|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1094-1675 |
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: 722.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1094 ILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKPPVAS-DLN 1172
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISqQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1173 TTLGPIRMmvDMSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWRRKNNNNcdtttsGSSGAASKEEIC 1252
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKW------GPHPPTRDGDTA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1253 YLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPS 1332
Cdd:cd05905 153 YIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1333 LFLTTLSNLKVRDAFTTYSTINTCVTQLATSVENLRERGCNLSMLRSCVAIAEERPRIALMSSFCKLFAPLALNNRAIST 1412
Cdd:cd05905 233 LWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVST 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1413 SFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGQCADSHLGEIW 1492
Cdd:cd05905 313 EFGTRVNPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1493 VASIHNASPLNRLASVTGFGDEGTMNTdvynaRLTTGDTKTRWARTGYLGFLRQTQSITEHGELHDAVFVVGALNESLVL 1572
Cdd:cd05905 393 VNSPANASGYFLLDGETNDTFKVFPST-----RLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1573 RGMRYHPFDVESTVSKAHRFVGNSAVFTWNHLVVIAAECT-GSESDALDLVPAITSAVLEEHHLIVGVVVVVDPGSIRHG 1651
Cdd:cd05905 468 RGLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKN 547
|
570 580
....*....|....*....|....
gi 808354807 1652 PGGEKLRSTIRSLFLEEKLNPIYV 1675
Cdd:cd05905 548 PLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
425-1025 |
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: 690.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 425 AAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKtvqvnkdgsknVMCKPGDRVALIYPNtqPLHFLAAFYGCLQAGVIP 504
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKK-----------VGLKPGDRVALMYPD--PLDFVAAFYGCLYAGVVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 505 VPVEMPSskreaGIAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSstfsapsgsnsltGTSSEIVDFRGWPRLWWAVTE 584
Cdd:cd05905 68 IPIEPPD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKLLKS-------------KTAAEIAKKKGWPKILDFVKI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 585 HMSKPS--RDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAI 662
Cdd:cd05905 130 PKSKRSklKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGC 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 663 LASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATTALVKSRDLHWAL------LATRDHKDISLASLRTLLVADGaNPW 736
Cdd:cd05905 210 LLSVYSGHHTILIPPELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 737 SLSSCDAFAAAFTPSPYSLRpdamcpcAGSSETGTISIRRRG-NAQLGSQSGRGILSMSALSHCVVRVDTENSLTSLTLQ 815
Cdd:cd05905 289 RISSCDSFLKLFQTLGLSPR-------AVSTEFGTRVNPFICwQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 816 DAGQIVAGAVVVVTAIDGSNrLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKLIGAVRYVRSGLIGFMG 895
Cdd:cd05905 362 DSGKVLPGAQVAIVNPETKG-LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 896 P----------DGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPmkfvYRGRICVFSTSvlrdERIVIVAEQKPnCSE 965
Cdd:cd05905 441 PtkctdlnveeHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSE 511
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 966 EEAFDWITRVLRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFENGDLHPSTL 1025
Cdd:cd05905 512 EEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
425-1017 |
3.73e-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: 234.83 E-value: 3.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 425 AAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKTvqvnkdgsknvmcKPGDRVALIYPntQPLHFLAAFYGCLQAGVIP 504
Cdd:cd05931 11 AYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-------------KPGDRVLLLAP--PGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 505 VPVEMPSSKREAgiAQLGFLLGNCGVKVALTSEScykglpkkvntsstfsapsgsnSLTGTSSEIVDFRGWPRLWWAVTE 584
Cdd:cd05931 76 VPLPPPTPGRHA--ERLAAILADAGPRVVLTTAA----------------------ALAAVRAFAASRPAAGTPRLLVVD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 585 HM-SKPSRDWTaPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAIL 663
Cdd:cd05931 132 LLpDTSAADWP-PPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 664 ASIFNGMKVIFV-PYSLMKmNPATWMHMVSKYQATTALVKSRDLHWALLATRDHK--DISLASLRTLLVadGANPWSLSS 740
Cdd:cd05931 211 TPLYSGGPSVLMsPAAFLR-RPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDleGLDLSSWRVALN--GAEPVRPAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 741 CDAFAAAFtpSPYSLRPDAMCPCAGSSE-TGTISIRRRGNAQLGSQSGRGILSMSALshcVVRVDTENS--LTSLTLQDA 817
Cdd:cd05931 288 LRRFAEAF--APFGFRPEAFRPSYGLAEaTLFVSGGPPGTGPVVLRVDRDALAGRAV---AVAADDPAAreLVSCGRPLP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 818 GQivagavvvVTAI--DGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGeygkliGAVRYVRSGLIGFMG 895
Cdd:cd05931 363 DQ--------EVRIvdPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAT------DEGGWLRTGDLGFLH 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 896 pDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPMkfVYRGRICVFSTSVLRDERIVIVAEQKPNCSEEEAFDWITRV 975
Cdd:cd05931 429 -DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAI 505
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 808354807 976 LRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFEN 1017
Cdd:cd05931 506 RAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1085-1666 |
3.77e-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: 190.53 E-value: 3.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1085 RAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLtdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIK 1164
Cdd:cd05931 2 RAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1165 PPVAsdlNTTLGPIRMMVDMSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDL--EDAPSSWRRKnnnncdtttsgs 1242
Cdd:cd05931 80 PPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLlpDTSAADWPPP------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1243 sgAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLI 1322
Cdd:cd05931 145 --SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1323 PPMEVEQQPSLFLTTLSnlKVRDAFT-----TYstiNTCVTqlATSVENLRerGCNLSMLRSCVAIAEeRPRIALMSSFC 1397
Cdd:cd05931 223 SPAAFLRRPLRWLRLIS--RYRATISaapnfAY---DLCVR--RVRDEDLE--GLDLSSWRVALNGAE-PVRPATLRRFA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1398 KLFAPLALNNRAI--------STSFSSRvnaaicmqGASGPEPSTVYVDARALRNdRISLVGKGAPHSVALIESGKLLPG 1469
Cdd:cd05931 293 EAFAPFGFRPEAFrpsyglaeATLFVSG--------GPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1470 VKIAIANPETRGQCADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTMNTdvYNARLTTGDtkTRWARTGYLGFLRQtq 1548
Cdd:cd05931 364 QEVRIVDPETGRELPDGEVGEIWVRGPSVASGyWGR--------PEATAET--FGALAATDE--GGWLRTGDLGFLHD-- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1549 sitehGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFTWN-----HLVVIAAECTGSESDALD- 1620
Cdd:cd05931 430 -----GEL----YITGRLKDLIIVRGRNHYPQDIEATAEEAHPALrpGCVAAFSVPddgeeRLVVVAEVERGADPADLAa 500
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 808354807 1621 LVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGeKL-RSTIRSLFL 1666
Cdd:cd05931 501 IAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSG-KIqRRACRAAYL 546
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
437-1004 |
7.40e-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: 7.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 437 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREa 516
Cdd:COG0318 23 RRLTYAELDARARRLAAALRALGV------------GPGDRVALLLPNS--PEFVVAFLAALRAGAVVVPLNPRLTAEE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 517 giaqLGFLLGNCGVKVALTsescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtap 596
Cdd:COG0318 88 ----LAYILEDSGARALVT------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 597 prladetiAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVV----DFkrevGLWHAILASIFNGMKV 672
Cdd:COG0318 103 --------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALplfhVF----GLTVGLLAPLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 673 IFVPyslmKMNPATWMHMVSKYQAT-TALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFTPs 751
Cdd:COG0318 171 VLLP----RFDPERVLELIERERVTvLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 752 pyslrpdAMCPCAGSSETG---TISIRRRGNAQLGSQsGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvv 828
Cdd:COG0318 242 -------RIVEGYGLTETSpvvTVNPEDPGERRPGSV-GR------PLPGVEVRI------------------------- 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 829 taIDGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFkvepvgeygkligAVRYVRSGLIGFMGPDGMVFVVARRQS 908
Cdd:COG0318 283 --VDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-------------RDGWLRTGDLGRLDEDGYLYIVGRKKD 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 909 LLAVSGRYHSADDIIATVLAVEPMKfvyrgRICVFS-TSVLRDERIV--IVAEQKPNCSEEEAFDWITRVLRAIDTIHQV 985
Cdd:COG0318 348 MIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGvPDEKWGERVVafVVLRPGAELDAEELRAFLRERLARYKVPRRV 422
|
570
....*....|....*....
gi 808354807 986 giyccALVPAnhLPKTPLG 1004
Cdd:COG0318 423 -----EFVDE--LPRTASG 434
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
437-906 |
2.21e-31 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 128.97 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 437 TQLTYGKLHSRAGKVAYMLLtktvqvnkdgSKNVmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKREA 516
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLR----------ALGV--GKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPL-NPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 517 giaqLGFLLGNCGVKVALTSEScyKGLPKkvntsstfSAPSGSNSLTGTSSEIVDFRGWPRLWWAvtEHMSKPSRDWTAP 596
Cdd:pfam00501 85 ----LAYILEDSGAKVLITDDA--LKLEE--------LLEALGKLEVVKLVLVLDRDPVLKEEPL--PEEAKPADVPPPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 597 PRLAD-ETIAYIEYTTGNDGTVKGCCVT----RQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMK 671
Cdd:pfam00501 149 PPPPDpDDLAYIIYTSGTTGKPKGVMLThrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 672 VIFVPYSLMKMnPATWMHMVSKYQAT-TALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFtp 750
Cdd:pfam00501 229 VVLPPGFPALD-PAALLELIERYKVTvLYGVPT--LLNMLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 751 spyslrPDAMCPCAGSSETGTISIRRRGNAQLGSQSGR-GIlsmsALSHCVVRV-Dtensltsltlqdagqivagavvvv 828
Cdd:pfam00501 302 ------GGALVNGYGLTETTGVVTTPLPLDEDLRSLGSvGR----PLPGTEVKIvD------------------------ 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354807 829 taiDGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkligavRYVRSGLIGFMGPDGMVFVVARR 906
Cdd:pfam00501 348 ---DETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------------GWYRTGDLGRRDEDGYLEIVGRK 410
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
405-1050 |
4.99e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 134.14 E-value: 4.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 405 MPRSLDSAFHRFGTTAAKNIAAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmckPGDRVALIYPN 484
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS-------------FGDRAVLLFPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 485 TQplHFLAAFYGCLQAGVIPVPVEMPSSKREAGIAQLGFLLGNCGVKVALTSESCYKGLpKKVNTSSTFSAPSgsnsltg 564
Cdd:PRK05691 74 GP--DYVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPE------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 565 tsseivdfrgwprlWWAVTEHMSKPSRDWTApPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTT--AMEYKE 642
Cdd:PRK05691 144 --------------LLCVDTLDPALAEAWQE-PALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDLNP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 643 DETMVCVVDFKREVGLWHAILASIFNGmkvifVPYSLMKMN-----PATWMHMVSKYQATTAlvKSRDLHWALLATRdhk 717
Cdd:PRK05691 209 DDVIVSWLPLYHDMGLIGGLLQPIFSG-----VPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER--- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 718 dISLASLRTL-----LVA-DGANPWSLSSCDAFAAAFTPSPYSlrPDAMCPCAGSSEtGTISIRrrgnaqlGSQSGRGI- 790
Cdd:PRK05691 279 -VSESALERLdlsrwRVAySGSEPIRQDSLERFAEKFAACGFD--PDSFFASYGLAE-ATLFVS-------GGRRGQGIp 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 791 ---LSMSALSHCVVRVDTENSLTSLTLQDAGQIVAGAVVVVTAIDGSNRlcqadeIGEICVSANSTAQLYWALDGQTHHT 867
Cdd:PRK05691 348 aleLDAEALARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVLGDNR------VGEIWASGPSIAHGYWRNPEASAKT 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 868 FkVEPVGEygkligavRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATVlaVEPMKFVYRGRICVFSTSV 947
Cdd:PRK05691 422 F-VEHDGR--------TWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTV--EREVEVVRKGRVAAFAVNH 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 948 LRDERIVIVAE-----QKPNCSEEeafdWITRVLRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFENGDLhp 1022
Cdd:PRK05691 490 QGEEGIGIAAEisrsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL-- 563
|
650 660
....*....|....*....|....*...
gi 808354807 1023 stllmcphNCVLNLPKPRERQADVGPAA 1050
Cdd:PRK05691 564 --------DSYALFPALQAVEAAQTAAS 583
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
439-1006 |
5.05e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 124.67 E-value: 5.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 439 LTYGKLHSRAGKVAYmlltktvQVNKDGSknvmckPGDRVALIYPntQPLHFLAAFYGCLQAGVIPVPVEMPssKREAGI 518
Cdd:PRK05850 36 LTWSQLYRRTLNVAE-------ELRRHGS------TGDRAVILAP--QGLEYIVAFLGALQAGLIAVPLSVP--QGGAHD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 519 AQLGFLLGNCGVKVALTSESCYKGLPKKVNTSSTFSAPSgsnsltgtsseIV-----DFrgwprlwwavtehmskPSRDW 593
Cdd:PRK05850 99 ERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPP-----------VIevdllDL----------------DSPRG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 594 TAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRAL-TTAMEYKE-----DETMVCVVDFKREVGLWHAILASIF 667
Cdd:PRK05850 152 SDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmSDYFGDTGgvpppDTTVVSWLPFYHDMGLVLGVCAPIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 668 NGMKVIFV-PYSLMkMNPATWMHMVSKYQATTalvkSRDLHWAL-LATRDHKDISLASL---RTLLVADGA---NPWSLS 739
Cdd:PRK05850 232 GGCPAVLTsPVAFL-QRPARWMQLLASNPHAF----SAAPNFAFeLAVRKTSDDDMAGLdlgGVLGIISGServHPATLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 740 S-CDAFAaaftpsPYSLRPDAMCPCAG---------SSETGTISIRRR--------GNAQL-GSQSGRGILSMSALSHCV 800
Cdd:PRK05850 307 RfADRFA------PFNLRETAIRPSYGlaeatvyvaTREPGQPPESVRfdyeklsaGHAKRcETGGGTPLVSYGSPRSPT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 801 VR-VDTEnsltsltlqdagqivagavvvvtaidgSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKvepvgeyGKL 879
Cdd:PRK05850 381 VRiVDPD---------------------------TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFG-------ATL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 880 IGAVR------YVRSGLIGFMGpDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEpmkfvyRGRICVFSTSVLRDERI 953
Cdd:PRK05850 427 VDPSPgtpegpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEATIQEIT------GGRVAAISVPDDGTEKL 499
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 808354807 954 VIVAE-QKPNCSEEEAFDWITRVLR----AIDTIHQVGIYCCALVPANHLPKTPLGGV 1006
Cdd:PRK05850 500 VAIIElKKRGDSDEEAMDRLRTVKRevtsAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1073-1662 |
2.86e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 115.27 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1073 EPSLPLLECLRSRAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARLsrGDHVALIFPPSIDLVAAFFG 1152
Cdd:PRK05691 6 ELPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1153 CLSAGLVPVCIKPPVASDLNTTLGPIRMMVDmSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPS-SWRRKn 1231
Cdd:PRK05691 84 CLYAGVIAVPAYPPESARRHHQERLLSIIAD-AEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAeAWQEP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1232 nnncdtttsgssgAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSS--ELYPSRHVVVCAPPYSGISLVLWC 1309
Cdd:PRK05691 162 -------------ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPLYHDMGLIGGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1310 LSSVYSGHHTTLIPPMEVEQQPSLFLTTLSNLKvrdafttySTIN--------TCVTQLA-TSVENLrergcNLSMLRsc 1380
Cdd:PRK05691 229 LQPIFSGVPCVLMSPAYFLERPLRWLEAISEYG--------GTISggpdfayrLCSERVSeSALERL-----DLSRWR-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1381 VAIAEERP-RIALMSSFCKLFAPLALNNRAISTSFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLvGKGAPhsva 1459
Cdd:PRK05691 294 VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEP-GTGSV---- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1460 LIESGKLLPGVKIAIANPETRGQCADSHLGEIWVA--SIHNASPLNRLASVTGFgdegtMNTDvynarlttGDTktrWAR 1537
Cdd:PRK05691 369 LMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASgpSIAHGYWRNPEASAKTF-----VEHD--------GRT---WLR 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1538 TGYLGFLRqtqsiteHGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFTWNHL----VVIAAEC 1611
Cdd:PRK05691 433 TGDLGFLR-------DGEL----FVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkGRVAAFAVNHQgeegIGIAAEI 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 808354807 1612 TGSESDAL---DLVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGEKLRSTIR 1662
Cdd:PRK05691 502 SRSVQKILppqALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACR 555
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
406-1018 |
3.29e-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: 112.38 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 406 PRSLDSAFHRfgttAAKNIAA--MVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYP 483
Cdd:cd05906 9 PRTLLELLLR----AAERGPTkgITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGL------------RPGDSVILQFD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 484 NTQplHFLAAFYGCLQAGVIPVPVEMPS-----SKREAGIAQLGFLLGNCgvkVALTSEscykglpkkvntsstfsapsg 558
Cdd:cd05906 73 DNE--DFIPAFWACVLAGFVPAPLTVPPtydepNARLRKLRHIWQLLGSP---VVLTDA--------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 559 snSLTGTSSEIVDFRGWPRLWWAVTEHMSKPSRDWTAPPRLADeTIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAM 638
Cdd:cd05906 127 --ELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD-DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 639 EYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATT------ALVKSRDlhwaLLA 712
Cdd:cd05906 204 GLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLND----LLE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 713 TRDHKDISLASLRTLLVADGANpwSLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSETGTISIRrrgNAQLGSQSGRGILS 792
Cdd:cd05906 280 EIEDGTWDLSSLRYLVNAGEAV--VAKTIRRLLRLL--EPYGLPPDAIRPAFGMTETCSGVIY---SRSFPTYDHSQALE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 793 MSALSHCV----VR-VDTENSLTSltlqdagqivagavvvvtaidgsnrlcqADEIGEICVSANSTAQLYWALDGQTHHT 867
Cdd:cd05906 353 FVSLGRPIpgvsMRiVDDEGQLLP----------------------------EGEVGRLQVRGPVVTKGYYNNPEANAEA 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 868 FKvepvgEYGkligavrYVRSGLIGFMGpDGMVFVVARRQSLLAVSGRYHSADDIIAtvlAVEPMKFVYRGRICVFSTsv 947
Cdd:cd05906 405 FT-----EDG-------WFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAV-- 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 948 lRD-----ERIVIVAeqkpnCSEEEAFDWITRVLRAIDTI--HQVGIYCCALVPANH--LPKTPLGGVHVSETKQRFENG 1018
Cdd:cd05906 467 -RDpgaetEELAIFF-----VPEYDLQDALSETLRAIRSVvsREVGVSPAYLIPLPKeeIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
438-1025 |
7.90e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 111.25 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 438 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIyPNTQPlHFLAAFYGCLQAGVIPVPVEMPSS--KRE 515
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGL------------KPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPMGfgGRE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 516 AGIAQLGFLLGNCGVKVALtsescykglpkkvntsstfsAPSGSNSLTgtsSEIVDFRgwpRLWWAVT--EHMSKPSRDW 593
Cdd:PRK09192 115 SYIAQLRGMLASAQPAAII--------------------TPDELLPWV---NEATHGN---PLLHVLShaWFKALPEADV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 594 TAPPRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALT-TAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKV 672
Cdd:PRK09192 169 ALPRPTPDD-IAYLQYSSGSTRFPRGVIITHRALMANLRAIShDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 673 IFVPYSLMKMNPATWMHMVSKYQATTALvkSRDLHWALLATR----DHKDISLASLRtlLVADGANPWSLSSCDAFAAAF 748
Cdd:PRK09192 248 DYLPTRDFARRPLQWLDLISRNRGTISY--SPPFGYELCARRvnskDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 749 TPSPYSlrPDAMCPCAGSSE-TGTISIrrrgnaqlgSQSGRGI----LSMSALSHCVVRVDT-ENSLTSLTLQDAGQIVA 822
Cdd:PRK09192 324 APAGFD--DKAFMPSYGLAEaTLAVSF---------SPLGSGIvveeVDRDRLEYQGKAVAPgAETRRVRTFVNCGKALP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 823 GAVVVVTAIDGS---NRlcqadEIGEICVSANSTAQLYWALDgqthhtfkvepvgEYGKLIGAVRYVRSGLIGFMGpDGM 899
Cdd:PRK09192 393 GHEIEIRNEAGMplpER-----VVGHICVRGPSLMSGYFRDE-------------ESQDVLAADGWLDTGDLGYLL-DGY 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 900 VFVVARRQSLLAVSGRYHSADDIiatVLAVEPMKFVYRGRICVFSTSVLRDERIVIVAEQKPNCSEEEA--FDWITRVLR 977
Cdd:PRK09192 454 LYITGRAKDLIIINGRNIWPQDI---EWIAEQEPELRSGDAAAFSIAQENGEKIVLLVQCRISDEERRGqlIHALAALVR 530
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 808354807 978 AIDTIHQVgiycCALVPANHLPKTPLGGVHVSETKQRFENGDLHPSTL 1025
Cdd:PRK09192 531 SEFGVEAA----VELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDV 574
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1082-1545 |
7.93e-25 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 109.32 E-value: 7.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1082 LRSRAQSSPDHRILTlvtskNAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPV 1161
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1162 CIkppvasdlNTTLGP--IRMMVDMSKAVAILApQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWRRKNNNNCDTTT 1239
Cdd:pfam00501 75 PL--------NPRLPAeeLAYILEDSGAKVLIT-DDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1240 SGSSGAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSE----LYPSRHVVVCAPPYSGISLVLWCLSSVYS 1315
Cdd:pfam00501 146 PPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1316 GhHTTLIPPMEVEQQPSLFLTTLSNLKVRDAFTTYSTINTCvtqlatsVENLRERGCNLSMLRSCVaIAEERPRIALMSS 1395
Cdd:pfam00501 226 G-ATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVL-SGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1396 FcklfapLALNNRAISTSFSSRVNAAICMQGASGPEPSTVyvdaralrndrislvgkgaPHSValiesGKLLPGVKIAIA 1475
Cdd:pfam00501 297 F------RELFGGALVNGYGLTETTGVVTTPLPLDEDLRS-------------------LGSV-----GRPLPGTEVKIV 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808354807 1476 NPETRGQCADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTmntdvyNARLTTGdtktRWARTGYLGFLR 1545
Cdd:pfam00501 347 DDETGEPVPPGEPGELCVRGPGVMKGyLND--------PELT------AEAFDED----GWYRTGDLGRRD 399
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
473-1020 |
3.52e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.82 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 473 KPGDRVALIYPntQPLHFLAAFYGCLQAGVIPVPVEMPSskrEAG-IAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSS 551
Cdd:PRK07769 77 KPGDRVAILAP--QNLDYLIAFFGALYAGRIAVPLFDPA---EPGhVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 552 TFSAPsgsnsltgtssEIVDFRGWPRlwwAVTEhmskpsrDWTaPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHC 631
Cdd:PRK07769 152 AKERP-----------RVIAVDAVPD---EVGA-------TWV-PPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 632 RALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKmNPATWMHMVSKYQATTALVKSRDLHWA-- 709
Cdd:PRK07769 210 LQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWIRELARKPGGTGGTFSAAPNFAfe 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 710 LLATR-----DHKDISLASLRTLLvaDGANPWSLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSE-TGTISIRRRGNAQLG 783
Cdd:PRK07769 289 HAAARglpkdGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAF--APYGLPPTAIKPSYGMAEaTLFVSTTPMDEEPTV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 784 SQSGRGILSmsalSHCVVRV--DTENSLTSLTlqdAGQIVAGAVVVVtaIDGSNRLCQAD-EIGEICVSANSTAQLYWAL 860
Cdd:PRK07769 365 IYVDRDELN----AGRFVEVpaDAPNAVAQVS---AGKVGVSEWAVI--VDPETASELPDgQIGEIWLHGNNIGTGYWGK 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 861 DGQTHHTFK------VEPVGEYGKLIGAvRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATvlAVEPMKF 934
Cdd:PRK07769 436 PEETAATFQnilksrLSESHAEGAPDDA-LWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLEYT--AQEATKA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 935 VYRGRICVFS---------------TSVLRD-----ERIVIVAEQKPNCSEEEAFDWITRVLRAIDTIHQVGIYCCALVP 994
Cdd:PRK07769 512 LRTGYVAAFSvpanqlpqvvfddshAGLKFDpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVP 591
|
570 580
....*....|....*....|....*.
gi 808354807 995 ANHLPKTPLGGVHVSETKQRFENGDL 1020
Cdd:PRK07769 592 AGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1078-1672 |
4.87e-20 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 96.35 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1078 LLECLRSRAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARlsRGDHVALIFPPSIDLVAAFFGCLSAG 1157
Cdd:PRK12476 39 LIERNIANVGDTVAYRYLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAAIKAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1158 LVPVCIKPPV----ASDLNTTLGPIRMMVDMSKAVAilaPQNVSKLLKSKEAAHSidsnawPMILDLEDAPSSwrrknnn 1233
Cdd:PRK12476 117 TIAVPLFAPElpghAERLDTALRDAEPTVVLTTTAA---AEAVEGFLRNLPRLRR------PRVIAIDAIPDS------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1234 ncdtttSGSSGAASK---EEICYLDFSINSSGQLQGSSMSEASAIT-VCKSIKVSSELYPSRHVVVCAPPYSGISLVLWC 1309
Cdd:PRK12476 181 ------AGESFVPVEldtDDVSHLQYTSGSTRPPVGVEITHRAVGTnLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1310 LSSVYSGHhTTLIPPMEVEQQPSLFLTTLSnlkvrDAFTTYSTInTCVTQLA---TSVENLRERGCNLSMLRSCVAIAEE 1386
Cdd:PRK12476 255 FPAVYGGH-STLMSPTAFVRRPQRWIKALS-----EGSRTGRVV-TAAPNFAyewAAQRGLPAEGDDIDLSNVVLIIGSE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1387 RPRIALMSSFCKLFAPLALNNRAISTSFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLVGKGAPHSVALIESGKL 1466
Cdd:PRK12476 328 PVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1467 LPGVKIAIANPETRGQCADSHLGEIWvasIHNAsplNRLASVTGFGDEGTMntdVYNARLTT----------GDTKTRWA 1536
Cdd:PRK12476 408 ARSQWAVIVDPDTGAELPDGEVGEIW---LHGD---NIGRGYWGRPEETER---TFGAKLQSrlaegshadgAADDGTWL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1537 RTGYLGFLRQtqsitehGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFT-----WNHLVVIAA 1609
Cdd:PRK12476 479 RTGDLGVYLD-------GEL----YITGRIADLIVIDGRNHYPQDIEATVAEASPMVrrGYVTAFTvpaedNERLVIVAE 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808354807 1610 ECTG-SESDALDLVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGEKLRSTIRSLFLEEKLNP 1672
Cdd:PRK12476 548 RAAGtSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
473-1018 |
8.09e-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: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 473 KPGDRValIYPNTQPLHFLAAFYGCLQAGVIPVPVEMPSSkreagiaqlgfllgncgvkvaltsESCYKGLPKKVNTSSt 552
Cdd:cd05908 38 KPGQEV--VFQITHNNKFLYLFWACLLGGMIAVPVSIGSN------------------------EEHKLKLNKVWNTLK- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 553 fsapsgsNSLTGTSSEIVDfrgwprlwwavtehmskpsrdwtappRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCR 632
Cdd:cd05908 91 -------NPYLITEEEVLC--------------------------ELADE-LAFIQFSSGSTGDPKGVMLTHENLVHNMF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 633 ALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATtaLVKSRDLHWALLA 712
Cdd:cd05908 137 AILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKAT--IVSSPNFGYKYFL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 713 TR--DHK--DISLASLRtlLVADGANPWSLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSE-------------TGTISIR 775
Cdd:cd05908 215 KTlkPEKanDWDLSSIR--MILNGAEPIDYELCHEFLDHM--SKYGLKRNAILPVYGLAEasvgaslpkaqspFKTITLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 776 RRgnaqlGSQSGRGIlsmsalshcvVRVDTENSlTSLTLQDAGQivAGAVVVVTAIDGSNRLCQADEIGEICVSANSTAQ 855
Cdd:cd05908 291 RR-----HVTHGEPE----------PEVDKKDS-ECLTFVEVGK--PIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 856 LYWAldgqthhtfkvEPVgEYGKLIGAVRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPmkfV 935
Cdd:cd05908 353 GYYN-----------NPE-ATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEG---V 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 936 YRGR--ICVFSTSVLRDERIVIVAEQKPncSEEEAFDWITRVLRAID-----TIHQVgiyccalVPANHLPKTPLGGVHV 1008
Cdd:cd05908 417 ELGRvvACGVNNSNTRNEEIFCFIEHRK--SEDDFYPLGKKIKKHLNkrggwQINEV-------LPIRRIPKTTSGKVKR 487
|
570
....*....|
gi 808354807 1009 SETKQRFENG 1018
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 ... |
603-1006 |
2.33e-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: 88.50 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 603 TIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKrEVGLWHAILASIFNGMKVIFVPYSlmkm 682
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 683 NPATWMHMVSKYQATTALVkSRDLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFTPSPYSlrpdamcp 762
Cdd:cd04433 76 DPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPGIKLVN-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 763 CAGSSETG--TISIRRRGNAQLGSQSGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvvtaIDGSNRLCQA 840
Cdd:cd04433 145 GYGLTETGgtVATGPPDDDARKPGSVGR------PVPGVEVRI---------------------------VDPDGGELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 841 DEIGEICVSANSTAQLYWALDGQTHHTFKvepvgeygklIGavrYVRSGLIGFMGPDGMVFVVARRQSLLAVSGRYHSAD 920
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAVDE----------DG---WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 921 DIIATVLAVEPMKfvyrgRICVFstsVLRDER------IVIVAEQKPNCSEEEAFDWITRVLRAIDTIHQVgiyccalVP 994
Cdd:cd04433 259 EVEAVLLGHPGVA-----EAAVV---GVPDPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VF 323
|
410
....*....|..
gi 808354807 995 ANHLPKTPLGGV 1006
Cdd:cd04433 324 VDALPRTASGKI 335
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
473-1004 |
2.39e-18 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 90.96 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 473 KPGDRVALIYPntQPLHFLAAFYGCLQAGVIPVPVEMPSSKREAgiAQLGFLLGNCGVKVALTsescykglpkkvntsst 552
Cdd:PRK12476 90 GPGDRVAILAP--QGIDYVAGFFAAIKAGTIAVPLFAPELPGHA--ERLDTALRDAEPTVVLT----------------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 553 fsapsgsnslTGTSSEIVD--FRGWPRL----WWAVTEHMSKPSRDWTAPPrLADETIAYIEYTTGNDGTVKGCCVTRQA 626
Cdd:PRK12476 149 ----------TTAAAEAVEgfLRNLPRLrrprVIAIDAIPDSAGESFVPVE-LDTDDVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 627 VFAHCRALTTAMEYKEDETM-VCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKmNPATWMHMVSKYQATTALVKSR- 704
Cdd:PRK12476 218 VGTNLVQMILSIDLLDRNTHgVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVR-RPQRWIKALSEGSRTGRVVTAAp 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 705 DLHWALLATR----DHKDISLaslRTLLVADGANPWSLSSCDAFAAAFtpSPYSLRPDAMCPCAG-------------SS 767
Cdd:PRK12476 297 NFAYEWAAQRglpaEGDDIDL---SNVVLIIGSEPVSIDAVTTFNKAF--APYGLPRTAFKPSYGiaeatlfvatiapDA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 768 ETGTISIRRRgnaQLGSqsGRGILSMSALSHCVVRVDtensltsltlqdAGQIVAGAVVVVTAIDGSNRLcQADEIGEIC 847
Cdd:PRK12476 372 EPSVVYLDRE---QLGA--GRAVRVAADAPNAVAHVS------------CGQVARSQWAVIVDPDTGAEL-PDGEVGEIW 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 848 VSANSTAQLYWALDGQTHHTFKVE-----PVGEY--GKLIGAvRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSAD 920
Cdd:PRK12476 434 LHGDNIGRGYWGRPEETERTFGAKlqsrlAEGSHadGAADDG-TWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQ 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 921 DIIATVLAVEPMkfVYRGRICVFSTSVLRDERIVIVAEQKPNCSEEEAFDWITRVLRAIDTIHQVGIYCCALVPANHLPK 1000
Cdd:PRK12476 512 DIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPR 589
|
....
gi 808354807 1001 TPLG 1004
Cdd:PRK12476 590 TTSG 593
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1075-1648 |
6.43e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 89.62 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1075 SLPLLecLRSRAQSSPDHRILTLVtskNAEQDTA------TCSTLLKRAERIAGLLtdRARLSRGDHVALIFPPSIDLVA 1148
Cdd:PRK05850 2 SVPSL--LRERASLQPDDAAFTFI---DYEQDPAgvaetlTWSQLYRRTLNVAEEL--RRHGSTGDRAVILAPQGLEYIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1149 AFFGCLSAGLVPVCIKPPV--ASDLNTTLgpirMMVDmSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSS 1226
Cdd:PRK05850 75 AFLGALQAGLIAVPLSVPQggAHDERVSA----VLRD-TSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1227 wrrknnNNCDtttsgsSGAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSI---------KVSSelyPSRHVVVCA 1297
Cdd:PRK05850 150 ------RGSD------ARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdyfgdtgGVPP---PDTTVVSWL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1298 PPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPSLFLTTLSnlKVRDAFTTYSTIntcVTQLA---TSVENLRerGCNL 1374
Cdd:PRK05850 215 PFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRPARWMQLLA--SNPHAFSAAPNF---AFELAvrkTSDDDMA--GLDL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1375 SMLRSCVAIAEeRPRIALMSSFCKLFAPLALNNRAISTSF---SSRVNAAIcmqGASGPEPSTVYVDARALRNDRI---- 1447
Cdd:PRK05850 288 GGVLGIISGSE-RVHPATLKRFADRFAPFNLRETAIRPSYglaEATVYVAT---REPGQPPESVRFDYEKLSAGHAkrce 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1448 -----SLVGKGAPHSvaliesgkllPGVKIAiaNPETRGQCADSHLGEIWVASIHNASplnrlasvtGF--GDEGTMNTd 1520
Cdd:PRK05850 364 tgggtPLVSYGSPRS----------PTVRIV--DPDTCIECPAGTVGEIWVHGDNVAA---------GYwqKPEETERT- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1521 vYNARLTT---GDTKTRWARTGYLGFlrqtqsITEhGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRfvGNSA 1597
Cdd:PRK05850 422 -FGATLVDpspGTPEGPWLRTGDLGF------ISE-GEL----FIVGRIKDLLIVDGRNHYPDDIEATIQEITG--GRVA 487
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354807 1598 VFT-----WNHLVVIA--AECTGSESDALDLVPA----ITSAVLEEHHLIVGVVVVVDPGSI 1648
Cdd:PRK05850 488 AISvpddgTEKLVAIIelKKRGDSDEEAMDRLRTvkreVTSAISKSHGLSVADLVLVAPGSI 549
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
4-114 |
2.31e-17 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 79.00 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 4 PDTLPDEVREKLAELDLELSEGDITKKGYDKKRDALLAPFkslraanALHAEQSSASPNSRSNRRNQRRVTQDDDRYHSE 83
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKF-------LLHPETPTKLSAEAQNQLASLETKLRDEELSEE 74
|
90 100 110
....*....|....*....|....*....|.
gi 808354807 84 IRVEAVHQALAEYSdGRKLGpQPVKPHRRNG 114
Cdd:pfam06464 75 VYLEKVKALLAKEL-ERENG-LNAPTKEQSG 103
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1128-1676 |
3.00e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 87.48 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1128 ARL----SRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikPPVASDLNTTLGPIRMMVDMSKAVAIL----APQNVSKL 1199
Cdd:PRK07769 70 ARLqqvtKPGDRVAILAPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGHVGRLHAVLDDCTPSAILtttdSAEGVRKF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1200 LKSKEAAHSidsnawPMILDLEDAP----SSWRRKNNNNCDTT----TSGSSGAASKEEICYLDFSINssgqlqgssmse 1271
Cdd:PRK07769 147 FRARPAKER------PRVIAVDAVPdevgATWVPPEANEDTIAylqyTSGSTRIPAGVQITHLNLPTN------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1272 asAITVCKSIkvssELYPSRHVVVCAPPYSGISLVLWCLSSVySGHHTTLIPPMEVEQQPSLFLTTLSNlKVRDAFTTYS 1351
Cdd:PRK07769 209 --VLQVIDAL----EGQEGDRGVSWLPFFHDMGLITVLLPAL-LGHYITFMSPAAFVRRPGRWIRELAR-KPGGTGGTFS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1352 TINTCVTQLATS--VENLRERGCNLSMLRSCVAiAEERPRIALMSSFCKLFAPLALNNRAISTSFSSrvnAAICMQGASG 1429
Cdd:PRK07769 281 AAPNFAFEHAAArgLPKDGEPPLDLSNVKGLLN-GSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGM---AEATLFVSTT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1430 P---EPSTVYVDARALRNDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGQCADSHLGEIWVASIHNASPLNRLA 1506
Cdd:PRK07769 357 PmdeEPTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1507 SVTGFGDEGTMNTDVYNARLTTGDTKTRWARTGYLGflrqtqsITEHGELhdavFVVGALNESLVLRGMRYHPFDVESTV 1586
Cdd:PRK07769 437 EETAATFQNILKSRLSESHAEGAPDDALWVRTGDYG-------VYFDGEL----YITGRVKDLVIIDGRNHYPQDLEYTA 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1587 ---SKAHR--FVG---------NSAVFTWNH-------------LVVIAAECTGS-ESDALDLVPAITSAVLEEHHLIVG 1638
Cdd:PRK07769 506 qeaTKALRtgYVAafsvpanqlPQVVFDDSHaglkfdpedtseqLVIVAERAPGAhKLDPQPIADDIRAAIAVRHGVTVR 585
|
570 580 590
....*....|....*....|....*....|....*...
gi 808354807 1639 VVVVVDPGSIRHGPGGEKLRSTIRSLFLEEKLNPIYVA 1676
Cdd:PRK07769 586 DVLLVPAGSIPRTSSGKIARRACRAAYLDGSLRSGYGQ 623
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
404-733 |
1.80e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 84.57 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 404 TMPRSLDSAFHRFGTTAAkniaamVLDQSakpsTQLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYP 483
Cdd:PRK07656 6 TLPELLARAARRFGDKEA------YVFGD----QRLTYAELNARVRRAAAALAALGIG------------KGDRVAIWAP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 484 NTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREAgiaqlGFLLGNCGVKVAL-------TSESCYKGLPK-KVNTSSTFSA 555
Cdd:PRK07656 64 NS--PHWVIAALGALKAGAVVVPLNTRYTADEA-----AYILARGDAKALFvlglflgVDYSATTRLPAlEHVVICETEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 556 PSGSNSLTGTSSEIVdfrgwprlwwavtehmSKPSRDWTAPPrLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALT 635
Cdd:PRK07656 137 DDPHTEKMKTFTDFL----------------AAGDPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 636 TAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPyslmKMNPATWMHMVSKYQATTaLVKSRDLHWALLATRD 715
Cdd:PRK07656 200 EYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFDPDEVFRLIETERITV-LPGPPTMYNSLLQHPD 274
|
330
....*....|....*...
gi 808354807 716 HKDISLASLRtLLVADGA 733
Cdd:PRK07656 275 RSAEDLSSLR-LAVTGAA 291
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
432-914 |
2.42e-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: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 432 SAKPSTQLTYGKLHSRAGKVAYMLltktvqvNKDGSKnvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPS 511
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGL-------RKLGLK-----KGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAANPIY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 512 SKREagiaqLGFLLGNCGVKVALTSESCYKglpkKVNTSSTFSAPSGSNSLTGTSSEIVDFRGwpRLWWAVTEhmskpSR 591
Cdd:cd05911 70 TADE-----LAHQLKISKPKVIFTDPDGLE----KVKEAAKELGPKDKIIVLDDKPDGVLSIE--DLLSPTLG-----EE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 592 DWTAPPRL--ADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCR--ALTTAMEYKEDETMVCVVDFKREVGLWhAILASIF 667
Cdd:cd05911 134 DEDLPPPLkdGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSqvQTFLYGNDGSNDVILGFLPLYHIYGLF-TTLASLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 668 NGMKVIFVPyslmKMNPATWMHMVSKYQATTALVKSRdlHWALLATR-DHKDISLASLRTLLVadGANPWSLSSCDAFAA 746
Cdd:cd05911 213 NGATVIIMP----KFDSELFLDLIEKYKITFLYLVPP--IAAALAKSpLLDKYDLSSLRVILS--GGAPLSKELQELLAK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 747 aftpspysLRPDAMCPCA-GSSETG-TISIRRRGNAQLGSqSGRGILSMSALshcVVRVDTENSLTSltlqdagqivaga 824
Cdd:cd05911 285 --------RFPNATIKQGyGMTETGgILTVNPDGDDKPGS-VGRLLPNVEAK---IVDDDGKDSLGP------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 825 vvvvtaidgsnrlcqaDEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkligavRYVRSGLIGFMGPDGMVFVVA 904
Cdd:cd05911 340 ----------------NEPGEICVRGPQVMKGYYNNPEATKETFDED------------GWLHTGDIGYFDEDGYLYIVD 391
|
490
....*....|
gi 808354807 905 RRQSLLAVSG 914
Cdd:cd05911 392 RKKELIKYKG 401
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1078-1599 |
2.79e-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: 83.71 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1078 LLECLRSRAQSSPDHRILTlvtsknAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG 1157
Cdd:COG0318 1 LADLLRRAAARHPDRPALV------FGGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1158 LVPVCikppvasdLNTTLGP--IRMMVDMSKAVAILApqnvskllkskeaahsidsnAWpMILdledapsswrrknnnnc 1235
Cdd:COG0318 74 AVVVP--------LNPRLTAeeLAYILEDSGARALVT--------------------AL-ILY----------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1236 dttTSGSSGaASKeeicyldfsinssgqlqGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYS 1315
Cdd:COG0318 108 ---TSGTTG-RPK-----------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1316 GHHTTLIPPMEveqqPSLFLTTLSNLKVrdafTTYSTINTCVTQLAtsvENLRERGCNLSMLRSCVAIAeERPRIALMSS 1395
Cdd:COG0318 167 GATLVLLPRFD----PERVLELIERERV----TVLFGVPTMLARLL---RHPEFARYDLSSLRLVVSGG-APLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1396 FCKLFaplalnNRAISTSF-SSRVNAAICMqgasGPEpstvyvDARALRndrislvgkgaPHSValiesGKLLPGVKIAI 1474
Cdd:COG0318 235 FEERF------GVRIVEGYgLTETSPVVTV----NPE------DPGERR-----------PGSV-----GRPLPGVEVRI 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1475 ANPETRgQCADSHLGEIWVASihnasplnrlASVTG--FGD-EGTmntdvyNARLTTGdtktrWARTGYLGFlrqtqsIT 1551
Cdd:COG0318 283 VDEDGR-ELPPGEVGEIVVRG----------PNVMKgyWNDpEAT------AEAFRDG-----WLRTGDLGR------LD 334
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 808354807 1552 EHGELhdavFVVGALNESLVLRGMRYHPFDVESTVSkAHRFVGNSAVF 1599
Cdd:COG0318 335 EDGYL----YIVGRKKDMIISGGENVYPAEVEEVLA-AHPGVAEAAVV 377
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
436-730 |
1.28e-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: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 436 STQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKRE 515
Cdd:COG0365 37 ERTLTYAELRREVNRFANALRALGV------------KKGDRVAIYLPNI--PEAVIAMLACARIGAVHSPV-FPGFGAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 516 AgiaqLGFLLGNCGVKVALTSESCYKGlPKKVNTSSTFS-APSGSNSLT-----GTSSEIVDFRGWprLWWAvtEHMSKP 589
Cdd:COG0365 102 A----LADRIEDAEAKVLITADGGLRG-GKVIDLKEKVDeALEELPSLEhvivvGRTGADVPMEGD--LDWD--ELLAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 590 SRDWTAPPRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHcrALTTAM---EYKEDETMVCVVDFKREVGLWHAILASI 666
Cdd:COG0365 173 SAEFEPEPTDADD-PLFILYTSGTTGKPKGVVHTHGGYLVH--AATTAKyvlDLKPGDVFWCTADIGWATGHSYIVYGPL 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354807 667 FNGMKVIFVPYSLMKMNPATWMHMVSKYQAT------TALvksRdlhwALLATRDH--KDISLASLRTLLVA 730
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 ... |
426-914 |
2.54e-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: 80.68 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 426 AMVLDQSA-----KPSTQ-----LTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFY 495
Cdd:cd05936 2 ADLLEEAArrfpdKTALIfmgrkLTYRELDALAEAFAAGLQNLGVQ------------PGDRVALMLPNC--PQFPIAYF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 496 GCLQAGVIPVPVEMPSSKREagiaqLGFLLGNCGVKValtsescykglpkkvntsstfsapsgsnsltgtsseIVDFRGW 575
Cdd:cd05936 68 GALKAGAVVVPLNPLYTPRE-----LEHILNDSGAKA------------------------------------LIVAVSF 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 576 prlwwavtEHMSKPSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAH---CRALTTAMEyKEDETMVCVVDF 652
Cdd:cd05936 107 --------TDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANalqIKAWLEDLL-EGDDVVLAALPL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 653 KREVGLWHAILASIFNGMKVIFVPyslmKMNPATWMHMVSKYQATT-ALVKSrdLHWALLATRDHKDISLASLRtlLVAD 731
Cdd:cd05936 178 FHVFGLTVALLLPLALGATIVLIP----RFRPIGVLKEIRKHRVTIfPGVPT--MYIALLNAPEFKKRDFSSLR--LCIS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 732 GANPWSLSSCDAFAAAF-TP----------SPYSlrpdAMCPCAGSSETGTIsirrrgnaqlgsqsGRGILSMSALshcV 800
Cdd:cd05936 250 GGAPLPVEVAERFEELTgVPivegygltetSPVV----AVNPLDGPRKPGSI--------------GIPLPGTEVK---I 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 801 VRVDTEnsltslTLQDagqivagavvvvtaidgsnrlcqaDEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkli 880
Cdd:cd05936 309 VDDDGE------ELPP------------------------GEVGELWVRGPQVMKGYWNRPEETAEAFVDG--------- 349
|
490 500 510
....*....|....*....|....*....|....
gi 808354807 881 gavrYVRSGLIGFMGPDGMVFVVARRQSLLAVSG 914
Cdd:cd05936 350 ----WLRTGDIGYMDEDGYFFIVDRKKDMIIVGG 379
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1111-1633 |
1.27e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 78.89 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1111 STLLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikpPVAsdLNTTLG-------PIRMMVD 1183
Cdd:PRK09192 53 QTLRARAEAGARRLL-ALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV----PLP--LPMGFGgresyiaQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1184 MSKAVAILAPQNVSKLLksKEAAHSID-----SNAWpmiLDLEDAPsswrrknnnNCDTTTsgssgaASKEEICYLDFSI 1258
Cdd:PRK09192 126 SAQPAAIITPDELLPWV--NEATHGNPllhvlSHAW---FKALPEA---------DVALPR------PTPDDIAYLQYSS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1259 NSS----GQL--QGSSMSEASAITvCKSIKVsselYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPS 1332
Cdd:PRK09192 186 GSTrfprGVIitHRALMANLRAIS-HDGLKV----RPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1333 LFLTTLSnlkvRDAFT-TYST---INTCvtqlATSVENLRERGCNLSMLRScVAIAEERPRIALMSSFCKLFAPLALNNR 1408
Cdd:PRK09192 261 QWLDLIS----RNRGTiSYSPpfgYELC----ARRVNSKDLAELDLSCWRV-AGIGADMIRPDVLHQFAEAFAPAGFDDK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1409 AISTSFSSRVNA-AICM----QGAsgpepSTVYVDARALRNDRISLVGKGAPHSV-ALIESGKLLPGVKIAIANpETRGQ 1482
Cdd:PRK09192 332 AFMPSYGLAEATlAVSFsplgSGI-----VVEEVDRDRLEYQGKAVAPGAETRRVrTFVNCGKALPGHEIEIRN-EAGMP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1483 CADSHLGEIWVA--SIHNASplnrlasvtgFGDEGTmnTDVYNArlttgdtkTRWARTGYLGFLrqtqsitEHGELhdav 1560
Cdd:PRK09192 406 LPERVVGHICVRgpSLMSGY----------FRDEES--QDVLAA--------DGWLDTGDLGYL-------LDGYL---- 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808354807 1561 FVVGALNESLVLRGMRYHPFDVESTVSKAHRF-VGNSAVF---TWNH-LVVIAAECTGSESDA-LDLVPAITSAVLEEH 1633
Cdd:PRK09192 455 YITGRAKDLIIINGRNIWPQDIEWIAEQEPELrSGDAAAFsiaQENGeKIVLLVQCRISDEERrGQLIHALAALVRSEF 533
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
440-730 |
3.09e-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: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 440 TYGKLHSRAGKVAYMLLTKtvqvnkdgsknVMCKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPV--EMPSSKREag 517
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-----------GGVGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLdpAYPAERLA-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 518 iaqlgFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsgsnsltGTSSEIVDFRgwPRLWWAVTEHMSKPSRDWTAPP 597
Cdd:TIGR01733 66 -----FILEDAGARLLLTDSALASRLA-------------------GLVLPVILLD--PLELAALDDAPAPPPPDAPSGP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 598 rladETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWhAILASIFNGMKVIFVPY 677
Cdd:TIGR01733 120 ----DDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 808354807 678 SLMKMNPATWMHMVSKYQATTA-LVKSrdlHWALLAtrDHKDISLASLRTLLVA 730
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 ... |
1288-1620 |
2.62e-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: 73.09 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1288 YPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPmeveQQPSLFLTTLSNLKVRDAFTTYSTINTCVtqlatsvENL 1367
Cdd:cd04433 38 LTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK----FDPEAALELIEREKVTILLGVPTLLARLL-------KAP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1368 RERGCNLSMLRSCVAIAEERPrIALMSSFcklfapLALNNRAISTSFssrvnaaicmqGAS--GPEPSTVYVDARALRnd 1445
Cdd:cd04433 107 ESAGYDLSSLRALVSGGAPLP-PELLERF------EEAPGIKLVNGY-----------GLTetGGTVATGPPDDDARK-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1446 rislvgkgaPHSValiesGKLLPGVKIAIANPETRGqCADSHLGEIWVASIHNasplnrlasvtgfgdegtMNTDVYNAR 1525
Cdd:cd04433 167 ---------PGSV-----GRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSV------------------MKGYWNNPE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1526 LTTGDTKTRWARTGYLGFLRqtqsitEHGELHdavfVVGALNESLVLRGMRYHPFDVESTVsKAHRFVGNSAVF-----T 1600
Cdd:cd04433 214 ATAAVDEDGWYRTGDLGRLD------EDGYLY----IVGRLKDMIKSGGENVYPAEVEAVL-LGHPGVAEAAVVgvpdpE 282
|
330 340
....*....|....*....|
gi 808354807 1601 WNHLVVIAAECTGSESDALD 1620
Cdd:cd04433 283 WGERVVAVVVLRPGADLDAE 302
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
370-895 |
2.85e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.22 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 370 LEAMAKirDPDAPRPEGTIMNP---VRGEAAHSNTNNTMPRSLdsAFH-RFGTTAAKN---IAAMVLDQsakpstQLTYG 442
Cdd:PRK12316 1963 LEQMAE--DAQAALGELALLDAgerQRILADWDRTPEAYPRGP--GVHqRIAEQAARApeaIAVVFGDQ------HLSYA 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 443 KLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmPSSKREagiaQLG 522
Cdd:PRK12316 2033 ELDSRANRLAHRLRARGV------------GPEVRVAIAAERSFEL--VVALLAVLKAGGAYVPLD-PNYPAE----RLA 2093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 523 FLLGNCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLTGTSSEivDFRGWPRlwwavtehmskpsrdwTAP-PRLAD 601
Cdd:PRK12316 2094 YMLEDSGAALLLTQRHLLERLP----------LPAGVARLPLDRDA--EWADYPD----------------TAPaVQLAG 2145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 602 ETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHaILASIFNGMKVIFVPYSLmk 681
Cdd:PRK12316 2146 ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIRDDEL-- 2222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 682 MNPATWMHMVSKYQATTALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAftpspysLRPDAMC 761
Cdd:PRK12316 2223 WDPEQLYDEMERHGVTILDFPP--VYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEA-------LRPVYLF 2291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 762 PCAGSSETGTISIRRRGNAQLGSQS-----GRGIlsmSALSHCVvrvdtensltsltlqdagqivagavvvvtaIDGSNR 836
Cdd:PRK12316 2292 NGYGPTEAVVTPLLWKCRPQDPCGAayvpiGRAL---GNRRAYI------------------------------LDADLN 2338
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808354807 837 LCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKLI----GAVRYVRSGLIGFMG 895
Cdd:PRK12316 2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLyrtgDLARYRADGVVEYLG 2401
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
472-1006 |
6.97e-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: 66.69 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 472 CKPGDRVALIYPNTQPLHFLAA--FYGCLQAGVIPVPVEmPSSKReagiAQLGFLLGNCGVKVALTSEScYKGLPKKVNT 549
Cdd:cd05922 15 GVRGERVVLILPNRFTYIELSFavAYAGGRLGLVFVPLN-PTLKE----SVLRYLVADAGGRIVLADAG-AADRLRDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 550 SStfsapsgsnsltGTSSEIVDFRGWprlwWAvtehmskpSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFA 629
Cdd:cd05922 89 AS------------PDPGTVLDADGI----RA--------ARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 630 HCRALTTAMEYKEDETMVCVVDFKREVGLwHAILASIFNGMKVIFVPYSLMkmnPATWMHMVSKYQATT-ALVKSrdlHW 708
Cdd:cd05922 145 NARSIAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVL---DDAFWEDLREHGATGlAGVPS---TY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 709 ALLATRDHKDISLASLRTLLVADGANPwslsscDAFAAAFTpspySLRPDAMcpcagssetgtisirrrgnaqlgsqsgr 788
Cdd:cd05922 218 AMLTRLGFDPAKLPSLRYLTQAGGRLP------QETIARLR----ELLPGAQ---------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 789 gILSMSALSHCVVR---VDTENSLTSLTlqDAGQIVAGAVVVVTAIDGSnrLCQADEIGEICVSANSTAQLYWalDGQTH 865
Cdd:cd05922 260 -VYVMYGQTEATRRmtyLPPERILEKPG--SIGLAIPGGEFEILDDDGT--PTPPGEPGEIVHRGPNVMKGYW--NDPPY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 866 HTFKVEPVGeygkligavrYVRSGLIGFMGPDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPMkfvyrGRICVFST 945
Cdd:cd05922 333 RRKEGRGGG----------VLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808354807 946 SVLRDERIVIVAEQKPNCSEEEafdwITRVLRAIDTIHQVGIYCcalVPANHLPKTPLGGV 1006
Cdd:cd05922 398 PDPLGEKLALFVTAPDKIDPKD----VLRSLAERLPPYKVPATV---RVVDELPLTASGKV 451
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
594-1017 |
1.08e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 66.17 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 594 TAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYK-EDETMVCVVDFKREVGLWHAILASIFNGMKV 672
Cdd:PRK07768 144 IDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 673 IFV-PYSLMKmNPATWMHMVSKYQAT-TAlvkSRDLHWALLATR-----DHKDISLASLRTLLvaDGANPWSLSSCDAFA 745
Cdd:PRK07768 224 VKVtPMDFLR-DPLLWAELISKYRGTmTA---APNFAYALLARRlrrqaKPGAFDLSSLRFAL--NGAEPIDPADVEDLL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 746 AAftPSPYSLRPDAMCPCAGSSETG-TISIRRRGN--------AQLGSQSGRGILSMSA-----------LSHCVVRVdt 805
Cdd:PRK07768 298 DA--GARFGLRPEAILPAYGMAEATlAVSFSPCGAglvvdevdADLLAALRRAVPATKGntrrlatlgppLPGLEVRV-- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 806 ensltsltlqdagqivagavvvvtaIDGSNRLCQADEIGEICVSANSTAQLYWALDGQthhtfkVEPVGEYGKLigavry 885
Cdd:PRK07768 374 -------------------------VDEDGQVLPPRGVGVIELRGESVTPGYLTMDGF------IPAQDADGWL------ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 886 vRSGLIGFMGPDGMVFVVARRQSLLAVSGRYHSADDI---IATVLAVEPmkfvyRGRICVFSTSVLRDERIVIVAEQKPN 962
Cdd:PRK07768 417 -DTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIeraAARVEGVRP-----GNAVAVRLDAGHSREGFAVAVESNAF 490
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 808354807 963 CSEEEafdwITRVLRAI--DTIHQVGI--YCCALVPANHLPKTPLGGVHVSETKQRFEN 1017
Cdd:PRK07768 491 EDPAE----VRRIRHQVahEVVAEVGVrpRNVVVLGPGSIPKTPSGKLRRANAAELVTP 545
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
376-699 |
1.18e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.64 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 376 IRDPDAPRPEGTIMNPVRGEAAHSNTNNTmprsldsafHRfGTTAAKNIAAMVLDQSAKP---------STQLTYGKLHS 446
Cdd:PRK12467 1538 VADPERRLGELDLLDEAERRQILEGWNAT---------HT-GYPLARLVHQLIEDQAAATpeavalvfgEQELTYGELNR 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 447 RAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEmPSSKREagiaQLGFLLG 526
Cdd:PRK12467 1608 RANRLAHRLIALGV------------GPEVLVGIAVERS--LEMVVGLLAILKAGGAYVPLD-PEYPRE----RLAYMIE 1668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 527 NCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLtgtsseIVDfrgwPRLWWAVTEHMSKPSRdwtappRLADETIAY 606
Cdd:PRK12467 1669 DSGIELLLTQSHLQARLP----------LPDGLRSL------VLD----QEDDWLEGYSDSNPAV------NLAPQNLAY 1722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 607 IEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHaILASIFNGMKVIFVPYSLMKmNPAT 686
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWE-LFWPLINGARLVIAPPGAHR-DPEQ 1800
|
330
....*....|...
gi 808354807 687 WMHMVSKYQATTA 699
Cdd:PRK12467 1801 LIQLIERQQVTTL 1813
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
437-647 |
3.08e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 61.49 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 437 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREa 516
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALLDLGL------------KKGDRVAALGHNS--DAYALLWLACARAGAVHVPVNFMLTGEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 517 giaqLGFLLGNCGVKVALTsESCYKGLPKKVNTSSTFSAPSGSNSLTGTSSE--IVDFRGWprlwwavtehmSKPSRDWT 594
Cdd:PRK08316 100 ----LAYILDHSGARAFLV-DPALAPTAEAALALLPVDTLILSLVLGGREAPggWLDFADW-----------AEAGSVAE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 808354807 595 APPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMV 647
Cdd:PRK08316 164 PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPL 216
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1102-1599 |
1.39e-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: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1102 NAEQDTATCSTLLKRAERIA-GLltDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLvpvcikppVASDLNTTLGP--I 1178
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAaGL--RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGG--------IFSAANPIYTAdeL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1179 RMMVDMSKAVAIL-APQNVSKLLKSKEAAHSIDSnawpmILDLEDAPSswrrKNNNNCDTTTSGSSGA---------ASK 1248
Cdd:cd05911 75 AHQLKISKPKVIFtDPDGLEKVKEAAKELGPKDK-----IIVLDDKPD----GVLSIEDLLSPTLGEEdedlppplkDGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1249 EEICYLDFSINSSGQLQGSSMSEASAITVCKSIK-VSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEV 1327
Cdd:cd05911 146 DDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQtFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1328 EqqpsLFLTTLSNLKVRDAFTTystiNTCVTQLATSVENLRErgcNLSMLRSCVAIAeerprialmssfcklfAPLAlnn 1407
Cdd:cd05911 226 E----LFLDLIEKYKITFLYLV----PPIAAALAKSPLLDKY---DLSSLRVILSGG----------------APLS--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1408 RAISTSFSSRVNAAICMQG----ASGPePSTVyvdaralrndrislvgkgAPHSVALIES-GKLLPGVKIAIANPETRGQ 1482
Cdd:cd05911 276 KELQELLAKRFPNATIKQGygmtETGG-ILTV------------------NPDGDDKPGSvGRLLPNVEAKIVDDDGKDS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1483 CADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTMNTdvynarlttgDTKTRWARTGYLGFLRqtqsitEHGELhdavF 1561
Cdd:cd05911 337 LGPNEPGEICVRGPQVMKGyYNN--------PEATKET----------FDEDGWLHTGDIGYFD------EDGYL----Y 388
|
490 500 510
....*....|....*....|....*....|....*...
gi 808354807 1562 VVGALNESLVLRGMRYHPFDVEStVSKAHRFVGNSAVF 1599
Cdd:cd05911 389 IVDRKKELIKYKGFQVAPAELEA-VLLEHPGVADAAVI 425
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
440-905 |
7.60e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 57.12 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 440 TYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQplHFLAAFYGCLQAGVIPVPVempsSKREAGiA 519
Cdd:PRK06187 33 TYAELDERVNRLANALRALGV------------KKGDRVAVFDWNSH--EYLEAYFAVPKIGAVLHPI----NIRLKP-E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 520 QLGFLLGNCGVKVALTSES---CYKGLPKKVNTSSTFSApSGSNSLTGTSSEIVDFRGwprlWWAVTEhmskPSRDWtap 596
Cdd:PRK06187 94 EIAYILNDAEDRVVLVDSEfvpLLAAILPQLPTVRTVIV-EGDGPAAPLAPEVGEYEE----LLAAAS----DTFDF--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 597 PRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDET-MVCVVDFkrEVGLWHAILASIFNGMKVI-- 673
Cdd:PRK06187 162 PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVyLVIVPMF--HVHAWGLPYLALMAGAKQVip 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 674 --FVPYSLMKM----NPaTWMHMV-SKYQattalvksrdlhwALLATRDHKDISLASLRtlLVADGANPWSLSSCDAFAA 746
Cdd:PRK06187 240 rrFDPENLLDLieteRV-TFFFAVpTIWQ-------------MLLKAPRAYFVDFSSLR--LVIYGGAALPPALLREFKE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 747 AFTpspyslrpdamCPCA---GSSETG-TISIRR------RGNAQLGSQsGRGILSMSalshcvVRVdtensltsltlqd 816
Cdd:PRK06187 304 KFG-----------IDLVqgyGMTETSpVVSVLPpedqlpGQWTKRRSA-GRPLPGVE------ARI------------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 817 agqivagavvvvtaIDGSNRLCQAD--EIGEICVSANSTAQLYWALDGQTHHTFkvepVGEygkligavrYVRSGLIGFM 894
Cdd:PRK06187 353 --------------VDDDGDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETI----DGG---------WLHTGDVGYI 405
|
490
....*....|.
gi 808354807 895 GPDGMVFVVAR 905
Cdd:PRK06187 406 DEDGYLYITDR 416
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
438-905 |
9.43e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 438 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEmPSSKREag 517
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALIARGV------------GPEVLVGIAMERS--AEMMVGLLAVLKAGGAYVPLD-PEYPRE-- 4638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 518 iaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLTgtsseiVDfrgwprlwwavtehmskPSRDWTAPP 597
Cdd:PRK12316 4639 --RLAYMMEDSGAALLLTQSHLLQRLP----------IPDGLASLA------LD-----------------RDEDWEGFP 4683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 598 ------RLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIfNGMK 671
Cdd:PRK12316 4684 ahdpavRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLI-NGAS 4762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 672 VIFVPYSLmkMNPATWMHMVSKYQATTALVKSrdLHWALLATRDHKDISLASLRTLLVADGANPwslssCDAFAAAFTps 751
Cdd:PRK12316 4763 VVIRDDSL--WDPERLYAEIHEHRVTVLVFPP--VYLQQLAEHAERDGEPPSLRVYCFGGEAVA-----QASYDLAWR-- 4831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 752 pySLRPDAMCPCAGSSETGTISIRRRgnAQLGSQSGRGILSMSALshcvvrvdtensLTSLtlqdAGQIvagavvvvtaI 831
Cdd:PRK12316 4832 --ALKPVYLFNGYGPTETTVTVLLWK--ARDGDACGAAYMPIGTP------------LGNR----SGYV----------L 4881
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808354807 832 DGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKligavRYVRSGLIGFMGPDGMVFVVAR 905
Cdd:PRK12316 4882 DGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGG-----RLYRTGDLARYRADGVIDYLGR 4950
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
438-752 |
1.37e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.09 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 438 QLTYGKLHSRAGKVAYMLLTKtvqvnkdgskNVMCKPGDRVALiypnTQPLHFLAAFYGCLQAGVIPVPVEmPSSKREag 517
Cdd:PRK12467 3120 QLSYAELNRRANRLAHRLIAI----------GVGPDVLVGVAV----ERSVEMIVALLAVLKAGGAYVPLD-PEYPRE-- 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 518 iaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLTgtsseiVDfRGwprLWWAVTEHmsKPSrdwtapP 597
Cdd:PRK12467 3183 --RLAYMIEDSGVKLLLTQAHLLEQLP----------APAGDTALT------LD-RL---DLNGYSEN--NPS------T 3232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 598 RLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHaILASIFNGMKVIFVPY 677
Cdd:PRK12467 3233 RVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDN 3311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808354807 678 SLmkMNPATWMHMVSKYQATTALVKSRDLHwALLAtrDHKDISLASLRTLLVADGANPwslssCDAFAAAFTPSP 752
Cdd:PRK12467 3312 DL--WDPEELWQAIHAHRISIACFPPAYLQ-QFAE--DAGGADCASLDIYVFGGEAVP-----PAAFEQVKRKLK 3376
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1079-1636 |
1.50e-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: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1079 LECLRSRAQSSPDHRILTLVtSKNAEQDTATCSTLLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGL 1158
Cdd:cd05906 12 LLELLLRAAERGPTKGITYI-DADGSEEFQSYQDLLEDARRLAAGLR-QLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1159 VPVCIKPPVASDL----NTTLGPIRMMVDmsKAVAILAPQNVSKLLKSKEAAHsidsnaWPMI--LDLEDAPSSWRRKNN 1232
Cdd:cd05906 90 VPAPLTVPPTYDEpnarLRKLRHIWQLLG--SPVVLTDAELVAEFAGLETLSG------LPGIrvLSIEELLDTAADHDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1233 NNCDTT-------TSGSSGAAskeeicyldfsinssgqlQGSSMSEASAITVCKSIKVSSELYPSR---------HVVvc 1296
Cdd:cd05906 162 PQSRPDdlallmlTSGSTGFP------------------KAVPLTHRNILARSAGKIQHNGLTPQDvflnwvpldHVG-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1297 appysgiSLVLWCLSSVYSGHHTTLIPPMEVEQQPSLFLTTLSNLKVRDAFTTystiNTCVTQLATSVENLRERGCNLSM 1376
Cdd:cd05906 222 -------GLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAP----NFAFALLNDLLEEIEDGTWDLSS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1377 LRSCVAIAEerPRIALMS-SFCKLFAPLALNNRAISTSFssrvnaaicmqGASgpEPSTVYVDARALRNDRIslvgkgaP 1455
Cdd:cd05906 291 LRYLVNAGE--AVVAKTIrRLLRLLEPYGLPPDAIRPAF-----------GMT--ETCSGVIYSRSFPTYDH-------S 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1456 HSVALIESGKLLPGVKIAIANPEtrGQCAD-SHLGEIWVasihnasplnRLASVTgfgdEGTMNTDVYNARLTTGDTktr 1534
Cdd:cd05906 349 QALEFVSLGRPIPGVSMRIVDDE--GQLLPeGEVGRLQV----------RGPVVT----KGYYNNPEANAEAFTEDG--- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1535 WARTGYLGFLRqtqsiteHGELHdavfVVGALNESLVLRGMRYHPFDVESTVSKA----HRFVGNSAVFTWN----HLVV 1606
Cdd:cd05906 410 WFRTGDLGFLD-------NGNLT----ITGRTKDTIIVNGVNYYSHEIEAAVEEVpgvePSFTAAFAVRDPGaeteELAI 478
|
570 580 590
....*....|....*....|....*....|....*
gi 808354807 1607 IAAECTGSESDALDLVPAITSAVLEE-----HHLI 1636
Cdd:cd05906 479 FFVPEYDLQDALSETLRAIRSVVSREvgvspAYLI 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
439-905 |
1.50e-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: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 439 LTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREagi 518
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGV------------AKGDRVAVLSKNS--PEFLELLFAAARLGAVFVPLNFRLTPPE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 519 aqLGFLLGNCGVKValtsescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtappr 598
Cdd:cd17631 84 --VAYILADSGAKV------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 599 LADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPys 678
Cdd:cd17631 96 LFDD-LALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILR-- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 679 lmKMNPATWMHMVSKYQATTA-LVKSrdLHWALLATRDHKDISLASLRTLLVADGANPWSL-SSCDAFAAAFtpspyslr 756
Cdd:cd17631 173 --KFDPETVLDLIERHRVTSFfLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMPERLlRALQARGVKF-------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 757 pdamCPCAGSSETG-TISIRRRGNAQ--LGSqSGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvvtaIDG 833
Cdd:cd17631 241 ----VQGYGMTETSpGVTFLSPEDHRrkLGS-AGR------PVFFVEVRI---------------------------VDP 282
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354807 834 SNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKvepvgeYGkligavrYVRSGLIGFMGPDGMVFVVAR 905
Cdd:cd17631 283 DGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR------DG-------WFHTGDLGRLDEDGYLYIVDR 341
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
438-1006 |
1.52e-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: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 438 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREag 517
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGV------------RKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPINPMLKERE-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 518 iaqLGFLLGNCGVKVALtsescykglpkkvntsstfsapsgsnsltgTSSEIVDfrgwprlwwavtehmskpsrdwtapp 597
Cdd:cd05935 65 ---LEYILNDSGAKVAV------------------------------VGSELDD-------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 598 rladetIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFvpy 677
Cdd:cd05935 86 ------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 678 sLMKMNPATWMHMVSKYQAT------TALVKsrdlhwaLLATRDHKDISLASLRTLlvadGANPWSLsscdafaaaftps 751
Cdd:cd05935 157 -MARWDRETALELIEKYKVTfwtnipTMLVD-------LLATPEFKTRDLSSLKVL----TGGGAPM------------- 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 752 pyslrPDAmcpcagssetgtISIRRRGNAQLGSQSGRGILSMSALSHCvvrvdteNSLTSLTLQDAGQIVAGAVVVVTAI 831
Cdd:cd05935 212 -----PPA------------VAEKLLKLTGLRFVEGYGLTETMSQTHT-------NPPLRPKLQCLGIP*FGVDARVIDI 267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 832 DgSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFkVEpvgeygklIGAVRYVRSGLIGFMGPDGMVFVVARRQSLLA 911
Cdd:cd05935 268 E-TGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESF-IE--------IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMIN 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 912 VSGryhsaddiiATVLAVEPMKFVYRGR----ICVFSTSvlrDER--------IVIVAEQKPNCSEEEAFDWITRVLRAI 979
Cdd:cd05935 338 VSG---------FKVWPAEVEAKLYKHPai*eVCVISVP---DERvgeevkafIVLRPEYRGKVTEEDIIEWAREQMAAY 405
|
570 580
....*....|....*....|....*..
gi 808354807 980 DTIHQVGIyccalvpANHLPKTPLGGV 1006
Cdd:cd05935 406 KYPREVEF-------VDELPRSASGKI 425
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1113-1244 |
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 808354807 1113 LLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP--PVASdlnttlgpIRMMVDMSKAVAI 1190
Cdd:TIGR01733 5 LDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPayPAER--------LAFILEDAGARLL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808354807 1191 LA-PQNVSKLLKSKEAAHSIDSNAWPMI--LDLEDAPSSWRRKNNNNCDTTTSGSSG 1244
Cdd:TIGR01733 77 LTdSALASRLAGLVLPVILLDPLELAALddAPAPPPPDAPSGPDDLAYVIYTSGSTG 133
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
426-691 |
2.81e-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: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 426 AMVLDQSAKpstQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPV 505
Cdd:cd05926 5 ALVVPGSTP---ALTYADLAELVDDLARQLAALGI------------KKGDRVAIALPNG--LEFVVAFLAAARAGAVVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 506 PVEmPSSKREagiaQLGFLLGNCGVKVALTSE----SCYKGLPKKVNTSSTFSAPSGSNSLTGTSSEIVDfrgwprlwwa 581
Cdd:cd05926 68 PLN-PAYKKA----EFEFYLADLGSKLVLTPKgelgPASRAASKLGLAILELALDVGVLIRAPSAESLSN---------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 582 vteHMSKPSRDWTAPPRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHA 661
Cdd:cd05926 133 ---LLADKKNAKSEGVPLPDD-LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVAS 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 808354807 662 ILASIFNGMKVIFVP-------YSLMKMNPATWMHMV 691
Cdd:cd05926 209 LLSTLAAGGSVVLPPrfsastfWPDVRDYNATWYTAV 245
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
438-649 |
2.91e-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: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 438 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmPSSKREag 517
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV------------GPGDRVAVYLPRSARL--VAAMLAVLKAGAAYVPLD-PDYPAD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 518 iaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsgsnsltgtsseiVDFRGWPRLWWAVTEhmsKPSRDWTAPp 597
Cdd:cd12116 75 --RLRYILEDAEPALVLTDDALPDRLP-------------------------AGLPVLLLALAAAAA---APAAPRTPV- 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 808354807 598 rlADETIAYIEYTTGNDGTVKGCCVTRQAV--FAHCRALTTAMeyKEDETMVCV 649
Cdd:cd12116 124 --SPDDLAYVIYTSGSTGRPKGVVVSHRNLvnFLHSMRERLGL--GPGDRLLAV 173
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
426-689 |
4.05e-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: 54.60 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 426 AMVLDQSakpstQLTYGKLHSRAGKVAYMLLTKTvqvnKDGsknvmckPGDRVALIYPNTQplHFLAAFYGCLQAGVIPV 505
Cdd:cd05941 4 AIVDDGD-----SITYADLVARAARLANRLLALG----KDL-------RGDRVAFLAPPSA--EYVVAQLAIWRAGGVAV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 506 PVEmpsskREAGIAQLGFLLGNcgvkvaltsescykglpkkvntsstfSAPSgsnsltgtssEIVDfrgwprlwwavteh 585
Cdd:cd05941 66 PLN-----PSYPLAELEYVITD--------------------------SEPS----------LVLD-------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 586 mskpsrdwtapprladetIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILAS 665
Cdd:cd05941 91 ------------------PALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCP 152
|
250 260
....*....|....*....|....
gi 808354807 666 IFNGMKVIFVPyslmKMNPATWMH 689
Cdd:cd05941 153 LFAGASVEFLP----KFDPKEVAI 172
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
437-725 |
4.46e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 54.58 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 437 TQLTYGKLHSRAGKVAYMLltktvqVNKDGsknvmCKPGDRVALIYPNTqPlHFLAAFYGCLQAGVIPVPVEmPSSKREa 516
Cdd:PRK08314 34 RAISYRELLEEAERLAGYL------QQECG-----VRKGDRVLLYMQNS-P-QFVIAYYAILRANAVVVPVN-PMNREE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 517 giaQLGFLLGNCGVKVALTSESCYKGLPKKVNT-----------SSTFSAPSGSN--SLTGTSSEIVDFRGWPRLWWavT 583
Cdd:PRK08314 99 ---ELAHYVTDSGARVAIVGSELAPKVAPAVGNlrlrhvivaqySDYLPAEPEIAvpAWLRAEPPLQALAPGGVVAW--K 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 584 EHMSKPSRdwtAPPRLAD-ETIAYIEYTTGNDGTVKGCCVTRQAVFAHcrALTTAMEYK--EDETMVCVVDFKREVGLWH 660
Cdd:PRK08314 174 EALAAGLA---PPPHTAGpDDLAVLPYTSGTTGVPKGCMHTHRTVMAN--AVGSVLWSNstPESVVLAVLPLFHVTGMVH 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808354807 661 AILASIFNGMKVIFVPyslmKMNPATWMHMVSKYQATtalvksrdlHWA--------LLATRDHKDISLASLR 725
Cdd:PRK08314 249 SMNAPIYAGATVVLMP----RWDREAAARLIERYRVT---------HWTniptmvvdFLASPGLAERDLSSLR 308
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
437-730 |
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 808354807 437 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLHflAAFYGCLQAGVIPVPVEmPSSKRea 516
Cdd:PRK06178 57 HVITYAELDELSDRFAALLRQRGV------------GAGDRVAVFLPNCPQFH--IVFFGILKLGAVHVPVS-PLFRE-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 517 giAQLGFLLGNCGVKVALTSESCYKgLPKKV--NTS-STFSAPSGSNSLTGTSSEIVDF--RGWPRLWWAVTEHMSKPsR 591
Cdd:PRK06178 120 --HELSYELNDAGAEVLLALDQLAP-VVEQVraETSlRHVIVTSLADVLPAEPTLPLPDslRAPRLAAAGAIDLLPAL-R 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 592 DWTAPPRLAD---ETIAYIEYTTGNDGTVKGCCVT-RQAVFAHCRALTTAMEYKEDETMvcvVDFKREvgLWHA-----I 662
Cdd:PRK06178 196 ACTAPVPLPPpalDALAALNYTGGTTGMPKGCEHTqRDMVYTAAAAYAVAVVGGEDSVF---LSFLPE--FWIAgenfgL 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 663 LASIFNGMKVIFvpysLMKMNPATWMHMVSKYQATTA--LVKSRDlhwALLATRDHKDISLASLRTLLVA 730
Cdd:PRK06178 271 LFPLFSGATLVL----LARWDAVAFMAAVERYRVTRTvmLVDNAV---ELMDHPRFAEYDLSSLRQVRVV 333
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
473-648 |
1.09e-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: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 473 KPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKREagiaQLGFLLGNCGVKVALTSEScykglpkkvntsst 552
Cdd:cd05907 28 EPGDRVAILSRNR--PEWTIADLAILAIGAVPVPI-YPTSSAE----QIAYILNDSEAKALFVEDP-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 553 fsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtapprladETIAYIEYTTGNDGTVKGCCVTRQAVFAHCR 632
Cdd:cd05907 87 -------------------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNAL 117
|
170
....*....|....*.
gi 808354807 633 ALTTAMEYKEDETMVC 648
Cdd:cd05907 118 ALAERLPATEGDRHLS 133
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
437-730 |
1.21e-06 |
|
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: 53.71 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 437 TQLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPV--EMPSskr 514
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVG------------PGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPA--- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 515 eagiAQLGFLLGNCGVKVALTSESCYKGLPKkvntsstfsapsgsnsltgtsseivdfRGWPRLWWAVTEHMSKPSRDwt 594
Cdd:COG1020 563 ----ERLAYMLEDAGARLVLTQSALAARLPE---------------------------LGVPVLALDALALAAEPATN-- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 595 APPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCV--VDFkrEVGLWhAILASIFNGMKV 672
Cdd:COG1020 610 PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW-EIFGALLSGATL 686
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 808354807 673 IFVPYSLMKmNPATWMHMVSKYQATTA-LVKSrdlHWALLAtrDHKDISLASLRTLLVA 730
Cdd:COG1020 687 VLAPPEARR-DPAALAELLARHRVTVLnLTPS---LLRALL--DAAPEALPSLRLVLVG 739
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
435-918 |
1.31e-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: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 435 PSTQLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKr 514
Cdd:cd05959 26 DAGSLTYAELEAEARRVAGALRALGVK------------REERVLLIMLDT--VDFPTAFLGAIRAGIVPVPVNTLLTP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 515 eagiAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSST------FSAPSGSNSLTGTSSEIvdfrgwprlwWAVTEHMSK 588
Cdd:cd05959 91 ----DDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHtlvvliVSGGAGPEAGALLLAEL----------VAAEAEQLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 589 PSRDWtapprlADEtIAYIEYTTGNDGTVKGccvtrqAVFAHCRALTTAMEY-------KEDETMVCVVDFKREVGLWHA 661
Cdd:cd05959 157 PAATH------ADD-PAFWLYSSGSTGRPKG------VVHLHADIYWTAELYarnvlgiREDDVCFSAAKLFFAYGLGNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 662 ILASIFNGMKVIFVPyslMKMNPATWMHMVSKYQATTaLVKSRDLHWALLATRDHKDISLASLRTLLVADGANPWSLSsc 741
Cdd:cd05959 224 LTFPLSVGATTVLMP---ERPTPAAVFKRIRRYRPTV-FFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVG-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 742 DAFAAAFTPSpyslrpdaMCPCAGSSETGTISIRRR-GNAQLGSqSGRGILSMSalshcVVRVDtensltsltlqDAGQI 820
Cdd:cd05959 298 ERWKARFGLD--------ILDGIGSTEMLHIFLSNRpGRVRYGT-TGKPVPGYE-----VELRD-----------EDGGD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 821 VAgavvvvtaidgsnrlcqADEIGEICVSANSTAQLYWALDGQTHHTFKvepvGEYGKliGAVRYVRSgligfmgPDGMV 900
Cdd:cd05959 353 VA-----------------DGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GEWTR--TGDKYVRD-------DDGFY 402
|
490
....*....|....*...
gi 808354807 901 FVVARRQSLLAVSGRYHS 918
Cdd:cd05959 403 TYAGRADDMLKVSGIWVS 420
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
403-706 |
1.53e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 53.08 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 403 NTMPRSLDSAFHRFGttaakniaamvldqsAKPST-----QLTYGKLHSRAGKVAymlltktvqvnkDGSKNVMCKPGDR 477
Cdd:PRK05605 32 TTLVDLYDNAVARFG---------------DRPALdffgaTTTYAELGKQVRRAA------------AGLRALGVRPGDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 478 VALIYPNTqPLHfLAAFYGCLQAGVIPV---PVEMPsskreagiAQLGFLLGNCGVKVAL---TSESCYKGLPKK----- 546
Cdd:PRK05605 85 VAIVLPNC-PQH-IVAFYAVLRLGAVVVehnPLYTA--------HELEHPFEDHGARVAIvwdKVAPTVERLRRTtplet 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 547 ---VNTSSTFSAP-------------SGSNSLTGTSSEIVDfrgwprlWWAVTEHMSKPSRDWTAPPRLADETIAYIEYT 610
Cdd:PRK05605 155 ivsVNMIAAMPLLqrlalrlpipalrKARAALTGPAPGTVP-------WETLVDAAIGGDGSDVSHPRPTPDDVALILYT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 611 TGNDGTVKGCCVTRQAVFAHC---RALTTAMEyKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVP-------YSLM 680
Cdd:PRK05605 228 SGTTGKPKGAQLTHRNLFANAaqgKAWVPGLG-DGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPapdidliLDAM 306
|
330 340
....*....|....*....|....*..
gi 808354807 681 KMNPATWMHMVSK-YQATTALVKSRDL 706
Cdd:PRK05605 307 KKHPPTWLPGVPPlYEKIAEAAEERGV 333
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1113-1205 |
2.97e-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: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1113 LLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikppvasDLNTTLGP--IRMMVDMSKAVAI 1190
Cdd:cd05936 30 LDALAEAFAAGLQ-NLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVV--------PLNPLYTPreLEHILNDSGAKAL 100
|
90
....*....|....*
gi 808354807 1191 LAPQNVSKLLKSKEA 1205
Cdd:cd05936 101 IVAVSFTDLLAAGAP 115
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1082-1165 |
2.18e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 49.13 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1082 LRSRAQSSPDHRILT----LVTSKNAEQDTATCSTLLKRAERIAGLLTDrARLSRGDHVALIFPPSIDLVAAFFGCLSAG 1157
Cdd:PRK09274 12 LPRAAQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNA-AGIGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
....*...
gi 808354807 1158 LVPVCIKP 1165
Cdd:PRK09274 91 AVPVLVDP 98
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1105-1621 |
4.01e-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: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1105 QDTATCSTLLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIkppvasdlNTTLGP--IRMMV 1182
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALR-ALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV--------NTLLTPddYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1183 DMSKAVAILAPQNVSKLLksKEAAHSIDSNAWPMIL---DLEDAPSSWRRknNNNCDTTTSGSSGAASKEEICYLDFSIN 1259
Cdd:cd05959 98 EDSRARVVVVSGELAPVL--AAALTKSEHTLVVLIVsggAGPEAGALLLA--ELVAAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1260 SSGQLQGssmseasAITVCKSIKVSSELYPSR-------HVVVCAP----PYsGISLVLWCLSSVysGHHTTLIP----P 1324
Cdd:cd05959 174 STGRPKG-------VVHLHADIYWTAELYARNvlgiredDVCFSAAklffAY-GLGNSLTFPLSV--GATTVLMPerptP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1325 MEV-----EQQPSLFLTtlsnlkvrdAFTTYSTIntcvtqlaTSVENLRERgcNLSMLRSCVAIAEERPrialmssfckl 1399
Cdd:cd05959 244 AAVfkrirRYRPTVFFG---------VPTLYAAM--------LAAPNLPSR--DLSSLRLCVSAGEALP----------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1400 faplalnnRAISTSFSSRVNAAIcMQGASGPEPSTVYVDARalrndrislvgkgaPHSVALIESGKLLPGVKIAIANpET 1479
Cdd:cd05959 294 --------AEVGERWKARFGLDI-LDGIGSTEMLHIFLSNR--------------PGRVRYGTTGKPVPGYEVELRD-ED 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1480 RGQCADSHLGEIWVASihnasplnrlasvtgfgdeGTMNTDVYNARLTTGDT-KTRWARTGYlGFLRQtqsitEHGELhd 1558
Cdd:cd05959 350 GGDVADGEPGELYVRG-------------------PSSATMYWNNRDKTRDTfQGEWTRTGD-KYVRD-----DDGFY-- 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354807 1559 avFVVGALNESLVLRGMRYHPFDVESTVsKAHRFVGNSAVFTWNH---------LVVIAAECTGSESDALDL 1621
Cdd:cd05959 403 --TYAGRADDMLKVSGIWVSPFEVESAL-VQHPAVLEAAVVGVEDedgltkpkaFVVLRPGYEDSEALEEEL 471
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
437-928 |
4.99e-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: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 437 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEmPSSKREA 516
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGI------------RPGDRVALMLDNC--PEFLFAWFALAKLGAVLVPIN-TALRGDE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 517 giaqLGFLLGNCGVKVALTSescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtap 596
Cdd:cd05934 67 ----LAYIIDHSGAQLVVVD------------------------------------------------------------ 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 597 prladetIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVP 676
Cdd:cd05934 83 -------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 677 yslmKMNPATWMHMVSKYQAT--TALVKSRDlhwALLAT------RDHKdislasLRTLLVAdgANPWSLSscDAFAAAF 748
Cdd:cd05934 156 ----RFSASRFWSDVRRYGATvtNYLGAMLS---YLLAQppspddRAHR------LRAAYGA--PNPPELH--EEFEERF 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 749 TpspyslrpdamCPCA---GSSETGTISIRRRGNAQLGSQSGRGIlsmsalSHCVVRVdtensltsltlqdagqivagav 825
Cdd:cd05934 219 G-----------VRLLegyGMTETIVGVIGPRDEPRRPGSIGRPA------PGYEVRI---------------------- 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 826 vvvtaIDGSNRLCQADEIGEICVSAN---STAQLYWaldGQTHHTFKVEPVGEYgkligavryvRSGLIGFMGPDGMVFV 902
Cdd:cd05934 260 -----VDDDGQELPAGEPGELVIRGLrgwGFFKGYY---NMPEATAEAMRNGWF----------HTGDLGYRDADGFFYF 321
|
490 500
....*....|....*....|....*.
gi 808354807 903 VARRQSLLAVSGRYHSADDIIATVLA 928
Cdd:cd05934 322 VDRKKDMIRRRGENISSAEVERAILR 347
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
437-738 |
6.64e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.03 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 437 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmPSSKREa 516
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGV------------GPDVLVGVAMERSIEM--VVALLAILKAGGAYVPLD-PEYPAE- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 517 giaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstFSApsgsnsltGTSSEIVDfrgWPRLWWavtehmskpSRDWTAP 596
Cdd:PRK12316 599 ---RLAYMLEDSGVQLLLSQSHLGRKLP--------LAA--------GVQVLDLD---RPAAWL---------EGYSEEN 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 597 P--RLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILAsIFNGMKVIF 674
Cdd:PRK12316 648 PgtELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVV 726
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808354807 675 VPYSLMKmNPATWMHMVSKYQATT-ALVKSrdLHWALLatRDHKDISLASLRTLLVADGANPWSL 738
Cdd:PRK12316 727 AAPGDHR-DPAKLVELINREGVDTlHFVPS--MLQAFL--QDEDVASCTSLRRIVCSGEALPADA 786
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
438-627 |
7.07e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 438 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVAlIYPNTQPlHFLAAFYGCLQAGVIPVPVEmpsskREAG 517
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYLRDKGV------------GPDVCVA-IAAERSP-QLLVGLLAILKAGGAYVPLD-----PDYP 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 518 IAQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsGSNSLTGTSSEIVDFRGWPrlwwavtehmskpsrdwTAPP 597
Cdd:PRK05691 1217 AERLAYMLADSGVELLLTQSHLLERLP-------------QAEGVSAIALDSLHLDSWP-----------------SQAP 1266
|
170 180 190
....*....|....*....|....*....|..
gi 808354807 598 RLA--DETIAYIEYTTGNDGTVKGCCVTRQAV 627
Cdd:PRK05691 1267 GLHlhGDNLAYVIYTSGSTGQPKGVGNTHAAL 1298
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
404-505 |
7.73e-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: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 404 TMPRSLDSAFHRFGTTAAkniaamVLDqsakPSTQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYP 483
Cdd:COG1021 26 TLGDLLRRRAERHPDRIA------VVD----GERRLSYAELDRRADRLAAGLLALGL------------RPGDRVVVQLP 83
|
90 100
....*....|....*....|..
gi 808354807 484 NTqpLHFLAAFYGCLQAGVIPV 505
Cdd:COG1021 84 NV--AEFVIVFFALFRAGAIPV 103
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1076-1161 |
7.73e-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: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1076 LPLLECLRSRAQSSPDHRILTlvtsknAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLS 1155
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFR 97
|
....*.
gi 808354807 1156 AGLVPV 1161
Cdd:COG1021 98 AGAIPV 103
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
438-770 |
1.52e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 46.42 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 438 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREag 517
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGL------------GPGDHVGIYARNR--IEYVEAMLGAFKARAVPVNVNYRYVEDE-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 518 iaqLGFLLGNCGVkVALTSESCYKG-----LPK--KVNTSSTFSAPSGSNSLTGTsseiVDFRGwprlwwAVTEhmSKPS 590
Cdd:PRK07798 92 ---LRYLLDDSDA-VALVYEREFAPrvaevLPRlpKLRTLVVVEDGSGNDLLPGA----VDYED------ALAA--GSPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 591 RDwtAPPRLADETiaYIEYTTGNDGTVKGccV------TRQAVFAHCRALTTamEYKEDE-------------TMVCVVD 651
Cdd:PRK07798 156 RD--FGERSPDDL--YLLYTGGTTGMPKG--VmwrqedIFRVLLGGRDFATG--EPIEDEeelakraaagpgmRRFPAPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 652 FKREVGLWhAILASIFNGMKVIFvpYSLMKMNPATWMHMVSKYQATTALVK----SRDLHWALLATRDHkDISlaSLRTl 727
Cdd:PRK07798 228 LMHGAGQW-AAFAALFSGQTVVL--LPDVRFDADEVWRTIEREKVNVITIVgdamARPLLDALEARGPY-DLS--SLFA- 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 808354807 728 lVADGANPWSLSSCDAFAAAFtpspyslrPDAMCPCA-GSSETG 770
Cdd:PRK07798 301 -IASGGALFSPSVKEALLELL--------PNVVLTDSiGSSETG 335
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1113-1170 |
2.51e-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: 2.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 808354807 1113 LLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKPPVASD 1170
Cdd:cd05935 7 LLEVVKKLASFLSNKG-VRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKER 63
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
606-730 |
2.87e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 45.71 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 606 YIEYTTGNDGTVKGccVTRQaVFAHCRALTTAMEY----KEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMK 681
Cdd:PRK10524 237 YILYTSGTTGKPKG--VQRD-TGGYAVALATSMDTifggKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTR 313
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 808354807 682 MNPATWMHMVSKYQ------ATTAL--VKSRDLhwALLATRDhkdisLASLRTLLVA 730
Cdd:PRK10524 314 PDAGIWWRIVEKYKvnrmfsAPTAIrvLKKQDP--ALLRKHD-----LSSLRALFLA 363
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
473-676 |
3.15e-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: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 473 KPGDRVALIYPNTqPLHFLAAFyGCLQAGVIPVPVEmPSSKREagiaQLGFLLGNCGVKVALTSEscyKGLPKKVNtsst 552
Cdd:COG1022 63 KPGDRVAILSDNR-PEWVIADL-AILAAGAVTVPIY-PTSSAE----EVAYILNDSGAKVLFVED---QEQLDKLL---- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 553 fSAPSGSNSLTgtssEIV--DFRGWPRLWWAVT-EHMSKPSRDWTAPPRLAD-------ETIAYIEYTTGNDGTVKGCCV 622
Cdd:COG1022 129 -EVRDELPSLR----HIVvlDPRGLRDDPRLLSlDELLALGREVADPAELEArraavkpDDLATIIYTSGTTGRPKGVML 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 808354807 623 TRQAVFAHCRALTTAMEYKEDETMVCVVDfkrevgLWH-----AILASIFNGMKVIFVP 676
Cdd:COG1022 204 THRNLLSNARALLERLPLGPGDRTLSFLP------LAHvfertVSYYALAAGATVAFAE 256
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1248-1586 |
3.19e-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: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1248 KEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEV 1327
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1328 EQQPSLFLTTLSNLKVRDAFTTYSTINTCVTQLATSVENlrerGCNLSMLRSCVAIAEErprIA--LMSSFCKLFAPLAL 1405
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKAN----DWDLSSIRMILNGAEP---IDyeLCHEFLDHMSKYGL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1406 NNRAISTSFS-SRVNAAICMQGASGPEpSTVYVDARALR-NDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGqC 1483
Cdd:cd05908 258 KRNAILPVYGlAEASVGASLPKAQSPF-KTITLGRRHVThGEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-L 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1484 ADSHLGEIWVasihnasplnRLASVTgfgdEGTMNTDVYNARLTTGDTktrWARTGYLGFLRQtqsitehGELhdavFVV 1563
Cdd:cd05908 336 PDGYIGHIQI----------RGKNVT----PGYYNNPEATAKVFTDDG---WLKTGDLGFIRN-------GRL----VIT 387
|
330 340
....*....|....*....|...
gi 808354807 1564 GALNESLVLRGMRYHPFDVESTV 1586
Cdd:cd05908 388 GREKDIIFVNGQNVYPHDIERIA 410
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1113-1165 |
4.35e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 44.95 E-value: 4.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 808354807 1113 LLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP 1165
Cdd:PRK08314 41 LLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
405-644 |
5.47e-04 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 44.75 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 405 MPRSLDSAfhrfgTTAAKNIAAMVLDQSA----KP-----STQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPG 475
Cdd:PRK06155 9 AARAVDPL-----PPSERTLPAMLARQAErypdRPllvfgGTRWTYAEAARAAAAAAHALAAAGV------------KRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 476 DRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKreagiAQLGFLLGNCGVKVaLTSEScykGLPKKVNTsstfsA 555
Cdd:PRK06155 72 DRVALMCGNR--IEFLDVFLGCAWLGAIAVPINTALRG-----PQLEHILRNSGARL-LVVEA---ALLAALEA-----A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 556 PSGSNSLTGTSseIVD---FRGWPRLWWAVtehmSKPSRDWTAPP---RLADetIAYIEYTTGNDGTVKGCCVTRQAVFA 629
Cdd:PRK06155 136 DPGDLPLPAVW--LLDapaSVSVPAGWSTA----PLPPLDAPAPAaavQPGD--TAAILYTSGTTGPSKGVCCPHAQFYW 207
|
250
....*....|....*
gi 808354807 630 HCRALTTAMEYKEDE 644
Cdd:PRK06155 208 WGRNSAEDLEIGADD 222
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
437-619 |
1.28e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 43.35 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 437 TQLTYGKLHSRAGKVAYMLltktvqvnkdgsKNVMCKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVempsSKREA 516
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGL------------RALGLREGDVVAILLENN--PEFFEVYWAARRSGLYYTPI----NWHLT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 517 GiAQLGFLLGNCGVKVALTSESC---YKGLPKkvntsstfSAPSGSNSLTGTSSEIVDFRGWPRLwwavtehmskpsRDW 593
Cdd:PRK08276 72 A-AEIAYIVDDSGAKVLIVSAALadtAAELAA--------ELPAGVPLLLVVAGPVPGFRSYEEA------------LAA 130
|
170 180
....*....|....*....|....*..
gi 808354807 594 TAPPRLADETIAY-IEYTTGNDGTVKG 619
Cdd:PRK08276 131 QPDTPIADETAGAdMLYSSGTTGRPKG 157
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
438-914 |
1.42e-03 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 43.09 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 438 QLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREag 517
Cdd:PRK07059 48 AITYGELDELSRALAAWLQSRGLA------------KGARVAIMMPNV--LQYPVAIAAVLRAGYVVVNVNPLYTPRE-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 518 iaqLGFLLGNCGVKVALTSESCYKGLPKKVNTSSTFSAPSGS-NSLTGTSSEIVDF--RGWPRL--WWAVTEH------M 586
Cdd:PRK07059 112 ---LEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASmGDLLGFKGHIVNFvvRRVKKMvpAWSLPGHvrfndaL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 587 SKPSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAME-----YKEDETMVCVVdfkrEVGLWH- 660
Cdd:PRK07059 189 AEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpafekKPRPDQLNFVC----ALPLYHi 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 661 -AILASIFNGMKV----IFVPyslmkmNPATWMHMV---SKYQATT--ALvksRDLHWALLATRDHKDISLASLRtllVA 730
Cdd:PRK07059 265 fALTVCGLLGMRTggrnILIP------NPRDIPGFIkelKKYQVHIfpAV---NTLYNALLNNPDFDKLDFSKLI---VA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 731 DG---------ANPWSLSSCDAFAAAFTPSPYSlrPDAMCPCAGSSE-TGTISirrrgnaqlgsqsgrgiLSMSAlSHCV 800
Cdd:PRK07059 333 NGggmavqrpvAERWLEMTGCPITEGYGLSETS--PVATCNPVDATEfSGTIG-----------------LPLPS-TEVS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 801 VRVDTENSLTsltlqdagqivagavvvvtaidgsnrlcqADEIGEICVSANSTAQLYWALDGQThhtfkvepvgeyGKLI 880
Cdd:PRK07059 393 IRDDDGNDLP-----------------------------LGEPGEICIRGPQVMAGYWNRPDET------------AKVM 431
|
490 500 510
....*....|....*....|....*....|....
gi 808354807 881 GAVRYVRSGLIGFMGPDGMVFVVARRQSLLAVSG 914
Cdd:PRK07059 432 TADGFFRTGDVGVMDERGYTKIVDRKKDMILVSG 465
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1113-1192 |
1.57e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 42.97 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1113 LLKRAERIAGLLtdRAR-LSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIkppvasdlNTTLGP--IRMMVDMSKAVA 1189
Cdd:PRK08276 17 LEARSNRLAHGL--RALgLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI--------NWHLTAaeIAYIVDDSGAKV 86
|
...
gi 808354807 1190 ILA 1192
Cdd:PRK08276 87 LIV 89
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1116-1583 |
1.76e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.83 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1116 RAERIAGLLTDRARLSRgdhVALIFPPSIDLVAAFFGCLSAGlVPVCIKPpvasdlnttlGPIRMMVDMSKAVAIL---A 1192
Cdd:PRK05851 40 RAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAG-AAVSILP----------GPVRGADDGRWADATLtrfA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1193 PQNVSKLLKSK---EAAHSIDSNAwpMILDLedapSSWRRKNnnncdttTSGSSGAASKEEICYLDFSINSSGQLQGSSM 1269
Cdd:PRK05851 106 GIGVRTVLSHGshlERLRAVDSSV--TVHDL----ATAAHTN-------RSASLTPPDSGGPAVLQGTAGSTGTPRTAIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1270 SEASAITVCKSIKVSSELYPSRHVVvCA--PPYSGISLVlWCLSSVYSGHHTTLIPPMEVEQQPSLFLTTLSnlkvrDAF 1347
Cdd:PRK05851 173 SPGAVLSNLRGLNARVGLDAATDVG-CSwlPLYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLS-----DSR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1348 TTYstinTCVTQLATSV---ENLRERGCNLSMLRscVAIAEERP-RIALMSSFCKLFAPLALNNRAISTSFSsrVNAAIC 1423
Cdd:PRK05851 246 ATL----TAAPNFAYNLigkYARRVSDVDLGALR--VALNGGEPvDCDGFERFATAMAPFGFDAGAAAPSYG--LAESTC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1424 mqGASGPEPSTvyvdarALRNDRISLVGKGAPHSVALIesGKLLPGVKIAIANPETRGQCADSHLGEIwvaSIHNASpln 1503
Cdd:PRK05851 318 --AVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEI---EIRGAS--- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1504 rlasvtgfgdegTMNTDVYNARLTTGDtktrWARTGYLGFLrqtqsitehgeLHDAVFVVGALNESLVLRGMRYHPFDVE 1583
Cdd:PRK05851 382 ------------MMSGYLGQAPIDPDD----WFPTGDLGYL-----------VDGGLVVCGRAKELITVAGRNIFPTEIE 434
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1078-1170 |
1.83e-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: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1078 LLECLRSRAQSSPDHRILTLVtsknAEQDTATCSTLLKRAERIAGLLtDRARLSRGDHVALIFPPSIDLVAAFFGCLSAG 1157
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADP----ARGLRLTYSELRARIEAVAARL-HARGLRPGQRVAVVLPNSVEAVIALLALHRLG 77
|
90
....*....|...
gi 808354807 1158 LVPVCIKPPVASD 1170
Cdd:cd05923 78 AVPALINPRLKAA 90
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1117-1228 |
1.94e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 42.61 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1117 AERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikpPVasdlNTTLGP--IRMMVDMSKAVAILAPQ 1194
Cdd:PRK08316 46 VNRVAAALLDLG-LKKGDRVAALGHNSDAYALLWLACARAGAVHV----PV----NFMLTGeeLAYILDHSGARAFLVDP 116
|
90 100 110
....*....|....*....|....*....|....
gi 808354807 1195 NVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWR 1228
Cdd:PRK08316 117 ALAPTAEAALALLPVDTLILSLVLGGREAPGGWL 150
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
589-769 |
2.63e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.45 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 589 PSRDWTAPPrLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEykedetmvcvVDFKREVG-----LWHA-- 661
Cdd:PRK05851 140 TNRSASLTP-PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG----------LDAATDVGcswlpLYHDmg 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 662 ---ILASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATtaLVKSRDLHWALLA--TRDHKDISLASLRTLLvaDGANPW 736
Cdd:PRK05851 209 lafLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRAT--LTAAPNFAYNLIGkyARRVSDVDLGALRVAL--NGGEPV 284
|
170 180 190
....*....|....*....|....*....|...
gi 808354807 737 SLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSET 769
Cdd:PRK05851 285 DCDGFERFATAM--APFGFDAGAAAPSYGLAES 315
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1077-1161 |
2.98e-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: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1077 PLLECLRSRAQSSPDHriLTLVTSKNaeqdTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSA 1156
Cdd:cd05920 16 PLGDLLARSAARHPDR--IAVVDGDR----RLTYRELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLRL 88
|
....*
gi 808354807 1157 GLVPV 1161
Cdd:cd05920 89 GAVPV 93
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1116-1191 |
3.32e-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: 3.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354807 1116 RAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG--LVPVCIKPPVASdlnttlgpIRMMVDMSKAVAIL 1191
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 ... |
437-535 |
4.01e-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: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 437 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmpsskREA 516
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGV------------GPGDRVALALPRSAEL--IVALLAILKAGGAYVPID-----PAY 71
|
90
....*....|....*....
gi 808354807 517 GIAQLGFLLGNCGVKVALT 535
Cdd:cd17643 72 PVERIAFILADSGPSLLLT 90
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1109-1165 |
5.33e-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: 5.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 808354807 1109 TCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP 1165
Cdd:cd05934 5 TYAELLRESARIAAALAALG-IRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT 60
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1070-1163 |
5.60e-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: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354807 1070 IDDEPSLPllECLRSRAQSSPDhRILtLVTSKNAEQDTATCSTLLKRAERIA-GLLtdRARLSRGDHVALIFPPSIDLVA 1148
Cdd:COG1022 7 VPPADTLP--DLLRRRAARFPD-RVA-LREKEDGIWQSLTWAEFAERVRALAaGLL--ALGVKPGDRVAILSDNRPEWVI 80
|
90
....*....|....*
gi 808354807 1149 AFFGCLSAGLVPVCI 1163
Cdd:COG1022 81 ADLAILAAGAVTVPI 95
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1116-1165 |
5.73e-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: 41.29 E-value: 5.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 808354807 1116 RAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP 1165
Cdd:cd05919 19 GANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP 67
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1113-1161 |
7.96e-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: 41.00 E-value: 7.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 808354807 1113 LLKRAERIAGLLtdRAR-LSRGDHVALIFPPSIDLVAAFFGCLSAG--LVPV 1161
Cdd:COG1020 507 LNARANRLAHHL--RALgVGPGDLVGVCLERSLEMVVALLAVLKAGaaYVPL 556
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1113-1161 |
9.61e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 40.66 E-value: 9.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 808354807 1113 LLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG--LVPV 1161
Cdd:PRK07656 36 LNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGavVVPL 85
|
|
| |
