|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1019-1583 |
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: 806.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1019 LYMLLNAKGVAVSTATCSQLHKRAEKITAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPH-PQNLS 1097
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1098 ATLPTVRMiiDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPA-----SIYKPPTAEMLAYLDFSV 1172
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1173 STTGMLTGVKMSHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELETSLPLWLSTL 1252
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1253 SQYKIRDTFCSYSVMELCTKGLGTQTEALKARNVNLSCVRSCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFGSRV 1332
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1333 NLAICLQGTAGPDPSTVYVDMKSLRHDRVRLVERGAPQSLPLMESGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHN 1412
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1413 ASGYYTIYGEESLQADHFN-TRLSFGDTETLWARTGYLGFVKRTELLDASGDRHDALFVVGSLDETLELRGLRYHPIDIE 1491
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPsTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1492 TSVSRAHRSIAESAVFTWTNLLVVVVELS-GSEQEALDLVPLVTNVVLKEHHLIVGVVVIVDPGVIPINSRGEKQRMHLR 1570
Cdd:cd05905 479 ATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIR 558
|
570
....*....|...
gi 688611670 1571 DSFLADQLDPIYV 1583
Cdd:cd05905 559 QAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
358-934 |
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: 730.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 358 ALTALDITGKPLYTLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPnsDPGMFWVAFYGCLLAEVIPVPIEV 437
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 438 PLsrkdaGSQQIGFLLGSCGVGLALTSEVCLKGLPKT-----PNGEIMQFKGWPRLKWVVTDTKYLTKPSKDWQPHIPTA 512
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 513 NTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWHGVLTSVMNRIHTISVPYAVM 592
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 593 KACPLSWVQRVHVHKARVALVKCRDLHWAMM------AHRDQKDTNLSSLRMLIVADGaNPWSVSSCDAFLNVFQSHGLK 666
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKdlsstlASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 667 PEmicpcASSPEAMTVAIRRPGAPGT--PLPARAILSMAGLSHGVIRVNTEDKNSALTVQDVGHVMPGALMCIVKPDGPP 744
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGTsgPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 745 mLCKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEVIPVNSGGTPIGDVPFTRTGLLGFVGPGS----------LVFVVGK 814
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTKctdlnveehdLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 815 IEGLLSVSGRRHNADDLVATALAVEPvktvYRGRIAVFSVTvfydERVVIVAEQRPdANEEDSFQWMSRVLQAIDSIHQV 894
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 688611670 895 GLYCLALVPANTLPKTPLGGIHVSETKHHFLEGSLHPCNI 934
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1009-1575 |
1.90e-74 |
|
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: 259.09 E-value: 1.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1009 WRAQTDPDHVLYMLLNAKGVAVSTATCSQLHKRAEKITAALLERGGinTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTV 1088
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1089 RPPHPqnlSATLPTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWpniIDTDDLPRKRPASIYKPPTAEM--LA 1166
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR---LLVVDLLPDTSAADWPPPSPDPddIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1167 YLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELETSLP 1246
Cdd:cd05931 153 YLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1247 LWLSTLSQYkiRDTFcsySVM-----ELCT-KGLGTQTEALkarnvNLSCVRScVVIAEERPRLALTQSFSKLFKDLGLS 1320
Cdd:cd05931 233 RWLRLISRY--RATI---SAApnfayDLCVrRVRDEDLEGL-----DLSSWRV-ALNGAEPVRPATLRRFAEAFAPFGFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1321 PRAVSTAFGsrvnLA-ICL---QGTAGPDPSTVYVDMKSLRHdRVRLVERGAPQSLPLMESGTMLPGVRVIIVNPETKGP 1396
Cdd:cd05931 302 PEAFRPSYG----LAeATLfvsGGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGRE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1397 LGDSHLGEIWVNSPHNASGYytiYGEESLQADHFNTRLsfGDTETLWARTGYLGFVKRTElldasgdrhdaLFVVGSLDE 1476
Cdd:cd05931 377 LPDGEVGEIWVRGPSVASGY---WGRPEATAETFGALA--ATDEGGWLRTGDLGFLHDGE-----------LYITGRLKD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1477 TLELRGLRYHPIDIETSVSRAHRSIAESAVFTWTNL------LVVVVELSGSeQEALDLVPLVTNV---VLKEHHLIVGV 1547
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPddgeerLVVVAEVERG-ADPADLAAIAAAIraaVAREHGVAPAD 519
|
570 580
....*....|....*....|....*...
gi 688611670 1548 VVIVDPGVIPINSRGEKQRMHLRDSFLA 1575
Cdd:cd05931 520 VVLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
348-925 |
5.64e-64 |
|
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: 228.28 E-value: 5.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 348 RWGATQAKSPALTALDITGKPLYTLTYGKLWSRSLKLAYTLLnklgtknePVLKPGDRVALVYPnsdPGM-FWVAFYGCL 426
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAP---PGLdFVAAFLGCL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 427 LAEVIPVPIEVPLSRKDAgsQQIGFLLGSCGVGLALTSEVCLKGLPKTpngeIMQFKGWPRLKWVVTDTKyLTKPSKDWQ 506
Cdd:cd05931 70 YAGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLL-PDTSAADWP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 507 PHIPTANtDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWHGVLTSVMNRIHTIS 586
Cdd:cd05931 143 PPSPDPD-DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 587 V-PYAVMKAcPLSWVQRVHVHKARV------ALVKCrdlhwAMMAHRDQKDT-NLSSLRMLIVadGANPWSVSSCDAFLN 658
Cdd:cd05931 222 MsPAAFLRR-PLRWLRLISRYRATIsaapnfAYDLC-----VRRVRDEDLEGlDLSSWRVALN--GAEPVRPATLRRFAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 659 VFQSHGLKPEMICPCASSPEA-MTVAIRRPGAPgtplPARAILSMAGLSHGViRVNTEDKNSALTVQDVGHVMPGALMCI 737
Cdd:cd05931 294 AFAPFGFRPEAFRPSYGLAEAtLFVSGGPPGTG----PVVLRVDRDALAGRA-VAVAADDPAARELVSCGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 738 VKPDGPPmLCKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEVIpvnsggTPIGDVPFTRTGLLGFVGPGSLvFVVGKIEG 817
Cdd:cd05931 369 VDPETGR-ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGAL------AATDEGGWLRTGDLGFLHDGEL-YITGRLKD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 818 LLSVSGRRHNADDLVATALAVEPVktVYRGRIAVFSVTVFYDERVVIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVGLY 897
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPA 518
|
570 580
....*....|....*....|....*...
gi 688611670 898 CLALVPANTLPKTPLGGIHVSETKHHFL 925
Cdd:cd05931 519 DVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1007-1481 |
3.52e-47 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 175.58 E-value: 3.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1007 LQWRAQTDPDHVLYMllnakGVAVSTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPV 1086
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1087 TVRPphpqnlSATLPTVRMIIDVSKAACILTTQTLmKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPASIYK-------- 1158
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDDAL-KLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAkpadvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1159 ---PPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCE----LYSSRQIAICMDPYCGLGFVLWCLSSVYSGH 1231
Cdd:pfam00501 148 pppPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1232 QSILIPPMELeTSLPLWLSTLSQYKIRDTFCSYSVMELCTKGLGTQTEALKArnvnlscVRsCVVIAEERPRLALTQSFS 1311
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSS-------LR-LVLSGGAPLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1312 KLFkdlglsPRAVSTAFGSRVNLAIClqgtagpdpstVYVDMKSLRHDRVRLVergapqslplmesGTMLPGVRVIIVNP 1391
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVV-----------TTPLPLDEDLRSLGSV-------------GRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1392 ETKGPLGDSHLGEIWVNSPHNASGYytiYGEESLQADHFntrlsfgdTETLWARTGYLGFvkrtelLDASGdrhdALFVV 1471
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGR------RDEDG----YLEIV 407
|
490
....*....|
gi 688611670 1472 GSLDETLELR 1481
Cdd:pfam00501 408 GRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1003-1581 |
3.03e-40 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 164.57 E-value: 3.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1003 LSEALQWRAQTDPDHV-LYMLLNAKGVAVsTATCSQLHKRAEKITAALLERGGIntGDNVVLLYPPGIDLIASFYGCLYA 1081
Cdd:PRK05691 11 LVQALQRRAAQTPDRLaLRFLADDPGEGV-VLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1082 GCIPVTVRPP------HPQNLSAtlptvrmIIDVSKAACILTTQTLMKTLRSKEAAASVNVktwPNIIDTDDLPrKRPAS 1155
Cdd:PRK05691 88 GVIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLD-PALAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1156 IYKPPT--AEMLAYLDFSVSTTGMLTGVKMSHSAVNAlcrsiklqCELYSSRQIAICMDP----------YCGLGFVLWC 1223
Cdd:PRK05691 157 AWQEPAlqPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1224 LSSVYSGHQSILIPPMELETSLPLWLSTLSQYkiRDT----------FCSYSVMELCTKGLgtqtealkarnvNLSCVRs 1293
Cdd:PRK05691 229 LQPIFSGVPCVLMSPAYFLERPLRWLEAISEY--GGTisggpdfayrLCSERVSESALERL------------DLSRWR- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1294 cVVIAEERP-RLALTQSFSKLFKDLGLSPRAVSTAFGSRVNLAICLQGTAGPDPSTVYVDMKSLRHDRvrlVERGAPQsl 1372
Cdd:PRK05691 294 -VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNR---AEPGTGS-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1373 PLMESGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYYTiYGEESLQAdhFNTRlsfgDTETlWARTGYLGFV 1452
Cdd:PRK05691 368 VLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR-NPEASAKT--FVEH----DGRT-WLRTGDLGFL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1453 krtelldasgdRHDALFVVGSLDETLELRGLRYHPIDIETSVSRAHRSIAES--AVFTWTNL----LVVVVELSGSEQEA 1526
Cdd:PRK05691 440 -----------RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGrvAAFAVNHQgeegIGIAAEISRSVQKI 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 688611670 1527 L---DLVPLVTNVVLKEHHLIVGVVVIVDPGVIPINSRGEKQRMHLRDSFLADQLDPI 1581
Cdd:PRK05691 509 LppqALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDSY 566
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1165-1565 |
3.24e-35 |
|
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: 138.19 E-value: 3.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1165 LAYLDFSVSTTGMLTGVKMSHSAVNALCRSIkLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELEts 1244
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1245 lpLWLSTLSQYKIRDTFCSYSVMELCTKglgtqteALKARNVNLSCVRSCVVIAEERPRlALTQSFSKLFKDlglsprAV 1324
Cdd:cd04433 79 --AALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLPP-ELLERFEEAPGI------KL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1325 STAFGSrvnlaiclqgT-AGPDPSTVYVDMKSLRHDRVrlverGAPqslplmesgtmLPGVRVIIVNPETkGPLGDSHLG 1403
Cdd:cd04433 143 VNGYGL----------TeTGGTVATGPPDDDARKPGSV-----GRP-----------VPGVEVRIVDPDG-GELPPGEIG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1404 EIWVNSPHNASGYYTiygeeslqadhfNTRLSFGDTETLWARTGYLGFVkrtelldasgDRHDALFVVGSLDETLELRGL 1483
Cdd:cd04433 196 ELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL----------DEDGYLYIVGRLKDMIKSGGE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1484 RYHPIDIETSVSRaHRSIAESAVF-----TWTNLLVVVVEL-SGSEQEALDLVPLVTNVVlkEHHLIVGVVVIVDPgvIP 1557
Cdd:cd04433 254 NVYPAEVEAVLLG-HPGVAEAAVVgvpdpEWGERVVAVVVLrPGADLDAEELRAHVRERL--APYKVPRRVVFVDA--LP 328
|
....*...
gi 688611670 1558 INSRGEKQ 1565
Cdd:cd04433 329 RTASGKID 336
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1007-1579 |
8.04e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 142.39 E-value: 8.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1007 LQWRAQTDPDHVLYMLL----NAKGVAvSTATCSQLHKRAEKITAALLERGGinTGDNVVLLYPPGIDLIASFYGCLYAG 1082
Cdd:PRK05850 7 LRERASLQPDDAAFTFIdyeqDPAGVA-ETLTWSQLYRRTLNVAEELRRHGS--TGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1083 CIPVTVRPPHPqnlSATLPTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPASIyKPPTA 1162
Cdd:PRK05850 84 LIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDA-RPRDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1163 EMLAYLDFSVSTTGMLTGVKMSHSAVNALCRsiKLQCELYSSRQIAICMD-------P-YCGLGFVLWCLSSVYSGHQSI 1234
Cdd:PRK05850 160 PSTAYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVCAPILGGCPAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1235 LIPPMELETSLPLWlstlsqykirdtfcsysvMELCTKGLGTQTEA------LKARN--------VNLSCVRsCVVIAEE 1300
Cdd:PRK05850 238 LTSPVAFLQRPARW------------------MQLLASNPHAFSAApnfafeLAVRKtsdddmagLDLGGVL-GIISGSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1301 RPRLALTQSFSKLFKDLGLSPRAVSTAFG---SRVNLAIclqGTAGPDPSTVYVDMKSLRHDRVR---------LVERGA 1368
Cdd:PRK05850 299 RVHPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKrcetgggtpLVSYGS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1369 PQSlplmesgtmlPGVRviIVNPETKGPLGDSHLGEIWVNSPHNASGYytiYGEESLQADHFNTRL---SFGDTETLWAR 1445
Cdd:PRK05850 376 PRS----------PTVR--IVDPDTCIECPAGTVGEIWVHGDNVAAGY---WQKPEETERTFGATLvdpSPGTPEGPWLR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1446 TGYLGFVkrtelldaSGdrhDALFVVGSLDETLELRGLRYHPIDIETSV---SRAhRSIAESAVFTWTNLLVVVVEL--- 1519
Cdd:PRK05850 441 TGDLGFI--------SE---GELFIVGRIKDLLIVDGRNHYPDDIEATIqeiTGG-RVAAISVPDDGTEKLVAIIELkkr 508
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611670 1520 SGSEQEALDLVPLVTNVVL----KEHHLIVGVVVIVDPGVIPINSRGEKQR-----MHLRDSFlaDQLD 1579
Cdd:PRK05850 509 GDSDEEAMDRLRTVKREVTsaisKSHGLSVADLVLVAPGSIPITTSGKIRRaacveQYRQDEF--TRLD 575
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
8-124 |
8.58e-34 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 125.99 E-value: 8.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 8 LAALPKEVREQLAELELELSEGDITQKGYEKKRAKLLAPFVPQtqnvdvsilstdstSSPITIPIAAPRQHRAHRSGGTR 87
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLH--------------PETPTKLSAEAQNQLASLETKLR 67
|
90 100 110
....*....|....*....|....*....|....*..
gi 688611670 88 DDRYRSDIHTEAVQAALARHKEEKMALPMPTKRRSAF 124
Cdd:pfam06464 68 DEELSEEVYLEKVKALLAKELERENGLNAPTKEQSGL 104
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
399-929 |
7.60e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 127.54 E-value: 7.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 399 VLKPGDRVALVYPNS-DpgmFWVAFYGCLLAEVIPVPIEVP-----LSRKDAgsqqigfLLGSCGVGLALTSEVC----- 467
Cdd:PRK07769 75 VTKPGDRVAILAPQNlD---YLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSaegvr 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 468 --LKGLPKtpngeimqfKGWPRLKWV--VTDTKYLTkpskdWQPhiPTANTDT-AYIEYKASKEGTVMGVAVSKISMLTH 542
Cdd:PRK07769 145 kfFRARPA---------KERPRVIAVdaVPDEVGAT-----WVP--PEANEDTiAYLQYTSGSTRIPAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 543 CQALTQACNYCEGETLVNVLDFKKDSGLWHGVLTSVMNRIHTISVPYAVMKAcPLSWVQRVhvhkARVALVKCRDL---- 618
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRR-PGRWIREL----ARKPGGTGGTFsaap 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 619 -----HWAM--MAHRDQKDTNLSSLRMLIvaDGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEA--MTVAIRRPGA 689
Cdd:PRK07769 284 nfafeHAAArgLPKDGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtlFVSTTPMDEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 690 PGTPLPARAILSmaglSHGVIRVNTEDKNsALTVQDVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVLNSRAGGTMYYGL 769
Cdd:PRK07769 362 PTVIYVDRDELN----AGRFVEVPADAPN-AVAQVSAGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGK 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 770 PGVTKNTFEVI------PVNSGGTPiGDVPFTRTGLLGFVGPGSLvFVVGKIEGLLSVSGRRHNADDLVATALavEPVKT 843
Cdd:PRK07769 436 PEETAATFQNIlksrlsESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--EATKA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 844 VYRGRIAVFSV-------TVFYD-------------ERVVIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVGLYCLALVP 903
Cdd:PRK07769 512 LRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVP 591
|
570 580
....*....|....*....|....*.
gi 688611670 904 ANTLPKTPLGGIHVSETKHHFLEGSL 929
Cdd:PRK07769 592 AGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1003-1580 |
1.10e-28 |
|
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: 121.46 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1003 LSEALQWRAQTDPDHVlymllnakgvAVSTA----TCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGC 1078
Cdd:COG0318 1 LADLLRRAAARHPDRP----------ALVFGgrrlTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1079 LYAGCIPVTVrpphpqNLSATLPTVRMIIDVSKAACILTtqtlmktlrskeaaasvnvktwpniidtddlprkrpasiyk 1158
Cdd:COG0318 70 LRAGAVVVPL------NPRLTAEELAYILEDSGARALVT----------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1159 pptaemlAYLDFSvS-TTGMLTGVKMSHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIP 1237
Cdd:COG0318 103 -------ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1238 PMELETslplWLSTLSQYKIrdTFCSYS---VMELCtkglgtqtEALKARNVNLSCVRsCVVIAEERPRLALTQSFSKLF 1314
Cdd:COG0318 175 RFDPER----VLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLR-LVVSGGAPLPPELLERFEERF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1315 KdlglspRAVSTAFGSrvnlaiclqgT-AGPdpsTVYVDMKSLRHDRVRLVergapqslplmesGTMLPGVRVIIVNPET 1393
Cdd:COG0318 240 G------VRIVEGYGL----------TeTSP---VVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVDEDG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1394 KgPLGDSHLGEIWVNSPHNASGYYTiYGEEslqadhfnTRLSFGDTetlWARTGYLGFvkrtelLDASGDrhdaLFVVGS 1473
Cdd:COG0318 288 R-ELPPGEVGEIVVRGPNVMKGYWN-DPEA--------TAEAFRDG---WLRTGDLGR------LDEDGY----LYIVGR 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1474 LDETLELRGLRYHPIDIETSVsRAHRSIAESAVF-----TWTNLLVVVVELsgSEQEALDLVPLVTnvVLKEH---HLIV 1545
Cdd:COG0318 345 KKDMIISGGENVYPAEVEEVL-AAHPGVAEAAVVgvpdeKWGERVVAFVVL--RPGAELDAEELRA--FLRERlarYKVP 419
|
570 580 590
....*....|....*....|....*....|....*
gi 688611670 1546 GVVVIVDPgvIPINSRGEKQRMHLRDSFLADQLDP 1580
Cdd:COG0318 420 RRVEFVDE--LPRTASGKIDRRALRERYAAGALEA 452
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1034-1580 |
2.28e-28 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 122.54 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1034 TCSQLHKRAEKITAALLERGGinTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPP----HPQNLSATL----PTVrm 1105
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1106 iidvskaacILTTQTLMKTLRSKEAAASVNVKtwPNIIDTDDLPrKRPASIYKPPTAEM--LAYLDFSVSTTGMLTGVKM 1183
Cdd:PRK12476 146 ---------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIP-DSAGESFVPVELDTddVSHLQYTSGSTRPPVGVEI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1184 SHSAVNALCRSIKLQCELYSSRQIAICMDP-YCGLGFVLWCLSSVYSGHqSILIPPMELETSLPLWLSTLSQ-YKIRDTF 1261
Cdd:PRK12476 214 THRAVGTNLVQMILSIDLLDRNTHGVSWLPlYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIKALSEgSRTGRVV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1262 CSYS--VMELCT-KGLGTQTEALKARNVNLscvrscvVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFGsrVNLAICL 1338
Cdd:PRK12476 293 TAAPnfAYEWAAqRGLPAEGDDIDLSNVVL-------IIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLF 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1339 QGTAGPD--PSTVYVDMKSLRHDRVRLVERGAPQSLPLMESGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGY 1416
Cdd:PRK12476 364 VATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGY 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1417 YTIYGEeslqadhfnTRLSFGDT----------------ETLWARTGYLGFvkrteLLDASgdrhdaLFVVGSLDETLEL 1480
Cdd:PRK12476 444 WGRPEE---------TERTFGAKlqsrlaegshadgaadDGTWLRTGDLGV-----YLDGE------LYITGRIADLIVI 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1481 RGLRYHPIDIETSVSRAHRSIAESAVFTWT------NLLVVVVELSG--SEQEALDLVPLVTNVVLKEHHLIVGVVVIVD 1552
Cdd:PRK12476 504 DGRNHYPQDIEATVAEASPMVRRGYVTAFTvpaednERLVIVAERAAgtSRADPAPAIDAIRAAVSRRHGLAVADVRLVP 583
|
570 580
....*....|....*....|....*...
gi 688611670 1553 PGVIPINSRGEKQRMHLRDSFLADQLDP 1580
Cdd:PRK12476 584 AGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
340-915 |
9.86e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 120.43 E-value: 9.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 340 PALQAALARwgaTQAKSPALTALDITGKP---LYTLTYGKLWSRSLKLAYTLlNKLGTknepvlkPGDRVALVYPNsdpG 416
Cdd:PRK05850 4 PSLLRERAS---LQPDDAAFTFIDYEQDPagvAETLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQ---G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 417 M-FWVAFYGCLLAEVIPVPIEVPLSRkdAGSQQIGFLLGSCGVGLALT-SEVClkglpktpnGEIMQF----KGWPRLKW 490
Cdd:PRK05850 70 LeYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTtSAVV---------DDVTEYvapqPGQSAPPV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 491 VVTDTKYLTKPSKdwqPHIPTAN-TDTAYIEYKASKEGTVMGVAVSKISMLTHC-QALTQACNYCEGE-----TLVNVLD 563
Cdd:PRK05850 139 IEVDLLDLDSPRG---SDARPRDlPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 564 FKKDSGLWHGVLTSVMNRIHtisvpyAVMKAcPLSWVQRvhvhKAR-VALVKCRDLHWAM-------MAHRDQKDTNLSS 635
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCP------AVLTS-PVAFLQR----PARwMQLLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 636 L---RMLIVADGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAMT-VAIRRPGAPgtplPARAILSMAGLSHGVIR 711
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEATVyVATREPGQP----PESVRFDYEKLSAGHAK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 712 VNTEDKNSALtvqdVGHVMPGA-LMCIVKPDgPPMLCKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEVIPVN-SGGTPI 789
Cdd:PRK05850 361 RCETGGGTPL----VSYGSPRSpTVRIVDPD-TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDpSPGTPE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 790 GdvPFTRTGLLGFVGPGSLvFVVGKIEGLLSVSGRRHNADDLVATalavepVKTVYRGRIAVFSVTVFYDERVVIVAE-Q 868
Cdd:PRK05850 436 G--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTEKLVAIIElK 506
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 688611670 869 RPDANEEDSFQWM----SRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGI 915
Cdd:PRK05850 507 KRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
331-927 |
3.76e-27 |
|
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: 118.15 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 331 PLGVVSNWPPALQAALARWgATQAKSPALTALDITGKPlYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVY 410
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRA-AERGPTKGITYIDADGSE-EFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 411 P-NSDpgmFWVAFYGCLLAEVIPVPIEVPLSRKDAGSQ-----QIGFLLGSCGVglaLTSEVCLKGLPKtpngeimQFKG 484
Cdd:cd05906 72 DdNED---FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELVAEFAG-------LETL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 485 WPRLKWVVTDTKYLTKPSKDWQPHIPTAnTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDF 564
Cdd:cd05906 139 SGLPGIRVLSIEELLDTAADHDLPQSRP-DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 565 KKDSGLWHGVLTSVMNRIHTISVPYAVMKACPLSWVQRVHVHKARV------ALVKCRDLhwamMAHRDQKDTNLSSLRM 638
Cdd:cd05906 218 DHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLNDL----LEEIEDGTWDLSSLRY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 639 LIVADGANpwSVSSCDAFLNVFQSHGLKPEMICPCasspeamtvairrpgapgtplparaiLSMAGLSHGVI---RVNTE 715
Cdd:cd05906 294 LVNAGEAV--VAKTIRRLLRLLEPYGLPPDAIRPA--------------------------FGMTETCSGVIysrSFPTY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 716 DKNSALTVQDVGHVMPGALMCIVKPDGPPMLckTDEIGEIVL--NSRAGGtmYYGLPGVTKNTFevipvnsggTPIGdvp 793
Cdd:cd05906 346 DHSQALEFVSLGRPIPGVSMRIVDDEGQLLP--EGEVGRLQVrgPVVTKG--YYNNPEANAEAF---------TEDG--- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 794 FTRTGLLGFVGPGSLVFvVGKIEGLLSVSGRRHNADDLVAtalAVEPVKTVYRGRIAVFSVTVFYD--ERVVIVAEqrPD 871
Cdd:cd05906 410 WFRTGDLGFLDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAetEELAIFFV--PE 483
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 872 ANEEDSfqwMSRVLQAIDSI--HQVGLYCLALVP--ANTLPKTPLGGIHVSETKHHFLEG 927
Cdd:cd05906 484 YDLQDA---LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
372-931 |
1.06e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 113.95 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 372 LTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVyPNSDPGmFWVAFYGCLLAEVIPVPIEVPLS--RKDAGSQQI 449
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLA-LG------LKPGDRVALI-AETDGD-FVEAFFACQYAGLVPVPLPLPMGfgGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 450 GFLLGSCGVGLALTSEVCLKGLPKTPNGEimqfkgwpRLKWVVTDTKYLTKPSKDWQPHIPTANtDTAYIEYKASKEGTV 529
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLHVLSHAWFKALPEADVALPRPTPD-DIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 530 MGVAVSKISMLTHCQALTQ-ACNYCEGETLVNVLDFKKDSGLWHGVLTSVMNRihtISVPYA-----VMKacPLSWVQRV 603
Cdd:PRK09192 192 RGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQ---LSVDYLptrdfARR--PLQWLDLI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 604 HVHKARVALVKC--RDLHWAMMAHRDQKDTNLSSLRmlIVADGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAmT 681
Cdd:PRK09192 267 SRNRGTISYSPPfgYELCARRVNSKDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 682 VAIrrpgapgtplparailSMAGLSHGvIRVNT------EDKNSALTVQD----------VGHVMPGALMCIVKPDGppm 745
Cdd:PRK09192 344 LAV----------------SFSPLGSG-IVVEEvdrdrlEYQGKAVAPGAetrrvrtfvnCGKALPGHEIEIRNEAG--- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 746 lcktdeigeIVLNSRAGGTMYYGLPGVTKNTFE------VIPVNSggtpigdvpFTRTGLLGFVGPGSLVfVVGKIEGLL 819
Cdd:PRK09192 404 ---------MPLPERVVGHICVRGPSLMSGYFRdeesqdVLAADG---------WLDTGDLGYLLDGYLY-ITGRAKDLI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 820 SVSGRRHNADDLVATALAVEPVKTvyrGRIAVFSVTVFYDERVVIVAEQRPdANEEDSFQWMSRVLQAIDSIHqvGLYCL 899
Cdd:PRK09192 465 IINGRNIWPQDIEWIAEQEPELRS---GDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAA 538
|
570 580 590
....*....|....*....|....*....|...
gi 688611670 900 -ALVPANTLPKTPLGGIHVSETKHHFLEGSLHP 931
Cdd:PRK09192 539 vELVPPHSLPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
988-1584 |
3.60e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 109.32 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 988 QSRKLCVWPTnmhqfLSEALQWRAQTDPDHVLYmllNAKGVAVSTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPP 1067
Cdd:PRK09192 13 LPRRYADFPT-----LVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAET 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1068 GIDLIASFYGCLYAGCIPVTVrpPHPQNL---SATLPTVRMIIDVSKAACILTTQTLMKTLrsKEAAASVNVKTWPNIID 1144
Cdd:PRK09192 84 DGDFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1145 TDDLPrkRPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSIK---LQCELySSRqiAICMDP-YCGLGFV 1220
Cdd:PRK09192 160 FKALP--EADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIShdgLKVRP-GDR--CVSWLPfYHDMGLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1221 LWCLSSVYSGHQSILIPPMELETSLPLWLSTLSqyKIRDTFcSYSV---MELCTKGLGTQTEAlkarNVNLSCVRSCVVI 1297
Cdd:PRK09192 235 GFLLTPVATQLSVDYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1298 AEE-RPRlaLTQSFSKLFKDLGLSPRAVSTAFG-SRVNLAICLqgtagPDPSTvyvDMKSLRHDRVRLVERG---APQSL 1372
Cdd:PRK09192 308 ADMiRPD--VLHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSF-----SPLGS---GIVVEEVDRDRLEYQGkavAPGAE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1373 PLMES-----GTMLPGVRVIIVNpETKGPLGDSHLGEIWVNSPHNASGYytiygeeslqadhfntrlsFGDTETL----- 1442
Cdd:PRK09192 378 TRRVRtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGY-------------------FRDEESQdvlaa 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1443 --WARTGYLGFvkrteLLDasGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVSR--AHRSiAESAVFTWTN----LLV 1514
Cdd:PRK09192 438 dgWLDTGDLGY-----LLD--GY----LYITGRAKDLIIINGRNIWPQDIEWIAEQepELRS-GDAAAFSIAQengeKIV 505
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688611670 1515 VVVELSGSEQEA-LDLVPLVTNVVLKEHHLIVgVVVIVDPGVIPINSRGEKQRMHLRDSFLADQLDPIYVA 1584
Cdd:PRK09192 506 LLVQCRISDEERrGQLIHALAALVRSEFGVEA-AVELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDVA 575
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
339-931 |
4.90e-24 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 109.06 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 339 PPA--LQAALARWGATQAKSPALTALDITGKPLYT---LTYGKLWSRslklaytlLNKLGTKNEPVLKPGDRVALVYPNs 413
Cdd:PRK12476 31 PPGttLISLIERNIANVGDTVAYRYLDHSHSAAGCaveLTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQ- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 414 dpGMFWVA-FYGCLLAEVIPVPIEVP-----LSRKDAgsqqigfLLGSCGVGLALTSEVC-------LKGLPKTpngeim 480
Cdd:PRK12476 102 --GIDYVAgFFAAIKAGTIAVPLFAPelpghAERLDT-------ALRDAEPTVVLTTTAAaeavegfLRNLPRL------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 481 qfkGWPRLKWV--VTDTKyltkpSKDWQPhIPTANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETL 558
Cdd:PRK12476 167 ---RRPRVIAIdaIPDSA-----GESFVP-VELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 559 -VNVLDFKKDSGLWHGVLTSVMNRIHTISVPYAVMKAcPLSWVQRVHV--HKARVaLVKCRDLHWAMMAHR----DQKDT 631
Cdd:PRK12476 238 gVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRR-PQRWIKALSEgsRTGRV-VTAAPNFAYEWAAQRglpaEGDDI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 632 NLSSLRMLIvadGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEA-MTVAIRRPGAPgtplPARAILSMAGLSHG-V 709
Cdd:PRK12476 316 DLSNVVLII---GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEAtLFVATIAPDAE----PSVVYLDREQLGAGrA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 710 IRVNTEDKNSALTVQdVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEV-----IPVNS 784
Cdd:PRK12476 389 VRVAADAPNAVAHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 785 --GGTPIGDVPFtRTGLLGFVGPGSLvFVVGKIEGLLSVSGRRHNADDLVATALAVEPVktVYRGRIAVFSVTVFYDERV 862
Cdd:PRK12476 467 haDGAADDGTWL-RTGDLGVYLDGEL-YITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERL 542
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611670 863 VIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGIHVSETKHHFLEGSLHP 931
Cdd:PRK12476 543 VIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1034-1550 |
7.29e-24 |
|
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: 107.30 E-value: 7.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1034 TCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCipvtvrPPHPQNLSATLPTVRMIIDVSKAA 1113
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1114 CILTTQTLMKTLRSKEAAASVNVKTW---------PNIIDTDDLPRKRPASIYKPP---TAEMLAYLDFSVSTTGMLTGV 1181
Cdd:cd05911 85 VIFTDPDGLEKVKEAAKELGPKDKIIvlddkpdgvLSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1182 KMSHS---AVNALCRSIKLQCELYSSRQIA-ICMDPYCGLGFVLWCLssvYSGHQSILIPPMELETslplWLSTLSQYKI 1257
Cdd:cd05911 165 CLSHRnliANLSQVQTFLYGNDGSNDVILGfLPLYHIYGLFTTLASL---LNGATVIIMPKFDSEL----FLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1258 RDTFCSYSVMELctkgLGTQTEALKArnvNLSCVRSCVVIAeerprlaltqsfSKLFKDLGlspravsTAFGSRVNLAIC 1337
Cdd:cd05911 238 TFLYLVPPIAAA----LAKSPLLDKY---DLSSLRVILSGG------------APLSKELQ-------ELLAKRFPNATI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1338 LQG---T-AGPdPSTVYVDmkslrhdrvRLVERGApqslplmeSGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNA 1413
Cdd:cd05911 292 KQGygmTeTGG-ILTVNPD---------GDDKPGS--------VGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1414 SGYYTiyGEESlqadhfnTRLSFgdTETLWARTGYLGFVkrtelldasgDRHDALFVVGSLDETLELRGLRYHPIDIEtS 1493
Cdd:cd05911 354 KGYYN--NPEA-------TKETF--DEDGWLHTGDIGYF----------DEDGYLYIVDRKKELIKYKGFQVAPAELE-A 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688611670 1494 VSRAHRSIAESAVF-----TWTNLLVVVVELSGSEQ-EALDLVPLVTNVVLKEHHLIVGVVVI 1550
Cdd:cd05911 412 VLLEHPGVADAAVIgipdeVSGELPRAYVVRKPGEKlTEKEVKDYVAKKVASYKQLRGGVVFV 474
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
342-913 |
1.06e-23 |
|
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: 106.43 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 342 LQAALARWGATQAKSPALTALDITgkplytLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSdPGMFwVA 421
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLA-AALRALG------VGPGDRVALLLPNS-PEFV-VA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 422 FYGCLLAEVIPVPIEVPLSRKdagsqQIGFLLGSCGVGLALTSEVCL----KGLPKtpngeimqfkgwprlkwvvtdtky 497
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVTALILYtsgtTGRPK------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 498 ltkpskdwqphiptantdtayieykaskegtvmGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWHGVLTS 577
Cdd:COG0318 117 ---------------------------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 578 VMNRIHTISVPYAVmkacPLSWVQRVHVHKA-RVALVKcrDLHWAMMAHRDQKDTNLSSLRMLIVadGANPWSVSSCDAF 656
Cdd:COG0318 164 LLAGATLVLLPRFD----PERVLELIERERVtVLFGVP--TMLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 657 LNVFQSHglkpemICPC-ASSpEAMTVAIRRPGAPGTPLPARailsmaglshgvirvntedknsaltvqdVGHVMPGALM 735
Cdd:COG0318 236 EERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 736 CIVKPDGPPmlCKTDEIGEIVLnsRAGGTM--YYGLPGVTKNTFEvipvnsGGtpigdvpFTRTGLLGFVGPGSLVFVVG 813
Cdd:COG0318 281 RIVDEDGRE--LPPGEVGEIVV--RGPNVMkgYWNDPEATAEAFR------DG-------WLRTGDLGRLDEDGYLYIVG 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 814 KIEGLLSVSGRRHNADDLVATALAVEPVKTVyrgriAVFSVTV-FYDERVV--IVAEQRPDANEEDSFQWMSRVL---QA 887
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEA-----AVVGVPDeKWGERVVafVVLRPGAELDAEELRAFLRERLaryKV 418
|
570 580
....*....|....*....|....*.
gi 688611670 888 IDSIHQVGlyclalvpanTLPKTPLG 913
Cdd:COG0318 419 PRRVEFVD----------ELPRTASG 434
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1007-1578 |
1.54e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 107.51 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1007 LQWRAQTDPDHVLYMLLN----AKGVAVSTaTCSQLHKRAEKITAALLERGgiNTGDNVVLLYPPGIDLIASFYGCLYAG 1082
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDfsteRDGVARDL-TWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1083 CIPVTV----RPPHPQNLSATLptvrmiiDVSKAACILTTQtlmktlrskEAAASVN-------VKTWPNIIDTDDLPRK 1151
Cdd:PRK07769 104 RIAVPLfdpaEPGHVGRLHAVL-------DDCTPSAILTTT---------DSAEGVRkffrarpAKERPRVIAVDAVPDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1152 rPASIYKPPTA--EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL--CRSIKLQcelYSSRQIAiCMDPYCGLGFVLWCLS 1225
Cdd:PRK07769 168 -VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLptNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGLITVLLP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1226 SVYSGHQSILIPPMELETslPL-WLSTLSQyKIRDTFCSYSV-----MELCT-KGLGTQTEAlkarNVNLSCVRsCVVIA 1298
Cdd:PRK07769 243 ALLGHYITFMSPAAFVRR--PGrWIRELAR-KPGGTGGTFSAapnfaFEHAAaRGLPKDGEP----PLDLSNVK-GLLNG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1299 EERPRLALTQSFSKLFKDLGLSPRAVSTAFGsrVNLAICLQGTAGPD--PSTVYVDMKSLRHDRVRLVERGAPQSLPLME 1376
Cdd:PRK07769 315 SEPVSPASMRKFNEAFAPYGLPPTAIKPSYG--MAEATLFVSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1377 SGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYYTiYGEESLQADH--FNTRLSFGDTE-----TLWARTGYL 1449
Cdd:PRK07769 393 AGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWG-KPEETAATFQniLKSRLSESHAEgapddALWVRTGDY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1450 G-FVKrtelldasgdrhDALFVVGSLDETLELRGLRYHPIDIETSVSRAHRSI--------------AESAVFTWTNL-- 1512
Cdd:PRK07769 472 GvYFD------------GELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALrtgyvaafsvpanqLPQVVFDDSHAgl 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1513 ----------LVVVVELS-GSEQeaLDLVPLVTNV---VLKEHHLIVGVVVIVDPGVIPINSRGEKQRMHLRDSFLADQL 1578
Cdd:PRK07769 540 kfdpedtseqLVIVAERApGAHK--LDPQPIADDIraaIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1003-1573 |
1.31e-22 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 103.90 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1003 LSEALQWRAQTDPD-HVLYMLLNAKGVAVSTAtcsQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYA 1081
Cdd:cd05906 12 LLELLLRAAERGPTkGITYIDADGSEEFQSYQ---DLLEDARRL-AAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1082 GCIPVTVRPPHP-QNLSATLPTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPAsiyKPP 1160
Cdd:cd05906 88 GFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDL---PQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1161 TAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSiKLQCELYSSRQIA---ICMDPYCGLGFVlwCLSSVYSGHQSILIP 1237
Cdd:cd05906 165 RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1238 PMELETSLPLWLSTLSQYKIRDTFCSYSvmeLCTKgLGTQTEALKARNVNLSCVRsCVVIAEERPRLALTQSFSKLFKDL 1317
Cdd:cd05906 242 TEEILADPLRWLDLIDRYRVTITWAPNF---AFAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1318 GLSPRAVSTAFGSRVNLAIClqgtagpdpsTVYVDMKSLRHdrvrlvergaPQSLPLMESGTMLPGVRVIIVNPETKGpL 1397
Cdd:cd05906 317 GLPPDAIRPAFGMTETCSGV----------IYSRSFPTYDH----------SQALEFVSLGRPIPGVSMRIVDDEGQL-L 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1398 GDSHLGEIWVNSPHNASGYytiYGEESLQADHFntrlsfgdTETLWARTGYLGFVkrtelldasgdRHDALFVVGSLDET 1477
Cdd:cd05906 376 PEGEVGRLQVRGPVVTKGY---YNNPEANAEAF--------TEDGWFRTGDLGFL-----------DNGNLTITGRTKDT 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1478 LELRGLRYHPIDIETSVSRA----HRSIAESAVF---TWTNLLVVVVELSGSEQEALD-LVPLVTNVVLKEHHLIVGVVV 1549
Cdd:cd05906 434 IIVNGVNYYSHEIEAAVEEVpgvePSFTAAFAVRdpgAETEELAIFFVPEYDLQDALSeTLRAIRSVVSREVGVSPAYLI 513
|
570 580
....*....|....*....|....
gi 688611670 1550 IVDPGVIPINSRGEKQRMHLRDSF 1573
Cdd:cd05906 514 PLPKEEIPKTSLGKIQRSKLKAAF 537
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1034-1506 |
1.15e-19 |
|
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: 93.48 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1034 TCSQLHKRAEKITAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQnlsatlPTVRMIIDVSKAA 1113
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1114 CILTTQTLMKTLRSKEAAASVNVKTWPNIIDtDDLPRKRPASiykPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCR 1193
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPVILLDPLELAALD-DAPAPPPPDA---PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1194 SIKlQCELYSSRQIAICmdpYCGLGF------VLWCLssvYSGHQSILIPPMELETSLPLWLSTLSQYKIRDTFCSYSVM 1267
Cdd:TIGR01733 151 WLA-RRYGLDPDDRVLQ---FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1268 ELCTKGLGTQTEALKArnvnlscvrscVVIAEERPRLALTQSFSKLFKDLGLspravstafgsrVNlaiclqgTAGPDPS 1347
Cdd:TIGR01733 224 ALLAAALPPALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN-------LYGPTET 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1348 TVYVDMKSLRHDRVRLVErgapqSLPLmesGTMLPGVRVIIVNPETKgPLGDSHLGEIWVNSPHNASGYytiYGEESLQA 1427
Cdd:TIGR01733 274 TVWSTATLVDPDDAPRES-----PVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTA 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611670 1428 DHFNTRLSFGDTETLWARTGYLGfvkRtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESAV 1506
Cdd:TIGR01733 342 ERFVPDPFAGGDGARLYRTGDLV---R---YLPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLRHPGVREAVV 409
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
354-832 |
5.12e-19 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 91.60 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 354 AKSPALTALDITGKplYTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSdPGMFwVAFYGCLLAEVIPV 433
Cdd:pfam00501 6 ARTPDKTALEVGEG--RRLTYRELDERANRLAAGLR-ALG------VGKGDRVAILLPNS-PEWV-VAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 434 PIEVplsrkDAGSQQIGFLLGSCGVGLALTSEVCL--KGLPKTPNGEIMQFKGW-PRLKWVVTDTKYLTKPSKDWQPHIP 510
Cdd:pfam00501 75 PLNP-----RLPAEELAYILEDSGAKVLITDDALKleELLEALGKLEVVKLVLVlDRDPVLKEEPLPEEAKPADVPPPPP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 511 TANT--DTAYIEYKASKEGTVMGVavskisMLTHCQALTQACN----------YCEGETLVNVLDFKKDSGLWHGVLTSV 578
Cdd:pfam00501 150 PPPDpdDLAYIIYTSGTTGKPKGV------MLTHRNLVANVLSikrvrprgfgLGPDDRVLSTLPLFHDFGLSLGLLGPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 579 MNRiHTISVPYAVMKACPLSWVQRVHVHKARV-----ALVKcrdlhwAMMAHRDQKDTNLSSLRMLIVadGANPWSVSSC 653
Cdd:pfam00501 224 LAG-ATVVLPPGFPALDPAALLELIERYKVTVlygvpTLLN------MLLEAGAPKRALLSSLRLVLS--GGAPLPPELA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 654 DAFLNVF-----QSHGLKpEMiCPCASSPEAMTVAIRRPGAPGTPLParailsmaglshgvirvNTEdknsaltvqdvgh 728
Cdd:pfam00501 295 RRFRELFggalvNGYGLT-ET-TGVVTTPLPLDEDLRSLGSVGRPLP-----------------GTE------------- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 729 vmpgalMCIVKPDG----PPmlcktDEIGEIVLNSRAGGTMYYGLPGVTKNTFevipVNSGgtpigdvpFTRTGLLGFVG 804
Cdd:pfam00501 343 ------VKIVDDETgepvPP-----GEPGELCVRGPGVMKGYLNDPELTAEAF----DEDG--------WYRTGDLGRRD 399
|
490 500
....*....|....*....|....*...
gi 688611670 805 PgslvfvvgkiEGLLSVSGRrhnADDLV 832
Cdd:pfam00501 400 E----------DGYLEIVGR---KKDQI 414
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
339-931 |
2.16e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.54 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 339 PPALQAALARWGATQAKSPALTALDITGKPLYTLTYGKLWSRSLKLAYTLLNKLGtknepvlkPGDRVALVYPnSDPGmF 418
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS--------FGDRAVLLFP-SGPD-Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 419 WVAFYGCLLAEVIPVPIEVPLSRKDAGSQQIGFLLGSCGVGLALTSEVCLKGLPktpngEIMQFKGWPRLKWVVTDTkYL 498
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLL-----QMEELAAANAPELLCVDT-LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 499 TKPSKDWQ-PHIPTanTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEG--ETLVNVLDFKKDSGLWHGVL 575
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 576 TSVMNRIHTISVPYAVMKACPLSWVQRVHVHKARVAlvKCRDLHWAMMAHRdQKDTNLSSL---RMLIVADGANPWSVSS 652
Cdd:PRK05691 230 QPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTIS--GGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEPIRQDS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 653 CDAFLNVFQSHGLKPEMICPCASSPEA-MTVAirrPGAPGTPLPARAILSMAglshgvIRVNTEDKNSALTVQDVGHVMP 731
Cdd:PRK05691 307 LERFAEKFAACGFDPDSFFASYGLAEAtLFVS---GGRRGQGIPALELDAEA------LARNRAEPGTGSVLMSCGRSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 732 GALMCIVKPDGPPMLcKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFevipVNSGGTpigdvPFTRTGLLGFVGPGSLvFV 811
Cdd:PRK05691 378 GHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGDLGFLRDGEL-FV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 812 VGKIEGLLSVSGRRHNADDLVATalAVEPVKTVYRGRIAVFSVTVFYDERVVIVAE-----QRPDANEEdsfqWMSRVLQ 886
Cdd:PRK05691 447 TGRLKDMLIVRGHNLYPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQA----LIKSIRQ 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 688611670 887 AIDSIHQVGLYCLALVPANTLPKTPLGGIHVSETKHHFLEGSLHP 931
Cdd:PRK05691 521 AVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDS 565
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1036-1575 |
1.23e-16 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 85.20 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1036 SQLHKRAEKITAALLERGGINTgdnVVLLYPPGIDLIASFYGCLYAG----CIPVTVRPPHPQNLSATLPTVRMIIDVSK 1111
Cdd:PRK05851 35 PEVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1112 aacILTTQTLMKTLRSKEAAASV-NVKTWPNiidtddlpRKRPASIYKPPTAEmLAYLDFSVSTTGMLTGVKMSHSAVNA 1190
Cdd:PRK05851 112 ---VLSHGSHLERLRAVDSSVTVhDLATAAH--------TNRSASLTPPDSGG-PAVLQGTAGSTGTPRTAILSPGAVLS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1191 LCRSIKLQCELYSSRQIAICMDPY---CGLGFVLwclSSVYSGHQSILIPPMELETSLPLWLSTLSQYkiRDTFCSYSVM 1267
Cdd:PRK05851 180 NLRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSDS--RATLTAAPNF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1268 ELCTKGlgtqTEALKARNVNLSCVRsCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFGsrvnLAICLQGTAGPDPS 1347
Cdd:PRK05851 255 AYNLIG----KYARRVSDVDLGALR-VALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYG----LAESTCAVTVPVPG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1348 TvyvdmkSLRHDRVRLVERGAPQSLPLMesGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYytiYGEESLQA 1427
Cdd:PRK05851 326 I------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---LGQAPIDP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1428 DHfntrlsfgdtetlWARTGYLGFvkrteLLDasgdrhDALFVVGSLDETLELRGLRYHPIDIETSVS--RAHRSIAESA 1505
Cdd:PRK05851 395 DD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERVAAqvRGVREGAVVA 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611670 1506 VFTWTNL----LVVVVELSGSEQ-----EALDLVPLVTNVVLKEhhlivgvVVIVDPGVIPINSRGEKQRMHLRDSFLA 1575
Cdd:PRK05851 451 VGTGEGSarpgLVIAAEFRGPDEagarsEVVQRVASECGVVPSD-------VVFVAPGSLPRTSSGKLRRLAVKRSLEA 522
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1028-1511 |
5.65e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 76.03 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1028 VAV----STATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLsatlptV 1103
Cdd:cd05930 4 VAVvdgdQSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1104 RMIIDVSKAACILTTQtlmktlrskeaaasvnvktwpniidtDDLprkrpasiykpptaemlAYLDFSVSTTGMLTGVKM 1183
Cdd:cd05930 77 AYILEDSGAKLVLTDP--------------------------DDL-----------------AYVIYTSGSTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1184 SHSAVNALCRSIKLQCELYSSRQIAICMdpycGLGF------VLWCLSSvysGHQSILIPPmELETSLPLWLSTLSQYKI 1257
Cdd:cd05930 114 EHRGLVNLLLWMQEAYPLTPGDRVLQFT----SFSFdvsvweIFGALLA---GATLVVLPE-EVRKDPEALADLLAEEGI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1258 RDTFCSYSVMELCTKGLGTQtealkarnvNLSCVRsCVVIAEERPRLALTQSFSKLFKDLGLspravstafgsrVNLAic 1337
Cdd:cd05930 186 TVLHLTPSLLRLLLQELELA---------ALPSLR-LVLVGGEALPPDLVRRWRELLPGARL------------VNLY-- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1338 lqgtaGPDPSTVYVDMKSLRHDRVrlvergAPQSLPLmesGTMLPGVRVIIVNPETKgPLGDSHLGEIWVNSPHNASGYy 1417
Cdd:cd05930 242 -----GPTEATVDATYYRVPPDDE------EDGRVPI---GRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLARGY- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1418 tiYGEESLQADHFnTRLSFGDTETLWaRTGYLGfvkRtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVsRA 1497
Cdd:cd05930 306 --LNRPELTAERF-VPNPFGPGERMY-RTGDLV---R---WLPDGN----LEFLGRIDDQVKIRGYRIELGEIEAAL-LA 370
|
490
....*....|....
gi 688611670 1498 HRSIAESAVFTWTN 1511
Cdd:cd05930 371 HPGVREAAVVARED 384
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1015-1491 |
4.12e-12 |
|
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: 70.59 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1015 PDHVLYMLLNAKGVAVSTatcSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVtvrpphpq 1094
Cdd:cd05908 1 PEGIIFILGDKKEKFVSY---RHLREEALGYLGALQELG-IKPGQEVVFQITHNNKFLYLFWACLLGGMIAV-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1095 nlsatlPTVRMIIDVSKaacilttqtlMKTLRSkeaaasVNVKTWPNIIDTDDLPRKRPasiykpptaEMLAYLDFSVST 1174
Cdd:cd05908 69 ------PVSIGSNEEHK----------LKLNKV------WNTLKNPYLITEEEVLCELA---------DELAFIQFSSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1175 TGMLTGVKMSHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELETSLPLWLSTLSQ 1254
Cdd:cd05908 118 TGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1255 YKIRDTFCSYSVMELCTKGLGTQtealKARNVNLSCVRscVVIAEERPRLA-LTQSFSKLFKDLGLSPRAVSTAFG-SRV 1332
Cdd:cd05908 198 HKATIVSSPNFGYKYFLKTLKPE----KANDWDLSSIR--MILNGAEPIDYeLCHEFLDHMSKYGLKRNAILPVYGlAEA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1333 NLAICLQgTAGPDPSTVYVDMKSLRH-DRVRLVERGAPQSLPLMESGTMLPGVRVIIVNPETKGpLGDSHLGEIWVNSPH 1411
Cdd:cd05908 272 SVGASLP-KAQSPFKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGHIQIRGKN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1412 NASGYYTiyGEESlqadhfnTRLSFgdTETLWARTGYLGFVKRTELLdASGDRHDALFVVGSldetlelrglRYHPIDIE 1491
Cdd:cd05908 350 VTPGYYN--NPEA-------TAKVF--TDDGWLKTGDLGFIRNGRLV-ITGREKDIIFVNGQ----------NVYPHDIE 407
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1011-1532 |
6.62e-12 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 69.58 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1011 AQTDPDHVLYMLLNAkgvavsTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGC--IPVTV 1088
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1089 RPPHPQnlsatlptVRMIIDVSKAACIlttqtlmktlrskeaaasvnvktwpnIIDTDDlprkrpasiykpptaemLAYL 1168
Cdd:cd05945 74 SSPAER--------IREILDAAKPALL--------------------------IADGDD-----------------NAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1169 DFSVSTTGMLTGVKMSHSAVNALCRSIkLQCELYSSRQIAIC----------MDPYCGL--GFVLWCLSsvysghQSILI 1236
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNqapfsfdlsvMDLYPALasGATLVPVP------RDATA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1237 PPMELETSLP-----LWLSTLsqykirdtfcsySVMELCTkGLGTQTEAlkarnvNLSCVRSCVVIAEERPrLALTQSFS 1311
Cdd:cd05945 176 DPKQLFRFLAehgitVWVSTP------------SFAAMCL-LSPTFTPE------SLPSLRHFLFCGEVLP-HKTARALQ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1312 KLFkdlglsPRAvstafgsRV-NlaiclqgTAGPDPSTVYVdmksLRHDRVRLVERGAPqSLPLmesGTMLPGVRVIIVN 1390
Cdd:cd05945 236 QRF------PDA-------RIyN-------TYGPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVILD 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1391 PETKgPLGDSHLGEIWVNSPHNASGYytiYGEESLQADHFntrlsFGDTETLWARTGYLGFvkrtelLDASGdrhdALFV 1470
Cdd:cd05945 288 EDGR-PVPPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQRAYRTGDLVR------LEADG----LLFY 348
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688611670 1471 VGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAVFTWTNL-----LVVVVELSGSEqEALDLVPL 1532
Cdd:cd05945 349 RGRLDFQVKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1034-1506 |
2.66e-11 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 68.03 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1034 TCSQLHKRAEKITAALLERGGINtGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPphpqnlSATLPTVRMIIDVSKAA 1113
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1114 CILTTQTLMKTLRSkeAAASVnvktwpniIDTDDLPrKRPASIYK---------PPTAEM----LAYLDFSVSTTGMLTG 1180
Cdd:cd05904 107 LAFTTAELAEKLAS--LALPV--------VLLDSAE-FDSLSFSDllfeadeaePPVVVIkqddVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1181 VKMSH-SAVNALCRSIKLQCELYSSRQIAICMDPYCGL-GFVLWCLSSVYSGHQSILIPPMELETslplWLSTLSQYKIR 1258
Cdd:cd05904 176 VMLTHrNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKVT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1259 DTFCSYSVMELCTKglgtqteALKARNVNLSCVRSCVViaeerprlaltqsfsklfkdlGLSP--RAVSTAFGSRVNLAI 1336
Cdd:cd05904 252 HLPVVPPIVLALVK-------SPIVDKYDLSSLRQIMS---------------------GAAPlgKELIEAFRAKFPNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1337 CLQG----TAGPDPSTVYVDMKSlrhdrvrlveRGAPQSlplmeSGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHN 1412
Cdd:cd05904 304 LGQGygmtESTGVVAMCFAPEKD----------RAKYGS-----VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1413 ASGYytiygeeslqadhfntrlsFGDTE----TL----WARTGYLGFVkrtellDASGDrhdaLFVVGSLDETLELRGLR 1484
Cdd:cd05904 369 MKGY-------------------LNNPEataaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQ 419
|
490 500
....*....|....*....|..
gi 688611670 1485 YHPIDIEtSVSRAHRSIAESAV 1506
Cdd:cd05904 420 VAPAELE-ALLLSHPEILDAAV 440
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
363-823 |
3.50e-11 |
|
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: 67.62 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 363 DITGKplyTLTYGKLWSRSLKLAYTLlNKLGtknepvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPI------- 435
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGL-RKLG------LKKGDVVGIISPNST--YYPPVFLGCLFAGGIFSAAnpiytad 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 436 EVPLSRKDAGSQqigFLLgscgvglaltseVCLKGLPKTpngeIMQFKGWPRLK--WVVTDTK-YLTKPSKDWQPHIPT- 511
Cdd:cd05911 73 ELAHQLKISKPK---VIF------------TDPDGLEKV----KEAAKELGPKDkiIVLDDKPdGVLSIEDLLSPTLGEe 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 512 ----------ANTDTAYIEYKASKEGTVMGVAVS---KISMLTHCQALTQAcNYCEGETLVNVLDFKKDSGLWhGVLTSV 578
Cdd:cd05911 134 dedlppplkdGKDDTAAILYSSGTTGLPKGVCLShrnLIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGLF-TTLASL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 579 MNRIHTIsvpyaVM-KACPLSWVQRVHVHKARVALVKCRdlHWAMMAHRDQKDT-NLSSLRMLIVadGANPWSVSSCDAF 656
Cdd:cd05911 212 LNGATVI-----IMpKFDSELFLDLIEKYKITFLYLVPP--IAAALAKSPLLDKyDLSSLRVILS--GGAPLSKELQELL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 657 LNVF------QSHGLKpEMICPCASSPEAmtvaIRRPGApgtplparailsmaglshgvirvntedknsaltvqdVGHVM 730
Cdd:cd05911 283 AKRFpnatikQGYGMT-ETGGILTVNPDG----DDKPGS------------------------------------VGRLL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 731 PGALMCIVKPDGPPMLcKTDEIGEIVLNsraGGTM---YYGLPGVTKNTFEvipvnSGGtpigdvpFTRTGLLGFVGPGS 807
Cdd:cd05911 322 PNVEAKIVDDDGKDSL-GPNEPGEICVR---GPQVmkgYYNNPEATKETFD-----EDG-------WLHTGDIGYFDEDG 385
|
490
....*....|....*.
gi 688611670 808 LVFVVGKIEGLLSVSG 823
Cdd:cd05911 386 YLYIVDRKKELIKYKG 401
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
400-913 |
4.56e-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: 67.08 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 400 LKPGDRVALVYPNSDPG---MFWVAFYGCLLAEVIpvpieVPLSrKDAGSQQIGFLLGSCGVGLALTSEVCL----KGLP 472
Cdd:cd05922 15 GVRGERVVLILPNRFTYielSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADAGAAdrlrDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 473 KTPNGEimqfkgwprlkwVVTDTKYLTKPSKDWQPHIPtANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNY 552
Cdd:cd05922 89 ASPDPG------------TVLDADGIRAARASAPAHEV-SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 553 CEGETLVNVLDFKKDSGLwhGVLTSVMNR-----IHTISV-PYAVMKACplswvqRVHvhkaRVALVKCRDLHWAMMAHR 626
Cdd:cd05922 156 TADDRALTVLPLSYDYGL--SVLNTHLLRgatlvLTNDGVlDDAFWEDL------REH----GATGLAGVPSTYAMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 627 DQKDTNLSSLRMLIVADGANPwsvsscdaflnvfqshglkpemicpcasspeAMTVAIRRPGAPGTplparAILSMAGLS 706
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLP-------------------------------QETIARLRELLPGA-----QVYVMYGQT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 707 HGVIRVNTEDKNSALTVQD-VGHVMPGALMCIVKPDGPPmlCKTDEIGEIVLNsraGGTMYYGLPgvtkNTFEVIPvnSG 785
Cdd:cd05922 268 EATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTP--TPPGEPGEIVHR---GPNVMKGYW----NDPPYRR--KE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 786 GTPIGDVpftRTGLLGFVGPGSLVFVVGKIEGLLSVSGRRHNADDLVATALAVEPVKTVyrgriAVFSVTVFYDERVVIV 865
Cdd:cd05922 337 GRGGGVL---HTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA-----AAVGLPDPLGEKLALF 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 688611670 866 AEqRPDANEEDSfqwMSRVLQAIDSIHQVGLYClalVPANTLPKTPLG 913
Cdd:cd05922 409 VT-APDKIDPKD---VLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
340-778 |
6.96e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 66.75 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 340 PALQAALARWGATqaKSPALTALDITGKplyTLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSDpgMFW 419
Cdd:PRK06187 5 PLTIGRILRHGAR--KHPDKEAVYFDGR---RTTYAELDERVNRLANALRA-LG------VKKGDRVAVFDWNSH--EYL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 420 VAFYGCLLAEVIPVPIEVPLSrkdagSQQIGFLLGSCG-----VGLALTSEVClKGLPKTPNGEimqfkgwprlKWVVTD 494
Cdd:PRK06187 71 EAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEdrvvlVDSEFVPLLA-AILPQLPTVR----------TVIVEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 495 TKYLTKPSKDWQ-------------PHIPTANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEgetlvnv 561
Cdd:PRK06187 135 DGPAAPLAPEVGeyeellaaasdtfDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 562 ldfkKDSGLwhgVLTSvMNRIHTISVPY-AVMKACPLSWVQRVH-------VHKARVALVKCRDLHWAMM-AHRDQKDTN 632
Cdd:PRK06187 208 ----DDVYL---VIVP-MFHVHAWGLPYlALMAGAKQVIPRRFDpenlldlIETERVTFFFAVPTIWQMLlKAPRAYFVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 633 LSSLRMLIVadGANPWSVSSCDAFLNVF-----QSHGLKpEMiCPCASS---PEAMTVAIRRPGAPGTPLParailsmag 704
Cdd:PRK06187 280 FSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGMT-ET-SPVVSVlppEDQLPGQWTKRRSAGRPLP--------- 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688611670 705 lshGV-IRvntedknsaltvqdvghvmpgalmcIVKPDGPPMLCKTDEIGEIVLnsRAGGTM--YYGLPGVTKNTFE 778
Cdd:PRK06187 347 ---GVeAR-------------------------IVDDDGDELPPDGGEVGEIIV--RGPWLMqgYWNRPEATAETID 393
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1011-1506 |
5.74e-10 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 63.52 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1011 AQTDPDHVLymlLNAKGVAVSTAtcsQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRP 1090
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRL-AHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1091 PHPQnlsatlPTVRMIIDVSKAACILTTQTLmkTLRSKEAAASVNVKTWPNIIDTDDLPRKRPasiykpPTAEMLAYLDF 1170
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPAL--AGELAVELVAVTLLDQPGAAAGADAEPDPA------LDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1171 SVSTTGMLTGVKMSHSAVNALCRSiklQCELYSsrqiaicMDP------YCGLGF--VLWCLSSVYSGHQSILIPPMELE 1242
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVAW---QARASS-------LGPgartlqFAGLGFdvSVQEIFSTLCAGATLVLPPEEVR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1243 TSLPLWLSTLSQYKIRDTFCSYSVME-LCtkglgtqtEALKARNVNLSCVRsCVVIAEErpRLALTQSFSKLFKDLGlsp 1321
Cdd:cd17651 214 TDPPALAAWLDEQRISRVFLPTVALRaLA--------EHGRPLGVRLAALR-YLLTGGE--QLVLTEDLREFCAGLP--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1322 ravstafGSRvnlaicLQGTAGPDPSTVyVDMKSLRHDRVRlveRGAPQSLplmesGTMLPGVRVIIVNPETKgPLGDSH 1401
Cdd:cd17651 280 -------GLR------LHNHYGPTETHV-VTALSLPGDPAA---WPAPPPI-----GRPIDNTRVYVLDAALR-PVPPGV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1402 LGEIWVNSPHNASGYYTIYG--EESLQADHFNtrlsfgdTETLWARTGYLGfvkrteLLDASGDrhdaLFVVGSLDETLE 1479
Cdd:cd17651 337 PGELYIGGAGLARGYLNRPEltAERFVPDPFV-------PGARMYRTGDLA------RWLPDGE----LEFLGRADDQVK 399
|
490 500
....*....|....*....|....*..
gi 688611670 1480 LRGLRYHPIDIETSVsRAHRSIAESAV 1506
Cdd:cd17651 400 IRGFRIELGEIEAAL-ARHPGVREAVV 425
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1028-1523 |
2.57e-09 |
|
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: 61.54 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1028 VAVS----TATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPqnlsatLPTV 1103
Cdd:cd12116 4 TAVRdddrSLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1104 RMIIDVSKAACILTTQTLMktlrskeAAASVNVKTWPNIIDTDDLPRKRPASiykPPTAEMLAYLDFSVSTTGMLTGVKM 1183
Cdd:cd12116 77 RYILEDAEPALVLTDDALP-------DRLPAGLPVLLLALAAAAAAPAAPRT---PVSPDDLAYVIYTSGSTGRPKGVVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1184 SHSAVNALCRSIKLQCELYSSRQIA----ICMDpycglgfvlwclssvysghqsILIppmeLETSLPLWlstlsqykird 1259
Cdd:cd12116 147 SHRNLVNFLHSMRERLGLGPGDRLLavttYAFD---------------------ISL----LELLLPLL----------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1260 tfcSYSVMELCTKGLGTQTEALKARnvnlscvrscvvIAEERPRLA-LTQSFSKLFKDLGLSPRAVSTAF-GSR---VNL 1334
Cdd:cd12116 191 ---AGARVVIAPRETQRDPEALARL------------IEAHSITVMqATPATWRMLLDAGWQGRAGLTALcGGEalpPDL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1335 AICLQGTA-------GPDPSTVYvdmkSLRHdRVRLVERGAPQSLPlmesgtmLPGVRVIIVNPETKgPLGDSHLGEIWV 1407
Cdd:cd12116 256 AARLLSRVgslwnlyGPTETTIW----STAA-RVTAAAGPIPIGRP-------LANTQVYVLDAALR-PVPPGVPGELYI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1408 NSPHNASGYytiYGEESLQADHFnTRLSFGDTETLWARTGYLgfVKRtelldasgDRHDALFVVGSLDETLELRGLRYHP 1487
Cdd:cd12116 323 GGDGVAQGY---LGRPALTAERF-VPDPFAGPGSRLYRTGDL--VRR--------RADGRLEYLGRADGQVKIRGHRIEL 388
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 688611670 1488 IDIETSVsRAHRSIAESAVFTWTN----LLVVVVELSGSE 1523
Cdd:cd12116 389 GEIEAAL-AAHPGVAQAAVVVREDggdrRLVAYVVLKAGA 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
342-699 |
1.00e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.74 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 342 LQAALARWGATQAKSPA------LTALDITGKP-----LY---TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVA 407
Cdd:PRK12316 4533 QQRIVALWNRTDAGYPAtrcvhqLVAERARMTPdavavVFdeeKLTYAELNRRANRLAHALI-ARG------VGPEVLVG 4605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 408 LVYPNSDPGMfwVAFYGCLLA--EVIPVPIEVPLSRkdagsqqIGFLLGSCGVGLALTSEVCLKGLPkTPNGeimqfkgw 485
Cdd:PRK12316 4606 IAMERSAEMM--VGLLAVLKAggAYVPLDPEYPRER-------LAYMMEDSGAALLLTQSHLLQRLP-IPDG-------- 4667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 486 prLKWVVTDtkyltkPSKDWQ------PHIPTANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLV 559
Cdd:PRK12316 4668 --LASLALD------RDEDWEgfpahdPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVL 4739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 560 NVLDFKKD---SGLWHGVLT--SVMNRIHTISVP---YAVMkacplswvqrvhvHKARVALVKCRDLHWAMMAHRDQKDT 631
Cdd:PRK12316 4740 QFMSFSFDgshEGLYHPLINgaSVVIRDDSLWDPerlYAEI-------------HEHRVTVLVFPPVYLQQLAEHAERDG 4806
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688611670 632 NLSSLRMLIVADGANP-------WSVSSCDAFLNVFqshGLKPEMICPCASSPEAMTVAIRRPGAPGTPLPARAI 699
Cdd:PRK12316 4807 EPPSLRVYCFGGEAVAqasydlaWRALKPVYLFNGY---GPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSG 4878
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
275-580 |
1.62e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.97 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 275 RVSTKIQQLLNTLKRPKRPPLSEFFLDDSEEIVEVPQPDPNTPRPEGRQiipvkgeplgvvsnwpPALQAALARWGATQA 354
Cdd:PRK12316 1954 RLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRG----------------PGVHQRIAEQAARAP 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 355 KSPALTALDitgkplYTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSDPGMfwVAFYGCLLA--EVIP 432
Cdd:PRK12316 2018 EAIAVVFGD------QHLSYAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERSFELV--VALLAVLKAggAYVP 2082
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 433 VPIEVPLSRkdagsqqIGFLLGSCGVGLALTSEVCLKGLPKTpngeimqfKGWPRLKwVVTDTKYLTKPSKDwqPHIPTA 512
Cdd:PRK12316 2083 LDPNYPAER-------LAYMLEDSGAALLLTQRHLLERLPLP--------AGVARLP-LDRDAEWADYPDTA--PAVQLA 2144
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688611670 513 NTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWhGVLTSVMN 580
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLN 2211
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
978-1195 |
2.34e-08 |
|
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: 59.10 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 978 RDLGLIDDQEQSRKLCVW-----PTNMHQFLSEALQWRAQTDPDHVlymllnakgvAVSTA----TCSQLHKRAEKITAA 1048
Cdd:COG1020 448 GDLPLLTAAERQQLLAEWnataaPYPADATLHELFEAQAARTPDAV----------AVVFGdqslTYAELNARANRLAHH 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1049 LLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGC--IPvtvrpphpqnLSATLPT--VRMIIDVSKAACILTTQTLMKT 1124
Cdd:COG1020 518 LRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGARLVLTQSALAAR 586
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688611670 1125 LRSKEAaasvnvktwpNIIDTDDL-----PRKRPASiykPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSI 1195
Cdd:COG1020 587 LPELGV----------PVLALDALalaaePATNPPV---PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM 649
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
973-1531 |
2.89e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 973 AQASGRDLGLIDDQEQSRKLCVWPTN---------MHQFLSEalqwRAQTDPDHVLyMLLNAKgvavsTATCSQLHKRAE 1043
Cdd:PRK12316 4518 PQRRLGELQLLEKAEQQRIVALWNRTdagypatrcVHQLVAE----RARMTPDAVA-VVFDEE-----KLTYAELNRRAN 4587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1044 KITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATlptvrMIIDvSKAACILTTQTLMK 1123
Cdd:PRK12316 4588 RLAHALIARG-VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAY-----MMED-SGAALLLTQSHLLQ 4660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1124 TLRSKEAAASVNV---KTWpniidtDDLPRKRPASiykPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCE 1200
Cdd:PRK12316 4661 RLPIPDGLASLALdrdEDW------EGFPAHDPAV---RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE 4731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1201 LYSSRQIAICMdPYCGLGFVlWCLSSVYSGHQSILIPPMELetSLPLWL-STLSQYKIRDTFCSYSVMELCTKGLGTQTE 1279
Cdd:PRK12316 4732 LTPDDRVLQFM-SFSFDGSH-EGLYHPLINGASVVIRDDSL--WDPERLyAEIHEHRVTVLVFPPVYLQQLAEHAERDGE 4807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1280 ALKARNVnlscvrscvviaeerprlaltqsfskLFKDLGLSPRAVSTAFGSRVNLAicLQGTAGPDPSTVYVdmkslRHD 1359
Cdd:PRK12316 4808 PPSLRVY--------------------------CFGGEAVAQASYDLAWRALKPVY--LFNGYGPTETTVTV-----LLW 4854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1360 RVRLVERGAPQSLPLmesGTMLPGVRVIIVNPETkGPLGDSHLGEIWVNSPHNASGYYTiygEESLQADHFNTRlSFGDT 1439
Cdd:PRK12316 4855 KARDGDACGAAYMPI---GTPLGNRSGYVLDGQL-NPLPVGVAGELYLGGEGVARGYLE---RPALTAERFVPD-PFGAP 4926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1440 ETLWARTGYLgfvkrtelldASGDRHDALFVVGSLDETLELRGLRYHPIDIETSVsRAHRSIAESavftwtnlLVVVVEL 1519
Cdd:PRK12316 4927 GGRLYRTGDL----------ARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA--------VVIAQEG 4987
|
570
....*....|..
gi 688611670 1520 SGSEQEALDLVP 1531
Cdd:PRK12316 4988 AVGKQLVGYVVP 4999
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
354-777 |
3.06e-08 |
|
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: 57.96 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 354 AKSPALTALDITGKPLytlTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSdPgMFWVAFYGCLLAEVIPV 433
Cdd:cd05936 10 RRFPDKTALIFMGRKL---TYRELDALAEAFAAGLQN-LG------VQPGDRVALMLPNC-P-QFPIAYFGALKAGAVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 434 PIEvPLSrkdaGSQQIGFLLGSCGVGLALTSEvclkglpktpngeimqfkgwPRLKWVVTDTKYLTKPskdwqphIPTAN 513
Cdd:cd05936 78 PLN-PLY----TPRELEHILNDSGAKALIVAV--------------------SFTDLLAAGAPLGERV-------ALTPE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 514 tDTAYIEYKAskeGTvmgVAVSKISMLTH---------CQALTQACNYcEGETLVNVLDFKKDSGLWHGVLTSVMNRIHT 584
Cdd:cd05936 126 -DVAVLQYTS---GT---TGVPKGAMLTHrnlvanalqIKAWLEDLLE-GDDVVLAALPLFHVFGLTVALLLPLALGATI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 585 ISVP----YAVMKACplswvqrvhvHKARV-ALVKCRDLHWAMMAHRDQKDTNLSSLRMLIvaDGANPWSVSSCDAFLNV 659
Cdd:cd05936 198 VLIPrfrpIGVLKEI----------RKHRVtIFPGVPTMYIALLNAPEFKKRDFSSLRLCI--SGGAPLPVEVAERFEEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 660 FQS-----HGLKpEMiCP--CASSPEamtvAIRRPGAPGTPLParailsmaglshgvirvNTEDKnsaltvqdvghvmpg 732
Cdd:cd05936 266 TGVpivegYGLT-ET-SPvvAVNPLD----GPRKPGSIGIPLP-----------------GTEVK--------------- 307
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 688611670 733 almcIVKPDGPPMlcKTDEIGEIVLnsRAGGTM--YYGLPGVTKNTF 777
Cdd:cd05936 308 ----IVDDDGEEL--PPGEVGELWV--RGPQVMkgYWNRPEETAEAF 346
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
531-915 |
3.09e-08 |
|
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: 57.30 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 531 GVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWhGVLTSVMNRIHTISVPyavmKACPLSWVQRVHVHKARV 610
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 611 ALVKcRDLHWAMMAHRDQKDTNLSSLRMLIVadGANPWSVSSCDAFLNVF-----QSHGLKPEMICPCASSPEAMtvaIR 685
Cdd:cd04433 92 LLGV-PTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPgiklvNGYGLTETGGTVATGPPDDD---AR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 686 RPGAPGTPLParailsmaglshgvirvNTEDKnsaltvqdvghvmpgalmcIVKPDGPPmlCKTDEIGEIVLNSRAGGTM 765
Cdd:cd04433 166 KPGSVGRPVP-----------------GVEVR-------------------IVDPDGGE--LPPGEIGELVVRGPSVMKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 766 YYGLPGVTKNTFEvipvnsGGtpigdvpFTRTGLLGFVGPGSLVFVVGKIEGLLSVSGRRHNADDLVATALAVEPVKTVy 845
Cdd:cd04433 208 YWNNPEATAAVDE------DG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEA- 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688611670 846 rgriAVFSVtvfYDER------VVIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVglyclalVPANTLPKTPLGGI 915
Cdd:cd04433 274 ----AVVGV---PDPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1003-1506 |
3.43e-08 |
|
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: 57.96 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1003 LSEALQWRAQTDPDHVLYMLLNAKgvavstATCSQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAG 1082
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK------LTYRELDALAEAF-AAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1083 CIPVTVRPphpqnlsatlptvrmiidvskaacILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPAsiykpPTA 1162
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1163 EMLAYLDFSVSTTGMLTGVKMSHSAV--NALcrsiklQC-----ELYSSRQIAICMDP-YCGLGFVLWCLSSVYSGHQSI 1234
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLvaNAL------QIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1235 LIP---PMELetslplwLSTLSQYKIrDTFCsysvmelctkGLGTQTEAL----KARNVNLSCVRSCvviaeerprlalt 1307
Cdd:cd05936 199 LIPrfrPIGV-------LKEIRKHRV-TIFP----------GVPTMYIALlnapEFKKRDFSSLRLC------------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1308 qsfsklfkdlgLS-----PRAVSTAFGSRVNLAIcLQG----TAGP----DPSTvyvdmkslRHDRVRLVergapqslpl 1374
Cdd:cd05936 248 -----------ISggaplPVEVAERFEELTGVPI-VEGygltETSPvvavNPLD--------GPRKPGSI---------- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1375 mesGTMLPGVRVIIVNPETKgPLGDSHLGEIWVNSPHNASGYYTiYGEEslqadhfnTRLSFGDTetlWARTGYLGFVkr 1454
Cdd:cd05936 298 ---GIPLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYWN-RPEE--------TAEAFVDG---WLRTGDIGYM-- 359
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 688611670 1455 tellDASG-----DRHDALFVVGsldetlelrGLRYHPIDIEtSVSRAHRSIAESAV 1506
Cdd:cd05936 360 ----DEDGyffivDRKKDMIIVG---------GFNVYPREVE-EVLYEHPAVAEAAV 402
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1034-1568 |
1.02e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 56.54 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1034 TCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCiPVTV--RPPHPQNLSA----TLPTVRMIi 1107
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGA-SLTMlhQPTPRTDLAVwaedTLRVIGMI- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1108 dvsKAACILTTQTLMktlrskeAAASVNVKTWPNIIDTDDLPRKRPASIykPPTAE-MLAYLDFSVSTTGMLTGVKMSH- 1185
Cdd:PRK07768 108 ---GAKAVVVGEPFL-------AAAPVLEEKGIRVLTVADLLAADPIDP--VETGEdDLALMQLTSGSTGSPKAVQITHg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1186 ---SAVNALCRSIKLQCElyssRQIAICMDPYC-GLGFVLWCLSSVYSGHQSILIPPMELETSLPLWLSTLSQYKIRDTF 1261
Cdd:PRK07768 176 nlyANAEAMFVAAEFDVE----TDVMVSWLPLFhDMGMVGFLTVPMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1262 CSYSVMELCTKGLGTQTEAlkaRNVNLSCVRsCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFG-SRVNLAICLQG 1340
Cdd:PRK07768 252 APNFAYALLARRLRRQAKP---GAFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGmAEATLAVSFSP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1341 T-AGPDPSTVYVDMKSLRHdRVRLVERGAPQSLPLMesGTMLPGVRVIIVNpETKGPLGDSHLGEIWVNSPHNASGYYTI 1419
Cdd:PRK07768 328 CgAGLVVDEVDADLLAALR-RAVPATKGNTRRLATL--GPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYLTM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1420 YGEESLQADHfntrlsfGdtetlWARTGYLGFvkrtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVSRAH- 1498
Cdd:PRK07768 404 DGFIPAQDAD-------G-----WLDTGDLGY------LTEEGE----VVVCGRVKDVIIMAGRNIYPTDIERAAARVEg 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1499 -RSIAESAVFTWTNL----LVVVVE--LSGSEQEALDLVPLVTNVVLKEhhliVGV----VVIVDPGVIPINSRGEKQRM 1567
Cdd:PRK07768 462 vRPGNAVAVRLDAGHsregFAVAVEsnAFEDPAEVRRIRHQVAHEVVAE----VGVrprnVVVLGPGSIPKTPSGKLRRA 537
|
.
gi 688611670 1568 H 1568
Cdd:PRK07768 538 N 538
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1034-1580 |
1.06e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.09 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1034 TCSQLHKRAEKITAALLERG-GINTGDNVVLlyPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATlptvrMIIDvSKA 1112
Cdd:PRK12467 3122 SYAELNRRANRLAHRLIAIGvGPDVLVGVAV--ERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY-----MIED-SGV 3193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1113 ACILTTQTLMKTLrskEAAASVNVKTwpniIDTDDLPRKRPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALC 1192
Cdd:PRK12467 3194 KLLLTQAHLLEQL---PAPAGDTALT----LDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHL 3266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1193 RSIKLQCELYSSRQIAICMdPYCGLGFVLWCLSSVYSGHQsILIPPMELETSLPLWlSTLSQYKIrdtfcsySVMELCTK 1272
Cdd:PRK12467 3267 CWIAEAYELDANDRVLLFM-SFSFDGAQERFLWTLICGGC-LVVRDNDLWDPEELW-QAIHAHRI-------SIACFPPA 3336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1273 GLgtQTEALKARNVNLSCVRSCVVIAEERPRLALTQSFSKLfkdlglsPRAvstafgsrvnlaiCLQGTAGPDPSTVYVD 1352
Cdd:PRK12467 3337 YL--QQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKL-------KPR-------------GLTNGYGPTEAVVTVT 3394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1353 MKSLRHDRVRLvergaPQSLPLmesGTMLPGVRVIIV----NPETKGPLGDSHLGEIWVnsphnASGYYTiygEESLQAD 1428
Cdd:PRK12467 3395 LWKCGGDAVCE-----APYAPI---GRPVAGRSIYVLdgqlNPVPVGVAGELYIGGVGL-----ARGYHQ---RPSLTAE 3458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1429 HFNTRLSFGDTETLWaRTGYLGFVKRTELLDasgdrhdalfVVGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAvft 1508
Cdd:PRK12467 3459 RFVADPFSGSGGRLY-RTGDLARYRADGVIE----------YLGRIDHQVKIRGFRIELGEIEARL-LQHPSVREAV--- 3523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688611670 1509 wtnllVVVVELSGSEQealdlvplvtnvvlkehhlIVGVVVIVDPGvipiNSRGEKQRMHLRDSfLADQLDP 1580
Cdd:PRK12467 3524 -----VLARDGAGGKQ-------------------LVAYVVPADPQ----GDWRETLRDHLAAS-LPDYMVP 3566
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
973-1195 |
2.44e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.12 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 973 AQASGRDLGLIDDQEQSRKLCVW-------PTN--MHQFLSEalqwRAQTDPDHVLymlLNAKGVAVSTAtcsQLHKRAE 1043
Cdd:PRK12316 1970 AQAALGELALLDAGERQRILADWdrtpeayPRGpgVHQRIAE----QAARAPEAIA---VVFGDQHLSYA---ELDSRAN 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1044 KITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATlptvrMIIDvSKAACILTTQTLMK 1123
Cdd:PRK12316 2040 RLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAY-----MLED-SGAALLLTQRHLLE 2112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688611670 1124 TLRSKEAAASVNVKT---WPniidtdDLPRKRPASIYKPptaEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSI 1195
Cdd:PRK12316 2113 RLPLPAGVARLPLDRdaeWA------DYPDTAPAVQLAG---ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAA 2178
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1047-1570 |
3.82e-07 |
|
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: 54.37 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1047 AALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATlpTVRMIIDVSKAACILTTQTLMKTLR 1126
Cdd:cd05922 7 ASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKES--VLRYLVADAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1127 sKEAAASVNVKTWpniIDTDDLPRKRPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCELYSSRQ 1206
Cdd:cd05922 85 -DALPASPDPGTV---LDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1207 IAICMdP--YC-GLGFVLwclSSVYSGHQSILIPPMELETSlplwlstlsqykirdtfcsysVMELCTKGLGT------Q 1277
Cdd:cd05922 161 ALTVL-PlsYDyGLSVLN---THLLRGATLVLTNDGVLDDA---------------------FWEDLREHGATglagvpS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1278 TEALKARnvnlscvrscVVIA-EERPRL-ALTQSFSKLfkdlglsPRAVSTAFGSrvnlaiclqgtAGPDpSTVYVdMKS 1355
Cdd:cd05922 216 TYAMLTR----------LGFDpAKLPSLrYLTQAGGRL-------PQETIARLRE-----------LLPG-AQVYV-MYG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1356 LRHDRVRLVERGAPQSLPLMES-GTMLPGVRVIIVNPEtKGPLGDSHLGEIWVNSPHNASGYYTIYGEEsLQADHFNTRL 1434
Cdd:cd05922 266 QTEATRRMTYLPPERILEKPGSiGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGGVL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1435 sfgdtetlwaRTGYLGFvkrtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAVF----TWT 1510
Cdd:cd05922 344 ----------HTGDLAR------RDEDGF----LFIVGRRDRMIKLFGNRISPTEIEAAA-RSIGLIIEAAAVglpdPLG 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1511 NLLVVVVELSgSEQEALDLVPLVTNVVlkEHHLIVGVVVIVDPgvIPINSRGEKQRMHLR 1570
Cdd:cd05922 403 EKLALFVTAP-DKIDPKDVLRSLAERL--PPYKVPATVRVVDE--LPLTASGKVDYAALR 457
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
996-1090 |
6.08e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 54.13 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 996 PTNMHQFLSEAlqwrAQTDPDHVLYMLLNAKG----VAVSTATCSQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDL 1071
Cdd:PRK09274 5 MANIARHLPRA----AQERPDQLAVAVPGGRGadgkLAYDELSFAELDARSDAI-AHGLNAAGIGRGMRAVLMVTPSLEF 79
|
90
....*....|....*....
gi 688611670 1072 IASFYGCLYAGCIPVTVRP 1090
Cdd:PRK09274 80 FALTFALFKAGAVPVLVDP 98
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1378-1574 |
1.00e-06 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 53.44 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1378 GTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYYTIYGEESLQADhfntrlsfgdtETLWARTGYLGFVkrtel 1457
Cdd:PLN02330 364 GFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTID-----------EDGWLHTGDIGYI----- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1458 lDASGDrhdaLFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESAVFTWTN-------LLVVVVELSGSEQEAlDLV 1530
Cdd:PLN02330 428 -DDDGD----IFIVDRIKELIKYKGFQVAPAELE-AILLTHPSVEDAAVVPLPDeeageipAACVVINPKAKESEE-DIL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 688611670 1531 PLVTNVVlkEHHLIVGVVVIVDPgvIPINSRGEKQRMHLRDSFL 1574
Cdd:PLN02330 501 NFVAANV--AHYKKVRVVQFVDS--IPKSLSGKIMRRLLKEKML 540
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1031-1505 |
1.33e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 52.85 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1031 STATCSQLHKRAEKITAALLErGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPhpqnlsatlptvrmiIDVS 1110
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTA-YGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG---------------MGRK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1111 K-AACIlttqtlmktlrsKEAAasvnvktwpniidtddlprkrPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVN 1189
Cdd:cd05910 65 NlKQCL------------QEAE---------------------PDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1190 ALCRSIKlqcELYSSRQIAICMDpycglGFVLWCLSSVYSGHQSIlIPPME----LETSLPLWLSTLSQYKIRDTFCSYS 1265
Cdd:cd05910 112 AQIDALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1266 VMELCtkglgtqTEALKARNVNLSCVRsCVVIAEERPRLALTQSFSKLfkdlgLSPRA-VSTAFGSRVNLAICLQGTagp 1344
Cdd:cd05910 183 LLERV-------ARYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEALPVSSIGS--- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1345 dpstvyvdmKSLRHDRVRLVERGAPQSLplmesGTMLPGVRVIIVnPETKGP---------LGDSHLGEIWVNSPHNASG 1415
Cdd:cd05910 247 ---------RELLATTTAATSGGAGTCV-----GRPIPGVRVRII-EIDDEPiaewddtleLPRGEIGEITVTGPTVTPT 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1416 YYTiygeeSLQADHFnTRLSFGDtETLWARTGYLGFvkrtelLDASGdrhdALFVVGSLDETLELRGLRYHPIDIEtSVS 1495
Cdd:cd05910 312 YVN-----RPVATAL-AKIDDNS-EGFWHRMGDLGY------LDDEG----RLWFCGRKAHRVITTGGTLYTEPVE-RVF 373
|
490
....*....|
gi 688611670 1496 RAHRSIAESA 1505
Cdd:cd05910 374 NTHPGVRRSA 383
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1003-1092 |
1.83e-06 |
|
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: 52.46 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1003 LSEALQWRAQTDPDHVlymllnakgvAV----STATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGC 1078
Cdd:COG1021 27 LGDLLRRRAERHPDRI----------AVvdgeRRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFAL 95
|
90
....*....|....
gi 688611670 1079 LYAGCIPVTVRPPH 1092
Cdd:COG1021 96 FRAGAIPVFALPAH 109
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
562-927 |
1.91e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 52.46 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 562 LDFKKDSG-----LWHG-----VLTSVMNRIHTISVPYAVMKACPLSWVQrvHVHKARVALVKCRDLHWAMMAH--RDQK 629
Cdd:PRK05851 190 LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLS--WLSDSRATLTAAPNFAYNLIGKyaRRVS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 630 DTNLSSLRMLIvaDGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAmTVAIRRPGaPGTplparailsmaGLShgV 709
Cdd:PRK05851 268 DVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAES-TCAVTVPV-PGI-----------GLR--V 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 710 IRVNTEDKNSALTVQDVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVLNsraGGTMYYGLpgvtkntfevipvnSGGTPI 789
Cdd:PRK05851 331 DEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGV-AGREIGEIEIR---GASMMSGY--------------LGQAPI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 790 GDVPFTRTGLLGFVGPGSLVfVVGKIEGLLSVSGRRHNADDLVATALAVEPVKtvyRGRIavfsVTVFYDE-----RVVI 864
Cdd:PRK05851 393 DPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVR---EGAV----VAVGTGEgsarpGLVI 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688611670 865 VAEQR-PDaneEDSFQwmSRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGIHVSETKHHFLEG 927
Cdd:PRK05851 465 AAEFRgPD---EAGAR--SEVVQRVASECGVVPSDVVFVAPGSLPRTSSGKLRRLAVKRSLEAA 523
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1007-1530 |
2.11e-06 |
|
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: 52.23 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1007 LQWRAQTDPDHVLYMLLNakgvavSTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPV 1086
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1087 tvrpPHPQNLSAtlPTVRMIIDVSKAACILttqtlmktlrskeaaasvnvktwpniidtDDLprkrpasiykpptaemlA 1166
Cdd:cd17631 74 ----PLNFRLTP--PEVAYILADSGAKVLF-----------------------------DDL-----------------A 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1167 YLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCELySSRQIAICMDPYC---GLGfvLWCLSSVYSGHQSILIPPMELET 1243
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1244 SLplwlSTLSQYKIRDTFcsysvmelctkGLGTQTEAL----KARNVNLSCVRsCVVIAEERPRLALTQSFsklfKDLGL 1319
Cdd:cd17631 179 VL----DLIERHRVTSFF-----------LVPTMIQALlqhpRFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1320 sprAVSTAFGsrvnlaiclQGTAGPdPSTVyvdMKSLRHDRvRLVERGAPqslplmesgtmLPGVRVIIVNPETKgPLGD 1399
Cdd:cd17631 239 ---KFVQGYG---------MTETSP-GVTF---LSPEDHRR-KLGSAGRP-----------VFFVEVRIVDPDGR-EVPP 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1400 SHLGEIWVNSPHNASGYYTiyGEESlqadhfnTRLSFGDTetlWARTGYLGFVkrtelldasgDRHDALFVVGSLDETLE 1479
Cdd:cd17631 290 GEVGEIVVRGPHVMAGYWN--RPEA-------TAAAFRDG---WFHTGDLGRL----------DEDGYLYIVDRKKDMII 347
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 688611670 1480 LRGLRYHPIDIETSVSRaHRSIAESAVF-----TWTNLLV-VVVELSGSEQEALDLV 1530
Cdd:cd17631 348 SGGENVYPAEVEDVLYE-HPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELI 403
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
329-433 |
3.42e-06 |
|
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: 51.68 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 329 GEPLGvvsnwppalqAALARWGATQAKSPALTALDitgkplYTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVAL 408
Cdd:COG1021 24 GETLG----------DLLRRRAERHPDRIAVVDGE------RRLSYAELDRRADRLAAGLL-ALG------LRPGDRVVV 80
|
90 100
....*....|....*....|....*
gi 688611670 409 VYPNSdpGMFWVAFYGCLLAEVIPV 433
Cdd:COG1021 81 QLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
373-548 |
5.20e-06 |
|
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: 50.73 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 373 TYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEV--PLSRkdagsqqIG 450
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERSAELV--VAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 451 FLLGSCGVGLALTSEvclkglpktPNGEIMQFKGWPRLKWVVTDTKYLTKPSKDWQPHIPTANTDTAYIEYKASKEGTVM 530
Cdd:TIGR01733 66 FILEDAGARLLLTDS---------ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170
....*....|....*...
gi 688611670 531 GVAVSKISMLTHCQALTQ 548
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLAR 154
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
371-492 |
9.75e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.34 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 371 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNSdPgMFWVAFYGCLLAEVIPVPIEvPLSRkdagSQQIG 450
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLLYMQNS-P-QFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 688611670 451 FLLGSCGVGLALTSEVCLkglpktpnGEIMQFKGWPRLKWVV 492
Cdd:PRK08314 102 HYVTDSGARVAIVGSELA--------PKVAPAVGNLRLRHVI 135
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
370-535 |
1.12e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 49.96 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 370 YTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEV--PLSRKDAgsq 447
Cdd:cd12114 11 GTLTYGELAERARRVA-GALKAAG------VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 448 qigfLLGSCGVGLALTSEVCLKGLPKTPNgeimqfkgwprlkwVVTDTKYLTKPSKDwQPHIPTANTDTAYIEYKASKEG 527
Cdd:cd12114 79 ----ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP-PPPVDVAPDDLAYVIFTSGSTG 139
|
....*...
gi 688611670 528 TVMGVAVS 535
Cdd:cd12114 140 TPKGVMIS 147
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1028-1569 |
1.89e-05 |
|
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: 49.23 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1028 VAVS----TATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPqnlsatLPTV 1103
Cdd:cd17643 4 VAVVdedrRLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1104 RMIIDVSKAACILTtqtlmktlrskeaaasvnvktwpniiDTDDlprkrpasiykpptaemLAYLDFSVSTTGMLTGVKM 1183
Cdd:cd17643 77 AFILADSGPSLLLT--------------------------DPDD-----------------LAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1184 SHSAVNALCRSIklQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELETS---LPLWL-----STLSQy 1255
Cdd:cd17643 114 SHANVLALFAAT--QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSpedFARLLrdegvTVLNQ- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1256 kirdTFCSYSVMELCTKGLGTQTEALKArnvnlscvrscVVIAEERPRLALTQSFSKLFKDlgLSPRAvstafgsrVNLa 1335
Cdd:cd17643 191 ----TPSAFYQLVEAADRDGRDPLALRY-----------VIFGGEALEAAMLRPWAGRFGL--DRPQL--------VNM- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1336 iclqgtAGPDPSTVYVDMKSLRHDRVRLVERGapqslPLmesGTMLPGVRVIIVNpETKGPLGDSHLGEIWVNSPHNASG 1415
Cdd:cd17643 245 ------YGITETTVHVTFRPLDAADLPAAAAS-----PI---GRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1416 YytiYGEESLQADHFNTRLSFGDTETLWaRTGYLgfVKRTelldASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVs 1495
Cdd:cd17643 310 Y---LGRPELTAERFVANPFGGPGSRMY-RTGDL--ARRL----PDGE----LEYLGRADEQVKIRGFRIELGEIEAAL- 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1496 RAHRSIAESAVFTWTN------LLVVVVELSGSEQEALDLVPLvtnvvLKEH---HLIVGVVVIVDpgVIPINSRGEKQR 1566
Cdd:cd17643 375 ATHPSVRDAAVIVREDepgdtrLVAYVVADDGAAADIAELRAL-----LKELlpdYMVPARYVPLD--ALPLTVNGKLDR 447
|
...
gi 688611670 1567 MHL 1569
Cdd:cd17643 448 AAL 450
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1037-1506 |
1.94e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 49.12 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1037 QLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNlsatlpTVRMIIDVSKAACIL 1116
Cdd:cd12117 27 ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE------RLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1117 TTQTLMKTLRSKEAAasvnvktwpniIDTDDLPRKRPASIYKPP-TAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRS- 1194
Cdd:cd12117 100 TDRSLAGRAGGLEVA-----------VVIDEALDAGPAGNPAVPvSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNt 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1195 --IKLQCELYSSRQIAICMDpycGLGFVLWclSSVYSGHQSILIPPMELETSLPLwLSTLSQYKIrdtfcsySVMELcTK 1272
Cdd:cd12117 169 nyVTLGPDDRVLQTSPLAFD---ASTFEIW--GALLNGARLVLAPKGTLLDPDAL-GALIAEEGV-------TVLWL-TA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1273 GLGTQtealkarnvnlscvrscvvIAEERPrlaltQSFSKLFKDL-G---LSPRAVSTAfgsrvnLAIC----LQGTAGP 1344
Cdd:cd12117 235 ALFNQ-------------------LADEDP-----ECFAGLRELLtGgevVSPPHVRRV------LAACpglrLVNGYGP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1345 DPSTVYvdmkSLRHdrvrLVERGAPQ--SLPLmesGTMLPGVRVIIVNpETKGPLGDSHLGEIWVNSPHNASGYytiYGE 1422
Cdd:cd12117 285 TENTTF----TTSH----VVTELDEVagSIPI---GRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGY---LNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1423 ESLQADHFnTRLSFGDTETLWaRTGYLgfVKRTElldasgdrhDALFV-VGSLDETLELRGLRYHPIDIETSVsRAHRSI 1501
Cdd:cd12117 350 PALTAERF-VADPFGPGERLY-RTGDL--ARWLP---------DGRLEfLGRIDDQVKIRGFRIELGEIEAAL-RAHPGV 415
|
....*
gi 688611670 1502 AESAV 1506
Cdd:cd12117 416 REAVV 420
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
354-441 |
2.52e-05 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 48.78 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 354 AKSPALTALDITGKplyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVAlVYPNSDPGMFwVAFYGCLLA--EVI 431
Cdd:cd05945 2 AANPDRPAVVEGGR---TLTYRELKERADALA-AALASLG------LDAGDPVV-VYGHKSPDAI-AAFLAALKAghAYV 69
|
90
....*....|
gi 688611670 432 PVPIEVPLSR 441
Cdd:cd05945 70 PLDASSPAER 79
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1009-1188 |
3.22e-05 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 48.43 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1009 WRAQTD--PDHVLymlLNAKGVAVSTAtcsQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPV 1086
Cdd:cd17646 4 VAEQAArtPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1087 TVRPPHPQnlsatlPTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPASiykpptaemLA 1166
Cdd:cd17646 77 PLDPGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDN---------LA 141
|
170 180
....*....|....*....|..
gi 688611670 1167 YLDFSVSTTGMLTGVKMSHSAV 1188
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHAGI 163
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
345-435 |
3.26e-05 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 48.57 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 345 ALARWGATQAKSPALTALDITGKPlYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSdPgMFWVAFYG 424
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDGEE-RTLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI-P-EAVIAMLA 83
|
90
....*....|.
gi 688611670 425 CLLAEVIPVPI 435
Cdd:COG0365 84 CARIGAVHSPV 94
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
347-457 |
4.81e-05 |
|
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: 47.60 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 347 ARWGATQakSPALTALDITGKplyTLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSDPgmFWVAFYGCL 426
Cdd:cd17631 1 LRRRARR--HPDRTALVFGGR---SLTYAELDERVNRLAHALRA-LG------VAKGDRVAVLSKNSPE--FLELLFAAA 66
|
90 100 110
....*....|....*....|....*....|.
gi 688611670 427 LAEVIPVPIEVPLSRKDagsqqIGFLLGSCG 457
Cdd:cd17631 67 RLGAVFVPLNFRLTPPE-----VAYILADSG 92
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1011-1185 |
6.18e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 47.58 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1011 AQTDPDHVLYMLLNAkgvavsTATCSQLHKRAEKITAALLERGgiNTGDNVVLLY----PpgiDLIASFYGCLYAGC--I 1084
Cdd:PRK04813 12 AQTQPDFPAYDYLGE------KLTYGQLKEDSDALAAFIDSLK--LPDKSPIIVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1085 PVTVRPPhpqnlsatLPTVRMIIDVSKAACILTTQTLMKTLrskeaaasVNVKtwpnIIDTDDLprkrPASIYKPPTAEM 1164
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIATEELPLEI--------LGIP----VITLDEL----KDIFATGNPYDF 136
|
170 180
....*....|....*....|....*....
gi 688611670 1165 LA--------YLDFSVSTTGMLTGVKMSH 1185
Cdd:PRK04813 137 DHavkgddnyYIIFTSGTTGKPKGVQISH 165
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1046-1507 |
6.60e-05 |
|
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: 47.31 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1046 TAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPvtvrppHPQNLSATLPTVRMIIDVSKAACILT-TQTLMKT 1124
Cdd:cd05926 27 LARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVV------APLNPAYKKAEFEFYLADLGSKLVLTpKGELGPA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1125 LRSKE------AAASVNVKTWPNIIDTDDLP----RKRPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSH----SAVNA 1190
Cdd:cd05926 101 SRAASklglaiLELALDVGVLIRAPSAESLSnllaDKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHrnlaASATN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1191 LCRSIKLqcelySSRQIAICMDP-YCGLGFVLWCLSSVYSGhQSILIPPMELETSL--------PLWLS---TLSQYKIR 1258
Cdd:cd05926 181 ITNTYKL-----TPDDRTLVVMPlFHVHGLVASLLSTLAAG-GSVVLPPRFSASTFwpdvrdynATWYTavpTIHQILLN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1259 DTfcsysvmelctkglGTQTEALKARnvnLSCVRSCvviaeerprlaltqSFSklfkdlgLSP---RAVSTAFGSRVNLA 1335
Cdd:cd05926 255 RP--------------EPNPESPPPK---LRFIRSC--------------SAS-------LPPavlEALEATFGAPVLEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1336 I-----CLQGTAGPdpstvyvdmksLRHDRVRLVERGAPQslplmesgtmlpGVRVIIVNpETKGPLGDSHLGEIWVNSP 1410
Cdd:cd05926 297 YgmteaAHQMTSNP-----------LPPGPRKPGSVGKPV------------GVEVRILD-EDGEILPPGVVGEICLRGP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1411 HNASGYYtiygeeslqADHFNTRLSFgdTETLWARTGYLGFvkrtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDI 1490
Cdd:cd05926 353 NVTRGYL---------NNPEANAEAA--FKDGWFRTGDLGY------LDADGY----LFLTGRIKELINRGGEKISPLEV 411
|
490
....*....|....*..
gi 688611670 1491 EtSVSRAHRSIAESAVF 1507
Cdd:cd05926 412 D-GVLLSHPAVLEAVAF 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
971-1506 |
9.81e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.64 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 971 RIAQASGRDLGLIDDQEQSRKL-------CVWPTN--MHQFLSEALQwraqtdpdhvlymlLNAKGVAVS----TATCSQ 1037
Cdd:PRK12316 476 ENPQARVDELPMLDAEERGQLVegwnataAEYPLQrgVHRLFEEQVE--------------RTPEAPALAfgeeTLDYAE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1038 LHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATLptvrmiIDVSKAACILT 1117
Cdd:PRK12316 542 LNRRANRLAHALIERG-VGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYM------LEDSGVQLLLS 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1118 TQTLMKTLrskEAAASVNVktwpniIDTDDLPRKRPASIYKPP----TAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCR 1193
Cdd:PRK12316 615 QSHLGRKL---PLAAGVQV------LDLDRPAAWLEGYSEENPgtelNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLC 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1194 SIKLQCELYSSRQIA----ICMDpyCGLGFVLWCLSsvySGHQSILIPPMELETSLPLWlSTLSQYKIRdtfcsysVMEL 1269
Cdd:PRK12316 686 WMQQAYGLGVGDTVLqktpFSFD--VSVWEFFWPLM---SGARLVVAAPGDHRDPAKLV-ELINREGVD-------TLHF 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1270 CTKGLgtQTEALKARNVNLSCVRSCVVIAEERPRLALTQSFSKLFKdlglspravstafGSRVNLaiclqgtAGPDPSTV 1349
Cdd:PRK12316 753 VPSML--QAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQ-------------AGLYNL-------YGPTEAAI 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1350 YVDMKSLRHDRVRLVERGAPqslplmesgtmLPGVRVIIVNPETkGPLGDSHLGEIWVNSPHNASGYytiYGEESLQADH 1429
Cdd:PRK12316 811 DVTHWTCVEEGGDSVPIGRP-----------IANLACYILDANL-EPVPVGVLGELYLAGRGLARGY---HGRPGLTAER 875
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688611670 1430 FnTRLSFGDTETLWaRTGYLGFVKRTELLDasgdrhdalfVVGSLDETLELRGLRYHPIDIETSVSRaHRSIAESAV 1506
Cdd:PRK12316 876 F-VPSPFVAGERMY-RTGDLARYRADGVIE----------YAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAV 939
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1003-1198 |
1.10e-04 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 47.02 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1003 LSEALQWRAQTDPDHVLYMLLNAkGVAVSTaTCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAG 1082
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKED-GIWQSL-TWAEFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1083 CIPVTVrpphpqnlSATLPT--VRMIIDVSKA-ACILTTQTLMKTLRS----------------KEAAASVNVKTWPNII 1143
Cdd:COG1022 90 AVTVPI--------YPTSSAeeVAYILNDSGAkVLFVEDQEQLDKLLEvrdelpslrhivvldpRGLRDDPRLLSLDELL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688611670 1144 D------TDDLPRKRPASIykppTAEMLAYLDFSVSTTGMLTGVKMSH----SAVNALCRSIKLQ 1198
Cdd:COG1022 162 AlgrevaDPAELEARRAAV----KPDDLATIIYTSGTTGRPKGVMLTHrnllSNARALLERLPLG 222
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
338-441 |
1.40e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 46.57 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 338 WPP-------------ALQAALARWGATQAKSPALtalDITGkplYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGD 404
Cdd:PRK06178 18 WPAgiprepeyphgerPLTEYLRAWARERPQRPAI---IFYG---HVITYAELDELSDRFA-ALLRQRG------VGAGD 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 688611670 405 RVALVYPNSdPgMFWVAFYGCLLAEVIPVPIEvPLSR 441
Cdd:PRK06178 85 RVAVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFR 118
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
371-645 |
2.90e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 45.28 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 371 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSdpGMFWVAFYGCLLAEVIPVPIEvPLSRKDagsqQIG 450
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAA-LG------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPLN-TRYTAD----EAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 451 FLLGSCGVGLAL-------TSEVCLKGLPK----------TPNGEIMQFKGWprlkwvvtdTKYLTKPSKDWQpHIPTAN 513
Cdd:PRK07656 96 YILARGDAKALFvlglflgVDYSATTRLPAlehvviceteEDDPHTEKMKTF---------TDFLAAGDPAER-APEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 514 TDTAYIEYKASKEGTVMGVavskisMLTHCQALTQA---CNYC---EGETLVNVLDFKKDSGLWHGVLTSVMNRIHTISV 587
Cdd:PRK07656 166 DDVADILFTSGTTGRPKGA------MLTHRQLLSNAadwAEYLgltEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 688611670 588 PyavmKACPLSWVQRVHVHKARVaLVKCRDLHWAMMAHRDQKDTNLSSLRmLIVADGA 645
Cdd:PRK07656 240 P----VFDPDEVFRLIETERITV-LPGPPTMYNSLLQHPDRSAEDLSSLR-LAVTGAA 291
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1378-1571 |
3.94e-04 |
|
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: 44.97 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1378 GTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYY-----TiygEESLQADHfntrlsfgdtetlWARTGYLGFV 1452
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWnkpeaT---KEEFTDDG-------------WFKTGDLGVV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1453 krtellDASGdrhdALFVVG-SLDETLELRGLRYHPIDIEtSVSRAHRSIAESAVF-----TWTNLLVVVVELSgSEQEA 1526
Cdd:cd05941 331 ------DEDG----YYWILGrSSVDIIKSGGYKVSALEIE-RVLLAHPGVSECAVIgvpdpDWGERVVAVVVLR-AGAAA 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 688611670 1527 LDLVPLVTNvvLKEH---HLIVGVVVIVDpgVIPINSRGEKQRMHLRD 1571
Cdd:cd05941 399 LSLEELKEW--AKQRlapYKRPRRLILVD--ELPRNAMGKVNKKELRK 442
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
371-546 |
4.44e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 44.92 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 371 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPIEVPLSRKDagsqqIG 450
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLD-LG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 451 FLLGSCGVGLALTSEVCLKGLPKTPNGEIMQFKGWPRL--------KWVVTDTKYLTKPSKDWQPHIptANTDTAYIEYK 522
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreapgGWLDFADWAEAGSVAEPDVEL--ADDDLAQILYT 179
|
170 180
....*....|....*....|....
gi 688611670 523 ASKEGTVMGVavskisMLTHcQAL 546
Cdd:PRK08316 180 SGTESLPKGA------MLTH-RAL 196
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1032-1506 |
5.56e-04 |
|
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: 44.37 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1032 TATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPphpqnlsatlptvrmiidvsk 1111
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1112 aacILTTQTLMKTLRSKEAAASvnvktwpnIIDTDDlprkrpasiykpptaemLAYLDFSVSTTGMLTGVKMSHSA---- 1187
Cdd:cd05919 68 ---LLHPDDYAYIARDCEARLV--------VTSADD-----------------IAYLLYSSGTTGPPKGVMHAHRDpllf 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1188 VNALCRSI-KLQCE--LYSSRQIAICMdpycGLGFVLWclSSVYSGHQSILIPPMELETSLplwLSTLSQYKIRdTFCSY 1264
Cdd:cd05919 120 ADAMAREAlGLTPGdrVFSSAKMFFGY----GLGNSLW--FPLAVGASAVLNPGWPTAERV---LATLARFRPT-VLYGV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1265 SVMELCTKGLGTQTEALkarnvnLSCVRSCVVIAEERPRlaltqSFSKLFKDLGLSPraVSTAFGSRVNLAICLqgtagp 1344
Cdd:cd05919 190 PTFYANLLDSCAGSPDA------LRSLRLCVSAGEALPR-----GLGERWMEHFGGP--ILDGIGATEVGHIFL------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1345 dpstvyvdmkSLRHDRVRLVERGAPqslplmesgtmLPGVRVIIVNPETKgPLGDSHLGEIWVNSPHNASGYYTIYGEes 1424
Cdd:cd05919 251 ----------SNRPGAWRLGSTGRP-----------VPGYEIRLVDEEGH-TIPPGEEGDLLVRGPSAAVGYWNNPEK-- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1425 lqadhfnTRLSFGDTetlWARTGYLGFVkrtellDASGdrhdALFVVGSLDETLELRGLRYHPIDIETSVSRaHRSIAES 1504
Cdd:cd05919 307 -------SRATFNGG---WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVSPVEVESLIIQ-HPAVAEA 365
|
..
gi 688611670 1505 AV 1506
Cdd:cd05919 366 AV 367
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1378-1497 |
7.32e-04 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 43.79 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1378 GTMLPGVRVIIVNPETKGPLGDSHlGEIWVNSPHNASGYYTiygEESLQADHFNTRlsfgdtetlWARTGYLGFVKrtel 1457
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 688611670 1458 ldasgdRHDALFVVGSLDETLELRGLRYHPIDIETSVSRA 1497
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVERIAEGV 269
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1003-1191 |
9.38e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 44.26 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1003 LSEALQWRAQTDPDhvlymllnAKGVAVSTATCSQLHKRAEKIT-AALLERGGINTGDNVVLLYPPGIDLIASFYGCLYA 1081
Cdd:PRK10252 460 LSALVAQQAAKTPD--------APALADARYQFSYREMREQVVAlANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1082 GCIPVTVRPPHPQNlsatlpTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPASiykppt 1161
Cdd:PRK10252 532 GAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHH------ 599
|
170 180 190
....*....|....*....|....*....|.
gi 688611670 1162 aemLAYLDFSVSTTGMLTGVKMSHSA-VNAL 1191
Cdd:PRK10252 600 ---TAYIIFTSGSTGRPKGVMVGQTAiVNRL 627
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1001-1092 |
1.74e-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: 42.70 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1001 QFLSEALQWRAQTDPDHVlymllnakgvAVSTA----TCSQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFY 1076
Cdd:cd05920 15 EPLGDLLARSAARHPDRI----------AVVDGdrrlTYRELDRRADRL-AAGLRGLGIRPGDRVVVQLPNVAEFVVLFF 83
|
90
....*....|....*.
gi 688611670 1077 GCLYAGCIPVTVRPPH 1092
Cdd:cd05920 84 ALLRLGAVPVLALPSH 99
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1377-1454 |
1.87e-03 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 42.73 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1377 SGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYY-----TiygEESLQADH-FNTrlsfGDTETlWARTGYLG 1450
Cdd:cd17640 266 VGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYknpeaT---SKVLDSDGwFNT----GDLGW-LTCGGELV 337
|
....
gi 688611670 1451 FVKR 1454
Cdd:cd17640 338 LTGR 341
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1037-1188 |
2.08e-03 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 42.64 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1037 QLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVrpphpqnlSATLPTVRM--IIDVSKAAC 1114
Cdd:cd12114 17 ELAERARRV-AGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV--------DIDQPAARReaILADAGARL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688611670 1115 ILTTQTLmktlrskeAAASVNVKTWPNIIDTDDLPRKRPASIykPPTAEMLAYLDFSVSTTGMLTGVKMSHSAV 1188
Cdd:cd12114 88 VLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPPV--DVAPDDLAYVIFTSGSTGTPKGVMISHRAA 151
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1010-1269 |
2.13e-03 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 42.70 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1010 RAQTDPDHVlymllnakgvAV----STATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIP 1085
Cdd:cd17655 6 QAEKTPDHT----------AVvfedQTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1086 VTVRPPHPQNlsatlpTVRMIIDVSKAACILTTqtlmKTLRSKEAAASVNVktwpnIIDTDDLPRKRPASIYKPPTAEML 1165
Cdd:cd17655 75 LPIDPDYPEE------RIQYILEDSGADILLTQ----SHLQPPIAFIGLID-----LLDEDTIYHEESENLEPVSKSDDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1166 AYLDFSVSTTGMLTGVKMSH--------SAVNALCRSIKLQCELYSSrqiaICMDpycglGFVLWCLSSVYSGHqSILIP 1237
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFD-----ASVTEIFASLLSGN-TLYIV 209
|
250 260 270
....*....|....*....|....*....|..
gi 688611670 1238 PMELETSLPLWLSTLSQYKIRDTFCSYSVMEL 1269
Cdd:cd17655 210 RKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1383-1507 |
2.71e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 42.18 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1383 GVRVIIVNPEtKGPLGDSHLGEIWVNSPHNASGYYtiygeeslqADHFNTRLSFGDTetlWARTGYLGfvkrteLLDASG 1462
Cdd:PRK05852 362 GAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYL---------GDPTITAANFTDG---WLRTGDLG------SLSAAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 688611670 1463 DrhdaLFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESAVF 1507
Cdd:PRK05852 423 D----LSIRGRIKELINRGGEKISPERVE-GVLASHPNVMEAAVF 462
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
371-465 |
2.87e-03 |
|
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: 42.20 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 371 TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSDPgmFWVAFYGCLLAEVIPVPIEVPLSrkdagSQQIG 450
Cdd:cd05907 5 PITWAEFAEEVRALAKGLI-ALG------VEPGDRVAILSRNRPE--WTIADLAILAIGAVPVPIYPTSS-----AEQIA 70
|
90
....*....|....*
gi 688611670 451 FLLGSCGVGLALTSE 465
Cdd:cd05907 71 YILNDSEAKALFVED 85
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1011-1190 |
2.89e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 42.07 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1011 AQTDPDHVLYMLLNAkgvavsTATCSQLHKRAEKITAALLERgGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVtvrp 1090
Cdd:PRK07786 27 ALMQPDAPALRFLGN------TTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAV---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1091 phPQNLSATLPTVRMIIDVSKAACILTTQTL-------------MKTLRSKEAAASVNVKTWPNIIDTD-------DLPR 1150
Cdd:PRK07786 96 --PVNFRLTPPEIAFLVSDCGAHVVVTEAALapvatavrdivplLSTVVVAGGSSDDSVLGYEDLLAEAgpahapvDIPN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 688611670 1151 KRPASIYkpptaemlayldFSVSTTGMLTGVKMSHSAVNA 1190
Cdd:PRK07786 174 DSPALIM------------YTSGTTGRPKGAVLTHANLTG 201
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
371-535 |
3.80e-03 |
|
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: 41.51 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 371 TLTYGKLWSRSLKLAYTLLNKLGtknepvlKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEvplsrKDAGSQQIG 450
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 451 FLLGSCGVGLALTSEVCLKGLPKTPngeimqfkgwprlkwVVTDTKYLTKPSKDWQPHIPTANTDTAYIEYKASKEGTVM 530
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLPAGL---------------PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPK 142
|
....*
gi 688611670 531 GVAVS 535
Cdd:cd12116 143 GVVVS 147
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
371-449 |
4.68e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 41.58 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 371 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPN--SDPgmfwVAFYGCLLAEVIPV-------PIEVPLSR 441
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNllQYP----IALFGILRAGMIVVnvnplytPRELEHQL 117
|
....*...
gi 688611670 442 KDAGSQQI 449
Cdd:PRK08974 118 NDSGAKAI 125
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1369-1506 |
4.72e-03 |
|
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: 41.31 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1369 PQSLPLMESGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYYTIYGEeslqadhfnTRLSF-GDTETLWARTG 1447
Cdd:cd05935 245 PLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEE---------TEESFiEIKGRRFFRTG 315
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 688611670 1448 YLGFvkrtelLDASGdrhdALFVVGSLDETLELRGLRYHPIDIETSVSRaHRSIAESAV 1506
Cdd:cd05935 316 DLGY------MDEEG----YFFFVDRVKRMINVSGFKVWPAEVEAKLYK-HPAI*EVCV 363
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1036-1185 |
5.55e-03 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 41.37 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1036 SQLHKRAEKITAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPphpqnLSATLPTVRMIIDVSKAACI 1115
Cdd:PLN02574 70 SELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP-----SSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 1116 LTTQTLmktlrSKEAAASVNVKTWPNIIDTDD----------LPRKRPASIYKPPTAEM-LAYLDFSVSTTGMLTGVKMS 1184
Cdd:PLN02574 145 TSPENV-----EKLSPLGVPVIGVPENYDFDSkriefpkfyeLIKEDFDFVPKPVIKQDdVAAIMYSSGTTGASKGVVLT 219
|
.
gi 688611670 1185 H 1185
Cdd:PLN02574 220 H 220
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
372-435 |
8.76e-03 |
|
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: 40.54 E-value: 8.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688611670 372 LTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPI 435
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNSP--QYVIAYFAIWRANAVVVPI 56
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
371-535 |
9.49e-03 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 40.26 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 371 TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSdPGMFwVAFYGCLLA--EVIPVPIEVPLSRkdagsqq 448
Cdd:cd12117 22 SLTYAELNERANRLARRLR-AAG------VGPGDVVGVLAERS-PELV-VALLAVLKAgaAYVPLDPELPAER------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611670 449 IGFLLGSCGVGLALTSEvclkGLPKTPNGEIMQfkgwprlkwVVTDTKYLTKPSKDwqPHIPTANTDTAYIEYKASKEGT 528
Cdd:cd12117 86 LAFMLADAGAKVLLTDR----SLAGRAGGLEVA---------VVIDEALDAGPAGN--PAVPVSPDDLAYVMYTSGSTGR 150
|
....*..
gi 688611670 529 VMGVAVS 535
Cdd:cd12117 151 PKGVAVT 157
|
|
| |
