|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
387-963 |
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: 656.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 387 CLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPnsDPVMFMVAFYGCLLAELVPVPIEV 466
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 467 PLtrkdaGSQQVGFLLGSCGVFLALTTDACQKGLPKA-----QTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDT 541
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 542 GTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALM 621
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 622 KANPLSWIQKVCFYKARAALVKSRDMHWSL------LAQRGQRDVSLSSLRMLIVADGaNPWSISSCDAFLNVFQSRGLR 695
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 696 PEvicpcASSPEALTVAIRRPPDLG--GPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEgTP 773
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGtsGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPE-TK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 774 YLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFDRPFTRTGLLGFIGP----------DNLVFIVGK 843
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPtkctdlnveeHDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 844 LDGLMVTGVRRHNADDVVATALAVEPmkfvYRGRIAVFSVTVlhddRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHQV 923
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSITG----LVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2462582313 924 GVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNV 963
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1039-1415 |
1.70e-146 |
|
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: 460.28 E-value: 1.70e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1039 LFLLLNAKGTVTSTATCVQLHKRAERVAAALMEKGRLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLG 1117
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1118 TTLPTVKMivEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKKKIASVFR-----PPSPDVLAYLDFSV 1192
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKwgphpPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1193 STTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAV 1272
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1273 SQYKARVTFCSYSVMEMCTKGLGAQTGVLRMKGVNLSCVRTCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGCRV 1352
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462582313 1353 NVAICLqpnrlgklaeQGTAGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKSLQAVD 1415
Cdd:cd05905 319 NPFICW----------QGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQ 371
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
377-954 |
1.50e-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: 229.82 E-value: 1.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 377 RWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLnkltsknePLLKPGDRVALVFPNSdpVMFMVAFYGCLL 456
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 457 AELVPVPIEVPLTRKDAgsQQVGFLLGSCGVFLALTTDACQKGLPKAqtgeVAAFKGWPPLSWLVIDGKHLAkPPKDWHP 536
Cdd:cd05931 71 AGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 537 LAQDTGTgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHV 613
Cdd:cd05931 144 PSPDPDD-IAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 614 VsvpyaLMK-----ANPLSWIQKVCFYKAR--AAlvksRDMHWSLLAQRGQR----DVSLSSLRMLIVadGANPWSISSC 682
Cdd:cd05931 220 V-----LMSpaaflRRPLRWLRLISRYRATisAA----PNFAYDLCVRRVRDedleGLDLSSWRVALN--GAEPVRPATL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 683 DAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlgGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQdVGQVMPG 761
Cdd:cd05931 289 RRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGGPP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 762 ANVCVVKLEGTPyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGapifdrPFTRTGLLGFIGPDNLvFIV 841
Cdd:cd05931 364 QEVRIVDPETGR-ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL-YIT 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 842 GKLDGLMVTGVRRHNADDVVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIH 921
Cdd:cd05931 436 GRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREH 513
|
570 580 590
....*....|....*....|....*....|...
gi 2462582313 922 QVGVYCLALVPANTLPKAPLGGIHISETKQRFL 954
Cdd:cd05931 514 GVAPADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1029-1415 |
1.26e-40 |
|
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: 159.33 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1029 WRAHTTPDHPLFLLLNAKGTVTSTATCVQLHKRAERVAAALMEKGRlsVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1108
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1109 RPPHPqnlGTTLPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRtwPTILDTDDIPKKKIASVFRP-PSPDVLAY 1187
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGT--PRLLVVDLLPDTSAADWPPPsPDPDDIAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1188 LDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLVPPLELESNV 1265
Cdd:cd05931 154 LQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1266 SLWLSAVSQYKARVT----FcSYsvmEMCT-KGLGAQTGvlrmkGVNLSCVRTCMVVAeERPRIALTQSFSKLFKDLGLP 1340
Cdd:cd05931 232 LRWLRLISRYRATISaapnF-AY---DLCVrRVRDEDLE-----GLDLSSWRVALNGA-EPVRPATLRRFAEAFAPFGFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1341 ARAVSTTFGcrvnvaiclqpnrlgkLAEQ------GTAGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKSLQAV 1414
Cdd:cd05931 302 PEAFRPSYG----------------LAEAtlfvsgGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQ 364
|
.
gi 2462582313 1415 D 1415
Cdd:cd05931 365 E 365
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1027-1408 |
1.86e-38 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 149.77 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1027 LQWRAHTTPDHPLFlllnAKGTVTSTaTCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1106
Cdd:pfam00501 1 LERQAARTPDKTAL----EVGEGRRL-TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1107 TVRPphpqnlGTTLPTVKMIVEVSKSACVLtTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPK-----------KKIAS 1175
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKeeplpeeakpaDVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1176 VFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE----LYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1251
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1252 QSVLVPPLELESnVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgVLRMKGVNLSCVRTCMVVAeERPRIALTQSFS 1331
Cdd:pfam00501 228 TVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNMLLE-------AGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462582313 1332 KLFkdlglpARAVSTTFGCRVN-VAICLQPNRLGKLAEQGTAGpdpttvyvdmRALRHDRVRLVERGSPHSLPLMESG 1408
Cdd:pfam00501 299 ELF------GGALVNGYGLTETtGVVTTPLPLDEDLRSLGSVG----------RPLPGTEVKIVDDETGEPVPPGEPG 360
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
368-956 |
8.88e-29 |
|
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: 123.16 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 368 PPSLLATLQRWGTTQPKSPClTALDTTGkAVYTLTYGKLWSRSLKLAyTLLNKLTskneplLKPGDRVALVFP-NSDpvm 446
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADG-SEEFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDdNED--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 447 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQ-----QVGFLLGSCGVflaLTTDACQkglpkAQTGEVAAFKGWPPLSWLV 521
Cdd:cd05906 77 FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELV-----AEFAGLETLSGLPGIRVLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 522 IDGKHLAKPPKDWHPLAQDtgtgTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAG 598
Cdd:cd05906 149 IEELLDTAADHDLPQSRPD----DLALLMLTS--GSTgfpKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 599 LWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKA------RAALVKSRDmhwsLLAQRGQRDVSLSSLRMLIVAD 672
Cdd:cd05906 223 LVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVtitwapNFAFALLND----LLEEIEDGTWDLSSLRYLVNAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 673 GANpwSISSCDAFLNVFQSRGLRPEVICPCASSPEalTVAirrppdlggppprkavlsmnglsyGVI--RVDTEEKLS-V 749
Cdd:cd05906 299 EAV--VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysRSFPTYDHSqA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 750 LTVQDVGQVMPGANVCVVKLEGTpyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLL 829
Cdd:cd05906 351 LEFVSLGRPIPGVSMRIVDDEGQ--LLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF-----TEDG-------WFRTGDL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 830 GFIGPDNLVFIVGKLDGLMVTGVrRHNADDVVAtalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSfqw 909
Cdd:cd05906 417 GFLDNGNLTITGRTKDTIIVNGV-NYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDA--- 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2462582313 910 MSRVLQAIDSI--HQVGVYCLALVP--ANTLPKAPLGGIHISETKQRFLEG 956
Cdd:cd05906 490 LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
370-954 |
1.07e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 120.05 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 370 SLLATLQRWGTTQPKSPCLT----ALDTTGKAvYTLTYGKLWSRSLKLAYTLlNKLTSknepllkPGDRVALVFPNSdpV 445
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAGVA-ETLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 446 MFMVAFYGCLLAELVPVPIEVPLTRkdAGSQQVGFLLGSCGVFLALTTDACqkglpkaqTGEVAAF----KGWPPLSWLV 521
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTSAV--------VDDVTEYvapqPGQSAPPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 522 IDGKHLAKPPKDwhPLAQDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQA----CGYSEAETLTNV--LD 592
Cdd:PRK05850 141 VDLLDLDSPRGS--DARPRDLPSTAYLQY-TS--GSTrtpAGVMVSHRNVIANFEQLMSDyfgdTGGVPPPDTTVVswLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 593 FKRDAGLWHGVLTSVMNRMHVV-SVPYALMkANPLSWIQkvcfykaraaLVKSRDMHWSL-------LAQRGQRDVSLSS 664
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCPAVlTSPVAFL-QRPARWMQ----------LLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 665 L---RMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlGGPPPrkavlsmnglsygVIR 740
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP---GQPPE-------------SVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 741 VDTEeKLSVltvqdvGQVMPGANVcvvklEGTPYL--------------------CKTDEVGEICVSSSATGTAYYGLLG 800
Cdd:PRK05850 349 FDYE-KLSA------GHAKRCETG-----GGTPLVsygsprsptvrivdpdtcieCPAGTVGEIWVHGDNVAAGYWQKPE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 801 ITKNVFEAVPVT-TGGAPifDRPFTRTGLLGFIGPDNLvFIVGKL-DGLMVTGvRRHNADDVVATalavepMKFVYRGRI 878
Cdd:PRK05850 417 ETERTFGATLVDpSPGTP--EGPWLRTGDLGFISEGEL-FIVGRIkDLLIVDG-RNHYPDDIEAT------IQEITGGRV 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 879 AVFSVTVLHDDRIVLVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRF 953
Cdd:PRK05850 487 AAISVPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQY 566
|
.
gi 2462582313 954 L 954
Cdd:PRK05850 567 R 567
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
375-851 |
5.52e-27 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 115.49 E-value: 5.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 375 LQRWGTTQPKSPCLTALDTTgkavyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 454
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGR-----RLTYRELDERANRLA----AGLRALG---VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 455 LLAELVPVPIEVpltrkDAGSQQVGFLLGSCGVFLALTTD--------ACQKGLPKAQTGEVAAFKGWPPLSWLVIDGKH 526
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 527 LAKPPKDWHPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQAC----GYSEAETLTNVLDFKRDAGL 599
Cdd:pfam00501 142 ADVPPPPPPPPDPDD---LAYIIY-TS--GTTgkpKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 600 WHGVLTSVMNRMHVVSVP--YALMKANPLSWIQKvcfYKARAALVKSRDMHWsLLAQRGQRDVSLSSLRMLIVadGANPW 677
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPPgfPALDPAALLELIER---YKVTVLYGVPTLLNM-LLEAGAPKRALLSSLRLVLS--GGAPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 678 SISSCDAFLNVFqsrglrPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSmnglsygvirvdteeklsvltvqdVGQ 757
Cdd:pfam00501 290 PPELARRFRELF------GGALVNGYGLTETTGVVTTPLPL---DEDLRSLGS------------------------VGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 758 VMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvttggapiFDRPFTRTGLLGFIGPDNL 837
Cdd:pfam00501 337 PLPGTEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPELTAEAF------------DEDGWYRTGDLGRRDEDGY 403
|
490
....*....|....
gi 2462582313 838 VFIVGKLDGLMVTG 851
Cdd:pfam00501 404 LEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
371-958 |
1.11e-26 |
|
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: 115.29 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 371 LLATLQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSDPvmFMVA 450
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLAAALRALG-------VGPGDRVALLLPNSPE--FVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 451 FYGCLLAELVPVPIEVPLTRKdagsqQVGFLLGSCGvflalttdacqkglPKAqtgevaafkgwpplswlVIdgkhlakp 530
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSG--------------ARA-----------------LV-------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 531 pkdwhplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSV 607
Cdd:COG0318 102 --------------TALILY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 608 MNRMHVVSVPyalmKANPLSWIQKVCFYKA-RAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFL 686
Cdd:COG0318 165 LAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 687 NVFQSRglrpevICPC-ASSpEALTVAIRRPPDLGGPPPRKavlsmnglsygvirvdteeklsvltvqdVGQVMPGANVC 765
Cdd:COG0318 237 ERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 766 VVKLEGTPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttGGapifdrpFTRTGLLGFIGPDNLVFIVGKLD 845
Cdd:COG0318 282 IVDEDGRE--LPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR------DG-------WLRTGDLGRLDEDGYLYIVGRKK 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 846 GLMVTGVRRHNADDVVATALAVEPMKfvyrgRIAVFSVTvlhDDR------IVLVAEQRPDASEEDSFQWMSRVLQAIDS 919
Cdd:COG0318 347 DMIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGVP---DEKwgervvAFVVLRPGAELDAEELRAFLRERLARYKV 418
|
570 580 590
....*....|....*....|....*....|....*....
gi 2462582313 920 IHQVgvyclalVPANTLPKAPLGGIHISETKQRFLEGTL 958
Cdd:COG0318 419 PRRV-------EFVDELPRTASGKIDRRALRERYAAGAL 450
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
392-960 |
6.87e-26 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 114.72 E-value: 6.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 392 DTTGKAVYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVfPNSDPvMFMVAFYGCLLAELVPVPIEVP--LT 469
Cdd:PRK09192 41 DRRGQLEEALPYQTLRARAEAGARRLLALG-------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 470 RKDAGSQQVGFLLGSCGVFLALTTDACQKGLPKAQTGEvaafkgwpPLSWlVIDGKHLAKPPKDWHPLAQDTGTGTAYIE 549
Cdd:PRK09192 112 GRESYIAQLRGMLASAQPAAIITPDELLPWVNEATHGN--------PLLH-VLSHAWFKALPEADVALPRPTPDDIAYLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 550 YkTSkeGST---VGVTVSHASLLAQCRALTQ-ACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANP 625
Cdd:PRK09192 183 Y-SS--GSTrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 626 LSWIQKVCfyKARAALVKSRDMHWSLLAQRGQ----RDVSLSSLRmlIVADGANPWSISSCDAFLNVFQSRGLRPEVICP 701
Cdd:PRK09192 260 LQWLDLIS--RNRGTISYSPPFGYELCARRVNskdlAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 702 CASSPEAlTVAIRRPPDLGGppPRKAVLSMNGLSYGVIRVDTEEK-LSVLTVQDVGQVMPGANVCVVKLEGTPYlcKTDE 780
Cdd:PRK09192 336 SYGLAEA-TLAVSFSPLGSG--IVVEEVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPL--PERV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 781 VGEICVSSSATGTAYYGllgitKNVFEAVPVTTGgapifdrpFTRTGLLGFIGPDNLVfIVGKLDGLMVTGVRRHNADDV 860
Cdd:PRK09192 411 VGHICVRGPSLMSGYFR-----DEESQDVLAADG--------WLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 861 VATAlavEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKA 939
Cdd:PRK09192 477 EWIA---EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRT 550
|
570 580
....*....|....*....|.
gi 2462582313 940 PLGGIHISETKQRFLEGTLHP 960
Cdd:PRK09192 551 SSGKLSRAKAKKRYLSGAFAS 571
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
430-958 |
2.30e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 103.66 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 430 KPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVFLALTTDACQKG----- 499
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSAEGvrkff 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 500 --LPKAQTGEVAAFKGWPP---LSWlvidgkhlaKPPkdwhPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQ 571
Cdd:PRK07769 148 raRPAKERPRVIAVDAVPDevgATW---------VPP----EANEDT---IAYLQY-TS--GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 572 CRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKaNPLSWIqkvcfykaRAALVKSRDMH--- 648
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWI--------RELARKPGGTGgtf 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 649 -------WSLLAQRG-----QRDVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRR 715
Cdd:PRK07769 280 saapnfaFEHAAARGlpkdgEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtLFVSTTP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 716 PPDlggpPPRKAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTA 794
Cdd:PRK07769 358 MDE----EPTVIYVDRDELNAGrFVEVPADAPNAVAQVS-AGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 795 YYGLLGITKNVFEAV------PVTTGGAPIfDRPFTRTGLLGFIGPDNLvFIVGKLDGLMVTGVRRHNADDVVATALavE 868
Cdd:PRK07769 432 YWGKPEETAATFQNIlksrlsESHAEGAPD-DALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--E 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 869 PMKFVYRGRIAVFSV-------TVLHD-------------DRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCL 928
Cdd:PRK07769 508 ATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDV 587
|
570 580 590
....*....|....*....|....*....|
gi 2462582313 929 ALVPANTLPKAPLGGIHISETKQRFLEGTL 958
Cdd:PRK07769 588 LLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
10-158 |
1.11e-21 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 91.33 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 10 AAPLPAEVRESLAELELELSEGDITQKGYEKKRAKLLARYIpliqgidpsLQAENripgPSQTTAAAPKQQKSRPTASRD 89
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFL---------LHPET----PTKLSAEAQNQLASLETKLRD 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462582313 90 ERFRSaniqpmfiwlllvwllrnkfiwtqdsnksytlqlvDVHTEAVQAALAKYKERKM--PMPSKRRSVL 158
Cdd:pfam06464 69 EELSE-----------------------------------EVYLEKVKALLAKELERENglNAPTKEQSGL 104
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
367-988 |
1.49e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.47 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 367 RPPSLLATLQRWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLlnkltsknEPLLKPGDRVALVFPnSDPvM 446
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFP-SGP-D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 447 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVFLALTTDACQKGLpkAQTGEVAAfKGWPPlsWLVIDGKh 526
Cdd:PRK05691 77 YVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL--LQMEELAA-ANAPE--LLCVDTL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 527 LAKPPKDWHPLAQDtGTGTAYIEYkTSkeGSTV---GVTVSHASLLAQCRALTQACG--YSEAETLTNVLDFKRDAGLWH 601
Cdd:PRK05691 151 DPALAEAWQEPALQ-PDDIAFLQY-TS--GSTAlpkGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 602 GVLTSVMNrmhvvSVPYALMK-----ANPLSWIQKVCFYkaRAALVKSRDMHWSLLAQRgqrdVSLSSLRML------IV 670
Cdd:PRK05691 227 GLLQPIFS-----GVPCVLMSpayflERPLRWLEAISEY--GGTISGGPDFAYRLCSER----VSESALERLdlsrwrVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 671 ADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAirrppdlGGPPprkavlsmnGLSYGVIRVDTEEKLSV 749
Cdd:PRK05691 296 YSGSEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS-------GGRR---------GQGIPALELDAEALARN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 750 LTVQDVGQVM-------PGANVCVV---KLEGTPylckTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGapif 819
Cdd:PRK05691 360 RAEPGTGSVLmscgrsqPGHAVLIVdpqSLEVLG----DNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDG---- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 820 dRPFTRTGLLGFIgPDNLVFIVGKLDGLMVtgVRRHN--ADDVVATalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAE- 896
Cdd:PRK05691 428 -RTWLRTGDLGFL-RDGELFVTGRLKDMLI--VRGHNlyPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEi 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 897 ----QRPDASEEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLhpcnvlmcphTCVT 972
Cdd:PRK05691 502 srsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYA 567
|
650
....*....|....*.
gi 2462582313 973 NLPKPRQKQPEVGPAS 988
Cdd:PRK05691 568 LFPALQAVEAAQTAAS 583
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
392-960 |
4.25e-19 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 93.27 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 392 DTTGKAVyTLTYGKLWSRslklaytlLNKLTSKNEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP---- 467
Cdd:PRK12476 61 SAAGCAV-ELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLFAPelpg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 468 -LTRKDAgsqqvgfLLGSCGVFLALTTDACQ-------KGLPKAQTGEVAAFKGWPplswlvidgkhlAKPPKDWHPLAQ 539
Cdd:PRK12476 130 hAERLDT-------ALRDAEPTVVLTTTAAAeavegflRNLPRLRRPRVIAIDAIP------------DSAGESFVPVEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 540 DTgTGTAYIEYkTSkeGST---VGVTVSHasllaqcRAltqACgyseaetlTNVLDFKRDAGLW----HGV--------- 603
Cdd:PRK12476 191 DT-DDVSHLQY-TS--GSTrppVGVEITH-------RA---VG--------TNLVQMILSIDLLdrntHGVswlplyhdm 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 604 -LTSVM------NRMHVVSvPYALMKaNPLSWIQKVCfYKARAALV--KSRDMHWSLLAQRG----QRDVSLSSLRMLIv 670
Cdd:PRK12476 249 gLSMIGfpavygGHSTLMS-PTAFVR-RPQRWIKALS-EGSRTGRVvtAAPNFAYEWAAQRGlpaeGDDIDLSNVVLII- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 671 adGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSMNGLSYG-VIRVDTEEKLSV 749
Cdd:PRK12476 325 --GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPD---AEPSVVYLDREQLGAGrAVRVAADAPNAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 750 LTVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTT-------GGAPIfDRP 822
Cdd:PRK12476 400 AHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRlaegshaDGAAD-DGT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 823 FTRTGLLGFIgPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDAS 902
Cdd:PRK12476 477 WLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTS 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462582313 903 EEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHP 960
Cdd:PRK12476 554 RADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1023-1294 |
9.34e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.15 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1023 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCVQLHKRAERVAAALMEkgRLSVGDHVALVYPPGVDLIAAFYGCLYCG 1102
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQA--RASFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1103 CVPVTVRPP------HPQNLGTtlptvkmIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIrtwPTILDTDDIPkKKIASV 1176
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLD-PALAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1177 FRPPS--PDVLAYLDFSVSTTGILAGVKMSHA---ATSALCRSiKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1251
Cdd:PRK05691 158 WQEPAlqPDDIAFLQYTSGSTALPKGVQVSHGnlvANEQLIRH-GFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462582313 1252 QSVLVPPLELESNVSLWLSAVSQYKARVT--------FCSYSVMEMCTKGL 1294
Cdd:PRK05691 237 PCVLMSPAYFLERPLRWLEAISEYGGTISggpdfayrLCSERVSESALERL 287
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1023-1394 |
1.38e-14 |
|
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: 77.93 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1023 LADVLQWRAHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1102
Cdd:COG0318 1 LADLLRRAAARHPDRPA---LVFGGRRLTYA---ELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1103 CVPVTVrpphpqNLGTTLPTVKMIVEVSKSACVLTtqavtrllrskeaaaavdirtwptildtddipkkkiasvfrppsp 1182
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1183 dvlAYLDFSvS-TTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1261
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1262 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgVLRMKGVNLSCVRTCMVVAEerpriALTQSFSKLFKDLglpa 1341
Cdd:COG0318 179 ER----VLELIERERVTVLFGVPTMLARLLR-------HPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER---- 238
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462582313 1342 ravsttFGCRV---------NVAICLQPNRLGkLAEQGTAGpdpttvyvdmRALRHDRVRLV 1394
Cdd:COG0318 239 ------FGVRIvegygltetSPVVTVNPEDPG-ERRPGSVG----------RPLPGVEVRIV 283
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1057-1414 |
2.46e-14 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 77.86 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGRLsvGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP----HPQNLGTTL----PTVkmive 1128
Cdd:PRK12476 73 QLGVRLRAVGARLQQVAGP--GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1129 vsksacVLTTQAVTRLLRSKEAAAAVDIRtwPTILDTDDIPkKKIASVFRPPSPDV--LAYLDFSVSTTGILAGVKMSH- 1205
Cdd:PRK12476 146 ------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIP-DSAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1206 AATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHqSVLVPPLELESNVSLW---LSAVSQYKARVTFC 1282
Cdd:PRK12476 217 AVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWikaLSEGSRTGRVVTAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1283 SYSVMEmctkgLGAQTGVLRM-KGVNLSCVrtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpn 1361
Cdd:PRK12476 296 PNFAYE-----WAAQRGLPAEgDDIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG------------ 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462582313 1362 rlgkLAEQ----GTAGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGK---SLQAV 1414
Cdd:PRK12476 357 ----IAEAtlfvATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQvarSQWAV 414
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1023-1205 |
3.08e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 77.68 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1023 LADVLQWRAHTTPDHPLFLLLN---AKGTVTSTATCVQLHKRAERVAAALMEKGrlSVGDHVALVYPPGVDLIAAFYGCL 1099
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDyeqDPAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1100 YCGCVPVTVRPPHPqnlGTTLPTVKMIVEVSKSACVLTTQAVTRLLRskEAAAAVDIRTWPTI--LDTDDIPKKKIASVF 1177
Cdd:PRK05850 81 QAGLIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTTSAVVDDVT--EYVAPQPGQSAPPVieVDLLDLDSPRGSDAR 155
|
170 180
....*....|....*....|....*...
gi 2462582313 1178 RPPSPDVlAYLDFSVSTTGILAGVKMSH 1205
Cdd:PRK05850 156 PRDLPST-AYLQYTSGSTRTPAGVMVSH 182
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1057-1349 |
1.79e-13 |
|
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: 75.01 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGRLSvGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHP-QNLGTTLPTVKMIVEVSKSACV 1135
Cdd:cd05906 44 DLLEDARRLAAGLRQLGLRP-GDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1136 LTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSi 1215
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAA---DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1216 KLQCELYPSRQIA---ICLDPYCGLGFAlwCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVMEM 1289
Cdd:cd05906 199 KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWApnfAFALLND 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1290 CTKGLGAQTGvlrmkgvNLSCVRtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFG 1349
Cdd:cd05906 277 LLEEIEDGTW-------DLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFG 328
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
429-938 |
1.89e-13 |
|
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: 74.40 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 429 LKPGDRVALVFPNSDP---VMFMVAFYGCLLAeLVPVPIEvpltrKDAGSQQVGFLLGSCGVFLALttdaCQKGL-PKAQ 504
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLG-LVFVPLN-----PTLKESVLRYLVADAGGRIVL----ADAGAaDRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 505 TGEVAAFKgwpPLSWLVIDGKHLAKPPKDWHPLAQDTgtgTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEA 584
Cdd:cd05922 85 DALPASPD---PGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 585 ETLTNVLDFKRDAGLwhGVLTS--------VMNRMHVVsvPYALMKAnplswiqkvcFYKARAALVKSRDMHWSLLAQRG 656
Cdd:cd05922 159 DRALTVLPLSYDYGL--SVLNThllrgatlVLTNDGVL--DDAFWED----------LREHGATGLAGVPSTYAMLTRLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 657 QRDVSLSSLRMLIVADGANPwsisscDAFLNVFQS--RGLRPEVIcpcasspEALTVAIRR----PPDLGGPPPrkavls 730
Cdd:cd05922 225 FDPAKLPSLRYLTQAGGRLP------QETIARLREllPGAQVYVM-------YGQTEATRRmtylPPERILEKP------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 731 mnglsygvirvdteeklsvltvQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIcVSSSATGTAYYGllgiTKNVFEAVP 810
Cdd:cd05922 286 ----------------------GSIGLAIPGGEFEILDDDGTP--TPPGEPGEI-VHRGPNVMKGYW----NDPPYRRKE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 811 VTTGGApifdrpfTRTGLLGFIGPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMkfvyrGRIAVFSVTVLHDDR 890
Cdd:cd05922 337 GRGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEK 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2462582313 891 IVLVAEqrpdASEEDSFQWMSRVLQAIDSIHQVGVYClalVPANTLPK 938
Cdd:cd05922 405 LALFVT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPL 445
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1057-1303 |
5.56e-13 |
|
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: 72.68 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGRLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgttlPTVKMIVEVSKSACVL 1136
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1137 TTQAvTRLLRSKEAAAAVDIRTWPTILDTDDIPKkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIk 1216
Cdd:TIGR01733 78 TDSA-LASRLAGLVLPVILLDPLELAALDDAPAP---PPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1217 lqCELYPSRQIAICLDpYCGLGF------ALWCLcsvYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMC 1290
Cdd:TIGR01733 153 --ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250
....*....|...
gi 2462582313 1291 TKGLGAQTGVLRM 1303
Cdd:TIGR01733 227 AAALPPALASLRL 239
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1031-1213 |
5.13e-12 |
|
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: 70.07 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1031 AHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1110
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1111 PHPQnlgttlPTVKMIVEVSKSACVLTTQAVTrllrskeAAAAVDiRTWPTILDTDDIPKKKIASVFRPPSPDVLAYLDF 1190
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPALA-------GELAVE-LVAVTLLDQPGAAAGADAEPDPALDADDLAYVIY 143
|
170 180
....*....|....*....|...
gi 2462582313 1191 SVSTTGILAGVKMSHAATSALCR 1213
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVA 166
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1023-1257 |
6.52e-12 |
|
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: 69.90 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1023 LADVLQWRAHTTPDHPLFLLLNAKGTVTstatcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1102
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYR------ELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1103 CVPVTVRPphpqnlgttlptvkmivevsksacVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKKKIAsvfrpPSP 1182
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1183 DVLAYLDFSVSTTGILAGVKMSHAATSAlcrsIKLQC-----ELYPSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLV 1256
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
.
gi 2462582313 1257 P 1257
Cdd:cd05936 201 P 201
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
545-851 |
6.22e-11 |
|
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: 65.77 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 545 TAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPyalm 621
Cdd:cd04433 2 PALILY-TS--GTTgkpKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 622 KANPLSWIQKVCFYKARAALVkSRDMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFLNVFqsrglRPEVICP 701
Cdd:cd04433 74 KFDPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP-----GIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 702 CASSPEALTVAIRRPPDLGGPPPrkavlsmnglsygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPylCKTDEV 781
Cdd:cd04433 146 YGLTETGGTVATGPPDDDARKPG-----------------------------SVGRPVPGVEVRIVDPDGGE--LPPGEI 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 782 GEICVSSsatgtaYYGLLGITKNVFEAVPVTTGGapifdrpFTRTGLLGFIGPDNLVFIVGKLDGLMVTG 851
Cdd:cd04433 195 GELVVRG------PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
402-845 |
9.16e-11 |
|
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: 65.75 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 402 TYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEV--PLTRKDagsqqvg 479
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 480 FLLGSCGVFLALTTdacqkglpkAQTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDTGTGTAYIEYkTSkeGST- 558
Cdd:TIGR01733 66 FILEDAGARLLLTD---------SALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 559 --VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHgVLTSVMNRMHVVSVPYALMKANPLSWiqkvcfyk 636
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 637 arAALVKSRDM-HWSLLAqrgqrdvslSSLRMLIVADganpwsisscdaflnVFQSRGLRpeVICPCAsspEALTVA-IR 714
Cdd:TIGR01733 205 --AALIAEHPVtVLNLTP---------SLLALLAAAL---------------PPALASLR--LVILGG---EALTPAlVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 715 RppdLGGPPPRKAVLSMnglsYG---------VIRVDtEEKLSVLTVQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIC 785
Cdd:TIGR01733 254 R---WRARGPGARLINL----YGptettvwstATLVD-PDDAPRESPVPIGRPLANTRLYVLDDDLRP--VPVGVVGELY 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 786 VSSSATGTAYYGLLGITKNVFEAVPVTTGGapifDRPFTRTGLLGFIGPDNLVFIVGKLD 845
Cdd:TIGR01733 324 IGGPGVARGYLNRPELTAERFVPDPFAGGD----GARLYRTGDLVRYLPDGNLEFLGRID 379
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
392-849 |
1.59e-10 |
|
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: 65.31 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 392 DTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIevpltrk 471
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 472 DAGSQQ--VGFLLGSCGVFLALTTdacQKGLPKAQtgevAAFKGWPPLSWLVIDGKHLAK---PPKDWHPLA-------- 538
Cdd:cd05911 66 NPIYTAdeLAHQLKISKPKVIFTD---PDGLEKVK----EAAKELGPKDKIIVLDDKPDGvlsIEDLLSPTLgeededlp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 539 ---QDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCralTQACGYSEA-----ETLTNVLDFKRDAGLWhGVLTSV 607
Cdd:cd05911 139 pplKDGKDDTAAILY-SS--GTTglpKGVCLSHRNLIANL---SQVQTFLYGndgsnDVILGFLPLYHIYGLF-TTLASL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 608 MNRMHVVSVPyalmKANPLSWIQKVCFYKARAALVKSRDMHWslLAQRGQRDV-SLSSLRMLIVadGANPWSISSCDAFL 686
Cdd:cd05911 212 LNGATVIIMP----KFDSELFLDLIEKYKITFLYLVPPIAAA--LAKSPLLDKyDLSSLRVILS--GGAPLSKELQELLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 687 NVFQSRGLRP-----EVICPCASSPEAltvairrpPDLGGppprkavlsmnglsygvirvdteeklsvltvqDVGQVMPG 761
Cdd:cd05911 284 KRFPNATIKQgygmtETGGILTVNPDG--------DDKPG--------------------------------SVGRLLPN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 762 ANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLLGFIGPDNLVFIV 841
Cdd:cd05911 324 VEAKIVDDDGKDSL-GPNEPGEICVRGPQVMKGYYNNPEATKETF-----DEDG-------WLHTGDIGYFDEDGYLYIV 390
|
490
....*....|....
gi 2462582313 842 G------KLDGLMV 849
Cdd:cd05911 391 DrkkeliKYKGFQV 404
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1013-1349 |
3.61e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 64.64 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1013 DSDQARK---FLFLADVLQWRAHTTPDHPLFlllNAKGTVTSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGV 1089
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1090 DLIAAFYGCLYCGCVPVTVrpPHPQNLG---TTLPTVKMIVEVSKSACVLTTQAVTRLLrsKEAAAAVDIRTWPTILDTD 1166
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFGgreSYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAWFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1167 DIPKKKIAsvFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQ-CELYPSRQIAICLDPYCGLGFaLWCLC 1245
Cdd:PRK09192 162 ALPEADVA--LPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1246 SVYSGHQSV-LVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTgvlrMKGVNLSCVRTCMVVAEE-RPR 1323
Cdd:PRK09192 239 TPVATQLSVdYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKD----LAELDLSCWRVAGIGADMiRPD 314
|
330 340
....*....|....*....|....*.
gi 2462582313 1324 IalTQSFSKLFKDLGLPARAVSTTFG 1349
Cdd:PRK09192 315 V--LHQFAEAFAPAGFDDKAFMPSYG 338
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1057-1280 |
6.73e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 63.44 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGC--VPVTVRPPhPQNLgttlptvKMIVEVSKSAC 1134
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARR-------EAILADAGARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1135 VLTTQAVtrllrskeAAAAVDIRTWPTILDTDDIPKKKIASvfRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRS 1214
Cdd:cd12114 88 VLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPP--VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462582313 1215 IKLQCELYPS-RQIAIcldpyCGLGFALwclcSVY-------SGHQSVLVPPLElESNVSLWLSAVSQYkaRVT 1280
Cdd:cd12114 158 INRRFAVGPDdRVLAL-----SSLSFDL----SVYdifgalsAGATLVLPDEAR-RRDPAHWAELIERH--GVT 219
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
304-845 |
1.83e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 304 RVSSKIQQLLNTLKRPKRPPLKEFFVDDFEELLEVQQPDPNQPKPEGSETSV-LRGEPLTAGVPRPPSLLATLQRwgttq 382
Cdd:PRK12316 1954 RLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVhQRIAEQAARAPEAIAVVFGDQH----- 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 383 pkspcltaldttgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPVMfmVAFYGCLLA--ELV 460
Cdd:PRK12316 2029 ------------------LSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYV 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 461 PVPIEVPLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKgwPPLSWlvidgkhlakppKDW---HPL 537
Cdd:PRK12316 2082 PLDPNYPAER-------LAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLD--RDAEW------------ADYpdtAPA 2140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 538 AQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVvsvp 617
Cdd:PRK12316 2141 VQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARV---- 2215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 618 yaLMKANPLsWIQKVCFYKARAALVKSRDM---HWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAflnvfQSRGL 694
Cdd:PRK12316 2216 --LIRDDEL-WDPEQLYDEMERHGVTILDFppvYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRL-----AWEAL 2285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 695 RPEVIcpcasspealtvairrppdLGGPPPRKAVLSMngLSYGVIRVDTEEKLSVltvqDVGQVMPGANVCVvkLEGTPY 774
Cdd:PRK12316 2286 RPVYL-------------------FNGYGPTEAVVTP--LLWKCRPQDPCGAAYV----PIGRALGNRRAYI--LDADLN 2338
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462582313 775 LCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 845
Cdd:PRK12316 2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLY-----RTGDLARYRADGVVEYLGRID 2404
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
389-574 |
2.71e-09 |
|
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: 61.42 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 389 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 468
Cdd:cd05936 16 TALIFMGR---KLTYRELDALAEAFAAGLQNLG-------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 469 TrkdagSQQVGFLLGSCGVFLALTtdacqkglpkaqtgeVAAFkgwpplswlvidgKHLAKPPKDWHPLAQDTGTGTAYI 548
Cdd:cd05936 84 T-----PRELEHILNDSGAKALIV---------------AVSF-------------TDLLAAGAPLGERVALTPEDVAVL 130
|
170 180 190
....*....|....*....|....*....|..
gi 2462582313 549 EYkTSkeGST---VGVTVSHASLLA---QCRA 574
Cdd:cd05936 131 QY-TS--GTTgvpKGAMLTHRNLVAnalQIKA 159
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
400-600 |
4.61e-09 |
|
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: 61.41 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 400 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 477
Cdd:COG1020 501 SLTYAELNARANRLAHHLRALG-------VGPGDLVGVCLERS--LEMVVALLAVLKAgaAYVPLDPAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 478 VGFLLGSCGVFLALTTDACQKGLPKAQtgevaafkgwppLSWLVIDGKHLAKPPKDWhPLAQDTGTGTAYIEYkTSkeGS 557
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TS--GS 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462582313 558 T---VGVTVSHASLLAQCRALTQACGYSEAETLTNV--LDFkrDAGLW 600
Cdd:COG1020 629 TgrpKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1057-1429 |
6.07e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.51 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGRlsVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV----RPPHPQNLGTTL----PTVkmIVE 1128
Cdd:PRK07769 60 QFGARNRAVGARLQQVTK--PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVLddctPSA--ILT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1129 VSKSAcvlttQAVTRLLRSKEAAAAvdirtwPTILDTDDIPkKKIASVFRPPSP--DVLAYLDFSVSTTGILAGVKMSH- 1205
Cdd:PRK07769 136 TTDSA-----EGVRKFFRARPAKER------PRVIAVDAVP-DEVGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1206 -AATSAL--CRSIKLQcelYPSRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLVPPLELESNVSLW---LSAVSQYKARV 1279
Cdd:PRK07769 204 nLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPGGTGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1280 tfcsYSVMEMCTKGLGAQTGVLR--MKGVNLSCVRtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGcrvnvaic 1357
Cdd:PRK07769 279 ----FSAAPNFAFEHAAARGLPKdgEPPLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG-------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1358 lqpnrlgkLAEQ----GTAGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGK---SLQAV--------DQPRVE 1420
Cdd:PRK07769 346 --------MAEAtlfvSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKvgvSEWAVivdpetasELPDGQ 417
|
410
....*....|.
gi 2462582313 1421 SGE--LSGQHI 1429
Cdd:PRK07769 418 IGEiwLHGNNI 428
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1030-1207 |
6.13e-09 |
|
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: 60.37 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1030 RAHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1109
Cdd:cd17646 7 QAARTPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1110 PPHPQnlgttlPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPkkkiasvfrPPSPDVLAYLD 1189
Cdd:cd17646 80 PGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV---------PPRPDNLAYVI 144
|
170
....*....|....*...
gi 2462582313 1190 FSVSTTGILAGVKMSHAA 1207
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAG 162
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1185-1382 |
6.45e-09 |
|
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: 59.61 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1185 LAYLDFSVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLVPPLEL 1261
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1262 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgVLRMKGVNLSCVRTCMVVAEERPrIALTQSFSKLFKDlglpa 1341
Cdd:cd04433 78 EA----ALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEAPGI----- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462582313 1342 rAVSTTFG---CRVNVAICLQPNRLGKLAEQGTAGPDPTTVYVD 1382
Cdd:cd04433 141 -KLVNGYGlteTGGTVATGPPDDDARKPGSVGRPVPGVEVRIVD 183
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1057-1281 |
7.27e-09 |
|
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: 60.64 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGC--VPvtvrpphpqnLGTTLPT--VKMIVEVSKS 1132
Cdd:COG1020 506 ELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1133 ACVLTTQAVTRLLRSKEAaaavdirtwPTI-LDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1211
Cdd:COG1020 575 RLVLTQSALAARLPELGV---------PVLaLDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1212 CRSIKLQCELYPSRQIaicldpycgLGFA-----------LWCLCsvySGHQSVLVPPlELESNVSLWLSAVSQYkaRVT 1280
Cdd:COG1020 646 LAWMQRRYGLGPGDRV---------LQFAslsfdasvweiFGALL---SGATLVLAPP-EARRDPAALAELLARH--RVT 710
|
.
gi 2462582313 1281 F 1281
Cdd:COG1020 711 V 711
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1054-1138 |
7.57e-09 |
|
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: 59.85 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1054 TCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLgttlptVKMIVEVSKSA 1133
Cdd:cd05930 14 TYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------LAYILEDSGAK 86
|
....*
gi 2462582313 1134 CVLTT 1138
Cdd:cd05930 87 LVLTD 91
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1057-1215 |
1.11e-08 |
|
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: 59.61 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGRlSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1136
Cdd:cd12116 17 ELDERANRLAARLRARGV-GPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462582313 1137 TTQAVtrllrskEAAAAVDIRTWPTILDTDDIPKkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSI 1215
Cdd:cd12116 90 TDDAL-------PDRLPAGLPVLLLALAAAAAAP---AAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1054-1281 |
5.96e-08 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 57.22 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1054 TCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCvpvtvrPPHPQNLGTTLPTVKMIVEVSKSA 1133
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1134 CVLTTQAVtrLLRSKEAAAAVDIRT----------WPTILDTDDIPKKKIASVFRPP----SPDVLAYLDFSVSTTGILA 1199
Cdd:cd05911 85 VIFTDPDG--LEKVKEAAKELGPKDkiivlddkpdGVLSIEDLLSPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1200 GVKMSH---AATSALCRSIKLQCELYPSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLVPPLELEsnvsLWLSAVSQY 1275
Cdd:cd05911 163 GVCLSHrnlIANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKY 235
|
....*.
gi 2462582313 1276 KARVTF 1281
Cdd:cd05911 236 KITFLY 241
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1030-1213 |
7.04e-08 |
|
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: 56.83 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1030 RAHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1109
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1110 PPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEaaaavdirtwpTILDTDDIPKKKIASVFRPP-SPDVLAYL 1188
Cdd:cd12117 79 PELPAE------RLAFMLADAGAKVLLTDRSLAGRAGGLE-----------VAVVIDEALDAGPAGNPAVPvSPDDLAYV 141
|
170 180
....*....|....*....|....*
gi 2462582313 1189 DFSVSTTGILAGVKMSHAATSALCR 1213
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
400-587 |
8.79e-08 |
|
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: 56.53 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 400 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEvpltrKDAGSQQVG 479
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 480 FLLGSCGVFLALTTDACQKGLPkaqtgevaafkGWPPLSWLVIDGKHLAKPPkdwhPLAQDTGTGTAYIEYkTSkeGST- 558
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP-----------AGLPVLLLALAAAAAAPAA----PRTPVSPDDLAYVIY-TS--GSTg 139
|
170 180 190
....*....|....*....|....*....|.
gi 2462582313 559 --VGVTVSHASLLAQCRALTQACGYSEAETL 587
Cdd:cd12116 140 rpKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1052-1205 |
3.97e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 54.62 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1052 TATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP--------------------- 1110
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaiv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1111 -----PHPQNLGTTLP-----TVKMIvevskSACVLTTQAVTRL----LRSKEAA---AAVDIRTWPTILDTDDIPKKKI 1173
Cdd:PRK05605 136 wdkvaPTVERLRRTTPletivSVNMI-----AAMPLLQRLALRLpipaLRKARAAltgPAPGTVPWETLVDAAIGGDGSD 210
|
170 180 190
....*....|....*....|....*....|..
gi 2462582313 1174 ASVFRpPSPDVLAYLDFSVSTTGILAGVKMSH 1205
Cdd:PRK05605 211 VSHPR-PTPDDVALILYTSGTTGKPKGAQLTH 241
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
429-583 |
5.37e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 54.17 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 429 LKPGDRVALVFPNSDpvMFMVAFYGCLLAELVPVPIEVPLTRKDagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEV 508
Cdd:PRK08316 58 LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAYILDHSGARAFLVDPALAPTAEAALALLP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 509 AAFKGWPPL--------SWLVIDgkHLAKPPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACG 580
Cdd:PRK08316 131 VDTLILSLVlggreapgGWLDFA--DWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD 208
|
...
gi 2462582313 581 YSE 583
Cdd:PRK08316 209 MSA 211
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1050-1257 |
6.61e-07 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 53.91 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1050 TSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGTTLPTVKMIVEV 1129
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1130 SKSACVLTTQAVTRLLRSKEAAAAVDIRT----------WPTILDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILA 1199
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462582313 1200 GVKMSHAatsalcrSIKLQCELYPSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLVP 1257
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMP 238
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
400-666 |
1.01e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 400 TLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 477
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALI-------ARGVGPEVLVGIAMERS--AEMMVGLLAVLKAggAYVPLDPEYPRER------- 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 478 VGFLLGSCGVFLALTTDACQKGLPKAqtgevaafKGwppLSWLVIDgkhlakPPKDW------HPLAQDTGTGTAYIEYK 551
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQSHLLQRLPIP--------DG---LASLALD------RDEDWegfpahDPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 552 TSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPYALmkANPLSWIQK 631
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHE-GLYHPLINGASVVIRDDSL--WDPERLYAE 4779
|
250 260 270
....*....|....*....|....*....|....*
gi 2462582313 632 VcfYKARAALVKSRDMHWSLLAQRGQRDVSLSSLR 666
Cdd:PRK12316 4780 I--HEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR 4812
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
363-495 |
4.17e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 51.20 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 363 AGVPRPP-------SLLATLQRWGTTQPKSPcltALDTTGkavYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRV 435
Cdd:PRK06178 20 AGIPREPeyphgerPLTEYLRAWARERPQRP---AIIFYG---HVITYAELDELSDRFAALLRQRG-------VGAGDRV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 436 ALVFPNSdPvMFMVAFYGCLLAELVPVPIEvPLTRKdagsQQVGFLLGSCGVFLALTTDA 495
Cdd:PRK06178 87 AVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
366-841 |
5.70e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 50.96 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 366 PRPPSLLATLQRWGTTQPKSpclTALDTTGKAVytlTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDpv 445
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDK---EAVYFDGRRT---TYAELDERVNRLA----NALRALG---VKKGDRVAVFDWNSH-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 446 MFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVGFLLGSCGVFLALTTDacqKGLPkaqtgEVAAFKGWPPL--SWLVID 523
Cdd:PRK06187 68 EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVDS---EFVP-----LLAAILPQLPTvrTVIVEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 524 GKHLAKPPKDWH------------PLAQDTGTGTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEaetlt 588
Cdd:PRK06187 135 DGPAAPLAPEVGeyeellaaasdtFDFPDIDENDAAAMLYTS--GTTghpKGVVLSHRNLFLHSLAVCAWLKLSR----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 589 nvldfkRDAGLwhgVLTSvMNRMHVVSVPY-ALMKANPLSWIQKVCFYKARAALVKSR--------DMHWSLLAQRGQRD 659
Cdd:PRK06187 208 ------DDVYL---VIVP-MFHVHAWGLPYlALMAGAKQVIPRRFDPENLLDLIETERvtfffavpTIWQMLLKAPRAYF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 660 VSLSSLRMLIVadGANPWSISSCDAFLNVF-----QSRGLrPEvICPcasspealTVAIRRPPDlgGPPPRKAVLSmngl 734
Cdd:PRK06187 278 VDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-TE-TSP--------VVSVLPPED--QLPGQWTKRR---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 735 sygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPYLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttG 814
Cdd:PRK06187 340 -------------------SAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------G 394
|
490 500
....*....|....*....|....*..
gi 2462582313 815 GapifdrpFTRTGLLGFIGPDNLVFIV 841
Cdd:PRK06187 395 G-------WLHTGDVGYIDEDGYLYIT 414
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
400-539 |
5.77e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 400 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRkdagSQQVG 479
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLLYMQNS--PQFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462582313 480 FLLGSCGVFLALTT-DACQKGLPKAQTGE-----VAAFKGW-------PPLSWLVIDGKHLAKPPKDWHPLAQ 539
Cdd:PRK08314 102 HYVTDSGARVAIVGsELAPKVAPAVGNLRlrhviVAQYSDYlpaepeiAVPAWLRAEPPLQALAPGGVVAWKE 174
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
375-851 |
1.50e-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: 49.15 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 375 LQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPvmFMVAFYGC 454
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS------LTYAELDERVNRLAHALR-------ALGVAKGDRVAVLSKNSPE--FLELLFAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 455 LLAELVPVPIEVPLTRKDagsqqVGFLLGSCGvflalttdacqkglpkaqtgevaafkgwpplSWLVIDgkhlakppkDw 534
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSG-------------------------------AKVLFD---------D- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 535 hplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETL--------TNVLDFKRDAGLWHGV 603
Cdd:cd17631 100 ----------LALLMY-TS--GTTgrpKGAMLTHRNLLWNAVNALAALDLGPDDVLlvvaplfhIGGLGVFTLPTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 604 LTSVMNRMHVVSVpyalmkanpLSWIQ--KVCFykarAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVADGANPwsiss 681
Cdd:cd17631 167 TVVILRKFDPETV---------LDLIErhRVTS----FFLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMP----- 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 682 cDAFLNVFQSRGLRpevICPCASSPEALTVAIRRPPDlggppprkavlsmnglsygvirvDTEEKLSvltvqDVGQVMPG 761
Cdd:cd17631 227 -ERLLRALQARGVK---FVQGYGMTETSPGVTFLSPE-----------------------DHRRKLG-----SAGRPVFF 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 762 ANVCVVKLEGTPylCKTDEVGEICVSSSATGTAYYGLlgitknvfeavPVTTGGApIFDRPFtRTGLLGFIGPDNLVFIV 841
Cdd:cd17631 275 VEVRIVDPDGRE--VPPGEVGEIVVRGPHVMAGYWNR-----------PEATAAA-FRDGWF-HTGDLGRLDEDGYLYIV 339
|
490
....*....|
gi 2462582313 842 GKLDGLMVTG 851
Cdd:cd17631 340 DRKKDMIISG 349
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1030-1289 |
1.86e-05 |
|
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: 49.25 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1030 RAHTTPDHPLFLLLNakgtvtSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1109
Cdd:cd17655 6 QAEKTPDHTAVVFED------QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1110 PPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEAAaavdirtwpTILDTDDIPKKKIASVFRPPSPDVLAYLD 1189
Cdd:cd17655 79 PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPVSKSDDLAYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1190 FSVSTTGILAGVKMSH--------AATSALCRSIKLQCELYPSrqiaICLDPYCGLGFAlwclcSVYSGHQSVLVPPLEL 1261
Cdd:cd17655 144 YTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTLYIVRKETV 214
|
250 260
....*....|....*....|....*...
gi 2462582313 1262 ESNVSLwLSAVSQYKARVTFCSYSVMEM 1289
Cdd:cd17655 215 LDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1031-1207 |
3.02e-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: 48.40 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1031 AHTTPDHPLFLLLNAkgtvtsTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1110
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1111 PHPqnlgttlptvkmivevsksacvlttqaVTRLLRSKEAAAavdirtwPTILDTDdipkkkiasvfrppsPDVLAYLDF 1190
Cdd:cd05945 74 SSP---------------------------AERIREILDAAK-------PALLIAD---------------GDDNAYIIF 104
|
170
....*....|....*..
gi 2462582313 1191 SVSTTGILAGVKMSHAA 1207
Cdd:cd05945 105 TSGSTGRPKGVQISHDN 121
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1030-1224 |
3.04e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.19 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1030 RAHTTPDHPLfLLLNAKgtvtsTATCVQLHKRAERVAAALMEKGrlsVGDH--VALVYPPGVDLIAAFYGCLYCGCVPVT 1107
Cdd:PRK12316 4560 RARMTPDAVA-VVFDEE-----KLTYAELNRRANRLAHALIARG---VGPEvlVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1108 VRPPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDI---RTWPTILDTDdiPKKKIAsvfrppsPDV 1184
Cdd:PRK12316 4631 LDPEYPRE------RLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD--PAVRLH-------PDN 4695
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462582313 1185 LAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPS 1224
Cdd:PRK12316 4696 LAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPD 4735
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1006-1207 |
3.63e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.50 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1006 RELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLflLLNAKGTVTSTatcvQLHKRAERVAAALMEKGrLSVGDHVALVY 1085
Cdd:PRK10252 443 AQLAQVNATAVEIPETTLSALVAQQAAKTPDAPA--LADARYQFSYR----EMREQVVALANLLRERG-VKPGDSVAVAL 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1086 PPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDt 1165
Cdd:PRK10252 516 PRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQG- 588
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462582313 1166 ddipkkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAA 1207
Cdd:PRK10252 589 --------AAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTA 622
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
999-1224 |
4.22e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.80 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 999 RIAQASGRELAHLEDSDQARKFLFLADvlqWRAHTTP---DHPLFLLLNAKGTVTSTATCV----------QLHKRAERV 1065
Cdd:PRK12316 1965 QMAEDAQAALGELALLDAGERQRILAD---WDRTPEAyprGPGVHQRIAEQAARAPEAIAVvfgdqhlsyaELDSRANRL 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1066 AAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLTTQAVT-RL 1144
Cdd:PRK12316 2042 AHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLLTQRHLLeRL 2114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1145 -----LRSKEAAAAVDIRTWPtildtDDIPKKKIAsvfrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQC 1219
Cdd:PRK12316 2115 plpagVARLPLDRDAEWADYP-----DTAPAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY 2182
|
....*
gi 2462582313 1220 ELYPS 1224
Cdd:PRK12316 2183 ELSPA 2187
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
386-845 |
6.77e-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: 47.24 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 386 PCLTALDTTGKavyTLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVAlVFPNSDPVMFmVAFYGCLLAELVPVPIe 465
Cdd:cd05945 5 PDRPAVVEGGR---TLTYRELKERADALAAALA-------SLGLDAGDPVV-VYGHKSPDAI-AAFLAALKAGHAYVPL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 466 vpltrkDAGSqqvgfllgscgvflalttdacqkglPKAQTGEVAAfkgwpplswlvidgkhLAKPpkdwhPLAQDTGTGT 545
Cdd:cd05945 72 ------DASS-------------------------PAERIREILD----------------AAKP-----ALLIADGDDN 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 546 AYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLwHGVLTSVMNRMHVVSVPYAlMK 622
Cdd:cd05945 100 AYIIF-TS--GSTgrpKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALASGATLVPVPRD-AT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 623 ANPLSWIqkvcfykarAALVKSRDMHWsllaqrgqrdVSL-SSLRMLIVADGANPWSISSCDAFLnvFqsrglrpevicp 701
Cdd:cd05945 175 ADPKQLF---------RFLAEHGITVW----------VSTpSFAAMCLLSPTFTPESLPSLRHFL--F------------ 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 702 CAsspEALTVA-----IRRPPD-----LGGPPPrkavlSMNGLSYGVIrvdTEEKLSVLTVQDVGQVMPGANVCVVKLEG 771
Cdd:cd05945 222 CG---EVLPHKtaralQQRFPDariynTYGPTE-----ATVAVTYIEV---TPEVLDGYDRLPIGYAKPGAKLVILDEDG 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462582313 772 TPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 845
Cdd:cd05945 291 RP--VPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAY-----RTGDLVRLEADGLLFYRGRLD 353
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
564-940 |
9.89e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 46.68 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 564 SHASLLAQCRALTQACGyseaetltnvLDFKRDAG-----LWHG-----VLTSVMNRMHVVSVPYALMKANPLSWIQKVC 633
Cdd:PRK05851 173 SPGAVLSNLRGLNARVG----------LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 634 fyKARAALVKSRDMHWSLLAQRGQR--DVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPC---ASSPEA 708
Cdd:PRK05851 243 --DSRATLTAAPNFAYNLIGKYARRvsDVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSyglAESTCA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 709 LTVairrppdlggPPPrkavlsmnGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSS 788
Cdd:PRK05851 319 VTV----------PVP--------GIGLRVDEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGV-AGREIGEIEIRG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 789 SATGTAYygllgitknvfeavpvtTGGAPIFDRPFTRTGLLGFIGPDNLVfIVGKLDGLMVTGVRRHNADDVVATALAVE 868
Cdd:PRK05851 380 ASMMSGY-----------------LGQAPIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVR 441
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462582313 869 PmkfVYRGRIavfsVTVLHDD-----RIVLVAEQRpdASEEDSFQwmSRVLQAIDSihQVGVyclalVPANTLPKAP 940
Cdd:PRK05851 442 G---VREGAV----VAVGTGEgsarpGLVIAAEFR--GPDEAGAR--SEVVQRVAS--ECGV-----VPSDVVFVAP 500
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1023-1112 |
1.03e-04 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 46.68 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1023 LADVLQWRAHTTPDHPLflLLNAKGTVTSTatcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1102
Cdd:COG1021 27 LGDLLRRRAERHPDRIA--VVDGERRLSYA----ELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 2462582313 1103 CVPVTVRPPH 1112
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
399-577 |
1.17e-04 |
|
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: 46.50 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 399 YTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEV--PLTRKDAgsq 476
Cdd:cd12114 11 GTLTYGELAERARRVA----GALKAAG---VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 477 qvgfLLGSCGVFLALTTDACQKGLPKAqtgevaafkgwPPLSWLVIDGKHLAKPPKDWHPLAQDTgtgtAYIEYkTSkeG 556
Cdd:cd12114 79 ----ILADAGARLVLTDGPDAQLDVAV-----------FDVLILDLDALAAPAPPPPVDVAPDDL----AYVIF-TS--G 136
|
170 180
....*....|....*....|....
gi 2462582313 557 ST---VGVTVSHASLLAQCRALTQ 577
Cdd:cd12114 137 STgtpKGVMISHRAALNTILDINR 160
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1057-1208 |
1.18e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 46.44 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLGTTLPT--VKMIV------ 1127
Cdd:PRK07656 35 ELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALFvlglfl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1128 EVSKSA--CVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKkkiasVFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1205
Cdd:PRK07656 114 GVDYSAttRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAE-----RAPEVDPDDVADILFTSGTTGRPKGAMLTH 188
|
...
gi 2462582313 1206 AAT 1208
Cdd:PRK07656 189 RQL 191
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
401-920 |
1.25e-04 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 46.32 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 401 LTYGKLWSRSLKLAYTLLNKLTSKnepllkpGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRKDagsqQVGF 480
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK-------GDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 481 LLGSCGVFLALTTDACQKglpkaqtgevaafkgwpplswlvidgkhlakppkdwhplaqdtgtgTAYIEYKTSKEGSTVG 560
Cdd:cd05935 68 ILNDSGAKVAVVGSELDD----------------------------------------------LALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 561 VTVSHASLLAQcrALTQACGY--SEAETLTNVLDFKRDAGLWHGVLTSVmnrmhVVSVPYALMKanplSWIQKVcfykAR 638
Cdd:cd05935 102 CMHTHFSAAAN--ALQSAVWTglTPSDVILACLPLFHVTGFVGSLNTAV-----YVGGTYVLMA----RWDRET----AL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 639 AALVKSRDMHWS--------LLAQRGQRDVSLSSLRMLivADGANPWSISSCDAFLNVFqsrGLRPEVIcpcasspEALT 710
Cdd:cd05935 167 ELIEKYKVTFWTniptmlvdLLATPEFKTRDLSSLKVL--TGGGAPMPPAVAEKLLKLT---GLRFVEG-------YGLT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 711 VAIrrPPDLGGPPPRKAVLSMnglsyGVIRVDTEEKlsVLTVQDVGQVMPGanvcvvklegtpylcktdEVGEICVSSSA 790
Cdd:cd05935 235 ETM--SQTHTNPPLRPKLQCL-----GIP*FGVDAR--VIDIETGRELPPN------------------EVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 791 TGTAYYGLLGITKNVFeavpVTTGGapifdRPFTRTGLLGFIGPDNLVFIVGKLDGLM-VTGVRRHNADdvVATALAVEP 869
Cdd:cd05935 288 IFKGYWNRPEETEESF----IEIKG-----RRFFRTGDLGYMDEEGYFFFVDRVKRMInVSGFKVWPAE--VEAKLYKHP 356
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 870 mkfvyrgriAVFSVTVLH--DDR--------IVLVAEQRPDASEEDSFQW----MS-----RVLQAIDSI 920
Cdd:cd05935 357 ---------AI*EVCVISvpDERvgeevkafIVLRPEYRGKVTEEDIIEWareqMAaykypREVEFVDEL 417
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
395-574 |
1.60e-04 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 46.21 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 395 GKAVY-----TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFpnSDPVMFMVAFYGCLLAELVPVPIEVPLT 469
Cdd:cd05959 19 DKTAFiddagSLTYAELEAEARRVAGALRALG-------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 470 rkdagSQQVGFLLGSCGVFLALTTDACqkgLPKAQTgevAAFKGWPPLSWLVIDGKHLAKPPKDWhpLAQDTGTGT---- 545
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGEL---APVLAA---ALTKSEHTLVVLIVSGGAGPEAGALL--LAELVAAEAeqlk 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462582313 546 ---------AYIEYKTSKEGSTVGVTVSHASLLAQCRA 574
Cdd:cd05959 157 paathaddpAFWLYSSGSTGRPKGVVHLHADIYWTAEL 194
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
755-858 |
2.18e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 45.72 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 755 VGQVMPGANVCVVKLEGT-PYL--CKTDEVGEICVSssatgtayygllgiTKNVFEA-VPVTTGGAPIFDRPFTRTGLLG 830
Cdd:PRK07529 388 VGLRLPYQRVRVVILDDAgRYLrdCAVDEVGVLCIA--------------GPNVFSGyLEAAHNKGLWLEDGWLNTGDLG 453
|
90 100
....*....|....*....|....*...
gi 2462582313 831 FIGPDNLVFIVGKLDGLMVTGvrRHNAD 858
Cdd:PRK07529 454 RIDADGYFWLTGRAKDLIIRG--GHNID 479
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1050-1213 |
2.96e-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: 45.15 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1050 TSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPphpqnlgttlptvkmivev 1129
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1130 sksacVLTTQAVTRLLRSKEAAAavdirtwpTILDTDDIpkkkiasvfrppspdvlAYLDFSVSTTGILAGVKMSHAATS 1209
Cdd:cd05919 68 -----LLHPDDYAYIARDCEARL--------VVTSADDI-----------------AYLLYSSGTTGPPKGVMHAHRDPL 117
|
....
gi 2462582313 1210 ALCR 1213
Cdd:cd05919 118 LFAD 121
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
354-692 |
3.17e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 45.72 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 354 SVLRGEPLTAGVPRppSLLATLQRwgttQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGD 433
Cdd:PRK12316 502 ATAAEYPLQRGVHR--LFEEQVER----TPEAPALAFGEET------LDYAELNRRANRLAHALI-------ERGVGPDV 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 434 RVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAF 511
Cdd:PRK12316 563 LVGVAMERSIEMV--VALLAILKAggAYVPLDPEYPAER-------LAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDL 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 512 KgwPPLSWLviDGKHLAKPPKDWHPLaqdtgtGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVL 591
Cdd:PRK12316 634 D--RPAAWL--EGYSEENPGTELNPE------NLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKT 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 592 DFKRDAGLWHGVLTsVMNRMHVVSVPYALMKaNPLSWIQkvcfYKARAAlVKSRDMHWSLLA--QRGQRDVSLSSLRMLI 669
Cdd:PRK12316 704 PFSFDVSVWEFFWP-LMSGARLVVAAPGDHR-DPAKLVE----LINREG-VDTLHFVPSMLQafLQDEDVASCTSLRRIV 776
|
330 340
....*....|....*....|...
gi 2462582313 670 VADGANPWsisscDAFLNVFQSR 692
Cdd:PRK12316 777 CSGEALPA-----DAQEQVFAKL 794
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
390-472 |
3.22e-04 |
|
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: 45.00 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 390 ALDTTGKAVyTLTYGKLwsrsLKLAYTLLNKLTSKNeplLKPGDRVALVFPNSDPvmFMVAFYGCLLAELVPVPIEvPLT 469
Cdd:cd05926 5 ALVVPGSTP-ALTYADL----AELVDDLARQLAALG---IKKGDRVAIALPNGLE--FVVAFLAAARAGAVVAPLN-PAY 73
|
...
gi 2462582313 470 RKD 472
Cdd:cd05926 74 KKA 76
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
359-575 |
3.30e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 45.14 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 359 EPLTAGVPRP------PSLLATL----QRWGTtqpkSPCLTALdttGKavyTLTYGKLWSRSLKLAYTLlnkltsKNEPL 428
Cdd:PRK05677 8 DKYPAGIAAEinpdeyPNIQAVLkqscQRFAD----KPAFSNL---GK---TLTYGELYKLSGAFAAWL------QQHTD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 429 LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV-------PIEVPLTRKDAGSQQVgfllgscgVFLALTTDACQKGLP 501
Cdd:PRK05677 72 LKPGDRIAVQLPNV--LQYPVAVFGAMRAGLIVVntnplytAREMEHQFNDSGAKAL--------VCLANMAHLAEKVLP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 502 KAQ-----TGEVAAFKgwPPLSWLVIDG--KHLAKPPKDWH-------PLAQDTGTG------------TAYIEYKTSKE 555
Cdd:PRK05677 142 KTGvkhviVTEVADML--PPLKRLLINAvvKHVKKMVPAYHlpqavkfNDALAKGAGqpvteanpqaddVAVLQYTGGTT 219
|
250 260
....*....|....*....|...
gi 2462582313 556 GSTVGVTVSHASLLA---QCRAL 575
Cdd:PRK05677 220 GVAKGAMLTHRNLVAnmlQCRAL 242
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1057-1211 |
3.54e-04 |
|
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: 44.99 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1136
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462582313 1137 TTqavtrllrskeaaaavdirtwptildtddipkkkiasvfrppsPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1211
Cdd:cd17643 90 TD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLAL 121
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1025-1207 |
4.03e-04 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 44.81 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1025 DVLQWRAHTTPDhPLFLLLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCV 1104
Cdd:cd05923 5 EMLRRAASRAPD-ACAIADPARGLRLTYS---ELRARIEAVAARLHARG-LRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1105 PVTVRPP-HPQNLGTTLPTVKM---IVEVSKSACVLTTQAVTRLLRskeaaAAVDIRTWPTILDTDDIPkkkiasvFRPP 1180
Cdd:cd05923 80 PALINPRlKAAELAELIERGEMtaaVIAVDAQVMDAIFQSGVRVLA-----LSDLVGLGEPESAGPLIE-------DPPR 147
|
170 180
....*....|....*....|....*..
gi 2462582313 1181 SPDVLAYLDFSVSTTGILAGVKMSHAA 1207
Cdd:cd05923 148 EPEQPAFVFYTSGTTGLPKGAVIPQRA 174
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
389-617 |
4.79e-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: 44.59 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 389 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLTSKnepllkPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI---- 464
Cdd:cd05941 3 IAIVDDGD---SITYADLVARAARLANRLLALGKDL------RGDRVAFLAPPS--AEYVVAQLAIWRAGGVAVPLnpsy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 465 ---EVPLTRKDAGSQqvgfllgscgvflalttdacqkglpkaqtgevaafkgwpplswLVIDGkhlakppkdwhplaqdt 541
Cdd:cd05941 72 plaELEYVITDSEPS-------------------------------------------LVLDP----------------- 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462582313 542 gtgtAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVP 617
Cdd:cd05941 92 ----ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
399-462 |
9.58e-04 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 43.60 E-value: 9.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462582313 399 YTLTYGKLWSRSLKLAYTLLNkltsknepL-LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 462
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLLA--------LgLRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1057-1357 |
1.12e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 43.60 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1057 QLHKRAERVAAALMEKGRLSVgdhVALVYPPGVDLIAAFYGCLYCG----CVPVTVRPPHPQNLGTTLPTVKMIVEVSKs 1132
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1133 acVLTTQAVTRLLRSKEAAAAVDirtwptilDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALC 1212
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVH--------DLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1213 RSIKLQCELYPSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVMe 1288
Cdd:PRK05851 182 RGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAApnfAYNLI- 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462582313 1289 mctkGLGAQtgvlRMKGVNLSCVRTCmVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFG-----CRVNVAIC 1357
Cdd:PRK05851 260 ----GKYAR----RVSDVDLGALRVA-LNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGlaestCAVTVPVP 324
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1061-1215 |
1.15e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 43.20 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1061 RAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPhpQNLGTTLPTVKMIVEVSKSACVLTTQA 1140
Cdd:cd05922 2 GVSAAASALLEAG-GVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVP--LNPTLKESVLRYLVADAGGRIVLADAG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462582313 1141 vtrlLRSKEAAAAVDIRTWPTILDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSI 1215
Cdd:cd05922 79 ----AADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSI 149
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1023-1205 |
1.17e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 43.49 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1023 LADVLQWRAHTTPDHPLFLLLnakGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1102
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIFY---GHVITYA---ELDELSDRFAALLRQRG-VGAGDRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1103 CVPVTVRP-------PHpqNLGTTLPTVKM-------IVEVSKSACVLTTQAVTRLLRSKEAAAAV---DIRTWPTILDT 1165
Cdd:PRK06178 108 AVHVPVSPlfrehelSY--ELNDAGAEVLLaldqlapVVEQVRAETSLRHVIVTSLADVLPAEPTLplpDSLRAPRLAAA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462582313 1166 DDI------PKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1205
Cdd:PRK06178 186 GAIdllpalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ 231
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1057-1108 |
2.59e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 42.41 E-value: 2.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2462582313 1057 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1108
Cdd:COG0365 44 ELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
400-462 |
2.97e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 41.96 E-value: 2.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462582313 400 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 462
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNL--LQYPIALFGILRAGMIVV 102
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1182-1411 |
3.21e-03 |
|
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: 42.09 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1182 PDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1261
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1262 ESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTgvlrMKGVNLSCVRtcMVVAEERP-RIALTQSFSKLFKDLGLP 1340
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEK----ANDWDLSSIR--MILNGAEPiDYELCHEFLDHMSKYGLK 258
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462582313 1341 ARAVSTTFG-CRVNVAICLQPnrlgklaeqgtAGPDPTTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKSL 1411
Cdd:cd05908 259 RNAILPVYGlAEASVGASLPK-----------AQSPFKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPI 320
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
375-596 |
3.59e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 41.64 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 375 LQRWGTTQPKSPCLTALDTTGKAVyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 454
Cdd:COG0365 15 LDRHAEGRGDKVALIWEGEDGEER-TLTYAELRREVNRFA----NALRALG---VKKGDRVAIYLPNI--PEAVIAMLAC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 455 LLAELVPVPIeVPLTRKDAgsqqVGFLLGSCGVFLALTTDA-CQKGLPKAQTGEV-AAFKGWPPL-SWLVIDGKHLAKPP 531
Cdd:COG0365 85 ARIGAVHSPV-FPGFGAEA----LADRIEDAEAKVLITADGgLRGGKVIDLKEKVdEALEELPSLeHVIVVGRTGADVPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 532 K---DWHPLAQDTGTG----------TAYIEYkTSkeGST---VGVTVSHASLLAQCRAltqacgyseaeTLTNVLDFKR 595
Cdd:COG0365 160 EgdlDWDELLAAASAEfepeptdaddPLFILY-TS--GTTgkpKGVVHTHGGYLVHAAT-----------TAKYVLDLKP 225
|
.
gi 2462582313 596 D 596
Cdd:COG0365 226 G 226
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1023-1206 |
3.75e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 41.67 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1023 LADVLQWRAHTTPDHPLFLllnAKGTVTSTATCVQlhkRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1102
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLV---FGGTRWTYAEAAR---AAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1103 CVPVtvrpphPQNLGTTLPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAA----------AVDIRTWPTILDTDDIPKKK 1172
Cdd:PRK06155 96 AIAV------PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDlplpavwlldAPASVSVPAGWSTAPLPPLD 169
|
170 180 190
....*....|....*....|....*....|....*
gi 2462582313 1173 IASVFRPPSP-DVLAYLDFSvSTTGILAGVKMSHA 1206
Cdd:PRK06155 170 APAPAAAVQPgDTAAILYTS-GTTGPSKGVCCPHA 203
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
400-464 |
4.18e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 41.43 E-value: 4.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462582313 400 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI 464
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALG-------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPL 85
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1051-1110 |
4.53e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 41.29 E-value: 4.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1051 STATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1110
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP 59
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
400-578 |
5.59e-03 |
|
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: 41.18 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 400 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVpltrkDAGSQQVG 479
Cdd:cd17651 20 RLTYAELDRRANRLAHRLRARGV-------GPGDLVALCARRS--AELVVALLAILKAGAAYVPLDP-----AYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 480 FLLGSCGVFLALTTDACQKGLPkaqtgeVAAFKGWPplswlvIDGKHLAKPPKDWHPLAQDTGTgTAYIEYkTSkeGST- 558
Cdd:cd17651 86 FMLADAGPVLVLTHPALAGELA------VELVAVTL------LDQPGAAAGADAEPDPALDADD-LAYVIY-TS--GSTg 149
|
170 180
....*....|....*....|..
gi 2462582313 559 --VGVTVSHASLLAQCRALTQA 578
Cdd:cd17651 150 rpKGVVMPHRSLANLVAWQARA 171
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
364-568 |
5.65e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 364 GVPRPPSLLATL---QRWGTtqPKSPCLTAldttgkAVYTLTYGKLWSRSLKLAYTLlnkltskNEPLLKPGDRVALVFP 440
Cdd:PRK10252 452 AVEIPETTLSALvaqQAAKT--PDAPALAD------ARYQFSYREMREQVVALANLL-------RERGVKPGDSVAVALP 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 441 NSdpVMFMVAFYGCLLAELVPVPIEV--PLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKGWPPls 518
Cdd:PRK10252 517 RS--VFLTLALHAIVEAGAAWLPLDTgyPDDR-------LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA-- 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462582313 519 wlvidgkhlakpPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASL 568
Cdd:PRK10252 586 ------------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1030-1140 |
6.24e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 40.83 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 1030 RAHTTPDHPLFlLLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVr 1109
Cdd:PRK13391 6 HAQTTPDKPAV-IMASTGEVVTYR---ELDERSNRLAHLFRSLG-LKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV- 79
|
90 100 110
....*....|....*....|....*....|.
gi 2462582313 1110 pphpqNLGTTLPTVKMIVEVSKSACVLTTQA 1140
Cdd:PRK13391 80 -----NSHLTPAEAAYIVDDSGARALITSAA 105
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
755-869 |
6.63e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 40.54 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462582313 755 VGQVMPGANVCVVKLEGTPYL---CKTDEVGEICVSSsatgtayygllgitKNVFEAVPVTTGGAPIFDRP-FTRTGLLG 830
Cdd:cd05944 176 VGLRLPYARVRIKVLDGVGRLlrdCAPDEVGEICVAG--------------PGVFGGYLYTEGNKNAFVADgWLNTGDLG 241
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462582313 831 FIGPDNLVFIVGKLDGLMVTGvrRHNADDV-VATALAVEP 869
Cdd:cd05944 242 RLDADGYLFITGRAKDLIIRG--GHNIDPAlIEEALLRHP 279
|
|
| |
