|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1017-1581 |
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 688611673 1017 LYMLLNAKGVAVSTATCSQLHKRAEKITAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPH-PQNLS 1095
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1096 ATLPTVRMiiDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPA-----SIYKPPTAEMLAYLDFSV 1170
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1171 STTGMLTGVKMSHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELETSLPLWLSTL 1250
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1251 SQYKIRDTFCSYSVMELCTKGLGTQTEALKARNVNLSCVRSCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFGSRV 1330
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1331 NLAICLQGTAGPDPSTVYVDMKSLRHDRVRLVERGAPQSLPLMESGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHN 1410
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1411 ASGYYTIYGEESLQADHFN-TRLSFGDTETLWARTGYLGFVKRTELLDASGDRHDALFVVGSLDETLELRGLRYHPIDIE 1489
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPsTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1490 TSVSRAHRSIAESAVFTWTNLLVVVVELS-GSEQEALDLVPLVTNVVLKEHHLIVGVVVIVDPGVIPINSRGEKQRMHLR 1568
Cdd:cd05905 479 ATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIR 558
|
570
....*....|...
gi 688611673 1569 DSFLADQLDPIYV 1581
Cdd:cd05905 559 QAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
356-932 |
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 688611673 356 ALTALDITGKPLYTLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPnsDPGMFWVAFYGCLLAEVIPVPIEV 435
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 436 PLsrkdaGSQQIGFLLGSCGVGLALTSEVCLKGLPKT-----PNGEIMQFKGWPRLKWVVTDTKYLTKPSKDWQPHIPTA 510
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 511 NTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWHGVLTSVMNRIHTISVPYAVM 590
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 591 KACPLSWVQRVHVHKARVALVKCRDLHWAMM------AHRDQKDTNLSSLRMLIVADGaNPWSVSSCDAFLNVFQSHGLK 664
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKdlsstlASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 665 PEmicpcASSPEAMTVAIRRPGAPGT--PLPARAILSMAGLSHGVIRVNTEDKNSALTVQDVGHVMPGALMCIVKPDGPP 742
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGTsgPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 743 mLCKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEVIPVNSGGTPIGDVPFTRTGLLGFVGPGS----------LVFVVGK 812
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTKctdlnveehdLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 813 IEGLLSVSGRRHNADDLVATALAVEPvktvYRGRIAVFSVTvfydERVVIVAEQRPdANEEDSFQWMSRVLQAIDSIHQV 892
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 688611673 893 GLYCLALVPANTLPKTPLGGIHVSETKHHFLEGSLHPCNI 932
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1007-1573 |
2.10e-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: 258.71 E-value: 2.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1007 WRAQTDPDHVLYMLLNAKGVAVSTATCSQLHKRAEKITAALLERGGinTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTV 1086
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1087 RPPHPqnlSATLPTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWpniIDTDDLPRKRPASIYKPPTAEM--LA 1164
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR---LLVVDLLPDTSAADWPPPSPDPddIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1165 YLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELETSLP 1244
Cdd:cd05931 153 YLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1245 LWLSTLSQYkiRDTFcsySVM-----ELCT-KGLGTQTEALkarnvNLSCVRScVVIAEERPRLALTQSFSKLFKDLGLS 1318
Cdd:cd05931 233 RWLRLISRY--RATI---SAApnfayDLCVrRVRDEDLEGL-----DLSSWRV-ALNGAEPVRPATLRRFAEAFAPFGFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1319 PRAVSTAFGsrvnLA-ICL---QGTAGPDPSTVYVDMKSLRHdRVRLVERGAPQSLPLMESGTMLPGVRVIIVNPETKGP 1394
Cdd:cd05931 302 PEAFRPSYG----LAeATLfvsGGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGRE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1395 LGDSHLGEIWVNSPHNASGYytiYGEESLQADHFNTRLsfGDTETLWARTGYLGFVKRTElldasgdrhdaLFVVGSLDE 1474
Cdd:cd05931 377 LPDGEVGEIWVRGPSVASGY---WGRPEATAETFGALA--ATDEGGWLRTGDLGFLHDGE-----------LYITGRLKD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1475 TLELRGLRYHPIDIETSVSRAHRSIAESAVFTWTNL------LVVVVELSGSeQEALDLVPLVTNV---VLKEHHLIVGV 1545
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPddgeerLVVVAEVERG-ADPADLAAIAAAIraaVAREHGVAPAD 519
|
570 580
....*....|....*....|....*...
gi 688611673 1546 VVIVDPGVIPINSRGEKQRMHLRDSFLA 1573
Cdd:cd05931 520 VVLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
346-923 |
6.19e-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: 6.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 346 RWGATQAKSPALTALDITGKPLYTLTYGKLWSRSLKLAYTLLnklgtknePVLKPGDRVALVYPnsdPGM-FWVAFYGCL 424
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAP---PGLdFVAAFLGCL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 425 LAEVIPVPIEVPLSRKDAgsQQIGFLLGSCGVGLALTSEVCLKGLPKTpngeIMQFKGWPRLKWVVTDTKyLTKPSKDWQ 504
Cdd:cd05931 70 YAGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLL-PDTSAADWP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 505 PHIPTANtDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWHGVLTSVMNRIHTIS 584
Cdd:cd05931 143 PPSPDPD-DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 585 V-PYAVMKAcPLSWVQRVHVHKARV------ALVKCrdlhwAMMAHRDQKDT-NLSSLRMLIVadGANPWSVSSCDAFLN 656
Cdd:cd05931 222 MsPAAFLRR-PLRWLRLISRYRATIsaapnfAYDLC-----VRRVRDEDLEGlDLSSWRVALN--GAEPVRPATLRRFAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 657 VFQSHGLKPEMICPCASSPEA-MTVAIRRPGAPgtplPARAILSMAGLSHGViRVNTEDKNSALTVQDVGHVMPGALMCI 735
Cdd:cd05931 294 AFAPFGFRPEAFRPSYGLAEAtLFVSGGPPGTG----PVVLRVDRDALAGRA-VAVAADDPAARELVSCGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 736 VKPDGPPmLCKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEVIpvnsggTPIGDVPFTRTGLLGFVGPGSLvFVVGKIEG 815
Cdd:cd05931 369 VDPETGR-ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGAL------AATDEGGWLRTGDLGFLHDGEL-YITGRLKD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 816 LLSVSGRRHNADDLVATALAVEPVktVYRGRIAVFSVTVFYDERVVIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVGLY 895
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPA 518
|
570 580
....*....|....*....|....*...
gi 688611673 896 CLALVPANTLPKTPLGGIHVSETKHHFL 923
Cdd:cd05931 519 DVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1005-1479 |
3.49e-47 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 175.58 E-value: 3.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1005 LQWRAQTDPDHVLYMllnakGVAVSTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPV 1084
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1085 TVRPphpqnlSATLPTVRMIIDVSKAACILTTQTLmKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPASIYK-------- 1156
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDDAL-KLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAkpadvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1157 ---PPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCE----LYSSRQIAICMDPYCGLGFVLWCLSSVYSGH 1229
Cdd:pfam00501 148 pppPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1230 QSILIPPMELeTSLPLWLSTLSQYKIRDTFCSYSVMELCTKGLGTQTEALKArnvnlscVRsCVVIAEERPRLALTQSFS 1309
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSS-------LR-LVLSGGAPLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1310 KLFkdlglsPRAVSTAFGSRVNLAIClqgtagpdpstVYVDMKSLRHDRVRLVergapqslplmesGTMLPGVRVIIVNP 1389
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVV-----------TTPLPLDEDLRSLGSV-------------GRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1390 ETKGPLGDSHLGEIWVNSPHNASGYytiYGEESLQADHFntrlsfgdTETLWARTGYLGFvkrtelLDASGdrhdALFVV 1469
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGR------RDEDG----YLEIV 407
|
490
....*....|
gi 688611673 1470 GSLDETLELR 1479
Cdd:pfam00501 408 GRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1001-1579 |
3.07e-40 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 164.57 E-value: 3.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1001 LSEALQWRAQTDPDHV-LYMLLNAKGVAVsTATCSQLHKRAEKITAALLERGGIntGDNVVLLYPPGIDLIASFYGCLYA 1079
Cdd:PRK05691 11 LVQALQRRAAQTPDRLaLRFLADDPGEGV-VLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1080 GCIPVTVRPP------HPQNLSAtlptvrmIIDVSKAACILTTQTLMKTLRSKEAAASVNVktwPNIIDTDDLPrKRPAS 1153
Cdd:PRK05691 88 GVIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLD-PALAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1154 IYKPPT--AEMLAYLDFSVSTTGMLTGVKMSHSAVNAlcrsiklqCELYSSRQIAICMDP----------YCGLGFVLWC 1221
Cdd:PRK05691 157 AWQEPAlqPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1222 LSSVYSGHQSILIPPMELETSLPLWLSTLSQYkiRDT----------FCSYSVMELCTKGLgtqtealkarnvNLSCVRs 1291
Cdd:PRK05691 229 LQPIFSGVPCVLMSPAYFLERPLRWLEAISEY--GGTisggpdfayrLCSERVSESALERL------------DLSRWR- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1292 cVVIAEERP-RLALTQSFSKLFKDLGLSPRAVSTAFGSRVNLAICLQGTAGPDPSTVYVDMKSLRHDRvrlVERGAPQsl 1370
Cdd:PRK05691 294 -VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNR---AEPGTGS-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1371 PLMESGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYYTiYGEESLQAdhFNTRlsfgDTETlWARTGYLGFV 1450
Cdd:PRK05691 368 VLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR-NPEASAKT--FVEH----DGRT-WLRTGDLGFL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1451 krtelldasgdRHDALFVVGSLDETLELRGLRYHPIDIETSVSRAHRSIAES--AVFTWTNL----LVVVVELSGSEQEA 1524
Cdd:PRK05691 440 -----------RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGrvAAFAVNHQgeegIGIAAEISRSVQKI 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 688611673 1525 L---DLVPLVTNVVLKEHHLIVGVVVIVDPGVIPINSRGEKQRMHLRDSFLADQLDPI 1579
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 ... |
1163-1563 |
3.26e-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: 3.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1163 LAYLDFSVSTTGMLTGVKMSHSAVNALCRSIkLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELEts 1242
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1243 lpLWLSTLSQYKIRDTFCSYSVMELCTKglgtqteALKARNVNLSCVRSCVVIAEERPRlALTQSFSKLFKDlglsprAV 1322
Cdd:cd04433 79 --AALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLPP-ELLERFEEAPGI------KL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1323 STAFGSrvnlaiclqgT-AGPDPSTVYVDMKSLRHDRVrlverGAPqslplmesgtmLPGVRVIIVNPETkGPLGDSHLG 1401
Cdd:cd04433 143 VNGYGL----------TeTGGTVATGPPDDDARKPGSV-----GRP-----------VPGVEVRIVDPDG-GELPPGEIG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1402 EIWVNSPHNASGYYTiygeeslqadhfNTRLSFGDTETLWARTGYLGFVkrtelldasgDRHDALFVVGSLDETLELRGL 1481
Cdd:cd04433 196 ELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL----------DEDGYLYIVGRLKDMIKSGGE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1482 RYHPIDIETSVSRaHRSIAESAVF-----TWTNLLVVVVEL-SGSEQEALDLVPLVTNVVlkEHHLIVGVVVIVDPgvIP 1555
Cdd:cd04433 254 NVYPAEVEAVLLG-HPGVAEAAVVgvpdpEWGERVVAVVVLrPGADLDAEELRAHVRERL--APYKVPRRVVFVDA--LP 328
|
....*...
gi 688611673 1556 INSRGEKQ 1563
Cdd:cd04433 329 RTASGKID 336
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1005-1577 |
8.25e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 142.00 E-value: 8.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1005 LQWRAQTDPDHVLYMLL----NAKGVAvSTATCSQLHKRAEKITAALLERGGinTGDNVVLLYPPGIDLIASFYGCLYAG 1080
Cdd:PRK05850 7 LRERASLQPDDAAFTFIdyeqDPAGVA-ETLTWSQLYRRTLNVAEELRRHGS--TGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1081 CIPVTVRPPHPqnlSATLPTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPASIyKPPTA 1160
Cdd:PRK05850 84 LIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDA-RPRDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1161 EMLAYLDFSVSTTGMLTGVKMSHSAVNALCRsiKLQCELYSSRQIAICMD-------P-YCGLGFVLWCLSSVYSGHQSI 1232
Cdd:PRK05850 160 PSTAYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVCAPILGGCPAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1233 LIPPMELETSLPLWlstlsqykirdtfcsysvMELCTKGLGTQTEA------LKARN--------VNLSCVRsCVVIAEE 1298
Cdd:PRK05850 238 LTSPVAFLQRPARW------------------MQLLASNPHAFSAApnfafeLAVRKtsdddmagLDLGGVL-GIISGSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1299 RPRLALTQSFSKLFKDLGLSPRAVSTAFG---SRVNLAIclqGTAGPDPSTVYVDMKSLRHDRVR---------LVERGA 1366
Cdd:PRK05850 299 RVHPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKrcetgggtpLVSYGS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1367 PQSlplmesgtmlPGVRviIVNPETKGPLGDSHLGEIWVNSPHNASGYytiYGEESLQADHFNTRL---SFGDTETLWAR 1443
Cdd:PRK05850 376 PRS----------PTVR--IVDPDTCIECPAGTVGEIWVHGDNVAAGY---WQKPEETERTFGATLvdpSPGTPEGPWLR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1444 TGYLGFVkrtelldaSGdrhDALFVVGSLDETLELRGLRYHPIDIETSV---SRAhRSIAESAVFTWTNLLVVVVEL--- 1517
Cdd:PRK05850 441 TGDLGFI--------SE---GELFIVGRIKDLLIVDGRNHYPDDIEATIqeiTGG-RVAAISVPDDGTEKLVAIIELkkr 508
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611673 1518 SGSEQEALDLVPLVTNVVL----KEHHLIVGVVVIVDPGVIPINSRGEKQR-----MHLRDSFlaDQLD 1577
Cdd:PRK05850 509 GDSDEEAMDRLRTVKREVTsaisKSHGLSVADLVLVAPGSIPITTSGKIRRaacveQYRQDEF--TRLD 575
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
8-124 |
8.57e-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: 8.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 8 LAALPKEVREQLAELELELSEGDITQKGYEKKRAKLLAPFVPQtqnvdvsilstdstSSPITIPIAAPRQHRAHRSGGTR 87
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLH--------------PETPTKLSAEAQNQLASLETKLR 67
|
90 100 110
....*....|....*....|....*....|....*..
gi 688611673 88 DDRYRSDIHTEAVQAALARHKEEKMALPMPTKRRSAF 124
Cdd:pfam06464 68 DEELSEEVYLEKVKALLAKELERENGLNAPTKEQSGL 104
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
397-927 |
7.59e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 127.54 E-value: 7.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 397 VLKPGDRVALVYPNS-DpgmFWVAFYGCLLAEVIPVPIEVP-----LSRKDAgsqqigfLLGSCGVGLALTSEVC----- 465
Cdd:PRK07769 75 VTKPGDRVAILAPQNlD---YLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSaegvr 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 466 --LKGLPKtpngeimqfKGWPRLKWV--VTDTKYLTkpskdWQPhiPTANTDT-AYIEYKASKEGTVMGVAVSKISMLTH 540
Cdd:PRK07769 145 kfFRARPA---------KERPRVIAVdaVPDEVGAT-----WVP--PEANEDTiAYLQYTSGSTRIPAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 541 CQALTQACNYCEGETLVNVLDFKKDSGLWHGVLTSVMNRIHTISVPYAVMKAcPLSWVQRVhvhkARVALVKCRDL---- 616
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRR-PGRWIREL----ARKPGGTGGTFsaap 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 617 -----HWAM--MAHRDQKDTNLSSLRMLIvaDGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEA--MTVAIRRPGA 687
Cdd:PRK07769 284 nfafeHAAArgLPKDGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtlFVSTTPMDEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 688 PGTPLPARAILSmaglSHGVIRVNTEDKNsALTVQDVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVLNSRAGGTMYYGL 767
Cdd:PRK07769 362 PTVIYVDRDELN----AGRFVEVPADAPN-AVAQVSAGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGK 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 768 PGVTKNTFEVI------PVNSGGTPiGDVPFTRTGLLGFVGPGSLvFVVGKIEGLLSVSGRRHNADDLVATALavEPVKT 841
Cdd:PRK07769 436 PEETAATFQNIlksrlsESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--EATKA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 842 VYRGRIAVFSV-------TVFYD-------------ERVVIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVGLYCLALVP 901
Cdd:PRK07769 512 LRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVP 591
|
570 580
....*....|....*....|....*.
gi 688611673 902 ANTLPKTPLGGIHVSETKHHFLEGSL 927
Cdd:PRK07769 592 AGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1001-1578 |
1.13e-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: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1001 LSEALQWRAQTDPDHVlymllnakgvAVSTA----TCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGC 1076
Cdd:COG0318 1 LADLLRRAAARHPDRP----------ALVFGgrrlTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1077 LYAGCIPVTVrpphpqNLSATLPTVRMIIDVSKAACILTtqtlmktlrskeaaasvnvktwpniidtddlprkrpasiyk 1156
Cdd:COG0318 70 LRAGAVVVPL------NPRLTAEELAYILEDSGARALVT----------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1157 pptaemlAYLDFSvS-TTGMLTGVKMSHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIP 1235
Cdd:COG0318 103 -------ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1236 PMELETslplWLSTLSQYKIrdTFCSYS---VMELCtkglgtqtEALKARNVNLSCVRsCVVIAEERPRLALTQSFSKLF 1312
Cdd:COG0318 175 RFDPER----VLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLR-LVVSGGAPLPPELLERFEERF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1313 KdlglspRAVSTAFGSrvnlaiclqgT-AGPdpsTVYVDMKSLRHDRVRLVergapqslplmesGTMLPGVRVIIVNPET 1391
Cdd:COG0318 240 G------VRIVEGYGL----------TeTSP---VVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVDEDG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1392 KgPLGDSHLGEIWVNSPHNASGYYTiYGEEslqadhfnTRLSFGDTetlWARTGYLGFvkrtelLDASGDrhdaLFVVGS 1471
Cdd:COG0318 288 R-ELPPGEVGEIVVRGPNVMKGYWN-DPEA--------TAEAFRDG---WLRTGDLGR------LDEDGY----LYIVGR 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1472 LDETLELRGLRYHPIDIETSVsRAHRSIAESAVF-----TWTNLLVVVVELsgSEQEALDLVPLVTnvVLKEH---HLIV 1543
Cdd:COG0318 345 KKDMIISGGENVYPAEVEEVL-AAHPGVAEAAVVgvpdeKWGERVVAFVVL--RPGAELDAEELRA--FLRERlarYKVP 419
|
570 580 590
....*....|....*....|....*....|....*
gi 688611673 1544 GVVVIVDPgvIPINSRGEKQRMHLRDSFLADQLDP 1578
Cdd:COG0318 420 RRVEFVDE--LPRTASGKIDRRALRERYAAGALEA 452
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1032-1578 |
2.35e-28 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 122.54 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1032 TCSQLHKRAEKITAALLERGGinTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPP----HPQNLSATL----PTVrm 1103
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1104 iidvskaacILTTQTLMKTLRSKEAAASVNVKtwPNIIDTDDLPrKRPASIYKPPTAEM--LAYLDFSVSTTGMLTGVKM 1181
Cdd:PRK12476 146 ---------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIP-DSAGESFVPVELDTddVSHLQYTSGSTRPPVGVEI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1182 SHSAVNALCRSIKLQCELYSSRQIAICMDP-YCGLGFVLWCLSSVYSGHqSILIPPMELETSLPLWLSTLSQ-YKIRDTF 1259
Cdd:PRK12476 214 THRAVGTNLVQMILSIDLLDRNTHGVSWLPlYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIKALSEgSRTGRVV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1260 CSYS--VMELCT-KGLGTQTEALKARNVNLscvrscvVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFGsrVNLAICL 1336
Cdd:PRK12476 293 TAAPnfAYEWAAqRGLPAEGDDIDLSNVVL-------IIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLF 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1337 QGTAGPD--PSTVYVDMKSLRHDRVRLVERGAPQSLPLMESGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGY 1414
Cdd:PRK12476 364 VATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGY 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1415 YTIYGEeslqadhfnTRLSFGDT----------------ETLWARTGYLGFvkrteLLDASgdrhdaLFVVGSLDETLEL 1478
Cdd:PRK12476 444 WGRPEE---------TERTFGAKlqsrlaegshadgaadDGTWLRTGDLGV-----YLDGE------LYITGRIADLIVI 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1479 RGLRYHPIDIETSVSRAHRSIAESAVFTWT------NLLVVVVELSG--SEQEALDLVPLVTNVVLKEHHLIVGVVVIVD 1550
Cdd:PRK12476 504 DGRNHYPQDIEATVAEASPMVRRGYVTAFTvpaednERLVIVAERAAgtSRADPAPAIDAIRAAVSRRHGLAVADVRLVP 583
|
570 580
....*....|....*....|....*...
gi 688611673 1551 PGVIPINSRGEKQRMHLRDSFLADQLDP 1578
Cdd:PRK12476 584 AGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
338-913 |
9.42e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 120.43 E-value: 9.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 338 PALQAALARwgaTQAKSPALTALDITGKP---LYTLTYGKLWSRSLKLAYTLlNKLGTknepvlkPGDRVALVYPNsdpG 414
Cdd:PRK05850 4 PSLLRERAS---LQPDDAAFTFIDYEQDPagvAETLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQ---G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 415 M-FWVAFYGCLLAEVIPVPIEVPLSRkdAGSQQIGFLLGSCGVGLALT-SEVClkglpktpnGEIMQF----KGWPRLKW 488
Cdd:PRK05850 70 LeYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTtSAVV---------DDVTEYvapqPGQSAPPV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 489 VVTDTKYLTKPSKdwqPHIPTAN-TDTAYIEYKASKEGTVMGVAVSKISMLTHC-QALTQACNYCEGE-----TLVNVLD 561
Cdd:PRK05850 139 IEVDLLDLDSPRG---SDARPRDlPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 562 FKKDSGLWHGVLTSVMNRIHtisvpyAVMKAcPLSWVQRvhvhKAR-VALVKCRDLHWAM-------MAHRDQKDTNLSS 633
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCP------AVLTS-PVAFLQR----PARwMQLLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 634 L---RMLIVADGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAMT-VAIRRPGAPgtplPARAILSMAGLSHGVIR 709
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEATVyVATREPGQP----PESVRFDYEKLSAGHAK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 710 VNTEDKNSALtvqdVGHVMPGA-LMCIVKPDgPPMLCKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEVIPVN-SGGTPI 787
Cdd:PRK05850 361 RCETGGGTPL----VSYGSPRSpTVRIVDPD-TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDpSPGTPE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 788 GdvPFTRTGLLGFVGPGSLvFVVGKIEGLLSVSGRRHNADDLVATalavepVKTVYRGRIAVFSVTVFYDERVVIVAE-Q 866
Cdd:PRK05850 436 G--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTEKLVAIIElK 506
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 688611673 867 RPDANEEDSFQWM----SRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGI 913
Cdd:PRK05850 507 KRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
329-925 |
3.82e-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: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 329 PLGVVSNWPPALQAALARWgATQAKSPALTALDITGKPlYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVY 408
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRA-AERGPTKGITYIDADGSE-EFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 409 P-NSDpgmFWVAFYGCLLAEVIPVPIEVPLSRKDAGSQ-----QIGFLLGSCGVglaLTSEVCLKGLPKtpngeimQFKG 482
Cdd:cd05906 72 DdNED---FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELVAEFAG-------LETL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 483 WPRLKWVVTDTKYLTKPSKDWQPHIPTAnTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDF 562
Cdd:cd05906 139 SGLPGIRVLSIEELLDTAADHDLPQSRP-DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 563 KKDSGLWHGVLTSVMNRIHTISVPYAVMKACPLSWVQRVHVHKARV------ALVKCRDLhwamMAHRDQKDTNLSSLRM 636
Cdd:cd05906 218 DHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLNDL----LEEIEDGTWDLSSLRY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 637 LIVADGANpwSVSSCDAFLNVFQSHGLKPEMICPCasspeamtvairrpgapgtplparaiLSMAGLSHGVI---RVNTE 713
Cdd:cd05906 294 LVNAGEAV--VAKTIRRLLRLLEPYGLPPDAIRPA--------------------------FGMTETCSGVIysrSFPTY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 714 DKNSALTVQDVGHVMPGALMCIVKPDGPPMLckTDEIGEIVL--NSRAGGtmYYGLPGVTKNTFevipvnsggTPIGdvp 791
Cdd:cd05906 346 DHSQALEFVSLGRPIPGVSMRIVDDEGQLLP--EGEVGRLQVrgPVVTKG--YYNNPEANAEAF---------TEDG--- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 792 FTRTGLLGFVGPGSLVFvVGKIEGLLSVSGRRHNADDLVAtalAVEPVKTVYRGRIAVFSVTVFYD--ERVVIVAEqrPD 869
Cdd:cd05906 410 WFRTGDLGFLDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAetEELAIFFV--PE 483
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 870 ANEEDSfqwMSRVLQAIDSI--HQVGLYCLALVP--ANTLPKTPLGGIHVSETKHHFLEG 925
Cdd:cd05906 484 YDLQDA---LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
370-929 |
1.07e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 113.95 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 370 LTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVyPNSDPGmFWVAFYGCLLAEVIPVPIEVPLS--RKDAGSQQI 447
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLA-LG------LKPGDRVALI-AETDGD-FVEAFFACQYAGLVPVPLPLPMGfgGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 448 GFLLGSCGVGLALTSEVCLKGLPKTPNGEimqfkgwpRLKWVVTDTKYLTKPSKDWQPHIPTANtDTAYIEYKASKEGTV 527
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLHVLSHAWFKALPEADVALPRPTPD-DIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 528 MGVAVSKISMLTHCQALTQ-ACNYCEGETLVNVLDFKKDSGLWHGVLTSVMNRihtISVPYA-----VMKacPLSWVQRV 601
Cdd:PRK09192 192 RGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQ---LSVDYLptrdfARR--PLQWLDLI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 602 HVHKARVALVKC--RDLHWAMMAHRDQKDTNLSSLRmlIVADGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAmT 679
Cdd:PRK09192 267 SRNRGTISYSPPfgYELCARRVNSKDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 680 VAIrrpgapgtplparailSMAGLSHGvIRVNT------EDKNSALTVQD----------VGHVMPGALMCIVKPDGppm 743
Cdd:PRK09192 344 LAV----------------SFSPLGSG-IVVEEvdrdrlEYQGKAVAPGAetrrvrtfvnCGKALPGHEIEIRNEAG--- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 744 lcktdeigeIVLNSRAGGTMYYGLPGVTKNTFE------VIPVNSggtpigdvpFTRTGLLGFVGPGSLVfVVGKIEGLL 817
Cdd:PRK09192 404 ---------MPLPERVVGHICVRGPSLMSGYFRdeesqdVLAADG---------WLDTGDLGYLLDGYLY-ITGRAKDLI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 818 SVSGRRHNADDLVATALAVEPVKTvyrGRIAVFSVTVFYDERVVIVAEQRPdANEEDSFQWMSRVLQAIDSIHqvGLYCL 897
Cdd:PRK09192 465 IINGRNIWPQDIEWIAEQEPELRS---GDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAA 538
|
570 580 590
....*....|....*....|....*....|...
gi 688611673 898 -ALVPANTLPKTPLGGIHVSETKHHFLEGSLHP 929
Cdd:PRK09192 539 vELVPPHSLPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
986-1582 |
3.56e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 109.32 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 986 QSRKLCVWPTnmhqfLSEALQWRAQTDPDHVLYmllNAKGVAVSTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPP 1065
Cdd:PRK09192 13 LPRRYADFPT-----LVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAET 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1066 GIDLIASFYGCLYAGCIPVTVrpPHPQNL---SATLPTVRMIIDVSKAACILTTQTLMKTLrsKEAAASVNVKTWPNIID 1142
Cdd:PRK09192 84 DGDFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1143 TDDLPrkRPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSIK---LQCELySSRqiAICMDP-YCGLGFV 1218
Cdd:PRK09192 160 FKALP--EADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIShdgLKVRP-GDR--CVSWLPfYHDMGLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1219 LWCLSSVYSGHQSILIPPMELETSLPLWLSTLSqyKIRDTFcSYSV---MELCTKGLGTQTEAlkarNVNLSCVRSCVVI 1295
Cdd:PRK09192 235 GFLLTPVATQLSVDYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1296 AEE-RPRlaLTQSFSKLFKDLGLSPRAVSTAFG-SRVNLAICLqgtagPDPSTvyvDMKSLRHDRVRLVERG---APQSL 1370
Cdd:PRK09192 308 ADMiRPD--VLHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSF-----SPLGS---GIVVEEVDRDRLEYQGkavAPGAE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1371 PLMES-----GTMLPGVRVIIVNpETKGPLGDSHLGEIWVNSPHNASGYytiygeeslqadhfntrlsFGDTETL----- 1440
Cdd:PRK09192 378 TRRVRtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGY-------------------FRDEESQdvlaa 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1441 --WARTGYLGFvkrteLLDasGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVSR--AHRSiAESAVFTWTN----LLV 1512
Cdd:PRK09192 438 dgWLDTGDLGY-----LLD--GY----LYITGRAKDLIIINGRNIWPQDIEWIAEQepELRS-GDAAAFSIAQengeKIV 505
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688611673 1513 VVVELSGSEQEA-LDLVPLVTNVVLKEHHLIVgVVVIVDPGVIPINSRGEKQRMHLRDSFLADQLDPIYVA 1582
Cdd:PRK09192 506 LLVQCRISDEERrGQLIHALAALVRSEFGVEA-AVELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDVA 575
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
337-929 |
4.94e-24 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 109.06 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 337 PPA--LQAALARWGATQAKSPALTALDITGKPLYT---LTYGKLWSRslklaytlLNKLGTKNEPVLKPGDRVALVYPNs 411
Cdd:PRK12476 31 PPGttLISLIERNIANVGDTVAYRYLDHSHSAAGCaveLTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQ- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 412 dpGMFWVA-FYGCLLAEVIPVPIEVP-----LSRKDAgsqqigfLLGSCGVGLALTSEVC-------LKGLPKTpngeim 478
Cdd:PRK12476 102 --GIDYVAgFFAAIKAGTIAVPLFAPelpghAERLDT-------ALRDAEPTVVLTTTAAaeavegfLRNLPRL------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 479 qfkGWPRLKWV--VTDTKyltkpSKDWQPhIPTANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETL 556
Cdd:PRK12476 167 ---RRPRVIAIdaIPDSA-----GESFVP-VELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 557 -VNVLDFKKDSGLWHGVLTSVMNRIHTISVPYAVMKAcPLSWVQRVHV--HKARVaLVKCRDLHWAMMAHR----DQKDT 629
Cdd:PRK12476 238 gVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRR-PQRWIKALSEgsRTGRV-VTAAPNFAYEWAAQRglpaEGDDI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 630 NLSSLRMLIvadGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEA-MTVAIRRPGAPgtplPARAILSMAGLSHG-V 707
Cdd:PRK12476 316 DLSNVVLII---GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEAtLFVATIAPDAE----PSVVYLDREQLGAGrA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 708 IRVNTEDKNSALTVQdVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEV-----IPVNS 782
Cdd:PRK12476 389 VRVAADAPNAVAHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 783 --GGTPIGDVPFtRTGLLGFVGPGSLvFVVGKIEGLLSVSGRRHNADDLVATALAVEPVktVYRGRIAVFSVTVFYDERV 860
Cdd:PRK12476 467 haDGAADDGTWL-RTGDLGVYLDGEL-YITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERL 542
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611673 861 VIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGIHVSETKHHFLEGSLHP 929
Cdd:PRK12476 543 VIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1032-1548 |
7.27e-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: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1032 TCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCipvtvrPPHPQNLSATLPTVRMIIDVSKAA 1111
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1112 CILTTQTLMKTLRSKEAAASVNVKTW---------PNIIDTDDLPRKRPASIYKPP---TAEMLAYLDFSVSTTGMLTGV 1179
Cdd:cd05911 85 VIFTDPDGLEKVKEAAKELGPKDKIIvlddkpdgvLSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1180 KMSHS---AVNALCRSIKLQCELYSSRQIA-ICMDPYCGLGFVLWCLssvYSGHQSILIPPMELETslplWLSTLSQYKI 1255
Cdd:cd05911 165 CLSHRnliANLSQVQTFLYGNDGSNDVILGfLPLYHIYGLFTTLASL---LNGATVIIMPKFDSEL----FLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1256 RDTFCSYSVMELctkgLGTQTEALKArnvNLSCVRSCVVIAeerprlaltqsfSKLFKDLGlspravsTAFGSRVNLAIC 1335
Cdd:cd05911 238 TFLYLVPPIAAA----LAKSPLLDKY---DLSSLRVILSGG------------APLSKELQ-------ELLAKRFPNATI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1336 LQG---T-AGPdPSTVYVDmkslrhdrvRLVERGApqslplmeSGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNA 1411
Cdd:cd05911 292 KQGygmTeTGG-ILTVNPD---------GDDKPGS--------VGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1412 SGYYTiyGEESlqadhfnTRLSFgdTETLWARTGYLGFVkrtelldasgDRHDALFVVGSLDETLELRGLRYHPIDIEtS 1491
Cdd:cd05911 354 KGYYN--NPEA-------TKETF--DEDGWLHTGDIGYF----------DEDGYLYIVDRKKELIKYKGFQVAPAELE-A 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688611673 1492 VSRAHRSIAESAVF-----TWTNLLVVVVELSGSEQ-EALDLVPLVTNVVLKEHHLIVGVVVI 1548
Cdd:cd05911 412 VLLEHPGVADAAVIgipdeVSGELPRAYVVRKPGEKlTEKEVKDYVAKKVASYKQLRGGVVFV 474
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
340-911 |
1.10e-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: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 340 LQAALARWGATQAKSPALTALDITgkplytLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSdPGMFwVA 419
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLA-AALRALG------VGPGDRVALLLPNS-PEFV-VA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 420 FYGCLLAEVIPVPIEVPLSRKdagsqQIGFLLGSCGVGLALTSEVCL----KGLPKtpngeimqfkgwprlkwvvtdtky 495
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVTALILYtsgtTGRPK------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 496 ltkpskdwqphiptantdtayieykaskegtvmGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWHGVLTS 575
Cdd:COG0318 117 ---------------------------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 576 VMNRIHTISVPYAVmkacPLSWVQRVHVHKA-RVALVKcrDLHWAMMAHRDQKDTNLSSLRMLIVadGANPWSVSSCDAF 654
Cdd:COG0318 164 LLAGATLVLLPRFD----PERVLELIERERVtVLFGVP--TMLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 655 LNVFQSHglkpemICPC-ASSpEAMTVAIRRPGAPGTPLPARailsmaglshgvirvntedknsaltvqdVGHVMPGALM 733
Cdd:COG0318 236 EERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 734 CIVKPDGPPmlCKTDEIGEIVLnsRAGGTM--YYGLPGVTKNTFEvipvnsGGtpigdvpFTRTGLLGFVGPGSLVFVVG 811
Cdd:COG0318 281 RIVDEDGRE--LPPGEVGEIVV--RGPNVMkgYWNDPEATAEAFR------DG-------WLRTGDLGRLDEDGYLYIVG 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 812 KIEGLLSVSGRRHNADDLVATALAVEPVKTVyrgriAVFSVTV-FYDERVV--IVAEQRPDANEEDSFQWMSRVL---QA 885
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEA-----AVVGVPDeKWGERVVafVVLRPGAELDAEELRAFLRERLaryKV 418
|
570 580
....*....|....*....|....*.
gi 688611673 886 IDSIHQVGlyclalvpanTLPKTPLG 911
Cdd:COG0318 419 PRRVEFVD----------ELPRTASG 434
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1005-1576 |
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 688611673 1005 LQWRAQTDPDHVLYMLLN----AKGVAVSTaTCSQLHKRAEKITAALLERGgiNTGDNVVLLYPPGIDLIASFYGCLYAG 1080
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDfsteRDGVARDL-TWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1081 CIPVTV----RPPHPQNLSATLptvrmiiDVSKAACILTTQtlmktlrskEAAASVN-------VKTWPNIIDTDDLPRK 1149
Cdd:PRK07769 104 RIAVPLfdpaEPGHVGRLHAVL-------DDCTPSAILTTT---------DSAEGVRkffrarpAKERPRVIAVDAVPDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1150 rPASIYKPPTA--EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL--CRSIKLQcelYSSRQIAiCMDPYCGLGFVLWCLS 1223
Cdd:PRK07769 168 -VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLptNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGLITVLLP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1224 SVYSGHQSILIPPMELETslPL-WLSTLSQyKIRDTFCSYSV-----MELCT-KGLGTQTEAlkarNVNLSCVRsCVVIA 1296
Cdd:PRK07769 243 ALLGHYITFMSPAAFVRR--PGrWIRELAR-KPGGTGGTFSAapnfaFEHAAaRGLPKDGEP----PLDLSNVK-GLLNG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1297 EERPRLALTQSFSKLFKDLGLSPRAVSTAFGsrVNLAICLQGTAGPD--PSTVYVDMKSLRHDRVRLVERGAPQSLPLME 1374
Cdd:PRK07769 315 SEPVSPASMRKFNEAFAPYGLPPTAIKPSYG--MAEATLFVSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1375 SGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYYTiYGEESLQADH--FNTRLSFGDTE-----TLWARTGYL 1447
Cdd:PRK07769 393 AGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWG-KPEETAATFQniLKSRLSESHAEgapddALWVRTGDY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1448 G-FVKrtelldasgdrhDALFVVGSLDETLELRGLRYHPIDIETSVSRAHRSI--------------AESAVFTWTNL-- 1510
Cdd:PRK07769 472 GvYFD------------GELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALrtgyvaafsvpanqLPQVVFDDSHAgl 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1511 ----------LVVVVELS-GSEQeaLDLVPLVTNV---VLKEHHLIVGVVVIVDPGVIPINSRGEKQRMHLRDSFLADQL 1576
Cdd:PRK07769 540 kfdpedtseqLVIVAERApGAHK--LDPQPIADDIraaIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1001-1571 |
1.29e-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: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1001 LSEALQWRAQTDPD-HVLYMLLNAKGVAVSTAtcsQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYA 1079
Cdd:cd05906 12 LLELLLRAAERGPTkGITYIDADGSEEFQSYQ---DLLEDARRL-AAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1080 GCIPVTVRPPHP-QNLSATLPTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPAsiyKPP 1158
Cdd:cd05906 88 GFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDL---PQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1159 TAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSiKLQCELYSSRQIA---ICMDPYCGLGFVlwCLSSVYSGHQSILIP 1235
Cdd:cd05906 165 RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1236 PMELETSLPLWLSTLSQYKIRDTFCSYSvmeLCTKgLGTQTEALKARNVNLSCVRsCVVIAEERPRLALTQSFSKLFKDL 1315
Cdd:cd05906 242 TEEILADPLRWLDLIDRYRVTITWAPNF---AFAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1316 GLSPRAVSTAFGSRVNLAIClqgtagpdpsTVYVDMKSLRHdrvrlvergaPQSLPLMESGTMLPGVRVIIVNPETKGpL 1395
Cdd:cd05906 317 GLPPDAIRPAFGMTETCSGV----------IYSRSFPTYDH----------SQALEFVSLGRPIPGVSMRIVDDEGQL-L 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1396 GDSHLGEIWVNSPHNASGYytiYGEESLQADHFntrlsfgdTETLWARTGYLGFVkrtelldasgdRHDALFVVGSLDET 1475
Cdd:cd05906 376 PEGEVGRLQVRGPVVTKGY---YNNPEANAEAF--------TEDGWFRTGDLGFL-----------DNGNLTITGRTKDT 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1476 LELRGLRYHPIDIETSVSRA----HRSIAESAVF---TWTNLLVVVVELSGSEQEALD-LVPLVTNVVLKEHHLIVGVVV 1547
Cdd:cd05906 434 IIVNGVNYYSHEIEAAVEEVpgvePSFTAAFAVRdpgAETEELAIFFVPEYDLQDALSeTLRAIRSVVSREVGVSPAYLI 513
|
570 580
....*....|....*....|....
gi 688611673 1548 IVDPGVIPINSRGEKQRMHLRDSF 1571
Cdd:cd05906 514 PLPKEEIPKTSLGKIQRSKLKAAF 537
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1032-1504 |
1.18e-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: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1032 TCSQLHKRAEKITAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQnlsatlPTVRMIIDVSKAA 1111
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1112 CILTTQTLMKTLRSKEAAASVNVKTWPNIIDtDDLPRKRPASiykPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCR 1191
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPVILLDPLELAALD-DAPAPPPPDA---PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1192 SIKlQCELYSSRQIAICmdpYCGLGF------VLWCLssvYSGHQSILIPPMELETSLPLWLSTLSQYKIRDTFCSYSVM 1265
Cdd:TIGR01733 151 WLA-RRYGLDPDDRVLQ---FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1266 ELCTKGLGTQTEALKArnvnlscvrscVVIAEERPRLALTQSFSKLFKDLGLspravstafgsrVNlaiclqgTAGPDPS 1345
Cdd:TIGR01733 224 ALLAAALPPALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN-------LYGPTET 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1346 TVYVDMKSLRHDRVRLVErgapqSLPLmesGTMLPGVRVIIVNPETKgPLGDSHLGEIWVNSPHNASGYytiYGEESLQA 1425
Cdd:TIGR01733 274 TVWSTATLVDPDDAPRES-----PVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTA 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611673 1426 DHFNTRLSFGDTETLWARTGYLGfvkRtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESAV 1504
Cdd:TIGR01733 342 ERFVPDPFAGGDGARLYRTGDLV---R---YLPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLRHPGVREAVV 409
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
352-830 |
5.16e-19 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 91.60 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 352 AKSPALTALDITGKplYTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSdPGMFwVAFYGCLLAEVIPV 431
Cdd:pfam00501 6 ARTPDKTALEVGEG--RRLTYRELDERANRLAAGLR-ALG------VGKGDRVAILLPNS-PEWV-VAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 432 PIEVplsrkDAGSQQIGFLLGSCGVGLALTSEVCL--KGLPKTPNGEIMQFKGW-PRLKWVVTDTKYLTKPSKDWQPHIP 508
Cdd:pfam00501 75 PLNP-----RLPAEELAYILEDSGAKVLITDDALKleELLEALGKLEVVKLVLVlDRDPVLKEEPLPEEAKPADVPPPPP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 509 TANT--DTAYIEYKASKEGTVMGVavskisMLTHCQALTQACN----------YCEGETLVNVLDFKKDSGLWHGVLTSV 576
Cdd:pfam00501 150 PPPDpdDLAYIIYTSGTTGKPKGV------MLTHRNLVANVLSikrvrprgfgLGPDDRVLSTLPLFHDFGLSLGLLGPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 577 MNRiHTISVPYAVMKACPLSWVQRVHVHKARV-----ALVKcrdlhwAMMAHRDQKDTNLSSLRMLIVadGANPWSVSSC 651
Cdd:pfam00501 224 LAG-ATVVLPPGFPALDPAALLELIERYKVTVlygvpTLLN------MLLEAGAPKRALLSSLRLVLS--GGAPLPPELA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 652 DAFLNVF-----QSHGLKpEMiCPCASSPEAMTVAIRRPGAPGTPLParailsmaglshgvirvNTEdknsaltvqdvgh 726
Cdd:pfam00501 295 RRFRELFggalvNGYGLT-ET-TGVVTTPLPLDEDLRSLGSVGRPLP-----------------GTE------------- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 727 vmpgalMCIVKPDG----PPmlcktDEIGEIVLNSRAGGTMYYGLPGVTKNTFevipVNSGgtpigdvpFTRTGLLGFVG 802
Cdd:pfam00501 343 ------VKIVDDETgepvPP-----GEPGELCVRGPGVMKGYLNDPELTAEAF----DEDG--------WYRTGDLGRRD 399
|
490 500
....*....|....*....|....*...
gi 688611673 803 PgslvfvvgkiEGLLSVSGRrhnADDLV 830
Cdd:pfam00501 400 E----------DGYLEIVGR---KKDQI 414
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
337-929 |
2.11e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.54 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 337 PPALQAALARWGATQAKSPALTALDITGKPLYTLTYGKLWSRSLKLAYTLLNKLGtknepvlkPGDRVALVYPnSDPGmF 416
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS--------FGDRAVLLFP-SGPD-Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 417 WVAFYGCLLAEVIPVPIEVPLSRKDAGSQQIGFLLGSCGVGLALTSEVCLKGLPktpngEIMQFKGWPRLKWVVTDTkYL 496
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLL-----QMEELAAANAPELLCVDT-LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 497 TKPSKDWQ-PHIPTanTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEG--ETLVNVLDFKKDSGLWHGVL 573
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 574 TSVMNRIHTISVPYAVMKACPLSWVQRVHVHKARVAlvKCRDLHWAMMAHRdQKDTNLSSL---RMLIVADGANPWSVSS 650
Cdd:PRK05691 230 QPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTIS--GGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEPIRQDS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 651 CDAFLNVFQSHGLKPEMICPCASSPEA-MTVAirrPGAPGTPLPARAILSMAglshgvIRVNTEDKNSALTVQDVGHVMP 729
Cdd:PRK05691 307 LERFAEKFAACGFDPDSFFASYGLAEAtLFVS---GGRRGQGIPALELDAEA------LARNRAEPGTGSVLMSCGRSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 730 GALMCIVKPDGPPMLcKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFevipVNSGGTpigdvPFTRTGLLGFVGPGSLvFV 809
Cdd:PRK05691 378 GHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGDLGFLRDGEL-FV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 810 VGKIEGLLSVSGRRHNADDLVATalAVEPVKTVYRGRIAVFSVTVFYDERVVIVAE-----QRPDANEEdsfqWMSRVLQ 884
Cdd:PRK05691 447 TGRLKDMLIVRGHNLYPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQA----LIKSIRQ 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 688611673 885 AIDSIHQVGLYCLALVPANTLPKTPLGGIHVSETKHHFLEGSLHP 929
Cdd:PRK05691 521 AVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDS 565
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1034-1573 |
1.22e-16 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 85.20 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1034 SQLHKRAEKITAALLERGGINTgdnVVLLYPPGIDLIASFYGCLYAG----CIPVTVRPPHPQNLSATLPTVRMIIDVSK 1109
Cdd:PRK05851 35 PEVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1110 aacILTTQTLMKTLRSKEAAASV-NVKTWPNiidtddlpRKRPASIYKPPTAEmLAYLDFSVSTTGMLTGVKMSHSAVNA 1188
Cdd:PRK05851 112 ---VLSHGSHLERLRAVDSSVTVhDLATAAH--------TNRSASLTPPDSGG-PAVLQGTAGSTGTPRTAILSPGAVLS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1189 LCRSIKLQCELYSSRQIAICMDPY---CGLGFVLwclSSVYSGHQSILIPPMELETSLPLWLSTLSQYkiRDTFCSYSVM 1265
Cdd:PRK05851 180 NLRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSDS--RATLTAAPNF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1266 ELCTKGlgtqTEALKARNVNLSCVRsCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFGsrvnLAICLQGTAGPDPS 1345
Cdd:PRK05851 255 AYNLIG----KYARRVSDVDLGALR-VALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYG----LAESTCAVTVPVPG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1346 TvyvdmkSLRHDRVRLVERGAPQSLPLMesGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYytiYGEESLQA 1425
Cdd:PRK05851 326 I------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---LGQAPIDP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1426 DHfntrlsfgdtetlWARTGYLGFvkrteLLDasgdrhDALFVVGSLDETLELRGLRYHPIDIETSVS--RAHRSIAESA 1503
Cdd:PRK05851 395 DD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERVAAqvRGVREGAVVA 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611673 1504 VFTWTNL----LVVVVELSGSEQ-----EALDLVPLVTNVVLKEhhlivgvVVIVDPGVIPINSRGEKQRMHLRDSFLA 1573
Cdd:PRK05851 451 VGTGEGSarpgLVIAAEFRGPDEagarsEVVQRVASECGVVPSD-------VVFVAPGSLPRTSSGKLRRLAVKRSLEA 522
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1026-1509 |
5.94e-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: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1026 VAV----STATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLsatlptV 1101
Cdd:cd05930 4 VAVvdgdQSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1102 RMIIDVSKAACILTTQtlmktlrskeaaasvnvktwpniidtDDLprkrpasiykpptaemlAYLDFSVSTTGMLTGVKM 1181
Cdd:cd05930 77 AYILEDSGAKLVLTDP--------------------------DDL-----------------AYVIYTSGSTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1182 SHSAVNALCRSIKLQCELYSSRQIAICMdpycGLGF------VLWCLSSvysGHQSILIPPmELETSLPLWLSTLSQYKI 1255
Cdd:cd05930 114 EHRGLVNLLLWMQEAYPLTPGDRVLQFT----SFSFdvsvweIFGALLA---GATLVVLPE-EVRKDPEALADLLAEEGI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1256 RDTFCSYSVMELCTKGLGTQtealkarnvNLSCVRsCVVIAEERPRLALTQSFSKLFKDLGLspravstafgsrVNLAic 1335
Cdd:cd05930 186 TVLHLTPSLLRLLLQELELA---------ALPSLR-LVLVGGEALPPDLVRRWRELLPGARL------------VNLY-- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1336 lqgtaGPDPSTVYVDMKSLRHDRVrlvergAPQSLPLmesGTMLPGVRVIIVNPETKgPLGDSHLGEIWVNSPHNASGYy 1415
Cdd:cd05930 242 -----GPTEATVDATYYRVPPDDE------EDGRVPI---GRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLARGY- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1416 tiYGEESLQADHFnTRLSFGDTETLWaRTGYLGfvkRtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVsRA 1495
Cdd:cd05930 306 --LNRPELTAERF-VPNPFGPGERMY-RTGDLV---R---WLPDGN----LEFLGRIDDQVKIRGYRIELGEIEAAL-LA 370
|
490
....*....|....
gi 688611673 1496 HRSIAESAVFTWTN 1509
Cdd:cd05930 371 HPGVREAAVVARED 384
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1013-1489 |
4.11e-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: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1013 PDHVLYMLLNAKGVAVSTatcSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVtvrpphpq 1092
Cdd:cd05908 1 PEGIIFILGDKKEKFVSY---RHLREEALGYLGALQELG-IKPGQEVVFQITHNNKFLYLFWACLLGGMIAV-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1093 nlsatlPTVRMIIDVSKaacilttqtlMKTLRSkeaaasVNVKTWPNIIDTDDLPRKRPasiykpptaEMLAYLDFSVST 1172
Cdd:cd05908 69 ------PVSIGSNEEHK----------LKLNKV------WNTLKNPYLITEEEVLCELA---------DELAFIQFSSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1173 TGMLTGVKMSHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELETSLPLWLSTLSQ 1252
Cdd:cd05908 118 TGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1253 YKIRDTFCSYSVMELCTKGLGTQtealKARNVNLSCVRscVVIAEERPRLA-LTQSFSKLFKDLGLSPRAVSTAFG-SRV 1330
Cdd:cd05908 198 HKATIVSSPNFGYKYFLKTLKPE----KANDWDLSSIR--MILNGAEPIDYeLCHEFLDHMSKYGLKRNAILPVYGlAEA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1331 NLAICLQgTAGPDPSTVYVDMKSLRH-DRVRLVERGAPQSLPLMESGTMLPGVRVIIVNPETKGpLGDSHLGEIWVNSPH 1409
Cdd:cd05908 272 SVGASLP-KAQSPFKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGHIQIRGKN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1410 NASGYYTiyGEESlqadhfnTRLSFgdTETLWARTGYLGFVKRTELLdASGDRHDALFVVGSldetlelrglRYHPIDIE 1489
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 ... |
1009-1530 |
6.67e-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: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1009 AQTDPDHVLYMLLNAkgvavsTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGC--IPVTV 1086
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1087 RPPHPQnlsatlptVRMIIDVSKAACIlttqtlmktlrskeaaasvnvktwpnIIDTDDlprkrpasiykpptaemLAYL 1166
Cdd:cd05945 74 SSPAER--------IREILDAAKPALL--------------------------IADGDD-----------------NAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1167 DFSVSTTGMLTGVKMSHSAVNALCRSIkLQCELYSSRQIAIC----------MDPYCGL--GFVLWCLSsvysghQSILI 1234
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNqapfsfdlsvMDLYPALasGATLVPVP------RDATA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1235 PPMELETSLP-----LWLSTLsqykirdtfcsySVMELCTkGLGTQTEAlkarnvNLSCVRSCVVIAEERPrLALTQSFS 1309
Cdd:cd05945 176 DPKQLFRFLAehgitVWVSTP------------SFAAMCL-LSPTFTPE------SLPSLRHFLFCGEVLP-HKTARALQ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1310 KLFkdlglsPRAvstafgsRV-NlaiclqgTAGPDPSTVYVdmksLRHDRVRLVERGAPqSLPLmesGTMLPGVRVIIVN 1388
Cdd:cd05945 236 QRF------PDA-------RIyN-------TYGPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVILD 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1389 PETKgPLGDSHLGEIWVNSPHNASGYytiYGEESLQADHFntrlsFGDTETLWARTGYLGFvkrtelLDASGdrhdALFV 1468
Cdd:cd05945 288 EDGR-PVPPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQRAYRTGDLVR------LEADG----LLFY 348
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688611673 1469 VGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAVFTWTNL-----LVVVVELSGSEqEALDLVPL 1530
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 ... |
1032-1504 |
2.75e-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: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1032 TCSQLHKRAEKITAALLERGGINtGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPphpqnlSATLPTVRMIIDVSKAA 1111
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1112 CILTTQTLMKTLRSkeAAASVnvktwpniIDTDDLPrKRPASIYK---------PPTAEM----LAYLDFSVSTTGMLTG 1178
Cdd:cd05904 107 LAFTTAELAEKLAS--LALPV--------VLLDSAE-FDSLSFSDllfeadeaePPVVVIkqddVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1179 VKMSH-SAVNALCRSIKLQCELYSSRQIAICMDPYCGL-GFVLWCLSSVYSGHQSILIPPMELETslplWLSTLSQYKIR 1256
Cdd:cd05904 176 VMLTHrNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKVT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1257 DTFCSYSVMELCTKglgtqteALKARNVNLSCVRSCVViaeerprlaltqsfsklfkdlGLSP--RAVSTAFGSRVNLAI 1334
Cdd:cd05904 252 HLPVVPPIVLALVK-------SPIVDKYDLSSLRQIMS---------------------GAAPlgKELIEAFRAKFPNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1335 CLQG----TAGPDPSTVYVDMKSlrhdrvrlveRGAPQSlplmeSGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHN 1410
Cdd:cd05904 304 LGQGygmtESTGVVAMCFAPEKD----------RAKYGS-----VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1411 ASGYytiygeeslqadhfntrlsFGDTE----TL----WARTGYLGFVkrtellDASGDrhdaLFVVGSLDETLELRGLR 1482
Cdd:cd05904 369 MKGY-------------------LNNPEataaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQ 419
|
490 500
....*....|....*....|..
gi 688611673 1483 YHPIDIEtSVSRAHRSIAESAV 1504
Cdd:cd05904 420 VAPAELE-ALLLSHPEILDAAV 440
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
361-821 |
3.52e-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: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 361 DITGKplyTLTYGKLWSRSLKLAYTLlNKLGtknepvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPI------- 433
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGL-RKLG------LKKGDVVGIISPNST--YYPPVFLGCLFAGGIFSAAnpiytad 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 434 EVPLSRKDAGSQqigFLLgscgvglaltseVCLKGLPKTpngeIMQFKGWPRLK--WVVTDTK-YLTKPSKDWQPHIPT- 509
Cdd:cd05911 73 ELAHQLKISKPK---VIF------------TDPDGLEKV----KEAAKELGPKDkiIVLDDKPdGVLSIEDLLSPTLGEe 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 510 ----------ANTDTAYIEYKASKEGTVMGVAVS---KISMLTHCQALTQAcNYCEGETLVNVLDFKKDSGLWhGVLTSV 576
Cdd:cd05911 134 dedlppplkdGKDDTAAILYSSGTTGLPKGVCLShrnLIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGLF-TTLASL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 577 MNRIHTIsvpyaVM-KACPLSWVQRVHVHKARVALVKCRdlHWAMMAHRDQKDT-NLSSLRMLIVadGANPWSVSSCDAF 654
Cdd:cd05911 212 LNGATVI-----IMpKFDSELFLDLIEKYKITFLYLVPP--IAAALAKSPLLDKyDLSSLRVILS--GGAPLSKELQELL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 655 LNVF------QSHGLKpEMICPCASSPEAmtvaIRRPGApgtplparailsmaglshgvirvntedknsaltvqdVGHVM 728
Cdd:cd05911 283 AKRFpnatikQGYGMT-ETGGILTVNPDG----DDKPGS------------------------------------VGRLL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 729 PGALMCIVKPDGPPMLcKTDEIGEIVLNsraGGTM---YYGLPGVTKNTFEvipvnSGGtpigdvpFTRTGLLGFVGPGS 805
Cdd:cd05911 322 PNVEAKIVDDDGKDSL-GPNEPGEICVR---GPQVmkgYYNNPEATKETFD-----EDG-------WLHTGDIGYFDEDG 385
|
490
....*....|....*.
gi 688611673 806 LVFVVGKIEGLLSVSG 821
Cdd:cd05911 386 YLYIVDRKKELIKYKG 401
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
398-911 |
4.63e-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: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 398 LKPGDRVALVYPNSDPG---MFWVAFYGCLLAEVIpvpieVPLSrKDAGSQQIGFLLGSCGVGLALTSEVCL----KGLP 470
Cdd:cd05922 15 GVRGERVVLILPNRFTYielSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADAGAAdrlrDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 471 KTPNGEimqfkgwprlkwVVTDTKYLTKPSKDWQPHIPtANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNY 550
Cdd:cd05922 89 ASPDPG------------TVLDADGIRAARASAPAHEV-SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 551 CEGETLVNVLDFKKDSGLwhGVLTSVMNR-----IHTISV-PYAVMKACplswvqRVHvhkaRVALVKCRDLHWAMMAHR 624
Cdd:cd05922 156 TADDRALTVLPLSYDYGL--SVLNTHLLRgatlvLTNDGVlDDAFWEDL------REH----GATGLAGVPSTYAMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 625 DQKDTNLSSLRMLIVADGANPwsvsscdaflnvfqshglkpemicpcasspeAMTVAIRRPGAPGTplparAILSMAGLS 704
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLP-------------------------------QETIARLRELLPGA-----QVYVMYGQT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 705 HGVIRVNTEDKNSALTVQD-VGHVMPGALMCIVKPDGPPmlCKTDEIGEIVLNsraGGTMYYGLPgvtkNTFEVIPvnSG 783
Cdd:cd05922 268 EATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTP--TPPGEPGEIVHR---GPNVMKGYW----NDPPYRR--KE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 784 GTPIGDVpftRTGLLGFVGPGSLVFVVGKIEGLLSVSGRRHNADDLVATALAVEPVKTVyrgriAVFSVTVFYDERVVIV 863
Cdd:cd05922 337 GRGGGVL---HTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA-----AAVGLPDPLGEKLALF 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 688611673 864 AEqRPDANEEDSfqwMSRVLQAIDSIHQVGLYClalVPANTLPKTPLG 911
Cdd:cd05922 409 VT-APDKIDPKD---VLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
338-776 |
6.95e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 66.75 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 338 PALQAALARWGATqaKSPALTALDITGKplyTLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSDpgMFW 417
Cdd:PRK06187 5 PLTIGRILRHGAR--KHPDKEAVYFDGR---RTTYAELDERVNRLANALRA-LG------VKKGDRVAVFDWNSH--EYL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 418 VAFYGCLLAEVIPVPIEVPLSrkdagSQQIGFLLGSCG-----VGLALTSEVClKGLPKTPNGEimqfkgwprlKWVVTD 492
Cdd:PRK06187 71 EAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEdrvvlVDSEFVPLLA-AILPQLPTVR----------TVIVEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 493 TKYLTKPSKDWQ-------------PHIPTANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEgetlvnv 559
Cdd:PRK06187 135 DGPAAPLAPEVGeyeellaaasdtfDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 560 ldfkKDSGLwhgVLTSvMNRIHTISVPY-AVMKACPLSWVQRVH-------VHKARVALVKCRDLHWAMM-AHRDQKDTN 630
Cdd:PRK06187 208 ----DDVYL---VIVP-MFHVHAWGLPYlALMAGAKQVIPRRFDpenlldlIETERVTFFFAVPTIWQMLlKAPRAYFVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 631 LSSLRMLIVadGANPWSVSSCDAFLNVF-----QSHGLKpEMiCPCASS---PEAMTVAIRRPGAPGTPLParailsmag 702
Cdd:PRK06187 280 FSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGMT-ET-SPVVSVlppEDQLPGQWTKRRSAGRPLP--------- 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688611673 703 lshGV-IRvntedknsaltvqdvghvmpgalmcIVKPDGPPMLCKTDEIGEIVLnsRAGGTM--YYGLPGVTKNTFE 776
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) ... |
1009-1504 |
5.83e-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: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1009 AQTDPDHVLymlLNAKGVAVSTAtcsQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRP 1088
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRL-AHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1089 PHPQnlsatlPTVRMIIDVSKAACILTTQTLmkTLRSKEAAASVNVKTWPNIIDTDDLPRKRPasiykpPTAEMLAYLDF 1168
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPAL--AGELAVELVAVTLLDQPGAAAGADAEPDPA------LDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1169 SVSTTGMLTGVKMSHSAVNALCRSiklQCELYSsrqiaicMDP------YCGLGF--VLWCLSSVYSGHQSILIPPMELE 1240
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVAW---QARASS-------LGPgartlqFAGLGFdvSVQEIFSTLCAGATLVLPPEEVR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1241 TSLPLWLSTLSQYKIRDTFCSYSVME-LCtkglgtqtEALKARNVNLSCVRsCVVIAEErpRLALTQSFSKLFKDLGlsp 1319
Cdd:cd17651 214 TDPPALAAWLDEQRISRVFLPTVALRaLA--------EHGRPLGVRLAALR-YLLTGGE--QLVLTEDLREFCAGLP--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1320 ravstafGSRvnlaicLQGTAGPDPSTVyVDMKSLRHDRVRlveRGAPQSLplmesGTMLPGVRVIIVNPETKgPLGDSH 1399
Cdd:cd17651 280 -------GLR------LHNHYGPTETHV-VTALSLPGDPAA---WPAPPPI-----GRPIDNTRVYVLDAALR-PVPPGV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1400 LGEIWVNSPHNASGYYTIYG--EESLQADHFNtrlsfgdTETLWARTGYLGfvkrteLLDASGDrhdaLFVVGSLDETLE 1477
Cdd:cd17651 337 PGELYIGGAGLARGYLNRPEltAERFVPDPFV-------PGARMYRTGDLA------RWLPDGE----LEFLGRADDQVK 399
|
490 500
....*....|....*....|....*..
gi 688611673 1478 LRGLRYHPIDIETSVsRAHRSIAESAV 1504
Cdd:cd17651 400 IRGFRIELGEIEAAL-ARHPGVREAVV 425
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1026-1521 |
2.87e-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: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1026 VAVS----TATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPqnlsatLPTV 1101
Cdd:cd12116 4 TAVRdddrSLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1102 RMIIDVSKAACILTTQTLMktlrskeAAASVNVKTWPNIIDTDDLPRKRPASiykPPTAEMLAYLDFSVSTTGMLTGVKM 1181
Cdd:cd12116 77 RYILEDAEPALVLTDDALP-------DRLPAGLPVLLLALAAAAAAPAAPRT---PVSPDDLAYVIYTSGSTGRPKGVVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1182 SHSAVNALCRSIKLQCELYSSRQIA----ICMDpycglgfvlwclssvysghqsILIppmeLETSLPLWlstlsqykird 1257
Cdd:cd12116 147 SHRNLVNFLHSMRERLGLGPGDRLLavttYAFD---------------------ISL----LELLLPLL----------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1258 tfcSYSVMELCTKGLGTQTEALKARnvnlscvrscvvIAEERPRLA-LTQSFSKLFKDLGLSPRAVSTAF-GSR---VNL 1332
Cdd:cd12116 191 ---AGARVVIAPRETQRDPEALARL------------IEAHSITVMqATPATWRMLLDAGWQGRAGLTALcGGEalpPDL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1333 AICLQGTA-------GPDPSTVYvdmkSLRHdRVRLVERGAPQSLPlmesgtmLPGVRVIIVNPETKgPLGDSHLGEIWV 1405
Cdd:cd12116 256 AARLLSRVgslwnlyGPTETTIW----STAA-RVTAAAGPIPIGRP-------LANTQVYVLDAALR-PVPPGVPGELYI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1406 NSPHNASGYytiYGEESLQADHFnTRLSFGDTETLWARTGYLgfVKRtelldasgDRHDALFVVGSLDETLELRGLRYHP 1485
Cdd:cd12116 323 GGDGVAQGY---LGRPALTAERF-VPDPFAGPGSRLYRTGDL--VRR--------RADGRLEYLGRADGQVKIRGHRIEL 388
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 688611673 1486 IDIETSVsRAHRSIAESAVFTWTN----LLVVVVELSGSE 1521
Cdd:cd12116 389 GEIEAAL-AAHPGVAQAAVVVREDggdrRLVAYVVLKAGA 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
340-697 |
1.06e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.74 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 340 LQAALARWGATQAKSPA------LTALDITGKP-----LY---TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVA 405
Cdd:PRK12316 4533 QQRIVALWNRTDAGYPAtrcvhqLVAERARMTPdavavVFdeeKLTYAELNRRANRLAHALI-ARG------VGPEVLVG 4605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 406 LVYPNSDPGMfwVAFYGCLLA--EVIPVPIEVPLSRkdagsqqIGFLLGSCGVGLALTSEVCLKGLPkTPNGeimqfkgw 483
Cdd:PRK12316 4606 IAMERSAEMM--VGLLAVLKAggAYVPLDPEYPRER-------LAYMMEDSGAALLLTQSHLLQRLP-IPDG-------- 4667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 484 prLKWVVTDtkyltkPSKDWQ------PHIPTANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLV 557
Cdd:PRK12316 4668 --LASLALD------RDEDWEgfpahdPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVL 4739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 558 NVLDFKKD---SGLWHGVLT--SVMNRIHTISVP---YAVMkacplswvqrvhvHKARVALVKCRDLHWAMMAHRDQKDT 629
Cdd:PRK12316 4740 QFMSFSFDgshEGLYHPLINgaSVVIRDDSLWDPerlYAEI-------------HEHRVTVLVFPPVYLQQLAEHAERDG 4806
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688611673 630 NLSSLRMLIVADGANP-------WSVSSCDAFLNVFqshGLKPEMICPCASSPEAMTVAIRRPGAPGTPLPARAI 697
Cdd:PRK12316 4807 EPPSLRVYCFGGEAVAqasydlaWRALKPVYLFNGY---GPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSG 4878
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
273-578 |
1.58e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.97 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 273 RVSTKIQQLLNTLKRPKRPPLSEFFLDDSEEIVEVPQPDPNTPRPEGRQiipvkgeplgvvsnwpPALQAALARWGATQA 352
Cdd:PRK12316 1954 RLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRG----------------PGVHQRIAEQAARAP 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 353 KSPALTALDitgkplYTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSDPGMfwVAFYGCLLA--EVIP 430
Cdd:PRK12316 2018 EAIAVVFGD------QHLSYAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERSFELV--VALLAVLKAggAYVP 2082
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 431 VPIEVPLSRkdagsqqIGFLLGSCGVGLALTSEVCLKGLPKTpngeimqfKGWPRLKwVVTDTKYLTKPSKDwqPHIPTA 510
Cdd:PRK12316 2083 LDPNYPAER-------LAYMLEDSGAALLLTQRHLLERLPLP--------AGVARLP-LDRDAEWADYPDTA--PAVQLA 2144
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688611673 511 NTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWhGVLTSVMN 578
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLN 2211
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
976-1193 |
2.57e-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: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 976 RDLGLIDDQEQSRKLCVW-----PTNMHQFLSEALQWRAQTDPDHVlymllnakgvAVSTA----TCSQLHKRAEKITAA 1046
Cdd:COG1020 448 GDLPLLTAAERQQLLAEWnataaPYPADATLHELFEAQAARTPDAV----------AVVFGdqslTYAELNARANRLAHH 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1047 LLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGC--IPvtvrpphpqnLSATLPT--VRMIIDVSKAACILTTQTLMKT 1122
Cdd:COG1020 518 LRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGARLVLTQSALAAR 586
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688611673 1123 LRSKEAaasvnvktwpNIIDTDDL-----PRKRPASiykPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSI 1193
Cdd:COG1020 587 LPELGV----------PVLALDALalaaePATNPPV---PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM 649
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
971-1529 |
2.96e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 971 AQASGRDLGLIDDQEQSRKLCVWPTN---------MHQFLSEalqwRAQTDPDHVLyMLLNAKgvavsTATCSQLHKRAE 1041
Cdd:PRK12316 4518 PQRRLGELQLLEKAEQQRIVALWNRTdagypatrcVHQLVAE----RARMTPDAVA-VVFDEE-----KLTYAELNRRAN 4587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1042 KITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATlptvrMIIDvSKAACILTTQTLMK 1121
Cdd:PRK12316 4588 RLAHALIARG-VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAY-----MMED-SGAALLLTQSHLLQ 4660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1122 TLRSKEAAASVNV---KTWpniidtDDLPRKRPASiykPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCE 1198
Cdd:PRK12316 4661 RLPIPDGLASLALdrdEDW------EGFPAHDPAV---RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE 4731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1199 LYSSRQIAICMdPYCGLGFVlWCLSSVYSGHQSILIPPMELetSLPLWL-STLSQYKIRDTFCSYSVMELCTKGLGTQTE 1277
Cdd:PRK12316 4732 LTPDDRVLQFM-SFSFDGSH-EGLYHPLINGASVVIRDDSL--WDPERLyAEIHEHRVTVLVFPPVYLQQLAEHAERDGE 4807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1278 ALKARNVnlscvrscvviaeerprlaltqsfskLFKDLGLSPRAVSTAFGSRVNLAicLQGTAGPDPSTVYVdmkslRHD 1357
Cdd:PRK12316 4808 PPSLRVY--------------------------CFGGEAVAQASYDLAWRALKPVY--LFNGYGPTETTVTV-----LLW 4854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1358 RVRLVERGAPQSLPLmesGTMLPGVRVIIVNPETkGPLGDSHLGEIWVNSPHNASGYYTiygEESLQADHFNTRlSFGDT 1437
Cdd:PRK12316 4855 KARDGDACGAAYMPI---GTPLGNRSGYVLDGQL-NPLPVGVAGELYLGGEGVARGYLE---RPALTAERFVPD-PFGAP 4926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1438 ETLWARTGYLgfvkrtelldASGDRHDALFVVGSLDETLELRGLRYHPIDIETSVsRAHRSIAESavftwtnlLVVVVEL 1517
Cdd:PRK12316 4927 GGRLYRTGDL----------ARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA--------VVIAQEG 4987
|
570
....*....|..
gi 688611673 1518 SGSEQEALDLVP 1529
Cdd:PRK12316 4988 AVGKQLVGYVVP 4999
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
352-775 |
3.03e-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: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 352 AKSPALTALDITGKPLytlTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSdPgMFWVAFYGCLLAEVIPV 431
Cdd:cd05936 10 RRFPDKTALIFMGRKL---TYRELDALAEAFAAGLQN-LG------VQPGDRVALMLPNC-P-QFPIAYFGALKAGAVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 432 PIEvPLSrkdaGSQQIGFLLGSCGVGLALTSEvclkglpktpngeimqfkgwPRLKWVVTDTKYLTKPskdwqphIPTAN 511
Cdd:cd05936 78 PLN-PLY----TPRELEHILNDSGAKALIVAV--------------------SFTDLLAAGAPLGERV-------ALTPE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 512 tDTAYIEYKAskeGTvmgVAVSKISMLTH---------CQALTQACNYcEGETLVNVLDFKKDSGLWHGVLTSVMNRIHT 582
Cdd:cd05936 126 -DVAVLQYTS---GT---TGVPKGAMLTHrnlvanalqIKAWLEDLLE-GDDVVLAALPLFHVFGLTVALLLPLALGATI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 583 ISVP----YAVMKACplswvqrvhvHKARV-ALVKCRDLHWAMMAHRDQKDTNLSSLRMLIvaDGANPWSVSSCDAFLNV 657
Cdd:cd05936 198 VLIPrfrpIGVLKEI----------RKHRVtIFPGVPTMYIALLNAPEFKKRDFSSLRLCI--SGGAPLPVEVAERFEEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 658 FQS-----HGLKpEMiCP--CASSPEamtvAIRRPGAPGTPLParailsmaglshgvirvNTEDKnsaltvqdvghvmpg 730
Cdd:cd05936 266 TGVpivegYGLT-ET-SPvvAVNPLD----GPRKPGSIGIPLP-----------------GTEVK--------------- 307
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 688611673 731 almcIVKPDGPPMlcKTDEIGEIVLnsRAGGTM--YYGLPGVTKNTF 775
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 ... |
529-913 |
3.12e-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: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 529 GVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWhGVLTSVMNRIHTISVPyavmKACPLSWVQRVHVHKARV 608
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 609 ALVKcRDLHWAMMAHRDQKDTNLSSLRMLIVadGANPWSVSSCDAFLNVF-----QSHGLKPEMICPCASSPEAMtvaIR 683
Cdd:cd04433 92 LLGV-PTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPgiklvNGYGLTETGGTVATGPPDDD---AR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 684 RPGAPGTPLParailsmaglshgvirvNTEDKnsaltvqdvghvmpgalmcIVKPDGPPmlCKTDEIGEIVLNSRAGGTM 763
Cdd:cd04433 166 KPGSVGRPVP-----------------GVEVR-------------------IVDPDGGE--LPPGEIGELVVRGPSVMKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 764 YYGLPGVTKNTFEvipvnsGGtpigdvpFTRTGLLGFVGPGSLVFVVGKIEGLLSVSGRRHNADDLVATALAVEPVKTVy 843
Cdd:cd04433 208 YWNNPEATAAVDE------DG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEA- 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688611673 844 rgriAVFSVtvfYDER------VVIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVglyclalVPANTLPKTPLGGI 913
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 ... |
1001-1504 |
3.39e-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: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1001 LSEALQWRAQTDPDHVLYMLLNAKgvavstATCSQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAG 1080
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK------LTYRELDALAEAF-AAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1081 CIPVTVRPphpqnlsatlptvrmiidvskaacILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPAsiykpPTA 1160
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1161 EMLAYLDFSVSTTGMLTGVKMSHSAV--NALcrsiklQC-----ELYSSRQIAICMDP-YCGLGFVLWCLSSVYSGHQSI 1232
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLvaNAL------QIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1233 LIP---PMELetslplwLSTLSQYKIrDTFCsysvmelctkGLGTQTEAL----KARNVNLSCVRSCvviaeerprlalt 1305
Cdd:cd05936 199 LIPrfrPIGV-------LKEIRKHRV-TIFP----------GVPTMYIALlnapEFKKRDFSSLRLC------------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1306 qsfsklfkdlgLS-----PRAVSTAFGSRVNLAIcLQG----TAGP----DPSTvyvdmkslRHDRVRLVergapqslpl 1372
Cdd:cd05936 248 -----------ISggaplPVEVAERFEELTGVPI-VEGygltETSPvvavNPLD--------GPRKPGSI---------- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1373 mesGTMLPGVRVIIVNPETKgPLGDSHLGEIWVNSPHNASGYYTiYGEEslqadhfnTRLSFGDTetlWARTGYLGFVkr 1452
Cdd:cd05936 298 ---GIPLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYWN-RPEE--------TAEAFVDG---WLRTGDIGYM-- 359
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 688611673 1453 tellDASG-----DRHDALFVVGsldetlelrGLRYHPIDIEtSVSRAHRSIAESAV 1504
Cdd:cd05936 360 ----DEDGyffivDRKKDMIIVG---------GFNVYPREVE-EVLYEHPAVAEAAV 402
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1032-1566 |
1.08e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 56.54 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1032 TCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCiPVTV--RPPHPQNLSA----TLPTVRMIi 1105
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGA-SLTMlhQPTPRTDLAVwaedTLRVIGMI- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1106 dvsKAACILTTQTLMktlrskeAAASVNVKTWPNIIDTDDLPRKRPASIykPPTAE-MLAYLDFSVSTTGMLTGVKMSH- 1183
Cdd:PRK07768 108 ---GAKAVVVGEPFL-------AAAPVLEEKGIRVLTVADLLAADPIDP--VETGEdDLALMQLTSGSTGSPKAVQITHg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1184 ---SAVNALCRSIKLQCElyssRQIAICMDPYC-GLGFVLWCLSSVYSGHQSILIPPMELETSLPLWLSTLSQYKIRDTF 1259
Cdd:PRK07768 176 nlyANAEAMFVAAEFDVE----TDVMVSWLPLFhDMGMVGFLTVPMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1260 CSYSVMELCTKGLGTQTEAlkaRNVNLSCVRsCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFG-SRVNLAICLQG 1338
Cdd:PRK07768 252 APNFAYALLARRLRRQAKP---GAFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGmAEATLAVSFSP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1339 T-AGPDPSTVYVDMKSLRHdRVRLVERGAPQSLPLMesGTMLPGVRVIIVNpETKGPLGDSHLGEIWVNSPHNASGYYTI 1417
Cdd:PRK07768 328 CgAGLVVDEVDADLLAALR-RAVPATKGNTRRLATL--GPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYLTM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1418 YGEESLQADHfntrlsfGdtetlWARTGYLGFvkrtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVSRAH- 1496
Cdd:PRK07768 404 DGFIPAQDAD-------G-----WLDTGDLGY------LTEEGE----VVVCGRVKDVIIMAGRNIYPTDIERAAARVEg 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1497 -RSIAESAVFTWTNL----LVVVVE--LSGSEQEALDLVPLVTNVVLKEhhliVGV----VVIVDPGVIPINSRGEKQRM 1565
Cdd:PRK07768 462 vRPGNAVAVRLDAGHsregFAVAVEsnAFEDPAEVRRIRHQVAHEVVAE----VGVrprnVVVLGPGSIPKTPSGKLRRA 537
|
.
gi 688611673 1566 H 1566
Cdd:PRK07768 538 N 538
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1032-1578 |
1.09e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.09 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1032 TCSQLHKRAEKITAALLERGginTGDNVV--LLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATlptvrMIIDvSK 1109
Cdd:PRK12467 3122 SYAELNRRANRLAHRLIAIG---VGPDVLvgVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY-----MIED-SG 3192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1110 AACILTTQTLMKTLrskEAAASVNVKTwpniIDTDDLPRKRPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNAL 1189
Cdd:PRK12467 3193 VKLLLTQAHLLEQL---PAPAGDTALT----LDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANH 3265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1190 CRSIKLQCELYSSRQIAICMdPYCGLGFVLWCLSSVYSGHQsILIPPMELETSLPLWlSTLSQYKIrdtfcsySVMELCT 1269
Cdd:PRK12467 3266 LCWIAEAYELDANDRVLLFM-SFSFDGAQERFLWTLICGGC-LVVRDNDLWDPEELW-QAIHAHRI-------SIACFPP 3335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1270 KGLgtQTEALKARNVNLSCVRSCVVIAEERPRLALTQSFSKLfkdlglsPRAvstafgsrvnlaiCLQGTAGPDPSTVYV 1349
Cdd:PRK12467 3336 AYL--QQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKL-------KPR-------------GLTNGYGPTEAVVTV 3393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1350 DMKSLRHDRVRLvergaPQSLPLmesGTMLPGVRVIIV----NPETKGPLGDSHLGEIWVnsphnASGYYTiygEESLQA 1425
Cdd:PRK12467 3394 TLWKCGGDAVCE-----APYAPI---GRPVAGRSIYVLdgqlNPVPVGVAGELYIGGVGL-----ARGYHQ---RPSLTA 3457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1426 DHFNTRLSFGDTETLWaRTGYLGFVKRTELLDasgdrhdalfVVGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAvf 1505
Cdd:PRK12467 3458 ERFVADPFSGSGGRLY-RTGDLARYRADGVIE----------YLGRIDHQVKIRGFRIELGEIEARL-LQHPSVREAV-- 3523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688611673 1506 twtnllVVVVELSGSEQealdlvplvtnvvlkehhlIVGVVVIVDPGvipiNSRGEKQRMHLRDSfLADQLDP 1578
Cdd:PRK12467 3524 ------VLARDGAGGKQ-------------------LVAYVVPADPQ----GDWRETLRDHLAAS-LPDYMVP 3566
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
971-1193 |
2.42e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.12 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 971 AQASGRDLGLIDDQEQSRKLCVW-------PTN--MHQFLSEalqwRAQTDPDHVLymlLNAKGVAVSTAtcsQLHKRAE 1041
Cdd:PRK12316 1970 AQAALGELALLDAGERQRILADWdrtpeayPRGpgVHQRIAE----QAARAPEAIA---VVFGDQHLSYA---ELDSRAN 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1042 KITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATlptvrMIIDvSKAACILTTQTLMK 1121
Cdd:PRK12316 2040 RLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAY-----MLED-SGAALLLTQRHLLE 2112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688611673 1122 TLRSKEAAASVNVKT---WPniidtdDLPRKRPASIYKPptaEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSI 1193
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 ... |
1045-1568 |
3.92e-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: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1045 AALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATlpTVRMIIDVSKAACILTTQTLMKTLR 1124
Cdd:cd05922 7 ASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKES--VLRYLVADAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1125 sKEAAASVNVKTWpniIDTDDLPRKRPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCELYSSRQ 1204
Cdd:cd05922 85 -DALPASPDPGTV---LDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1205 IAICMdP--YC-GLGFVLwclSSVYSGHQSILIPPMELETSlplwlstlsqykirdtfcsysVMELCTKGLGT------Q 1275
Cdd:cd05922 161 ALTVL-PlsYDyGLSVLN---THLLRGATLVLTNDGVLDDA---------------------FWEDLREHGATglagvpS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1276 TEALKARnvnlscvrscVVIA-EERPRL-ALTQSFSKLfkdlglsPRAVSTAFGSrvnlaiclqgtAGPDpSTVYVdMKS 1353
Cdd:cd05922 216 TYAMLTR----------LGFDpAKLPSLrYLTQAGGRL-------PQETIARLRE-----------LLPG-AQVYV-MYG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1354 LRHDRVRLVERGAPQSLPLMES-GTMLPGVRVIIVNPEtKGPLGDSHLGEIWVNSPHNASGYYTIYGEEsLQADHFNTRL 1432
Cdd:cd05922 266 QTEATRRMTYLPPERILEKPGSiGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGGVL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1433 sfgdtetlwaRTGYLGFvkrtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAVF----TWT 1508
Cdd:cd05922 344 ----------HTGDLAR------RDEDGF----LFIVGRRDRMIKLFGNRISPTEIEAAA-RSIGLIIEAAAVglpdPLG 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1509 NLLVVVVELSgSEQEALDLVPLVTNVVlkEHHLIVGVVVIVDPgvIPINSRGEKQRMHLR 1568
Cdd:cd05922 403 EKLALFVTAP-DKIDPKDVLRSLAERL--PPYKVPATVRVVDE--LPLTASGKVDYAALR 457
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
994-1088 |
6.18e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 54.13 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 994 PTNMHQFLSEAlqwrAQTDPDHVLYMLLNAKG----VAVSTATCSQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDL 1069
Cdd:PRK09274 5 MANIARHLPRA----AQERPDQLAVAVPGGRGadgkLAYDELSFAELDARSDAI-AHGLNAAGIGRGMRAVLMVTPSLEF 79
|
90
....*....|....*....
gi 688611673 1070 IASFYGCLYAGCIPVTVRP 1088
Cdd:PRK09274 80 FALTFALFKAGAVPVLVDP 98
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1376-1572 |
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 688611673 1376 GTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYYTIYGEESLQADhfntrlsfgdtETLWARTGYLGFVkrtel 1455
Cdd:PLN02330 364 GFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTID-----------EDGWLHTGDIGYI----- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1456 lDASGDrhdaLFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESAVFTWTN-------LLVVVVELSGSEQEAlDLV 1528
Cdd:PLN02330 428 -DDDGD----IFIVDRIKELIKYKGFQVAPAELE-AILLTHPSVEDAAVVPLPDeeageipAACVVINPKAKESEE-DIL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 688611673 1529 PLVTNVVlkEHHLIVGVVVIVDPgvIPINSRGEKQRMHLRDSFL 1572
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 ... |
1029-1503 |
1.35e-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: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1029 STATCSQLHKRAEKITAALLErGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPhpqnlsatlptvrmiIDVS 1108
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTA-YGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG---------------MGRK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1109 K-AACIlttqtlmktlrsKEAAasvnvktwpniidtddlprkrPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSHSAVN 1187
Cdd:cd05910 65 NlKQCL------------QEAE---------------------PDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1188 ALCRSIKlqcELYSSRQIAICMDpycglGFVLWCLSSVYSGHQSIlIPPME----LETSLPLWLSTLSQYKIRDTFCSYS 1263
Cdd:cd05910 112 AQIDALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1264 VMELCtkglgtqTEALKARNVNLSCVRsCVVIAEERPRLALTQSFSKLfkdlgLSPRA-VSTAFGSRVNLAICLQGTagp 1342
Cdd:cd05910 183 LLERV-------ARYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEALPVSSIGS--- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1343 dpstvyvdmKSLRHDRVRLVERGAPQSLplmesGTMLPGVRVIIVnPETKGP---------LGDSHLGEIWVNSPHNASG 1413
Cdd:cd05910 247 ---------RELLATTTAATSGGAGTCV-----GRPIPGVRVRII-EIDDEPiaewddtleLPRGEIGEITVTGPTVTPT 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1414 YYTiygeeSLQADHFnTRLSFGDtETLWARTGYLGFvkrtelLDASGdrhdALFVVGSLDETLELRGLRYHPIDIEtSVS 1493
Cdd:cd05910 312 YVN-----RPVATAL-AKIDDNS-EGFWHRMGDLGY------LDDEG----RLWFCGRKAHRVITTGGTLYTEPVE-RVF 373
|
490
....*....|
gi 688611673 1494 RAHRSIAESA 1503
Cdd:cd05910 374 NTHPGVRRSA 383
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1001-1090 |
1.82e-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: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1001 LSEALQWRAQTDPDHVlymllnakgvAV----STATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGC 1076
Cdd:COG1021 27 LGDLLRRRAERHPDRI----------AVvdgeRRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFAL 95
|
90
....*....|....
gi 688611673 1077 LYAGCIPVTVRPPH 1090
Cdd:COG1021 96 FRAGAIPVFALPAH 109
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
560-925 |
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 688611673 560 LDFKKDSG-----LWHG-----VLTSVMNRIHTISVPYAVMKACPLSWVQrvHVHKARVALVKCRDLHWAMMAH--RDQK 627
Cdd:PRK05851 190 LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLS--WLSDSRATLTAAPNFAYNLIGKyaRRVS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 628 DTNLSSLRMLIvaDGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAmTVAIRRPGaPGTplparailsmaGLShgV 707
Cdd:PRK05851 268 DVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAES-TCAVTVPV-PGI-----------GLR--V 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 708 IRVNTEDKNSALTVQDVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVLNsraGGTMYYGLpgvtkntfevipvnSGGTPI 787
Cdd:PRK05851 331 DEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGV-AGREIGEIEIR---GASMMSGY--------------LGQAPI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 788 GDVPFTRTGLLGFVGPGSLVfVVGKIEGLLSVSGRRHNADDLVATALAVEPVKtvyRGRIavfsVTVFYDE-----RVVI 862
Cdd:PRK05851 393 DPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVR---EGAV----VAVGTGEgsarpGLVI 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688611673 863 VAEQR-PDaneEDSFQwmSRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGIHVSETKHHFLEG 925
Cdd:PRK05851 465 AAEFRgPD---EAGAR--SEVVQRVASECGVVPSDVVFVAPGSLPRTSSGKLRRLAVKRSLEAA 523
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1005-1528 |
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 688611673 1005 LQWRAQTDPDHVLYMLLNakgvavSTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPV 1084
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1085 tvrpPHPQNLSAtlPTVRMIIDVSKAACILttqtlmktlrskeaaasvnvktwpniidtDDLprkrpasiykpptaemlA 1164
Cdd:cd17631 74 ----PLNFRLTP--PEVAYILADSGAKVLF-----------------------------DDL-----------------A 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1165 YLDFSVSTTGMLTGVKMSHSAVNALCRSIKLQCELySSRQIAICMDPYC---GLGfvLWCLSSVYSGHQSILIPPMELET 1241
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1242 SLplwlSTLSQYKIRDTFcsysvmelctkGLGTQTEAL----KARNVNLSCVRsCVVIAEERPRLALTQSFsklfKDLGL 1317
Cdd:cd17631 179 VL----DLIERHRVTSFF-----------LVPTMIQALlqhpRFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1318 sprAVSTAFGsrvnlaiclQGTAGPdPSTVyvdMKSLRHDRvRLVERGAPqslplmesgtmLPGVRVIIVNPETKgPLGD 1397
Cdd:cd17631 239 ---KFVQGYG---------MTETSP-GVTF---LSPEDHRR-KLGSAGRP-----------VFFVEVRIVDPDGR-EVPP 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1398 SHLGEIWVNSPHNASGYYTiyGEESlqadhfnTRLSFGDTetlWARTGYLGFVkrtelldasgDRHDALFVVGSLDETLE 1477
Cdd:cd17631 290 GEVGEIVVRGPHVMAGYWN--RPEA-------TAAAFRDG---WFHTGDLGRL----------DEDGYLYIVDRKKDMII 347
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 688611673 1478 LRGLRYHPIDIETSVSRaHRSIAESAVF-----TWTNLLV-VVVELSGSEQEALDLV 1528
Cdd:cd17631 348 SGGENVYPAEVEDVLYE-HPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELI 403
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
327-431 |
3.41e-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: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 327 GEPLGvvsnwppalqAALARWGATQAKSPALTALDitgkplYTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVAL 406
Cdd:COG1021 24 GETLG----------DLLRRRAERHPDRIAVVDGE------RRLSYAELDRRADRLAAGLL-ALG------LRPGDRVVV 80
|
90 100
....*....|....*....|....*
gi 688611673 407 VYPNSdpGMFWVAFYGCLLAEVIPV 431
Cdd:COG1021 81 QLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
371-546 |
5.19e-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: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 371 TYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEV--PLSRkdagsqqIG 448
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERSAELV--VAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 449 FLLGSCGVGLALTSEvclkglpktPNGEIMQFKGWPRLKWVVTDTKYLTKPSKDWQPHIPTANTDTAYIEYKASKEGTVM 528
Cdd:TIGR01733 66 FILEDAGARLLLTDS---------ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170
....*....|....*...
gi 688611673 529 GVAVSKISMLTHCQALTQ 546
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLAR 154
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
369-490 |
9.82e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.34 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 369 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNSdPgMFWVAFYGCLLAEVIPVPIEvPLSRkdagSQQIG 448
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLLYMQNS-P-QFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 688611673 449 FLLGSCGVGLALTSEVCLkglpktpnGEIMQFKGWPRLKWVV 490
Cdd:PRK08314 102 HYVTDSGARVAIVGSELA--------PKVAPAVGNLRLRHVI 135
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
368-533 |
1.15e-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: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 368 YTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEV--PLSRKDAgsq 445
Cdd:cd12114 11 GTLTYGELAERARRVA-GALKAAG------VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 446 qigfLLGSCGVGLALTSEVCLKGLPKTPNgeimqfkgwprlkwVVTDTKYLTKPSKDwQPHIPTANTDTAYIEYKASKEG 525
Cdd:cd12114 79 ----ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP-PPPVDVAPDDLAYVIFTSGSTG 139
|
....*...
gi 688611673 526 TVMGVAVS 533
Cdd:cd12114 140 TPKGVMIS 147
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1026-1567 |
1.88e-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: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1026 VAVS----TATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPqnlsatLPTV 1101
Cdd:cd17643 4 VAVVdedrRLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1102 RMIIDVSKAACILTtqtlmktlrskeaaasvnvktwpniiDTDDlprkrpasiykpptaemLAYLDFSVSTTGMLTGVKM 1181
Cdd:cd17643 77 AFILADSGPSLLLT--------------------------DPDD-----------------LAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1182 SHSAVNALCRSIklQCELYSSRQIAICMDPYCGLGFVLWCLSSVYSGHQSILIPPMELETS---LPLWL-----STLSQy 1253
Cdd:cd17643 114 SHANVLALFAAT--QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSpedFARLLrdegvTVLNQ- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1254 kirdTFCSYSVMELCTKGLGTQTEALKArnvnlscvrscVVIAEERPRLALTQSFSKLFKDlgLSPRAvstafgsrVNLa 1333
Cdd:cd17643 191 ----TPSAFYQLVEAADRDGRDPLALRY-----------VIFGGEALEAAMLRPWAGRFGL--DRPQL--------VNM- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1334 iclqgtAGPDPSTVYVDMKSLRHDRVRLVERGapqslPLmesGTMLPGVRVIIVNpETKGPLGDSHLGEIWVNSPHNASG 1413
Cdd:cd17643 245 ------YGITETTVHVTFRPLDAADLPAAAAS-----PI---GRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1414 YytiYGEESLQADHFNTRLSFGDTETLWaRTGYLgfVKRTelldASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVs 1493
Cdd:cd17643 310 Y---LGRPELTAERFVANPFGGPGSRMY-RTGDL--ARRL----PDGE----LEYLGRADEQVKIRGFRIELGEIEAAL- 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1494 RAHRSIAESAVFTWTN------LLVVVVELSGSEQEALDLVPLvtnvvLKEH---HLIVGVVVIVDpgVIPINSRGEKQR 1564
Cdd:cd17643 375 ATHPSVRDAAVIVREDepgdtrLVAYVVADDGAAADIAELRAL-----LKELlpdYMVPARYVPLD--ALPLTVNGKLDR 447
|
...
gi 688611673 1565 MHL 1567
Cdd:cd17643 448 AAL 450
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1035-1504 |
1.99e-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: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1035 QLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNlsatlpTVRMIIDVSKAACIL 1114
Cdd:cd12117 27 ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE------RLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1115 TTQTLMKTLRSKEAAasvnvktwpniIDTDDLPRKRPASIYKPP-TAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRS- 1192
Cdd:cd12117 100 TDRSLAGRAGGLEVA-----------VVIDEALDAGPAGNPAVPvSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNt 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1193 --IKLQCELYSSRQIAICMDpycGLGFVLWclSSVYSGHQSILIPPMELETSLPLwLSTLSQYKIrdtfcsySVMELcTK 1270
Cdd:cd12117 169 nyVTLGPDDRVLQTSPLAFD---ASTFEIW--GALLNGARLVLAPKGTLLDPDAL-GALIAEEGV-------TVLWL-TA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1271 GLGTQtealkarnvnlscvrscvvIAEERPrlaltQSFSKLFKDL-G---LSPRAVSTAfgsrvnLAIC----LQGTAGP 1342
Cdd:cd12117 235 ALFNQ-------------------LADEDP-----ECFAGLRELLtGgevVSPPHVRRV------LAACpglrLVNGYGP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1343 DPSTVYvdmkSLRHdrvrLVERGAPQ--SLPLmesGTMLPGVRVIIVNpETKGPLGDSHLGEIWVNSPHNASGYytiYGE 1420
Cdd:cd12117 285 TENTTF----TTSH----VVTELDEVagSIPI---GRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGY---LNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1421 ESLQADHFnTRLSFGDTETLWaRTGYLgfVKRTElldasgdrhDALFV-VGSLDETLELRGLRYHPIDIETSVsRAHRSI 1499
Cdd:cd12117 350 PALTAERF-VADPFGPGERLY-RTGDL--ARWLP---------DGRLEfLGRIDDQVKIRGFRIELGEIEAAL-RAHPGV 415
|
....*
gi 688611673 1500 AESAV 1504
Cdd:cd12117 416 REAVV 420
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
352-439 |
2.54e-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: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 352 AKSPALTALDITGKplyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVAlVYPNSDPGMFwVAFYGCLLA--EVI 429
Cdd:cd05945 2 AANPDRPAVVEGGR---TLTYRELKERADALA-AALASLG------LDAGDPVV-VYGHKSPDAI-AAFLAALKAghAYV 69
|
90
....*....|
gi 688611673 430 PVPIEVPLSR 439
Cdd:cd05945 70 PLDASSPAER 79
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1007-1186 |
3.24e-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: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1007 WRAQTD--PDHVLymlLNAKGVAVSTAtcsQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPV 1084
Cdd:cd17646 4 VAEQAArtPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1085 TVRPPHPQnlsatlPTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPASiykpptaemLA 1164
Cdd:cd17646 77 PLDPGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDN---------LA 141
|
170 180
....*....|....*....|..
gi 688611673 1165 YLDFSVSTTGMLTGVKMSHSAV 1186
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHAGI 163
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
343-433 |
3.28e-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: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 343 ALARWGATQAKSPALTALDITGKPlYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSdPgMFWVAFYG 422
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDGEE-RTLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI-P-EAVIAMLA 83
|
90
....*....|.
gi 688611673 423 CLLAEVIPVPI 433
Cdd:COG0365 84 CARIGAVHSPV 94
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
345-455 |
4.80e-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: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 345 ARWGATQakSPALTALDITGKplyTLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSDPgmFWVAFYGCL 424
Cdd:cd17631 1 LRRRARR--HPDRTALVFGGR---SLTYAELDERVNRLAHALRA-LG------VAKGDRVAVLSKNSPE--FLELLFAAA 66
|
90 100 110
....*....|....*....|....*....|.
gi 688611673 425 LAEVIPVPIEVPLSRKDagsqqIGFLLGSCG 455
Cdd:cd17631 67 RLGAVFVPLNFRLTPPE-----VAYILADSG 92
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1009-1183 |
6.17e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 47.58 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1009 AQTDPDHVLYMLLNAkgvavsTATCSQLHKRAEKITAALLERGgiNTGDNVVLLY----PpgiDLIASFYGCLYAGC--I 1082
Cdd:PRK04813 12 AQTQPDFPAYDYLGE------KLTYGQLKEDSDALAAFIDSLK--LPDKSPIIVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1083 PVTVRPPhpqnlsatLPTVRMIIDVSKAACILTTQTLMKTLrskeaaasVNVKtwpnIIDTDDLprkrPASIYKPPTAEM 1162
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIATEELPLEI--------LGIP----VITLDEL----KDIFATGNPYDF 136
|
170 180
....*....|....*....|....*....
gi 688611673 1163 LA--------YLDFSVSTTGMLTGVKMSH 1183
Cdd:PRK04813 137 DHavkgddnyYIIFTSGTTGKPKGVQISH 165
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1044-1505 |
6.65e-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: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1044 TAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPvtvrppHPQNLSATLPTVRMIIDVSKAACILT-TQTLMKT 1122
Cdd:cd05926 27 LARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVV------APLNPAYKKAEFEFYLADLGSKLVLTpKGELGPA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1123 LRSKE------AAASVNVKTWPNIIDTDDLP----RKRPASIYKPPTAEMLAYLDFSVSTTGMLTGVKMSH----SAVNA 1188
Cdd:cd05926 101 SRAASklglaiLELALDVGVLIRAPSAESLSnllaDKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHrnlaASATN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1189 LCRSIKLqcelySSRQIAICMDP-YCGLGFVLWCLSSVYSGhQSILIPPMELETSL--------PLWLS---TLSQYKIR 1256
Cdd:cd05926 181 ITNTYKL-----TPDDRTLVVMPlFHVHGLVASLLSTLAAG-GSVVLPPRFSASTFwpdvrdynATWYTavpTIHQILLN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1257 DTfcsysvmelctkglGTQTEALKARnvnLSCVRSCvviaeerprlaltqSFSklfkdlgLSP---RAVSTAFGSRVNLA 1333
Cdd:cd05926 255 RP--------------EPNPESPPPK---LRFIRSC--------------SAS-------LPPavlEALEATFGAPVLEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1334 I-----CLQGTAGPdpstvyvdmksLRHDRVRLVERGAPQslplmesgtmlpGVRVIIVNpETKGPLGDSHLGEIWVNSP 1408
Cdd:cd05926 297 YgmteaAHQMTSNP-----------LPPGPRKPGSVGKPV------------GVEVRILD-EDGEILPPGVVGEICLRGP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1409 HNASGYYtiygeeslqADHFNTRLSFgdTETLWARTGYLGFvkrtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDI 1488
Cdd:cd05926 353 NVTRGYL---------NNPEANAEAA--FKDGWFRTGDLGY------LDADGY----LFLTGRIKELINRGGEKISPLEV 411
|
490
....*....|....*..
gi 688611673 1489 EtSVSRAHRSIAESAVF 1505
Cdd:cd05926 412 D-GVLLSHPAVLEAVAF 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
969-1504 |
1.03e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.26 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 969 RIAQASGRDLGLIDDQEQSRKL-------CVWPTN--MHQFLSEALQwraqtdpdhvlymlLNAKGVAVS----TATCSQ 1035
Cdd:PRK12316 476 ENPQARVDELPMLDAEERGQLVegwnataAEYPLQrgVHRLFEEQVE--------------RTPEAPALAfgeeTLDYAE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1036 LHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLSATLptvrmiIDVSKAACILT 1115
Cdd:PRK12316 542 LNRRANRLAHALIERG-VGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYM------LEDSGVQLLLS 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1116 TQTLMKTLrskEAAASVNVktwpniIDTDDLPRKRPASIYKPP----TAEMLAYLDFSVSTTGMLTGVKMSHSAVNALCR 1191
Cdd:PRK12316 615 QSHLGRKL---PLAAGVQV------LDLDRPAAWLEGYSEENPgtelNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLC 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1192 SIKLQCELYSSRQIA----ICMDpyCGLGFVLWCLSsvySGHQSILIPPMELETSLPLWlSTLSQYKIRdtfcsysVMEL 1267
Cdd:PRK12316 686 WMQQAYGLGVGDTVLqktpFSFD--VSVWEFFWPLM---SGARLVVAAPGDHRDPAKLV-ELINREGVD-------TLHF 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1268 CTKGLgtQTEALKARNVNLSCVRSCVVIAEERPRLALTQSFSKLFKdlglspravstafGSRVNLaiclqgtAGPDPSTV 1347
Cdd:PRK12316 753 VPSML--QAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQ-------------AGLYNL-------YGPTEAAI 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1348 YVDMKSLRHDRVRLVERGAPqslplmesgtmLPGVRVIIVNPETkGPLGDSHLGEIWVNSPHNASGYytiYGEESLQADH 1427
Cdd:PRK12316 811 DVTHWTCVEEGGDSVPIGRP-----------IANLACYILDANL-EPVPVGVLGELYLAGRGLARGY---HGRPGLTAER 875
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688611673 1428 FnTRLSFGDTETLWaRTGYLGFVKRTELLDasgdrhdalfVVGSLDETLELRGLRYHPIDIETSVSRaHRSIAESAV 1504
Cdd:PRK12316 876 F-VPSPFVAGERMY-RTGDLARYRADGVIE----------YAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAV 939
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1001-1196 |
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 688611673 1001 LSEALQWRAQTDPDHVLYMLLNAkGVAVSTaTCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAG 1080
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKED-GIWQSL-TWAEFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1081 CIPVTVrpphpqnlSATLPT--VRMIIDVSKA-ACILTTQTLMKTLRS----------------KEAAASVNVKTWPNII 1141
Cdd:COG1022 90 AVTVPI--------YPTSSAeeVAYILNDSGAkVLFVEDQEQLDKLLEvrdelpslrhivvldpRGLRDDPRLLSLDELL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688611673 1142 D------TDDLPRKRPASIykppTAEMLAYLDFSVSTTGMLTGVKMSH----SAVNALCRSIKLQ 1196
Cdd:COG1022 162 AlgrevaDPAELEARRAAV----KPDDLATIIYTSGTTGRPKGVMLTHrnllSNARALLERLPLG 222
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
336-439 |
1.42e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 46.57 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 336 WPP-------------ALQAALARWGATQAKSPALtalDITGkplYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGD 402
Cdd:PRK06178 18 WPAgiprepeyphgerPLTEYLRAWARERPQRPAI---IFYG---HVITYAELDELSDRFA-ALLRQRG------VGAGD 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 688611673 403 RVALVYPNSdPgMFWVAFYGCLLAEVIPVPIEvPLSR 439
Cdd:PRK06178 85 RVAVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFR 118
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
369-643 |
2.92e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 45.28 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 369 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSdpGMFWVAFYGCLLAEVIPVPIEvPLSRKDagsqQIG 448
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAA-LG------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPLN-TRYTAD----EAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 449 FLLGSCGVGLAL-------TSEVCLKGLPK----------TPNGEIMQFKGWprlkwvvtdTKYLTKPSKDWQpHIPTAN 511
Cdd:PRK07656 96 YILARGDAKALFvlglflgVDYSATTRLPAlehvviceteEDDPHTEKMKTF---------TDFLAAGDPAER-APEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 512 TDTAYIEYKASKEGTVMGVavskisMLTHCQALTQA---CNYC---EGETLVNVLDFKKDSGLWHGVLTSVMNRIHTISV 585
Cdd:PRK07656 166 DDVADILFTSGTTGRPKGA------MLTHRQLLSNAadwAEYLgltEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 688611673 586 PyavmKACPLSWVQRVHVHKARVaLVKCRDLHWAMMAHRDQKDTNLSSLRmLIVADGA 643
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 ... |
1376-1569 |
3.93e-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: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1376 GTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYY-----TiygEESLQADHfntrlsfgdtetlWARTGYLGFV 1450
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWnkpeaT---KEEFTDDG-------------WFKTGDLGVV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1451 krtellDASGdrhdALFVVG-SLDETLELRGLRYHPIDIEtSVSRAHRSIAESAVF-----TWTNLLVVVVELSgSEQEA 1524
Cdd:cd05941 331 ------DEDG----YYWILGrSSVDIIKSGGYKVSALEIE-RVLLAHPGVSECAVIgvpdpDWGERVVAVVVLR-AGAAA 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 688611673 1525 LDLVPLVTNvvLKEH---HLIVGVVVIVDpgVIPINSRGEKQRMHLRD 1569
Cdd:cd05941 399 LSLEELKEW--AKQRlapYKRPRRLILVD--ELPRNAMGKVNKKELRK 442
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
369-544 |
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 688611673 369 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPIEVPLSRKDagsqqIG 448
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLD-LG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 449 FLLGSCGVGLALTSEVCLKGLPKTPNGEIMQFKGWPRL--------KWVVTDTKYLTKPSKDWQPHIptANTDTAYIEYK 520
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreapgGWLDFADWAEAGSVAEPDVEL--ADDDLAQILYT 179
|
170 180
....*....|....*....|....
gi 688611673 521 ASKEGTVMGVavskisMLTHcQAL 544
Cdd:PRK08316 180 SGTESLPKGA------MLTH-RAL 196
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1030-1504 |
5.51e-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: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1030 TATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPphpqnlsatlptvrmiidvsk 1109
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1110 aacILTTQTLMKTLRSKEAAASvnvktwpnIIDTDDlprkrpasiykpptaemLAYLDFSVSTTGMLTGVKMSHSA---- 1185
Cdd:cd05919 68 ---LLHPDDYAYIARDCEARLV--------VTSADD-----------------IAYLLYSSGTTGPPKGVMHAHRDpllf 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1186 VNALCRSI-KLQCE--LYSSRQIAICMdpycGLGFVLWclSSVYSGHQSILIPPMELETSLplwLSTLSQYKIRdTFCSY 1262
Cdd:cd05919 120 ADAMAREAlGLTPGdrVFSSAKMFFGY----GLGNSLW--FPLAVGASAVLNPGWPTAERV---LATLARFRPT-VLYGV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1263 SVMELCTKGLGTQTEALkarnvnLSCVRSCVVIAEERPRlaltqSFSKLFKDLGLSPraVSTAFGSRVNLAICLqgtagp 1342
Cdd:cd05919 190 PTFYANLLDSCAGSPDA------LRSLRLCVSAGEALPR-----GLGERWMEHFGGP--ILDGIGATEVGHIFL------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1343 dpstvyvdmkSLRHDRVRLVERGAPqslplmesgtmLPGVRVIIVNPETKgPLGDSHLGEIWVNSPHNASGYYTIYGEes 1422
Cdd:cd05919 251 ----------SNRPGAWRLGSTGRP-----------VPGYEIRLVDEEGH-TIPPGEEGDLLVRGPSAAVGYWNNPEK-- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1423 lqadhfnTRLSFGDTetlWARTGYLGFVkrtellDASGdrhdALFVVGSLDETLELRGLRYHPIDIETSVSRaHRSIAES 1502
Cdd:cd05919 307 -------SRATFNGG---WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVSPVEVESLIIQ-HPAVAEA 365
|
..
gi 688611673 1503 AV 1504
Cdd:cd05919 366 AV 367
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1376-1495 |
7.31e-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: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1376 GTMLPGVRVIIVNPETKGPLGDSHlGEIWVNSPHNASGYYTiygEESLQADHFNTRlsfgdtetlWARTGYLGFVKrtel 1455
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 688611673 1456 ldasgdRHDALFVVGSLDETLELRGLRYHPIDIETSVSRA 1495
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVERIAEGV 269
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1001-1189 |
1.00e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 43.88 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1001 LSEALQWRAQTDPDhvlymllnAKGVAVSTATCSQLHKRAEKIT-AALLERGGINTGDNVVLLYPPGIDLIASFYGCLYA 1079
Cdd:PRK10252 460 LSALVAQQAAKTPD--------APALADARYQFSYREMREQVVAlANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1080 GCIPVTVRPPHPQNlsatlpTVRMIIDVSKAACILTTQTLMKTLRSKEAAASVNVKTWPNIIDTDDLPRKRPASiykppt 1159
Cdd:PRK10252 532 GAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHH------ 599
|
170 180 190
....*....|....*....|....*....|.
gi 688611673 1160 aemLAYLDFSVSTTGMLTGVKMSHSA-VNAL 1189
Cdd:PRK10252 600 ---TAYIIFTSGSTGRPKGVMVGQTAiVNRL 627
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
999-1090 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 999 QFLSEALQWRAQTDPDHVlymllnakgvAVSTA----TCSQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFY 1074
Cdd:cd05920 15 EPLGDLLARSAARHPDRI----------AVVDGdrrlTYRELDRRADRL-AAGLRGLGIRPGDRVVVQLPNVAEFVVLFF 83
|
90
....*....|....*.
gi 688611673 1075 GCLYAGCIPVTVRPPH 1090
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 ... |
1375-1452 |
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 688611673 1375 SGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYY-----TiygEESLQADH-FNTrlsfGDTETlWARTGYLG 1448
Cdd:cd17640 266 VGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYknpeaT---SKVLDSDGwFNT----GDLGW-LTCGGELV 337
|
....
gi 688611673 1449 FVKR 1452
Cdd:cd17640 338 LTGR 341
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1035-1186 |
2.11e-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: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1035 QLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVrpphpqnlSATLPTVRM--IIDVSKAAC 1112
Cdd:cd12114 17 ELAERARRV-AGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV--------DIDQPAARReaILADAGARL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688611673 1113 ILTTQTLmktlrskeAAASVNVKTWPNIIDTDDLPRKRPASIykPPTAEMLAYLDFSVSTTGMLTGVKMSHSAV 1186
Cdd:cd12114 88 VLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPPV--DVAPDDLAYVIFTSGSTGTPKGVMISHRAA 151
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1008-1267 |
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 688611673 1008 RAQTDPDHVlymllnakgvAV----STATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIP 1083
Cdd:cd17655 6 QAEKTPDHT----------AVvfedQTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1084 VTVRPPHPQNlsatlpTVRMIIDVSKAACILTTqtlmKTLRSKEAAASVNVktwpnIIDTDDLPRKRPASIYKPPTAEML 1163
Cdd:cd17655 75 LPIDPDYPEE------RIQYILEDSGADILLTQ----SHLQPPIAFIGLID-----LLDEDTIYHEESENLEPVSKSDDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1164 AYLDFSVSTTGMLTGVKMSH--------SAVNALCRSIKLQCELYSSrqiaICMDpycglGFVLWCLSSVYSGHqSILIP 1235
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFD-----ASVTEIFASLLSGN-TLYIV 209
|
250 260 270
....*....|....*....|....*....|..
gi 688611673 1236 PMELETSLPLWLSTLSQYKIRDTFCSYSVMEL 1267
Cdd:cd17655 210 RKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1381-1505 |
2.73e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 42.18 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1381 GVRVIIVNPEtKGPLGDSHLGEIWVNSPHNASGYYtiygeeslqADHFNTRLSFGDTetlWARTGYLGfvkrteLLDASG 1460
Cdd:PRK05852 362 GAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYL---------GDPTITAANFTDG---WLRTGDLG------SLSAAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 688611673 1461 DrhdaLFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESAVF 1505
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 ... |
369-463 |
2.84e-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: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 369 TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSDPgmFWVAFYGCLLAEVIPVPIEVPLSrkdagSQQIG 448
Cdd:cd05907 5 PITWAEFAEEVRALAKGLI-ALG------VEPGDRVAILSRNRPE--WTIADLAILAIGAVPVPIYPTSS-----AEQIA 70
|
90
....*....|....*
gi 688611673 449 FLLGSCGVGLALTSE 463
Cdd:cd05907 71 YILNDSEAKALFVED 85
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1009-1188 |
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 688611673 1009 AQTDPDHVLYMLLNAkgvavsTATCSQLHKRAEKITAALLERgGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVtvrp 1088
Cdd:PRK07786 27 ALMQPDAPALRFLGN------TTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAV---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1089 phPQNLSATLPTVRMIIDVSKAACILTTQTL-------------MKTLRSKEAAASVNVKTWPNIIDTD-------DLPR 1148
Cdd:PRK07786 96 --PVNFRLTPPEIAFLVSDCGAHVVVTEAALapvatavrdivplLSTVVVAGGSSDDSVLGYEDLLAEAgpahapvDIPN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 688611673 1149 KRPASIYkpptaemlayldFSVSTTGMLTGVKMSHSAVNA 1188
Cdd:PRK07786 174 DSPALIM------------YTSGTTGRPKGAVLTHANLTG 201
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
369-533 |
3.96e-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: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 369 TLTYGKLWSRSLKLAYTLLNKLGtknepvlKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEvplsrKDAGSQQIG 448
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 449 FLLGSCGVGLALTSEVCLKGLPKTPngeimqfkgwprlkwVVTDTKYLTKPSKDWQPHIPTANTDTAYIEYKASKEGTVM 528
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLPAGL---------------PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPK 142
|
....*
gi 688611673 529 GVAVS 533
Cdd:cd12116 143 GVVVS 147
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
369-447 |
4.67e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 41.58 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 369 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPN--SDPgmfwVAFYGCLLAEVIPV-------PIEVPLSR 439
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNllQYP----IALFGILRAGMIVVnvnplytPRELEHQL 117
|
....*...
gi 688611673 440 KDAGSQQI 447
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 ... |
1367-1504 |
4.71e-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: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1367 PQSLPLMESGTMLPGVRVIIVNPETKGPLGDSHLGEIWVNSPHNASGYYTIYGEeslqadhfnTRLSF-GDTETLWARTG 1445
Cdd:cd05935 245 PLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEE---------TEESFiEIKGRRFFRTG 315
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 688611673 1446 YLGFvkrtelLDASGdrhdALFVVGSLDETLELRGLRYHPIDIETSVSRaHRSIAESAV 1504
Cdd:cd05935 316 DLGY------MDEEG----YFFFVDRVKRMINVSGFKVWPAEVEAKLYK-HPAI*EVCV 363
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1034-1183 |
5.54e-03 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 41.37 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1034 SQLHKRAEKITAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPphpqnLSATLPTVRMIIDVSKAACI 1113
Cdd:PLN02574 70 SELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP-----SSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 1114 LTTQTLmktlrSKEAAASVNVKTWPNIIDTDD----------LPRKRPASIYKPPTAEM-LAYLDFSVSTTGMLTGVKMS 1182
Cdd:PLN02574 145 TSPENV-----EKLSPLGVPVIGVPENYDFDSkriefpkfyeLIKEDFDFVPKPVIKQDdVAAIMYSSGTTGASKGVVLT 219
|
.
gi 688611673 1183 H 1183
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 ... |
370-433 |
8.75e-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: 8.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688611673 370 LTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPI 433
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNSP--QYVIAYFAIWRANAVVVPI 56
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
369-533 |
9.39e-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: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 369 TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSdPGMFwVAFYGCLLA--EVIPVPIEVPLSRkdagsqq 446
Cdd:cd12117 22 SLTYAELNERANRLARRLR-AAG------VGPGDVVGVLAERS-PELV-VALLAVLKAgaAYVPLDPELPAER------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611673 447 IGFLLGSCGVGLALTSEvclkGLPKTPNGEIMQfkgwprlkwVVTDTKYLTKPSKDwqPHIPTANTDTAYIEYKASKEGT 526
Cdd:cd12117 86 LAFMLADAGAKVLLTDR----SLAGRAGGLEVA---------VVIDEALDAGPAGN--PAVPVSPDDLAYVMYTSGSTGR 150
|
....*..
gi 688611673 527 VMGVAVS 533
Cdd:cd12117 151 PKGVAVT 157
|
|
| |
