|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1070-1651 |
0e+00 |
|
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: 720.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1070 ILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKPPVAS-DLN 1148
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISqQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1149 TTLGPIRMmvDMSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWRRKNNNNcdtttsGSSGAASKEEIC 1228
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKW------GPHPPTRDGDTA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1229 YLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPS 1308
Cdd:cd05905 153 YIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1309 LFLTTLSNLKVRDAFTTYSTINTCVTQLATSVENLRERGCNLSMLRSCVAIAEERPRIALMSSFCKLFAPLALNNRAIST 1388
Cdd:cd05905 233 LWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVST 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1389 SFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGQCADSHLGEIW 1468
Cdd:cd05905 313 EFGTRVNPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1469 VASIHNASPLNRLASVTGFGDEGTMNTdvynaRLTTGDTKTRWARTGYLGFLRQTQSITEHGELHDAVFVVGALNESLVL 1548
Cdd:cd05905 393 VNSPANASGYFLLDGETNDTFKVFPST-----RLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1549 RGMRYHPFDVESTVSKAHRFVGNSAVFTWNHLVVIAAECT-GSESDALDLVPAITSAVLEEHHLIVGVVVVVDPGSIRHG 1627
Cdd:cd05905 468 RGLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKN 547
|
570 580
....*....|....*....|....
gi 808354811 1628 PGGEKLRSTIRSLFLEEKLNPIYV 1651
Cdd:cd05905 548 PLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
401-1001 |
0e+00 |
|
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: 687.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 401 AAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKtvqvnkdgsknVMCKPGDRVALIYPNtqPLHFLAAFYGCLQAGVIP 480
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKK-----------VGLKPGDRVALMYPD--PLDFVAAFYGCLYAGVVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 481 VPVEMPSskreaGIAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSstfsapsgsnsltGTSSEIVDFRGWPRLWWAVTE 560
Cdd:cd05905 68 IPIEPPD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKLLKS-------------KTAAEIAKKKGWPKILDFVKI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 561 HMSKPS--RDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAI 638
Cdd:cd05905 130 PKSKRSklKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGC 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 639 LASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATTALVKSRDLHWAL------LATRDHKDISLASLRTLLVADGaNPW 712
Cdd:cd05905 210 LLSVYSGHHTILIPPELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 713 SLSSCDAFAAAFTPSPYSLRpdamcpcAGSSETGTISIRRRG-NAQLGSQSGRGILSMSALSHCVVRVDTENSLTSLTLQ 791
Cdd:cd05905 289 RISSCDSFLKLFQTLGLSPR-------AVSTEFGTRVNPFICwQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 792 DAGQIVAGAVVVVTAIDGSNrLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKLIGAVRYVRSGLIGFMG 871
Cdd:cd05905 362 DSGKVLPGAQVAIVNPETKG-LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 872 P----------DGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPmkfvYRGRICVFSTSvlrdERIVIVAEQKPnCSE 941
Cdd:cd05905 441 PtkctdlnveeHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSE 511
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 942 EEAFDWITRVLRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFENGDLHPSTL 1001
Cdd:cd05905 512 EEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
401-993 |
5.34e-66 |
|
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: 234.44 E-value: 5.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 401 AAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKTvqvnkdgsknvmcKPGDRVALIYPntQPLHFLAAFYGCLQAGVIP 480
Cdd:cd05931 11 AYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-------------KPGDRVLLLAP--PGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 481 VPVEMPSSKREAgiAQLGFLLGNCGVKVALTSEScykglpkkvntsstfsapsgsnSLTGTSSEIVDFRGWPRLWWAVTE 560
Cdd:cd05931 76 VPLPPPTPGRHA--ERLAAILADAGPRVVLTTAA----------------------ALAAVRAFAASRPAAGTPRLLVVD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 561 HM-SKPSRDWTaPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAIL 639
Cdd:cd05931 132 LLpDTSAADWP-PPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 640 ASIFNGMKVIFV-PYSLMKmNPATWMHMVSKYQATTALVKSRDLHWALLATRDHK--DISLASLRTLLVadGANPWSLSS 716
Cdd:cd05931 211 TPLYSGGPSVLMsPAAFLR-RPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDleGLDLSSWRVALN--GAEPVRPAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 717 CDAFAAAFtpSPYSLRPDAMCPCAGSSE-TGTISIRRRGNAQLGSQSGRGILSMSALshcVVRVDTENS--LTSLTLQDA 793
Cdd:cd05931 288 LRRFAEAF--APFGFRPEAFRPSYGLAEaTLFVSGGPPGTGPVVLRVDRDALAGRAV---AVAADDPAAreLVSCGRPLP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 794 GQivagavvvVTAI--DGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGeygkliGAVRYVRSGLIGFMG 871
Cdd:cd05931 363 DQ--------EVRIvdPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAT------DEGGWLRTGDLGFLH 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 872 pDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPMkfVYRGRICVFSTSVLRDERIVIVAEQKPNCSEEEAFDWITRV 951
Cdd:cd05931 429 -DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAI 505
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 808354811 952 LRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFEN 993
Cdd:cd05931 506 RAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1061-1642 |
4.98e-51 |
|
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: 190.14 E-value: 4.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1061 RAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLtdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIK 1140
Cdd:cd05931 2 RAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1141 PPVAsdlNTTLGPIRMMVDMSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDL--EDAPSSWRRKnnnncdtttsgs 1218
Cdd:cd05931 80 PPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLlpDTSAADWPPP------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1219 sgAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLI 1298
Cdd:cd05931 145 --SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1299 PPMEVEQQPSLFLTTLSnlKVRDAFT-----TYstiNTCVTqlATSVENLRerGCNLSMLRSCVAIAEeRPRIALMSSFC 1373
Cdd:cd05931 223 SPAAFLRRPLRWLRLIS--RYRATISaapnfAY---DLCVR--RVRDEDLE--GLDLSSWRVALNGAE-PVRPATLRRFA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1374 KLFAPLALNNRAI--------STSFSSRvnaaicmqGASGPEPSTVYVDARALRNdRISLVGKGAPHSVALIESGKLLPG 1445
Cdd:cd05931 293 EAFAPFGFRPEAFrpsyglaeATLFVSG--------GPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1446 VKIAIANPETRGQCADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTMNTdvYNARLTTGDtkTRWARTGYLGFLRQtq 1524
Cdd:cd05931 364 QEVRIVDPETGRELPDGEVGEIWVRGPSVASGyWGR--------PEATAET--FGALAATDE--GGWLRTGDLGFLHD-- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1525 sitehGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFTWN-----HLVVIAAECTGSESDALD- 1596
Cdd:cd05931 430 -----GEL----YITGRLKDLIIVRGRNHYPQDIEATAEEAHPALrpGCVAAFSVPddgeeRLVVVAEVERGADPADLAa 500
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 808354811 1597 LVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGeKL-RSTIRSLFL 1642
Cdd:cd05931 501 IAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSG-KIqRRACRAAYL 546
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
413-980 |
7.75e-33 |
|
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: 134.17 E-value: 7.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREa 492
Cdd:COG0318 23 RRLTYAELDARARRLAAALRALGV------------GPGDRVALLLPNS--PEFVVAFLAALRAGAVVVPLNPRLTAEE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 493 giaqLGFLLGNCGVKVALTsescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtap 572
Cdd:COG0318 88 ----LAYILEDSGARALVT------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 573 prladetiAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVV----DFkrevGLWHAILASIFNGMKV 648
Cdd:COG0318 103 --------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALplfhVF----GLTVGLLAPLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 649 IFVPyslmKMNPATWMHMVSKYQAT-TALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFTPs 727
Cdd:COG0318 171 VLLP----RFDPERVLELIERERVTvLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 728 pyslrpdAMCPCAGSSETG---TISIRRRGNAQLGSQsGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvv 804
Cdd:COG0318 242 -------RIVEGYGLTETSpvvTVNPEDPGERRPGSV-GR------PLPGVEVRI------------------------- 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 805 taIDGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFkvepvgeygkligAVRYVRSGLIGFMGPDGMVFVVARRQS 884
Cdd:COG0318 283 --VDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-------------RDGWLRTGDLGRLDEDGYLYIVGRKKD 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 885 LLAVSGRYHSADDIIATVLAVEPMKfvyrgRICVFS-TSVLRDERIV--IVAEQKPNCSEEEAFDWITRVLRAIDTIHQV 961
Cdd:COG0318 348 MIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGvPDEKWGERVVafVVLRPGAELDAEELRAFLRERLARYKVPRRV 422
|
570
....*....|....*....
gi 808354811 962 giyccALVPAnhLPKTPLG 980
Cdd:COG0318 423 -----EFVDE--LPRTASG 434
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
413-882 |
3.09e-31 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 128.58 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLLtktvqvnkdgSKNVmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKREA 492
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLR----------ALGV--GKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPL-NPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 493 giaqLGFLLGNCGVKVALTSEScyKGLPKkvntsstfSAPSGSNSLTGTSSEIVDFRGWPRLWWAvtEHMSKPSRDWTAP 572
Cdd:pfam00501 85 ----LAYILEDSGAKVLITDDA--LKLEE--------LLEALGKLEVVKLVLVLDRDPVLKEEPL--PEEAKPADVPPPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 573 PRLAD-ETIAYIEYTTGNDGTVKGCCVT----RQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMK 647
Cdd:pfam00501 149 PPPPDpDDLAYIIYTSGTTGKPKGVMLThrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 648 VIFVPYSLMKMnPATWMHMVSKYQAT-TALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFtp 726
Cdd:pfam00501 229 VVLPPGFPALD-PAALLELIERYKVTvLYGVPT--LLNMLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 727 spyslrPDAMCPCAGSSETGTISIRRRGNAQLGSQSGR-GIlsmsALSHCVVRV-Dtensltsltlqdagqivagavvvv 804
Cdd:pfam00501 302 ------GGALVNGYGLTETTGVVTTPLPLDEDLRSLGSvGR----PLPGTEVKIvD------------------------ 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811 805 taiDGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkligavRYVRSGLIGFMGPDGMVFVVARR 882
Cdd:pfam00501 348 ---DETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------------GWYRTGDLGRRDEDGYLEIVGRK 410
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
379-1026 |
9.51e-30 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 129.90 E-value: 9.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 379 MPRSLdsFSAFHRFGTTAAKNIAAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmckPGDRVALIY 458
Cdd:PRK05691 7 LPLTL--VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS-------------FGDRAVLLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 459 PNTQplHFLAAFYGCLQAGVIPVPVEMPSSKREAGIAQLGFLLGNCGVKVALTSESCYKGLpKKVNTSSTFSAPSgsnsl 538
Cdd:PRK05691 72 PSGP--DYVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPE----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 539 tgtsseivdfrgwprlWWAVTEHMSKPSRDWTApPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTT--AMEY 616
Cdd:PRK05691 144 ----------------LLCVDTLDPALAEAWQE-PALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 617 KEDETMVCVVDFKREVGLWHAILASIFNGmkvifVPYSLMKMN-----PATWMHMVSKYQATTAlvKSRDLHWALLATRd 691
Cdd:PRK05691 207 NPDDVIVSWLPLYHDMGLIGGLLQPIFSG-----VPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 692 hkdISLASLRTL-----LVA-DGANPWSLSSCDAFAAAFTPSPYSlrPDAMCPCAGSSEtGTISIRrrgnaqlGSQSGRG 765
Cdd:PRK05691 279 ---VSESALERLdlsrwRVAySGSEPIRQDSLERFAEKFAACGFD--PDSFFASYGLAE-ATLFVS-------GGRRGQG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 766 I----LSMSALSHCVVRVDTENSLTSLTLQDAGQIVAGAVVVVTAIDGSNRlcqadeIGEICVSANSTAQLYWALDGQTH 841
Cdd:PRK05691 346 IpaleLDAEALARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVLGDNR------VGEIWASGPSIAHGYWRNPEASA 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 842 HTFkVEPVGEygkligavRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATVlaVEPMKFVYRGRICVFST 921
Cdd:PRK05691 420 KTF-VEHDGR--------TWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTV--EREVEVVRKGRVAAFAV 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 922 SVLRDERIVIVAE-----QKPNCSEEeafdWITRVLRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFENGDL 996
Cdd:PRK05691 488 NHQGEEGIGIAAEisrsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL 563
|
650 660 670
....*....|....*....|....*....|
gi 808354811 997 hpstllmcphNCVLNLPKPRERQADVGPAA 1026
Cdd:PRK05691 564 ----------DSYALFPALQAVEAAQTAAS 583
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
415-982 |
1.14e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 123.51 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 415 LTYGKLHSRAGKVAYmlltktvQVNKDGSknvmckPGDRVALIYPntQPLHFLAAFYGCLQAGVIPVPVEMPssKREAGI 494
Cdd:PRK05850 36 LTWSQLYRRTLNVAE-------ELRRHGS------TGDRAVILAP--QGLEYIVAFLGALQAGLIAVPLSVP--QGGAHD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 495 AQLGFLLGNCGVKVALTSESCYKGLPKKVNTSSTFSAPSgsnsltgtsseIV-----DFrgwprlwwavtehmskPSRDW 569
Cdd:PRK05850 99 ERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPP-----------VIevdllDL----------------DSPRG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 570 TAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRAL-TTAMEYKE-----DETMVCVVDFKREVGLWHAILASIF 643
Cdd:PRK05850 152 SDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmSDYFGDTGgvpppDTTVVSWLPFYHDMGLVLGVCAPIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 644 NGMKVIFV-PYSLMkMNPATWMHMVSKYQATTalvkSRDLHWAL-LATRDHKDISLASL---RTLLVADGA---NPWSLS 715
Cdd:PRK05850 232 GGCPAVLTsPVAFL-QRPARWMQLLASNPHAF----SAAPNFAFeLAVRKTSDDDMAGLdlgGVLGIISGServHPATLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 716 S-CDAFAaaftpsPYSLRPDAMCPCAG---------SSETGTISIRRR--------GNAQL-GSQSGRGILSMSALSHCV 776
Cdd:PRK05850 307 RfADRFA------PFNLRETAIRPSYGlaeatvyvaTREPGQPPESVRfdyeklsaGHAKRcETGGGTPLVSYGSPRSPT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 777 VR-VDTEnsltsltlqdagqivagavvvvtaidgSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKvepvgeyGKL 855
Cdd:PRK05850 381 VRiVDPD---------------------------TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFG-------ATL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 856 IGAVR------YVRSGLIGFMGpDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEpmkfvyRGRICVFSTSVLRDERI 929
Cdd:PRK05850 427 VDPSPgtpegpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEATIQEIT------GGRVAAISVPDDGTEKL 499
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811 930 VIVAE-QKPNCSEEEAFDWITRVLR----AIDTIHQVGIYCCALVPANHLPKTPLGGV 982
Cdd:PRK05850 500 VAIIElKKRGDSDEEAMDRLRTVKRevtsAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1049-1638 |
1.92e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 115.65 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1049 EPSLPLLECLRSRAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARLsrGDHVALIFPPSIDLVAAFFG 1128
Cdd:PRK05691 6 ELPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1129 CLSAGLVPVCIKPPVASDLNTTLGPIRMMVDmSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPS-SWRRKn 1207
Cdd:PRK05691 84 CLYAGVIAVPAYPPESARRHHQERLLSIIAD-AEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAeAWQEP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1208 nnncdtttsgssgAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSS--ELYPSRHVVVCAPPYSGISLVLWC 1285
Cdd:PRK05691 162 -------------ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPLYHDMGLIGGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1286 LSSVYSGHHTTLIPPMEVEQQPSLFLTTLSNLKvrdafttySTIN--------TCVTQLA-TSVENLrergcNLSMLRsc 1356
Cdd:PRK05691 229 LQPIFSGVPCVLMSPAYFLERPLRWLEAISEYG--------GTISggpdfayrLCSERVSeSALERL-----DLSRWR-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1357 VAIAEERP-RIALMSSFCKLFAPLALNNRAISTSFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLvGKGAPhsva 1435
Cdd:PRK05691 294 VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEP-GTGSV---- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1436 LIESGKLLPGVKIAIANPETRGQCADSHLGEIWVA--SIHNASPLNRLASVTGFgdegtMNTDvynarlttGDTktrWAR 1513
Cdd:PRK05691 369 LMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASgpSIAHGYWRNPEASAKTF-----VEHD--------GRT---WLR 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1514 TGYLGFLRqtqsiteHGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFTWNHL----VVIAAEC 1587
Cdd:PRK05691 433 TGDLGFLR-------DGEL----FVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkGRVAAFAVNHQgeegIGIAAEI 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 808354811 1588 TGSESDAL---DLVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGEKLRSTIR 1638
Cdd:PRK05691 502 SRSVQKILppqALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACR 555
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
407-994 |
5.19e-25 |
|
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: 111.61 E-value: 5.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 407 QSAKPSTQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQplHFLAAFYGCLQAGVIPVPVEMP 486
Cdd:cd05906 32 DADGSEEFQSYQDLLEDARRLAAGLRQLGL------------RPGDSVILQFDDNE--DFIPAFWACVLAGFVPAPLTVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 487 S-----SKREAGIAQLGFLLGNCgvkVALTSEscykglpkkvntsstfsapsgsnSLTGTSSEIVDFRGWPRLWWAVTEH 561
Cdd:cd05906 98 PtydepNARLRKLRHIWQLLGSP---VVLTDA-----------------------ELVAEFAGLETLSGLPGIRVLSIEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 562 MSKPSRDWTAPPRLADeTIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILAS 641
Cdd:cd05906 152 LLDTAADHDLPQSRPD-DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 642 IFNGMKVIFVPYSLMKMNPATWMHMVSKYQATT------ALVKSRDlhwaLLATRDHKDISLASLRTLLVADGANpwSLS 715
Cdd:cd05906 231 VYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLND----LLEEIEDGTWDLSSLRYLVNAGEAV--VAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 716 SCDAFAAAFtpSPYSLRPDAMCPCAGSSETGTISIRrrgNAQLGSQSGRGILSMSALSHCV----VR-VDTENSLTSltl 790
Cdd:cd05906 305 TIRRLLRLL--EPYGLPPDAIRPAFGMTETCSGVIY---SRSFPTYDHSQALEFVSLGRPIpgvsMRiVDDEGQLLP--- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 791 qdagqivagavvvvtaidgsnrlcqADEIGEICVSANSTAQLYWALDGQTHHTFKvepvgEYGkligavrYVRSGLIGFM 870
Cdd:cd05906 377 -------------------------EGEVGRLQVRGPVVTKGYYNNPEANAEAFT-----EDG-------WFRTGDLGFL 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 871 GpDGMVFVVARRQSLLAVSGRYHSADDIIAtvlAVEPMKFVYRGRICVFSTsvlRD-----ERIVIVAeqkpnCSEEEAF 945
Cdd:cd05906 420 D-NGNLTITGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAV---RDpgaetEELAIFF-----VPEYDLQ 487
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 808354811 946 DWITRVLRAIDTI--HQVGIYCCALVPANH--LPKTPLGGVHVSETKQRFENG 994
Cdd:cd05906 488 DALSETLRAIRSVvsREVGVSPAYLIPLPKeeIPKTSLGKIQRSKLKAAFEAG 540
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1058-1521 |
9.99e-25 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 108.94 E-value: 9.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1058 LRSRAQSSPDHRILTlvtskNAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPV 1137
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1138 CIkppvasdlNTTLGP--IRMMVDMSKAVAILApQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWRRKNNNNCDTTT 1215
Cdd:pfam00501 75 PL--------NPRLPAeeLAYILEDSGAKVLIT-DDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1216 SGSSGAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSE----LYPSRHVVVCAPPYSGISLVLWCLSSVYS 1291
Cdd:pfam00501 146 PPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1292 GhHTTLIPPMEVEQQPSLFLTTLSNLKVRDAFTTYSTINTCvtqlatsVENLRERGCNLSMLRSCVaIAEERPRIALMSS 1371
Cdd:pfam00501 226 G-ATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVL-SGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1372 FcklfapLALNNRAISTSFSSRVNAAICMQGASGPEPSTVyvdaralrndrislvgkgaPHSValiesGKLLPGVKIAIA 1451
Cdd:pfam00501 297 F------RELFGGALVNGYGLTETTGVVTTPLPLDEDLRS-------------------LGSV-----GRPLPGTEVKIV 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808354811 1452 NPETRGQCADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTmntdvyNARLTTGdtktRWARTGYLGFLR 1521
Cdd:pfam00501 347 DDETGEPVPPGEPGELCVRGPGVMKGyLND--------PELT------AEAFDED----GWYRTGDLGRRD 399
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
414-1001 |
1.11e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 110.87 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIyPNTQPlHFLAAFYGCLQAGVIPVPVEMPSS--KRE 491
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGL------------KPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPMGfgGRE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 492 AGIAQLGFLLGNCGVKVALtsescykglpkkvntsstfsAPSGSNSLTgtsSEIVDFRgwpRLWWAVT--EHMSKPSRDW 569
Cdd:PRK09192 115 SYIAQLRGMLASAQPAAII--------------------TPDELLPWV---NEATHGN---PLLHVLShaWFKALPEADV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 570 TAPPRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALT-TAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKV 648
Cdd:PRK09192 169 ALPRPTPDD-IAYLQYSSGSTRFPRGVIITHRALMANLRAIShDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 649 IFVPYSLMKMNPATWMHMVSKYQATTALvkSRDLHWALLATR----DHKDISLASLRtlLVADGANPWSLSSCDAFAAAF 724
Cdd:PRK09192 248 DYLPTRDFARRPLQWLDLISRNRGTISY--SPPFGYELCARRvnskDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 725 TPSPYSlrPDAMCPCAGSSE-TGTISIrrrgnaqlgSQSGRGI----LSMSALSHCVVRVDT-ENSLTSLTLQDAGQIVA 798
Cdd:PRK09192 324 APAGFD--DKAFMPSYGLAEaTLAVSF---------SPLGSGIvveeVDRDRLEYQGKAVAPgAETRRVRTFVNCGKALP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 799 GAVVVVTAIDGS---NRlcqadEIGEICVSANSTAQLYWALDgqthhtfkvepvgEYGKLIGAVRYVRSGLIGFMGpDGM 875
Cdd:PRK09192 393 GHEIEIRNEAGMplpER-----VVGHICVRGPSLMSGYFRDE-------------ESQDVLAADGWLDTGDLGYLL-DGY 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 876 VFVVARRQSLLAVSGRYHSADDIiatVLAVEPMKFVYRGRICVFSTSVLRDERIVIVAEQKPNCSEEEA--FDWITRVLR 953
Cdd:PRK09192 454 LYITGRAKDLIIINGRNIWPQDI---EWIAEQEPELRSGDAAAFSIAQENGEKIVLLVQCRISDEERRGqlIHALAALVR 530
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 808354811 954 AIDTIHQVgiycCALVPANHLPKTPLGGVHVSETKQRFENGDLHPSTL 1001
Cdd:PRK09192 531 SEFGVEAA----VELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDV 574
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
449-996 |
5.73e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.05 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 449 KPGDRVALIYPntQPLHFLAAFYGCLQAGVIPVPVEMPSskrEAG-IAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSS 527
Cdd:PRK07769 77 KPGDRVAILAP--QNLDYLIAFFGALYAGRIAVPLFDPA---EPGhVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 528 TFSAPsgsnsltgtssEIVDFRGWPRlwwAVTEhmskpsrDWTaPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHC 607
Cdd:PRK07769 152 AKERP-----------RVIAVDAVPD---EVGA-------TWV-PPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 608 RALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKmNPATWMHMVSKYQATTALVKSRDLHWA-- 685
Cdd:PRK07769 210 LQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWIRELARKPGGTGGTFSAAPNFAfe 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 686 LLATR-----DHKDISLASLRTLLvaDGANPWSLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSE-TGTISIRRRGNAQLG 759
Cdd:PRK07769 289 HAAARglpkdGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAF--APYGLPPTAIKPSYGMAEaTLFVSTTPMDEEPTV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 760 SQSGRGILSmsalSHCVVRV--DTENSLTSLTlqdAGQIVAGAVVVVtaIDGSNRLCQAD-EIGEICVSANSTAQLYWAL 836
Cdd:PRK07769 365 IYVDRDELN----AGRFVEVpaDAPNAVAQVS---AGKVGVSEWAVI--VDPETASELPDgQIGEIWLHGNNIGTGYWGK 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 837 DGQTHHTFK------VEPVGEYGKLIGAvRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATvlAVEPMKF 910
Cdd:PRK07769 436 PEETAATFQnilksrLSESHAEGAPDDA-LWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLEYT--AQEATKA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 911 VYRGRICVFS---------------TSVLRD-----ERIVIVAEQKPNCSEEEAFDWITRVLRAIDTIHQVGIYCCALVP 970
Cdd:PRK07769 512 LRTGYVAAFSvpanqlpqvvfddshAGLKFDpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVP 591
|
570 580
....*....|....*....|....*.
gi 808354811 971 ANHLPKTPLGGVHVSETKQRFENGDL 996
Cdd:PRK07769 592 AGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1054-1648 |
7.25e-20 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 95.96 E-value: 7.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1054 LLECLRSRAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARlsRGDHVALIFPPSIDLVAAFFGCLSAG 1133
Cdd:PRK12476 39 LIERNIANVGDTVAYRYLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAAIKAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1134 LVPVCIKPPV----ASDLNTTLGPIRMMVDMSKAVAilaPQNVSKLLKSKEAAHSidsnawPMILDLEDAPSSwrrknnn 1209
Cdd:PRK12476 117 TIAVPLFAPElpghAERLDTALRDAEPTVVLTTTAA---AEAVEGFLRNLPRLRR------PRVIAIDAIPDS------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1210 ncdtttSGSSGAASK---EEICYLDFSINSSGQLQGSSMSEASAIT-VCKSIKVSSELYPSRHVVVCAPPYSGISLVLWC 1285
Cdd:PRK12476 181 ------AGESFVPVEldtDDVSHLQYTSGSTRPPVGVEITHRAVGTnLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1286 LSSVYSGHhTTLIPPMEVEQQPSLFLTTLSnlkvrdAFTTYSTINTCVTQLA---TSVENLRERGCNLSMLRSCVAIAEE 1362
Cdd:PRK12476 255 FPAVYGGH-STLMSPTAFVRRPQRWIKALS------EGSRTGRVVTAAPNFAyewAAQRGLPAEGDDIDLSNVVLIIGSE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1363 RPRIALMSSFCKLFAPLALNNRAISTSFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLVGKGAPHSVALIESGKL 1442
Cdd:PRK12476 328 PVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1443 LPGVKIAIANPETRGQCADSHLGEIWVASihnasplNRLASvtGFGDEGTMNTDVYNARLTT----------GDTKTRWA 1512
Cdd:PRK12476 408 ARSQWAVIVDPDTGAELPDGEVGEIWLHG-------DNIGR--GYWGRPEETERTFGAKLQSrlaegshadgAADDGTWL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1513 RTGYLGFLRQtqsitehGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFT-----WNHLVVIAA 1585
Cdd:PRK12476 479 RTGDLGVYLD-------GEL----YITGRIADLIVIDGRNHYPQDIEATVAEASPMVrrGYVTAFTvpaedNERLVIVAE 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808354811 1586 ECTG-SESDALDLVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGEKLRSTIRSLFLEEKLNP 1648
Cdd:PRK12476 548 RAAGtSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
449-994 |
7.73e-19 |
|
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: 91.78 E-value: 7.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 449 KPGDRValIYPNTQPLHFLAAFYGCLQAGVIPVPVEMPSSkreagiaqlgfllgncgvkvaltsESCYKGLPKKVNTSSt 528
Cdd:cd05908 38 KPGQEV--VFQITHNNKFLYLFWACLLGGMIAVPVSIGSN------------------------EEHKLKLNKVWNTLK- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 529 fsapsgsNSLTGTSSEIVDfrgwprlwwavtehmskpsrdwtappRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCR 608
Cdd:cd05908 91 -------NPYLITEEEVLC--------------------------ELADE-LAFIQFSSGSTGDPKGVMLTHENLVHNMF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 609 ALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATtaLVKSRDLHWALLA 688
Cdd:cd05908 137 AILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKAT--IVSSPNFGYKYFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 689 TR--DHK--DISLASLRtlLVADGANPWSLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSE-------------TGTISIR 751
Cdd:cd05908 215 KTlkPEKanDWDLSSIR--MILNGAEPIDYELCHEFLDHM--SKYGLKRNAILPVYGLAEasvgaslpkaqspFKTITLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 752 RRgnaqlGSQSGRGIlsmsalshcvVRVDTENSlTSLTLQDAGQivAGAVVVVTAIDGSNRLCQADEIGEICVSANSTAQ 831
Cdd:cd05908 291 RR-----HVTHGEPE----------PEVDKKDS-ECLTFVEVGK--PIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 832 LYWAldgqthhtfkvEPVgEYGKLIGAVRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPmkfV 911
Cdd:cd05908 353 GYYN-----------NPE-ATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEG---V 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 912 YRGR--ICVFSTSVLRDERIVIVAEQKPncSEEEAFDWITRVLRAID-----TIHQVgiyccalVPANHLPKTPLGGVHV 984
Cdd:cd05908 417 ELGRvvACGVNNSNTRNEEIFCFIEHRK--SEDDFYPLGKKIKKHLNkrggwQINEV-------LPIRRIPKTTSGKVKR 487
|
570
....*....|
gi 808354811 985 SETKQRFENG 994
Cdd:cd05908 488 YELAQRYQSG 497
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
579-982 |
2.68e-18 |
|
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: 88.11 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 579 TIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKrEVGLWHAILASIFNGMKVIFVPYSlmkm 658
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 659 NPATWMHMVSKYQATTALVkSRDLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFTPSPYSlrpdamcp 738
Cdd:cd04433 76 DPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPGIKLVN-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 739 CAGSSETG--TISIRRRGNAQLGSQSGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvvtaIDGSNRLCQA 816
Cdd:cd04433 145 GYGLTETGgtVATGPPDDDARKPGSVGR------PVPGVEVRI---------------------------VDPDGGELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 817 DEIGEICVSANSTAQLYWALDGQTHHTFKvepvgeygklIGavrYVRSGLIGFMGPDGMVFVVARRQSLLAVSGRYHSAD 896
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAVDE----------DG---WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 897 DIIATVLAVEPMKfvyrgRICVFstsVLRDER------IVIVAEQKPNCSEEEAFDWITRVLRAIDTIHQVgiyccalVP 970
Cdd:cd04433 259 EVEAVLLGHPGVA-----EAAVV---GVPDPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VF 323
|
410
....*....|..
gi 808354811 971 ANHLPKTPLGGV 982
Cdd:cd04433 324 VDALPRTASGKI 335
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
449-980 |
3.62e-18 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 90.57 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 449 KPGDRVALIYPntQPLHFLAAFYGCLQAGVIPVPVEMPSSKREAgiAQLGFLLGNCGVKVALTsescykglpkkvntsst 528
Cdd:PRK12476 90 GPGDRVAILAP--QGIDYVAGFFAAIKAGTIAVPLFAPELPGHA--ERLDTALRDAEPTVVLT----------------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 529 fsapsgsnslTGTSSEIVD--FRGWPRL----WWAVTEHMSKPSRDWTAPPrLADETIAYIEYTTGNDGTVKGCCVTRQA 602
Cdd:PRK12476 149 ----------TTAAAEAVEgfLRNLPRLrrprVIAIDAIPDSAGESFVPVE-LDTDDVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 603 VFAHCRALTTAMEYKEDETM-VCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKmNPATWMHMVSKYQATTALVKSR- 680
Cdd:PRK12476 218 VGTNLVQMILSIDLLDRNTHgVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVR-RPQRWIKALSEGSRTGRVVTAAp 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 681 DLHWALLATR----DHKDISLaslRTLLVADGANPWSLSSCDAFAAAFtpSPYSLRPDAMCPCAG-------------SS 743
Cdd:PRK12476 297 NFAYEWAAQRglpaEGDDIDL---SNVVLIIGSEPVSIDAVTTFNKAF--APYGLPRTAFKPSYGiaeatlfvatiapDA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 744 ETGTISIRRRgnaQLGSqsGRGILSMSALSHCVVRVDtensltsltlqdAGQIVAGAVVVVTAIDGSNRLcQADEIGEIC 823
Cdd:PRK12476 372 EPSVVYLDRE---QLGA--GRAVRVAADAPNAVAHVS------------CGQVARSQWAVIVDPDTGAEL-PDGEVGEIW 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 824 VSANSTAQLYWALDGQTHHTFKVE-----PVGEY--GKLIGAvRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSAD 896
Cdd:PRK12476 434 LHGDNIGRGYWGRPEETERTFGAKlqsrlAEGSHadGAADDG-TWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQ 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 897 DIIATVLAVEPMkfVYRGRICVFSTSVLRDERIVIVAEQKPNCSEEEAFDWITRVLRAIDTIHQVGIYCCALVPANHLPK 976
Cdd:PRK12476 512 DIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPR 589
|
....
gi 808354811 977 TPLG 980
Cdd:PRK12476 590 TTSG 593
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1051-1624 |
1.23e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 88.46 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1051 SLPLLecLRSRAQSSPDHRILTLVtskNAEQDTA------TCSTLLKRAERIAGLLtdRARLSRGDHVALIFPPSIDLVA 1124
Cdd:PRK05850 2 SVPSL--LRERASLQPDDAAFTFI---DYEQDPAgvaetlTWSQLYRRTLNVAEEL--RRHGSTGDRAVILAPQGLEYIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1125 AFFGCLSAGLVPVCIKPPV--ASDLNTTLgpirMMVDmSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSS 1202
Cdd:PRK05850 75 AFLGALQAGLIAVPLSVPQggAHDERVSA----VLRD-TSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1203 wrrknnNNCDtttsgsSGAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSI---------KVSSelyPSRHVVVCA 1273
Cdd:PRK05850 150 ------RGSD------ARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdyfgdtgGVPP---PDTTVVSWL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1274 PPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPSLFLTTLSnlKVRDAFTTYSTIntcVTQLA---TSVENLRerGCNL 1350
Cdd:PRK05850 215 PFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRPARWMQLLA--SNPHAFSAAPNF---AFELAvrkTSDDDMA--GLDL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1351 SMLRSCVAIAEeRPRIALMSSFCKLFAPLALNNRAISTSF---SSRVNAAIcmqGASGPEPSTVYVDARALRNDRI---- 1423
Cdd:PRK05850 288 GGVLGIISGSE-RVHPATLKRFADRFAPFNLRETAIRPSYglaEATVYVAT---REPGQPPESVRFDYEKLSAGHAkrce 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1424 -----SLVGKGAPHSvaliesgkllPGVKIAiaNPETRGQCADSHLGEIWVASIHNASplnrlasvtGF--GDEGTMNTd 1496
Cdd:PRK05850 364 tgggtPLVSYGSPRS----------PTVRIV--DPDTCIECPAGTVGEIWVHGDNVAA---------GYwqKPEETERT- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1497 vYNARLTT---GDTKTRWARTGYLGFlrqtqsITEhGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRfvGNSA 1573
Cdd:PRK05850 422 -FGATLVDpspGTPEGPWLRTGDLGF------ISE-GEL----FIVGRIKDLLIVDGRNHYPDDIEATIQEITG--GRVA 487
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354811 1574 VFT-----WNHLVVIA--AECTGSESDALDLVPA----ITSAVLEEHHLIVGVVVVVDPGSI 1624
Cdd:PRK05850 488 AISvpddgTEKLVAIIelKKRGDSDEEAMDRLRTvkreVTSAISKSHGLSVADLVLVAPGSI 549
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1104-1652 |
3.81e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 87.48 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1104 ARL----SRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikPPVASDLNTTLGPIRMMVDMSKAVAIL----APQNVSKL 1175
Cdd:PRK07769 70 ARLqqvtKPGDRVAILAPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGHVGRLHAVLDDCTPSAILtttdSAEGVRKF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1176 LKSKEAAHSidsnawPMILDLEDAP----SSWRRKNNNNCDTT----TSGSSGAASKEEICYLDFSINssgqlqgssmse 1247
Cdd:PRK07769 147 FRARPAKER------PRVIAVDAVPdevgATWVPPEANEDTIAylqyTSGSTRIPAGVQITHLNLPTN------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1248 asAITVCKSIkvssELYPSRHVVVCAPPYSGISLVLWCLSSVySGHHTTLIPPMEVEQQPSLFLTTLSNlKVRDAFTTYS 1327
Cdd:PRK07769 209 --VLQVIDAL----EGQEGDRGVSWLPFFHDMGLITVLLPAL-LGHYITFMSPAAFVRRPGRWIRELAR-KPGGTGGTFS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1328 TINTCVTQLATS--VENLRERGCNLSMLRSCVAiAEERPRIALMSSFCKLFAPLALNNRAISTSFSSrvnAAICMQGASG 1405
Cdd:PRK07769 281 AAPNFAFEHAAArgLPKDGEPPLDLSNVKGLLN-GSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGM---AEATLFVSTT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1406 P---EPSTVYVDARALRNDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGQCADSHLGEIWVASIHNASPLNRLA 1482
Cdd:PRK07769 357 PmdeEPTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1483 SVTGFGDEGTMNTDVYNARLTTGDTKTRWARTGYLGflrqtqsITEHGELhdavFVVGALNESLVLRGMRYHPFDVESTV 1562
Cdd:PRK07769 437 EETAATFQNILKSRLSESHAEGAPDDALWVRTGDYG-------VYFDGEL----YITGRVKDLVIIDGRNHYPQDLEYTA 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1563 ---SKAHR--FVG---------NSAVFTWNH-------------LVVIAAECTGS-ESDALDLVPAITSAVLEEHHLIVG 1614
Cdd:PRK07769 506 qeaTKALRtgYVAafsvpanqlPQVVFDDSHaglkfdpedtseqLVIVAERAPGAhKLDPQPIADDIRAAIAVRHGVTVR 585
|
570 580 590
....*....|....*....|....*....|....*...
gi 808354811 1615 VVVVVDPGSIRHGPGGEKLRSTIRSLFLEEKLNPIYVA 1652
Cdd:PRK07769 586 DVLLVPAGSIPRTSSGKIARRACRAAYLDGSLRSGYGQ 623
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
408-890 |
2.38e-16 |
|
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: 84.19 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 408 SAKPSTQLTYGKLHSRAGKVAYMLltktvqvNKDGSKnvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPS 487
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGL-------RKLGLK-----KGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAANPIY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 488 SKREagiaqLGFLLGNCGVKVALTSESCYKglpkKVNTSSTFSAPSGSNSLTGTSSEIVDFRGwpRLWWAVTEhmskpSR 567
Cdd:cd05911 70 TADE-----LAHQLKISKPKVIFTDPDGLE----KVKEAAKELGPKDKIIVLDDKPDGVLSIE--DLLSPTLG-----EE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 568 DWTAPPRL--ADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCR--ALTTAMEYKEDETMVCVVDFKREVGLWhAILASIF 643
Cdd:cd05911 134 DEDLPPPLkdGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSqvQTFLYGNDGSNDVILGFLPLYHIYGLF-TTLASLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 644 NGMKVIFVPyslmKMNPATWMHMVSKYQATTALVKSRdlHWALLATR-DHKDISLASLRTLLVadGANPWSLSSCDAFAA 722
Cdd:cd05911 213 NGATVIIMP----KFDSELFLDLIEKYKITFLYLVPP--IAAALAKSpLLDKYDLSSLRVILS--GGAPLSKELQELLAK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 723 aftpspysLRPDAMCPCA-GSSETG-TISIRRRGNAQLGSqSGRGILSMSALshcVVRVDTENSLTSltlqdagqivaga 800
Cdd:cd05911 285 --------RFPNATIKQGyGMTETGgILTVNPDGDDKPGS-VGRLLPNVEAK---IVDDDGKDSLGP------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 801 vvvvtaidgsnrlcqaDEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkligavRYVRSGLIGFMGPDGMVFVVA 880
Cdd:cd05911 340 ----------------NEPGEICVRGPQVMKGYYNNPEATKETFDED------------GWLHTGDIGYFDEDGYLYIVD 391
|
490
....*....|
gi 808354811 881 RRQSLLAVSG 890
Cdd:cd05911 392 RKKELIKYKG 401
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1054-1575 |
2.89e-16 |
|
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: 83.32 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1054 LLECLRSRAQSSPDHRILTlvtsknAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG 1133
Cdd:COG0318 1 LADLLRRAAARHPDRPALV------FGGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1134 LVPVCikppvasdLNTTLGP--IRMMVDMSKAVAILApqnvskllkskeaahsidsnAWpMILdledapsswrrknnnnc 1211
Cdd:COG0318 74 AVVVP--------LNPRLTAeeLAYILEDSGARALVT--------------------AL-ILY----------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1212 dttTSGSSGaASKeeicyldfsinssgqlqGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYS 1291
Cdd:COG0318 108 ---TSGTTG-RPK-----------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1292 GHHTTLIPPMEveqqPSLFLTTLSNLKVrdafTTYSTINTCVTQLAtsvENLRERGCNLSMLRSCVAIAeERPRIALMSS 1371
Cdd:COG0318 167 GATLVLLPRFD----PERVLELIERERV----TVLFGVPTMLARLL---RHPEFARYDLSSLRLVVSGG-APLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1372 FCKLFaplalnNRAISTSF-SSRVNAAICMqgasGPEpstvyvDARALRndrislvgkgaPHSValiesGKLLPGVKIAI 1450
Cdd:COG0318 235 FEERF------GVRIVEGYgLTETSPVVTV----NPE------DPGERR-----------PGSV-----GRPLPGVEVRI 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1451 ANPETRgQCADSHLGEIWVASihnasplnrlASVTG--FGD-EGTmntdvyNARLTTGdtktrWARTGYLGFlrqtqsIT 1527
Cdd:COG0318 283 VDEDGR-ELPPGEVGEIVVRG----------PNVMKgyWNDpEAT------AEAFRDG-----WLRTGDLGR------LD 334
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 808354811 1528 EHGELhdavFVVGALNESLVLRGMRYHPFDVESTVSkAHRFVGNSAVF 1575
Cdd:COG0318 335 EDGYL----YIVGRKKDMIISGGENVYPAEVEEVLA-AHPGVAEAAVV 377
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
412-706 |
1.26e-15 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 82.08 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 412 STQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKRE 491
Cdd:COG0365 37 ERTLTYAELRREVNRFANALRALGV------------KKGDRVAIYLPNI--PEAVIAMLACARIGAVHSPV-FPGFGAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 492 AgiaqLGFLLGNCGVKVALTSESCYKGlPKKVNTSSTFS-APSGSNSLT-----GTSSEIVDFRGWprLWWAvtEHMSKP 565
Cdd:COG0365 102 A----LADRIEDAEAKVLITADGGLRG-GKVIDLKEKVDeALEELPSLEhvivvGRTGADVPMEGD--LDWD--ELLAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 566 SRDWTAPPRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHcrALTTAM---EYKEDETMVCVVDFKREVGLWHAILASI 642
Cdd:COG0365 173 SAEFEPEPTDADD-PLFILYTSGTTGKPKGVVHTHGGYLVH--AATTAKyvlDLKPGDVFWCTADIGWATGHSYIVYGPL 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354811 643 FNGMKVIFVPYSLMKMNPATWMHMVSKYQAT------TALvksRdlhwALLATRDH--KDISLASLRTLLVA 706
Cdd:COG0365 250 LNGATVVLYEGRPDFPDPGRLWELIEKYGVTvfftapTAI---R----ALMKAGDEplKKYDLSSLRLLGSA 314
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
402-890 |
2.96e-15 |
|
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: 80.30 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 402 AMVLDQSA-----KPSTQ-----LTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFY 471
Cdd:cd05936 2 ADLLEEAArrfpdKTALIfmgrkLTYRELDALAEAFAAGLQNLGVQ------------PGDRVALMLPNC--PQFPIAYF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 472 GCLQAGVIPVPVEMPSSKREagiaqLGFLLGNCGVKValtsescykglpkkvntsstfsapsgsnsltgtsseIVDFRGW 551
Cdd:cd05936 68 GALKAGAVVVPLNPLYTPRE-----LEHILNDSGAKA------------------------------------LIVAVSF 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 552 prlwwavtEHMSKPSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAH---CRALTTAMEyKEDETMVCVVDF 628
Cdd:cd05936 107 --------TDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANalqIKAWLEDLL-EGDDVVLAALPL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 629 KREVGLWHAILASIFNGMKVIFVPyslmKMNPATWMHMVSKYQATT-ALVKSrdLHWALLATRDHKDISLASLRtlLVAD 707
Cdd:cd05936 178 FHVFGLTVALLLPLALGATIVLIP----RFRPIGVLKEIRKHRVTIfPGVPT--MYIALLNAPEFKKRDFSSLR--LCIS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 708 GANPWSLSSCDAFAAAF-TP----------SPYSlrpdAMCPCAGSSETGTIsirrrgnaqlgsqsGRGILSMSALshcV 776
Cdd:cd05936 250 GGAPLPVEVAERFEELTgVPivegygltetSPVV----AVNPLDGPRKPGSI--------------GIPLPGTEVK---I 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 777 VRVDTEnsltslTLQDagqivagavvvvtaidgsnrlcqaDEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkli 856
Cdd:cd05936 309 VDDDGE------ELPP------------------------GEVGELWVRGPQVMKGYWNRPEETAEAFVDG--------- 349
|
490 500 510
....*....|....*....|....*....|....
gi 808354811 857 gavrYVRSGLIGFMGPDGMVFVVARRQSLLAVSG 890
Cdd:cd05936 350 ----WLRTGDIGYMDEDGYFFIVDRKKDMIIVGG 379
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
412-701 |
5.97e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 79.95 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 412 STQLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKRE 491
Cdd:PRK07656 28 DQRLTYAELNARVRRAAAALAALGIG------------KGDRVAIWAPNS--PHWVIAALGALKAGAVVVPLNTRYTADE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 492 AgiaqlGFLLGNCGVKVAL-------TSESCYKGLPK-KVNTSSTFSAPSGSNSLTGTSSEIVdfrgwprlwwavtehmS 563
Cdd:PRK07656 94 A-----AYILARGDAKALFvlglflgVDYSATTRLPAlEHVVICETEEDDPHTEKMKTFTDFL----------------A 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 564 KPSRDWTAPPrLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIF 643
Cdd:PRK07656 153 AGDPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811 644 NGMKVIFVPyslmKMNPATWMHMVSKYQATTaLVKSRDLHWALLATRDHKDISLASLR 701
Cdd:PRK07656 232 RGATILPLP----VFDPDEVFRLIETERITV-LPGPPTMYNSLLQHPDRSAEDLSSLR 284
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1087-1609 |
1.59e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 78.51 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1087 STLLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikpPVAsdLNTTLG-------PIRMMVD 1159
Cdd:PRK09192 53 QTLRARAEAGARRLL-ALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV----PLP--LPMGFGgresyiaQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1160 MSKAVAILAPQNVSKLLksKEAAHSID-----SNAWpmiLDLEDAPsswrrknnnNCDTTTsgssgaASKEEICYLDFSI 1234
Cdd:PRK09192 126 SAQPAAIITPDELLPWV--NEATHGNPllhvlSHAW---FKALPEA---------DVALPR------PTPDDIAYLQYSS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1235 NSS----GQL--QGSSMSEASAITvCKSIKVsselYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPS 1308
Cdd:PRK09192 186 GSTrfprGVIitHRALMANLRAIS-HDGLKV----RPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1309 LFLTTLSnlkvRDAFT-TYST---INTCvtqlATSVENLRERGCNLSMLRScVAIAEERPRIALMSSFCKLFAPLALNNR 1384
Cdd:PRK09192 261 QWLDLIS----RNRGTiSYSPpfgYELC----ARRVNSKDLAELDLSCWRV-AGIGADMIRPDVLHQFAEAFAPAGFDDK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1385 AISTSFSSRVNA-AICM----QGAsgpepSTVYVDARALRNDRISLVGKGAPHSV-ALIESGKLLPGVKIAIANpETRGQ 1458
Cdd:PRK09192 332 AFMPSYGLAEATlAVSFsplgSGI-----VVEEVDRDRLEYQGKAVAPGAETRRVrTFVNCGKALPGHEIEIRN-EAGMP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1459 CADSHLGEIWVA--SIHNASplnrlasvtgFGDEGTmnTDVYNArlttgdtkTRWARTGYLGFLrqtqsitEHGELhdav 1536
Cdd:PRK09192 406 LPERVVGHICVRgpSLMSGY----------FRDEES--QDVLAA--------DGWLDTGDLGYL-------LDGYL---- 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808354811 1537 FVVGALNESLVLRGMRYHPFDVESTVSKAHRF-VGNSAVF---TWNH-LVVIAAECTGSESDA-LDLVPAITSAVLEEH 1609
Cdd:PRK09192 455 YITGRAKDLIIINGRNIWPQDIEWIAEQEPELrSGDAAAFsiaQENGeKIVLLVQCRISDEERrGQLIHALAALVRSEF 533
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
416-706 |
3.14e-14 |
|
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: 76.92 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 416 TYGKLHSRAGKVAYMLLTKtvqvnkdgsknVMCKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPV--EMPSSKREag 493
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-----------GGVGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLdpAYPAERLA-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 494 iaqlgFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsgsnsltGTSSEIVDFRgwPRLWWAVTEHMSKPSRDWTAPP 573
Cdd:TIGR01733 66 -----FILEDAGARLLLTDSALASRLA-------------------GLVLPVILLD--PLELAALDDAPAPPPPDAPSGP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 574 rladETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWhAILASIFNGMKVIFVPY 653
Cdd:TIGR01733 120 ----DDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 808354811 654 SLMKMNPATWMHMVSKYQATTA-LVKSrdlHWALLAtrDHKDISLASLRTLLVA 706
Cdd:TIGR01733 195 DEERDDAALLAALIAEHPVTVLnLTPS---LLALLA--AALPPALASLRLVILG 243
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1264-1596 |
3.35e-13 |
|
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: 72.70 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1264 YPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPmeveQQPSLFLTTLSNLKVRDAFTTYSTINTCVtqlatsvENL 1343
Cdd:cd04433 38 LTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK----FDPEAALELIEREKVTILLGVPTLLARLL-------KAP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1344 RERGCNLSMLRSCVAIAEERPrIALMSSFcklfapLALNNRAISTSFssrvnaaicmqGAS--GPEPSTVYVDARALRnd 1421
Cdd:cd04433 107 ESAGYDLSSLRALVSGGAPLP-PELLERF------EEAPGIKLVNGY-----------GLTetGGTVATGPPDDDARK-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1422 rislvgkgaPHSValiesGKLLPGVKIAIANPETRGqCADSHLGEIWVASIHNasplnrlasvtgfgdegtMNTDVYNAR 1501
Cdd:cd04433 167 ---------PGSV-----GRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSV------------------MKGYWNNPE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1502 LTTGDTKTRWARTGYLGFLRqtqsitEHGELHdavfVVGALNESLVLRGMRYHPFDVESTVsKAHRFVGNSAVF-----T 1576
Cdd:cd04433 214 ATAAVDEDGWYRTGDLGRLD------EDGYLY----IVGRLKDMIKSGGENVYPAEVEAVL-LGHPGVAEAAVVgvpdpE 282
|
330 340
....*....|....*....|
gi 808354811 1577 WNHLVVIAAECTGSESDALD 1596
Cdd:cd04433 283 WGERVVAVVVLRPGADLDAE 302
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
344-871 |
7.01e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.14 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 344 LEAMAKirDPDAPRPEGTIMNP---VRGEAAHSNTNNTMPRSLDSFSAFHRFGTTAAKNIAAMVLDQsakpstQLTYGKL 420
Cdd:PRK12316 1963 LEQMAE--DAQAALGELALLDAgerQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQ------HLSYAEL 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 421 HSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmPSSKREagiaQLGFL 500
Cdd:PRK12316 2035 DSRANRLAHRLRARGV------------GPEVRVAIAAERSFEL--VVALLAVLKAGGAYVPLD-PNYPAE----RLAYM 2095
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 501 LGNCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLTGTSSEivDFRGWPRlwwavtehmskpsrdwTAP-PRLADET 579
Cdd:PRK12316 2096 LEDSGAALLLTQRHLLERLP----------LPAGVARLPLDRDA--EWADYPD----------------TAPaVQLAGEN 2147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 580 IAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHaILASIFNGMKVIFVPYSLmkMN 659
Cdd:PRK12316 2148 LAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIRDDEL--WD 2224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 660 PATWMHMVSKYQATTALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAftpspysLRPDAMCPC 739
Cdd:PRK12316 2225 PEQLYDEMERHGVTILDFPP--VYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEA-------LRPVYLFNG 2293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 740 AGSSETGTISIRRRGNAQLGSQS-----GRGIlsmSALSHCVvrvdtensltsltlqdagqivagavvvvtaIDGSNRLC 814
Cdd:PRK12316 2294 YGPTEAVVTPLLWKCRPQDPCGAayvpiGRAL---GNRRAYI------------------------------LDADLNLL 2340
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808354811 815 QADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKLI----GAVRYVRSGLIGFMG 871
Cdd:PRK12316 2341 APGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLyrtgDLARYRADGVVEYLG 2401
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
448-982 |
8.74e-11 |
|
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: 66.31 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 448 CKPGDRVALIYPNTQPLHFLAA--FYGCLQAGVIPVPVEmPSSKReagiAQLGFLLGNCGVKVALTSEScYKGLPKKVNT 525
Cdd:cd05922 15 GVRGERVVLILPNRFTYIELSFavAYAGGRLGLVFVPLN-PTLKE----SVLRYLVADAGGRIVLADAG-AADRLRDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 526 SStfsapsgsnsltGTSSEIVDFRGWprlwWAvtehmskpSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFA 605
Cdd:cd05922 89 AS------------PDPGTVLDADGI----RA--------ARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 606 HCRALTTAMEYKEDETMVCVVDFKREVGLwHAILASIFNGMKVIFVPYSLMkmnPATWMHMVSKYQATT-ALVKSrdlHW 684
Cdd:cd05922 145 NARSIAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVL---DDAFWEDLREHGATGlAGVPS---TY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 685 ALLATRDHKDISLASLRTLLVADGANPwslsscDAFAAAFTpspySLRPDAMcpcagssetgtisirrrgnaqlgsqsgr 764
Cdd:cd05922 218 AMLTRLGFDPAKLPSLRYLTQAGGRLP------QETIARLR----ELLPGAQ---------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 765 gILSMSALSHCVVR---VDTENSLTSLTlqDAGQIVAGAVVVVTAIDGSnrLCQADEIGEICVSANSTAQLYWalDGQTH 841
Cdd:cd05922 260 -VYVMYGQTEATRRmtyLPPERILEKPG--SIGLAIPGGEFEILDDDGT--PTPPGEPGEIVHRGPNVMKGYW--NDPPY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 842 HTFKVEPVGeygkligavrYVRSGLIGFMGPDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPMkfvyrGRICVFST 921
Cdd:cd05922 333 RRKEGRGGG----------VLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808354811 922 SVLRDERIVIVAEQKPNCSEEEafdwITRVLRAIDTIHQVGIYCcalVPANHLPKTPLGGV 982
Cdd:cd05922 398 PDPLGEKLALFVTAPDKIDPKD----VLRSLAERLPPYKVPATV---RVVDELPLTASGKV 451
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
570-993 |
1.52e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 65.79 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 570 TAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYK-EDETMVCVVDFKREVGLWHAILASIFNGMKV 648
Cdd:PRK07768 144 IDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 649 IFV-PYSLMKmNPATWMHMVSKYQAT-TAlvkSRDLHWALLATR-----DHKDISLASLRTLLvaDGANPWSLSSCDAFA 721
Cdd:PRK07768 224 VKVtPMDFLR-DPLLWAELISKYRGTmTA---APNFAYALLARRlrrqaKPGAFDLSSLRFAL--NGAEPIDPADVEDLL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 722 AAftPSPYSLRPDAMCPCAGSSETG-TISIRRRGN--------AQLGSQSGRGILSMSA-----------LSHCVVRVdt 781
Cdd:PRK07768 298 DA--GARFGLRPEAILPAYGMAEATlAVSFSPCGAglvvdevdADLLAALRRAVPATKGntrrlatlgppLPGLEVRV-- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 782 ensltsltlqdagqivagavvvvtaIDGSNRLCQADEIGEICVSANSTAQLYWALDGQthhtfkVEPVGEYGKLigavry 861
Cdd:PRK07768 374 -------------------------VDEDGQVLPPRGVGVIELRGESVTPGYLTMDGF------IPAQDADGWL------ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 862 vRSGLIGFMGPDGMVFVVARRQSLLAVSGRYHSADDI---IATVLAVEPmkfvyRGRICVFSTSVLRDERIVIVAEQKPN 938
Cdd:PRK07768 417 -DTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIeraAARVEGVRP-----GNAVAVRLDAGHSREGFAVAVESNAF 490
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 808354811 939 CSEEEafdwITRVLRAI--DTIHQVGI--YCCALVPANHLPKTPLGGVHVSETKQRFEN 993
Cdd:PRK07768 491 EDPAE----VRRIRHQVahEVVAEVGVrpRNVVVLGPGSIPKTPSGKLRRANAAELVTP 545
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
350-675 |
2.94e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.57 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 350 IRDPDAPRPEGTIMNPVRGEAAhsntnntmprsLDSFSAFHRfGTTAAKNIAAMVLDQSAKP---------STQLTYGKL 420
Cdd:PRK12467 1538 VADPERRLGELDLLDEAERRQI-----------LEGWNATHT-GYPLARLVHQLIEDQAAATpeavalvfgEQELTYGEL 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 421 HSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEmPSSKREagiaQLGFL 500
Cdd:PRK12467 1606 NRRANRLAHRLIALGV------------GPEVLVGIAVERS--LEMVVGLLAILKAGGAYVPLD-PEYPRE----RLAYM 1666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 501 LGNCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLtgtsseIVDfrgwPRLWWAVTEHMSKPSRdwtappRLADETI 580
Cdd:PRK12467 1667 IEDSGIELLLTQSHLQARLP----------LPDGLRSL------VLD----QEDDWLEGYSDSNPAV------NLAPQNL 1720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 581 AYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHaILASIFNGMKVIFVPYSLMKmNP 660
Cdd:PRK12467 1721 AYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWE-LFWPLINGARLVIAPPGAHR-DP 1798
|
330
....*....|....*
gi 808354811 661 ATWMHMVSKYQATTA 675
Cdd:PRK12467 1799 EQLIQLIERQQVTTL 1813
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
413-623 |
2.90e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 61.49 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREa 492
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALLDLGL------------KKGDRVAALGHNS--DAYALLWLACARAGAVHVPVNFMLTGEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 493 giaqLGFLLGNCGVKVALTsESCYKGLPKKVNTSSTFSAPSGSNSLTGTSSE--IVDFRGWprlwwavtehmSKPSRDWT 570
Cdd:PRK08316 100 ----LAYILDHSGARAFLV-DPALAPTAEAALALLPVDTLILSLVLGGREAPggWLDFADW-----------AEAGSVAE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 808354811 571 APPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMV 623
Cdd:PRK08316 164 PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPL 216
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1078-1575 |
1.36e-08 |
|
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: 59.15 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1078 NAEQDTATCSTLLKRAERIA-GLltDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLvpvcikppVASDLNTTLGP--I 1154
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAaGL--RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGG--------IFSAANPIYTAdeL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1155 RMMVDMSKAVAIL-APQNVSKLLKSKEAAHSIDSnawpmILDLEDAPSswrrKNNNNCDTTTSGSSGA---------ASK 1224
Cdd:cd05911 75 AHQLKISKPKVIFtDPDGLEKVKEAAKELGPKDK-----IIVLDDKPD----GVLSIEDLLSPTLGEEdedlppplkDGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1225 EEICYLDFSINSSGQLQGSSMSEASAITVCKSIK-VSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEV 1303
Cdd:cd05911 146 DDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQtFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1304 EqqpsLFLTTLSNLKVRDAFTTystiNTCVTQLATSVENLRErgcNLSMLRSCVAIAeerprialmssfcklfAPLAlnn 1383
Cdd:cd05911 226 E----LFLDLIEKYKITFLYLV----PPIAAALAKSPLLDKY---DLSSLRVILSGG----------------APLS--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1384 RAISTSFSSRVNAAICMQG----ASGPePSTVyvdaralrndrislvgkgAPHSVALIES-GKLLPGVKIAIANPETRGQ 1458
Cdd:cd05911 276 KELQELLAKRFPNATIKQGygmtETGG-ILTV------------------NPDGDDKPGSvGRLLPNVEAKIVDDDGKDS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1459 CADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTMNTdvynarlttgDTKTRWARTGYLGFLRqtqsitEHGELhdavF 1537
Cdd:cd05911 337 LGPNEPGEICVRGPQVMKGyYNN--------PEATKET----------FDEDGWLHTGDIGYFD------EDGYL----Y 388
|
490 500 510
....*....|....*....|....*....|....*...
gi 808354811 1538 VVGALNESLVLRGMRYHPFDVEStVSKAHRFVGNSAVF 1575
Cdd:cd05911 389 IVDRKKELIKYKGFQVAPAELEA-VLLEHPGVADAAVI 425
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
344-881 |
1.59e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.97 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 344 LEAMAkiRDPDAPRPEGTIMNPVRGEAAHSNTNNTMPRSLDSFSAFHRFGTTAAKNIAAMVLDQSAKpstQLTYGKLHSR 423
Cdd:PRK12316 4511 LEAMA--EDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEE---KLTYAELNRR 4585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 424 AGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEmPSSKREagiaQLGFLLGN 503
Cdd:PRK12316 4586 ANRLAHALIARGV------------GPEVLVGIAMERS--AEMMVGLLAVLKAGGAYVPLD-PEYPRE----RLAYMMED 4646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 504 CGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLTgtsseiVDfrgwprlwwavtehmskPSRDWTAPP------RLAD 577
Cdd:PRK12316 4647 SGAALLLTQSHLLQRLP----------IPDGLASLA------LD-----------------RDEDWEGFPahdpavRLHP 4693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 578 ETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIfNGMKVIFVPYSLmk 657
Cdd:PRK12316 4694 DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLI-NGASVVIRDDSL-- 4770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 658 MNPATWMHMVSKYQATTALVKSrdLHWALLATRDHKDISLASLRTLLVADGANPwslssCDAFAAAFTpspySLRPDAMC 737
Cdd:PRK12316 4771 WDPERLYAEIHEHRVTVLVFPP--VYLQQLAEHAERDGEPPSLRVYCFGGEAVA-----QASYDLAWR----ALKPVYLF 4839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 738 PCAGSSETGTISIRRRgnAQLGSQSGRGILSMSALshcvvrvdtensLTSLtlqdAGQIvagavvvvtaIDGSNRLCQAD 817
Cdd:PRK12316 4840 NGYGPTETTVTVLLWK--ARDGDACGAAYMPIGTP------------LGNR----SGYV----------LDGQLNPLPVG 4891
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808354811 818 EIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKligavRYVRSGLIGFMGPDGMVFVVAR 881
Cdd:PRK12316 4892 VAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGG-----RLYRTGDLARYRADGVIDYLGR 4950
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
416-881 |
7.48e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 57.12 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 416 TYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQplHFLAAFYGCLQAGVIPVPVempsSKREAGiA 495
Cdd:PRK06187 33 TYAELDERVNRLANALRALGV------------KKGDRVAVFDWNSH--EYLEAYFAVPKIGAVLHPI----NIRLKP-E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 496 QLGFLLGNCGVKVALTSES---CYKGLPKKVNTSSTFSApSGSNSLTGTSSEIVDFRGwprlWWAVTEhmskPSRDWtap 572
Cdd:PRK06187 94 EIAYILNDAEDRVVLVDSEfvpLLAAILPQLPTVRTVIV-EGDGPAAPLAPEVGEYEE----LLAAAS----DTFDF--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 573 PRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDET-MVCVVDFkrEVGLWHAILASIFNGMKVI-- 649
Cdd:PRK06187 162 PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVyLVIVPMF--HVHAWGLPYLALMAGAKQVip 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 650 --FVPYSLMKM----NPaTWMHMV-SKYQattalvksrdlhwALLATRDHKDISLASLRtlLVADGANPWSLSSCDAFAA 722
Cdd:PRK06187 240 rrFDPENLLDLieteRV-TFFFAVpTIWQ-------------MLLKAPRAYFVDFSSLR--LVIYGGAALPPALLREFKE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 723 AFTpspyslrpdamCPCA---GSSETG-TISIRR------RGNAQLGSQsGRGILSMSalshcvVRVdtensltsltlqd 792
Cdd:PRK06187 304 KFG-----------IDLVqgyGMTETSpVVSVLPpedqlpGQWTKRRSA-GRPLPGVE------ARI------------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 793 agqivagavvvvtaIDGSNRLCQAD--EIGEICVSANSTAQLYWALDGQTHHTFkvepVGEygkligavrYVRSGLIGFM 870
Cdd:PRK06187 353 --------------VDDDGDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETI----DGG---------WLHTGDVGYI 405
|
490
....*....|.
gi 808354811 871 GPDGMVFVVAR 881
Cdd:PRK06187 406 DEDGYLYITDR 416
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
414-728 |
1.12e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.09 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 414 QLTYGKLHSRAGKVAYMLLTKtvqvnkdgskNVMCKPGDRVALiypnTQPLHFLAAFYGCLQAGVIPVPVEmPSSKREag 493
Cdd:PRK12467 3120 QLSYAELNRRANRLAHRLIAI----------GVGPDVLVGVAV----ERSVEMIVALLAVLKAGGAYVPLD-PEYPRE-- 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 494 iaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLTgtsseiVDfRGwprLWWAVTEHmsKPSrdwtapP 573
Cdd:PRK12467 3183 --RLAYMIEDSGVKLLLTQAHLLEQLP----------APAGDTALT------LD-RL---DLNGYSEN--NPS------T 3232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 574 RLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHaILASIFNGMKVIFVPY 653
Cdd:PRK12467 3233 RVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDN 3311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808354811 654 SLmkMNPATWMHMVSKYQATTALVKSRDLHwALLAtrDHKDISLASLRTLLVADGANPwslssCDAFAAAFTPSP 728
Cdd:PRK12467 3312 DL--WDPEELWQAIHAHRISIACFPPAYLQ-QFAE--DAGGADCASLDIYVFGGEAVP-----PAAFEQVKRKLK 3376
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
414-982 |
1.51e-07 |
|
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: 55.95 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREag 493
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGV------------RKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPINPMLKERE-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 494 iaqLGFLLGNCGVKVALtsescykglpkkvntsstfsapsgsnsltgTSSEIVDfrgwprlwwavtehmskpsrdwtapp 573
Cdd:cd05935 65 ---LEYILNDSGAKVAV------------------------------VGSELDD-------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 574 rladetIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFvpy 653
Cdd:cd05935 86 ------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 654 sLMKMNPATWMHMVSKYQAT------TALVKsrdlhwaLLATRDHKDISLASLRTLlvadGANPWSLsscdafaaaftps 727
Cdd:cd05935 157 -MARWDRETALELIEKYKVTfwtnipTMLVD-------LLATPEFKTRDLSSLKVL----TGGGAPM------------- 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 728 pyslrPDAmcpcagssetgtISIRRRGNAQLGSQSGRGILSMSALSHCvvrvdteNSLTSLTLQDAGQIVAGAVVVVTAI 807
Cdd:cd05935 212 -----PPA------------VAEKLLKLTGLRFVEGYGLTETMSQTHT-------NPPLRPKLQCLGIP*FGVDARVIDI 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 808 DgSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFkVEpvgeygklIGAVRYVRSGLIGFMGPDGMVFVVARRQSLLA 887
Cdd:cd05935 268 E-TGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESF-IE--------IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMIN 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 888 VSGryhsaddiiATVLAVEPMKFVYRGR----ICVFSTSvlrDER--------IVIVAEQKPNCSEEEAFDWITRVLRAI 955
Cdd:cd05935 338 VSG---------FKVWPAEVEAKLYKHPai*eVCVISVP---DERvgeevkafIVLRPEYRGKVTEEDIIEWAREQMAAY 405
|
570 580
....*....|....*....|....*..
gi 808354811 956 DTIHQVGIyccalvpANHLPKTPLGGV 982
Cdd:cd05935 406 KYPREVEF-------VDELPRSASGKI 425
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1055-1612 |
1.62e-07 |
|
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: 56.14 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1055 LECLRSRAQSSPDHRILTLVtSKNAEQDTATCSTLLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGL 1134
Cdd:cd05906 12 LLELLLRAAERGPTKGITYI-DADGSEEFQSYQDLLEDARRLAAGLR-QLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1135 VPVCIKPPVASDL----NTTLGPIRMMVDmsKAVAILAPQNVSKLLKSKEAAHsidsnaWPMI--LDLEDAPSSWRRKNN 1208
Cdd:cd05906 90 VPAPLTVPPTYDEpnarLRKLRHIWQLLG--SPVVLTDAELVAEFAGLETLSG------LPGIrvLSIEELLDTAADHDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1209 NNCDTT-------TSGSSGAAskeeicyldfsinssgqlQGSSMSEASAITVCKSIKVSSELYPSR---------HVVvc 1272
Cdd:cd05906 162 PQSRPDdlallmlTSGSTGFP------------------KAVPLTHRNILARSAGKIQHNGLTPQDvflnwvpldHVG-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1273 appysgiSLVLWCLSSVYSGHHTTLIPPMEVEQQPSLFLTTLSNLKVRDAFTTystiNTCVTQLATSVENLRERGCNLSM 1352
Cdd:cd05906 222 -------GLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAP----NFAFALLNDLLEEIEDGTWDLSS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1353 LRSCVAIAEerPRIALMS-SFCKLFAPLALNNRAISTSFssrvnaaicmqGASgpEPSTVYVDARALRNDRIslvgkgaP 1431
Cdd:cd05906 291 LRYLVNAGE--AVVAKTIrRLLRLLEPYGLPPDAIRPAF-----------GMT--ETCSGVIYSRSFPTYDH-------S 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1432 HSVALIESGKLLPGVKIAIANPEtrGQCAD-SHLGEIWVasihnasplnRLASVTgfgdEGTMNTDVYNARLTTGDTktr 1510
Cdd:cd05906 349 QALEFVSLGRPIPGVSMRIVDDE--GQLLPeGEVGRLQV----------RGPVVT----KGYYNNPEANAEAFTEDG--- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1511 WARTGYLGFLRqtqsiteHGELHdavfVVGALNESLVLRGMRYHPFDVESTVSKA----HRFVGNSAVFTWN----HLVV 1582
Cdd:cd05906 410 WFRTGDLGFLD-------NGNLT----ITGRTKDTIIVNGVNYYSHEIEAAVEEVpgvePSFTAAFAVRDPGaeteELAI 478
|
570 580 590
....*....|....*....|....*....|....*
gi 808354811 1583 IAAECTGSESDALDLVPAITSAVLEE-----HHLI 1612
Cdd:cd05906 479 FFVPEYDLQDALSETLRAIRSVVSREvgvspAYLI 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
415-881 |
1.62e-07 |
|
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: 55.69 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 415 LTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREagi 494
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGV------------AKGDRVAVLSKNS--PEFLELLFAAARLGAVFVPLNFRLTPPE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 495 aqLGFLLGNCGVKValtsescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtappr 574
Cdd:cd17631 84 --VAYILADSGAKV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 575 LADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPys 654
Cdd:cd17631 96 LFDD-LALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILR-- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 655 lmKMNPATWMHMVSKYQATTA-LVKSrdLHWALLATRDHKDISLASLRTLLVADGANPWSL-SSCDAFAAAFtpspyslr 732
Cdd:cd17631 173 --KFDPETVLDLIERHRVTSFfLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMPERLlRALQARGVKF-------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 733 pdamCPCAGSSETG-TISIRRRGNAQ--LGSqSGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvvtaIDG 809
Cdd:cd17631 241 ----VQGYGMTETSpGVTFLSPEDHRrkLGS-AGR------PVFFVEVRI---------------------------VDP 282
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354811 810 SNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKvepvgeYGkligavrYVRSGLIGFMGPDGMVFVVAR 881
Cdd:cd17631 283 DGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR------DG-------WFHTGDLGRLDEDGYLYIVDR 341
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1089-1220 |
2.08e-07 |
|
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: 55.35 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1089 LLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP--PVASdlnttlgpIRMMVDMSKAVAI 1166
Cdd:TIGR01733 5 LDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPayPAER--------LAFILEDAGARLL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808354811 1167 LA-PQNVSKLLKSKEAAHSIDSNAWPMI--LDLEDAPSSWRRKNNNNCDTTTSGSSG 1220
Cdd:TIGR01733 77 LTdSALASRLAGLVLPVILLDPLELAALddAPAPPPPDAPSGPDDLAYVIYTSGSTG 133
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
414-625 |
2.84e-07 |
|
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: 54.99 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmPSSKREag 493
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV------------GPGDRVAVYLPRSARL--VAAMLAVLKAGAAYVPLD-PDYPAD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 494 iaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsgsnsltgtsseiVDFRGWPRLWWAVTEhmsKPSRDWTAPp 573
Cdd:cd12116 75 --RLRYILEDAEPALVLTDDALPDRLP-------------------------AGLPVLLLALAAAAA---APAAPRTPV- 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 808354811 574 rlADETIAYIEYTTGNDGTVKGCCVTRQAV--FAHCRALTTAMeyKEDETMVCV 625
Cdd:cd12116 124 --SPDDLAYVIYTSGSTGRPKGVVVSHRNLvnFLHSMRERLGL--GPGDRLLAV 173
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
402-667 |
3.20e-07 |
|
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: 55.01 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 402 AMVLDQSAKpstQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPV 481
Cdd:cd05926 5 ALVVPGSTP---ALTYADLAELVDDLARQLAALGI------------KKGDRVAIALPNG--LEFVVAFLAAARAGAVVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 482 PVEmPSSKREagiaQLGFLLGNCGVKVALTSE----SCYKGLPKKVNTSSTFSAPSGSNSLTGTSSEIVDfrgwprlwwa 557
Cdd:cd05926 68 PLN-PAYKKA----EFEFYLADLGSKLVLTPKgelgPASRAASKLGLAILELALDVGVLIRAPSAESLSN---------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 558 vteHMSKPSRDWTAPPRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHA 637
Cdd:cd05926 133 ---LLADKKNAKSEGVPLPDD-LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVAS 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 808354811 638 ILASIFNGMKVIFVP-------YSLMKMNPATWMHMV 667
Cdd:cd05926 209 LLSTLAAGGSVVLPPrfsastfWPDVRDYNATWYTAV 245
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
402-665 |
4.27e-07 |
|
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: 54.22 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 402 AMVLDQSakpstQLTYGKLHSRAGKVAYMLLTKTvqvnKDGsknvmckPGDRVALIYPNTQplHFLAAFYGCLQAGVIPV 481
Cdd:cd05941 4 AIVDDGD-----SITYADLVARAARLANRLLALG----KDL-------RGDRVAFLAPPSA--EYVVAQLAIWRAGGVAV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 482 PVEmpsskREAGIAQLGFLLGNcgvkvaltsescykglpkkvntsstfSAPSgsnsltgtssEIVDfrgwprlwwavteh 561
Cdd:cd05941 66 PLN-----PSYPLAELEYVITD--------------------------SEPS----------LVLD-------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 562 mskpsrdwtapprladetIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILAS 641
Cdd:cd05941 91 ------------------PALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCP 152
|
250 260
....*....|....*....|....
gi 808354811 642 IFNGMKVIFVPyslmKMNPATWMH 665
Cdd:cd05941 153 LFAGASVEFLP----KFDPKEVAI 172
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
413-701 |
5.72e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 54.20 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLltktvqVNKDGsknvmCKPGDRVALIYPNTqPlHFLAAFYGCLQAGVIPVPVEmPSSKREa 492
Cdd:PRK08314 34 RAISYRELLEEAERLAGYL------QQECG-----VRKGDRVLLYMQNS-P-QFVIAYYAILRANAVVVPVN-PMNREE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 493 giaQLGFLLGNCGVKVALTSESCYKGLPKKVNT-----------SSTFSAPSGSN--SLTGTSSEIVDFRGWPRLWWavT 559
Cdd:PRK08314 99 ---ELAHYVTDSGARVAIVGSELAPKVAPAVGNlrlrhvivaqySDYLPAEPEIAvpAWLRAEPPLQALAPGGVVAW--K 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 560 EHMSKPSRdwtAPPRLAD-ETIAYIEYTTGNDGTVKGCCVTRQAVFAHcrALTTAMEYK--EDETMVCVVDFKREVGLWH 636
Cdd:PRK08314 174 EALAAGLA---PPPHTAGpDDLAVLPYTSGTTGVPKGCMHTHRTVMAN--AVGSVLWSNstPESVVLAVLPLFHVTGMVH 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808354811 637 AILASIFNGMKVIFVPyslmKMNPATWMHMVSKYQATtalvksrdlHWA--------LLATRDHKDISLASLR 701
Cdd:PRK08314 249 SMNAPIYAGATVVLMP----RWDREAAARLIERYRVT---------HWTniptmvvdFLASPGLAERDLSSLR 308
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
413-706 |
6.35e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 54.28 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLHflAAFYGCLQAGVIPVPVEmPSSKRea 492
Cdd:PRK06178 57 HVITYAELDELSDRFAALLRQRGV------------GAGDRVAVFLPNCPQFH--IVFFGILKLGAVHVPVS-PLFRE-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 493 giAQLGFLLGNCGVKVALTSESCYKgLPKKV--NTS-STFSAPSGSNSLTGTSSEIVDF--RGWPRLWWAVTEHMSKPsR 567
Cdd:PRK06178 120 --HELSYELNDAGAEVLLALDQLAP-VVEQVraETSlRHVIVTSLADVLPAEPTLPLPDslRAPRLAAAGAIDLLPAL-R 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 568 DWTAPPRLAD---ETIAYIEYTTGNDGTVKGCCVT-RQAVFAHCRALTTAMEYKEDETMvcvVDFKREvgLWHA-----I 638
Cdd:PRK06178 196 ACTAPVPLPPpalDALAALNYTGGTTGMPKGCEHTqRDMVYTAAAAYAVAVVGGEDSVF---LSFLPE--FWIAgenfgL 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 639 LASIFNGMKVIFvpysLMKMNPATWMHMVSKYQATTA--LVKSRDlhwALLATRDHKDISLASLRTLLVA 706
Cdd:PRK06178 271 LFPLFSGATLVL----LARWDAVAFMAAVERYRVTRTvmLVDNAV---ELMDHPRFAEYDLSSLRQVRVV 333
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
413-706 |
8.52e-07 |
|
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: 54.09 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPV--EMPSskr 490
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVG------------PGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPA--- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 491 eagiAQLGFLLGNCGVKVALTSESCYKGLPKkvntsstfsapsgsnsltgtsseivdfRGWPRLWWAVTEHMSKPSRDwt 570
Cdd:COG1020 563 ----ERLAYMLEDAGARLVLTQSALAARLPE---------------------------LGVPVLALDALALAAEPATN-- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 571 APPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCV--VDFkrEVGLWhAILASIFNGMKV 648
Cdd:COG1020 610 PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW-EIFGALLSGATL 686
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 808354811 649 IFVPYSLMKmNPATWMHMVSKYQATTA-LVKSrdlHWALLAtrDHKDISLASLRTLLVA 706
Cdd:COG1020 687 VLAPPEARR-DPAALAELLARHRVTVLnLTPS---LLRALL--DAAPEALPSLRLVLVG 739
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
449-624 |
1.11e-06 |
|
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: 52.98 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 449 KPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKREagiaQLGFLLGNCGVKVALTSEScykglpkkvntsst 528
Cdd:cd05907 28 EPGDRVAILSRNR--PEWTIADLAILAIGAVPVPI-YPTSSAE----QIAYILNDSEAKALFVEDP-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 529 fsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtapprladETIAYIEYTTGNDGTVKGCCVTRQAVFAHCR 608
Cdd:cd05907 87 -------------------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNAL 117
|
170
....*....|....*.
gi 808354811 609 ALTTAMEYKEDETMVC 624
Cdd:cd05907 118 ALAERLPATEGDRHLS 133
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
411-894 |
1.28e-06 |
|
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: 53.14 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 411 PSTQLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKr 490
Cdd:cd05959 26 DAGSLTYAELEAEARRVAGALRALGVK------------REERVLLIMLDT--VDFPTAFLGAIRAGIVPVPVNTLLTP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 491 eagiAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSST------FSAPSGSNSLTGTSSEIvdfrgwprlwWAVTEHMSK 564
Cdd:cd05959 91 ----DDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHtlvvliVSGGAGPEAGALLLAEL----------VAAEAEQLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 565 PSRDWtapprlADEtIAYIEYTTGNDGTVKGccvtrqAVFAHCRALTTAMEY-------KEDETMVCVVDFKREVGLWHA 637
Cdd:cd05959 157 PAATH------ADD-PAFWLYSSGSTGRPKG------VVHLHADIYWTAELYarnvlgiREDDVCFSAAKLFFAYGLGNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 638 ILASIFNGMKVIFVPyslMKMNPATWMHMVSKYQATTaLVKSRDLHWALLATRDHKDISLASLRTLLVADGANPWSLSsc 717
Cdd:cd05959 224 LTFPLSVGATTVLMP---ERPTPAAVFKRIRRYRPTV-FFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVG-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 718 DAFAAAFTPSpyslrpdaMCPCAGSSETGTISIRRR-GNAQLGSqSGRGILSMSalshcVVRVDtensltsltlqDAGQI 796
Cdd:cd05959 298 ERWKARFGLD--------ILDGIGSTEMLHIFLSNRpGRVRYGT-TGKPVPGYE-----VELRD-----------EDGGD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 797 VAgavvvvtaidgsnrlcqADEIGEICVSANSTAQLYWALDGQTHHTFKvepvGEYGKliGAVRYVRSgligfmgPDGMV 876
Cdd:cd05959 353 VA-----------------DGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GEWTR--TGDKYVRD-------DDGFY 402
|
490
....*....|....*...
gi 808354811 877 FVVARRQSLLAVSGRYHS 894
Cdd:cd05959 403 TYAGRADDMLKVSGIWVS 420
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1089-1181 |
3.08e-06 |
|
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: 51.79 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1089 LLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikppvasDLNTTLGP--IRMMVDMSKAVAI 1166
Cdd:cd05936 30 LDALAEAFAAGLQ-NLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVV--------PLNPLYTPreLEHILNDSGAKAL 100
|
90
....*....|....*
gi 808354811 1167 LAPQNVSKLLKSKEA 1181
Cdd:cd05936 101 IVAVSFTDLLAAGAP 115
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
413-682 |
3.73e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 51.54 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAymlltktvqvnkDGSKNVMCKPGDRVALIYPNTqPLHfLAAFYGCLQAGVIPV---PVEMPssk 489
Cdd:PRK05605 56 ATTTYAELGKQVRRAA------------AGLRALGVRPGDRVAIVLPNC-PQH-IVAFYAVLRLGAVVVehnPLYTA--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 490 reagiAQLGFLLGNCGVKVAL---TSESCYKGLPKK--------VNTSSTFSAP-------------SGSNSLTGTSSEI 545
Cdd:PRK05605 119 -----HELEHPFEDHGARVAIvwdKVAPTVERLRRTtpletivsVNMIAAMPLLqrlalrlpipalrKARAALTGPAPGT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 546 VDfrgwprlWWAVTEHMSKPSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHC---RALTTAMEyKEDETM 622
Cdd:PRK05605 194 VP-------WETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAaqgKAWVPGLG-DGPERV 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811 623 VCVVDFKREVGLWHAILASIFNGMKVIFVP-------YSLMKMNPATWMHMVSK-YQATTALVKSRDL 682
Cdd:PRK05605 266 LAALPMFHAYGLTLCLTLAVSIGGELVLLPapdidliLDAMKKHPPTWLPGVPPlYEKIAEAAEERGV 333
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1058-1141 |
2.42e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 49.13 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1058 LRSRAQSSPDHRILT----LVTSKNAEQDTATCSTLLKRAERIAGLLTDrARLSRGDHVALIFPPSIDLVAAFFGCLSAG 1133
Cdd:PRK09274 12 LPRAAQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNA-AGIGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
....*...
gi 808354811 1134 LVPVCIKP 1141
Cdd:PRK09274 91 AVPVLVDP 98
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1081-1597 |
3.95e-05 |
|
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: 48.13 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1081 QDTATCSTLLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIkppvasdlNTTLGP--IRMMV 1158
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALR-ALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV--------NTLLTPddYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1159 DMSKAVAILAPQNVSKLLksKEAAHSIDSNAWPMIL---DLEDAPSSWRRknNNNCDTTTSGSSGAASKEEICYLDFSIN 1235
Cdd:cd05959 98 EDSRARVVVVSGELAPVL--AAALTKSEHTLVVLIVsggAGPEAGALLLA--ELVAAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1236 SSGQLQGssmseasAITVCKSIKVSSELYPSR-------HVVVCAP----PYsGISLVLWCLSSVysGHHTTLIP----P 1300
Cdd:cd05959 174 STGRPKG-------VVHLHADIYWTAELYARNvlgiredDVCFSAAklffAY-GLGNSLTFPLSV--GATTVLMPerptP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1301 MEV-----EQQPSLFLTtlsnlkvrdAFTTYSTIntcvtqlaTSVENLRERgcNLSMLRSCVAIAEERPrialmssfckl 1375
Cdd:cd05959 244 AAVfkrirRYRPTVFFG---------VPTLYAAM--------LAAPNLPSR--DLSSLRLCVSAGEALP----------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1376 faplalnnRAISTSFSSRVNAAIcMQGASGPEPSTVYVDARalrndrislvgkgaPHSVALIESGKLLPGVKIAIANpET 1455
Cdd:cd05959 294 --------AEVGERWKARFGLDI-LDGIGSTEMLHIFLSNR--------------PGRVRYGTTGKPVPGYEVELRD-ED 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1456 RGQCADSHLGEIWVASihnasplnrlasvtgfgdeGTMNTDVYNARLTTGDT-KTRWARTGYlGFLRQtqsitEHGELhd 1534
Cdd:cd05959 350 GGDVADGEPGELYVRG-------------------PSSATMYWNNRDKTRDTfQGEWTRTGD-KYVRD-----DDGFY-- 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354811 1535 avFVVGALNESLVLRGMRYHPFDVESTVsKAHRFVGNSAVFTWNH---------LVVIAAECTGSESDALDL 1597
Cdd:cd05959 403 --TYAGRADDMLKVSGIWVSPFEVESAL-VQHPAVLEAAVVGVEDedgltkpkaFVVLRPGYEDSEALEEEL 471
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
413-714 |
4.75e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.41 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmPSSKREa 492
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGV------------GPDVLVGVAMERSIEM--VVALLAILKAGGAYVPLD-PEYPAE- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 493 giaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstFSApsgsnsltGTSSEIVDfrgWPRLWWavtehmskpSRDWTAP 572
Cdd:PRK12316 599 ---RLAYMLEDSGVQLLLSQSHLGRKLP--------LAA--------GVQVLDLD---RPAAWL---------EGYSEEN 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 573 P--RLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILAsIFNGMKVIF 650
Cdd:PRK12316 648 PgtELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVV 726
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808354811 651 VPYSLMKmNPATWMHMVSKYQATT-ALVKSrdLHWALLatRDHKDISLASLRTLLVADGANPWSL 714
Cdd:PRK12316 727 AAPGDHR-DPAKLVELINREGVDTlHFVPS--MLQAFL--QDEDVASCTSLRRIVCSGEALPADA 786
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
413-904 |
5.84e-05 |
|
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: 47.67 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEmPSSKREA 492
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGI------------RPGDRVALMLDNC--PEFLFAWFALAKLGAVLVPIN-TALRGDE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 493 giaqLGFLLGNCGVKVALTSescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtap 572
Cdd:cd05934 67 ----LAYIIDHSGAQLVVVD------------------------------------------------------------ 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 573 prladetIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVP 652
Cdd:cd05934 83 -------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 653 yslmKMNPATWMHMVSKYQAT--TALVKSRDlhwALLAT------RDHKdislasLRTLLVAdgANPWSLSscDAFAAAF 724
Cdd:cd05934 156 ----RFSASRFWSDVRRYGATvtNYLGAMLS---YLLAQppspddRAHR------LRAAYGA--PNPPELH--EEFEERF 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 725 TpspyslrpdamCPCA---GSSETGTISIRRRGNAQLGSQSGRGIlsmsalSHCVVRVdtensltsltlqdagqivagav 801
Cdd:cd05934 219 G-----------VRLLegyGMTETIVGVIGPRDEPRRPGSIGRPA------PGYEVRI---------------------- 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 802 vvvtaIDGSNRLCQADEIGEICVSAN---STAQLYWaldGQTHHTFKVEPVGEYgkligavryvRSGLIGFMGPDGMVFV 878
Cdd:cd05934 260 -----VDDDGQELPAGEPGELVIRGLrgwGFFKGYY---NMPEATAEAMRNGWF----------HTGDLGYRDADGFFYF 321
|
490 500
....*....|....*....|....*.
gi 808354811 879 VARRQSLLAVSGRYHSADDIIATVLA 904
Cdd:cd05934 322 VDRKKDMIRRRGENISSAEVERAILR 347
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
414-603 |
6.19e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.24 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVAlIYPNTQPlHFLAAFYGCLQAGVIPVPVEmpsskREAG 493
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYLRDKGV------------GPDVCVA-IAAERSP-QLLVGLLAILKAGGAYVPLD-----PDYP 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 494 IAQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsGSNSLTGTSSEIVDFRGWPrlwwavtehmskpsrdwTAPP 573
Cdd:PRK05691 1217 AERLAYMLADSGVELLLTQSHLLERLP-------------QAEGVSAIALDSLHLDSWP-----------------SQAP 1266
|
170 180 190
....*....|....*....|....*....|..
gi 808354811 574 RLA--DETIAYIEYTTGNDGTVKGCCVTRQAV 603
Cdd:PRK05691 1267 GLHlhGDNLAYVIYTSGSTGQPKGVGNTHAAL 1298
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1052-1137 |
7.35e-05 |
|
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: 47.45 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1052 LPLLECLRSRAQSSPDHRILTlvtsknAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLS 1131
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFR 97
|
....*.
gi 808354811 1132 AGLVPV 1137
Cdd:COG1021 98 AGAIPV 103
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
414-481 |
1.17e-04 |
|
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: 46.68 E-value: 1.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811 414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPV 481
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGL------------RPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
414-746 |
1.47e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 46.42 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREag 493
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGL------------GPGDHVGIYARNR--IEYVEAMLGAFKARAVPVNVNYRYVEDE-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 494 iaqLGFLLGNCGVkVALTSESCYKG-----LPK--KVNTSSTFSAPSGSNSLTGTsseiVDFRGwprlwwAVTEhmSKPS 566
Cdd:PRK07798 92 ---LRYLLDDSDA-VALVYEREFAPrvaevLPRlpKLRTLVVVEDGSGNDLLPGA----VDYED------ALAA--GSPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 567 RDwtAPPRLADETiaYIEYTTGNDGTVKGccV------TRQAVFAHCRALTTamEYKEDE-------------TMVCVVD 627
Cdd:PRK07798 156 RD--FGERSPDDL--YLLYTGGTTGMPKG--VmwrqedIFRVLLGGRDFATG--EPIEDEeelakraaagpgmRRFPAPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 628 FKREVGLWhAILASIFNGMKVIFvpYSLMKMNPATWMHMVSKYQATTALVK----SRDLHWALLATRDHkDISlaSLRTl 703
Cdd:PRK07798 228 LMHGAGQW-AAFAALFSGQTVVL--LPDVRFDADEVWRTIEREKVNVITIVgdamARPLLDALEARGPY-DLS--SLFA- 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 808354811 704 lVADGANPWSLSSCDAFAAAFtpspyslrPDAMCPCA-GSSETG 746
Cdd:PRK07798 301 -IASGGALFSPSVKEALLELL--------PNVVLTDSiGSSETG 335
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
379-620 |
1.82e-04 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 46.29 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 379 MPRSLDSFSAfhrfgttAAKNIAAMVLDQSA----KP-----STQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcK 449
Cdd:PRK06155 9 AARAVDPLPP-------SERTLPAMLARQAErypdRPllvfgGTRWTYAEAARAAAAAAHALAAAGV------------K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 450 PGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKreagiAQLGFLLGNCGVKVaLTSEScykGLPKKVNTsstf 529
Cdd:PRK06155 70 RGDRVALMCGNR--IEFLDVFLGCAWLGAIAVPINTALRG-----PQLEHILRNSGARL-LVVEA---ALLAALEA---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 530 sAPSGSNSLTGTSseIVD---FRGWPRLWWAVtehmSKPSRDWTAPP---RLADetIAYIEYTTGNDGTVKGCCVTRQAV 603
Cdd:PRK06155 135 -ADPGDLPLPAVW--LLDapaSVSVPAGWSTA----PLPPLDAPAPAaavQPGD--TAAILYTSGTTGPSKGVCCPHAQF 205
|
250
....*....|....*..
gi 808354811 604 FAHCRALTTAMEYKEDE 620
Cdd:PRK06155 206 YWWGRNSAEDLEIGADD 222
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1089-1146 |
2.47e-04 |
|
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: 45.55 E-value: 2.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811 1089 LLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKPPVASD 1146
Cdd:cd05935 7 LLEVVKKLASFLSNKG-VRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKER 63
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
582-706 |
2.82e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 45.71 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 582 YIEYTTGNDGTVKGccVTRQaVFAHCRALTTAMEY----KEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMK 657
Cdd:PRK10524 237 YILYTSGTTGKPKG--VQRD-TGGYAVALATSMDTifggKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTR 313
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808354811 658 MNPATWMHMVSKYQ------ATTAL--VKSRDLhwALLATRDhkdisLASLRTLLVA 706
Cdd:PRK10524 314 PDAGIWWRIVEKYKvnrmfsAPTAIrvLKKQDP--ALLRKHD-----LSSLRALFLA 363
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
449-652 |
2.97e-04 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 45.48 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 449 KPGDRVALIYPNTqPLHFLAAFyGCLQAGVIPVPVEmPSSKREagiaQLGFLLGNCGVKVALTSEscyKGLPKKVNtsst 528
Cdd:COG1022 63 KPGDRVAILSDNR-PEWVIADL-AILAAGAVTVPIY-PTSSAE----EVAYILNDSGAKVLFVED---QEQLDKLL---- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 529 fSAPSGSNSLTgtssEIV--DFRGWPRLWWAVT-EHMSKPSRDWTAPPRLAD-------ETIAYIEYTTGNDGTVKGCCV 598
Cdd:COG1022 129 -EVRDELPSLR----HIVvlDPRGLRDDPRLLSlDELLALGREVADPAELEArraavkpDDLATIIYTSGTTGRPKGVML 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 808354811 599 TRQAVFAHCRALTTAMEYKEDETMVCVVDfkrevgLWH-----AILASIFNGMKVIFVP 652
Cdd:COG1022 204 THRNLLSNARALLERLPLGPGDRTLSFLP------LAHvfertVSYYALAAGATVAFAE 256
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1224-1562 |
3.14e-04 |
|
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: 45.17 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1224 KEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEV 1303
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1304 EQQPSLFLTTLSNLKVRDAFTTYSTINTCVTQLATSVENlrerGCNLSMLRSCVAIAEErprIA--LMSSFCKLFAPLAL 1381
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKAN----DWDLSSIRMILNGAEP---IDyeLCHEFLDHMSKYGL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1382 NNRAISTSFS-SRVNAAICMQGASGPEpSTVYVDARALR-NDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGqC 1459
Cdd:cd05908 258 KRNAILPVYGlAEASVGASLPKAQSPF-KTITLGRRHVThGEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-L 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1460 ADSHLGEIWVasihnasplnRLASVTgfgdEGTMNTDVYNARLTTGDTktrWARTGYLGFLRQtqsitehGELhdavFVV 1539
Cdd:cd05908 336 PDGYIGHIQI----------RGKNVT----PGYYNNPEATAKVFTDDG---WLKTGDLGFIRN-------GRL----VIT 387
|
330 340
....*....|....*....|...
gi 808354811 1540 GALNESLVLRGMRYHPFDVESTV 1562
Cdd:cd05908 388 GREKDIIFVNGQNVYPHDIERIA 410
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1089-1141 |
4.43e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 44.95 E-value: 4.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 808354811 1089 LLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP 1141
Cdd:PRK08314 41 LLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
413-595 |
1.26e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 43.35 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLltktvqvnkdgsKNVMCKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVempsSKREA 492
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGL------------RALGLREGDVVAILLENN--PEFFEVYWAARRSGLYYTPI----NWHLT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 493 GiAQLGFLLGNCGVKVALTSESC---YKGLPKkvntsstfSAPSGSNSLTGTSSEIVDFRGWPRLwwavtehmskpsRDW 569
Cdd:PRK08276 72 A-AEIAYIVDDSGAKVLIVSAALadtAAELAA--------ELPAGVPLLLVVAGPVPGFRSYEEA------------LAA 130
|
170 180
....*....|....*....|....*..
gi 808354811 570 TAPPRLADETIAY-IEYTTGNDGTVKG 595
Cdd:PRK08276 131 QPDTPIADETAGAdMLYSSGTTGRPKG 157
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1089-1168 |
1.54e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 42.97 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1089 LLKRAERIAGLLtdRAR-LSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIkppvasdlNTTLGP--IRMMVDMSKAVA 1165
Cdd:PRK08276 17 LEARSNRLAHGL--RALgLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI--------NWHLTAaeIAYIVDDSGAKV 86
|
...
gi 808354811 1166 ILA 1168
Cdd:PRK08276 87 LIV 89
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
414-890 |
1.80e-03 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 43.09 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 414 QLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREag 493
Cdd:PRK07059 48 AITYGELDELSRALAAWLQSRGLA------------KGARVAIMMPNV--LQYPVAIAAVLRAGYVVVNVNPLYTPRE-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 494 iaqLGFLLGNCGVKVALTSESCYKGLPKKVNTSSTFSAPSGS-NSLTGTSSEIVDF--RGWPRL--WWAVTEH------M 562
Cdd:PRK07059 112 ---LEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASmGDLLGFKGHIVNFvvRRVKKMvpAWSLPGHvrfndaL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 563 SKPSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAME-----YKEDETMVCVVdfkrEVGLWH- 636
Cdd:PRK07059 189 AEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpafekKPRPDQLNFVC----ALPLYHi 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 637 -AILASIFNGMKV----IFVPyslmkmNPATWMHMV---SKYQATT--ALvksRDLHWALLATRDHKDISLASLRtllVA 706
Cdd:PRK07059 265 fALTVCGLLGMRTggrnILIP------NPRDIPGFIkelKKYQVHIfpAV---NTLYNALLNNPDFDKLDFSKLI---VA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 707 DG---------ANPWSLSSCDAFAAAFTPSPYSlrPDAMCPCAGSSE-TGTISirrrgnaqlgsqsgrgiLSMSAlSHCV 776
Cdd:PRK07059 333 NGggmavqrpvAERWLEMTGCPITEGYGLSETS--PVATCNPVDATEfSGTIG-----------------LPLPS-TEVS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 777 VRVDTENSLTsltlqdagqivagavvvvtaidgsnrlcqADEIGEICVSANSTAQLYWALDGQThhtfkvepvgeyGKLI 856
Cdd:PRK07059 393 IRDDDGNDLP-----------------------------LGEPGEICIRGPQVMAGYWNRPDET------------AKVM 431
|
490 500 510
....*....|....*....|....*....|....
gi 808354811 857 GAVRYVRSGLIGFMGPDGMVFVVARRQSLLAVSG 890
Cdd:PRK07059 432 TADGFFRTGDVGVMDERGYTKIVDRKKDMILVSG 465
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1093-1204 |
1.83e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 43.00 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1093 AERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikpPVasdlNTTLGP--IRMMVDMSKAVAILAPQ 1170
Cdd:PRK08316 46 VNRVAAALLDLG-LKKGDRVAALGHNSDAYALLWLACARAGAVHV----PV----NFMLTGeeLAYILDHSGARAFLVDP 116
|
90 100 110
....*....|....*....|....*....|....
gi 808354811 1171 NVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWR 1204
Cdd:PRK08316 117 ALAPTAEAALALLPVDTLILSLVLGGREAPGGWL 150
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1054-1146 |
1.96e-03 |
|
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: 42.88 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1054 LLECLRSRAQSSPDHRILTLVtsknAEQDTATCSTLLKRAERIAGLLtDRARLSRGDHVALIFPPSIDLVAAFFGCLSAG 1133
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADP----ARGLRLTYSELRARIEAVAARL-HARGLRPGQRVAVVLPNSVEAVIALLALHRLG 77
|
90
....*....|...
gi 808354811 1134 LVPVCIKPPVASD 1146
Cdd:cd05923 78 AVPALINPRLKAA 90
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1092-1559 |
2.79e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.45 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1092 RAERIAGLLTDRARLSRgdhVALIFPPSIDLVAAFFGCLSAGlVPVCIKPpvasdlnttlGPIRMMVDMSKAVAIL---A 1168
Cdd:PRK05851 40 RAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAG-AAVSILP----------GPVRGADDGRWADATLtrfA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1169 PQNVSKLLKSK---EAAHSIDSNAwpMILDLedapSSWRRKNnnncdttTSGSSGAASKEEICYLDFSINSSGQLQGSSM 1245
Cdd:PRK05851 106 GIGVRTVLSHGshlERLRAVDSSV--TVHDL----ATAAHTN-------RSASLTPPDSGGPAVLQGTAGSTGTPRTAIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1246 SEASAITVCKSIKVSSELYPSRHVVvCA--PPYSGISLVlWCLSSVYSGHHTTLIPPMEVEQQPSLFLTTLSnlkvrDAF 1323
Cdd:PRK05851 173 SPGAVLSNLRGLNARVGLDAATDVG-CSwlPLYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLS-----DSR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1324 TTYstinTCVTQLATSV---ENLRERGCNLSMLRscVAIAEERP-RIALMSSFCKLFAPLALNNRAISTSFSsrVNAAIC 1399
Cdd:PRK05851 246 ATL----TAAPNFAYNLigkYARRVSDVDLGALR--VALNGGEPvDCDGFERFATAMAPFGFDAGAAAPSYG--LAESTC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1400 mqGASGPEPSTvyvdarALRNDRISLVGKGAPHSVALIesGKLLPGVKIAIANPETRGQCADSHLGEIwvaSIHNASpln 1479
Cdd:PRK05851 318 --AVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEI---EIRGAS--- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1480 rlasvtgfgdegTMNTDVYNARLTTGDtktrWARTGYLGFLrqtqsitehgeLHDAVFVVGALNESLVLRGMRYHPFDVE 1559
Cdd:PRK05851 382 ------------MMSGYLGQAPIDPDD----WFPTGDLGYL-----------VDGGLVVCGRAKELITVAGRNIFPTEIE 434
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1053-1137 |
2.91e-03 |
|
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: 42.31 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1053 PLLECLRSRAQSSPDHriLTLVTSKNaeqdTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSA 1132
Cdd:cd05920 16 PLGDLLARSAARHPDR--IAVVDGDR----RLTYRELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLRL 88
|
....*
gi 808354811 1133 GLVPV 1137
Cdd:cd05920 89 GAVPV 93
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
565-745 |
3.04e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.06 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 565 PSRDWTAPPrLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEykedetmvcvVDFKREVG-----LWHA-- 637
Cdd:PRK05851 140 TNRSASLTP-PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG----------LDAATDVGcswlpLYHDmg 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 638 ---ILASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATtaLVKSRDLHWALLA--TRDHKDISLASLRTLLvaDGANPW 712
Cdd:PRK05851 209 lafLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRAT--LTAAPNFAYNLIGkyARRVSDVDLGALRVAL--NGGEPV 284
|
170 180 190
....*....|....*....|....*....|...
gi 808354811 713 SLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSET 745
Cdd:PRK05851 285 DCDGFERFATAM--APFGFDAGAAAPSYGLAES 315
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1092-1167 |
3.35e-03 |
|
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: 41.91 E-value: 3.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811 1092 RAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG--LVPVCIKPPVASdlnttlgpIRMMVDMSKAVAIL 1167
Cdd:cd17643 21 RANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGgaYVPIDPAYPVER--------IAFILADSGPSLLL 89
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
413-511 |
4.15e-03 |
|
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: 41.52 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmpsskREA 492
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGV------------GPGDRVALALPRSAEL--IVALLAILKAGGAYVPID-----PAY 71
|
90
....*....|....*....
gi 808354811 493 GIAQLGFLLGNCGVKVALT 511
Cdd:cd17643 72 PVERIAFILADSGPSLLLT 90
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1046-1139 |
5.33e-03 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 41.24 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1046 IDDEPSLPllECLRSRAQSSPDhRILtLVTSKNAEQDTATCSTLLKRAERIA-GLLtdRARLSRGDHVALIFPPSIDLVA 1124
Cdd:COG1022 7 VPPADTLP--DLLRRRAARFPD-RVA-LREKEDGIWQSLTWAEFAERVRALAaGLL--ALGVKPGDRVAILSDNRPEWVI 80
|
90
....*....|....*
gi 808354811 1125 AFFGCLSAGLVPVCI 1139
Cdd:COG1022 81 ADLAILAAGAVTVPI 95
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1085-1141 |
5.47e-03 |
|
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: 41.12 E-value: 5.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 808354811 1085 TCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP 1141
Cdd:cd05934 5 TYAELLRESARIAAALAALG-IRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT 60
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1092-1141 |
6.04e-03 |
|
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: 40.91 E-value: 6.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808354811 1092 RAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP 1141
Cdd:cd05919 19 GANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP 67
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1089-1137 |
6.97e-03 |
|
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: 41.38 E-value: 6.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 808354811 1089 LLKRAERIAGLLtdRAR-LSRGDHVALIFPPSIDLVAAFFGCLSAG--LVPV 1137
Cdd:COG1020 507 LNARANRLAHHL--RALgVGPGDLVGVCLERSLEMVVALLAVLKAGaaYVPL 556
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1089-1137 |
9.46e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 40.66 E-value: 9.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808354811 1089 LLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG--LVPV 1137
Cdd:PRK07656 36 LNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGavVVPL 85
|
|
|