVGSLRRGDAVLVLASPGLRLVKL 101
Cdd:PRK06155 17 PPSERTLPAMLARQAerYPDRPLLVFGG-------TRWTYAEAARAAAAAAHAL--AAAGVKRGDRVALMCGNRIEFLDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 102 LFACQRAGLTAVPVvpPDPARfdGPAHAHLLRavsQTRPTAAVADAGYIDSVAktvsssvAAAGGDNARARLAATAMLGS 181
Cdd:PRK06155 88 FLGCAWLGAIAVPI--NTALR--GPQLEHILR---NSGARLLVVEAALLAALE-------AADPGDLPLPAVWLLDAPAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 182 LRWLAvdeleREREGGGDGPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWL 261
Cdd:PRK06155 154 VSVPA-----GWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 262 PQYHDCGLVFLLLTVVAGATCVLaapGVFLRRPRLWLELVsEFGATCTPVPSFALPlvlrrgrghrrdrrrllelgslrn 341
Cdd:PRK06155 229 PLFHTNALNAFFQALLAGATYVL---EPRFSASGFWPAVR-RHGATVTYLLGAMVS------------------------ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 342 lILINEPIYESSVDefveafcsHGLR---ATSVSPSYGLAENCTFVSTAWRTSESSSGHIPSYMKlLPSARlsppPSSAA 418
Cdd:PRK06155 281 -ILLSQPARESDRA--------HRVRvalGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVT-HGSQR----PGSMG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 419 NEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSP---SNASGYLGHPSATREVFcarvpgraGACFVRTGDRgVVRGPERYL 495
Cdd:PRK06155 347 RLAPGFEARVVDEH-DQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAW--------RNLWFHTGDR-VVRDADGWF 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205983844 496 YVVGRSADVItlddgvgggRRR---VHAHYVETaAFGSAPDRLRggcVAAFATSSTL 549
Cdd:PRK06155 417 RFVDRIKDAI---------RRRgenISSFEVEQ-VLLSHPAVAA---AAVFPVPSEL 460
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
212-510 |
1.89e-13 |
|
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: 73.25 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVF-LLLTVVAGATCvlaapgVF 290
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFtLLLPLLNGAHV------VF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 291 LRRPRLWLELVSEFgATCTPVPSFALPLVLRRGRGHRRDRRRLLELGSLR-NLILINEPIYESSVDEFVEAF-------C 362
Cdd:cd05914 162 LDKIPSAKIIALAF-AQVTPTLGVPVPLVIEKIFKMDIIPKLTLKKFKFKlAKKINNRKIRKLAFKKVHEAFggnikefV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 363 SHG----------LRATS--VSPSYGLAEnctfvstawrTSESSSGHIPSYMKLlpsarlspppSSAANEVPEIEIAVVD 430
Cdd:cd05914 241 IGGakinpdveefLRTIGfpYTIGYGMTE----------TAPIISYSPPNRIRL----------GSAGKVIDGVEVRIDS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 431 EDTGEPvedgvEGEIWVSSPSNASGYLGHPSATREVFCARvpgragaCFVRTGDRGVVrGPERYLYVVGRSADVITLDDG 510
Cdd:cd05914 301 PDPATG-----EGEIIVRGPNVMKGYYKNPEATAEAFDKD-------GWFHTGDLGKI-DAEGYLYIRGRKKEMIVLSSG 367
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
212-500 |
4.75e-13 |
|
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: 71.98 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGL-VFLLLTVVAGatcvlaAPGVF 290
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLtGCLWLPLLSG------IKVVF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 291 LRRP---RLWLELVSEFGATC---TPVpsFalplvlrrgRGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcsh 364
Cdd:cd05909 220 HPNPldyKKIPELIYDKKATIllgTPT--F---------LRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF--- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 365 GLRatsVSPSYGLAENCTFVSTawrtsesssgHIPSYMKllpsarlspPPSSAANEVPEIEIAVVDEDTGEPVEDGVEGE 444
Cdd:cd05909 286 GIR---ILEGYGTTECSPVISV----------NTPQSPN---------KEGTVGRPLPGMEVKIVSVETHEEVPIGEGGL 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1205983844 445 IWVSSPSNASGYLGHPSATREVFcarvpgraGACFVRTGDRGVVrGPERYLYVVGR 500
Cdd:cd05909 344 LLVRGPNVMLGYLNEPELTSFAF--------GDGWYDTGDIGKI-DGEGFLTITGR 390
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
39-513 |
6.85e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 71.47 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 39 FATKPAFIwaDDDaastrTALTYAQLDAAAGRMARNL--LGtvgsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVv 116
Cdd:PRK07656 18 FGDKEAYV--FGD-----QRLTYAELNARVRRAAAALaaLG----IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 117 ppdparfdgpahahllravsQTRPTAAvaDAGYI--DSVAKTVSSSVAAAGGDnaRARLAATAMLGSLRWLAVDELERER 194
Cdd:PRK07656 86 --------------------NTRYTAD--EAAYIlaRGDAKALFVLGLFLGVD--YSATTRLPALEHVVICETEEDDPHT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 195 EGGGD------GPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCG 268
Cdd:PRK07656 142 EKMKTftdflaAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 269 L-VFLLLTVVAGATcVLAAPgVFlrRPRLWLELVSEFGATCTP-VPSFALPLVLRRGRGHRRDRrrllelgSLRnlilin 346
Cdd:PRK07656 222 YkAGVNAPLMRGAT-ILPLP-VF--DPDEVFRLIETERITVLPgPPTMYNSLLQHPDRSAEDLS-------SLR------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 347 epiyessvdefveaFCSHGlrATSVSPSygLAEN------CTFVSTAWRTSESSsghipsymkllPSARLSPP------- 413
Cdd:PRK07656 285 --------------LAVTG--AASMPVA--LLERfeselgVDIVLTGYGLSEAS-----------GVTTFNRLdddrktv 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 414 PSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcaRVPGragacFVRTGDRGVV--RGp 491
Cdd:PRK07656 336 AGTIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAI--DADG-----WLHTGDLGRLdeEG- 406
|
490 500
....*....|....*....|..
gi 1205983844 492 erYLYVVGRSADVITlddgVGG 513
Cdd:PRK07656 407 --YLYIVDRKKDMFI----VGG 422
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
20-505 |
1.71e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 70.46 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 20 YP--DQPVVDrYLPVWAKLPAfaTKPAFIWADddaastrTALTYAQLDAAAGRMArNLLGTVGsLRRGDAVLVLASPGLR 97
Cdd:PRK06178 28 YPhgERPLTE-YLRAWARERP--QRPAIIFYG-------HVITYAELDELSDRFA-ALLRQRG-VGAGDRVAVFLPNCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 98 LVKLLFACQRAGLTAVPVVPPDPArfdgpahAHLLRAVSQTRPTAAVAdagyIDSVAKTVSSsVAAAGGDNARARLAATA 177
Cdd:PRK06178 96 FHIVFFGILKLGAVHVPVSPLFRE-------HELSYELNDAGAEVLLA----LDQLAPVVEQ-VRAETSLRHVIVTSLAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 178 MLGSLRWLAVDELEREREGGGD----------GPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAG----SAAHNVR 243
Cdd:PRK06178 164 VLPAEPTLPLPDSLRAPRLAAAgaidllpalrACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRdmvyTAAAAYA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 244 AARKAydlHPGSVIVSWLPQY----HDCGLVFLLltvVAGATCVLAA---PGVFLrrprlwlELVSEFGATCTPVPsfal 316
Cdd:PRK06178 244 VAVVG---GEDSVFLSFLPEFwiagENFGLLFPL---FSGATLVLLArwdAVAFM-------AAVERYRVTRTVML---- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 317 plvlrrgrghrrdrrrllelgslrnlilinepiyessVDEFVE--------AFCSHGLRATSVS-------PSY----GL 377
Cdd:PRK06178 307 -------------------------------------VDNAVElmdhprfaEYDLSSLRQVRVVsfvkklnPDYrqrwRA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 378 AENCTFVSTAWRTSES------SSGHIPSYMKLLPSarlsppPSSAANEVPEIEIAVVDEDTGEPVEDGVEGEIWVSSPS 451
Cdd:PRK06178 350 LTGSVLAEAAWGMTEThtcdtfTAGFQDDDFDLLSQ------PVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPS 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1205983844 452 NASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVrGPERYLYVVGRSADVI 505
Cdd:PRK06178 424 LLKGYWNKPEATAEAL------RDG--WLHTGDIGKI-DEQGFLHYLGRRKEML 468
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
42-313 |
2.26e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 69.72 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 42 KPAFIwadddAASTRTALTYAQLDAAAGRMARnLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdpa 121
Cdd:PRK13391 13 KPAVI-----MASTGEVVTYRELDERSNRLAH-LFRSLG-LKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 122 rfdgpaHAHLLravsqtrptaaVADAGYI--DSVAKTVSSSVAAAggDNARARLAAT-AMLGSLRWLAVDELEREREGGG 198
Cdd:PRK13391 80 ------NSHLT-----------PAEAAYIvdDSGARALITSAAKL--DVARALLKQCpGVRHRLVLDGDGELEGFVGYAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 199 DGPGPEApyvGCGPDDVY--LIQYTSGATGVP----RPVVVTAGSAAHNVRA-ARKAYDLHPGSVIVSWLPQYHDCGLVF 271
Cdd:PRK13391 141 AVAGLPA---TPIADESLgtDMLYSSGTTGRPkgikRPLPEQPPDTPLPLTAfLQRLWGFRSDMVYLSPAPLYHSAPQRA 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1205983844 272 LLLTVVAGATCVLaapgvfLRR--PRLWLELVSEFGATCTP-VPS 313
Cdd:PRK13391 218 VMLVIRLGGTVIV------MEHfdAEQYLALIEEYGVTHTQlVPT 256
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
212-500 |
8.55e-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: 67.66 E-value: 8.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFL 291
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 292 RRPRLwLELVSEFGATCTPVPSFALPLVlrrgrghrrdrrRLLELGSLRNLILINEPIYESSVDEFveafcSHGLRatsV 371
Cdd:cd17652 172 PGEPL-ADLLREHRITHVTLPPAALAAL------------PPDDLPDLRTLVVAGEACPAELVDRW-----APGRR---M 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 372 SPSYGLAEnCTFVSTawrtsesssghipsYMKLLPSARlsPPPSSAAneVPEIEIAVVDeDTGEPVEDGVEGEIWVSSPS 451
Cdd:cd17652 231 INAYGPTE-TTVCAT--------------MAGPLPGGG--VPPIGRP--VPGTRVYVLD-ARLRPVPPGVPGELYIAGAG 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1205983844 452 NASGYLGHPSATREVFCARVPGRAGACFVRTGDRgVVRGPERYLYVVGR 500
Cdd:cd17652 291 LARGYLNRPGLTAERFVADPFGAPGSRMYRTGDL-ARWRADGQLEFLGR 338
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-618 |
1.13e-11 |
|
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: 67.46 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 55 TRTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdPARFdGPahahllra 134
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEI--GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL----FALF-GP-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 135 vsqtrptaavadagyiDSVAKTVSSSVAAAggdnararlaatamlgslrwlavdelereregggdgpgpeapYVGCGPDD 214
Cdd:cd05971 68 ----------------EALEYRLSNSGASA------------------------------------------LVTDGSDD 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 215 VYLIQYTSGATGVPRPVVvtagsAAHNVR-----AARKAYDLHPGSVIVSWLPQyhDCGLVFLLLTVVAgATCVLAAPGV 289
Cdd:cd05971 90 PALIIYTSGTTGPPKGAL-----HAHRVLlghlpGVQFPFNLFPRDGDLYWTPA--DWAWIGGLLDVLL-PSLYFGVPVL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 290 FLRR----PRLWLELVSEFGATCTPVPSFALPLVLRRGRGHRRDRRrllelgSLRNLILINEPIYESSVDEFVEAFcshg 365
Cdd:cd05971 162 AHRMtkfdPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQV------KLRAIATGGESLGEELLGWAREQF---- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 366 lrATSVSPSYGLAEnCTFVSTAwrtsesssghipsymkllpSARLSPP-PSSAANEVPEIEIAVVDeDTGEPVEDGVEGE 444
Cdd:cd05971 232 --GVEVNEFYGQTE-CNLVIGN-------------------CSALFPIkPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGE 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 445 IWVSSPSNAS--GYLGHPSATREVFcarvpgrAGAcFVRTGDRGVVRGpERYLYVVGRSADVITlddgVGGGR------- 515
Cdd:cd05971 289 IAVELPDPVAflGYWNNPSATEKKM-------AGD-WLLTGDLGRKDS-DGYFWYVGRDDDVIT----SSGYRigpaeie 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 516 --RRVHAHYVETAAFGsAPDRLRGGCVAAFatssTLWSRSQTGVVAVVAELQK-VIAGVGDHrglcDGIRAAVWRDEgvm 592
Cdd:cd05971 356 ecLLKHPAVLMAAVVG-IPDPIRGEIVKAF----VVLNPGETPSDALAREIQElVKTRLAAH----EYPREIEFVNE--- 423
|
570 580
....*....|....*....|....*.
gi 1205983844 593 vglavlvdggvVPKTTSGKLRRGAAR 618
Cdd:cd05971 424 -----------LPRTATGKIRRRELR 438
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
213-505 |
2.83e-11 |
|
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: 65.83 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 213 DDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLaapgvfLR 292
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYL------VD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 293 R--PRLWLELVSEFGATCTPVPSFALplvlrrgrGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEafcshglRATS 370
Cdd:cd05912 151 KfdAEQVLHLINSGKVTIISVVPTML--------QRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKE-------KGIP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 371 VSPSYGLAENCTFVSTAwrTSESSSGHIPSYMKLLPSArlspppssaanevpEIEIAvvdEDTGEPVEDGvegEIWVSSP 450
Cdd:cd05912 216 VYQSYGMTETCSQIVTL--SPEDALNKIGSAGKPLFPV--------------ELKIE---DDGQPPYEVG---EILLKGP 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1205983844 451 SNASGYLGHPSATREVFcarvpgrAGACFvRTGDRGVVrGPERYLYVVGRSADVI 505
Cdd:cd05912 274 NVTKGYLNRPDATEESF-------ENGWF-KTGDIGYL-DEEGFLYVLDRRSDLI 319
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
48-526 |
3.43e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 66.17 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 48 ADDDAASTR---TALTYAQLDAAAGRMArnllgtvGSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvPPDparfD 124
Cdd:PRK07787 12 AADIADAVRiggRVLSRSDLAGAATAVA-------ERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPV-PPD----S 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 125 GPAH-AHLLRavsqtrptaavadagyiDSvaktvsssvaaaggdnararlAATAMLGSLRWlavDELEREREGGGDGPGP 203
Cdd:PRK07787 80 GVAErRHILA-----------------DS---------------------GAQAWLGPAPD---DPAGLPHVPVRLHARS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 204 EAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLL--------- 274
Cdd:PRK07787 119 WHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLgplrignrf 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 275 -------------TVVAGATCVLAAPGVF------------LRRPRLwleLVSefGATCTPVPSFalplvlrrgrghrrd 329
Cdd:PRK07787 199 vhtgrptpeayaqALSEGGTLYFGVPTVWsriaadpeaaraLRGARL---LVS--GSAALPVPVF--------------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 330 rrrllelgslrnlilinepiyessvdEFVEAFCSHglratSVSPSYGLAEncTFVSTAWRtsesssghipsymkllpsAR 409
Cdd:PRK07787 259 --------------------------DRLAALTGH-----RPVERYGMTE--TLITLSTR------------------AD 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 410 LSPPPSSAANEVPEIEIAVVDEDtGEPVEDGVE--GEIWVSSPSNASGYLGHPSATREVFcarvpgrAGACFVRTGDRGv 487
Cdd:PRK07787 288 GERRPGWVGLPLAGVETRLVDED-GGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAF-------TADGWFRTGDVA- 358
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1205983844 488 VRGPERYLYVVGR-SADVITlddgvgGGRRRVHAHYVETA 526
Cdd:PRK07787 359 VVDPDGMHRIVGReSTDLIK------SGGYRIGAGEIETA 392
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
36-505 |
4.75e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 65.78 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 36 LPAFATKPAFIWADddaastrTALTYAQLDAAAGRMARnLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPV 115
Cdd:PRK06188 22 LKRYPDRPALVLGD-------TRLTYGQLADRISRYIQ-AFEALG-LGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 116 vppdparfdgpahaHllravsqtrPTAAVADAGYIDSVAKtVSSSVAAAGGDNARARLAATAMLGSLRWLAVDELE--RE 193
Cdd:PRK06188 93 --------------H---------PLGSLDDHAYVLEDAG-ISTLIVDPAPFVERALALLARVPSLKHVLTLGPVPdgVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 194 REGGGDGPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLvFLL 273
Cdd:PRK06188 149 LLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA-FFL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 274 LTVVAGATCVLAA---PGVFLRRprlwlelVSEFGATCT-PVPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPI 349
Cdd:PRK06188 228 PTLLRGGTVIVLAkfdPAEVLRA-------IEEQRITATfLVPTMIYALLDHPDLRTRDLS-------SLETVYYGASPM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 350 YESSVDEFVEAFcshglrATSVSPSYGLAEnCTFVSTAWRTSEsssgHIPSYMKLLpsarlspppSSAANEVPEIEIAVV 429
Cdd:PRK06188 294 SPVRLAEAIERF------GPIFAQYYGQTE-APMVITYLRKRD----HDPDDPKRL---------TSCGRPTPGLRVALL 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205983844 430 DEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDrgVVRGPER-YLYVVGRSADVI 505
Cdd:PRK06188 354 DED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDG--WLHTGD--VAREDEDgFYYIVDRKKDMI 419
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
54-505 |
6.04e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 65.27 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 54 STRTALTYAQLDAAAGRMARNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdparfdgpahahllr 133
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELN-VKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 134 avsQTRPTAAVADAGYIDSVAKTVSSSVAAAggdNARARLAATAMLGSLRWL-AVDELEREREGGgdgpgpeapYVGCGP 212
Cdd:PRK06839 84 ---NIRLTENELIFQLKDSGTTVLFVEKTFQ---NMALSMQKVSYVQRVISItSLKEIEDRKIDN---------FVEKNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 213 DDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGL-VFLLLTVVAGATCVLaaPGVFl 291
Cdd:PRK06839 149 SASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIgLFAFPTLFAGGVIIV--PRKF- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 292 rRPRLWLELVSEFGATCTpvpsFALPLVlrrgrghrrdrrrlleLGSLRNLILINEPIYES----------SVDEFVEAF 361
Cdd:PRK06839 226 -EPTKALSMIEKHKVTVV----MGVPTI----------------HQALINCSKFETTNLQSvrwfynggapCPEELMREF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 362 CSHGLRatsVSPSYGLAENCTFVstawrtsesssghipsYMKLLPSARLSppPSSAANEVPEIEIAVVDEDTGEpVEDGV 441
Cdd:PRK06839 285 IDRGFL---FGQGFGMTETSPTV----------------FMLSEEDARRK--VGSIGKPVLFCDYELIDENKNK-VEVGE 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205983844 442 EGEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVrGPERYLYVVGRSADVI 505
Cdd:PRK06839 343 VGELLIRGPNVMKEYWNRPDATEETI------QDG--WLCTGDLARV-DEDGFVYIVGRKKEMI 397
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
57-485 |
7.07e-11 |
|
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: 64.80 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 57 TALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPARfdgpahahllravs 136
Cdd:cd17650 11 RQLTYRELNERANQLARTLRGL--GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAE-------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 qtRPTAAVADAGyidsvaktvsssvaaaggdnarARLAATAmlgslrwlavdelereregggdgpgpeapyvgcgPDDVY 216
Cdd:cd17650 75 --RLQYMLEDSG----------------------AKLLLTQ----------------------------------PEDLA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 217 LIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYH-DCGLVFLLLTVVAGATCVLAAPGVFLRRPR 295
Cdd:cd17650 97 YVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSfDVFAGDFARSLLNGGTLVICPDEVKLDPAA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 296 LWLELVSEFGATCTPVPSFALPLVlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFCSHglraTSVSPSY 375
Cdd:cd17650 177 LYDLILKSRITLMESTPALIRPVM-------AYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQG----MRIINSY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 376 GLAENCTfvstawrtsesSSGHIPSYMKLLPSARLSPppssAANEVPEIEIAVVDEdTGEPVEDGVEGEIWVSSPSNASG 455
Cdd:cd17650 246 GVTEATI-----------DSTYYEEGRDPLGDSANVP----IGRPLPNTAMYVLDE-RLQPQPVGVAGELYIGGAGVARG 309
|
410 420 430
....*....|....*....|....*....|
gi 1205983844 456 YLGHPSATREVFcARVPGRAGACFVRTGDR 485
Cdd:cd17650 310 YLNRPELTAERF-VENPFAPGERMYRTGDL 338
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
59-284 |
1.15e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 64.53 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGltAVPVVPpDParfdGPAHAHLLRAVSQT 138
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNAA--GIGRGMRAVLMVTPSLEFFALTFALFKAG--AVPVLV-DP----GMGIKNLKQCLAEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 139 RPTAAVAdagyidsVAK-TVSSSVAAAGGDNARARLAATamlGSLRWLAV--DELEREREGGGDGPGPEapyvgcGPDDV 215
Cdd:PRK09274 113 QPDAFIG-------IPKaHLARRLFGWGKPSVRRLVTVG---GRLLWGGTtlATLLRDGAAAPFPMADL------APDDM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205983844 216 YLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPqyhdcglVFLLLTVVAGATCVL 284
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFP-------LFALFGPALGMTSVI 238
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
59-505 |
1.18e-10 |
|
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: 64.15 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPArfdgPAHAHLLRavsqt 138
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIAL--GVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSA----EQIAYILN----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 139 rptaavadagyidsvaktvsssvaaaggdNARARLAatamlgslrwlavdelereregggdgpgpeapyVGCGPDDVYLI 218
Cdd:cd05907 75 -----------------------------DSEAKAL---------------------------------FVEDPDDLATI 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 219 QYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHdcglVF-----LLLTVVAGATCVLAA------- 286
Cdd:cd05907 93 IYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAH----VFerragLYVPLLAGARIYFASsaetlld 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 287 ------PGVFLRRPRLWlELVSEfGATCTPVPSFALPLVLRRGRGhrrdrrrllelgSLRNLILINEPIyESSVDEFVEA 360
Cdd:cd05907 169 dlsevrPTVFLAVPRVW-EKVYA-AIKVKAVPGLKRKLFDLAVGG------------RLRFAASGGAPL-PAELLHFFRA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 361 FCSHglratsVSPSYGLAENC--TFVSTAWRTSESSSGHIpsymkllpsarlspppssaaneVPEIEIAVVDEdtgepve 438
Cdd:cd05907 234 LGIP------VYEGYGLTETSavVTLNPPGDNRIGTVGKP----------------------LPGVEVRIADD------- 278
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205983844 439 dgveGEIWVSSPSNASGYLGHPSATREVFCArvPGragacFVRTGDRGVVRgPERYLYVVGRSADVI 505
Cdd:cd05907 279 ----GEILVRGPNVMLGYYKNPEATAEALDA--DG-----WLHTGDLGEID-EDGFLHITGRKKDLI 333
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
39-503 |
1.24e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 64.29 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 39 FATKPAFIWADddaastRTAlTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPV--- 115
Cdd:PRK07470 20 FPDRIALVWGD------RSW-TWREIDARVDALAAALAAR--GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTnfr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 116 -VPPDPARFdgpahahllraVSQTRPTAAVADAGYIDSVAktvssSVAAAGGDnARARLAATAMLGSLrwlAVDELERER 194
Cdd:PRK07470 91 qTPDEVAYL-----------AEASGARAMICHADFPEHAA-----AVRAASPD-LTHVVAIGGARAGL---DYEALVARH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 195 EGGGDGPGPEAPyvgcgpDDVYLIQYTSGATGVPRPVVVTAGSAAHNVraARKAYDLHPG------SVIVSwlPQYHDCG 268
Cdd:PRK07470 151 LGARVANAAVDH------DDPCWFFFTSGTTGRPKAAVLTHGQMAFVI--TNHLADLMPGtteqdaSLVVA--PLSHGAG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 269 lVFLLLTVVAGATCVLAaPGVFLRRPRLWlELVSEFGAT-CTPVPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINE 347
Cdd:PRK07470 221 -IHQLCQVARGAATVLL-PSERFDPAEVW-ALVERHRVTnLFTVPTILKMLVEHPAVDRYDHS-------SLRYVIYAGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 348 PIYEssVDEfveafcSHGLRATS--VSPSYGLAE---NCTFVSTAWRTSESSsghipsymkllPSARLSpppsSAANEVP 422
Cdd:PRK07470 291 PMYR--ADQ------KRALAKLGkvLVQYFGLGEvtgNITVLPPALHDAEDG-----------PDARIG----TCGFERT 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 423 EIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVrGPERYLYVVGRSA 502
Cdd:PRK07470 348 GMEVQIQDDE-GRELPPGETGEICVIGPAVFAGYYNNPEANAKAF------RDG--WFRTGDLGHL-DARGFLYITGRAS 417
|
.
gi 1205983844 503 D 503
Cdd:PRK07470 418 D 418
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
60-624 |
1.68e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 64.06 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 60 TYAQLDAAAGRMARnLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdPARFDGPAHAHLLravSQTR 139
Cdd:PRK09088 24 TYAELDALVGRLAA-VLRRRG-CVDGERLAVLARNSVWLVALHFACARVGAIYVPL----NWRLSASELDALL---QDAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 140 PTAAVADAGyidsvaktvsssVAAAGGDN-ARARLAAtamlgslrwlAVDELEREREGGGDgpgpeapyvgcgPDDVYLI 218
Cdd:PRK09088 95 PRLLLGDDA------------VAAGRTDVeDLAAFIA----------SADALEPADTPSIP------------PERVSLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 219 QYTSGATGVPRPVVVT---AGSAAHNVRAARKAyDLHpgSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLRRPR 295
Cdd:PRK09088 141 LFTSGTSGQPKGVMLSernLQQTAHNFGVLGRV-DAH--SSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 296 LWLELVSeFGAT---CTPVPSFALplvlrrgrghrrDRRRLLELGSLRNLILI---NEPIYESSV----DEFVEAFCSHG 365
Cdd:PRK09088 218 GRLGDPA-LGIThyfCVPQMAQAF------------RAQPGFDAAALRHLTALftgGAPHAAEDIlgwlDDGIPMVDGFG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 366 LraTSVSPSYGLAENCTFVStawrtSESSSGHIPSymkllpsarlspppssaanevPEIEIAVVDEDtGEPVEDGVEGEI 445
Cdd:PRK09088 285 M--SEAGTVFGMSVDCDVIR-----AKAGAAGIPT---------------------PTVQTRVVDDQ-GNDCPAGVPGEL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 446 WVSSPSNASGYLGHPSATREVFcarvpgrAGACFVRTGDRgVVRGPERYLYVVGRSADVItlddgVGGGRRRV------- 518
Cdd:PRK09088 336 LLRGPNLSPGYWRRPQATARAF-------TGDGWFRTGDI-ARRDADGFFWVVDRKKDMF-----ISGGENVYpaeieav 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 519 ---HAHYVETAAFGSAPDRlrggcvaafatsstlWSRSQTGVVAVVAELQKVIAGVGDHRglcdGIRAAVWRdegVMVGL 595
Cdd:PRK09088 403 ladHPGIRECAVVGMADAQ---------------WGEVGYLAIVPADGAPLDLERIRSHL----STRLAKYK---VPKHL 460
|
570 580
....*....|....*....|....*....
gi 1205983844 596 aVLVDGgvVPKTTSGKLRRGAAREMLAAG 624
Cdd:PRK09088 461 -RLVDA--LPRTASGKLQKARLRDALAAG 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
59-485 |
1.73e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.80 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGT-VGSlrrGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDParfdgpahahllravsQ 137
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAgVGP---DVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP----------------Q 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 138 TRPTAAVADAGyidsVAKTVSSSvaaaggdNARARLAATAmlgSLRWLAVDELEREREGGGDGPGPeapyVGCGPDDVYL 217
Cdd:PRK12467 599 DRLAYMLDDSG----VRLLLTQS-------HLLAQLPVPA---GLRSLCLDEPADLLCGYSGHNPE----VALDPDNLAY 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 218 IQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVfLRRPRLW 297
Cdd:PRK12467 661 VIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDC-ARDAEAF 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 298 LELVSEFGATCTPVPSFALPLVLRRGRGHRRDrrrllelgSLRNLILINEPIYESSVDEFVEAfcshgLRATSVSPSYGL 377
Cdd:PRK12467 740 AALMADQGVTVLKIVPSHLQALLQASRVALPR--------PQRALVCGGEALQVDLLARVRAL-----GPGARLINHYGP 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 378 AENcTFVSTAWRTSESS--SGHIPsymkllpsarLSPPpssaaneVPEIEIAVVDEDTgEPVEDGVEGEIWVSSPSNASG 455
Cdd:PRK12467 807 TET-TVGVSTYELSDEErdFGNVP----------IGQP-------LANLGLYILDHYL-NPVPVGVVGELYIGGAGLARG 867
|
410 420 430
....*....|....*....|....*....|
gi 1205983844 456 YLGHPSATREVFCARVPGRAGACFVRTGDR 485
Cdd:PRK12467 868 YHRRPALTAERFVPDPFGADGGRLYRTGDL 897
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
53-284 |
2.43e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 63.38 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 53 ASTRTALTYAQLDAAAGRMARNL--LGtvgsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdparfdgpaHAH 130
Cdd:PRK08276 6 APSGEVVTYGELEARSNRLAHGLraLG----LREGDVVAILLENNPEFFEVYWAARRSGLYYTPI------------NWH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 131 LlravsqtrptaAVADAGYI--DSVAKTVsssVAAAGGDNARARLAATAMLGSLRWLAVDELEREREGGGDGPGPEAPYV 208
Cdd:PRK08276 70 L-----------TAAEIAYIvdDSGAKVL---IVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 209 GCGPDDVYLIQYTSGATGVP----RPVVVTAGSAAHNVRAARKAYDLH--PGSVIVSWLPQYHDCGLVFLLLTVVAGATC 282
Cdd:PRK08276 136 IADETAGADMLYSSGTTGRPkgikRPLPGLDPDEAPGMMLALLGFGMYggPDSVYLSPAPLYHTAPLRFGMSALALGGTV 215
|
..
gi 1205983844 283 VL 284
Cdd:PRK08276 216 VV 217
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
59-500 |
4.91e-10 |
|
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: 62.29 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLlgTVGSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPArfdgpahAHLLRAVSQT 138
Cdd:cd12114 13 LTYGELAERARRVAGAL--KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPA-------ARREAILADA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 139 RPTAAVADAGY-----IDSVAKTVSSSVAAAGGDNARARLAATAMLgslrwlavdelereregggdgpgpeapyvgcgpd 213
Cdd:cd12114 84 GARLVLTDGPDaqldvAVFDVLILDLDALAAPAPPPPVDVAPDDLA---------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 214 dvYLIqYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVfLRR 293
Cdd:cd12114 130 --YVI-FTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEAR-RRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 294 PRLWLELVSEFGATC-TPVPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPIYESSVDEfveafcshgLRAtsvs 372
Cdd:cd12114 206 PAHWAELIERHGVTLwNSVPALLEMLLDVLEAAQALLP-------SLRLVLLSGDWIPLDLPAR---------LRA---- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 373 psygLAENCTFVS--------------------TAWRTsesssghIPsYMKLLPSARlspppssaanevpeieIAVVDED 432
Cdd:cd12114 266 ----LAPDARLISlggateasiwsiyhpidevpPDWRS-------IP-YGRPLANQR----------------YRVLDPR 317
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205983844 433 tGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarVPGRAGACFVRTGDRGVVRgPERYLYVVGR 500
Cdd:cd12114 318 -GRDCPDWVPGELWIGGRGVALGYLGDPELTAARF---VTHPDGERLYRTGDLGRYR-PDGTLEFLGR 380
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
212-484 |
6.44e-10 |
|
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: 61.79 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDV-YLIqYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVI---------VSWLPQyhdcglvflLLTVVAGAT 281
Cdd:cd05918 105 PSDAaYVI-FTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVlqfasytfdVSILEI---------FTTLAAGGC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 282 -CVlaaPGVFLRRPRLwLELVSEFGAT-CTPVPSFA-------LPlvlrrgrghrrdrrrllelgSLRNLILINEPIYES 352
Cdd:cd05918 175 lCI---PSEEDRLNDL-AGFINRLRVTwAFLTPSVArlldpedVP--------------------SLRTLVLGGEALTQS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 353 SVDEFveafcSHGLRATSvspSYGLAENCTFVSTAWRTSESSSGHIpsymkllpsarlsPPPSSAAnevpeieIAVVD-E 431
Cdd:cd05918 231 DVDTW-----ADRVRLIN---AYGPAECTIAATVSPVVPSTDPRNI-------------GRPLGAT-------CWVVDpD 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1205983844 432 DTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVF------CARVPGRAGACFVRTGD 484
Cdd:cd05918 283 NHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFiedpawLKQEGSGRGRRLYRTGD 341
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
216-485 |
9.63e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 216 YLIqYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFlRRPR 295
Cdd:PRK05691 1277 YVI-YTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEH-RDPQ 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 296 LWLELVSEFGATCTpvpSFALPLVlrrgrGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAfcshgLRATSVSPSY 375
Cdd:PRK05691 1355 RIAELVQQYGVTTL---HFVPPLL-----QLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQR-----LPQVQLHNRY 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 376 GLAENCTFVsTAWRTSESSSGHIPsymkllpsarLSPPPSSAANEVPEIEIavvdedtgEPVEDGVEGEIWVSSPSNASG 455
Cdd:PRK05691 1422 GPTETAINV-THWQCQAEDGERSP----------IGRPLGNVLCRVLDAEL--------NLLPPGVAGELCIGGAGLARG 1482
|
250 260 270
....*....|....*....|....*....|
gi 1205983844 456 YLGHPSATREVFCARVPGRAGACFVRTGDR 485
Cdd:PRK05691 1483 YLGRPALTAERFVPDPLGEDGARLYRTGDR 1512
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
207-620 |
1.04e-09 |
|
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: 61.56 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 207 YVGCGP---DDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAA-RKAYDLHPGSVI-----VSWL--PQYhdcgLVFLLLt 275
Cdd:cd05967 221 PVDCVPvaaTDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSmRNIYGIKPGDVWwaasdVGWVvgHSY----IVYGPL- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 276 vVAGATCVL--------AAPGVFLRrprlwleLVSEFGATCTpvpsFALP--LVLRRGRGHRRDRRRLLELGSLRNLILI 345
Cdd:cd05967 296 -LHGATTVLyegkpvgtPDPGAFWR-------VIEKYQVNAL----FTAPtaIRAIRKEDPDGKYIKKYDLSSLRTLFLA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 346 NEPIyessvDefveafcshglratsvSPSYGLAENCTFVSTA---WRTsESSSGHIPSYMKLLPsarLSPPPSSAANEVP 422
Cdd:cd05967 364 GERL-----D----------------PPTLEWAENTLGVPVIdhwWQT-ETGWPITANPVGLEP---LPIKAGSPGKPVP 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 423 EIEIAVVDEDtGEPVEDGVEGEIWVS---SPSNASGYLGHPSATREVFCARVPGragacFVRTGDRGVvRGPERYLYVVG 499
Cdd:cd05967 419 GYQVQVLDED-GEPVGPNELGNIVIKlplPPGCLLTLWKNDERFKKLYLSKFPG-----YYDTGDAGY-KDEDGYLFIMG 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 500 RSADVITlddgVGGGR-------RRVHAH--YVETAAFGsAPDRLRGGCVAAFATSSTLWSRSQTGVV-AVVAELQKVIA 569
Cdd:cd05967 492 RTDDVIN----VAGHRlstgemeESVLSHpaVAECAVVG-VRDELKGQVPLGLVVLKEGVKITAEELEkELVALVREQIG 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1205983844 570 GVGDHRglcdgiraavwrdegvmvgLAVLVDGgvVPKTTSGKLRRGAAREM 620
Cdd:cd05967 567 PVAAFR-------------------LVIFVKR--LPKTRSGKILRRTLRKI 596
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
48-505 |
1.28e-09 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 61.04 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 48 ADDDAASTRTA----LTYAQLDAAAGRMArNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVP--------- 114
Cdd:PRK07514 14 ADRDAPFIETPdglrYTYGDLDAASARLA-NLLVALG-VKPGDRVAVQVEKSPEALALYLATLRAGAVFLPlntaytlae 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 115 -----------VVPPDPARFDGpahahlLRAVSQTRPTAAVADAGyidsvaktvsssvaAAGGdnararlaatamlGSLR 183
Cdd:PRK07514 92 ldyfigdaepaLVVCDPANFAW------LSKIAAAAGAPHVETLD--------------ADGT-------------GSLL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 184 WLAVDELEREREgggdgpgpeapyVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQ 263
Cdd:PRK07514 139 EAAAAAPDDFET------------VPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 264 YHDCGLvFllltvVAGATCVLA-APGVFLrrPRLWLELVSEFGATCTP---VPSFALPLVLRRGRGHRRDRrrllelgSL 339
Cdd:PRK07514 207 FHTHGL-F-----VATNVALLAgASMIFL--PKFDPDAVLALMPRATVmmgVPTFYTRLLQEPRLTREAAA-------HM 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 340 RNLILINEPIYESSVDEFvEAFCSHglratSVSPSYGLAEnctfvsTAWRTSESSSGhipsymkllpsARLsppPSSAAN 419
Cdd:PRK07514 272 RLFISGSAPLLAETHREF-QERTGH-----AILERYGMTE------TNMNTSNPYDG-----------ERR---AGTVGF 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 420 EVPEIEIAVVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcaRVPGragacFVRTGDRGVVrGPERYLYVVG 499
Cdd:PRK07514 326 PLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF--RADG-----FFITGDLGKI-DERGYVHIVG 397
|
....*.
gi 1205983844 500 RSADVI 505
Cdd:PRK07514 398 RGKDLI 403
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
57-485 |
1.47e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.90 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 57 TALTYAQLDAAAGRMARNLLGT-VGSLRRGdAVLVLASPGLrlVKLLFACQRAGLTAVPVVPPDPArfdgpahahllrav 135
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERgVGPDVLV-GVAMERSIEM--VVALLAILKAGGAYVPLDPEYPA-------------- 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 136 sqtrptaavadagyiDSVAKTVSSSvaaaggdNARARLAATAMLGSL---RWLAVDELEREREGGGDGPGPEAPYVGCGP 212
Cdd:PRK12316 598 ---------------ERLAYMLEDS-------GVQLLLSQSHLGRKLplaAGVQVLDLDRPAAWLEGYSEENPGTELNPE 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 213 DDVYLIqYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLR 292
Cdd:PRK12316 656 NLAYVI-YTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRD 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 293 RPRLWlELVSEFGA-TCTPVPSFALPLVlrrgrghrrDRRRLLELGSLRNLILINEPIYESSVdEFVEAfcshGLRATSV 371
Cdd:PRK12316 735 PAKLV-ELINREGVdTLHFVPSMLQAFL---------QDEDVASCTSLRRIVCSGEALPADAQ-EQVFA----KLPQAGL 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 372 SPSYGLAENcTFVSTAWRTSESSSGHIPsymkllpsarLSPPPSSAANEvpeieiaVVDEDtGEPVEDGVEGEIWVSSPS 451
Cdd:PRK12316 800 YNLYGPTEA-AIDVTHWTCVEEGGDSVP----------IGRPIANLACY-------ILDAN-LEPVPVGVLGELYLAGRG 860
|
410 420 430
....*....|....*....|....*....|....
gi 1205983844 452 NASGYLGHPSATREVFCARvPGRAGACFVRTGDR 485
Cdd:PRK12316 861 LARGYHGRPGLTAERFVPS-PFVAGERMYRTGDL 893
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
212-505 |
1.98e-09 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 60.45 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYD--LHPGS-VIVSWLPQYHDCGL-VFLLLTVVAGATCVLaap 287
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGKeLVVTALPLYHIFALtVNCLLFIELGGQNLL--- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 288 gvfLRRPRLWLELVSEFGAtctpVPSFALPLVLrrgrghrrdrrrllelgSLRNLILINEPIYE-------------SSV 354
Cdd:PRK08974 282 ---ITNPRDIPGFVKELKK----YPFTAITGVN-----------------TLFNALLNNEEFQEldfsslklsvgggMAV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 355 DEFVeAFCSHGLRATSVSPSYGLAENCTFVSTAWRTSESSSGHIPsymklLPsarlspppssaaneVPEIEIAVVDEDtG 434
Cdd:PRK08974 338 QQAV-AERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIG-----LP--------------VPSTEIKLVDDD-G 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205983844 435 EPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVrGPERYLYVVGRSADVI 505
Cdd:PRK08974 397 NEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI------KDG--WLATGDIAVM-DEEGFLRIVDRKKDMI 458
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
38-286 |
2.94e-09 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 60.16 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 38 AFATKPAFIWAD----DDAASTRTAL---------TYAQLDAAAGRMArNLLGTVGSLRRGDAVLVLASPGLRLVKLLFA 104
Cdd:cd17632 34 GYADRPALGQRAtelvTDPATGRTTLrllprfetiTYAELWERVGAVA-AAHDPEQPVRPGDFVAVLGFTSPDYATVDLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 105 CQRAGLTAVPVvppdPArfdGPAHAHLLRAVSQTRPTAAVADAGYIDSVAKTVSSSVA----------------AAGGDN 168
Cdd:cd17632 113 LTRLGAVSVPL----QA---GASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEGGTpprlvvfdhrpevdahRAALES 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 169 ARARLAATAMlgslrwlAVDELEREREGGGDGPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKA 248
Cdd:cd17632 186 ARERLAAVGI-------PVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSI 258
|
250 260 270
....*....|....*....|....*....|....*....
gi 1205983844 249 YDLHPGSVIV-SWLPQYHDCGLVFLLLTVVAGATCVLAA 286
Cdd:cd17632 259 QDIRPPASITlNFMPMSHIAGRISLYGTLARGGTAYFAA 297
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
212-505 |
4.55e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 59.63 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARkAY--DLHPG-SVIVSWLPQYHDCGLVF-LLLTVVAGATCVLaap 287
Cdd:PRK05605 218 PDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGK-AWvpGLGDGpERVLAALPMFHAYGLTLcLTLAVSIGGELVL--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 288 gvfLRRPR--LWLELVSEFGATCTP-VPsfalplvlrrgrghrrdrrrllelgslrnlilinePIYESSVDEFVEafcsH 364
Cdd:PRK05605 294 ---LPAPDidLILDAMKKHPPTWLPgVP-----------------------------------PLYEKIAEAAEE----R 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 365 GLRATSVSPSYGLAENCTfVSTAWRTSESSSGHIPSYMKLLPSArlsppPSSAANEV-------------PEIEIAVVD- 430
Cdd:PRK05605 332 GVDLSGVRNAFSGAMALP-VSTVELWEKLTGGLLVEGYGLTETS-----PIIVGNPMsddrrpgyvgvpfPDTEVRIVDp 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205983844 431 EDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarVPGragacFVRTGDRGVVRgPERYLYVVGRSADVI 505
Cdd:PRK05605 406 EDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF---LDG-----WFRTGDVVVME-EDGFIRIVDRIKELI 471
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-484 |
4.87e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.97 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 17 DACYPDQPVVDRYlpVWAKLPAFATKPAFIWADDDaastrtaLTYAQLDAAAGRMARNLLgtvgSLRRGDAVLV-LASP- 94
Cdd:PRK12316 4544 DAGYPATRCVHQL--VAERARMTPDAVAVVFDEEK-------LTYAELNRRANRLAHALI----ARGVGPEVLVgIAMEr 4610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 95 GLRLVKLLFACQRAGLTAVPVVPPDP----ARFDGPAHAHLLraVSQTRPTAAVADAGYIDSVAKTVSSSVAAAGGDNAR 170
Cdd:PRK12316 4611 SAEMMVGLLAVLKAGGAYVPLDPEYPrerlAYMMEDSGAALL--LTQSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPA 4688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 171 ARLAatamlgslrwlavdelereregggdgpgpeapyvgcgPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYD 250
Cdd:PRK12316 4689 VRLH-------------------------------------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE 4731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 251 LHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLrrPRLWLELVSEFGAT---CTPVPSFALplvlrrgrghR 327
Cdd:PRK12316 4732 LTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWD--PERLYAEIHEHRVTvlvFPPVYLQQL----------A 4799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 328 RDRRRLLELGSLRNLILINEPIYESSVDEFVEAfcshgLRATSVSPSYGLAEnCTFVSTAWRTSESSSGhIPSYMkllPS 407
Cdd:PRK12316 4800 EHAERDGEPPSLRVYCFGGEAVAQASYDLAWRA-----LKPVYLFNGYGPTE-TTVTVLLWKARDGDAC-GAAYM---PI 4869
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205983844 408 ARLspppssaaneVPEIEIAVVDeDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCARVPGRAGACFVRTGD 484
Cdd:PRK12316 4870 GTP----------LGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGD 4935
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
14-619 |
6.87e-09 |
|
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: 58.66 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 14 ENYDACYPdqpVVDRylpvWAKlpAFATKPAFIWADDdaASTRTALTYAQLDAAAGRMArNLLGTVGsLRRGDAVLVLAS 93
Cdd:cd05970 14 ENFNFAYD---VVDA----MAK--EYPDKLALVWCDD--AGEERIFTFAELADYSDKTA-NFFKAMG-IGKGDTVMLTLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 94 PGLRLVKLLFACQRAGLTAVPVvppdparfdgpahAHLLRA------VSQTRPTAAVADAGyiDSVAKTVSSSVAAAGGD 167
Cdd:cd05970 81 RRYEFWYSLLALHKLGAIAIPA-------------THQLTAkdivyrIESADIKMIVAIAE--DNIPEEIEKAAPECPSK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 168 NARARLAATAMLGslrWLAVDELEREREGGGDGPGPEAPYVGcgpDDVYLIQYTSGATGVPRPV----------VVTaGS 237
Cdd:cd05970 146 PKLVWVGDPVPEG---WIDFRKLIKNASPDFERPTANSYPCG---EDILLVYFSSGTTGMPKMVehdftyplghIVT-AK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 238 AAHNVRAArkayDLHPGSVIVSWlpqyHDCGLVFLLLTVVAGATCVLAAPGVFLrrPRLWLELVSEFGAT--CTPvPSFA 315
Cdd:cd05970 219 YWQNVREG----GLHLTVADTGW----GKAVWGKIYGQWIAGAAVFVYDYDKFD--PKALLEKLSKYGVTtfCAP-PTIY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 316 LPLVlrrgrghrRDRRRLLELGSLRNLILINEPIYESSVDEFVEafcshglrATSVSPSYGLAENCTFVSTAwrtsesss 395
Cdd:cd05970 288 RFLI--------REDLSRYDLSSLRYCTTAGEALNPEVFNTFKE--------KTGIKLMEGFGQTETTLTIA-------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 396 ghIPSYMKllpsarlsPPPSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNA-----SGYLGHPSATREVFcar 470
Cdd:cd05970 344 --TFPWME--------PKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSKGKpvglfGGYYKDAEKTAEVW--- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 471 vpgRAGacFVRTGDRGvVRGPERYLYVVGRSADVITlDDGVGGGRRRV------HAHYVETAAFGsAPDRLRGGCVAAFA 544
Cdd:cd05970 410 ---HDG--YYHTGDAA-WMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVesaliqHPAVLECAVTG-VPDPIRGQVVKATI 481
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205983844 545 TSSTLWSRSQtgvvAVVAELQKVIAGVgdhrglcdgirAAVWRDEGVMVGLAVLvdggvvPKTTSGKLRRGAARE 619
Cdd:cd05970 482 VLAKGYEPSE----ELKKELQDHVKKV-----------TAPYKYPRIVEFVDEL------PKTISGKIRRVEIRE 535
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
59-506 |
1.09e-08 |
|
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: 57.86 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLlgTVGSLRRGDAVLVLASPGLRLVKLLFACQRAGltAVPVVPpDParfdGPAHAHLLRAVSQT 138
Cdd:cd05910 3 LSFRELDERSDRIAQGL--TAYGIRRGMRAVLMVPPGPDFFALTFALFKAG--AVPVLI-DP----GMGRKNLKQCLQEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 139 RPTAavadagyidsvaktvsssvaaaggdnararlaataMLGSLRwlavdelereregggdgpgpeapyvgcgPDDVYLI 218
Cdd:cd05910 74 EPDA-----------------------------------FIGIPK----------------------------ADEPAAI 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 219 QYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPqyhdcglVFLLLTVVAGATCVlaAPGVFLRR----- 293
Cdd:cd05910 91 LFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFP-------LFALFGPALGLTSV--IPDMDPTRparad 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 294 PRLWLELVSEFGATCTpvpsFALPLVlrRGRGHRRDRRRLLELGSLRNLILINEPIYESSVDEFvEAFCSHGlrATSVSP 373
Cdd:cd05910 162 PQKLVGAIRQYGVSIV----FGSPAL--LERVARYCAQHGITLPSLRRVLSAGAPVPIALAARL-RKMLSDE--AEILTP 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 374 sYGLAENCTFVSTAWRTSESSSGHIPSYMKLLPSARLSPPPSSAANEVPEIEIAVVDEDTGEPveDGVEGEIWVSSPSNA 453
Cdd:cd05910 233 -YGATEALPVSSIGSRELLATTTAATSGGAGTCVGRPIPGVRVRIIEIDDEPIAEWDDTLELP--RGEIGEITVTGPTVT 309
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1205983844 454 SGYLGHPSATRevfCARVPGRAGACFVRTGDRGVVRGPERyLYVVGRSADVIT 506
Cdd:cd05910 310 PTYVNRPVATA---LAKIDDNSEGFWHRMGDLGYLDDEGR-LWFCGRKAHRVI 358
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
41-544 |
1.33e-08 |
|
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: 57.89 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 41 TKPAFIWADDDAAStRTaLTYAQLDAAAGRMArNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVvppdp 120
Cdd:cd05968 76 TRPALRWEGEDGTS-RT-LTYGELLYEVKRLA-NGLRALG-VGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPI----- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 121 arFDGPAHAHLLravsqTRPTAAVADA----------GYIDSVAKTVSSSVAAAGG-DNA----RARLAATAMLGSLRWL 185
Cdd:cd05968 147 --FSGFGKEAAA-----TRLQDAEAKAlitadgftrrGREVNLKEEADKACAQCPTvEKVvvvrHLGNDFTPAKGRDLSY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 186 AvDELEREREGGGDGpgpeapyvgcGPDDVYLIQYTSGATGVPRPVVVTagSAAHNVRAARKAY---DLHPGSvIVSWLP 262
Cdd:cd05968 220 D-EEKETAGDGAERT----------ESEDPLMIIYTSGTTGKPKGTVHV--HAGFPLKAAQDMYfqfDLKPGD-LLTWFT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 263 qyhDCGLV---FLLL-TVVAGATCVL--AAPGvFLRRPRLWlELVSEFGATCTPVPsfalPLVLRRGRGHRRDRRRLLEL 336
Cdd:cd05968 286 ---DLGWMmgpWLIFgGLILGATMVLydGAPD-HPKADRLW-RMVEDHEITHLGLS----PTLIRALKPRGDAPVNAHDL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 337 GSLRNLILINEPIYESSVDEFVEAFcshglratsvspsygLAENCTFVSTAWRTsESSSGhipsymkLLPSARLSP-PPS 415
Cdd:cd05968 357 SSLRVLGSTGEPWNPEPWNWLFETV---------------GKGRNPIINYSGGT-EISGG-------ILGNVLIKPiKPS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 416 SAANEVPEIEIAVVDEDtGEPVEDGVeGEIWVSSP--SNASGYLGHPSATREVFCARVPGragacFVRTGDRGVVrGPER 493
Cdd:cd05968 414 SFNGPVPGMKADVLDES-GKPARPEV-GELVLLAPwpGMTRGFWRDEDRYLETYWSRFDN-----VWVHGDFAYY-DEEG 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205983844 494 YLYVVGRSADVITlddgVGGgrRRV-----------HAHYVETAAFGsAPDRLRGGCVAAFA 544
Cdd:cd05968 486 YFYILGRSDDTIN----VAG--KRVgpaeiesvlnaHPAVLESAAIG-VPHPVKGEAIVCFV 540
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
43-543 |
1.66e-08 |
|
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: 57.48 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 43 PAFIWADDDAASTRtaLTYAQLdAAAGRMARNLLGTVGSLRRGDAVLVLAS--PGLRLVKLlfACQRAGLTAVPVVPPDP 120
Cdd:cd05928 28 PALWWVNGKGDEVK--WSFREL-GSLSRKAANVLSGACGLQRGDRVAVILPrvPEWWLVNV--ACIRTGLVFIPGTIQLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 121 ARfdgpahaHLLRAVSQTRPTAAVADagyiDSVAKTVSSSVAAAGGDNARARLAATAMLGslrWLAVDELEREREGGGDG 200
Cdd:cd05928 103 AK-------DILYRLQASKAKCIVTS----DELAPEVDSVASECPSLKTKLLVSEKSRDG---WLNFKELLNEASTEHHC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 201 pgpeapyVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRA-ARKAYDLHPGSVIvsWlpQYHDCGLVfllltvvAG 279
Cdd:cd05928 169 -------VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVnGRYWLDLTASDIM--W--NTSDTGWI-------KS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 280 ATCVLAAP-----GVFLRR-----PRLWLELVSEFGAT--CTpVPSFALPLVLRRGRGHRRDrrrllelgSLRNLILINE 347
Cdd:cd05928 231 AWSSLFEPwiqgaCVFVHHlprfdPLVILKTLSSYPITtfCG-APTVYRMLVQQDLSSYKFP--------SLQHCVTGGE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 348 PIYESSVDEFVEafcSHGLratSVSPSYGLAENCTFVSTAWRtsesssghipsyMKLlpsarlspPPSSAANEVPEIEIA 427
Cdd:cd05928 302 PLNPEVLEKWKA---QTGL---DIYEGYGQTETGLICANFKG------------MKI--------KPGSMGKASPPYDVQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 428 VVDEDtGEPVEDGVEGEIWVSSPSNA-----SGYLGHPSATREVFCARvpgragacFVRTGDRGVVrGPERYLYVVGRSA 502
Cdd:cd05928 356 IIDDN-GNVLPPGTEGDIGIRVKPIRpfglfSGYVDNPEKTAATIRGD--------FYLTGDRGIM-DEDGYFWFMGRAD 425
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1205983844 503 DVItLDDGVGGGRRRV------HAHYVETAAFGSaPDRLRGGCVAAF 543
Cdd:cd05928 426 DVI-NSSGYRIGPFEVesalieHPAVVESAVVSS-PDPIRGEVVKAF 470
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
33-268 |
1.88e-08 |
|
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: 57.44 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 33 WAklpafATKPAFIW-ADDDAASTRTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLT 111
Cdd:cd05921 4 WA-----RQAPDRTWlAEREGNGGWRRVTYAEALRQVRAIAQGLLDL--GLSAERPLLILSGNSIEHALMALAAMYAGVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 112 AVPVVPPdpARFDGPAHAHLLRAVSQTRPTAAVADAG--------YIDSVAKTVSSSVAAAGGDNA--RARLAATAMLGs 181
Cdd:cd05921 77 AAPVSPA--YSLMSQDLAKLKHLFELLKPGLVFAQDAapfaralaAIFPLGTPLVVSRNAVAGRGAisFAELAATPPTA- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 182 lrwlAVDELereregggdgpgpeapYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGS--VIVS 259
Cdd:cd05921 154 ----AVDAA----------------FAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVD 213
|
....*....
gi 1205983844 260 WLPQYHDCG 268
Cdd:cd05921 214 WLPWNHTFG 222
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
8-265 |
2.55e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 57.20 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 8 RAAMSTENYDACYPDQpvvdryLPVWAklpafATKPAFIW-ADDDAASTRTALTYAQLDAAAGRMARNLLGTvgSLRRGD 86
Cdd:PRK08180 29 RSAEPLGDYPRRLTDR------LVHWA-----QEAPDRVFlAERGADGGWRRLTYAEALERVRAIAQALLDR--GLSAER 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 87 AVLVLASPGLRLVKLLFACQRAGLTAVPVVPP------DPARFdgpahAHLLRAVsqtRPTAAVADAG--YIDSVAKTVS 158
Cdd:PRK08180 96 PLMILSGNSIEHALLALAAMYAGVPYAPVSPAyslvsqDFGKL-----RHVLELL---TPGLVFADDGaaFARALAAVVP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 159 SS---VAAAGGDNARARLAATAMLGSLRWLAVDELereregggdgpgpeapYVGCGPDDVYLIQYTSGATGVPRPVVVTA 235
Cdd:PRK08180 168 ADvevVAVRGAVPGRAATPFAALLATPPTAAVDAA----------------HAAVGPDTIAKFLFTSGSTGLPKAVINTH 231
|
250 260 270
....*....|....*....|....*....|..
gi 1205983844 236 GSAAHNVRAARKAYD--LHPGSVIVSWLPQYH 265
Cdd:PRK08180 232 RMLCANQQMLAQTFPflAEEPPVLVDWLPWNH 263
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
212-297 |
1.39e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 54.72 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATC--------- 282
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVgfyqgdnlk 299
|
90 100
....*....|....*....|
gi 1205983844 283 ---VLAA--PGVFLRRPRLW 297
Cdd:PLN02736 300 lmdDLAAlrPTIFCSVPRLY 319
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
214-502 |
1.81e-07 |
|
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: 53.43 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 214 DVYLIQYTSGATGVPRPVVVTAGS-AAHNVRAArKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLaapgvfLR 292
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNlIAANLQLI-HAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVV------ME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 293 R--PRLWLELVSEFGATCtpVPSFAlPLVLRRGRGHRRDRRRLLelgSLRNLILINEPiyessvdEFVEAFCSHGlRATS 370
Cdd:cd17637 74 KfdPAEALELIEEEKVTL--MGSFP-PILSNLLDAAEKSGVDLS---SLRHVLGLDAP-------ETIQRFEETT-GATF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 371 VSpSYGLAENCTFVSTAwrtsesssghiPSYMKllpsarlsppPSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSP 450
Cdd:cd17637 140 WS-LYGQTETSGLVTLS-----------PYRER----------PGSAGRPGPLVRVRIVDDN-DRPVPAGETGEIVVRGP 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1205983844 451 SNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVrGPERYLYVVGRSA 502
Cdd:cd17637 197 LVFQGYWNLPELTAYTF------RNG--WHHTGDLGRF-DEDGYLWYAGRKP 239
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
422-505 |
3.01e-07 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 53.66 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 422 PEIEIAVVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCArvpgrAGacFVRTGDRGVVRgPERYLYVVGRS 501
Cdd:PRK08315 378 PHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDA-----DG--WMHTGDLAVMD-EEGYVNIVGRI 449
|
....
gi 1205983844 502 ADVI 505
Cdd:PRK08315 450 KDMI 453
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
58-540 |
3.37e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.19 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 58 ALTYAQLDAAAGRMARNLLGT-VGSLRrgdAVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPArfdgpahahllravs 136
Cdd:PRK12316 3082 RLSYAELNRRANRLAHRLIERgVGPDV---LVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPE--------------- 3143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 137 qtrptaavadagyiDSVAKTVSSSVAAAGGDNARARLAATAMLGSLRWLAVDELEREREGGGDGPGPEAPYVgcgpddvy 216
Cdd:PRK12316 3144 --------------ERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYV-------- 3201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 217 liQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFlRRPRL 296
Cdd:PRK12316 3202 --IYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDW-RDPAL 3278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 297 WLELVSEFGATCTPvpsfalplVLRRGRGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEafcshglrATSVSPSYG 376
Cdd:PRK12316 3279 LVELINSEGVDVLH--------AYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFA--------GLPLYNLYG 3342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 377 LAENcTFVSTAWRTSESSSGHIPsymkllpsarlspppssAANEVPEIEIAVVDeDTGEPVEDGVEGEIWVSSPSNASGY 456
Cdd:PRK12316 3343 PTEA-TITVTHWQCVEEGKDAVP-----------------IGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGY 3403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 457 LGHPSATREVFCARvPGRAGACFVRTGD------RGVVRGPERYLYVVGRSADVITLddGVGGGRRRVHAHYVETAAFGS 530
Cdd:PRK12316 3404 HNRPGLTAERFVPD-PFVPGERLYRTGDlaryraDGVIEYIGRVDHQVKIRGFRIEL--GEIEARLLEHPWVREAVVLAV 3480
|
490
....*....|
gi 1205983844 531 APDRLRGGCV 540
Cdd:PRK12316 3481 DGRQLVAYVV 3490
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
423-505 |
5.84e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 52.66 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 423 EIEIavvdEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVrGPERYLYVVGRSA 502
Cdd:PRK03640 317 ELKI----EKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF------QDG--WFKTGDIGYL-DEEGFLYVLDRRS 383
|
...
gi 1205983844 503 DVI 505
Cdd:PRK03640 384 DLI 386
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
11-505 |
7.57e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 52.47 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 11 MSTENYDACYPDQPVVDRYLP--VWAKLPAFATKPAFIWADDDaastrTALTYAQLDAAAGRMARNLLGTvgSLRRGD-- 86
Cdd:PRK12583 1 MPQPSYYQGGGDKPLLTQTIGdaFDATVARFPDREALVVRHQA-----LRYTWRQLADAVDRLARGLLAL--GVQPGDrv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 87 ---------------------AVLVLASPGLRLVKLLFACQRAGLTAVPVVPpdpaRFDGPAHAHLLRAVSqtrPTAAVA 145
Cdd:PRK12583 74 giwapncaewlltqfatarigAILVNINPAYRASELEYALGQSGVRWVICAD----AFKTSDYHAMLQELL---PGLAEG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 146 DAGYIDS-----VAKTVSSSVAAAGGDNARARLAATAMLGSLRWLAvdelEREREGGgdgpgpeapyvgcgPDDVYLIQY 220
Cdd:PRK12583 147 QPGALACerlpeLRGVVSLAPAPPPGFLAWHELQARGETVSREALA----ERQASLD--------------RDDPINIQY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 221 TSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFlrRPRLWLEL 300
Cdd:PRK12583 209 TSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAF--DPLATLQA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 301 VSEFGATCT-PVPSFALPLVlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcshglratsvspsyglae 379
Cdd:PRK12583 287 VEEERCTALyGVPTMFIAEL-------DHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEM------------------ 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 380 NCTFVSTAWRTSESSsghiPSYMKLLPSARLSPPPSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGH 459
Cdd:PRK12583 342 HMAEVQIAYGMTETS----PVSLQTTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNN 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1205983844 460 PSATREVFcarvpGRAGacFVRTGDRGVVRGpERYLYVVGRSADVI 505
Cdd:PRK12583 417 PEATAESI-----DEDG--WMHTGDLATMDE-QGYVRIVGRSKDMI 454
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
42-503 |
9.28e-07 |
|
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: 51.69 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 42 KPAFIWADddaastrTALTYAQLDAAAGRMArNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPpdpa 121
Cdd:cd05919 1 KTAFYAAD-------RSVTYGQLHDGANRLG-SALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 122 RFDGPAHAHLLRavsQTRPTAAVADAgyidsvaktvsssvaaaggdnararlaatamlgslrwlavdelereregggdgp 201
Cdd:cd05919 68 LLHPDDYAYIAR---DCEARLVVTSA------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 202 gpeapyvgcgpDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRA-ARKAYDLHPGSVIVSWLPQYHDCGL---VFLLLTVv 277
Cdd:cd05919 91 -----------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAmAREALGLTPGDRVFSSAKMFFGYGLgnsLWFPLAV- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 278 aGATCVLAAPGvflRRPRLWLELVSEFGATCT-PVPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPIYESSVDE 356
Cdd:cd05919 159 -GASAVLNPGW---PTAERVLATLARFRPTVLyGVPTFYANLLDSCAGSPDALR-------SLRLCVSAGEALPRGLGER 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 357 FVEAF---CSHGLRATSVSPsyglaencTFVST---AWRtsesssghipsymkllpsarlsppPSSAANEVPEIEIAVVD 430
Cdd:cd05919 228 WMEHFggpILDGIGATEVGH--------IFLSNrpgAWR------------------------LGSTGRPVPGYEIRLVD 275
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205983844 431 EDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRgVVRGPERYLYVVGRSAD 503
Cdd:cd05919 276 EE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG--WYRTGDK-FCRDADGWYTHAGRADD 338
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
220-506 |
9.75e-07 |
|
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: 51.92 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 220 YTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATcvlaapGVFLRR--PRLW 297
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGT------NVCLRKvdAKAI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 298 LELVSEFGAT--CtpvpsfALPLVLrrgrghrrdrrrllelgslrNLILINEPIYESSVDEFVeafcsHGLRATSVSP-- 373
Cdd:cd12118 214 YDLIEKHKVThfC------GAPTVL--------------------NMLANAPPSDARPLPHRV-----HVMTAGAPPPaa 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 374 --------------SYGLAEncTF---VSTAWRtSESSSGHIPSYMKLlpSARlspppsSAANEVPEIEIAVVDEDTGEP 436
Cdd:cd12118 263 vlakmeelgfdvthVYGLTE--TYgpaTVCAWK-PEWDELPTEERARL--KAR------QGVRYVGLEEVDVLDPETMKP 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205983844 437 VE-DGVE-GEIWVSSPSNASGYLGHPSATREVFcarvpgrAGACFvRTGDRGVVRgPERYLYVVGRSADVIT 506
Cdd:cd12118 332 VPrDGKTiGEIVFRGNIVMKGYLKNPEATAEAF-------RGGWF-HSGDLAVIH-PDGYIEIKDRSKDIII 394
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
32-319 |
1.43e-06 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 51.52 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 32 VWAKLPAFATKPAFIwaddDAASTRTaLTYAQLDAAAGRMARNL--LGtvgsLRRGDAVLVLASPGLRLVKLLFACQRAG 109
Cdd:PLN02246 29 CFERLSEFSDRPCLI----DGATGRV-YTYADVELLSRRVAAGLhkLG----IRQGDVVMLLLPNCPEFVLAFLGASRRG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 110 LTAVPVVPpdparFDGPAHAHllRAVSQTRPTAAVADAGYIDSVAK-TVSSSVAAAGGDNARARLAATAMLgslrwLAVD 188
Cdd:PLN02246 100 AVTTTANP-----FYTPAEIA--KQAKASGAKLIITQSCYVDKLKGlAEDDGVTVVTIDDPPEGCLHFSEL-----TQAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 189 ELERERegggdgpgpeapyVGCGPDDVYLIQYTSGATGVPRPVVVT----AGSAAHNVRAARKAYDLHPGSVIVSWLPQY 264
Cdd:PLN02246 168 ENELPE-------------VEISPDDVVALPYSSGTTGLPKGVMLThkglVTSVAQQVDGENPNLYFHSDDVILCVLPMF 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1205983844 265 HDCGL-VFLLLTVVAGATCVLaapgvfLRRPRL--WLELVSEFGATCTPvpsFALPLV 319
Cdd:PLN02246 235 HIYSLnSVLLCGLRVGAAILI------MPKFEIgaLLELIQRHKVTIAP---FVPPIV 283
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
212-500 |
1.55e-06 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 51.85 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGL-VFLLLTVVAGATCV-----LA 285
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLtVTLWLPLLEGIKVVyhpdpTD 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 286 APGVflrrprlwLELVSEFGAT---CTPvpSF---------ALPLvlrrgrghrrdrrrllELGSLRNLILINEPIYESS 353
Cdd:PRK08633 861 ALGI--------AKLVAKHRATillGTP--TFlrlylrnkkLHPL----------------MFASLRLVVAGAEKLKPEV 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 354 VDEFVEAFcshGLR------ATSVSPSygLAENC--TFVSTAWR---TSESSSGHipsymkllpsarlsPPPSSAanevp 422
Cdd:PRK08633 915 ADAFEEKF---GIRilegygATETSPV--ASVNLpdVLAADFKRqtgSKEGSVGM--------------PLPGVA----- 970
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205983844 423 eieIAVVDEDTGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVfcarVPGRAGACFVRTGDRGVVrGPERYLYVVGR 500
Cdd:PRK08633 971 ---VRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEV----IKDIDGIGWYVTGDKGHL-DEDGFLTITDR 1040
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
56-505 |
2.01e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 51.04 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 56 RTALTYAQLDAAAGRMARNLLGTVGSL-----RRGDAVLVLASPGLRLVKLLFACQRAGLTAVPV----VPPDPARFDGP 126
Cdd:PRK06145 18 RAALVYRDQEISYAEFHQRILQAAGMLhargiGQGDVVALLMKNSAAFLELAFAASYLGAVFLPInyrlAADEVAYILGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 127 AHAHLLRAVSQ-TRPTAAVADAGYIDSVAKTvSSSVAAAGGdnararLAATAMLGSlrwlavdelereregggdgpgpea 205
Cdd:PRK06145 98 AGAKLLLVDEEfDAIVALETPKIVIDAAAQA-DSRRLAQGG------LEIPPQAAV------------------------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 206 pyvgcGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYH--DCGLVFLLLTVVAGATC- 282
Cdd:PRK06145 147 -----APTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHvgAFDLPGIAVLWVGGTLRi 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 283 --------VLAApgvfLRRPRL---WLELVSEFGATCTPVPS-FALplvlrrgrghrrdrrrllelGSLRNLILINEPIY 350
Cdd:PRK06145 222 hrefdpeaVLAA----IERHRLtcaWMAPVMLSRVLTVPDRDrFDL--------------------DSLAWCIGGGEKTP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 351 ESSVDEFVEAFcshglRATSVSPSYGLAENCtfvstawrtsessSGHipsymKLLPSARLSPPPSSAANEVPEIEIAVVD 430
Cdd:PRK06145 278 ESRIRDFTRVF-----TRARYIDAYGLTETC-------------SGD-----TLMEAGREIEKIGSTGRALAHVEIRIAD 334
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205983844 431 EDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCARvpgragacFVRTGDRGVVrGPERYLYVVGRSADVI 505
Cdd:PRK06145 335 GA-GRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--------WFRSGDVGYL-DEEGFLYLTDRKKDMI 399
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
59-495 |
2.14e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.50 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNL--LGTVGSLRrgdaVLVLASPGLRLVKLLFACQRAGLTAVPVVPPDPA-RFdgpahAHLLRav 135
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLraRGVGPEVR----VAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAeRL-----AYMLE-- 2097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 136 sqtrptaavadagyiDSVAKTVSSSVAAAggdnarARLAATAMLGSLRWLAVDELEREREGGGDgpgpeapyVGCGPDDV 215
Cdd:PRK12316 2098 ---------------DSGAALLLTQRHLL------ERLPLPAGVARLPLDRDAEWADYPDTAPA--------VQLAGENL 2148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 216 YLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATcVLAAPGVfLRRPR 295
Cdd:PRK12316 2149 AYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGAR-VLIRDDE-LWDPE 2226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 296 LWLELVSEFGATCTPVPSFALPLVlrrgrghRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAfcshgLRATSVSPSY 375
Cdd:PRK12316 2227 QLYDEMERHGVTILDFPPVYLQQL-------AEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEA-----LRPVYLFNGY 2294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 376 GLAEnCTFVSTAWRTSESSsghipsymkllPSARLSPPPSSAaneVPEIEIAVVDEDTgEPVEDGVEGEIWVSSPSNASG 455
Cdd:PRK12316 2295 GPTE-AVVTPLLWKCRPQD-----------PCGAAYVPIGRA---LGNRRAYILDADL-NLLAPGMAGELYLGGEGLARG 2358
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1205983844 456 YLGHPSATREVFCARVPGRAGACFVRTGD--RGVVRGPERYL 495
Cdd:PRK12316 2359 YLNRPGLTAERFVPDPFSASGERLYRTGDlaRYRADGVVEYL 2400
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
59-285 |
3.21e-06 |
|
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: 50.37 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLtavPVVPPDPARFDGPahahLLRAVSQT 138
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHAG-LRPGDTVALLLGNEPAFLWIWLGLAKLGC---PVAFLNTNIRSKS----LLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 139 RPTAAVADAGYIDSVAKT-------------VSSSVAAAGGDNARARLAAtamlgslrwlAVDELEREREGGGDGPGPEA 205
Cdd:cd05938 78 GAKVLVVAPELQEAVEEVlpalradgvsvwyLSHTSNTEGVISLLDKVDA----------ASDEPVPASLRAHVTIKSPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 206 PYVgcgpddvyliqYTSGATGVPRPVVVT-----AGSAAHNVRAARkAYDlhpgsVIVSWLPQYHDCGLVF-LLLTVVAG 279
Cdd:cd05938 148 LYI-----------YTSGTTGLPKAARIShlrvlQCSGFLSLCGVT-ADD-----VIYITLPLYHSSGFLLgIGGCIELG 210
|
....*.
gi 1205983844 280 ATCVLA 285
Cdd:cd05938 211 ATCVLK 216
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
210-543 |
3.85e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 50.03 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 210 CGPD-DVYLIQYTSGATGVPRPVVVTAGSAAHN-VRAARKAYDLHPGS-VIVSWLPQYHDCGLVFLL-LTVVAGATCVLA 285
Cdd:PRK06710 202 CDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQWLYNCKEGEeVVLGVLPFFHVYGMTAVMnLSIMQGYKMVLI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 286 aPGVFLRrprLWLELVSEFGATCTP-VPSFALPLVLRRGRGHRRDRrrllelgSLRNLILINEPIYESSVDEFveafcsH 364
Cdd:PRK06710 282 -PKFDMK---MVFEAIKKHKVTLFPgAPTIYIALLNSPLLKEYDIS-------SIRACISGSAPLPVEVQEKF------E 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 365 GLRATSVSPSYGLAENCTFvstawrtsesssghipSYMKLLPSARLsppPSSAANEVPEIEIAVVDEDTGEPVEDGVEGE 444
Cdd:PRK06710 345 TVTGGKLVEGYGLTESSPV----------------THSNFLWEKRV---PGSIGVPWPDTEAMIMSLETGEALPPGEIGE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 445 IWVSSPSNASGYLGHPSATREVFcarvpgRAGacFVRTGDRGVVrGPERYLYVVGRSADVItLDDGVGGGRRRV------ 518
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEETAAVL------QDG--WLHTGDVGYM-DEDGFFYVKDRKKDMI-VASGFNVYPREVeevlye 475
|
330 340
....*....|....*....|....*
gi 1205983844 519 HAHYVETAAFGsAPDRLRGGCVAAF 543
Cdd:PRK06710 476 HEKVQEVVTIG-VPDPYRGETVKAF 499
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
422-500 |
3.87e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.89 E-value: 3.87e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205983844 422 PEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCARVPGRAgacfVRTGDRGVVrgPERYLYVVGR 500
Cdd:PRK04813 325 PDSPLLIIDEE-GTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQPA----YHTGDAGYL--EDGLLFYQGR 396
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
47-560 |
4.37e-06 |
|
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: 49.81 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 47 WADDDAASTrTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPpdpaRFDGP 126
Cdd:cd05923 18 CAIADPARG-LRLTYSELRARIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINP----RLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 127 AHAHLLRAVSQTRPTAAVaDAGYIDSVAktvsssvaaaggdnararlaatamLGSLRWLAVDELEREREGGGDGPGPEAP 206
Cdd:cd05923 91 ELAELIERGEMTAAVIAV-DAQVMDAIF------------------------QSGVRVLALSDLVGLGEPESAGPLIEDP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 207 yvGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRA-ARKAYDLH-PGSVIVSWLPQYHDCGLVFLLLTVVAGAT--C 282
Cdd:cd05923 146 --PREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFmSTQAGLRHgRHNVVLGLMPLYHVIGFFAVLVAALALDGtyV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 283 VLAApgvflRRPRLWLELVSEFGATCTpvpsFALPlvLRRGRGHRRDRRRLLELGSLRNLIL----INEPIYEsSVDEFV 358
Cdd:cd05923 224 VVEE-----FDPADALKLIEQERVTSL----FATP--THLDALAAAAEFAGLKLSSLRHVTFagatMPDAVLE-RVNQHL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 359 EA-FCSHglratsvspsYGLAEncTFVSTAWRTSESSSGHIPSYMKllpsarlspppssaanevpEIEIAVVDEDTGEPV 437
Cdd:cd05923 292 PGeKVNI----------YGTTE--AMNSLYMRDARTGTEMRPGFFS-------------------EVRIVRIGGSPDEAL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 438 EDGVEGEIWVSSPSNAS--GYLGHPSATREVFCARvpgragacFVRTGDRGVVRgPERYLYVVGRsadvitLDDGVGGGR 515
Cdd:cd05923 341 ANGEEGELIVAAAADAAftGYLNQPEATAKKLQDG--------WYRTGDVGYVD-PSGDVRILGR------VDDMIISGG 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1205983844 516 RRVHAHYVETaAFGSAPDRLRggcVAAFATSSTLWSRSQTGVVAV 560
Cdd:cd05923 406 ENIHPSEIER-VLSRHPGVTE---VVVIGVADERWGQSVTACVVP 446
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
211-505 |
4.54e-06 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 49.84 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 211 GPDDVYLIQYTSGATGVPRPVVVTAG----SAAHNVRAARKAYDlHPGS--VIVSWLPQYHDCGLVFLLLTVVAgatcvL 284
Cdd:PLN02574 196 KQDDVAAIMYSSGTTGASKGVVLTHRnliaMVELFVRFEASQYE-YPGSdnVYLAALPMFHIYGLSLFVVGLLS-----L 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 285 AAPGVFLRR--PRLWLELVSEFGATCTPV-PSFALPLVLRRGRGHRRdrrrllelgSLRNLILIN---EPIYESSVDEFV 358
Cdd:PLN02574 270 GSTIVVMRRfdASDMVKVIDRFKVTHFPVvPPILMALTKKAKGVCGE---------VLKSLKQVScgaAPLSGKFIQDFV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 359 EAFcSHglraTSVSPSYGLAEnctfvSTAWRTSESSSGHIPSYmkllpsarlspppSSAANEVPEIEIAVVDEDTGEPVE 438
Cdd:PLN02574 341 QTL-PH----VDFIQGYGMTE-----STAVGTRGFNTEKLSKY-------------SSVGLLAPNMQAKVVDWSTGCLLP 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205983844 439 DGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgrAGACFVRTGDRgVVRGPERYLYVVGRSADVI 505
Cdd:PLN02574 398 PGNCGELWIQGPGVMKGYLNNPKATQSTI-------DKDGWLRTGDI-AYFDEDGYLYIVDRLKEII 456
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
211-504 |
4.70e-06 |
|
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: 49.77 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 211 GPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCV------- 283
Cdd:cd05932 135 FPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesld 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 284 -------LAAPGVFLRRPRLWlelvSEFG-ATCTPVPSFALPLVLRRGRGHRRDRRRLLELGSL---RNLILINEPIYES 352
Cdd:cd05932 215 tfvedvqRARPTLFFSVPRLW----TKFQqGVQDKIPQQKLNLLLKIPVVNSLVKRKVLKGLGLdqcRLAGCGSAPVPPA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 353 svdeFVEAFCSHGLRATSVspsYGLAENCTFvSTAWRTSESSSGHIpsymkllpsarlspppssaANEVPEIEIAVVDed 432
Cdd:cd05932 291 ----LLEWYRSLGLNILEA---YGMTENFAY-SHLNYPGRDKIGTV-------------------GNAGPGVEVRISE-- 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205983844 433 tgepvedgvEGEIWVSSPSNASGYLGHPSATREVFCARvpgragaCFVRTGDRGVVRGpERYLYVVGRSADV 504
Cdd:cd05932 342 ---------DGEILVRSPALMMGYYKDPEATAEAFTAD-------GFLRTGDKGELDA-DGNLTITGRVKDI 396
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
221-505 |
6.10e-06 |
|
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: 48.87 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 221 TSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAapgvflrrPRLWLEL 300
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLL--------ERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 301 VSEfgatcTPVPSFALPLVLRRGRGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAfcshGLRatsVSPSYGLAEN 380
Cdd:cd17630 80 EDL-----APPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR----GIP---LYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 381 CTFVsTAWRTSESSSGhipsymkllpsarlspppsSAANEVPEIEIAVVDedtgepvedgvEGEIWVSSPSNASGYLGHP 460
Cdd:cd17630 148 ASQV-ATKRPDGFGRG-------------------GVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLRGQ 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1205983844 461 satrevfcaRVPGRAGACFVRTGDRGVVRGpERYLYVVGRSADVI 505
Cdd:cd17630 197 ---------LVPEFNEDGWFTTKDLGELHA-DGRLTVLGRADNMI 231
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
209-500 |
9.58e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 48.66 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 209 GCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYH-----DCGLVFLLltvvAGATCV 283
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHaygfnSCTLFPLL----SGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 284 LAAPGVFlrrPRLWLELVSEFGAT---CTPV-PSFALplvlrrgrghRRDRRRLLELGSLRnLILINEPIYESSVDEFVE 359
Cdd:PRK06334 255 FAYNPLY---PKKIVEMIDEAKVTflgSTPVfFDYIL----------KTAKKQESCLPSLR-FVVIGGDAFKDSLYQEAL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 360 AFCSHglraTSVSPSYGLAEnCTFVSTAwrTSESSSGHipsymkllpsarlsppPSSAANEVPEIEIAVVDEDTGEPVED 439
Cdd:PRK06334 321 KTFPH----IQLRQGYGTTE-CSPVITI--NTVNSPKH----------------ESCVGMPIRGMDVLIVSEETKVPVSS 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205983844 440 GVEGEIWVSSPSNASGYLG-HPSatrevfCARVPgRAGACFVRTGDRGVVrGPERYLYVVGR 500
Cdd:PRK06334 378 GETGLVLTRGTSLFSGYLGeDFG------QGFVE-LGGETWYVTGDLGYV-DRHGELFLKGR 431
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
39-505 |
1.23e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 48.61 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 39 FATKPAFiwadddAASTRTaLTYAQLDAAAGRMARNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPP 118
Cdd:PRK05677 37 FADKPAF------SNLGKT-LTYGELYKLSGAFAAWLQQHTD-LKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 119 DPAR-----F-DGPAH--------AHLLRAV---SQTRPT--AAVADA------GYIDSVAKTVSSSVAAAGGDNArarL 173
Cdd:PRK05677 109 YTARemehqFnDSGAKalvclanmAHLAEKVlpkTGVKHVivTEVADMlpplkrLLINAVVKHVKKMVPAYHLPQA---V 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 174 AATAMLGSLRWLAVDElereregggdgpgpeapyVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARK--AYDL 251
Cdd:PRK05677 186 KFNDALAKGAGQPVTE------------------ANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRAlmGSNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 252 HPGS-VIVSWLPQYHdcglvFLLLTVVAGATCVLAAPGVFLRRPRLWLELVSEFGATctpvpSFAlplvlrrgrghrrdr 330
Cdd:PRK05677 248 NEGCeILIAPLPLYH-----IYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKW-----KFS--------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 331 rrllELGSLRNLI--LINEpiyessvdefvEAFCSHGLRATSVSPSYGLAENctfVSTAWRTSESSSGHIPSYMKLL--- 405
Cdd:PRK05677 303 ----GFVGLNTLFvaLCNN-----------EAFRKLDFSALKLTLSGGMALQ---LATAERWKEVTGCAICEGYGMTets 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 406 PSARLSPP----PSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCARvpgragaCFVR 481
Cdd:PRK05677 365 PVVSVNPSqaiqVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSD-------GWLK 436
|
490 500
....*....|....*....|....
gi 1205983844 482 TGDRGVVRgPERYLYVVGRSADVI 505
Cdd:PRK05677 437 TGDIALIQ-EDGYMRIVDRKKDMI 459
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
212-543 |
1.24e-05 |
|
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: 48.27 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVI-----VSWLpqyhdCGLVFLLLTVVAGATCVLAA 286
Cdd:cd05969 88 PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYwctadPGWV-----TGTVYGIWAPWLNGVTNVVY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 287 PGVFlrRPRLWLELVSEFGATCTpvpsFALPLVLRRGRGHRRDRRRLLELGSLRNLILINEPIYESSVDEFVEAFcshgl 366
Cdd:cd05969 163 EGRF--DAESWYGIIERVKVTVW----YTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF----- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 367 ratsvspsyglaeNCTFVSTAWRTsESSSGHIPSYmkllPSARLSppPSSAANEVPEIEIAVVDEDtGEPVEDGVEGEIW 446
Cdd:cd05969 232 -------------GVPIHDTWWQT-ETGSIMIANY----PCMPIK--PGSMGKPLPGVKAAVVDEN-GNELPPGTKGILA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 447 VSS--PSNASGYLGHPSATREVFcarVPGragacFVRTGDRGvVRGPERYLYVVGRSADVITLdDGVGGGRRRVHAHYVE 524
Cdd:cd05969 291 LKPgwPSMFRGIWNDEERYKNSF---IDG-----WYLTGDLA-YRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALME 360
|
330 340
....*....|....*....|....
gi 1205983844 525 TAAFGSA-----PDRLRGGCVAAF 543
Cdd:cd05969 361 HPAVAEAgvigkPDPLRGEIIKAF 384
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
45-505 |
1.29e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 48.41 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 45 FIWADDDAASTRtaLTYAQLDAAAGRMArNLLGTVGsLRRGDAVLVLASPGLRLVKLLFACQRAGLtAVPVVPpdpaRFD 124
Cdd:PRK07529 47 LLDADPLDRPET--WTYAELLADVTRTA-NLLHSLG-VGPGDVVAFLLPNLPETHFALWGGEAAGI-ANPINP----LLE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 125 GPAHAHLLRAvSQTRPTAAVA---DAGYIDSVAKTVSS--------SVAAAGGDNARARLAATAMLGSLRWLAVD---EL 190
Cdd:PRK07529 118 PEQIAELLRA-AGAKVLVTLGpfpGTDIWQKVAEVLAAlpelrtvvEVDLARYLPGPKRLAVPLIRRKAHARILDfdaEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 191 EREREGGGDGPGPEapyvgcGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGL- 269
Cdd:PRK07529 197 ARQPGDRLFSGRPI------GPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALl 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 270 VFLLLTVVAGATCVLAAP------GVFlrrPRLWlELVSEFGATC-TPVPSFALPLVlrrgrghrRDRRRLLELGSLRNL 342
Cdd:PRK07529 271 VTGLAPLARGAHVVLATPqgyrgpGVI---ANFW-KIVERYRINFlSGVPTVYAALL--------QVPVDGHDISSLRYA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 343 ILINEPIYESSVDEFVEAfcsHGLRatsVSPSYGLAENCTFVSTAWRTSESSSGhipSYMKLLPSARlspppssaanevp 422
Cdd:PRK07529 339 LCGAAPLPVEVFRRFEAA---TGVR---IVEGYGLTEATCVSSVNPPDGERRIG---SVGLRLPYQR------------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 423 eIEIAVVDEDTGEPVEDGVE--GEIWVSSPSNASGYLghpsATREVFCARVPGRagacFVRTGDRGVVrGPERYLYVVGR 500
Cdd:PRK07529 397 -VRVVILDDAGRYLRDCAVDevGVLCIAGPNVFSGYL----EAAHNKGLWLEDG----WLNTGDLGRI-DADGYFWLTGR 466
|
....*
gi 1205983844 501 SADVI 505
Cdd:PRK07529 467 AKDLI 471
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
39-543 |
2.24e-05 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 47.71 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 39 FATKPAFIWADddaastrTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPP 118
Cdd:PRK07059 36 YADRPAFICMG-------KAITYGELDELSRALAAWLQSR--GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 119 DPAR------FDGPAHA--------HLLRAVsqtrptaavadagyidsVAKT-VSSSVAAAGGD--------------NA 169
Cdd:PRK07059 107 YTPRelehqlKDSGAEAivvlenfaTTVQQV-----------------LAKTaVKHVVVASMGDllgfkghivnfvvrRV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 170 RARLAATAMLGSLRWLAVDELEREREGGGdgpgpeapyVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAA---- 245
Cdd:PRK07059 170 KKMVPAWSLPGHVRFNDALAEGARQTFKP---------VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMeawl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 246 RKAYDLHPGS---VIVSWLPQYHDCGL-VFLLLTVVAGATCVLAApgvflrRPRLWLELVSEFGATctPVPSFalPLVLr 321
Cdd:PRK07059 241 QPAFEKKPRPdqlNFVCALPLYHIFALtVCGLLGMRTGGRNILIP------NPRDIPGFIKELKKY--QVHIF--PAVN- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 322 rgrghrrdrrrllelgSLRNlILINEPIYES--------------SVDEFVeAFCSHGLRATSVSPSYGLAENCTfVSTA 387
Cdd:PRK07059 310 ----------------TLYN-ALLNNPDFDKldfsklivangggmAVQRPV-AERWLEMTGCPITEGYGLSETSP-VATC 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 388 WR-TSESSSGHIPsymklLPsarlspppssaaneVPEIEIAVVDEDtGEPVEDGVEGEIWVSSPSNASGYLGHPSATrev 466
Cdd:PRK07059 371 NPvDATEFSGTIG-----LP--------------LPSTEVSIRDDD-GNDLPLGEPGEICIRGPQVMAGYWNRPDET--- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 467 fcARVPGRAGacFVRTGDRGVV--RGperYLYVVGRSADVITLD---------DGVGGGrrrvHAHYVETAAFGsAPDRL 535
Cdd:PRK07059 428 --AKVMTADG--FFRTGDVGVMdeRG---YTKIVDRKKDMILVSgfnvypneiEEVVAS----HPGVLEVAAVG-VPDEH 495
|
....*...
gi 1205983844 536 RGGCVAAF 543
Cdd:PRK07059 496 SGEAVKLF 503
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
211-616 |
2.36e-05 |
|
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: 47.31 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 211 GPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVF 290
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 291 LrrprlwLELVSEFGAT-CTPVPSFALPLVLRRGRGHrrdrrrllelgSLRNLILINEPIYESSVDEFVEAfcshgLRAT 369
Cdd:cd12115 183 L------PDLPAAAEVTlINTVPSAAAELLRHDALPA-----------SVRVVNLAGEPLPRDLVQRLYAR-----LQVE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 370 SVSPSYGLAENCTFvstawrtsesSSGHipsymkLLPSARLSPPPSSAAneVPEIEIAVVDEdTGEPVEDGVEGEIWVSS 449
Cdd:cd12115 241 RVVNLYGPSEDTTY----------STVA------PVPPGASGEVSIGRP--LANTQAYVLDR-ALQPVPLGVPGELYIGG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 450 PSNASGYLGHPSATREVFCARvPGRAGACFVRTGDRgVVRGPERYLYVVGRsadvitLDDGVGGGRRRVHAHYVEtAAFG 529
Cdd:cd12115 302 AGVARGYLGRPGLTAERFLPD-PFGPGARLYRTGDL-VRWRPDGLLEFLGR------ADNQVKVRGFRIELGEIE-AALR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 530 SAPDrLRGGCVAAFATSSTLwsRSQTGVVAVVAELQKVIAGVGDHRGLcdgiraavwRDEGVMV-GLAVLVDggVVPKTT 608
Cdd:cd12115 373 SIPG-VREAVVVAIGDAAGE--RRLVAYIVAEPGAAGLVEDLRRHLGT---------RLPAYMVpSRFVRLD--ALPLTP 438
|
....*...
gi 1205983844 609 SGKLRRGA 616
Cdd:cd12115 439 NGKIDRSA 446
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
48-231 |
2.44e-05 |
|
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: 47.75 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 48 ADDDAASTRTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTaVPVVppDPARfdGPA 127
Cdd:TIGR03443 260 SFLDPSSKTRSFTYKQINEASNILAHYLLKT--GIKRGDVVMIYAYRGVDLVVAVMGVLKAGAT-FSVI--DPAY--PPA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 128 HAHLLRAVSQTRPTAAVADAGYID-SVAKTVSSSVaaaggdNARARLAATAML--GSLRWLAVDELEREREGGGDGPGPE 204
Cdd:TIGR03443 333 RQTIYLSVAKPRALIVIEKAGTLDqLVRDYIDKEL------ELRTEIPALALQddGSLVGGSLEGGETDVLAPYQALKDT 406
|
170 180
....*....|....*....|....*..
gi 1205983844 205 APYVGCGPDDVYLIQYTSGATGVPRPV 231
Cdd:TIGR03443 407 PTGVVVGPDSNPTLSFTSGSEGIPKGV 433
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
212-511 |
4.71e-05 |
|
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: 46.65 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPqyhdcgLVFL---LLTVVAGATCVLA--- 285
Cdd:cd17641 157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLP------LPWIgeqMYSVGQALVCGFIvnf 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 286 --------------APGVFLRRPRLWLELVSEFGAT---CTPVPSFALPLVLRRGRGHRRDRRRLLELGSLRNLI--LIN 346
Cdd:cd17641 231 peepetmmedlreiGPTFVLLPPRVWEGIAADVRARmmdATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLRLAswLAD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 347 EPIYESSVDEFVEAFCSHG--------------LRATSVSPS--YGLAENCTFvSTAWRTsesssGHIPSYMKLLPSARL 410
Cdd:cd17641 311 ALLFRPLRDRLGFSRLRSAatggaalgpdtfrfFHAIGVPLKqlYGQTELAGA-YTVHRD-----GDVDPDTVGVPFPGT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 411 spppssaanevpEIEIAVVdedtgepvedgveGEIWVSSPSNASGYLGHPSATREVFcarvpgrAGACFVRTGDRGVVRg 490
Cdd:cd17641 385 ------------EVRIDEV-------------GEILVRSPGVFVGYYKNPEATAEDF-------DEDGWLHTGDAGYFK- 431
|
330 340
....*....|....*....|.
gi 1205983844 491 PERYLYVVGRSADVITLDDGV 511
Cdd:cd17641 432 ENGHLVVIDRAKDVGTTSDGT 452
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
59-265 |
6.59e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 46.19 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 59 LTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPP------DPARF--------- 123
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDL--GLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAyslmshDHAKLkhlfdlvkp 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 124 ------DGPAHAHLLRAVSQTRPTAAVADA--------GYIDSVAKTVSSSVAAAggdnaRARLaatamlgslrwlavde 189
Cdd:PRK12582 159 rvvfaqSGAPFARALAALDLLDVTVVHVTGpgegiasiAFADLAATPPTAAVAAA-----IAAI---------------- 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205983844 190 lereregggdgpgpeapyvgcGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPG---SVIVSWLPQYH 265
Cdd:PRK12582 218 ---------------------TPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDpppPVSLDWMPWNH 275
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
212-503 |
9.09e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 45.81 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFl 291
Cdd:PRK10252 597 PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAH- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 292 RRPRLWLELVSEFGATCTP-VPSFALPLVlrrgrGHRRDRRRLLELGSLRNLILINEPIYESSVDEFveafcsHGLRATS 370
Cdd:PRK10252 676 RDPLAMQQFFAEYGVTTTHfVPSMLAAFV-----ASLTPEGARQSCASLRQVFCSGEALPADLCREW------QQLTGAP 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 371 VSPSYGLAENCTFVStAWrtsesssghiPSYMKLLPSARLSPPPssAANEVPEIEIAVVDeDTGEPVEDGVEGEIWVSSP 450
Cdd:PRK10252 745 LHNLYGPTEAAVDVS-WY----------PAFGEELAAVRGSSVP--IGYPVWNTGLRILD-ARMRPVPPGVAGDLYLTGI 810
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205983844 451 SNASGYLGHPSATREVFCARvPGRAGACFVRTGDrgVVR----GPERYLyvvGRSAD 503
Cdd:PRK10252 811 QLAQGYLGRPDLTASRFIAD-PFAPGERMYRTGD--VARwlddGAVEYL---GRSDD 861
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
39-272 |
1.59e-04 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 44.87 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 39 FATKPAFiwadddaASTRTALTYAQLDAAAGRMARNLLGTVgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPVVPP 118
Cdd:PRK08751 38 FADRPAY-------HSFGKTITYREADQLVEQFAAYLLGEL-QLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 119 DPARfdgpahaHLLRAVSQTRPTAAVAdagyIDSVAKTVSSSVAaaggDNARARLAATA---MLG----SLRWLAVDELE 191
Cdd:PRK08751 110 YTPR-------ELKHQLIDSGASVLVV----IDNFGTTVQQVIA----DTPVKQVITTGlgdMLGfpkaALVNFVVKYVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 192 ------------REREGGGDGPGPEAPYVGCGPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARK----AYDLHPG- 254
Cdd:PRK08751 175 klvpeyringaiRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagTGKLEEGc 254
|
250 260
....*....|....*....|...
gi 1205983844 255 SVIVSWLPQYH-----DCGLVFL 272
Cdd:PRK08751 255 EVVITALPLYHifaltANGLVFM 277
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
212-510 |
1.59e-04 |
|
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: 44.90 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGS--VIVSWLPQYHDCGLVFLLLTVVAGAT-------- 281
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPddRYLAYLPLAHIFELAAENVCLYRGGTigygsprt 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 282 ------------CVLAAPGVFLRRPRLW-------LELVSEFGAT--------------------CTPVPS---FALPlv 319
Cdd:cd17639 167 ltdkskrgckgdLTEFKPTLMVGVPAIWdtirkgvLAKLNPMGGLkrtlfwtayqsklkalkegpGTPLLDelvFKKV-- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 320 lrrgrghrrdrrRLLELGSLRNLILINEPIYESSvDEFVEAFCShglratSVSPSYGLAENCtfvstawrtsesSSGHIP 399
Cdd:cd17639 245 ------------RAALGGRLRYMLSGGAPLSADT-QEFLNIVLC------PVIQGYGLTETC------------AGGTVQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 400 SYMKLLPSARLSPPPSsaanevpeIEIAVVD-------EDTGEPvedgvEGEIWVSSPSNASGYLGHPSATREVFcarvp 472
Cdd:cd17639 294 DPGDLETGRVGPPLPC--------CEIKLVDweeggysTDKPPP-----RGEILIRGPNVFKGYYKNPEKTKEAF----- 355
|
330 340 350
....*....|....*....|....*....|....*...
gi 1205983844 473 grAGACFVRTGDRGVVRgPERYLYVVGRSADVITLDDG 510
Cdd:cd17639 356 --DGDGWFHTGDIGEFH-PDGTLKIIDRKKDLVKLQNG 390
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
425-505 |
1.79e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 44.55 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 425 EIAVVDEDTGEPV-EDGVE-GEIWVSSPSNASGYLGHPSATREVFcarvpgrAGACFvRTGDRGVVRgPERYLYVVGRSA 502
Cdd:PRK08162 369 GVTVLDPDTMQPVpADGETiGEIMFRGNIVMKGYLKNPKATEEAF-------AGGWF-HTGDLAVLH-PDGYIKIKDRSK 439
|
...
gi 1205983844 503 DVI 505
Cdd:PRK08162 440 DII 442
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
355-484 |
2.01e-04 |
|
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: 44.39 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 355 DEFVEAFCSHGLratSVSPSYGLAEncTFVSTAWRTSESSsgHIPSYmkllpsarlsPPPSSAANEVpeiEIAVVDEDtG 434
Cdd:cd17656 261 NEFKEMLHEHNV---HLHNHYGPSE--THVVTTYTINPEA--EIPEL----------PPIGKPISNT---WIYILDQE-Q 319
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1205983844 435 EPVEDGVEGEIWVSSPSNASGYLGHPSATREVFCARvPGRAGACFVRTGD 484
Cdd:cd17656 320 QLQPQGIVGELYISGASVARGYLNRQELTAEKFFPD-PFDPNERMYRTGD 368
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
53-285 |
5.38e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 53 ASTRTALTYAQLDAAAGRMARNLLGtvGSLRRGDAVLVLASPGLRLVKLLFACQRAGL--TAVP--VVPPDPARFDGPAH 128
Cdd:PRK13390 19 AETGEQVSYRQLDDDSAALARVLYD--AGLRTGDVVALLSDNSPEALVVLWAALRSGLyiTAINhhLTAPEADYIVGDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 129 AHLLRAVSQTRPTAAVADA---------GYIDSVAkTVSSSVAAAGgdnarARLAATAmlgslrwlavdelereregggd 199
Cdd:PRK13390 97 ARVLVASAALDGLAAKVGAdlplrlsfgGEIDGFG-SFEAALAGAG-----PRLTEQP---------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 200 gpgpeapyvgCGPddvyLIQYTSGATGVPRPV--------VVTAGSAAhnVRAARKAYDLHPGSVIVSWLPQYHDCGLVF 271
Cdd:PRK13390 149 ----------CGA----VMLYSSGTTGFPKGIqpdlpgrdVDAPGDPI--VAIARAFYDISESDIYYSSAPIYHAAPLRW 212
|
250
....*....|....
gi 1205983844 272 LLLTVVAGATCVLA 285
Cdd:PRK13390 213 CSMVHALGGTVVLA 226
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
212-275 |
8.37e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.78 E-value: 8.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLT 275
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFT 427
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
212-282 |
1.23e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 42.03 E-value: 1.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAY-DLHPGSVIVSWLPQYHdcglVFLLL--TVVAGATC 282
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAH----ILELAaeSVMAAVGA 318
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
212-265 |
1.33e-03 |
|
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: 41.82 E-value: 1.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAA----RKAYDLHPGSVIVSWLPQYH 265
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNKINPTDVYISYLPLAH 170
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
213-265 |
2.02e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 41.50 E-value: 2.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1205983844 213 DDVYLIQYTSGATGVPRPVVVTAGSAAHNVRA-ARKAYDL----HPGSVIVSWLPQYH 265
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHGSLTAGILAlEDRLNDLigppEEDETYCSYLPLAH 321
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
43-115 |
2.45e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 41.02 E-value: 2.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205983844 43 PAFIWADddaastrTALTYAQLDAAAGRMARNLLGTvgSLRRGDAVLVLASPGLRLVKLLFACQRAGLTAVPV 115
Cdd:PRK07798 20 VALVCGD-------RRLTYAELEERANRLAHYLIAQ--GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
212-307 |
3.75e-03 |
|
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: 40.49 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 212 PDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFL 291
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSA 165
|
90
....*....|....*.
gi 1205983844 292 RrpRLWLElVSEFGAT 307
Cdd:cd05937 166 S--QFWKD-VRDSGAT 178
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
428-620 |
3.90e-03 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 40.21 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 428 VVDEDTGEPV-EDGVE-GEIWVSSPSNASGYLGHPSATREVFcarvpgrAGACFvRTGDRGvVRGPERYLYVVGRSADVI 505
Cdd:PLN02479 386 VVDTKTMKPVpADGKTmGEIVMRGNMVMKGYLKNPKANEEAF-------ANGWF-HSGDLG-VKHPDGYIEIKDRSKDII 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 506 tlddgVGGG--------RRRVHAH-YVETAAFGSAPDRLRGGCVAAFATSSTLWSRSQTGVVAvvaelqkviagvGDHRG 576
Cdd:PLN02479 457 -----ISGGenisslevENVVYTHpAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALA------------EDIMK 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1205983844 577 LCDGIRAAVWRDEGVMVglavlvdgGVVPKTTSGKLR----RGAAREM 620
Cdd:PLN02479 520 FCRERLPAYWVPKSVVF--------GPLPKTATGKIQkhvlRAKAKEM 559
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
216-505 |
4.11e-03 |
|
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: 40.15 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 216 YLIQyTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLLLTVVAGATCVLAAPGVFLRRPR 295
Cdd:cd17654 122 YVIH-TSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 296 LWLELVSEFGATCTpvpsFALPLVLRRGRGHRRDRRRLLELGSLRNLILINEPIYESSVDefvEAFCSHGLRaTSVSPSY 375
Cdd:cd17654 201 LADILFKRHRITVL----QATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVIL---SSWRGKGNR-TRIFNIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 376 GLAENCtfvstAWrtseSSSGHIPSymkllpsaRLSPPPSSAANEVPEIEiaVVDEDTGEpvedgVEGEIWVSSPSnasg 455
Cdd:cd17654 273 GITEVS-----CW----ALAYKVPE--------EDSPVQLGSPLLGTVIE--VRDQNGSE-----GTGQVFLGGLN---- 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1205983844 456 ylghpsatREVFCARVPGRAGACFVRTGDRgvVRGPERYLYVVGRSADVI 505
Cdd:cd17654 325 --------RVCILDDEVTVPKGTMRATGDF--VTVKDGELFFLGRKDSQI 364
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
211-307 |
7.84e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 39.24 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 211 GPDDVYLIQYTSGATGVPRPVVVTAGSAAHNVRAARKAYDLHPGSVIVSWLPQYHDCGLVFLL-LTVVAGATcvLAAPGV 289
Cdd:PRK13388 148 DAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWaPAVASGAA--VALPAK 225
|
90
....*....|....*...
gi 1205983844 290 FlrRPRLWLELVSEFGAT 307
Cdd:PRK13388 226 F--SASGFLDDVRRYGAT 241
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
416-505 |
9.49e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 38.99 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205983844 416 SAANEVPEIEIAVVDEDTGEpVEDGVEGEIWVSSPSNASGYLGHPSATREVFcarvpgrAGACFvRTGDrgVVR-GPERY 494
Cdd:PRK07786 346 SVGKVIPTVAARVVDENMND-VPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-------AGGWF-HSGD--LVRqDEEGY 414
|
90
....*....|.
gi 1205983844 495 LYVVGRSADVI 505
Cdd:PRK07786 415 VWVVDRKKDMI 425
|
|
| |
