|
Name |
Accession |
Description |
Interval |
E-value |
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
22-632 |
0e+00 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 1131.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 22 MKSLGYEDYETFYKKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGTPFAQWYNGGTCNVVESVLSRWLADdeTRTQP 101
Cdd:cd05968 1 MASLGIPDLEAFLERSAEDNAWFWGEFVKDVGIEWYEPPYQTLDLSGGKPWAAWFVGGRMNIVEQLLDKWLAD--TRTRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 102 ALQYEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTR 181
Cdd:cd05968 79 ALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 182 VQAAGSKMIITADGFSRRGKVVSLKDEVDKACEHCPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFVHAEEMHSDDP 261
Cdd:cd05968 159 LQDAEAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAERTESEDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 262 LMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVPDFPEA 341
Cdd:cd05968 239 LMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGAPDHPKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 342 DRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSNVPICNYSGGTEIS 421
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEIS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 422 GGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRDEVGELCLEKPWVGMTKSFWEDDERYVNTYWSRFENKWVHGDW 501
Cdd:cd05968 399 GGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 502 VVYD-GEQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMS 580
Cdd:cd05968 479 AYYDeEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELME 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 446729151 581 LVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSLVNP 632
Cdd:cd05968 559 RVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
74-639 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 735.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 74 QWYNGGTCNVVESVLSRWLADDetRTQPALQYEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETV 153
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGR--GDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 154 VAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKVVSLKDEVDKACEHCPTVEKVVIVRHAGNDFT 233
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 234 PHNyDFSWSTL-EKEKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGW 312
Cdd:COG0365 159 MEG-DLDWDELlAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 313 MMG-PFLLFGSLINGATMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEP 391
Cdd:COG0365 238 ATGhSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 392 WNPDPWMWLFETVGksnVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPW 470
Cdd:COG0365 318 LNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPgEEGELVIKGPW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 471 VGMTKSFWEDDERYVNTYWSRFENKWVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGV 549
Cdd:COG0365 395 PGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFwILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 550 PDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSL 629
Cdd:COG0365 475 PDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGDTSTL 554
|
570
....*....|
gi 446729151 630 VNPEVVPFIQ 639
Cdd:COG0365 555 EDPEALDEIK 564
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
28-631 |
0e+00 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 657.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 28 EDYETFYKKSIEETAWFWGEAEKAVgyQWMKPYTEVLDLENGTPFAQWYNGGTCNVVESVLSRWLAddETRTQPALQYEG 107
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKEL--DWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLK--ERGDKVAIIWEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 108 ENGT-SKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAG 186
Cdd:cd05966 77 DEPDqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 187 SKMIITADGFSRRGKVVSLKDEVDKACEHCPTVEKVVIVRHAGNDFTPHN-YDFSWSTL-EKEKPFVHAEEMHSDDPLML 264
Cdd:cd05966 157 CKLVITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMTEgRDLWWHDLmAKQSPECEPEWMDSEDPLFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 265 IYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDrVLWVT-DMGWMMG-PFLLFGSLINGATMVMYEGVPDFPEAD 342
Cdd:cd05966 237 LYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDD-IYWCTaDIGWITGhSYIVYGPLANGATTVMFEGTPTYPDPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 343 RLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSNVPICNYSGGTEiSG 422
Cdd:cd05966 316 RYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTE-TG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 423 GIfgnvLIKPIA------PISFNASLPGMAAVVLDDQGNPIRDEV-GELCLEKPWVGMTKSFWEDDERYVNTYWSRFENK 495
Cdd:cd05966 395 GI----MITPLPgatplkPGSATRPFFGIEPAILDEEGNEVEGEVeGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGY 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 496 WVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGEL 574
Cdd:cd05966 471 YFTGDGARRDEDGYYwITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDEL 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 575 KKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLG-KELGDLSSLVN 631
Cdd:cd05966 551 RKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGeEELGDTSTLAD 608
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
28-635 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 636.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 28 EDYETFYKKSIEETAWFWGEAEKAVgYQWMKPYTEVLDlENGTPFAQWYNGGTCNVVESVLSRWLADDETRTqpALQYEG 107
Cdd:TIGR02188 5 EQYKELYEESIEDPDKFWAKLAREL-LDWFKPFTKVLD-WSFPPFYKWFVGGELNVSYNCVDRHLEARPDKV--AIIWEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 108 EN-GTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAG 186
Cdd:TIGR02188 81 DEpGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 187 SKMIITADGFSRRGKVVSLKDEVDKACEHCP-TVEKVVIVRHAGNDFTP--HNYDFSWSTL-EKEKPFVHAEEMHSDDPL 262
Cdd:TIGR02188 161 AKLVITADEGLRGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVVPwvEGRDVWWHDLmAKASAYCEPEPMDSEDPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 263 MLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDrVLWVT-DMGWMMG-PFLLFGSLINGATMVMYEGVPDFPE 340
Cdd:TIGR02188 241 FILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGD-IFWCTaDVGWITGhSYIVYGPLANGATTVMFEGVPTYPD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 341 ADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSNVPICNYSGGTEi 420
Cdd:TIGR02188 320 PGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTE- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 421 SGGIfgnvLIKPIA------PISFNASLPGMAAVVLDDQGNPIR--DEVGELCLEKPWVGMTKSFWEDDERYVNTYWSRF 492
Cdd:TIGR02188 399 TGGI----MITPLPgatptkPGSATLPFFGIEPAVVDEEGNPVEgpGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 493 ENKWVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFS 571
Cdd:TIGR02188 475 PGYYFTGDGARRDKDGYIwITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPD 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 572 GELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKE--LGDLSSLVNPEVV 635
Cdd:TIGR02188 555 DELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAeiLGDTSTLEDPSVV 620
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
8-645 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 629.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 8 PTEEYKEKTRLygwmkslGYEDYETFYKKSIEETAWFWGEAEKAVgyQWMKPYTEVLDLENgtPFAQWYNGGTCNVVESV 87
Cdd:PRK00174 4 PPAEFAANALI-------DMEQYKALYQESVEDPEGFWAEQAKRL--DWFKPFDTVLDWNA--PFIKWFEDGELNVSYNC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 88 LSRWLADDetRTQPALQYEGEN-GTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAII 166
Cdd:PRK00174 73 LDRHLKTR--GDKVAIIWEGDDpGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 167 SPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKVVSLKDEVDKACEHCPTVEKVVIVRHAGND--FTPHNyDFSWSTL 244
Cdd:PRK00174 151 SVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDvdWVEGR-DLWWHEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 245 -EKEKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAA------FDagfgmnIKQGDrVLWVT-DMGWMMG- 315
Cdd:PRK00174 230 vAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAmtmkyvFD------YKDGD-VYWCTaDVGWVTGh 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 316 PFLLFGSLINGATMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPD 395
Cdd:PRK00174 303 SYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 396 PWMWLFETVGKSNVPICNYSGGTEiSGGIfgnvLIKPIA------PISFNASLPGMAAVVLDDQGNPIRDEV-GELCLEK 468
Cdd:PRK00174 383 AWEWYYKVVGGERCPIVDTWWQTE-TGGI----MITPLPgatplkPGSATRPLPGIQPAVVDEEGNPLEGGEgGNLVIKD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 469 PWVGMTKSFWEDDERYVNTYWSRFENKWVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAI 547
Cdd:PRK00174 458 PWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYwITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 548 GVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKE-LGDL 626
Cdd:PRK00174 538 GRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEiLGDT 617
|
650 660
....*....|....*....|
gi 446729151 627 SSLVNPEVVP-FIQGLQSSK 645
Cdd:PRK00174 618 STLADPSVVEkLIEARQNRK 637
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
30-610 |
0e+00 |
|
acetate-CoA ligase; This family 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: 341289 [Multi-domain] Cd Length: 587 Bit Score: 614.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 30 YETFYKKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGTPFAQWYNGGTCNVVESVLSRWLADDETRTqpALQYEGEN 109
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRT--AIIYEGDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 110 GT-SKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:cd17634 79 TSqSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 189 MIITADGFSRRGKVVSLKDEVDKACE-HCPTVEKVVIVRHAGNDF--TPhNYDFSWSTL-EKEKPFVHAEEMHSDDPLML 264
Cdd:cd17634 159 LLITADGGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIdwQE-GRDLWWRDLiAKASPEHQPEAMNAEDPLFI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 265 IYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMG-PFLLFGSLINGATMVMYEGVPDFPEADR 343
Cdd:cd17634 238 LYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLYEGVPNWPTPAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 344 LWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSNVPICNYSGGTEISGG 423
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 424 IFGN--VLIKPIAPISFNAsLPGMAAVVLDDQGNPIR-DEVGELCLEKPWVGMTKSFWEDDERYVNTYWSRFENKWVHGD 500
Cdd:cd17634 398 MITPlpGAIELKAGSATRP-VFGVQPAVVDNEGHPQPgGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 501 WVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELM 579
Cdd:cd17634 477 GARRDEDGYYwITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELR 556
|
570 580 590
....*....|....*....|....*....|.
gi 446729151 580 SLVNSHIGKALCPKDIHVVEDLPKTRNSKVM 610
Cdd:cd17634 557 NWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
30-638 |
3.41e-152 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 453.31 E-value: 3.41e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 30 YETFYKKSIEETAWFWGEAekAVGYQWMKPYTEVLDLENGtPFAQWYNGGTCNVVESVLSRWlADDETRTQPALQYE-GE 108
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQ--ARLIDWFKPPEKILDNSNP-PFTRWFVGGRLNTCYNALDRH-VEAGRGDQIALIYDsPV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 109 NGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:cd05967 77 TGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 189 MIITADGFSRRGKVVSLKDEVDKACEHCPTVEKVVIVRHAGN---DFTPHNYDFSWSTLEKEKPFVHAEEMHSDDPLMLI 265
Cdd:cd05967 157 LIVTASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQvpaDLTKPGRDLDWSELLAKAEPVDCVPVAATDPLYIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 266 YTSGTTGKPKGTVHTHAGF--PLKAAFDAGFGMniKQGDrVLWVT-DMGWMMG-PFLLFGSLINGATMVMYEGVPDF-PE 340
Cdd:cd05967 237 YTSGTTGKPKGVVRDNGGHavALNWSMRNIYGI--KPGD-VWWAAsDVGWVVGhSYIVYGPLLHGATTVLYEGKPVGtPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 341 ADRLWETVDKYEITHLGISPTLIRALmAKGD---EYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnVPICNYSGG 417
Cdd:cd05967 314 PGAFWRVIEKYQVNALFTAPTAIRAI-RKEDpdgKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 418 TEISGGIFGN---VLIKPIAPISFNASLPGMAAVVLDDQGNPIR-DEVGELCLEKPWV-GMTKSFWEDDERYVNTYWSRF 492
Cdd:cd05967 390 TETGWPITANpvgLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGpNELGNIVIKLPLPpGCLLTLWKNDERFKKLYLSKF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 493 ENKWVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFS 571
Cdd:cd05967 470 PGYYDTGDAGYKDEDGYLfIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKIT 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 572 GE-LKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSLVNPEVVPFI 638
Cdd:cd05967 550 AEeLEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
28-635 |
1.42e-139 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 422.38 E-value: 1.42e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 28 EDYETFYKKSIEETAWFWgeAEKAVGYQWMKPY------TEVLDLENGTPFAQWYNGGTCNVVESVLSRWLaDDETRTQP 101
Cdd:PLN02654 30 QQYMEMYKRSVDDPAGFW--SDIASQFYWKQKWegdevcSENLDVRKGPISIEWFKGGKTNICYNCLDRNV-EAGNGDKI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 102 ALQYEG-ENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PLN02654 107 AIYWEGnEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIITADGFSRRGKVVSLKDEVDKACEH----------CPTVEKVVIVRHAGNDFTPHNyDFSWSTLEKEKPF 250
Cdd:PLN02654 187 RIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDEsakngvsvgiCLTYENQLAMKREDTKWQEGR-DVWWQDVVPNYPT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 251 -VHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDrVLWVT-DMGWMMG-PFLLFGSLINGA 327
Cdd:PLN02654 266 kCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTD-VYWCTaDCGWITGhSYVTYGPMLNGA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 328 TMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKS 407
Cdd:PLN02654 345 TVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 408 NVPICNYSGGTEiSGGIFGNVL--IKPIAPISfnASLP--GMAAVVLDDQGNPIRDEV-GELCLEKPWVGMTKSFWEDDE 482
Cdd:PLN02654 425 RCPISDTWWQTE-TGGFMITPLpgAWPQKPGS--ATFPffGVQPVIVDEKGKEIEGECsGYLCVKKSWPGAFRTLYGDHE 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 483 RYVNTYWSRFENKWVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCF 561
Cdd:PLN02654 502 RYETTYFKPFAGYYFSGDGCSRDKDGYYwLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAF 581
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 562 VVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK--AAYLGKELGDLSSLVNPEVV 635
Cdd:PLN02654 582 VTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRkiASRQLDELGDTSTLADPGVV 657
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
28-632 |
1.30e-137 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 415.89 E-value: 1.30e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 28 EDYETFYKKSIEETAWFWGEAEKAVgyQWMKPYTEVLDLENgTPFAQWYNGGTCNVVESVLSRWLAddETRTQPALQY-E 106
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRI--DWQTPFTQVLDYSN-PPFARWFVGGRTNLCHNAVDRHLA--KRPEQLALIAvS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 107 GENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAG 186
Cdd:PRK10524 77 TETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 187 SKMIITADGFSRRGKVVSLKDEVDKAC---EHCPtvEKVVIV-RHAGNDFTPHNYDFSWSTLeKEKPF---VHAEEMHSD 259
Cdd:PRK10524 157 PVLIVSADAGSRGGKVVPYKPLLDEAIalaQHKP--RHVLLVdRGLAPMARVAGRDVDYATL-RAQHLgarVPVEWLESN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGF--PLKAAFDAGFGMniKQGDRVLWVTDMGWMMG-PFLLFGSLINGATMVMYEGVP 336
Cdd:PRK10524 234 EPSYILYTSGTTGKPKGVQRDTGGYavALATSMDTIFGG--KAGETFFCASDIGWVVGhSYIVYAPLLAGMATIMYEGLP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 337 DFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKsnvPIC-NY- 414
Cdd:PRK10524 312 TRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVIdNYw 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 415 ---SGGTEISggIFGNVLIKPIAPISFNASLPGMAAVVLDDQ-GNPIR-DEVGELCLEKPW-VGMTKSFWEDDERYVNTY 488
Cdd:PRK10524 389 qteTGWPILA--IARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGpNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 489 WSRFeNKWVHG--DWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLR 565
Cdd:PRK10524 467 WSLF-GRQVYStfDWGIRDADGYYfILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPK 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729151 566 DNVTFSGE-----LKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSLVNP 632
Cdd:PRK10524 546 DSDSLADRearlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDP 617
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1-641 |
2.67e-134 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 408.41 E-value: 2.67e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 1 MKQAVWFPTEEYKEKTRLYGWM------KSLGYEDYETFYKKSIEETAWFWGEAEKAVGYQWMKPYTEVLDlENGTPFAQ 74
Cdd:PRK03584 1 MGDPLWTPSAERIAASRMTAFIrwlaarRGLSFDDYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVLA-GRRMPGAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 75 WYNGGTCNVVESVLsRWLADDEtrtqPALQYEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVV 154
Cdd:PRK03584 80 WFPGARLNYAENLL-RHRRDDR----PAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 155 AMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKVVSLKDEVDKACEHCPTVEKVVIVRHAGN--DF 232
Cdd:PRK03584 155 AMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPaaAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 233 TPHNYDFSWSTL--EKEKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDM 310
Cdd:PRK03584 235 AALPGALLWEDFlaPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFFWYTTC 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 311 GWMMGPFLLfGSLINGATMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGE 390
Cdd:PRK03584 315 GWMMWNWLV-SGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 391 PWNPDPWMWLFETVgKSNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRDEVGELCLEKPW 470
Cdd:PRK03584 394 PLPPEGFDWVYEHV-KADVWLASISGGTDICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPVVGEVGELVCTKPF 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 471 VGMTKSFW--EDDERYVNTYWSRFENKWVHGDWVvydgEQ-----YIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIE 543
Cdd:PRK03584 473 PSMPLGFWndPDGSRYRDAYFDTFPGVWRHGDWI----EItehggVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLD 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 544 AAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLG--- 620
Cdd:PRK03584 549 SLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVELPVKKLLHGrpv 628
|
650 660
....*....|....*....|.
gi 446729151 621 KELGDLSSLVNPEVVPFIQGL 641
Cdd:PRK03584 629 KKAVNRDALANPEALDWFADL 649
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
22-633 |
3.05e-128 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 392.02 E-value: 3.05e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 22 MKSLGYEDYETFYKKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGTPFAQWYNGGTCNVVESVLSRWLADDetrtqP 101
Cdd:cd05943 11 RHGLSLADYAALHRWSVDDPGAFWAAVWDFSGVRGSKPYDVVVVSGRIMPGARWFPGARLNYAENLLRHADADD-----P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 102 ALQYEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTR 181
Cdd:cd05943 86 AAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 182 VQAAGSKMIITADGFSRRGKVVSLKDEVDKACEHCPTVEKVVIVrhaGNDFTPHNYDFS----WSTLEK--------EKP 249
Cdd:cd05943 166 FGQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVV---PYTVAAGQPDLSkiakALTLEDflatgaagELE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 250 FVHAEemhSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLfGSLINGATM 329
Cdd:cd05943 243 FEPLP---FDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV-SGLAVGATI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 330 VMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVgKSNV 409
Cdd:cd05943 319 VLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHI-KPDV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 410 PICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRDEVGELCLEKPWVGMTKSFWEDDE--RYVNT 487
Cdd:cd05943 398 LLASISGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKPFPSMPVGFWNDPDgsRYRAA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 488 YWSRFENKWVHGDWVVYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRD 566
Cdd:cd05943 478 YFAKYPGVWAHGDWIEITPRgGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLRE 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446729151 567 NVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSLVNPE 633
Cdd:cd05943 558 GVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANPE 624
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
75-629 |
5.18e-120 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 368.45 E-value: 5.18e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 75 WYNGGTCNVVESVLSRWlADDETRTQPALQYEGENgTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVV 154
Cdd:PRK04319 36 WLETGKVNIAYEAIDRH-ADGGRKDKVALRYLDAS-RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 155 AMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKVVSLkdevdkacehcPTVEKVVIVRHAGnDFTP 234
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDL-----------PSLKHVLLVGEDV-EEGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 235 HNYDFsWSTLEKEKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAfDAGFGMNIKQGDrVLWVT-DMGWM 313
Cdd:PRK04319 182 GTLDF-NALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQ-TGKYVLDLHEDD-VYWCTaDPGWV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 314 MG-PFLLFGSLINGATMVMYEGvpDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPW 392
Cdd:PRK04319 259 TGtSYGIFAPWLNGATNVIDGG--RF-SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 393 NP---------------DPWmWLFETVGksnVPICNYSGgteisggifgnvliKPIAPISFNASLPGMAAVVLDDQGNPI 457
Cdd:PRK04319 336 NPevvrwgmkvfglpihDNW-WMTETGG---IMIANYPA--------------MDIKPGSMGKPLPGIEAAIVDDQGNEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 458 -RDEVGELCLEKPWVGMTKSFWEDDERYvNTYwsrFENKW-VHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESI 534
Cdd:PRK04319 398 pPNRMGNLAIKKGWPSMMRGIWNNPEKY-ESY---FAGDWyVSGDSAYMDEDGYFwFQGRVDDVIKTSGERVGPFEVESK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 535 LVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:PRK04319 474 LMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
570
....*....|....*
gi 446729151 615 KAAYLGKELGDLSSL 629
Cdd:PRK04319 554 KAWELGLPEGDLSTM 568
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
3-645 |
5.98e-108 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 339.93 E-value: 5.98e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 3 QAVWFPTEEYKEKTRLYGWMKSLG------YEDYETFYKKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGtPFAQWY 76
Cdd:TIGR01217 4 QPLWQPDAQRIAQARMTRFQAWAGehhgaaEGGYDALHRWSVDELDTFWKAVWEWFDVRFSTPCARVVDDRTM-PGAQWF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 77 NGGTCNVVESVLSRwladdeTRTQPALQYEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAM 156
Cdd:TIGR01217 83 PGARLNYAENLLRA------AGTEPALLYVDETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 157 LAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKVVSLKDEVDKACEHCPTVEKVVIVRHAGNDFT--- 233
Cdd:TIGR01217 157 LATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVHIPYLGPRETeap 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 234 --PHNYDFSWSTLEKEKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMG 311
Cdd:TIGR01217 237 kiDGALDLEDFTAAAQAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 312 WMMGPFLLFGsLINGATMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEP 391
Cdd:TIGR01217 317 WMMWNWLVSG-LATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 392 WNPDPWMWLFETVgKSNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRDEVGELCLEKPWV 471
Cdd:TIGR01217 396 LPPDGFRWVYDEI-KADVWLASISGGTDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTGEVGELVCTNPMP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 472 GMTKSFW--EDDERYVNTYWSRFENKWVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:TIGR01217 475 SMPIRFWndPDGSKYRDAYFDTYPGVWRHGDWITLTPRGGIvIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 549 VPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSS 628
Cdd:TIGR01217 555 QEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQGTPVDNPGA 634
|
650
....*....|....*..
gi 446729151 629 LVNPEVVPFIQGLQSSK 645
Cdd:TIGR01217 635 IDNPELLDLYEELAELR 651
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
115-616 |
1.38e-102 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 319.45 E-value: 1.38e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITad 194
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 gfsrrgkvvslkdevdkacehcptvekvvivrhagndfTPHNYdfswstlekekpfvhaEEMHSDDPLMLIYTSGTTGKP 274
Cdd:cd05969 79 --------------------------------------TEELY----------------ERTDPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 275 KGTVHTHAGFpLKAAFDAGFGMNIKQGDrVLWVT-DMGWMMGPFL-LFGSLINGATMVMYEGvpDFpEADRLWETVDKYE 352
Cdd:cd05969 105 KGVLHVHDAM-IFYYFTGKYVLDLHPDD-IYWCTaDPGWVTGTVYgIWAPWLNGVTNVVYEG--RF-DAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 353 ITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFEtvgKSNVPICNYSGGTEISGGIFGNVLIKP 432
Cdd:cd05969 180 VTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGME---VFGVPIHDTWWQTETGSIMIANYPCMP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 433 IAPISFNASLPGMAAVVLDDQGNPIR-DEVGELCLEKPWVGMTKSFWEDDERYVNTywsrFENKW-VHGDWVVYDGEQYI 510
Cdd:cd05969 257 IKPGSMGKPLPGVKAAVVDENGNELPpGTKGILALKPGWPSMFRGIWNDEERYKNS----FIDGWyLTGDLAYRDEDGYF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 511 -ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKA 589
Cdd:cd05969 333 wFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAH 412
|
490 500
....*....|....*....|....*..
gi 446729151 590 LCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05969 413 VAPREIEFVDNLPKTRSGKIMRRVLKA 439
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
115-616 |
7.81e-95 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 298.48 E-value: 7.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAd 194
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 gfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhSDDPLMLIYTSGTTGKP 274
Cdd:cd05972 80 ---------------------------------------------------------------AEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 275 KGTVHTHAgFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGP-FLLFGSLINGATMVMYEGVPdFpEADRLWETVDKYEI 353
Cdd:cd05972 97 KGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAwSSFFGPWLLGATVFVYEGPR-F-DAERILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 354 THLGISPTLIRALMAKG-DEYVnkhsLKSLEVFASTGEPWNPDPWMWLFETVGksnVPICNYSGGTEiSGGIFGNVLIKP 432
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDlSSYK----FSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTE-TGLTVGNFPDMP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 433 IAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPWVGMTKSFWEDDERYVntywSRFENKWVH-GDWVVYDGEQYI 510
Cdd:cd05972 246 VKPGSMGRPTPGYDVAIIDDDGRELPPgEEGDIAIKLPPPGLFLGYVGDPEKTE----ASIRGDYYLtGDRAYRDEDGYF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 511 -ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKA 589
Cdd:cd05972 322 wFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPY 401
|
490 500
....*....|....*....|....*..
gi 446729151 590 LCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05972 402 KYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
88-624 |
1.71e-89 |
|
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: 285.55 E-value: 1.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 88 LSRWLAD--DETRTQPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI 165
Cdd:COG0318 1 LADLLRRaaARHPDRPALVFGGR-----RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 166 ISPIFSGFASDAVMTRVQAAGSKMIITAdgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstle 245
Cdd:COG0318 76 VVPLNPRLTAEELAYILEDSGARALVTA---------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 246 kekpfvhaeemhsddplMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVT----DMGWMMGpflLFG 321
Cdd:COG0318 104 -----------------LILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGLTVG---LLA 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 322 SLINGATMVMyegVPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWNPDPWMWLF 401
Cdd:COG0318 163 PLLAGATLVL---LPRF-DPERVLELIERERVTVLFGVPTMLARLLRHPE--FARYDLSSLRLVVSGGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 402 ETVGksnVPICNYSGGTEISGGIFGNVLIKPIAPIsfnAS----LPGMAAVVLDDQGNPI-RDEVGELCLEKPWVgmTKS 476
Cdd:COG0318 237 ERFG---VRIVEGYGLTETSPVVTVNPEDPGERRP---GSvgrpLPGVEVRIVDEDGRELpPGEVGEIVVRGPNV--MKG 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 477 FWEDDERYVNTywsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVK 554
Cdd:COG0318 309 YWNDPEATAEA----FRDGWLRtGDLGRLDEDGYLyIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW 384
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 555 GEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELG 624
Cdd:COG0318 385 GERVVAFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
5-616 |
3.96e-84 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 279.27 E-value: 3.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 5 VWFPTEEYKEKTRLYGWMKSLGYE-----------DYETFYKKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGT-PF 72
Cdd:PLN03052 86 AWFPSPEIAKLTNLGRLLEARGKEllgskykdpisSFSEFQRFSVENPEVYWSIVLDELSLVFSVPPRCILDTSDESnPG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 73 AQWYNGGTCNVVESVLSrwLADDETRTQPALQY--EGENGTSKSF-TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMI 149
Cdd:PLN03052 166 GQWLPGAVLNVAECCLT--PKPSKTDDSIAIIWrdEGSDDLPVNRmTLSELRSQVSRVANALDALGFEKGDAIAIDMPMN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 150 PETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKVVSLKDEVDKACEHcptveKVVIVRHAG 229
Cdd:PLN03052 244 VHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEAKAP-----KAIVLPADG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 230 NDFTP--HNYDFSW-------STLEKEKPFVhAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGfPLKAAFDAGFGMNIKQ 300
Cdd:PLN03052 319 KSVRVklREGDMSWddflaraNGLRRPDEYK-AVEQPVEAFTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRK 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 301 GDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVPDFPEADRLwetVDKYEITHLGISPTLIRALmaKGDEYVNKHSLK 380
Cdd:PLN03052 397 GDIVCWPTNLGWMMGPWLVYASLLNGATLALYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVKTW--KNTNCMAGLDWS 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 381 SLEVFASTGEPWNPDPWMWLFETVGKSnvPICNYSGGTEISGGIFGNVLIKPIAPISFnaSLPGM--AAVVLDDQGNPIR 458
Cdd:PLN03052 472 SIRCFGSTGEASSVDDYLWLMSRAGYK--PIIEYCGGTELGGGFVTGSLLQPQAFAAF--STPAMgcKLFILDDSGNPYP 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 459 DEV---GELCLEKPWVGMTKSFWEDDerYVNTYWS---RFENKWV--HGDwvVYD---GEQYIITGRSDDTLNIAGKRIG 527
Cdd:PLN03052 548 DDApctGELALFPLMFGASSTLLNAD--HYKVYFKgmpVFNGKILrrHGD--IFErtsGGYYRAHGRADDTMNLGGIKVS 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 528 PAEYESILVK-HNDVIEAAAIGVPDDVKG-EVCHCFVVLRDnVTFSGELKKELMSLVNSHIGKALCP----KDIHVVEDL 601
Cdd:PLN03052 624 SVEIERVCNAaDESVLETAAIGVPPPGGGpEQLVIAAVLKD-PPGSNPDLNELKKIFNSAIQKKLNPlfkvSAVVIVPSF 702
|
650
....*....|....*
gi 446729151 602 PKTRNSKVMRRVIKA 616
Cdd:PLN03052 703 PRTASNKVMRRVLRQ 717
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
109-616 |
3.34e-77 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 252.74 E-value: 3.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 109 NGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 189 MIITaDGfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhSDDPLMLIYTS 268
Cdd:cd05971 81 ALVT-DG--------------------------------------------------------------SDDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 269 GTTGKPKGTVHTHAgFPLKAAFDAGFGMNI-KQGDRVLWVT-DMGWMMGPF-LLFGSLINGATMVMYEGVPdFpEADRLW 345
Cdd:cd05971 98 GTTGPPKGALHAHR-VLLGHLPGVQFPFNLfPRDGDLYWTPaDWAWIGGLLdVLLPSLYFGVPVLAHRMTK-F-DPKAAL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 346 ETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnVPICNYSGGTEISGGIF 425
Cdd:cd05971 175 DLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFG---VEVNEFYGQTECNLVIG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 426 GNVLIKPIAPISFNASLPGMAAVVLDDQGNPI-RDEVGELCLEKPWVGMTKSFWEDDERYVntywSRFENKW-VHGDWVV 503
Cdd:cd05971 250 NCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLpPGEVGEIAVELPDPVAFLGYWNNPSATE----KKMAGDWlLTGDLGR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 504 YDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLV 582
Cdd:cd05971 326 KDSDGYFwYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELV 405
|
490 500 510
....*....|....*....|....*....|....
gi 446729151 583 NSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05971 406 KTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
108-522 |
1.65e-76 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 250.31 E-value: 1.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 108 ENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGS 187
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 188 KMIITADGFsrrgkvvslkdEVDKACEHCPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFVHAEEMHSDDPLMLIYT 267
Cdd:pfam00501 95 KVLITDDAL-----------KLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 268 SGTTGKPKGTVHTHAG-----FPLKAAFDAGFGMNikQGDRVLWVTDMGWMMG-PFLLFGSLINGATMVMYEGVPDFPeA 341
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNlvanvLSIKRVRPRGFGLG--PDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALD-P 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 342 DRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSlkSLEVFASTGEPWNPDPWMWLFETVGksnVPICNYSGGTEIS 421
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 422 GGIFGNVLikPIAPISFNAS----LPGMAAVVLDDQ-GNPIRD-EVGELCLEKPWVgmTKSFWEDDERYVNTYWsrfENK 495
Cdd:pfam00501 316 GVVTTPLP--LDEDLRSLGSvgrpLPGTEVKIVDDEtGEPVPPgEPGELCVRGPGV--MKGYLNDPELTAEAFD---EDG 388
|
410 420
....*....|....*....|....*....
gi 446729151 496 WVH-GDWVVYDGEQYI-ITGRSDDTLNIA 522
Cdd:pfam00501 389 WYRtGDLGRRDEDGYLeIVGRKKDQIKLG 417
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-615 |
1.50e-71 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 237.80 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIT-A 193
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTdA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 DgfsRRGKVvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhSDDPLMLIYTSGTTGK 273
Cdd:cd05973 81 A---NRHKL-------------------------------------------------------DSDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 274 PKGTVHthagfPLKA--AFDA--GFGMNIKQGDRVLWVTDMGWMMGPFL-LFGSLINGATMVMYEGvpDFpEADRLWETV 348
Cdd:cd05973 103 PKGVPV-----PLRAlaAFGAylRDAVDLRPEDSFWNAADPGWAYGLYYaITGPLALGHPTILLEG--GF-SVESTWRVI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 349 DKYEITHLGISPTLIRALMAKGDEYVNKHSLKsLEVFASTGEPWNPDPWMWLFETVGksnVPICNYSGGTEIsGGIFGN- 427
Cdd:cd05973 175 ERLGVTNLAGSPTAYRLLMAAGAEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTEL-GMVLANh 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 428 -VLIKPIAPISFNASLPGMAAVVLDDQGN-PIRDEVGELCLE---KP--WVGmtkSFWEDDERYVNTYWSRfenkwvHGD 500
Cdd:cd05973 250 hALEHPVHAGSAGRAMPGWRVAVLDDDGDeLGPGEPGRLAIDianSPlmWFR---GYQLPDTPAIDGGYYL------TGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 501 WVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELM 579
Cdd:cd05973 321 TVEFDPDGSFsFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQ 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 446729151 580 SLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05973 401 LHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
260-610 |
3.83e-71 |
|
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: 233.72 E-value: 3.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGvpdfP 339
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK----F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 340 EADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnVPICNYSGGTE 419
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPES--AGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 420 ISGGI-FGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPWVgmTKSFWEDDERyvnTYwSRFENKWV 497
Cdd:cd04433 151 TGGTVaTGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPgEIGELVVRGPSV--MKGYWNNPEA---TA-AVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 498 H-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNvtfSGELK 575
Cdd:cd04433 225 RtGDLGRLDEDGYLyIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG---ADLDA 301
|
330 340 350
....*....|....*....|....*....|....*
gi 446729151 576 KELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVM 610
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
111-610 |
9.20e-70 |
|
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: 234.41 E-value: 9.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 111 TSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 191 ITAdgfsrrgkvVSLKDEVDKACEHCPTVEKVVIVRHAGnDFTPHNYDFSWSTLEKEKPFVHAEEMHS-DDPLMLIYTSG 269
Cdd:cd05911 87 FTD---------PDGLEKVKEAAKELGPKDKIIVLDDKP-DGVLSIEDLLSPTLGEEDEDLPPPLKDGkDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 270 TTGKPKGTVHTH----AGFPLKAAFdagFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyegVPDFpEADRLW 345
Cdd:cd05911 157 TTGLPKGVCLSHrnliANLSQVQTF---LYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVII---MPKF-DSELFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 346 ETVDKYEITHLGISPTLIrALMAKgDEYVNKHSLKSLEVFASTGEPWNPDpwmwLFETVGK--SNVPICNYSGGTEISGG 423
Cdd:cd05911 230 DLIEKYKITFLYLVPPIA-AALAK-SPLLDKYDLSSLRVILSGGAPLSKE----LQELLAKrfPNATIKQGYGMTETGGI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 424 IFgnvlIKPIAPISFNAS---LPGMAAVVLDDQGNPI--RDEVGELCLEKPwvGMTKSFWEDDEryvNTYWSRFENKWVH 498
Cdd:cd05911 304 LT----VNPDGDDKPGSVgrlLPNVEAKIVDDDGKDSlgPNEPGEICVRGP--QVMKGYYNNPE---ATKETFDEDGWLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 499 -GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSgelKK 576
Cdd:cd05911 375 tGDIGYFDEDGYLyIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLT---EK 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 446729151 577 ELMSLVNSHIGKAlcpKDIH----VVEDLPKTRNSKVM 610
Cdd:cd05911 452 EVKDYVAKKVASY---KQLRggvvFVDEIPKSASGKIL 486
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
146-616 |
1.57e-69 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 234.32 E-value: 1.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 146 MPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKVVSLKDEVDKACEHcptveKVVIV 225
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPA-----KAIVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 226 RHAGNDFTP--HNYDFSWST-LEKEKPFVHAEEMH-------SDDPLMLIYTSGTTGKPKGTVHTHAGfPLKAAFDAGFG 295
Cdd:PLN03051 76 PAAGEPVAVplREQDLSWCDfLGVAAAQGSVGGNEyspvyapVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 296 MNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVP------DFPEADRlwetvdkyeITHLGISPTLIRALMAK 369
Cdd:PLN03051 155 MDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAPlgrgfgKFVQDAG---------VTVLGLVPSIVKAWRHT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 370 GDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSNvPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVV 449
Cdd:PLN03051 226 GAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQAPGAFSTASLGTRFVL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 450 LDDQGNPIRDE---VGELCLEKPWVGMTKSFWEDDERYVntYWS---RFENKWV----HGDWVV-YDGEQYIITGRSDDT 518
Cdd:PLN03051 305 LNDNGVPYPDDqpcVGEVALAPPMLGASDRLLNADHDKV--YYKgmpMYGSKGMplrrHGDIMKrTPGGYFCVQGRADDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 519 LNIAGKRIGPAEYESILVKHND-VIEAAAIGV-PDDVKGEVCHCFVvlrdnvtFSGELKK--------ELMSLVNSHIGK 588
Cdd:PLN03051 383 MNLGGIKTSSVEIERACDRAVAgIAETAAVGVaPPDGGPELLVIFL-------VLGEEKKgfdqarpeALQKKFQEAIQT 455
|
490 500 510
....*....|....*....|....*....|..
gi 446729151 589 ALCP----KDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PLN03051 456 NLNPlfkvSRVKIVPELPRNASNKLLRRVLRD 487
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
99-622 |
1.30e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 229.69 E-value: 1.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 99 TQPALQYEGENgtsksFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAV 178
Cdd:PRK06187 21 DKEAVYFDGRR-----TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 179 MTRVQAAGSKMIITADGFSrrgkvvslkDEVDKACEHCPTVEKVVIVRHAGNDFTP---HNYDFSWSTLEKEKPFVHAEE 255
Cdd:PRK06187 96 AYILNDAEDRVVLVDSEFV---------PLLAAILPQLPTVRTVIVEGDGPAAPLApevGEYEELLAAASDTFDFPDIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 256 mhsDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGfGMNIKQGDRVLWVTDM------GWMMGPFLLfgslinGATM 329
Cdd:PRK06187 167 ---NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCA-WLKLSRDDVYLVIVPMfhvhawGLPYLALMA------GAKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 330 VMyegvPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPWNPDpwmWLFETVGKSNV 409
Cdd:PRK06187 237 VI----PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAY--FVDFSSLRLVIYGGAALPPA---LLREFKEKFGI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 410 PICNYSGGTEISGGIFGNVL---IKPIAPISFNA--SLPGMAAVVLDDQGNPI-RD--EVGELCLEKPWvgMTKSFWEDD 481
Cdd:PRK06187 308 DLVQGYGMTETSPVVSVLPPedqLPGQWTKRRSAgrPLPGVEARIVDDDGDELpPDggEVGEIIVRGPW--LMQGYWNRP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 482 ERYVNTywsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCH 559
Cdd:PRK06187 386 EATAET----IDGGWLHtGDVGYIDEDGYLyITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446729151 560 CFVVLRDNVTFSgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKE 622
Cdd:PRK06187 462 AVVVLKPGATLD---AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
82-615 |
7.35e-66 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). 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 family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 225.45 E-value: 7.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 82 NVVESVLSRWLADDETRTqpALQYEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMK 161
Cdd:cd05970 17 NFAYDVVDAMAKEYPDKL--ALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 162 IGAIISPIFSGFASDAVMTRVQAAGSKMIITADGfsrrgkvVSLKDEVDKACEHCPTVEKVVIVrhaGNDFTPHNYDFSw 241
Cdd:cd05970 95 LGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE-------DNIPEEIEKAAPECPSKPKLVWV---GDPVPEGWIDFR- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 242 STLEKEKPFV---HAE-EMHSDDPLMLIYTSGTTGKPKGTVHTHAgFPLKAAFDAGFGMNIKQGDRVLWVTDMGW---MM 314
Cdd:cd05970 164 KLIKNASPDFerpTANsYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWgkaVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 315 GPFllFGSLINGATMVMYEGVPDFPEAdrLWETVDKYEITHLGISPTLIRALMakgDEYVNKHSLKSLEVFASTGEPWNP 394
Cdd:cd05970 243 GKI--YGQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFCAPPTIYRFLI---REDLSRYDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 395 DpwmwLFETV-GKSNVPICNYSGGTEISGGIfGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIR-DEVGELCLE----K 468
Cdd:cd05970 316 E----VFNTFkEKTGIKLMEGFGQTETTLTI-ATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEaGEEGEIVIRtskgK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 469 PwVGMTKSFWEDDERYVNTYwsrFENKWVHGD--WVVYDGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:cd05970 391 P-VGLFGGYYKDAEKTAEVW---HDGYYHTGDaaWMDEDGYLWFV-GRTDDLIKSSGYRIGPFEVESALIQHPAVLECAV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446729151 547 IGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05970 466 TGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
100-611 |
2.37e-62 |
|
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: 213.24 E-value: 2.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 100 QPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:cd17631 11 RTALVFGGR-----SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 180 TRVQAAGSKMIItadgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhsD 259
Cdd:cd17631 86 YILADSGAKVLF-------------------------------------------------------------------D 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDM--GWMMGPFLLFGsLINGATMVMYEGvpd 337
Cdd:cd17631 99 DLALLMYTSGTTGRPKGAMLTHRNL-LWNAVNALAALDLGPDDVLLVVAPLfhIGGLGVFTLPT-LLRGGTVVILRK--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 338 fPEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWnPDPwmwLFETVGKSNVPICNYSGG 417
Cdd:cd17631 174 -FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPM-PER---LLRALQARGVKFVQGYGM 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 418 TEISGGIFGN----VLIKPIapiSFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPwvGMTKSFWEDDERYVNTywsrF 492
Cdd:cd17631 247 TETSPGVTFLspedHRRKLG---SAGRPVFFVEVRIVDPDGREVPPgEVGEIVVRGP--HVMAGYWNRPEATAAA----F 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 493 ENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTF 570
Cdd:cd17631 318 RDGWFHtGDLGRLDEDGYLyIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAEL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446729151 571 SGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17631 398 DED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
82-615 |
2.54e-60 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 210.40 E-value: 2.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 82 NVVESVLSRWlADDETRTQ----PALQYEGENGTSKSFTYEELDSWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAM 156
Cdd:cd05928 6 NFASDVLDQW-ADKEKAGKrppnPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 157 LAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADgfsrrgkvvSLKDEVDKACEHCPTVEKVVIVrhagndfTPHN 236
Cdd:cd05928 85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD---------ELAPEVDSVASECPSLKTKLLV-------SEKS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 237 YDfSWstLEKEKPFVHAEEMH------SDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDrVLW-VTD 309
Cdd:cd05928 149 RD-GW--LNFKELLNEASTEHhcvetgSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASD-IMWnTSD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 310 MGWMMGPF-LLFGSLINGATMVMYEgVPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGdeyVNKHSLKSLEVFAST 388
Cdd:cd05928 225 TGWIKSAWsSLFEPWIQGACVFVHH-LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 389 GEPWNPD---PW-----MWLFETVGKSN-VPICNYSGGTEISGGIFGnvliKPIapisfnaslPGMAAVVLDDQGN--PI 457
Cdd:cd05928 300 GEPLNPEvleKWkaqtgLDIYEGYGQTEtGLICANFKGMKIKPGSMG----KAS---------PPYDVQIIDDNGNvlPP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 458 RDEvGELCL----EKPwVGMTKSFWEDDERYVNTYWSRFenkWVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYE 532
Cdd:cd05928 367 GTE-GDIGIrvkpIRP-FGLFSGYVDNPEKTAATIRGDF---YLTGDRGIMDEDGYFwFMGRADDVINSSGYRIGPFEVE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 533 SILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLrdNVTFSG----ELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSK 608
Cdd:cd05928 442 SALIEHPAVVESAVVSSPDPIRGEVVKAFVVL--APQFLShdpeQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGK 519
|
....*..
gi 446729151 609 VMRRVIK 615
Cdd:cd05928 520 IQRNELR 526
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-616 |
1.47e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 205.14 E-value: 1.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 82 NVVESVLSrwlADDETRTQPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMK 161
Cdd:PRK07656 6 TLPELLAR---AARRFGDKEAYVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 162 IGAI---ISPIFSGFASDAVMTRvqaAGSKMIITADGFsrRGKVVSLKDEVdkacehcPTVEKVVIVR-HAGNDFTPHNY 237
Cdd:PRK07656 78 AGAVvvpLNTRYTADEAAYILAR---GDAKALFVLGLF--LGVDYSATTRL-------PALEHVVICEtEEDDPHTEKMK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 238 DFSwSTLEKEKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMgwmmgpF 317
Cdd:PRK07656 146 TFT-DFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQL-LSNAADWAEYLGLTEGDRYLAANPF------F 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 318 LLFG-------SLINGATMVMyegVPDFpEADRLWETVDKYEITHLGISPTLIRALMA--KGDEYvnkhSLKSLEVFAST 388
Cdd:PRK07656 218 HVFGykagvnaPLMRGATILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQhpDRSAE----DLSSLRLAVTG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 389 GEPWNPDpwmwLFETV-GKSNVPIC--NYsGGTEISggifGNVLIKPI------APISFNASLPGMAAVVLDDQGNPI-R 458
Cdd:PRK07656 290 AASMPVA----LLERFeSELGVDIVltGY-GLSEAS----GVTTFNRLdddrktVAGTIGTAIAGVENKIVNELGEEVpV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 459 DEVGELCLEKPWVgMtKSFWEDDERYVNTYwsRFENkWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILV 536
Cdd:PRK07656 361 GEVGELLVRGPNV-M-KGYYDDPEATAAAI--DADG-WLHtGDLGRLDEEGYLyIVDRKKDMFIVGGFNVYPAEVEEVLY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 537 KHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK07656 436 EHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
100-615 |
1.66e-57 |
|
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: 201.25 E-value: 1.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 100 QPALQYEGengtsKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:cd05936 15 KTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 180 TRVQAAGSKMIITADGFSRRGKvvslkdevdkacehcptvekvvivrhagndfTPHNYDFswstlekeKPFVHAeemhsD 259
Cdd:cd05936 90 HILNDSGAKALIVAVSFTDLLA-------------------------------AGAPLGE--------RVALTP-----E 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGFplkaafdagfGMNIKQGDRvlWVTDMGW----MMGP---FLLFG-------SLIN 325
Cdd:cd05936 126 DVAVLQYTSGTTGVPKGAMLTHRNL----------VANALQIKA--WLEDLLEgddvVLAAlplFHVFGltvalllPLAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 326 GATMVMyegVPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWNPDpwmwLFETVG 405
Cdd:cd05936 194 GATIVL---IPRF-RPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVE----VAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 406 K-SNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPI-RDEVGELCLEKPWVgmTKSFWEDDER 483
Cdd:cd05936 264 ElTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELpPGEVGELWVRGPQV--MKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 484 YVNTywsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCF 561
Cdd:cd05936 342 TAEA----FVDGWLRtGDIGYMDEDGYFfIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAF 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446729151 562 VVLRDNVTFSgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05936 418 VVLKEGASLT---EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
113-611 |
3.94e-54 |
|
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: 191.14 E-value: 3.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispifsgfasdAVMTRVQAAgskmiit 192
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAI-----------AVVINPLLH------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 193 adgfsrrgkvvslKDEVDKACEHCptvEKVVIVRHAgndftphnydfswstlekekpfvhaeemhsDDPLMLIYTSGTTG 272
Cdd:cd05919 71 -------------PDDYAYIARDC---EARLVVTSA------------------------------DDIAYLLYSSGTTG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 273 KPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDM--GWMMGPFLLFGsLINGATMVMYEGVPDfpeADRLWETVDK 350
Cdd:cd05919 105 PPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNSLWFP-LAVGASAVLNPGWPT---AERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 351 YEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnVPICNYSGGTEIsGGIFGNVLI 430
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEV-GHIFLSNRP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 431 KPIAPISFNASLPGMAAVVLDDQGNPIR-DEVGELCLEKPwvGMTKSFWEDDERYVntywSRFENKWVH-GDWVVYDGEQ 508
Cdd:cd05919 255 GAWRLGSTGRPVPGYEIRLVDEEGHTIPpGEEGDLLVRGP--SAAVGYWNNPEKSR----ATFNGGWYRtGDKFCRDADG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 509 -YIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIG 587
Cdd:cd05919 329 wYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLS 408
|
490 500
....*....|....*....|....
gi 446729151 588 KALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd05919 409 AHKVPRRIAFVDELPRTATGKLQR 432
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
100-612 |
1.01e-53 |
|
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: 190.43 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 100 QPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDavm 179
Cdd:cd05930 3 AVAVVDGDQ-----SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 180 tRVQA----AGSKMIITadgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaee 255
Cdd:cd05930 75 -RLAYiledSGAKLVLT--------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 256 mHSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVT----DMGWMMgpflLFGSLINGATMVM 331
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRGL-VNLLLWMQEAYPLTPGDRVLQFTsfsfDVSVWE----IFGALLAGATLVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 332 yegVPDFPEAD--RLWETVDKYEITHLGISPTLIRALMakgdEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVgkSNV 409
Cdd:cd05930 165 ---LPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLL----QELELAALPSLRLVLVGGEALPPDLVRRWRELL--PGA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 410 PICNYSGGTEISGGI-FGNVL--IKPIAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPwvGMTKSFWED----D 481
Cdd:cd05930 236 RLVNLYGPTEATVDAtYYRVPpdDEEDGRVPIGRPIPNTRVYVLDENLRPVPPgVPGELYIGGA--GLARGYLNRpeltA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 482 ERYVNTYWsrFENKWVH--GDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGE 556
Cdd:cd05930 314 ERFVPNPF--GPGERMYrtGDLVRWlpDGNlEFL--GRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEK 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446729151 557 VCHCFVVLRDNVTFS-GELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd05930 390 RLVAYVVPDEGGELDeEELRAHLAERLPDY----MVPSAFVVLDALPLTPNGKVDRK 442
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
113-615 |
2.05e-50 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 181.14 E-value: 2.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispifsgfaSDAVMTRVQAAGSKMII 191
Cdd:cd05958 9 REWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAI---------AVATMPLLRPKELAYIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 tadGFSRRGKVVslkdevdkaCEHcptvekvvivrhagndftphnydfswstlekekpfvhaEEMHSDDPLMLIYTSGTT 271
Cdd:cd05958 80 ---DKARITVAL---------CAH--------------------------------------ALTASDDICILAFTSGTT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 272 GKPKGTVHTHAGfpLKAAFDaGFGMNI---KQGDRVLWVTDM--GWMMGPFLLFgSLINGATMVMYEGVpdfpEADRLWE 346
Cdd:cd05958 110 GAPKATMHFHRD--PLASAD-RYAVNVlrlREDDRFVGSPPLafTFGLGGVLLF-PFGVGASGVLLEEA----TPDLLLS 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 347 TVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnVPICNYSGGTEISGgIFG 426
Cdd:cd05958 182 AIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFH-IFI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 427 NVLIKPIAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPwvgmtKSFWEDDERYVNTYwsrFENKW-VHGDWVVY 504
Cdd:cd05958 256 SARPGDARPGATGKPVPGYEAKVVDDEGNPVPDgTIGRLAVRGP-----TGCRYLADKRQRTY---VQGGWnITGDTYSR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 505 DGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVN 583
Cdd:cd05958 328 DPDGYFrHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAK 407
|
490 500 510
....*....|....*....|....*....|..
gi 446729151 584 SHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05958 408 AHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
110-615 |
1.23e-49 |
|
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: 180.64 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 110 GTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 190 IITADGFSRRgkvvsLKDEVDKACehcPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPfvhAEEMHSDDPLMLIYTSG 269
Cdd:cd05959 105 VVVSGELAPV-----LAAALTKSE---HTLVVLIVSGGAGPEAGALLLAELVAAEAEQLK---PAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 270 TTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDM--GWMMGPFLLFgSLINGATMVMYegvPDFPEADRLWET 347
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLffAYGLGNSLTF-PLSVGATTVLM---PERPTPAAVFKR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 348 VDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFASTGEPwnpdpwmwLFETVGKS-----NVPICNYSGGTEIsG 422
Cdd:cd05959 250 IRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEA--------LPAEVGERwkarfGLDILDGIGSTEM-L 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 423 GIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPWVGMTksfwedderyvntYWSR-------FEN 494
Cdd:cd05959 319 HIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADgEPGELYVRGPSSATM-------------YWNNrdktrdtFQG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 495 KWVH-GDWVVYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSG 572
Cdd:cd05959 386 EWTRtGDKYVRDDDgFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSE 465
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446729151 573 ELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05959 466 ALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
110-615 |
7.31e-49 |
|
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: 178.27 E-value: 7.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 110 GTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 190 IITADGFSrrgkvvslkDEVDKACEHcptvEKVVIVRHAGNDFTPHNYD--FSWSTLEKEKPFVHAE-EMHSDDPLMLIY 266
Cdd:cd05926 90 VLTPKGEL---------GPASRAASK----LGLAILELALDVGVLIRAPsaESLSNLLADKKNAKSEgVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 267 TSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDM----GWMMGpflLFGSLINGATMVMyegvPDFPEAD 342
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNL-AASATNITNTYKLTPDDRTLVVMPLfhvhGLVAS---LLSTLAAGGSVVL----PPRFSAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 343 RLWETVDKYEITHLGISPTLIRAL--MAKGDEYVNKHSLKslevFA-STGEPWNPDPWMWLFETVGksnVP-ICNYsGGT 418
Cdd:cd05926 229 TFWPDVRDYNATWYTAVPTIHQILlnRPEPNPESPPPKLR----FIrSCSASLPPAVLEALEATFG---APvLEAY-GMT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 419 EISGGIFGNVLikPIAPISF-NASLP-GMAAVVLDDQGNPIRD-EVGELCLEKPWVgmTKSFWEDDEryvNTYWSRFENK 495
Cdd:cd05926 301 EAAHQMTSNPL--PPGPRKPgSVGKPvGVEVRILDEDGEILPPgVVGEICLRGPNV--TRGYLNNPE---ANAEAAFKDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 496 WVH-GDWVVYDGEQY-IITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSge 573
Cdd:cd05926 374 WFRtGDLGYLDADGYlFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVT-- 451
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446729151 574 lKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05926 452 -EEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
111-612 |
9.11e-49 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 178.20 E-value: 9.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 111 TSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:cd05904 29 TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 191 IT----ADGFSRRGKVVSLKDEVDKACEHcptvekvvivrhagndftphnydFSWSTLEKEKPFVHAEEMHSDDPLMLIY 266
Cdd:cd05904 109 FTtaelAEKLASLALPVVLLDSAEFDSLS-----------------------FSDLLFEADEAEPPVVVIKQDDVAALLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 267 TSGTTGKPKGTVHTHAGF-PLKAAFDAGFGMNIKQGDRVLWVTDMGWMMG-PFLLFGSLINGATMVMyegVPDFpEADRL 344
Cdd:cd05904 166 SSGTTGRSKGVMLTHRNLiAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGlSSFALGLLRLGATVVV---MPRF-DLEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 345 WETVDKYEITHLGISPTLIRAlMAKGDEyVNKHSLKSLEVFASTGEPWNPDpwmwLFETVGKS--NVPICNYSGGTEISG 422
Cdd:cd05904 242 LAAIERYKVTHLPVVPPIVLA-LVKSPI-VDKYDLSSLRQIMSGAAPLGKE----LIEAFRAKfpNVDLGQGYGMTESTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 423 GI--FGNVLIKPIAPISFNASLPGMAAVVLD-DQGNPI-RDEVGELCLEKPWVgMTKsfwedderYVN----TYWSRFEN 494
Cdd:cd05904 316 VVamCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLpPNQTGELWIRGPSI-MKG--------YLNnpeaTAATIDKE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 495 KWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSG 572
Cdd:cd05904 387 GWLHtGDLCYIDEDGYLfIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTE 466
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446729151 573 elkKELMSLVNSHIG--KALcpKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd05904 467 ---DEIMDFVAKQVApyKKV--RKVAFVDAIPKSPSGKILRK 503
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
116-546 |
1.16e-47 |
|
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: 172.84 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLK-HAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDavmtRVQA----AGSKMI 190
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAE----RLAFiledAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 191 ITADGFSrrgkvvSLKDEVDKACEHCPTVEKVVIVRHAgndftphnydfswstlekeKPFVHAEEMHSDDPLMLIYTSGT 270
Cdd:TIGR01733 77 LTDSALA------SRLAGLVLPVILLDPLELAALDDAP-------------------APPPPDAPSGPDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 271 TGKPKGTVHTHAGFplkAAFDAGFG--MNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVPDFPEADRLWETV 348
Cdd:TIGR01733 132 TGRPKGVVVTHRSL---VNLLAWLArrYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 349 DKYEITHLGISPTLIRALMAKGDEyvnkhSLKSLEVFASTGEPWNP---DPWMWLFEtvgksNVPICNYSGGTEISGGIF 425
Cdd:TIGR01733 209 AEHPVTVLNLTPSLLALLAAALPP-----ALASLRLVILGGEALTPalvDRWRARGP-----GARLINLYGPTETTVWST 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 426 GNVLIKPIAPISFNAS----LPGMAAVVLDDQGNPI-RDEVGELCLEKPWVGmtKSFWEDD----ERYV-NTYWSRFENK 495
Cdd:TIGR01733 279 ATLVDPDDAPRESPVPigrpLANTRLYVLDDDLRPVpVGVVGELYIGGPGVA--RGYLNRPeltaERFVpDPFAGGDGAR 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446729151 496 WVH-GDWVVY--DGEqYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:TIGR01733 357 LYRtGDLVRYlpDGN-LEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
29-614 |
1.44e-46 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 174.54 E-value: 1.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 29 DYETFYKKSIEETAWFWGEAEKAVGYqWMKPYTEVLDLENGTPfaQWYNGGTCNVVESVLSRWLADDETRTQPALQYEGE 108
Cdd:PTZ00237 9 DYENDSNYANSNPESFWDEVAKKYVH-WDKMYDKVYSGDEIYP--DWFKGGELNTCYNVLDIHVKNPLKRDQDALIYECP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 109 --NGTSKsFTYEELDSWV---SRVangLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQ 183
Cdd:PTZ00237 86 ylKKTIK-LTYYQLYEKVcefSRV---LLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 184 AAGSKMIITADGFSRRGKVVSLKDEVDKACEhCPTVEKVVIVRHAGNDFTPHNYD------------FSW-STLEK---- 246
Cdd:PTZ00237 162 TITPKLIITTNYGILNDEIITFTPNLKEAIE-LSTFKPSNVITLFRNDITSESDLkkietiptipntLSWyDEIKKiken 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 247 -EKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLIN 325
Cdd:PTZ00237 241 nQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 326 GATMVMYEG--VPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHS---LKSLEVFASTGEPWNPDPWMWL 400
Cdd:PTZ00237 321 GNTFVMFEGgiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSkydLSNLKEIWCGGEVIEESIPEYI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 401 FEtvgKSNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPW-VGMTKSFW 478
Cdd:PTZ00237 401 EN---KLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVnEIGEVAFKLPMpPSFATTFY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 479 EDDERYVNTYwSRFENKWVHGDwVVYDGEQ--YIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGE 556
Cdd:PTZ00237 478 KNDEKFKQLF-SKFPGYYNSGD-LGFKDENgyYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYN 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729151 557 VCHCFVVLRDNVTFSG----ELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:PTZ00237 556 VPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
101-617 |
4.06e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 170.14 E-value: 4.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQY---EGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGaIISPIFSGFASDA 177
Cdd:PRK07529 42 PALSFlldADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 178 VMTRVQAAGSKMIITADGFSRrgkvVSLKDEVDKACEHCPTVEKVVIVRHAGNDFTP------------HNYDFSWSTLE 245
Cdd:PRK07529 121 IAELLRAAGAKVLVTLGPFPG----TDIWQKVAEVLAALPELRTVVEVDLARYLPGPkrlavplirrkaHARILDFDAEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 246 KEKPFVH---AEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGfPLKAAFDAGFGMNIKQGDRVLWVTDMgwmmgpFLLFGS 322
Cdd:PRK07529 197 ARQPGDRlfsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPL------FHVNAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 323 LIN-------GATMVM-----YEGvpdfPEA-DRLWETVDKYEITHLGISPTLIRALMAKGdeyVNKHSLKSLEVFASTG 389
Cdd:PRK07529 270 LVTglaplarGAHVVLatpqgYRG----PGViANFWKIVERYRINFLSGVPTVYAALLQVP---VDGHDISSLRYALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 390 EPWNPDpwmwLFETV-GKSNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPG--MAAVVLDDQGNPIRD----EVG 462
Cdd:PRK07529 343 APLPVE----VFRRFeAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYqrVRVVILDDAGRYLRDcavdEVG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 463 ELCLEKPWV--GMT-----KSFWEDDeRYVNTywsrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESI 534
Cdd:PRK07529 419 VLCIAGPNVfsGYLeaahnKGLWLED-GWLNT-----------GDLGRIDADGYFwLTGRAKDLIIRGGHNIDPAAIEEA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 535 LVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIG-KALCPKDIHVVEDLPKTRNSKV---- 609
Cdd:PRK07529 487 LLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEA---ELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIfkpa 563
|
570
....*....|...
gi 446729151 610 -----MRRVIKAA 617
Cdd:PRK07529 564 lrrdaIRRVLRAA 576
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-613 |
9.80e-45 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 165.43 E-value: 9.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQaagskmiitad 194
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 gfsRRGKVVSLKDEVdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeeMHSDDPLMLIYTSGTTGKP 274
Cdd:cd05974 70 ---RGGAVYAAVDEN----------------------------------------------THADDPMLLYFTSGTTSKP 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 275 KGTVHTHAGFPLkAAFDAGFGMNIKQGDRVLWVTDMGWMMGPF-LLFGSLINGATMVMYEgVPDFpEADRLWETVDKYEI 353
Cdd:cd05974 101 KLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWsCFFAPWNAGATVFLFN-YARF-DAKRVLAALVRYGV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 354 THLGISPTLIRALMakgDEYVNKHSLKSLEVFAStGEPWNPDpwmwLFETVGKS-NVPICNYSGGTEISGGIfGNVLIKP 432
Cdd:cd05974 178 TTLCAPPTVWRMLI---QQDLASFDVKLREVVGA-GEPLNPE----VIEQVRRAwGLTIRDGYGQTETTALV-GNSPGQP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 433 IAPISFNASLPGMAAVVLDDQGNPIRDevGELCLE----KPwVGMTKSFWEDDERyvnTYWSRFENKWVHGDWVVYDGEQ 508
Cdd:cd05974 249 VKAGSMGRPLPGYRVALLDPDGAPATE--GEVALDlgdtRP-VGLMKGYAGDPDK---TAHAMRGGYYRTGDIAMRDEDG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 509 YII-TGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMslvnSHIG 587
Cdd:cd05974 323 YLTyVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIF----RFSR 398
|
490 500
....*....|....*....|....*....
gi 446729151 588 KALCP-KDIHVVE--DLPKTRNSKVmRRV 613
Cdd:cd05974 399 ERLAPyKRIRRLEfaELPKTISGKI-RRV 426
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
101-618 |
1.72e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 166.65 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK08316 28 TALVFGDR-----SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIITADGFSRRgkvvsLKDEVDKACEHCPTVEKVVIVRHAGNDFTPHNydfSWstLEKEKPFVHAEEMHSDD 260
Cdd:PRK08316 103 ILDHSGARAFLVDPALAPT-----AEAALALLPVDTLILSLVLGGREAPGGWLDFA---DW--AEAGSVAEPDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 261 PLMLIYTSGTTGKPKGTVHTHAGFP---LKAAFDAGfgmnIKQGDRVLWV------TDMGWMMGPFLLFGslingATMVM 331
Cdd:PRK08316 173 LAQILYTSGTESLPKGAMLTHRALIaeyVSCIVAGD----MSADDIPLHAlplyhcAQLDVFLGPYLYVG-----ATNVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 332 YEGvpdfPEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSL------------EVFASTGEPWnPDPWMW 399
Cdd:PRK08316 244 LDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLrkgyygasimpvEVLKELRERL-PGLRFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 400 lfetvgksnvpicNYSGGTEIsgGIFGNVLiKP----IAPISfnASLPG--MAAVVLDDQGNPI-RDEVGELCLEKPWVg 472
Cdd:PRK08316 317 -------------NCYGQTEI--APLATVL-GPeehlRRPGS--AGRPVlnVETRVVDDDGNDVaPGEVGEIVHRSPQL- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 473 MTkSFWEDDERYVNTywsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVP 550
Cdd:PRK08316 378 ML-GYWDDPEKTAEA----FRGGWFHsGDLGVMDEEGYItVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 551 DDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAY 618
Cdd:PRK08316 453 DPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERY 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
115-615 |
4.39e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 163.23 E-value: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITad 194
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 gfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhsdDPLMLIYTSGTTGKP 274
Cdd:cd05934 82 -----------------------------------------------------------------DPASILYTSGTTGPP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 275 KGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWV--------TDMGWMmgpfllfGSLINGATMVMyegVPDFpEADRLWE 346
Cdd:cd05934 97 KGVVITHANL-TFAGYYSARRFGLGEDDVYLTVlplfhinaQAVSVL-------AALSVGATLVL---LPRF-SASRFWS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 347 TVDKYEITHLGISPTLIRALMAKGD-EYVNKHSLKslEVFAStgePWNPDPWMWLFETVGksnVPICNYSGGTEISGGIF 425
Cdd:cd05934 165 DVRRYGATVTNYLGAMLSYLLAQPPsPDDRAHRLR--AAYGA---PNPPELHEEFEERFG---VRLLEGYGMTETIVGVI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 426 GNVlIKPIAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCL--EKPWvGMTKSFWEDDERYVntywSRFENKWVH-GDW 501
Cdd:cd05934 237 GPR-DEPRRPGSIGRPAPGYEVRIVDDDGQELPAgEPGELVIrgLRGW-GFFKGYYNMPEATA----EAMRNGWFHtGDL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 502 VVYDGEQYII-TGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMS 580
Cdd:cd05934 311 GYRDADGFFYfVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFA 387
|
490 500 510
....*....|....*....|....*....|....*
gi 446729151 581 LVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05934 388 FCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
111-611 |
5.44e-44 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 165.01 E-value: 5.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 111 TSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGaiISPIfsgfasdAVMTRVQAAGSKMI 190
Cdd:TIGR02262 27 DISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAG--IVPV-------ALNTLLTADDYAYM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 191 ITadgfSRRGKVVSLKDE----VDKACEHCPTVEKVVIVrhagNDFTPHNYDFSwSTLEKEKPFVHAEEMHSDDPLMLIY 266
Cdd:TIGR02262 98 LE----DSRARVVFVSGAllpvIKAALGKSPHLEHRVVV----GRPEAGEVQLA-ELLATESEQFKPAATQADDPAFWLY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 267 TSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDM--GWMMGPFLLFGSLInGATMVMYegvPDFPEADRL 344
Cdd:TIGR02262 169 SSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLffAYGLGNALTFPMSV-GATTVLM---GERPTPDAV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 345 WETVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFASTGEPwnpdpwmwLFETVGKS-----NVPICNYSGGTE 419
Cdd:TIGR02262 245 FDRLRRHQPTIFYGVPTLYAAMLA--DPNLPSEDQVRLRLCTSAGEA--------LPAEVGQRwqarfGVDIVDGIGSTE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 420 IsGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPWVGmtKSFWEDDERYVNTY---WSRFENK 495
Cdd:TIGR02262 315 M-LHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADgEPGELLISGPSSA--TMYWNNRAKSRDTFqgeWTRSGDK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 496 WVHGDwvvyDGeQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNvtfSGELK 575
Cdd:TIGR02262 392 YVRND----DG-SYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPG---QTALE 463
|
490 500 510
....*....|....*....|....*....|....*.
gi 446729151 576 KELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:TIGR02262 464 TELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
96-612 |
8.60e-40 |
|
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: 151.63 E-value: 8.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 96 ETRTQPALQYEGengtsKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFAS 175
Cdd:cd05945 3 ANPDRPAVVEGG-----RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 176 DAVMTRVQAAGSKMIITADgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaee 255
Cdd:cd05945 78 ERIREILDAAKPALLIADG------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 256 mhsDDPLMLIYTSGTTGKPKGTVHTHAGFplkAAF----DAGFgmNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVM 331
Cdd:cd05945 97 ---DDNAYIIFTSGSTGRPKGVQISHDNL---VSFtnwmLSDF--PLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 332 yegVPDFPEAD--RLWETVDKYEITHLGISPTLIRalMAKGDEYVNKHSLKSLEVFASTGEPWnPDP----WMWLFetvg 405
Cdd:cd05945 169 ---VPRDATADpkQLFRFLAEHGITVWVSTPSFAA--MCLLSPTFTPESLPSLRHFLFCGEVL-PHKtaraLQQRF---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 406 kSNVPICNYSGGTEISGGIFGNVLIKPIA------PISFnaSLPGMAAVVLDDQGNPIRD-EVGELCLEKPWVgmTKSFW 478
Cdd:cd05945 239 -PDARIYNTYGPTEATVAVTYIEVTPEVLdgydrlPIGY--AKPGAKLVILDEDGRPVPPgEKGELVISGPSV--SKGYL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 479 EDDERyVNTYWSRFENKWVH--GDWVVYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKG 555
Cdd:cd05945 314 NNPEK-TAAAFFPDEGQRAYrtGDLVRLEADgLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446729151 556 EVCHCFVVLRDNVTFSG--ELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd05945 393 TELIAFVVPKPGAEAGLtkAIKAELAERLPPY----MIPRRFVYLDELPLNANGKIDRK 447
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
95-612 |
1.47e-39 |
|
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: 152.11 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 95 DETRTQPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFA 174
Cdd:cd17651 6 ARTPDAPALVAEGR-----RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 175 SDAVMTRVQAAGSKMIITADGFSRRGkvvslkdevdkacehcpTVEKVVIVRHAgndftphnyDFSWSTLEKEKPFVhae 254
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGEL-----------------AVELVAVTLLD---------QPGAAAGADAEPDP--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 255 EMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyeg 334
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARA-SSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVL--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 335 VPD--FPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSlkSLEVFASTGEPWNPDPWMWLFeTVGKSNVPIC 412
Cdd:cd17651 208 PPEevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLA--ALRYLLTGGEQLVLTEDLREF-CAGLPGLRLH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 413 NYSGGTE---ISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPI-RDEVGELC----------LEKPwvGMTKsfw 478
Cdd:cd17651 285 NHYGPTEthvVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVpPGVPGELYiggaglargyLNRP--ELTA--- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 479 eddERYVNTYWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKG 555
Cdd:cd17651 360 ---ERFVPDPFVPGARMYRTGDLARWlpDGElEFL--GRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGE 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 556 EVCHCFVVLR-DNVTFSGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17651 435 KRLVAYVVGDpEAPVDAAELRAALATHLPEY----MVPSAFVLLDALPLTPNGKLDRR 488
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
87-614 |
1.86e-39 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation 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. The 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. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 152.01 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 87 VLSRWLADDETRTqpalqyegengtsksfTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAII 166
Cdd:cd12119 14 IVSRTHEGEVHRY----------------TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 167 SPIFSGFASDAVMTRVQAAGSKMIITADGFSRRgkvvslkdeVDKACEHCPTVEKVVIV---RHAGNDFTPHNYDFsWST 243
Cdd:cd12119 78 HTINPRLFPEQIAYIINHAEDRVVFVDRDFLPL---------LEAIAPRLPTVEHVVVMtddAAMPEPAGVGVLAY-EEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 244 LEKEKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKA----AFDagfGMNIKQGDRVLWVTDM----GWMMg 315
Cdd:cd12119 148 LAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAmaalLTD---GLGLSESDVVLPVVPMfhvnAWGL- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 316 PFLLFGSlinGATMVMyegvPD-FPEADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNP 394
Cdd:cd12119 224 PYAAAMV---GAKLVL----PGpYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVVIGGSAVPR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 395 DpwmwLFETVGKSNVPICNYSGGTEISG-GIFG---------------NVLIKPIAPIsfnaslPGMAAVVLDDQGNPI- 457
Cdd:cd12119 295 S----LIEAFEERGVRVIHAWGMTETSPlGTVArppsehsnlsedeqlALRAKQGRPV------PGVELRIVDDDGRELp 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 458 RD--EVGELCLEKPWVgmTKSFWEDDERYVNTywsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYES 533
Cdd:cd12119 365 WDgkAVGELQVRGPWV--TKSYYKNDEESEAL----TEDGWLRtGDVATIDEDGYLtITDRSKDVIKSGGEWISSVELEN 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 534 ILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRV 613
Cdd:cd12119 439 AIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVT---AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKA 515
|
.
gi 446729151 614 I 614
Cdd:cd12119 516 L 516
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
101-612 |
1.87e-39 |
|
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: 151.29 E-value: 1.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd12116 4 TAVRDDDR-----SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIITADgfsrrgkvvslkDEVDKACEHCPTVEKVVIVRHAGndftphnydfswstlekekPFVHAEEMHSDD 260
Cdd:cd12116 79 ILEDAEPALVLTDD------------ALPDRLPAGLPVLLLALAAAAAA-------------------PAAPRTPVSPDD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 261 PLMLIYTSGTTGKPKGTVHTHAGFplkAAFDAGFG--MNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGvPDF 338
Cdd:cd12116 128 LAYVIYTSGSTGRPKGVVVSHRNL---VNFLHSMRerLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPR-ETQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 339 PEADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLevfaSTGEPWNPDPWMWLFETVGKsnvpICNYSGGT 418
Cdd:cd12116 204 RDPEALARLIEAHSITVMQATPATWRMLLDAGWQ--GRAGLTAL----CGGEALPPDLAARLLSRVGS----LWNLYGPT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 419 EISggIFGNV--LIKPIAPISFNASLPGMAAVVLDDQGNPI-RDEVGELCLEKPwvGMTKSFWED----DERYV-NTYWS 490
Cdd:cd12116 274 ETT--IWSTAarVTAAAGPIPIGRPLANTQVYVLDAALRPVpPGVPGELYIGGD--GVAQGYLGRpaltAERFVpDPFAG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 491 RFENKWVHGDWVVYDGE---QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVChCFVVLRDN 567
Cdd:cd12116 350 PGSRLYRTGDLVRRRADgrlEYL--GRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAG 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446729151 568 VTFS-GELKKELmslvNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd12116 427 AAPDaAALRAHL----RATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
70-618 |
3.77e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 151.29 E-value: 3.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 70 TPFAQWYNGGT-CNVVESVLSRWladdetRTQPALqYEGEngtsKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPM 148
Cdd:PRK06188 3 TMADLLHSGATyGHLLVSALKRY------PDRPAL-VLGD----TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 149 IPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADG-FSRRGKVVSlkdevdkacEHCPTVEKVVIVRH 227
Cdd:PRK06188 72 RPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPApFVERALALL---------ARVPSLKHVLTLGP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 228 A--GNDFtphnydfsWSTLEKE--KPFVHAEEmhSDDPLMLIYTSGTTGKPKGTVHTH---AGFP--LKAAFDagfgmnI 298
Cdd:PRK06188 143 VpdGVDL--------LAAAAKFgpAPLVAAAL--PPDIAGLAYTGGTTGKPKGVMGTHrsiATMAqiQLAEWE------W 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 299 KQGDRVLWVTDMGWMMGPFLLfGSLINGATMVMYEGvpdFpEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHS 378
Cdd:PRK06188 207 PADPRFLMCTPLSHAGGAFFL-PTLLRGGTVIVLAK---F-DPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 379 LKSLEVFASTGEPWNPDPWMWLFETVGksnvPI-CNYSGGTEISGGIfgNVLIK----PIAPISFnAS----LPGMAAVV 449
Cdd:PRK06188 280 LSSLETVYYGASPMSPVRLAEAIERFG----PIfAQYYGQTEAPMVI--TYLRKrdhdPDDPKRL-TScgrpTPGLRVAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 450 LDDQGNPI-RDEVGELCLEKPWVgmtksfwedderyVNTYWSR-------FENKWVH-GDWVVYDGEQYI-ITGRSDDTL 519
Cdd:PRK06188 353 LDEDGREVaQGEVGEICVRGPLV-------------MDGYWNRpeetaeaFRDGWLHtGDVAREDEDGFYyIVDRKKDMI 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 520 NIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVE 599
Cdd:PRK06188 420 VTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA---ELQAHVKERKGSVHAPKQVDFVD 496
|
570
....*....|....*....
gi 446729151 600 DLPKTRNSKVMRRVIKAAY 618
Cdd:PRK06188 497 SLPLTALGKPDKKALRARY 515
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
92-616 |
2.23e-38 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 149.16 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 92 LADDETRTQPALQYEGengtsKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFS 171
Cdd:TIGR03098 8 DAAARLPDATALVHHD-----RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 172 GFASDAVMTRVQAAGSKMIITADgfsrrgkvvSLKDEVDKACEHCPTVEKVVIV--RHAGNDFTPHNYDFSWSTLEKEKP 249
Cdd:TIGR03098 83 LLKAEQVAHILADCNVRLLVTSS---------ERLDLLHPALPGCHDLRTLIIVgdPAHASEGHPGEEPASWPKLLALGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 250 FVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATM 329
Cdd:TIGR03098 154 ADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATY-LENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 330 VMYegvpDFPEADRLWETVDKYEITHLGISPTLIrALMAKGDeyVNKHSLKSLEVFASTGEPWNPDPWMWLFETVgkSNV 409
Cdd:TIGR03098 233 VLH----DYLLPRDVLKALEKHGITGLAAVPPLW-AQLAQLD--WPESAAPSLRYLTNSGGAMPRATLSRLRSFL--PNA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 410 PICNYSGGTEisggIFGNVLIKPIA----PISFNASLPGMAAVVLDDQGN---PirDEVGELCLEKPWVgmTKSFWEDDE 482
Cdd:TIGR03098 304 RLFLMYGLTE----AFRSTYLPPEEvdrrPDSIGKAIPNAEVLVLREDGSecaP--GEEGELVHRGALV--AMGYWNDPE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 483 RYVNTY--WSRFENKWVHGDWVVY---------DGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPD 551
Cdd:TIGR03098 376 KTAERFrpLPPFPGELHLPELAVWsgdtvrrdeEGFLYFV-GRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPD 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446729151 552 DVKGEVCHCFVVLRDNVTFSgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:TIGR03098 455 PTLGQAIVLVVTPPGGEELD---RAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
114-617 |
2.25e-38 |
|
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: 149.14 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIisPIFSGFAS-----DAVMTRVQAAGsk 188
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFALPAHrraeiSHFAEQSEAVA-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 189 mIITAD---GFSRRGKVVSLKDEvdkacehCPTVEKVVIVRHAGnDFTphnydfSWSTLEKEKPFVHAEEMHSDDPLMLI 265
Cdd:COG1021 126 -YIIPDrhrGFDYRALARELQAE-------VPSLRHVLVVGDAG-EFT------SLDALLAAPADLSEPRPDPDDVAFFQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 266 YTSGTTGKPKGTVHTHA--GFPLKAAFDAgfgMNIKQGDRVLWVTDMG--WMMGPFLLFGSLINGATMVMyegVPDfPEA 341
Cdd:COG1021 191 LSGGTTGLPKLIPRTHDdyLYSVRASAEI---CGLDADTVYLAALPAAhnFPLSSPGVLGVLYAGGTVVL---APD-PSP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 342 DRLWETVDKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPWNP--------------------------- 394
Cdd:COG1021 264 DTAFPLIERERVTVTALVPPLALLWLDAAERS--RYDLSSLRVLQVGGAKLSPelarrvrpalgctlqqvfgmaeglvny 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 395 ----DPWMWLFETVGKsnvPICNYSggtEISggifgnvlikpiapisfnaslpgmaavVLDDQGNPIRD-EVGELCLEKP 469
Cdd:COG1021 342 trldDPEEVILTTQGR---PISPDD---EVR---------------------------IVDEDGNPVPPgEVGELLTRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 470 WvgmT------------KSFweDDERYvntYWSrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILV 536
Cdd:COG1021 389 Y---TirgyyrapehnaRAF--TPDGF---YRT--------GDLVRRTPDGYLvVEGRAKDQINRGGEKIAAEEVENLLL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 537 KHNDVIEAAAIGVPDDVKGEVCHCFVVLRD-NVTFSgELKKELMSLvnsHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:COG1021 453 AHPAVHDAAVVAMPDEYLGERSCAFVVPRGePLTLA-ELRRFLRER---GLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
..
gi 446729151 616 AA 617
Cdd:COG1021 529 AA 530
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
96-612 |
3.87e-38 |
|
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: 147.73 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 96 ETRTQPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFAS 175
Cdd:cd12117 9 RTPDAVAVVYGDR-----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 176 DAVMTRVQAAGSKMIITADGFSRRGKVVSLKDEVDKACEHCPTVEKVVIVrhagndftphnydfswstlekekpfvhaee 255
Cdd:cd12117 84 ERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPV------------------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 256 mHSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgv 335
Cdd:cd12117 134 -SPDDLAYVMYTSGSTGRPKGVAVTHRGV-VRLVKNTNY-VTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAP-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 336 PDFPE-ADRLWETVDKYEITHLGISPTLIRALMakgDEYVNkhSLKSLEVFASTGEPWNPdPWMwlfETVGKSNVP--IC 412
Cdd:cd12117 209 KGTLLdPDALGALIAEEGVTVLWLTAALFNQLA---DEDPE--CFAGLRELLTGGEVVSP-PHV---RRVLAACPGlrLV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 413 NYSGGTE---------ISGGIF--GNVLI-KPIApisfnaslpGMAAVVLDDQGNPIR-DEVGELCLEKPwvGMTKSFWE 479
Cdd:cd12117 280 NGYGPTEnttfttshvVTELDEvaGSIPIgRPIA---------NTRVYVLDEDGRPVPpGVPGELYVGGD--GLALGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 480 D----DERYVNTYWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDD 552
Cdd:cd12117 349 RpaltAERFVADPFGPGERLYRTGDLARWlpDGRlEFL--GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDA 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446729151 553 -VKGEVChCFVVLRDNVTfSGELKKelmslvnsHIGKAL----CPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd12117 427 gGDKRLV-AYVVAEGALD-AAELRA--------FLRERLpaymVPAAFVVLDELPLTANGKVDRR 481
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
100-551 |
9.44e-38 |
|
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: 150.78 E-value: 9.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 100 QPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD--A 177
Cdd:COG1020 492 AVAVVFGDQ-----SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAErlA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 178 VMtrVQAAGSKMIITADGFSRR-----GKVVSLkDEVDkacehcptvekvvivrhagndftphnydfsWSTLEKEKPFVH 252
Cdd:COG1020 567 YM--LEDAGARLVLTQSALAARlpelgVPVLAL-DALA------------------------------LAAEPATNPPVP 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 253 AeemHSDDPLMLIYTSGTTGKPKGTVHTHAGFP-LKAAFDAGFGMNikQGDRVLWVTDMGWMMGPFLLFGSLINGATMVM 331
Cdd:COG1020 614 V---TPDDLAYVIYTSGSTGRPKGVMVEHRALVnLLAWMQRRYGLG--PGDRVLQFASLSFDASVWEIFGALLSGATLVL 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 332 Y--EGVPDfpeADRLWETVDKYEITHLGISPTLIRALMAKGDEyvnkhSLKSLEVFASTGEPWNPDPWMWLFETVGksNV 409
Cdd:COG1020 689 AppEARRD---PAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRWRARLP--GA 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 410 PICN-YsGGTEISggIFgnVLIKPIAPISFNAS-------LPGMAAVVLDDQGNPIRDEV-GELC----------LEKPw 470
Cdd:COG1020 759 RLVNlY-GPTETT--VD--STYYEVTPPDADGGsvpigrpIANTRVYVLDAHLQPVPVGVpGELYiggaglargyLNRP- 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 471 vGMTKS------FWEDDERYVNTywsrfenkwvhGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDV 541
Cdd:COG1020 833 -ELTAErfvadpFGFPGARLYRT-----------GDLARWlpDGNlEFL--GRADDQVKIRGFRIELGEIEAALLQHPGV 898
|
490
....*....|
gi 446729151 542 IEAAAIGVPD 551
Cdd:COG1020 899 REAVVVARED 908
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
102-615 |
1.17e-36 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 144.05 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 102 ALQYEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTR 181
Cdd:PRK08008 25 ALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 182 VQAAGSKMIITADGFSrrGKVVSLKDEVDKACEHcptvekVVIVRHAGNDFTP-HNYDfswsTLEKEKP--FVHAEEMHS 258
Cdd:PRK08008 105 LQNSQASLLVTSAQFY--PMYRQIQQEDATPLRH------ICLTRVALPADDGvSSFT----QLKAQQPatLCYAPPLST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 259 DDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLwvtdmgWMMGPF-------LLFGSLINGATMVM 331
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNL-RFAGYYSAWQCALRDDDVYL------TVMPAFhidcqctAAMAAFSAGATFVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 332 YEGVpdfpEADRLWETVDKYEITHLGISPTLIRALM---AKGDEyvNKHSLKSLEVFASTGEPWNPDpwmwlFETvgKSN 408
Cdd:PRK08008 246 LEKY----SARAFWGQVCKYRATITECIPMMIRTLMvqpPSAND--RQHCLREVMFYLNLSDQEKDA-----FEE--RFG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 409 VPICNYSGGTEISGGIFGNvliKPIAPISF-NASLPGMA--AVVLDDQGNPI-RDEVGELCLeKPWVGMT--KSFWEDDE 482
Cdd:PRK08008 313 VRLLTSYGMTETIVGIIGD---RPGDKRRWpSIGRPGFCyeAEIRDDHNRPLpAGEIGEICI-KGVPGKTifKEYYLDPK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 483 RYVNTYwsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHC 560
Cdd:PRK08008 389 ATAKVL---EADGWLHtGDTGYVDEEGFFyFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446729151 561 FVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK08008 466 FVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
115-615 |
1.27e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 144.53 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD 194
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 GFsRRGKVVSLKDEVDK----------ACEHCPTVEKVviVRHAGNDfTPHNydFSWSTLEKEKPFVHAEE-------MH 257
Cdd:PRK12583 126 AF-KTSDYHAMLQELLPglaegqpgalACERLPELRGV--VSLAPAP-PPGF--LAWHELQARGETVSREAlaerqasLD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 258 SDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFdAGFGMNIKQGDRVLWVTDMGWMMGPFLL-FGSLINGATMVMyegvP 336
Cdd:PRK12583 200 RDDPINIQYTSGTTGFPKGATLSHHNILNNGYF-VAESLGLTEHDRLCVPVPLYHCFGMVLAnLGCMTVGACLVY----P 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 337 -DFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSNVPICnYs 415
Cdd:PRK12583 275 nEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQR--GNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIA-Y- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 416 GGTEISGGIFGNVLIKPIAP--ISFNASLPGMAAVVLDDQGNPI-RDEVGELCLEKPWVgmTKSFWEDDERyvnTYWSRF 492
Cdd:PRK12583 351 GMTETSPVSLQTTAADDLERrvETVGRTQPHLEVKVVDPDGATVpRGEIGELCTRGYSV--MKGYWNNPEA---TAESID 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 493 ENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTF 570
Cdd:PRK12583 426 EDGWMHtGDLATMDEQGYVrIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAA 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446729151 571 SGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK12583 506 SEE---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-611 |
3.48e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 142.96 E-value: 3.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:PRK06087 49 SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 DGFSRRG---KVVSLKDEVdkacehcPTVEKVVIVRHAGndftPHNYDFSWS-TLEKEKPFVHAEEMHSDDPLMLIYTSG 269
Cdd:PRK06087 129 TLFKQTRpvdLILPLQNQL-------PQLQQIVGVDKLA----PATSSLSLSqIIADYEPLTTAITTHGDELAAVLFTSG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 270 TTGKPKGTVHTHAGFPL-KAAFDAGFGMNikqgdrvlWvTDMGWMMGP------FL--LFGSLINGATMVMYEgvpDFpE 340
Cdd:PRK06087 198 TEGLPKGVMLTHNNILAsERAYCARLNLT--------W-QDVFMMPAPlghatgFLhgVTAPFLIGARSVLLD---IF-T 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 341 ADRLWETVDKYEIT-HLGISPtLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDpwmwLFETVGKSNVPICNYSGGTE 419
Cdd:PRK06087 265 PDACLALLEQQRCTcMLGATP-FIYDLLNLLEK--QPADLSALRFFLCGGTTIPKK----VARECQQRGIKLLSVYGSTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 420 ISGGIFgnvlIKPIAPISFNASLPGMAAV-----VLDDQGNPI-RDEVGELCLEKPWVGMtkSFWEDDERyvnTYWSRFE 493
Cdd:PRK06087 338 SSPHAV----VNLDDPLSRFMHTDGYAAAgveikVVDEARKTLpPGCEGEEASRGPNVFM--GYLDEPEL---TARALDE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 494 NKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTfS 571
Cdd:PRK06087 409 EGWYYsGDLCRMDEAGYIkITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHH-S 487
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446729151 572 GELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PRK06087 488 LTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQK 527
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
101-609 |
1.14e-35 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 141.73 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PAL-QYEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:PRK13295 41 TAVtAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 180 TRVQAAGSKMII---TADGFSRRGKVVSLKDEVdkacehcPTVEKVVIVRHAG-NDFTPHNYDFSWSTLEKEKPFVHAEE 255
Cdd:PRK13295 121 FMLKHAESKVLVvpkTFRGFDHAAMARRLRPEL-------PALRHVVVVGGDGaDSFEALLITPAWEQEPDAPAILARLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 256 MHSDDPLMLIYTSGTTGKPKGTVHTH-----AGFPLKAAFDAGfgmnikQGDRVLWVTDM----GWMMG---PFLLfgsl 323
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTAntlmaNIVPYAERLGLG------ADDVILMASPMahqtGFMYGlmmPVML---- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 324 inGATMVMYegvpDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFET 403
Cdd:PRK13295 264 --GATAVLQ----DIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKE--SGRPVSSLRTFLCAGAPIPGALVERARAA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 404 VGKSnvpICNYSGGTE---ISGGIFGNVLIKPIAPISFnaSLPGMAAVVLDDQGNPI-RDEVGEL----C------LEKP 469
Cdd:PRK13295 336 LGAK---IVSAWGMTEngaVTLTKLDDPDERASTTDGC--PLPGVEVRVVDADGAPLpAGQIGRLqvrgCsnfggyLKRP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 470 -WVGMtksfweDDERYVNTywsrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAI 547
Cdd:PRK13295 411 qLNGT------DADGWFDT-----------GDLARIDADGYIrISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIV 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729151 548 GVPDDVKGEVCHCFVVLRDNVTFSGELKKELmsLVNSHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:PRK13295 474 AYPDERLGERACAFVVPRPGQSLDFEEMVEF--LKAQKVAKQYIPERLVVRDALPRTPSGKI 533
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
113-626 |
3.50e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 139.79 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIT 192
Cdd:PRK07470 31 RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 193 ADGFSrrgkvvslkDEVDKACEHCPTVEKVVIVrhAGNDFTPhnydfSWSTLEKEkpfvHAEEMHS------DDPLMLIY 266
Cdd:PRK07470 111 HADFP---------EHAAAVRAASPDLTHVVAI--GGARAGL-----DYEALVAR----HLGARVAnaavdhDDPCWFFF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 267 TSGTTGKPKGTVHTHAgfplKAAF-------DAGFGMNikQGDRVLWVTDMGWMMGPFLLFgSLINGATMVMYEGVP-DF 338
Cdd:PRK07470 171 TSGTTGRPKAAVLTHG----QMAFvitnhlaDLMPGTT--EQDASLVVAPLSHGAGIHQLC-QVARGAATVLLPSERfDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 339 PEAdrlWETVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFASTGEP-WNPDPWMWLfETVGKSNVpicNYSGG 417
Cdd:PRK07470 244 AEV---WALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSLRYVIYAGAPmYRADQKRAL-AKLGKVLV---QYFGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 418 TEISGGIfgNVLikpiaPISFNASLP--------------GMAAVVLDDQGNPIR-DEVGELCLEKPWVGMtkSFWEDDE 482
Cdd:PRK07470 315 GEVTGNI--TVL-----PPALHDAEDgpdarigtcgfertGMEVQIQDDEGRELPpGETGEICVIGPAVFA--GYYNNPE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 483 ryVNTywSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHC 560
Cdd:PRK07470 386 --ANA--KAFRDGWFRtGDLGHLDARGFLyITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 561 FVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDL 626
Cdd:PRK07470 462 VCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEERGLLDL 524
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
114-611 |
5.70e-35 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 137.51 E-value: 5.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 DGFSRRgkvvslkdevdkacehcptvekvvivRHAgndftphnydfswstlekEKPfvhaeemhsDDPLMLIYTSGTTGK 273
Cdd:cd05903 81 ERFRQF--------------------------DPA------------------AMP---------DAVALLLFTSGTTGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 274 PKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGpfllfgsLINGATMVMYEGVP----DFPEADRLWETVD 349
Cdd:cd05903 108 PKGVMHSHNTL-SASIRQYAERLGLGPGDVFLVASPMAHQTG-------FVYGFTLPLLLGAPvvlqDIWDPDKALALMR 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 350 KYEITHLGISPT----LIRALMAKGDEyvnkhsLKSLEVFASTGEPWNPDPWMWLFETVGKSnvpICNYSGGTEISGGIf 425
Cdd:cd05903 180 EHGVTFMMGATPfltdLLNAVEEAGEP------LSRLRTFVCGGATVPRSLARRAAELLGAK---VCSAYGSTECPGAV- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 426 gnVLIKPIAPISFNAS----LPGMAAVVLDDQGNPI-RDEVGELCLEKPWV--GMTK----SFWEDDERYVNTywsrfen 494
Cdd:cd05903 250 --TSITPAPEDRRLYTdgrpLPGVEIKVVDDTGATLaPGVEGELLSRGPSVflGYLDrpdlTADAAPEGWFRT------- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 495 kwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGE 573
Cdd:cd05903 321 ----GDLARLDEDGYLrITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFD 396
|
490 500 510
....*....|....*....|....*....|....*...
gi 446729151 574 LKKELMSLVNshIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd05903 397 ELVAYLDRQG--VAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
56-614 |
5.80e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 139.78 E-value: 5.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 56 WMKPYTEVLdlengtPFAQWYNGGTCNV-VESVLSRWladdetRTQPALQYEGengtsKSFTYEELDSWVSRVANGLKHA 134
Cdd:PRK06710 7 WLKSYPEEI------PSTISYDIQPLHKyVEQMASRY------PEKKALHFLG-----KDITFSVFHDKVKRFANYLQKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 135 GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD-GFSRRGKVVSlkdevdkac 213
Cdd:PRK06710 70 GVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDlVFPRVTNVQS--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 214 ehCPTVEKVVIVRHAgnDFTPHN----YDFS-------------------WSTLEKEKPfvHAEEMHSD---DPLMLIYT 267
Cdd:PRK06710 141 --ATKIEHVIVTRIA--DFLPFPknllYPFVqkkqsnlvvkvsesetihlWNSVEKEVN--TGVEVPCDpenDLALLQYT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 268 SGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLwvtdMGWMmgPFL-LFG-------SLINGATMVMyegVPDFp 339
Cdd:PRK06710 215 GGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVV----LGVL--PFFhVYGmtavmnlSIMQGYKMVL---IPKF- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 340 EADRLWETVDKYEITHLGISPTLIRALMakGDEYVNKHSLKSLEVFASTGEPWnPDPWMWLFETV--GKsnvpICNYSGG 417
Cdd:PRK06710 285 DMKMVFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPL-PVEVQEKFETVtgGK----LVEGYGL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 418 TEISGGIFGNVLIKPIAPISFNASLPGMAAVVLD-DQGNPIR-DEVGELCLEKPWVgmTKSFWEDDERYVntywSRFENK 495
Cdd:PRK06710 358 TESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPpGEIGEIVVKGPQI--MKGYWNKPEETA----AVLQDG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 496 WVHGDWVVYDGEQ--YIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGE 573
Cdd:PRK06710 432 WLHTGDVGYMDEDgfFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEE 511
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 446729151 574 lkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:PRK06710 512 ---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
114-614 |
7.05e-35 |
|
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: 137.23 E-value: 7.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIta 193
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 dgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfVHAEEmhsDDPLMLIYTSGTTGK 273
Cdd:cd05935 79 ---------------------------------------------------------VGSEL---DDLALIPYTSGTTGL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 274 PKGTVHTHAGFPLKAAFDAgFGMNIKQGDRVL------WVTDM-GWMMGPfllfgsLINGATMVMYEGVpdfpEADRLWE 346
Cdd:cd05935 99 PKGCMHTHFSAAANALQSA-VWTGLTPSDVILaclplfHVTGFvGSLNTA------VYVGGTYVLMARW----DRETALE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 347 TVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSNVPIcnySGGTEISGGIFG 426
Cdd:cd05935 168 LIEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEG---YGLTETMSQTHT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 427 NvliKPIAPISFNASLP--GMAAVVLD-DQGNPIRD-EVGELCLEKPWV---------GMTKSFWEDD-ERYVNTywsrf 492
Cdd:cd05935 243 N---PPLRPKLQCLGIP*fGVDARVIDiETGRELPPnEVGEIVVRGPQIfkgywnrpeETEESFIEIKgRRFFRT----- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 493 enkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNvtFS 571
Cdd:cd05935 315 ------GDLGYMDEEGYFfFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPE--YR 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729151 572 GELKKE-LMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:cd05935 387 GKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
110-611 |
2.74e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 136.91 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 110 GTSKSFTYEELDSWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 189 MIITADGFSrrGKVVSLKDEVdkacehcpTVEKVVIVRhagndftphnydfSWSTLEKEKPfVHAEEMHSDDPLMLIYTS 268
Cdd:PRK06839 103 VLFVEKTFQ--NMALSMQKVS--------YVQRVISIT-------------SLKEIEDRKI-DNFVEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 269 GTTGKPKGTVHTHAGFPLKAAFDAgFGMNIKQGDRVLWVTDMGWMMGPFLL-FGSLINGATMVmyegVPDFPEADRLWET 347
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNT-FAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVII----VPRKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 348 VDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWnPDPWMWLFETVGksnVPICNYSGGTEISGGIFgn 427
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPC-PEELMREFIDRG---FLFGQGFGMTETSPTVF-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 428 VLIKPIA---PISFNASLPGMAAVVLDDQGNPI-RDEVGELCLEKPWVgmTKSFWEDDERYVNTywsrFENKWVH-GDWV 502
Cdd:PRK06839 306 MLSEEDArrkVGSIGKPVLFCDYELIDENKNKVeVGEVGELLIRGPNV--MKEYWNRPDATEET----IQDGWLCtGDLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 503 VYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSgelKKELMSL 581
Cdd:PRK06839 380 RVDEDGFVyIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLI---EKDVIEH 456
|
490 500 510
....*....|....*....|....*....|
gi 446729151 582 VNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PRK06839 457 CRLFLAKYKIPKEIVFLKELPKNATGKIQK 486
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
101-612 |
4.25e-34 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. 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: 341304 [Multi-domain] Cd Length: 450 Bit Score: 135.57 E-value: 4.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd17649 4 VALVFGDQ-----SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIITADGfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhsDD 260
Cdd:cd17649 79 MLEDSGAGLLLTHHP---------------------------------------------------------------RQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 261 PLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyEGVPDFPE 340
Cdd:cd17649 96 LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVL-RPDELWAS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 341 ADRLWETVDKYEITHLGISPTLIRALMAKGDEyVNKHSLKSLEVFASTGEPWNPDPW-MWLfetvgKSNVPICNYSGGTE 419
Cdd:cd17649 174 ADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPELLrRWL-----KAPVRLFNAYGPTE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 420 --ISGGIF----GNVLIKPIAPISfnASLPGMAAVVLDDQGNPI-RDEVGEL-----CL-----EKPwvGMTKsfweddE 482
Cdd:cd17649 248 atVTPLVWkceaGAARAGASMPIG--RPLGGRSAYILDADLNPVpVGVTGELyiggeGLargylGRP--ELTA------E 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 483 RYVNTYWSRFENKWVH-GDWVVY--DGeQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCH 559
Cdd:cd17649 318 RFVPDPFGAPGSRLYRtGDLARWrdDG-VIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVA 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446729151 560 CfVVLRDNVTfSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17649 397 Y-VVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
100-618 |
5.39e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 136.45 E-value: 5.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 100 QPALQYEGengtsKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:PRK07786 33 APALRFLG-----NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 180 TRVQAAGSKMIITADGFSrrgKVVSLKDEVDkacehcPTVEKVVIVRHAGNDFTphnydFSWSTLEKEKPFVHAE-EMHS 258
Cdd:PRK07786 108 FLVSDCGAHVVVTEAALA---PVATAVRDIV------PLLSTVVVAGGSSDDSV-----LGYEDLLAEAGPAHAPvDIPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 259 DDPLMLIYTSGTTGKPKGTVHTHAGFplkaafdAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYeGVPD- 337
Cdd:PRK07786 174 DSPALIMYTSGTTGRPKGAVLTHANL-------TGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLL-GAPTv 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 338 -FP----EADRLWETVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKsLEVFASTGEPWNPDPWMWLFETVGKSNvpIC 412
Cdd:PRK07786 246 iYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVCA--EQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQ--IL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 413 NYSGGTEISG---GIFGNVLIKPIApiSFNASLPGMAAVVLDDQGNPI-RDEVGELCLEKPwvGMTKSFWEDDERYVNTy 488
Cdd:PRK07786 321 AAFGQTEMSPvtcMLLGEDAIRKLG--SVGKVIPTVAARVVDENMNDVpVGEVGEIVYRAP--TLMSGYWNNPEATAEA- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 489 wsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRD 566
Cdd:PRK07786 396 ---FAGGWFHsGDLVRQDEEGYVwVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446729151 567 NvtfSGELK-KELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAY 618
Cdd:PRK07786 473 D---DAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERY 522
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
101-612 |
3.24e-33 |
|
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: 133.55 E-value: 3.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd17646 15 PAVVDEGR-----TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIIT----ADGFSRRGKVVSLKDEVDKAceHCPTVEKVVIvrhagndftphnydfswstlekekpfvhaeem 256
Cdd:cd17646 90 MLADAGPAVVLTtadlAARLPAGGDVALLGDEALAA--PPATPPLVPP-------------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 257 HSDDPLMLIYTSGTTGKPKGTVHTHAGFP-----LKAAFDAGfgmnikQGDRVLWVTDMGWMMGPFLLFGSLINGATMVM 331
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMVTHAGIVnrllwMQDEYPLG------PGDRVLQKTPLSFDVSVWELFWPLVAGARLVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 332 YEgvpdfPEADR----LWETVDKYEITHLGISPTLIRALMAKGDeyvnKHSLKSLEVFASTGEPWNPDpwmwLFETVGK- 406
Cdd:cd17646 210 AR-----PGGHRdpayLAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPE----LAARFLAl 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 407 SNVPICNYSGGTEISGGI-----FGNVLIKPIaPISfnASLPGMAAVVLDDQGNPIRDEV-GELCLEKPWV--------G 472
Cdd:cd17646 277 PGAELHNLYGPTEAAIDVthwpvRGPAETPSV-PIG--RPVPNTRLYVLDDALRPVPVGVpGELYLGGVQLargylgrpA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 473 MTKsfweddERYVntywsrfENKWVHGDwVVY----------DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDV 541
Cdd:cd17646 354 LTA------ERFV-------PDPFGPGS-RMYrtgdlarwrpDGAlEFL--GRSDDQVKIRGFRVEPGEIEAALAAHPAV 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729151 542 IEAAAIGVPDDVKGEVCHCFVVLRDnvTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17646 418 THAVVVARAAPAGAARLVGYVVPAA--GAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRA 486
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
111-615 |
3.33e-33 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; 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: 341297 [Multi-domain] Cd Length: 532 Bit Score: 134.19 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 111 TSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 191 ITadgfSRRG--KVVSLKDEVdkacehcPTVEKVVIVrHAGNDFTPHNYDFSWSTLE-----KEKPFVHAEEMHSDDPLM 263
Cdd:cd17642 121 FC----SKKGlqKVLNVQKKL-------KIIKTIIIL-DSKEDYKGYQCLYTFITQNlppgfNEYDFKPPSFDRDEQVAL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 264 LIYTSGTTGKPKGTVHTHAGF--PLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyegVPDFPEA 341
Cdd:cd17642 189 IMNSSGSTGLPKGVQLTHKNIvaRFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVL---MYKFEEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 342 DRLwETVDKYEITHLGISPTLIrALMAKgDEYVNKHSLKSLEVFASTGEPWNPDpwmwLFETVGKS-NVP-ICNYSGGTE 419
Cdd:cd17642 266 LFL-RSLQDYKVQSALLVPTLF-AFFAK-STLVDKYDLSNLHEIASGGAPLSKE----VGEAVAKRfKLPgIRQGYGLTE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 420 ISGGIfgnvLIKP---IAPISFNASLPGMAAVVLD-DQGNPI-RDEVGELCLEKPwvGMTKSFWEDDEryvNTYWSRFEN 494
Cdd:cd17642 339 TTSAI----LITPegdDKPGAVGKVVPFFYAKVVDlDTGKTLgPNERGELCVKGP--MIMKGYVNNPE---ATKALIDKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 495 KWVH-GDWVVYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSg 572
Cdd:cd17642 410 GWLHsGDIAYYDEDgHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT- 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729151 573 elKKELMSLVNSHIGKALCPK-DIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd17642 489 --EKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
112-615 |
3.61e-33 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. 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: 341308 [Multi-domain] Cd Length: 433 Bit Score: 132.43 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 112 SKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:cd17653 20 GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 TADGfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhSDDPLMLIYTSGTT 271
Cdd:cd17653 100 TTDS--------------------------------------------------------------PDDLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 272 GKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgvPDFPeadrlWETVDKy 351
Cdd:cd17653 118 GIPKGVMVPHRGV-LNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD--PSDP-----FAHVAR- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 352 EITHLGISPTLIRALmaKGDEYVNkhslksLEVFASTGEPWNP---DPWmwlfetvgKSNVPICNYSGGTEISGGIFgNV 428
Cdd:cd17653 189 TVDALMSTPSILSTL--SPQDFPN------LKTIFLGGEAVPPsllDRW--------SPGRRLYNAYGPTECTISST-MT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 429 LIKPIAPISFNASLPGMAAVVLDDQGNPI-RDEVGELCLEKPwvGMTKSFWEDDERYVntywSRF-ENKWVHGdWVVY-- 504
Cdd:cd17653 252 ELLPGQPVTIGKPIPNSTCYILDADLQPVpEGVVGEICISGV--QVARGYLGNPALTA----SKFvPDPFWPG-SRMYrt 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 505 --------DGEQYIItGRSDDTLNIAGKRIG-PAEYESILVKHNDVIEAAAIGVPDDVkgevchCFVVLRDNVTFSGeLK 575
Cdd:cd17653 325 gdygrwteDGGLEFL-GREDNQVKVRGFRINlEEIEEVVLQSQPEVTQAAAIVVNGRL------VAFVTPETVDVDG-LR 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446729151 576 KELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd17653 397 SELAKHLPSY----AVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
108-616 |
4.25e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 133.90 E-value: 4.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 108 ENGTsksFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGS 187
Cdd:PRK07788 71 ERGT---LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 188 KMIITADGFSRRgkVVSLKDEVDKAcehcptvekVVIVRHAGNDFTPhnyDFSWSTLEKekpfvhAEEMHSDDPL----- 262
Cdd:PRK07788 148 KALVYDDEFTDL--LSALPPDLGRL---------RAWGGNPDDDEPS---GSTDETLDD------LIAGSSTAPLpkppk 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 263 ---MLIYTSGTTGKPKGTVHTHagfPLKAAFDAGFgmnikqGDRVLWVTDM----------GWMMGPFLLfgSLINGATM 329
Cdd:PRK07788 208 pggIVILTSGTTGTPKGAPRPE---PSPLAPLAGL------LSRVPFRAGEttllpapmfhATGWAHLTL--AMALGSTV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 330 VMYEgvpDF-PEAdrLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSn 408
Cdd:PRK07788 277 VLRR---RFdPEA--TLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 409 vpICNYSGGTEISggiFGNVlIKP----IAPISFNASLPGMAAVVLDDQGNPI-RDEVGELclekpWVGMTKSFweddER 483
Cdd:PRK07788 351 --LYNLYGSTEVA---FATI-ATPedlaEAPGTVGRPPKGVTVKILDENGNEVpRGVVGRI-----FVGNGFPF----EG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 484 YVNTYWSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCF 561
Cdd:PRK07788 416 YTDGRDKQIIDGLLSsGDVGYFDEDGLLfVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAF 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446729151 562 VVLRDNvtfSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK07788 496 VVKAPG---AALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
97-620 |
2.46e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 131.16 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 97 TRTQPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD 176
Cdd:PRK06145 15 TPDRAALVYRDQ-----EISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 177 AVMTRVQAAGSKMIITADGFsrrgkvvslkdEVDKACEHcptvEKVVIVRHAGNDFTphnydfswstlEKEKPFVHAEEM 256
Cdd:PRK06145 90 EVAYILGDAGAKLLLVDEEF-----------DAIVALET----PKIVIDAAAQADSR-----------RLAQGGLEIPPQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 257 HS---DDPLMLIYTSGTTGKPKGTVHTHAGFPLKAaFDAGFGMNIKQGDRVLWVtdmgwmmGPFLLFGSLINGATMVMYE 333
Cdd:PRK06145 144 AAvapTDLVRLMYTSGTTDRPKGVMHSYGNLHWKS-IDHVIALGLTASERLLVV-------GPLYHVGAFDLPGIAVLWV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 334 G-----VPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPwNPDPWMWLFETVGKSN 408
Cdd:PRK06145 216 GgtlriHREF-DPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGGGEK-TPESRIRDFTRVFTRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 409 VPICNYsGGTEISGGifgNVLI---KPIAPI-SFNASLPGMAAVVLDDQGNPIRDEV-GELCLEKPWVgmTKSFWEDDER 483
Cdd:PRK06145 292 RYIDAY-GLTETCSG---DTLMeagREIEKIgSTGRALAHVEIRIADGAGRWLPPNMkGEICMRGPKV--TKGYWKDPEK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 484 YVNTywsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCF 561
Cdd:PRK06145 366 TAEA----FYGDWFRsGDVGYLDEEGFLyLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAV 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446729151 562 VVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLG 620
Cdd:PRK06145 442 VVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
114-616 |
2.69e-32 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 129.39 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIfsgfasdavMTRVqaagskmiita 193
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLL---------NTRL----------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 dgfsrrgkvvslkdevdkacehcptvekvvivrhagndfTPHNYDFSWSTLEkekpfVHAEEMHSddplmLIYTSGTTGK 273
Cdd:cd05912 61 ---------------------------------------TPNELAFQLKDSD-----VKLDDIAT-----IMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 274 PKGTVHThAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgvpDFpEADRLWETVDKYEI 353
Cdd:cd05912 92 PKGVQQT-FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVD---KF-DAEQVLHLINSGKV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 354 THLGISPTLIRALMAKGDEYVNKHslksLEVFASTGEPWNPDpwmwLFETVGKSNVPICNYSGGTEISGGIFG-NVLIKP 432
Cdd:cd05912 167 TIISVVPTMLQRLLEILGEGYPNN----LRCILLGGGPAPKP----LLEQCKEKGIPVYQSYGMTETCSQIVTlSPEDAL 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 433 IAPISFNASLPGMAAVVLDDQGNPirDEVGELCLEKPWVgmTKSFWEDDERyvnTYWSrFENKWVH-GD--WVVYDGEQY 509
Cdd:cd05912 239 NKIGSAGKPLFPVELKIEDDGQPP--YEVGEILLKGPNV--TKGYLNRPDA---TEES-FENGWFKtGDigYLDEEGFLY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 510 IITGRSDdtLNIAG-KRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTfsgelKKELMSLVNSHIGK 588
Cdd:cd05912 311 VLDRRSD--LIISGgENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPIS-----EEELIAYCSEKLAK 383
|
490 500
....*....|....*....|....*...
gi 446729151 589 ALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05912 384 YKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
110-621 |
2.81e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 130.79 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 110 GTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 190 IITADGFSrrgkvvslkDEVDKACEHCPT-VEKVVIVRHAGNDFTPhnydfswstlekekpFVHAEEMHSDDPL------ 262
Cdd:PRK08276 87 LIVSAALA---------DTAAELAAELPAgVPLLLVVAGPVPGFRS---------------YEEALAAQPDTPIadetag 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 263 -MLIYTSGTTGKPKGT------VHTHAGfPLKAAFDAGFGMNIKQGDRVLwvtdmgwMMGPF-----LLFG--SLINGAT 328
Cdd:PRK08276 143 aDMLYSSGTTGRPKGIkrplpgLDPDEA-PGMMLALLGFGMYGGPDSVYL-------SPAPLyhtapLRFGmsALALGGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 329 MVMYEGvpdFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksn 408
Cdd:PRK08276 215 VVVMEK---F-DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWG--- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 409 vPICN-YSGGTEISGGIFGNV---LIKPiapisFNASLPGMAAV-VLDDQGNPI-RDEVGELCLEKPwvGMTKSFWEDDE 482
Cdd:PRK08276 288 -PIIHeYYASSEGGGVTVITSedwLAHP-----GSVGKAVLGEVrILDEDGNELpPGEIGTVYFEMD--GYPFEYHNDPE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 483 RyvnTYWSRFENKWVH-GD--WVVYDGEQYIiTGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCH 559
Cdd:PRK08276 360 K---TAAARNPHGWVTvGDvgYLDEDGYLYL-TDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVK 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729151 560 CFVVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGK 621
Cdd:PRK08276 436 AVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEG 497
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
97-616 |
5.21e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.54 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 97 TRTQPALQYeGEngtsKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD 176
Cdd:PRK12316 524 TPEAPALAF-GE----ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 177 AVMTRVQAAGSKMIITAdgfSRRGKVVSLKDEVDKACEHCPTvekvvivrhagndftphnydfSW-STLEKEKPFVHAee 255
Cdd:PRK12316 599 RLAYMLEDSGVQLLLSQ---SHLGRKLPLAAGVQVLDLDRPA---------------------AWlEGYSEENPGTEL-- 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 256 mHSDDPLMLIYTSGTTGKPKGTVHTHAGFP--LKAAFDAgFGMNIkqGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyE 333
Cdd:PRK12316 653 -NPENLAYVIYTSGSTGKPKGAGNRHRALSnrLCWMQQA-YGLGV--GDTVLQKTPFSFDVSVWEFFWPLMSGARLVV-A 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 334 GVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEyvnkHSLKSLEVFASTGEPWNPDPWMWLFETvgKSNVPICN 413
Cdd:PRK12316 728 APGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEALPADAQEQVFAK--LPQAGLYN 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 414 YSGGTEISGGIFGNVLIKPIA-PISFNASLPGMAAVVLDDQGNPIRDEV-GELCLEKpwVGMTKSFWE----DDERYVNT 487
Cdd:PRK12316 802 LYGPTEAAIDVTHWTCVEEGGdSVPIGRPIANLACYILDANLEPVPVGVlGELYLAG--RGLARGYHGrpglTAERFVPS 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 488 YWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGvpddVKGEVCHCFVVL 564
Cdd:PRK12316 880 PFVAGERMYRTGDLARYraDGViEYA--GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL 953
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446729151 565 RDNvtfSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK12316 954 ESE---GGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA 1002
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
115-616 |
5.44e-32 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation 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. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 129.73 E-value: 5.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIItad 194
Cdd:cd12118 30 YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 gfsrrgkvvslkdeVDKACEHcptvEKVVIvrhAGNDftphnyDFSWstlekEKPfvhAEEmhsDDPLMLIYTSGTTGKP 274
Cdd:cd12118 107 --------------VDREFEY----EDLLA---EGDP------DFEW-----IPP---ADE---WDPIALNYTSGTTGRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 275 KGTVHTHAGFPLkAAFDAGFGMNIKQGDRVLWVTDM----GWMmGPFLLFGsliNGATMVMYEGVpdfpEADRLWETVDK 350
Cdd:cd12118 149 KGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPMfhcnGWC-FPWTVAA---VGGTNVCLRKV----DAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 351 YEITHLGISPTLIRALmAKGDEYVNKHSLKSLEVFaSTGEPwnPDPWMwlFETVGKSNVPICNYSGGTEISGgifgnvli 430
Cdd:cd12118 220 HKVTHFCGAPTVLNML-ANAPPSDARPLPHRVHVM-TAGAP--PPAAV--LAKMEELGFDVTHVYGLTETYG-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 431 kpiaPISFNASLPGMAAVVLDDQ---------GNPIRDEV----GELCLEKPWVGMT------------KSFWEDDERyv 485
Cdd:cd12118 286 ----PATVCAWKPEWDELPTEERarlkarqgvRYVGLEEVdvldPETMKPVPRDGKTigeivfrgnivmKGYLKNPEA-- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 486 nTYWSrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVV 563
Cdd:cd12118 360 -TAEA-FRGGWFHsGDLAVIHPDGYIeIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446729151 564 LRDNVTFSGElkkELMSLVNSHIGKALCPKDIhVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd12118 438 LKEGAKVTEE---EIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
101-613 |
5.81e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 130.47 E-value: 5.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGengtsKSFTYEELDSWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:PRK08314 27 TAIVFYG-----RAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 180 TRVQAAGSKMIITADgfsrrgkvvSLKDEVDKAceHCPTVEKVVIVRHAGNDFTPHNYDF--SWSTLEKEKP------FV 251
Cdd:PRK08314 102 HYVTDSGARVAIVGS---------ELAPKVAPA--VGNLRLRHVIVAQYSDYLPAEPEIAvpAWLRAEPPLQalapggVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 252 HAEEM------------HSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVL------WVTDM-GW 312
Cdd:PRK08314 171 AWKEAlaaglappphtaGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLavlplfHVTGMvHS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 313 MMGPfllfgsLINGATMVMyegvpdFPEADR--LWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGE 390
Cdd:PRK08314 250 MNAP------IYAGATVVL------MPRWDReaAARLIERYRVTHWTNIPTMVVDFLASPG--LAERDLSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 391 PwnpdpwM------WLFETVGksnVPICNYSGGTEISGGIFGNVLIKP------IApiSFNASlpgmAAVVLDDQGNPI- 457
Cdd:PRK08314 316 A------MpeavaeRLKELTG---LDYVEGYGLTETMAQTHSNPPDRPklqclgIP--TFGVD----ARVIDPETLEELp 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 458 RDEVGELCLEKPWV---------GMTKSFWE-DDERYVNTywsrfenkwvhGDWVVYDGEQY-IITGRSDDTLNIAGKRI 526
Cdd:PRK08314 381 PGEVGEIVVHGPQVfkgywnrpeATAEAFIEiDGKRFFRT-----------GDLGRMDEEGYfFITDRLKRMINASGFKV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 527 GPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDN--VTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKT 604
Cdd:PRK08314 450 WPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEarGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKS 526
|
....*....
gi 446729151 605 RNSKVMRRV 613
Cdd:PRK08314 527 GSGKILWRQ 535
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
101-612 |
8.21e-32 |
|
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: 128.58 E-value: 8.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd17643 4 VAVVDEDR-----RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIITadgfsrrgkvvslkdevdkacehcptvekvvivrhagndfTPhnydfswstlekekpfvhaeemhsDD 260
Cdd:cd17643 79 ILADSGPSLLLT----------------------------------------DP------------------------DD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 261 PLMLIYTSGTTGKPKGTVHTHAGF-PLKAAFDAGFGMNikQGDRVLWVTDMG-----WMMgpfllFGSLINGATMVMyeg 334
Cdd:cd17643 95 LAYVIYTSGSTGRPKGVVVSHANVlALFAATQRWFGFN--EDDVWTLFHSYAfdfsvWEI-----WGALLHGGRLVV--- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 335 VPdfPEADR----LWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFAstGEPWNPD---PWmwlFETVGKS 407
Cdd:cd17643 165 VP--YEVARspedFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--GEALEAAmlrPW---AGRFGLD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 408 NVPICNYSGGTEISggIFgnVLIKPIAPISFNAS--------LPGMAAVVLDDQGNPI-RDEVGELCLEKPWV------- 471
Cdd:cd17643 238 RPQLVNMYGITETT--VH--VTFRPLDAADLPAAaaspigrpLPGLRVYVLDADGRPVpPGVVGELYVSGAGVargylgr 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 472 -GMTKS------FWEDDERYVNTywsrfenkwvhGDWVVY--DGEqYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVI 542
Cdd:cd17643 314 pELTAErfvanpFGGPGSRMYRT-----------GDLARRlpDGE-LEYLGRADEQVKIRGFRIELGEIEAALATHPSVR 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 543 EAAAIGVPDDVKGEVCHCFVVLRDNvtfSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17643 382 DAAVIVREDEPGDTRLVAYVVADDG---AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRA 448
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
116-612 |
9.67e-32 |
|
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: 128.93 E-value: 9.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADG 195
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDGP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 fsrrgkvvslkdevdkACEHCPTVEKVVIVRHagndftphnydfswSTLEKEKPFVhAEEMHSDDPLMLIYTSGTTGKPK 275
Cdd:cd12114 94 ----------------DAQLDVAVFDVLILDL--------------DALAAPAPPP-PVDVAPDDLAYVIFTSGSTGTPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 276 GTVHTHAG-FPLKAAFDAGFGMNIKqgDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVPDfPEADRLWETVDKYEIT 354
Cdd:cd12114 143 GVMISHRAaLNTILDINRRFAVGPD--DRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARR-RDPAHWAELIERHGVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 355 HLGISPTLIRALMAKGdEYVNKHsLKSLEVFASTGEpW----NPDPWMWLFetvgksnvPICNY---SGGTEisGGIFGN 427
Cdd:cd12114 220 LWNSVPALLEMLLDVL-EAAQAL-LPSLRLVLLSGD-WipldLPARLRALA--------PDARLislGGATE--ASIWSI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 428 VLikPIAP-------ISFNASLPGMAAVVLDDQGNPIRDEV-GELclekpW---VGMTKSFWED----DERYVN----TY 488
Cdd:cd12114 287 YH--PIDEvppdwrsIPYGRPLANQRYRVLDPRGRDCPDWVpGEL-----WiggRGVALGYLGDpeltAARFVThpdgER 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 489 WSRfenkwvHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDvKGEVCHCFVVLR-- 565
Cdd:cd12114 360 LYR------TGDLGRYRPDGTLeFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDnd 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446729151 566 DNVTFSGELKKELMSLVNSHIGkalcPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd12114 433 GTPIAPDALRAFLAQTLPAYMI----PSRVIALEALPLTANGKVDRA 475
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
116-608 |
1.96e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 128.85 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADG 195
Cdd:PRK07798 30 TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYERE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 FSrrGKVVSLKDEvdkacehCPTVEKVVIVRHA-GNDFTPHNYDFSwSTLEKEKPFVHAEEMHSDDpLMLIYTSGTTGKP 274
Cdd:PRK07798 110 FA--PRVAEVLPR-------LPKLRTLVVVEDGsGNDLLPGAVDYE-DALAAGSPERDFGERSPDD-LYLLYTGGTTGMP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 275 KGTVHTHAGFpLKAAF---DAGFGMNIK----QGDRVLWVTDMGWMMGPFLL--------FGSLINGATMVMYEgVPDFp 339
Cdd:PRK07798 179 KGVMWRQEDI-FRVLLggrDFATGEPIEdeeeLAKRAAAGPGMRRFPAPPLMhgagqwaaFAALFSGQTVVLLP-DVRF- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 340 EADRLWETVDKYEITHLGI------SPtLIRALMAKGDeyvnkHSLKSLEVFASTGEPWNP---DPWMWLFEtvgksNVP 410
Cdd:PRK07798 256 DADEVWRTIEREKVNVITIvgdamaRP-LLDALEARGP-----YDLSSLFAIASGGALFSPsvkEALLELLP-----NVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 411 ICNYSGGTEisGGIFGNVLIKPIAPISFNASL-PGMAAVVLDDQGNPIR---DEVGelclekpWVGMT------------ 474
Cdd:PRK07798 325 LTDSIGSSE--TGFGGSGTVAKGAVHTGGPRFtIGPRTVVLDEDGNPVEpgsGEIG-------WIARRghiplgyykdpe 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 475 ---KSFWE-DDERYVntywsrfenkwVHGDW--VVYDGeqyIIT--GRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:PRK07798 396 ktaETFPTiDGVRYA-----------IPGDRarVEADG---TITllGRGSVCINTGGEKVFPEEVEEALKAHPDVADALV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729151 547 IGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSK 608
Cdd:PRK07798 462 VGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
114-616 |
3.03e-31 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 128.34 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 DGFSrrgkvvslkDEVDKACEHCPTVEKVVivrhagnDFTPHNYDFSWSTLEKEkpfvHAEEMHSDDPL---MLIYTSGT 270
Cdd:PRK13382 148 EEFS---------ATVDRALADCPQATRIV-------AWTDEDHDLTVEVLIAA----HAGQRPEPTGRkgrVILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 271 TGKPKGTVHTHAG--FPLKAAFDAgfgMNIKQGDRVLWVTDM--GWMMGPFLLFGSLINgaTMVMYEgvpDF-PEADrlW 345
Cdd:PRK13382 208 TGTPKGARRSGPGgiGTLKAILDR---TPWRAEEPTVIVAPMfhAWGFSQLVLAASLAC--TIVTRR---RFdPEAT--L 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 346 ETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSnvpICNYSGGTEISggif 425
Cdd:PRK13382 278 DLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV---IYNNYNATEAG---- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 426 gnvLIKPIAPISF-----NASLPGMAAV--VLDDQGNPIRD-EVGELclekpWV-----------GMTKSFwedDERYVN 486
Cdd:PRK13382 351 ---MIATATPADLraapdTAGRPAEGTEirILDQDFREVPTgEVGTI-----FVrndtqfdgytsGSTKDF---HDGFMA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 487 TywsrfenkwvhGDWVVYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLR 565
Cdd:PRK13382 420 S-----------GDVGYLDENgRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446729151 566 DNvtfSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK13382 489 PG---ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
124-615 |
1.03e-30 |
|
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: 125.63 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 124 VSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIF---SGFASDAVMTRVQA-AGSKMIITADGfsrr 199
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplNPTLKESVLRYLVAdAGGRIVLADAG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 200 gkvvsLKDEVDKACEHCPTVEKVVIV---RHAGNDFTPHnydfswstlekekPFVHaeemhsDDPLMLIYTSGTTGKPKG 276
Cdd:cd05922 79 -----AADRLRDALPASPDPGTVLDAdgiRAARASAPAH-------------EVSH------EDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 277 TVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYE-GVPDfpeaDRLWETVDKYEITH 355
Cdd:cd05922 135 VRLSHQNLLANARSIAEY-LGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNdGVLD----DAFWEDLREHGATG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 356 LGISPTLIRALMAKGdeyVNKHSLKSLEVFASTGEPWnPDPWMWLFETVGKSNVPICNYsGGTEIsggiFGNVLIKPI-- 433
Cdd:cd05922 210 LAGVPSTYAMLTRLG---FDPAKLPSLRYLTQAGGRL-PQETIARLRELLPGAQVYVMY-GQTEA----TRRMTYLPPer 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 434 ---APISFNASLPGMAAVVLDDQGNPIR-DEVGELCLEKPWVgmTKSFWeDDERYVnTYWSRFENKWVHGDWVVYDGEQY 509
Cdd:cd05922 281 ileKPGSIGLAIPGGEFEILDDDGTPTPpGEPGEIVHRGPNV--MKGYW-NDPPYR-RKEGRGGGVLHTGDLARRDEDGF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 510 I-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVkGEVCHCFVVLRDNVTfsgelKKELMSLVNSHIGK 588
Cdd:cd05922 357 LfIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKID-----PKDVLRSLAERLPP 430
|
490 500
....*....|....*....|....*..
gi 446729151 589 ALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05922 431 YKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
97-617 |
1.34e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 125.85 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 97 TRTQPALQYEGengtsKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD 176
Cdd:PRK03640 15 TPDRTAIEFEE-----KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 177 AVMTRVQAAGSKMIITADGFsrrgkvvslKDEVdkacehcpTVEKVVIvrhagndftphnydfsWSTLEK--EKPFVHAE 254
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDF---------EAKL--------IPGISVK----------------FAELMNgpKEEAEIQE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 255 EMHSDDPLMLIYTSGTTGKPKGTVHTHaGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEg 334
Cdd:PRK03640 137 EFDLDEVATIMYTSGTTGKPKGVIQTY-GNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVE- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 335 vpDFpEADRLWETVDKYEITHLGISPTLIRALMAK--GDEYVNkhslkSLEVFASTGEPWNPDpwmwLFETVGKSNVPIC 412
Cdd:PRK03640 215 --KF-DAEKINKLLQTGGVTIISVVSTMLQRLLERlgEGTYPS-----SFRCMLLGGGPAPKP----LLEQCKEKGIPVY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 413 NYSGGTEISGGI-----------FGNVLiKPIAPisfnaslpgmAAVVLDDQGNPIR-DEVGELCLEKPWVgmTKSFWED 480
Cdd:PRK03640 283 QSYGMTETASQIvtlspedaltkLGSAG-KPLFP----------CELKIEKDGVVVPpFEEGEIVVKGPNV--TKGYLNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 481 DERyvnTYWSrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVC 558
Cdd:PRK03640 350 EDA---TRET-FQDGWFKtGDIGYLDEEGFLyVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVP 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446729151 559 HCFVVLRDNVTfsgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAA 617
Cdd:PRK03640 426 VAFVVKSGEVT-----EEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
113-616 |
1.36e-30 |
|
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: 125.09 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAG-IEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIfsgfasdavmtrvqaagskmii 191
Cdd:cd05941 10 DSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPL---------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 tadgfsrrgkvvslkdevdkacehCPTVEkVVIVRHAGNDftphnydfSWSTLekekpFVhaeemhsdDPLMLIYTSGTT 271
Cdd:cd05941 68 ------------------------NPSYP-LAELEYVITD--------SEPSL-----VL--------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 272 GKPKGTVHTHA--GFPLKAAFDAgfgMNIKQGDRVLWVTDMGWMMGPFL-LFGSLINGATMVMyegVPDFpEADRLWETV 348
Cdd:cd05941 102 GRPKGVVLTHAnlAANVRALVDA---WRWTEDDVLLHVLPLHHVHGLVNaLLCPLFAGASVEF---LPKF-DPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 349 DKYEITHLGISPT----LIRA--LMAKGDEYVNKHSLKSLEVFASTGEPWnPDPWMWLFETVGkSNVPICNYsGGTEIsG 422
Cdd:cd05941 175 LMPSITVFMGVPTiytrLLQYyeAHFTDPQFARAAAAERLRLMVSGSAAL-PVPTLEEWEAIT-GHTLLERY-GMTEI-G 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 423 GIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPI--RDEVGELCLEKPwvGMTKSFWEDDERyvnTYWSRFENKW-VHG 499
Cdd:cd05941 251 MALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPlpRGEVGEIQVRGP--SVFKEYWNKPEA---TKEEFTDDGWfKTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 500 DWVVYDGE-QYIITGR-SDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVT--FSGELK 575
Cdd:cd05941 326 DLGVVDEDgYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAalSLEELK 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729151 576 ---KELMSlvnshigKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05941 406 ewaKQRLA-------PYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
69-609 |
3.47e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 125.54 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 69 GTPFAQWYNGGTCNVVEsVLSRWLAddETRTQPALQYEGengtsKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPM 148
Cdd:PRK06178 21 GIPREPEYPHGERPLTE-YLRAWAR--ERPQRPAIIFYG-----HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 149 IPETVVAMLAVMKIGAI---ISPIFSGFasdAVMTRVQAAGSKMIITADGFS------------RRGKVVSLKDEVDKAc 213
Cdd:PRK06178 93 CPQFHIVFFGILKLGAVhvpVSPLFREH---ELSYELNDAGAEVLLALDQLApvveqvraetslRHVIVTSLADVLPAE- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 214 ehcPTVEKVVIVR-----HAG-NDFTPHnydfswstLEKEKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLK 287
Cdd:PRK06178 169 ---PTLPLPDSLRaprlaAAGaIDLLPA--------LRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 288 AAFDAGFGMNIKQGDRVLWVTDMGWMMGP-FLLFGSLINGATMVMYEGVpdfpEADRLWETVDKYEITHLGISPTLIRAL 366
Cdd:PRK06178 238 AAAAYAVAVVGGEDSVFLSFLPEFWIAGEnFGLLFPLFSGATLVLLARW----DAVAFMAAVERYRVTRTVMLVDNAVEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 367 MAKGDeyVNKHSLKSLEVF--ASTGEPWNPD---PWMWLFETV------GKSNVPICNysggtEISGGIFGNVLIKPIAP 435
Cdd:PRK06178 314 MDHPR--FAEYDLSSLRQVrvVSFVKKLNPDyrqRWRALTGSVlaeaawGMTETHTCD-----TFTAGFQDDDFDLLSQP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 436 ISFNASLPGMAAVVLD-DQGN--PIRDEvGELCLEKPwvGMTKSFWEDDERYVNTywsrFENKWVH-GDWVVYDGEQYI- 510
Cdd:PRK06178 387 VFVGLPVPGTEFKICDfETGEllPLGAE-GEIVVRTP--SLLKGYWNKPEATAEA----LRDGWLHtGDIGKIDEQGFLh 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 511 ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKAL 590
Cdd:PRK06178 460 YLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCRENMAVYK 536
|
570
....*....|....*....
gi 446729151 591 CPkDIHVVEDLPKTRNSKV 609
Cdd:PRK06178 537 VP-EIRIVDALPMTATGKV 554
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
116-622 |
5.90e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 124.73 E-value: 5.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAII---SPIFSG------FASDAvmTRVQAAG 186
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVvehNPLYTAhelehpFEDHG--ARVAIVW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 187 SKMIITADGFSRRG---KVVSlkdeVDkACEHCPTVEK------VVIVRHAGNDFTPHNYDF-SWSTLEK-----EKPFV 251
Cdd:PRK05605 137 DKVAPTVERLRRTTpleTIVS----VN-MIAAMPLLQRlalrlpIPALRKARAALTGPAPGTvPWETLVDaaiggDGSDV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 252 HAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGfpLKAafdagfgmNIKQG-----------DRVLWVTDM----GWMMGp 316
Cdd:PRK05605 212 SHPRPTPDDVALILYTSGTTGKPKGAQLTHRN--LFA--------NAAQGkawvpglgdgpERVLAALPMfhayGLTLC- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 317 fLLFGSLInGATMVMYegvPDfPEADRLWETVDKYEITHLGISPTLIRALMAKGDEY-VNKHSLK-------SLEVfaST 388
Cdd:PRK05605 281 -LTLAVSI-GGELVLL---PA-PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgVDLSGVRnafsgamALPV--ST 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 389 GEPWNPDPWMWLFEtvgksnvpicNYsGGTEISGGIFGNvlikpiaPISfNASLPGMAAVVLD-------DQGNPIRD-- 459
Cdd:PRK05605 353 VELWEKLTGGLLVE----------GY-GLTETSPIIVGN-------PMS-DDRRPGYVGVPFPdtevrivDPEDPDETmp 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 460 --EVGELCLEKPWVgmTKSFWEDDERYVNTywsrFENKWVH-GDWVVYDGEQY----------IITGrsddtlniaGKRI 526
Cdd:PRK05605 414 dgEEGELLVRGPQV--FKGYWNRPEETAKS----FLDGWFRtGDVVVMEEDGFirivdrikelIITG---------GFNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 527 GPAEYESILVKHNDVIEAAAIGVP-DDVKGEVCHCfVVLRDNVTFSGELKKElmsLVNSHIGKALCPKDIHVVEDLPKTR 605
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGLPrEDGSEEVVAA-VVLEPGAALDPEGLRA---YCREHLTRYKVPRRFYHVDELPRDQ 554
|
570
....*....|....*..
gi 446729151 606 NSKVMRRVIKAAYLGKE 622
Cdd:PRK05605 555 LGKVRRREVREELLEKL 571
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
116-612 |
1.00e-29 |
|
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: 123.39 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAV--------MTRVQAAGS 187
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELaeliergeMTAAVIAVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 188 KMIITADgFSRRGKVVSLKDEVDkacehcptvekvvivrhagndfTPHNYDFSwstlekekPFVHAEEMHSDDPLMLIYT 267
Cdd:cd05923 110 AQVMDAI-FQSGVRVLALSDLVG----------------------LGEPESAG--------PLIEDPPREPEQPAFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 268 SGTTGKPKGTVHTHAGFPLKAAFDAG-FGMNIKQGDRVLWVTDMGWMMGPF-LLFGSLINGATMVMyegVPDFPEADRLw 345
Cdd:cd05923 159 SGTTGLPKGAVIPQRAAESRVLFMSTqAGLRHGRHNVVLGLMPLYHVIGFFaVLVAALALDGTYVV---VEEFDPADAL- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 346 ETVDKYEITHLGISPTLIRALMAKgdEYVNKHSLKSLE--VFASTGEPwnpDPwmwLFETVGKS-NVPICNYSGGTEI-- 420
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALAAA--AEFAGLKLSSLRhvTFAGATMP---DA---VLERVNQHlPGEKVNIYGTTEAmn 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 421 -------------SGGIFGNVLIKPIAPISFNASLPGmaavvldDQGNPIRDEVGelclekpwvgmtksfwedDERYVNt 487
Cdd:cd05923 307 slymrdartgtemRPGFFSEVRIVRIGGSPDEALANG-------EEGELIVAAAA------------------DAAFTG- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 488 YWSRFE--------NKWVHGDWVVYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVC 558
Cdd:cd05923 361 YLNQPEatakklqdGWYRTGDVGYVDPSgDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSV 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446729151 559 HCFVVLRDNVTFSGELKKELMSlvnSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd05923 441 TACVVPREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRR 491
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
101-612 |
1.61e-29 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 121.59 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd17652 4 PAVVFGDE-----TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIITadgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemHSDD 260
Cdd:cd17652 79 MLADARPALLLT----------------------------------------------------------------TPDN 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 261 PLMLIYTSGTTGKPKGTVHTHAGFP-LKAAFDAGFgmNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVM---YEGVP 336
Cdd:cd17652 95 LAYVIYTSGSTGRPKGVVVTHRGLAnLAAAQIAAF--DVGPGSRVLQFASPSFDASVWELLMALLAGATLVLapaEELLP 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 337 DFPEADRLWEtvdkYEITHLGISPTLIRALMAKGdeyvnkhsLKSLEVFASTGEP--------WNPDPWMwlFETVGKSN 408
Cdd:cd17652 173 GEPLADLLRE----HRITHVTLPPAALAALPPDD--------LPDLRTLVVAGEAcpaelvdrWAPGRRM--INAYGPTE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 409 VPIC-NYSGGTEISGGIfgnvlikPI-APIsfnaslPGMAAVVLDDQGNPIRDEV-GELCLEKPwvGMTKSFWE----DD 481
Cdd:cd17652 239 TTVCaTMAGPLPGGGVP-------PIgRPV------PGTRVYVLDARLRPVPPGVpGELYIAGA--GLARGYLNrpglTA 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 482 ERYV-NTYWSRFENKWVHGDWVVY--DGeQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIgVPDDVKGE-- 556
Cdd:cd17652 304 ERFVaDPFGAPGSRMYRTGDLARWraDG-QLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV-VRDDRPGDkr 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 557 VCHCFVVLRDNVTFSGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17652 382 LVAYVVPAPGAAPTAAELRAHLAERLPGY----MVPAAFVVLDALPLTPNGKLDRR 433
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
111-616 |
2.37e-29 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 122.78 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 111 TSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:PLN02246 47 TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 191 ITADGFSrrGKVVSLKDEVDKacehcptveKVVIVrhagnDFTPHNYDFSWSTLEKEKPFVHAEEMHSDDPLMLIYTSGT 270
Cdd:PLN02246 127 ITQSCYV--DKLKGLAEDDGV---------TVVTI-----DDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 271 TGKPKGTVHTHAGFPLKAA--FDagfGMN----IKQGDRVLWVTDMgwmmgpF-------LLFGSLINGATMVMyegVPD 337
Cdd:PLN02246 191 TGLPKGVMLTHKGLVTSVAqqVD---GENpnlyFHSDDVILCVLPM------FhiyslnsVLLCGLRVGAAILI---MPK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 338 FpEADRLWETVDKYEITHLGISPTLIRALmAKGDEyVNKHSLKSLEVFASTGEPWNPDpwmwLFETVGKS--NVPICNYS 415
Cdd:PLN02246 259 F-EIGALLELIQRHKVTIAPFVPPIVLAI-AKSPV-VEKYDLSSIRMVLSGAAPLGKE----LEDAFRAKlpNAVLGQGY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 416 GGTEIsggifGNVL------------IKPIA--PISFNASLpgmaAVVLDDQGNPI-RDEVGELCLEKPWVgMtKSFWED 480
Cdd:PLN02246 332 GMTEA-----GPVLamclafakepfpVKSGScgTVVRNAEL----KIVDPETGASLpRNQPGEICIRGPQI-M-KGYLND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 481 DERYVNTYwsrFENKWVH-GDwVVY--DGEQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEV 557
Cdd:PLN02246 401 PEATANTI---DKDGWLHtGD-IGYidDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEV 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446729151 558 CHCFVVLRDNVTFSGELKKElmslvnsHIGKALC-PKDIHVV---EDLPKTRNSKVMRRVIKA 616
Cdd:PLN02246 477 PVAFVVRSNGSEITEDEIKQ-------FVAKQVVfYKRIHKVffvDSIPKAPSGKILRKDLRA 532
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
114-618 |
4.35e-29 |
|
The adenylation (A) domain of siderophore-synthesizing 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 to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. 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: 341242 [Multi-domain] Cd Length: 481 Bit Score: 121.11 E-value: 4.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIfsgfasDAVMTR------VQAAGS 187
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL------DPSHPLqrlqeiLQDTGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 188 KMIITADgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhSDDPLMLIYT 267
Cdd:cd05918 98 KVVLTSS---------------------------------------------------------------PSDAAYVIFT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 268 SGTTGKPKGTVHTHAGFplKAAFDAgFG--MNIKQGDRVLW---------VTDMgwmmgpfllFGSLINGATMVmyegVP 336
Cdd:cd05918 115 SGSTGKPKGVVIEHRAL--STSALA-HGraLGLTSESRVLQfasytfdvsILEI---------FTTLAAGGCLC----IP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 337 dfPEADR---LWETVDKYEITHLGISPTLIRALmakgdeyvNKHSLKSLEVFASTGEPWNP---DPWmwlfetvgKSNVP 410
Cdd:cd05918 179 --SEEDRlndLAGFINRLRVTWAFLTPSVARLL--------DPEDVPSLRTLVLGGEALTQsdvDTW--------ADRVR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 411 ICNYSGGTEISggIFGNVlikPIAPISFNASLPGMAA-----VVldDQGNPIR----DEVGELCLEKPWVGmtKSFWEDD 481
Cdd:cd05918 241 LINAYGPAECT--IAATV---SPVVPSTDPRNIGRPLgatcwVV--DPDNHDRlvpiGAVGELLIEGPILA--RGYLNDP 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 482 ER-----YVNTYWSRFENKWVH------GDWVVY--DGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:cd05918 312 EKtaaafIEDPAWLKQEGSGRGrrlyrtGDLVRYnpDGSLEYV-GRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVE 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 549 V--PDDVKGE---VchCFVVLR-------DNVTFSGELKKELMSLV---NSHIGKAL----CPKDIHVVEDLPKTRNSKV 609
Cdd:cd05918 391 VvkPKDGSSSpqlV--AFVVLDgsssgsgDGDSLFLEPSDEFRALVaelRSKLRQRLpsymVPSVFLPLSHLPLTASGKI 468
|
....*....
gi 446729151 610 MRRVIKAAY 618
Cdd:cd05918 469 DRRALRELA 477
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
110-621 |
1.93e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 119.80 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 110 GTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:PRK13391 20 STGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 190 IITAdgfSRRGKVVSLkdevdkACEHCPTVEKVVIVRHAGndftphnydfswsTLEKEKPFVHAEEMHSDDPL------- 262
Cdd:PRK13391 100 LITS---AAKLDVARA------LLKQCPGVRHRLVLDGDG-------------ELEGFVGYAEAVAGLPATPIadeslgt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 263 MLIYTSGTTGKPKGTVHTHAGFPLKAAFD-AGFGMNIKQGDRvlwvtDMGWM-------MGPfLLFGSLIN--GATMVMY 332
Cdd:PRK13391 158 DMLYSSGTTGRPKGIKRPLPEQPPDTPLPlTAFLQRLWGFRS-----DMVYLspaplyhSAP-QRAVMLVIrlGGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 333 EgvpDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnvPIC 412
Cdd:PRK13391 232 E---HF-DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWG----PII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 413 N-YSGGTEISGGIFGNVLIKPIAPISFNASLPGMAaVVLDDQGNPI-RDEVGELCLEKpwvGMTKSFWEDDERyvnTYWS 490
Cdd:PRK13391 304 HeYYAATEGLGFTACDSEEWLAHPGTVGRAMFGDL-HILDDDGAELpPGEPGTIWFEG---GRPFEYLNDPAK---TAEA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 491 RFEnkwvHGDW-----VVY-DGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVV 563
Cdd:PRK13391 377 RHP----DGTWstvgdIGYvDEDGYLyLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQ 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 564 LRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGK 621
Cdd:PRK13391 453 PVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGN 510
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
116-612 |
2.18e-28 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. 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: 341305 [Multi-domain] Cd Length: 447 Bit Score: 118.72 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITadg 195
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 fsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekeKPfvhaeemhsDDPLMLIYTSGTTGKPK 275
Cdd:cd17650 91 ----------------------------------------------------QP---------EDLAYVIYTSGTTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 276 GTVHTHAGFP-LKAAFDAGFGMNIKQgDRVLWVTDMGW--MMGPFLLfgSLINGATMVMyegVPDFPEAD--RLWETVDK 350
Cdd:cd17650 110 GVMVEHRNVAhAAHAWRREYELDSFP-VRLLQMASFSFdvFAGDFAR--SLLNGGTLVI---CPDEVKLDpaALYDLILK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 351 YEITHLGISPTLIRALMakgdEYVNKHSLK--SLEVFASTGEPWNPDPWMWLFETVGKSNVPICNYsGGTE--ISGGIF- 425
Cdd:cd17650 184 SRITLMESTPALIRPVM----AYVYRNGLDlsAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSY-GVTEatIDSTYYe 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 426 -GNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRDEV-GELCLEKPwvGMTKSFWEDDE----RYVNTYWSRFENKWVHG 499
Cdd:cd17650 259 eGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVaGELYIGGA--GVARGYLNRPEltaeRFVENPFAPGERMYRTG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 500 D---WVVyDGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIgVPDDVKGEVCHCFVVLRDNVTFSGELKK 576
Cdd:cd17650 337 DlarWRA-DGNVELL-GRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEARLCAYVVAAATLNTAELRA 413
|
490 500 510
....*....|....*....|....*....|....*.
gi 446729151 577 ELMslvnSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17650 414 FLA----KELPSYMIPSYYVQLDALPLTPNGKVDRR 445
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
100-548 |
1.88e-27 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 117.51 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 100 QPALQYEgENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:COG1022 27 RVALREK-EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 180 TRVQAAGSKMIITADGFsRRGKVVSLKDEvdkacehCPTVEKVVIVRHAGNDFTPHNYdfSWSTL-----EKEKPFVHAE 254
Cdd:COG1022 106 YILNDSGAKVLFVEDQE-QLDKLLEVRDE-------LPSLRHIVVLDPRGLRDDPRLL--SLDELlalgrEVADPAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 255 EMHS---DDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVL------WVtdMGWMMGpfllFGSLIN 325
Cdd:COG1022 176 RRAAvkpDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRTLsflplaHV--FERTVS----YYALAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 326 GATMVMYEGVPDFPEA------------DRLWETVdkYE--ITHLGISPTLIRAL----MAKGDEYVN------------ 375
Cdd:COG1022 249 GATVAFAESPDTLAEDlrevkptfmlavPRVWEKV--YAgiQAKAEEAGGLKRKLfrwaLAVGRRYARarlagkspslll 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 376 --KHSL--------------KSLEVFASTGEPWNPDpwmwL---FETVGksnVPICN-YsGGTEISGGIFGNvlikpiap 435
Cdd:COG1022 327 rlKHALadklvfsklrealgGRLRFAVSGGAALGPE----LarfFRALG---IPVLEgY-GLTETSPVITVN-------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 436 iSFNASLPGMAAVVLDdqGNPIR-DEVGELCLEKPwvGMTKSFWEDDERYVNTYwsrFENKWVH-GDWVVYDGEQYI-IT 512
Cdd:COG1022 391 -RPGDNRIGTVGPPLP--GVEVKiAEDGEILVRGP--NVMKGYYKNPEATAEAF---DADGWLHtGDIGELDEDGFLrIT 462
|
490 500 510
....*....|....*....|....*....|....*..
gi 446729151 513 GRSDDTL-NIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:COG1022 463 GRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
112-618 |
1.90e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 116.72 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 112 SKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 T-ADGFSrrgkvvSLKDEVDKACE--HCPT-VEKVVIVRHAGNDFTPHNYDFSWST-LEKEKPFvhaEEMHSDDPLMLIY 266
Cdd:PRK12406 89 AhADLLH------GLASALPAGVTvlSVPTpPEIAAAYRISPALLTPPAGAIDWEGwLAQQEPY---DGPPVPQPQSMIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 267 TSGTTGKPKGtVHTHAGFPLKAAFD---AGFGMNIKQGDRVLwvtdmgwMMGPflLFGSLIN---------GATMVMyeg 334
Cdd:PRK12406 160 TSGTTGHPKG-VRRAAPTPEQAAAAeqmRALIYGLKPGIRAL-------LTGP--LYHSAPNayglragrlGGVLVL--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 335 VPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnvP-ICN 413
Cdd:PRK12406 227 QPRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWG----PvIYE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 414 YSGGTEISGGIFGN---VLIKpiaPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPwvGMtksfweDDERYVNTYW 489
Cdd:PRK12406 302 YYGSTESGAVTFATsedALSH---PGTVGKAAPGAELRFVDEDGRPLPQgEIGEIYSRIA--GN------PDFTYHNKPE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 490 SRFE---NKWVH-GD--WVVYDGEQYIITGRSDDTLNiAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVV 563
Cdd:PRK12406 371 KRAEidrGGFITsGDvgYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVE 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 564 LRDNVTFS-GELKKELmslvNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAY 618
Cdd:PRK12406 450 PQPGATLDeADIRAQL----KARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
113-619 |
2.76e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 115.67 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPI---FSGFASDAVMTRVQAAgskM 189
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnwrLSASELDALLQDAEPR---L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 190 IITADGFSR-RGKVVSLKDEVDKACEHCPtvekvvivrhagnDFTPHnydfswstlekekpfvhaeeMHSDDPLMLIYTS 268
Cdd:PRK09088 98 LLGDDAVAAgRTDVEDLAAFIASADALEP-------------ADTPS--------------------IPPERVSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 269 GTTGKPKGTVHTHagfplKAAFDAG--FGMNIKQGDRVLWVTD--MGWMMGpflLFGS----LINGATMVMYEGVPdfPE 340
Cdd:PRK09088 145 GTSGQPKGVMLSE-----RNLQQTAhnFGVLGRVDAHSSFLCDapMFHIIG---LITSvrpvLAVGGSILVSNGFE--PK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 341 ADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPW-NPDPWMWLFEtvgksNVPICNYSGGTE 419
Cdd:PRK09088 215 RTLGRLGDPALGITHYFCVPQMAQAFRAQPG--FDAAALRHLTALFTGGAPHaAEDILGWLDD-----GIPMVDGFGMSE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 420 iSGGIFG-NVLIKPIAPISFNASL--PGMAAVVLDDQGNPIRDEV-GELCLEKPwvGMTKSFWEDDEryvNTYWSRFENK 495
Cdd:PRK09088 288 -AGTVFGmSVDCDVIRAKAGAAGIptPTVQTRVVDDQGNDCPAGVpGELLLRGP--NLSPGYWRRPQ---ATARAFTGDG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 496 WVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGE 573
Cdd:PRK09088 362 WFRtGDIARRDADGFFwVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446729151 574 lkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYL 619
Cdd:PRK09088 442 ---RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALA 484
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
113-548 |
3.42e-27 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 115.00 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIT 192
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 193 adgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekEKPfvhaeemhsDDPLMLIYTSGTTG 272
Cdd:cd05907 84 ------------------------------------------------------EDP---------DDLATIIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 273 KPKGTVHTHAGF--PLKAAFDAgfgMNIKQGDRVLWVTDMGWMMGP-FLLFGSLINGATMVMYE----GVPDFPEAD--- 342
Cdd:cd05907 101 RPKGVMLSHRNIlsNALALAER---LPATEGDRHLSFLPLAHVFERrAGLYVPLLAGARIYFASsaetLLDDLSEVRptv 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 343 -----RLWETVdkYEITHLGISPTLIRALMAkgdeyvnKHSLKSLEVFASTGEPWNPDpwmwLFETVGKSNVPICNYSGG 417
Cdd:cd05907 178 flavpRVWEKV--YAAIKVKAVPGLKRKLFD-------LAVGGRLRFAASGGAPLPAE----LLHFFRALGIPVYEGYGL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 418 TEISGGIFGNVlikpiaPISFNASLPGMAAvvlddQGNPIR-DEVGELCLEKPwvGMTKSFWEDDERyvnTYWSRFENKW 496
Cdd:cd05907 245 TETSAVVTLNP------PGDNRIGTVGKPL-----PGVEVRiADDGEILVRGP--NVMLGYYKNPEA---TAEALDADGW 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446729151 497 VH-GDWVVYDGEQYI-ITGRSDDTL-NIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:cd05907 309 LHtGDLGEIDEDGFLhITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
111-615 |
4.25e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 116.09 E-value: 4.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 111 TSKSFTYEELDSWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:PLN02574 63 TGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 190 IITadgfsrrgkvvslkdEVDKACEHCPTVEKVVIVRHAG--NDFTPHNYDFSWSTLEKEKPFVhAEEMHSDDPLMLIYT 267
Cdd:PLN02574 143 AFT---------------SPENVEKLSPLGVPVIGVPENYdfDSKRIEFPKFYELIKEDFDFVP-KPVIKQDDVAAIMYS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 268 SGTTGKPKGTVHTHAGF----PLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLIN-GATMVMYEGVpdfpEAD 342
Cdd:PLN02574 207 SGTTGASKGVVLTHRNLiamvELFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRF----DAS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 343 RLWETVDKYEITHLGISPTLIRALM--AKGdeyVNKHSLKSLEVFASTGEPWNPDPWMWLFETVgkSNVPICNYSGGTEi 420
Cdd:PLN02574 283 DMVKVIDRFKVTHFPVVPPILMALTkkAKG---VCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL--PHVDFIQGYGMTE- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 421 SGGI----FGNVLIKPIAPISFNAslPGMAAVVLD-------DQGNpirdeVGELCLEKPwvGMTKSFWEDDERyvnTYW 489
Cdd:PLN02574 357 STAVgtrgFNTEKLSKYSSVGLLA--PNMQAKVVDwstgcllPPGN-----CGELWIQGP--GVMKGYLNNPKA---TQS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 490 SRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDN 567
Cdd:PLN02574 425 TIDKDGWLRtGDIAYFDEDGYLyIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446729151 568 VTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PLN02574 505 STLSQE---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-611 |
3.12e-25 |
|
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: 107.57 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 258 SDDPLMLIYTSGTTGKPKGTVHTHAGfplkaafdagfgmnikqgdrvlwVTDMGWMMGPFLLFGS--------------- 322
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-----------------------EVYNAWMLALNSLFDPddvllcglplfhvng 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 323 --------LINGATMVM-----YEGVPDFpeaDRLWETVDKYEITHLGISPTLIRALMAKGDEyVNKHSLKslevFASTG 389
Cdd:cd05944 58 svvtlltpLASGAHVVLagpagYRNPGLF---DNFWKLVERYRITSLSTVPTVYAALLQVPVN-ADISSLR----FAMSG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 390 EPWNPDPWMWLFETvgKSNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLP--GMAAVVLDDQGNPIRD----EVGE 463
Cdd:cd05944 130 AAPLPVELRARFED--ATGLPVVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPyaRVRIKVLDGVGRLLRDcapdEVGE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 464 LCLEKPWV--GMTksfweDDERYVNTYwsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHN 539
Cdd:cd05944 208 ICVAGPGVfgGYL-----YTEGNKNAF---VADGWLNtGDLGRLDADGYLfITGRAKDLIIRGGHNIDPALIEEALLRHP 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446729151 540 DVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIG-KALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd05944 280 AVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEE---ELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFK 349
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
115-611 |
3.32e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 110.29 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI---ISPIFSGFASDAVMTRVqaaGSKMII 191
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIlvtINPAYRLSELEYALNQS---GCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 TADGFsRRGKVVSLKDEVDKACEHC----------PTVEKVVIVrhaGNDFTPHNYdfSWSTLEKEKPFVH-------AE 254
Cdd:PRK08315 121 AADGF-KDSDYVAMLYELAPELATCepgqlqsarlPELRRVIFL---GDEKHPGML--NFDELLALGRAVDdaelaarQA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 255 EMHSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRV-LWVtdmgwmmgPFL-LFG-------SLIN 325
Cdd:PRK08315 195 TLDPDDPINIQYTSGTTGFPKGATLTHRNI-LNNGYFIGEAMKLTEEDRLcIPV--------PLYhCFGmvlgnlaCVTH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 326 GATMV-MYEGvpdF-PEAdrLWETVDKYEITHL-GIsPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWnPDPWMwlfE 402
Cdd:PRK08315 266 GATMVyPGEG---FdPLA--TLAAVEEERCTALyGV-PTMFIAELDHPD--FARFDLSSLRTGIMAGSPC-PIEVM---K 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 403 TV----GKSNVPICnYsGGTEISggifgnvlikpiaPISFNAS---------------LPGMAAVVLD-DQGNPI-RDEV 461
Cdd:PRK08315 334 RVidkmHMSEVTIA-Y-GMTETS-------------PVSTQTRtddplekrvttvgraLPHLEVKIVDpETGETVpRGEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 462 GELCLEKPWVgMtKSFWEDDERyvnTYWSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHN 539
Cdd:PRK08315 399 GELCTRGYSV-M-KGYWNDPEK---TAEAIDADGWMHtGDLAVMDEEGYVnIVGRIKDMIIRGGENIYPREIEEFLYTHP 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 540 DVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKV----MR 611
Cdd:PRK08315 474 KIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE---DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIqkfkMR 546
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
97-612 |
3.42e-25 |
|
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: 109.34 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 97 TRTQPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD 176
Cdd:cd17655 10 TPDHTAVVFEDQ-----TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 177 AVMTRVQAAGSKMIITadgfsrrgkvvslkdevdkaceHCPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKpfvhaeem 256
Cdd:cd17655 85 RIQYILEDSGADILLT----------------------QSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVS-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 257 HSDDPLMLIYTSGTTGKPKGTVHTHAGFP-LKAAFDAgfGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGV 335
Cdd:cd17655 135 KSDDLAYVIYTSGSTGKPKGVMIEHRGVVnLVEWANK--VIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 336 PDFPeADRLWETVDKYEITHLGISPTLIRALmakgdEYVNKHSLKSLEVFASTGEPWNPD---PWMWLFETvgksNVPIC 412
Cdd:cd17655 213 TVLD-GQALTQYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIVGGEALSTElakKIIELFGT----NPTIT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 413 NYSGGTE-----ISGGIFGNVLIKPIAPISfnASLPGMAAVVLDDQGNPIR-DEVGELCLEKPwvGMTKSFWE----DDE 482
Cdd:cd17655 283 NAYGPTEttvdaSIYQYEPETDQQVSVPIG--KPLGNTRIYILDQYGRPQPvGVAGELYIGGE--GVARGYLNrpelTAE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 483 RYVNTYWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCH 559
Cdd:cd17655 359 KFVDDPFVPGERMYRTGDLARWlpDGNiEFL--GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLC 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446729151 560 CFVVLRDNVTFSG---ELKKELMS-LVNSHIGKalcpkdihvVEDLPKTRNSKVMRR 612
Cdd:cd17655 437 AYIVSEKELPVAQlreFLARELPDyMIPSYFIK---------LDEIPLTPNGKVDRK 484
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
260-616 |
3.51e-25 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 106.65 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGfpLKAAFDAGfGMNIKQGDRVLWVTDM--GWMMGPFLLFGSLINGATMVMYEGVPD 337
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN--LLASAAGL-HSRLGFGGGDSWLLSLplYHVGGLAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 338 fpeadrLWETVDKYEITHLGISPT-LIRALMAKGDeyvnKHSLKSLEVFASTGEPWNPDpwmwLFETVGKSNVPICNYSG 416
Cdd:cd17630 78 ------LAEDLAPPGVTHVSLVPTqLQRLLDSGQG----PAALKSLRAVLLGGAPIPPE----LLERAADRGIPLYTTYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 417 GTEISGGIFGNVLIKPIAPISFNAsLPGmAAVVLDDQGnpiRDEVGELCLEKpwvGMTKSFWEDDeryvntywsRFENKW 496
Cdd:cd17630 144 MTETASQVATKRPDGFGRGGVGVL-LPG-RELRIVEDG---EIWVGGASLAM---GYLRGQLVPE---------FNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 497 VH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSgel 574
Cdd:cd17630 207 FTtKDLGELHADGRLtVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA--- 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446729151 575 kkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd17630 284 --ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
96-619 |
5.69e-25 |
|
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: 109.25 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 96 ETRTQPALQY-EGENGTSKSFTYEELDSWVSRVANGLKHAGiEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIF---S 171
Cdd:cd05931 5 ARPDRPAYTFlDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPpptP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 172 GFASDAVMTRVQAAGSKMIITADGFsrrgkvvslKDEVDKACEHCPTVEKVVIVRHAGNDFTPHNydfSWSTLEKEkpfv 251
Cdd:cd05931 84 GRHAERLAAILADAGPRVVLTTAAA---------LAAVRAFAASRPAAGTPRLLVVDLLPDTSAA---DWPPPSPD---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 252 haeemhSDDPLMLIYTSGTTGKPKGTVHTHAGfpLKAAFDAGF-GMNIKQGDR-VLWVT---DMGWMMGpflLFGSLING 326
Cdd:cd05931 148 ------PDDIAYLQYTSGSTGTPKGVVVTHRN--LLANVRQIRrAYGLDPGDVvVSWLPlyhDMGLIGG---LLTPLYSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 327 ATMVMYEGVpDFPEADRLW-ETVDKYEITHLGiSPT-----LIRALMAKGDEYVNKHSLK------------SLEVFAST 388
Cdd:cd05931 217 GPSVLMSPA-AFLRRPLRWlRLISRYRATISA-APNfaydlCVRRVRDEDLEGLDLSSWRvalngaepvrpaTLRRFAEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 389 GEPWNPDPWMW----------LFETVGKSN-VPICNYSGGTEISGGIFGNVLIKPIAP--ISFNASLPGMAAVVLDDQGN 455
Cdd:cd05931 295 FAPFGFRPEAFrpsyglaeatLFVSGGPPGtGPVVLRVDRDALAGRAVAVAADDPAARelVSCGRPLPDQEVRIVDPETG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 456 PIR--DEVGELCLEKPwvGMTKSFWEDDERYVNTYWSRFENKwvHGDW-------VVYDGEQYiITGRSDDTLNIAGKRI 526
Cdd:cd05931 375 RELpdGEVGEIWVRGP--SVASGYWGRPEATAETFGALAATD--EGGWlrtgdlgFLHDGELY-ITGRLKDLIIVRGRNH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 527 GPAEYESILVKHNDVIE---AAAIGVPDDVKGEVchcFVVLRDNVTFSGE----LKKELMSLVNSHIGkaLCPKDIHVVE 599
Cdd:cd05931 450 YPQDIEATAEEAHPALRpgcVAAFSVPDDGEERL---VVVAEVERGADPAdlaaIAAAIRAAVAREHG--VAPADVVLVR 524
|
570 580
....*....|....*....|..
gi 446729151 600 --DLPKTRNSKVMRRVIKAAYL 619
Cdd:cd05931 525 pgSIPRTSSGKIQRRACRAAYL 546
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
75-612 |
5.94e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 111.41 E-value: 5.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 75 WYNGGTCNVVESVLSRWLADDETRT--QPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPET 152
Cdd:PRK12467 3084 WNATAAAYPSERLVHQLIEAQVARTpeAPALVFGDQ-----QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEM 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 153 VVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKVVSlkdeVDKAcehcptvekVVIVRHAGNDF 232
Cdd:PRK12467 3159 IVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPA----GDTA---------LTLDRLDLNGY 3225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 233 TPHNYDfswstlekekPFVHAEEMhsddpLMLIYTSGTTGKPKGTVHTHAGFPLK-AAFDAGFGMNIkqGDRVLWVTDMG 311
Cdd:PRK12467 3226 SENNPS----------TRVMGENL-----AYVIYTSGSTGKPKGVGVRHGALANHlCWIAEAYELDA--NDRVLLFMSFS 3288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 312 WMMGPFLLFGSLINGATMVMYEGvpDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDeyvnKHSLKSLEVFASTGEP 391
Cdd:PRK12467 3289 FDGAQERFLWTLICGGCLVVRDN--DLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFGGEA 3362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 392 WNPDPWMWLFETVgkSNVPICNYSGGTEIS--------GGifGNVLIKPIAPISfnASLPGMAAVVLDDQGNPIRDEV-G 462
Cdd:PRK12467 3363 VPPAAFEQVKRKL--KPRGLTNGYGPTEAVvtvtlwkcGG--DAVCEAPYAPIG--RPVAGRSIYVLDGQLNPVPVGVaG 3436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 463 ELCLEKpwVGMTKSFWE----DDERYV-NTYWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESI 534
Cdd:PRK12467 3437 ELYIGG--VGLARGYHQrpslTAERFVaDPFSGSGGRLYRTGDLARYraDGViEYL--GRIDHQVKIRGFRIELGEIEAR 3512
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 535 LVKHNDVIEAAAIGVpDDVKGEVCHCFVVLRDNvtfSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK12467 3513 LLQHPSVREAVVLAR-DGAGGKQLVAYVVPADP---QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRK 3586
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
530-608 |
1.08e-24 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 97.62 E-value: 1.08e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446729151 530 EYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTfsgELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSK 608
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE---LLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
259-615 |
1.63e-24 |
|
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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 105.44 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 259 DDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDM----GWMMGpflLFGSLINGATMVMYEg 334
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNI-VNNGYFIGERLGLTEQDRLCIPVPLfhcfGSVLG---VLACLTHGATMVFPS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 335 vPDFPEADRLwETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWnPDPWM-WLFETVGKSNVPICn 413
Cdd:cd05917 77 -PSFDPLAVL-EAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRTGIMAGAPC-PPELMkRVIEVMNMKDVTIA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 414 YsGGTEISGGIFGNVLIKPIAP--ISFNASLPGMAAVVLDDQGN--PIRDEVGELCLEKpwVGMTKSFWEDDERyvnTYW 489
Cdd:cd05917 151 Y-GMTETSPVSTQTRTDDSIEKrvNTVGRIMPHTEAKIVDPEGGivPPVGVPGELCIRG--YSVMKGYWNDPEK---TAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 490 SRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDN 567
Cdd:cd05917 225 AIDGDGWLHtGDLAVMDEDGYCrIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEG 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446729151 568 VTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05917 305 AELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
108-615 |
2.46e-24 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 107.37 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 108 ENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispiFSGFASDAVMT----RVQ 183
Cdd:PLN02330 49 EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTALESeikkQAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 184 AAGSKMIITADgfSRRGKVVSLkdevdkacehcptvEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFVHAEEMHSDDPLM 263
Cdd:PLN02330 125 AAGAKLIVTND--TNYGKVKGL--------------GLPVIVLGEEKIEGAVNWKELLEAADRAGDTSDNEEILQTDLCA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 264 LIYTSGTTGKPKGTVHTHAGFP---LKAAFDAGFGMnIKQgdrvlwVTDMGWMmgPF--------LLFGSLINGATMVMy 332
Cdd:PLN02330 189 LPFSSGTTGISKGVMLTHRNLVanlCSSLFSVGPEM-IGQ------VVTLGLI--PFfhiygitgICCATLRNKGKVVV- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 333 egVPDFpEADRLWETVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFA--STGEPWNPDpWMWLFETvGKSNVP 410
Cdd:PLN02330 259 --MSRF-ELRTFLNALITQEVSFAPIVPPIILNLVK--NPIVEEFDLSKLKLQAimTAAAPLAPE-LLTAFEA-KFPGVQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 411 ICNYSGGTEIS---------------------GGIFGNVLIKPIAPISfNASLPgmaavvlddqgnpiRDEVGELCLEKP 469
Cdd:PLN02330 332 VQEAYGLTEHScitlthgdpekghgiakknsvGFILPNLEVKFIDPDT-GRSLP--------------KNTPGELCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 470 WVgmTKSFWEDDERYVNTYwsrFENKWVH-GD--WVVYDGEQYIITgRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:PLN02330 397 CV--MQGYYNNKEETDRTI---DEDGWLHtGDigYIDDDGDIFIVD-RIKELIKYKGFQVAPAELEAILLTHPSVEDAAV 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446729151 547 IGVPDDVKGEVCHCFVVLRDNVTfsgELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PLN02330 471 VPLPDEEAGEIPAACVVINPKAK---ESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
113-621 |
4.29e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.77 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGL-KHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAII---SPIFSgfaSDAVMTRVQAAGSK 188
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVvntNPLYT---AREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 189 MIitadgfsrrgkvVSLKDEVDKACEHCP-TVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFVHAEEM----------- 256
Cdd:PRK05677 125 AL------------VCLANMAHLAEKVLPkTGVKHVIVTEVADMLPPLKRLLINAVVKHVKKMVPAYHLpqavkfndala 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 257 ------------HSDDPLMLIYTSGTTGKPKGTVHTHAGFPLK-AAFDAGFGMNIKQGDRVLwvtdmgwmMGPFLLFG-- 321
Cdd:PRK05677 193 kgagqpvteanpQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmLQCRALMGSNLNEGCEIL--------IAPLPLYHiy 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 322 --SLINGATMVMYEG---VPDFPEADRLWETVDKYEIT-HLGISpTLIRALMakGDEYVNKHSLKSLEVFASTGepwnpd 395
Cdd:PRK05677 265 afTFHCMAMMLIGNHnilISNPRDLPAMVKELGKWKFSgFVGLN-TLFVALC--NNEAFRKLDFSALKLTLSGG------ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 396 pwMWLFETVGK-----SNVPICNYSGGTEISGGIFGNVlIKPIAPISFNASLPGMAAVVLDDQGNPI-RDEVGELCLEKP 469
Cdd:PRK05677 336 --MALQLATAErwkevTGCAICEGYGMTETSPVVSVNP-SQAIQVGTIGIPVPSTLCKVIDDDGNELpLGEVGELCVKGP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 470 WVgmTKSFWEDDEryvNTYWSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAI 547
Cdd:PRK05677 413 QV--MKGYWQRPE---ATDEILDSDGWLKtGDIALIQEDGYMrIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAI 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446729151 548 GVPDDVKGEVCHCFVVLRDNVTFSgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGK 621
Cdd:PRK05677 488 GVPDEKSGEAIKVFVVVKPGETLT---KEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKK 558
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
116-609 |
5.61e-24 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 105.87 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIisPIFsgfasdAVmtrvqaagskmiitadg 195
Cdd:cd05920 42 TYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVL------AL----------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 FSRRGKvvslkdEVDKACEHCPTVEKVVIVRHAGNDFTPHnydfswstlekekpfvhAEEMHSD--DPLMLIYTSGTTGK 273
Cdd:cd05920 97 PSHRRS------ELSAFCAHAEAVAYIVPDRHAGFDHRAL-----------------ARELAESipEVALFLLSGGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 274 PKGTVHTHA--GFPLKAAFDAgfgMNIKQGDRVLWVTDMGW---MMGPFLLfGSLINGATMVMyegVPDfPEADRLWETV 348
Cdd:cd05920 154 PKLIPRTHNdyAYNVRASAEV---CGLDQDTVYLAVLPAAHnfpLACPGVL-GTLLAGGRVVL---APD-PSPDAAFPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 349 DKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnvpiC-------------NYs 415
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAAASR--RADLSSLRLLQVGGARLSPALARRVPPVLG------CtlqqvfgmaegllNY- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 416 ggTEI--SGGIFGNVLIKPIAPisfnaslpGMAAVVLDDQGNPIRD-EVGELCLEKPWV--GM-------TKSFWEDder 483
Cdd:cd05920 297 --TRLddPDEVIIHTQGRPMSP--------DDEIRVVDEEGNPVPPgEEGELLTRGPYTirGYyrapehnARAFTPD--- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 484 yvNTYWSrfenkwvhGDWVVYDGEQYII-TGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFV 562
Cdd:cd05920 364 --GFYRT--------GDLVRRTPDGYLVvEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFV 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446729151 563 VLRDNVTFSGELKKELMslvNSHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:cd05920 434 VLRDPPPSAAQLRRFLR---ERGLAAYKLPDRIEFVDSLPLTAVGKI 477
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
116-615 |
9.00e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 105.74 E-value: 9.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI-ITAD 194
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVlIDAD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 GfsrrgkvvslkdevdkACEHC-PTVEKVVIVRHAGNDFTPhnydfSWSTLE-------KEKPFVHAEEMHSDDPLMLIY 266
Cdd:PRK05852 125 G----------------PHDRAePTTRWWPLTVNVGGDSGP-----SGGTLSvhldaatEPTPATSTPEGLRPDDAMIMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 267 TSGTTGKPKGTVHTHAGFPLKA-AFDAGFGMnikqGDRVLWVTDMGWMMGPFL---LFGSLINGATmVMYEGVPDFpEAD 342
Cdd:PRK05852 184 TGGTTGLPKMVPWTHANIASSVrAIITGYRL----SPRDATVAVMPLYHGHGLiaaLLATLASGGA-VLLPARGRF-SAH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 343 RLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnVPICNYSGGTEISG 422
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA---APVVCAFGMTEATH 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 423 GIfGNVLIKPIAPISFNASLPGMAA--------VVLDDQGNPIRDEVGELCLEKPWVgmTKSFWEDDEryvNTYwSRFEN 494
Cdd:PRK05852 335 QV-TTTQIEGIGQTENPVVSTGLVGrstgaqirIVGSDGLPLPAGAVGEVWLRGTTV--VRGYLGDPT---ITA-ANFTD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 495 KWVH-GDWVVYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSG 572
Cdd:PRK05852 408 GWLRtGDLGSLSAAgDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446729151 573 ElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK05852 488 E---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVA 527
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
92-612 |
9.94e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 107.35 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 92 LADDETRTQP---ALQYEGEngtskSFTYEELDswvsRVANGLKHAGIEKG----DRVTIYMPMIPETVVAMLAVMKIGA 164
Cdd:PRK12316 4556 LVAERARMTPdavAVVFDEE-----KLTYAELN----RRANRLAHALIARGvgpeVLVGIAMERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 165 IISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRgkvVSLKDEVdkaceHCPTVEKvvivrhagndftphnyDFSWSTL 244
Cdd:PRK12316 4627 AYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQR---LPIPDGL-----ASLALDR----------------DEDWEGF 4682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 245 EKEKPfvhAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGF-PLKAAFDAGFGMNikQGDRVLWVTDMGWMMGPFLLFGSL 323
Cdd:PRK12316 4683 PAHDP---AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLvNHLHATGERYELT--PDDRVLQFMSFSFDGSHEGLYHPL 4757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 324 INGATMVMYEgvPDFPEADRLWETVDKYEITHLGISPTLIRALmAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFET 403
Cdd:PRK12316 4758 INGASVVIRD--DSLWDPERLYAEIHEHRVTVLVFPPVYLQQL-AEHAE--RDGEPPSLRVYCFGGEAVAQASYDLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 404 VgkSNVPICNYSGGTEISGGIF------GNVLIKPIAPISfnASLPGMAAVVLDDQGNPIR-DEVGELCLEKPwvGMTKS 476
Cdd:PRK12316 4833 L--KPVYLFNGYGPTETTVTVLlwkardGDACGAAYMPIG--TPLGNRSGYVLDGQLNPLPvGVAGELYLGGE--GVARG 4906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 477 FWE----DDERYV-NTYWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:PRK12316 4907 YLErpalTAERFVpDPFGAPGGRLYRTGDLARYraDGViDYL--GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA 4984
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446729151 549 VPDDVkGEVCHCFVV-----LRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK12316 4985 QEGAV-GKQLVGYVVpqdpaLADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRK 5052
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
97-616 |
1.08e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 107.35 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 97 TRTQPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD 176
Cdd:PRK12316 3070 TPDAVALAFGEQ-----RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEE 3144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 177 AVMTRVQAAGSKMIITADGFSrrgkvvslkdevdkaCEHCPTVEKVVIVRHAGNdftphnydfswstLEKEKPFVHAEem 256
Cdd:PRK12316 3145 RLAYMLEDSGAQLLLSQSHLR---------------LPLAQGVQVLDLDRGDEN-------------YAEANPAIRTM-- 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 257 hSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyEGVP 336
Cdd:PRK12316 3195 -PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVL-AGPE 3271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 337 DFPEADRLWETVDKYEITHLGISPTLIRALMakgdEYVNKHSLKSLEVFASTGEPWNPDPWMWLFetvgkSNVPICNYSG 416
Cdd:PRK12316 3272 DWRDPALLVELINSEGVDVLHAYPSMLQAFL----EEEDAHRCTSLKRIVCGGEALPADLQQQVF-----AGLPLYNLYG 3342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 417 GTEISGGIFGNVLIKPIAPISFNAS-LPGMAAVVLDDQGNPI-RDEVGELCLEKpwVGMTKSFWE----DDERYVNTYWS 490
Cdd:PRK12316 3343 PTEATITVTHWQCVEEGKDAVPIGRpIANRACYILDGSLEPVpVGALGELYLGG--EGLARGYHNrpglTAERFVPDPFV 3420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 491 RFENKWVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIgvpdDVKGEVCHCFVVLRDNvt 569
Cdd:PRK12316 3421 PGERLYRTGDLARYRADGVIeYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDE-- 3494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446729151 570 fSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK12316 3495 -AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
114-612 |
1.77e-23 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; 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 saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 103.94 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDavmtRVQAagskmIITa 193
Cdd:cd12115 24 SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPE----RLRF-----ILE- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 dgfsrrgkvvslkdevDKACEHcptvekvVIVRhagndftphnydfswstlekekpfvhaeemhSDDPLMLIYTSGTTGK 273
Cdd:cd12115 94 ----------------DAQARL-------VLTD-------------------------------PDDLAYVIYTSGSTGR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 274 PKGTVHTHAG-----FPLKAAFDAgfgmniKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGV---PDFPEADrlw 345
Cdd:cd12115 120 PKGVAIEHRNaaaflQWAAAAFSA------EELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVlalPDLPAAA--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 346 etvdkyEITHLGISPTLIRALMAKGDeyvnkhSLKSLEVFASTGEPWNPD---------PWMWLFETVGKSNVpiCNYSG 416
Cdd:cd12115 191 ------EVTLINTVPSAAAELLRHDA------LPASVRVVNLAGEPLPRDlvqrlyarlQVERVVNLYGPSED--TTYST 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 417 GTEISGGIFGnvlikpiaPISFNASLPGMAAVVLDDQGNPIRD-EVGELCLEKPwvGMTKSFWEDD----ERYVNTYWSR 491
Cdd:cd12115 257 VAPVPPGASG--------EVSIGRPLANTQAYVLDRALQPVPLgVPGELYIGGA--GVARGYLGRPgltaERFLPDPFGP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 492 FENKWVHGDWVVYDGE---QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVL-RDN 567
Cdd:cd12115 327 GARLYRTGDLVRWRPDgllEFL--GRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAePGA 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446729151 568 VTFSGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd12115 405 AGLVEDLRRHLGTRLPAY----MVPSRFVRLDALPLTPNGKIDRS 445
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
260-611 |
2.29e-23 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which 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: 341288 [Multi-domain] Cd Length: 320 Bit Score: 101.33 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGFplKAAFDAG-FGMNIKQGDRVLwvtdmgwMMGPFLLFGSLiNGATMVMYEG---- 334
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSW--IESFVCNeDLFNISGEDAIL-------APGPLSHSLFL-YGAISALYLGgtfi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 335 VPDFPEADRLWETVDKYEITHLGISPTLIRALMAkgdEYVNKHSLKSlevFASTGEPWNPDpwmwLFETVGK--SNVPIC 412
Cdd:cd17633 71 GQRKFNPKSWIRKINQYNATVIYLVPTMLQALAR---TLEPESKIKS---IFSSGQKLFES----TKKKLKNifPKANLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 413 NYSGGTEISGgIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNpirdEVGELCLEKPwvgMTKSFWEDDERYVNTYWSrf 492
Cdd:cd17633 141 EFYGTSELSF-ITYNFNQESRPPNSVGRPFPNVEIEIRNADGG----EIGKIFVKSE---MVFSGYVRGGFSNPDGWM-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 493 enkwVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVChCFVVLRDNVTfs 571
Cdd:cd17633 211 ----SVGDIGYVDEEGYLyLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGDKLT-- 283
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446729151 572 gelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17633 284 ---YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
260-611 |
3.30e-23 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. 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: 341292 [Multi-domain] Cd Length: 333 Bit Score: 101.19 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSL-INGATMVMyegvPDF 338
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNL-IAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFhAGGANVVM----EKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 339 PEADRLwETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPwnpdpwmwlfETVGK--SNVPICNYS- 415
Cdd:cd17637 76 DPAEAL-ELIEEEKVTLMGSFPPILSNLLDAAEK--SGVDLSSLRHVLGLDAP----------ETIQRfeETTGATFWSl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 416 -GGTEISGGI-FGNVLIKPIApisfnASLPGMAAVV--LDDQGNPI-RDEVGELCLEKPWVgmTKSFWEDDEryVNTYws 490
Cdd:cd17637 143 yGQTETSGLVtLSPYRERPGS-----AGRPGPLVRVriVDDNDRPVpAGETGEIVVRGPLV--FQGYWNLPE--LTAY-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 491 RFENKWVH-GDWVVYDGEQYI-ITGRS--DDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRD 566
Cdd:cd17637 212 TFRNGWHHtGDLGRFDEDGYLwYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446729151 567 NVTFSgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17637 292 GATLT---ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
113-550 |
5.35e-23 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 102.43 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIfsgfasdavmtrvqaagskmiit 192
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 193 adGFSRRGKVVSlkdevdkaceHCPTV--EKVVIVrhagndftphnydfswstlekekpfvhaeemhsdDPLMLIYTSGT 270
Cdd:cd05940 59 --NYNLRGESLA----------HCLNVssAKHLVV----------------------------------DAALYIYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 271 TGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGdrVLWVT-----DMGWMMGpflLFGSLINGATMVMYEgvpDFpEADRLW 345
Cdd:cd05940 93 TGLPKAAIISHRRAWRGGAFFAGSGGALPSD--VLYTClplyhSTALIVG---WSACLASGATLVIRK---KF-SASNFW 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 346 ETVDKYEITHLGISPTLIRALM-AKGDEYVNKHSLKslevfASTGEPWNPDPWMwlfETVGKSNVP-ICNYSGGTEISGG 423
Cdd:cd05940 164 DDIRKYQATIFQYIGELCRYLLnQPPKPTERKHKVR-----MIFGNGLRPDIWE---EFKERFGVPrIAEFYAATEGNSG 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 424 iFGNVLIKPIApISFNASLP----GMAAVVLD-DQGNPIRD-----------EVGELCLE----KPWVGMTKS------- 476
Cdd:cd05940 236 -FINFFGKPGA-IGRNPSLLrkvaPLALVKYDlESGEPIRDaegrcikvprgEPGLLISRinplEPFDGYTDPaatekki 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 477 ---FWEDDERYVNTywsrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVP 550
Cdd:cd05940 314 lrdVFKKGDAWFNT-----------GDLMRLDGEGFWyFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
109-618 |
1.61e-22 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 101.39 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 109 NGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 189 MIITadgfsrrGKVvslkdevdkacEHCPTVEKVV---IVRHAGNDFTPHNYDFSWSTLEKEKPFVHAEEMHSDDPLM-L 264
Cdd:cd05932 81 ALFV-------GKL-----------DDWKAMAPGVpegLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLAtL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 265 IYTSGTTGKPKGTVHTHAGFplkaAFDAGFGMN---IKQGDRVLWVTDMGWMMGPFLLF-GSLINGATMVMYEGVPDFPE 340
Cdd:cd05932 143 IYTSGTTGQPKGVMLTFGSF----AWAAQAGIEhigTEENDRMLSYLPLAHVTERVFVEgGSLYGGVLVAFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 341 ------------ADRLWETVDKYEITHLGISP-----------TLIRALMAKGdeyvnkHSLKSLEVFASTGEPWNPDPW 397
Cdd:cd05932 219 dvqrarptlffsVPRLWTKFQQGVQDKIPQQKlnlllkipvvnSLVKRKVLKG------LGLDQCRLAGCGSAPVPPALL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 398 MWlFETVGksnVPICNYSGGTEISGGIFGNVlikpiaPISFNASLPGMAAvvlddQGNPIR-DEVGELCLEKPwvGMTKS 476
Cdd:cd05932 293 EW-YRSLG---LNILEAYGMTENFAYSHLNY------PGRDKIGTVGNAG-----PGVEVRiSEDGEILVRSP--ALMMG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 477 FWEDDERyvnTYWSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIA-GKRIGPAEYESILVKHnDVIEAAAI---GVP 550
Cdd:cd05932 356 YYKDPEA---TAEAFTADGFLRtGDKGELDADGNLtITGRVKDIFKTSkGKYVAPAPIENKLAEH-DRVEMVCVigsGLP 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446729151 551 DDVKGEVCHCFVVLRDNVTFSGELK---KELMSLVNSHIGKALCPKDIHVVEDLPKTRNS------KVMRRVIKAAY 618
Cdd:cd05932 432 APLALVVLSEEARLRADAFARAELEaslRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGiltptlKIKRNVLEKAY 508
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
115-617 |
1.10e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 99.06 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPI---FSGFASDAVMTRVQAAgsKMII 191
Cdd:PRK06155 47 WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPIntaLRGPQLEHILRNSGAR--LLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 TADGFsrrgkvvslkDEVDKACEHCPTVEKVVIVRHAGNDFTPHNYDFSwsTLEKEKPFVHAEEMHSDDPLMLIYTSGTT 271
Cdd:PRK06155 125 EAALL----------AALEAADPGDLPLPAVWLLDAPASVSVPAGWSTA--PLPPLDAPAPAAAVQPGDTAAILYTSGTT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 272 GKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDrVLWVTdmgwmmgpFLLF---------GSLINGATMVMyegVPDFpEAD 342
Cdd:PRK06155 193 GPSKGVCCPHAQFYWWGRNSAED-LEIGADD-VLYTT--------LPLFhtnalnaffQALLAGATYVL---EPRF-SAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 343 RLWETVDKYEIT---HLGISPTLIRALMAKGDEyvNKHSLKsleVFASTGEPwnPDPWMWLFETVGksnVPICNYSGGTE 419
Cdd:PRK06155 259 GFWPAVRRHGATvtyLLGAMVSILLSQPARESD--RAHRVR---VALGPGVP--AALHAAFRERFG---VDLLDGYGSTE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 420 iSGGIFGNVLIKPiAPISFNASLPGMAAVVLDDQGNPIRD-EVGELCL--EKPWVGMTKSFwEDDERYVNTyWsrfENKW 496
Cdd:PRK06155 329 -TNFVIAVTHGSQ-RPGSMGRLAPGFEARVVDEHDQELPDgEPGELLLraDEPFAFATGYF-GMPEKTVEA-W---RNLW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 497 VH-GDWVV--YDGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGE 573
Cdd:PRK06155 402 FHtGDRVVrdADGWFRFV-DRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729151 574 lkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAA 617
Cdd:PRK06155 481 ---ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
101-550 |
1.23e-21 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 99.18 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGengtsKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK08279 54 PALLFED-----QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIITADGFSRRgkVVSLKDEVDKACEHCPTVEKVVIVRHAGNDftphnYDFSWSTLEKEKPfVHAEEMHSDD 260
Cdd:PRK08279 129 SLNLVDAKHLIVGEELVEA--FEEARADLARPPRLWVAGGDTLDDPEGYED-----LAAAAAGAPTTNP-ASRSGVTAKD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 261 PLMLIYTSGTTGKPKGTVHTHAGFpLKAAfdAGFG--MNIKQGDRVLWVTDMGWMMGPFLLFGSLIN-GATMVMYEgvpD 337
Cdd:PRK08279 201 TAFYIYTSGTTGLPKAAVMSHMRW-LKAM--GGFGglLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAaGATLALRR---K 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 338 FpEADRLWETVDKYEITHLGISPTLIRALM---AKGDEyvNKHSLKSLevfasTGEPWNPDPWMWLFETVGksnVP-ICN 413
Cdd:PRK08279 275 F-SASRFWDDVRRYRATAFQYIGELCRYLLnqpPKPTD--RDHRLRLM-----IGNGLRPDIWDEFQQRFG---IPrILE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 414 YSGGTEISGGIF---------GNV---LIKPIAPISFNaslPGMAAVVLDDQGNPIRDEVGE--LCLEK-----PWVGMT 474
Cdd:PRK08279 344 FYAASEGNVGFInvfnfdgtvGRVplwLAHPYAIVKYD---VDTGEPVRDADGRCIKVKPGEvgLLIGRitdrgPFDGYT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 475 KS-----------FwEDDERYVNTywsrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVI 542
Cdd:PRK08279 421 DPeasekkilrdvF-KKGDAWFNT-----------GDLMRDDGFGHAqFVDRLGDTFRWKGENVATTEVENALSGFPGVE 488
|
....*...
gi 446729151 543 EAAAIGVP 550
Cdd:PRK08279 489 EAVVYGVE 496
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-608 |
2.13e-21 |
|
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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 96.30 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 258 SDDPLMLIYTSGTTGKPKGTVHTHAGFP--LKAAFDAGFG---MNIKQGDRVLWVTDMGWMMGPFLL--------FGSLI 324
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEDIFrmLMGGADFGTGeftPSEDAHKAAAAAAGTVMFPAPPLMhgtgswtaFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 325 NGATMVmyegVPDFP-EADRLWETVDKYEITHLGI-----SPTLIRALMAKGDeyvnkHSLKSLEVFASTGEPWNPD--- 395
Cdd:cd05924 82 GGQTVV----LPDDRfDPEEVWRTIEKHKVTSMTIvgdamARPLIDALRDAGP-----YDLSSLFAISSGGALLSPEvkq 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 396 ------PWMWLFETVGKSnvpicnysggteiSGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPI---RDEVGelcl 466
Cdd:cd05924 153 gllelvPNITLVDAFGSS-------------ETGFTGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVppgSGGVG---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 467 ekpWVG----MTKSFWEDDERYVNTYWSRFENKW-VHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHND 540
Cdd:cd05924 216 ---WIArrghIPLGYYGDEAKTAETFPEVDGVRYaVPGDRATVEADGTVtLLGRGSVCINTGGEKVFPEEVEEALKSHPA 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 541 VIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSK 608
Cdd:cd05924 293 VYDVLVVGRPDERWGQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
260-611 |
2.96e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 95.41 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgvpDFP 339
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGG---ENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 340 EADRLWETVDKYEITHLGISPTLIRALMakgDEYVNK-HSLKSLEVFASTGE-PWNPDpwMWLFETVGKSNvpICNYSGG 417
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLV---SELKSAnATVPSLRLIGYGGSrAIAAD--VRFIEATGLTN--TAQVYGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 418 TEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQG-NPIRDEVGELCLEKPWvgMTKSFWEDDERYVntywSRFENKW 496
Cdd:cd17635 152 SETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGiAGPSASFGTIWIKSPA--NMLGYWNNPERTA----EVLIDGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 497 VH-GD--WVVYDGEQYIiTGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLrdnvtfSGE 573
Cdd:cd17635 226 VNtGDlgERREDGFLFI-TGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA------SAE 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446729151 574 LKKELMS----LVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17635 299 LDENAIRalkhTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
101-616 |
3.41e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.26 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGENgtsksFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK12316 2020 IAVVFGDQH-----LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAY 2094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIITADGFSRR----GKVVSLkdEVDKACEhcptvekvvivrhagndftphnydfsWSTLEKEKPfvhAEEM 256
Cdd:PRK12316 2095 MLEDSGAALLLTQRHLLERlplpAGVARL--PLDRDAE--------------------------WADYPDTAP---AVQL 2143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 257 HSDDPLMLIYTSGTTGKPKGTVHTHAgfPLKAAFDA-GFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGV 335
Cdd:PRK12316 2144 AGENLAYVIYTSGSTGLPKGVAVSHG--ALVAHCQAaGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDE 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 336 PDFPEadRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEV------FASTGEPWNPDPWMWLFETVG--KS 407
Cdd:PRK12316 2222 LWDPE--QLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFggeavpAASLRLAWEALRPVYLFNGYGptEA 2299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 408 NVPICNYSGGTEISGGIFGnvlikpiAPISfnASLPGMAAVVLDDQGNPIRDE-VGELCLEKpwVGMTKSFWE----DDE 482
Cdd:PRK12316 2300 VVTPLLWKCRPQDPCGAAY-------VPIG--RALGNRRAYILDADLNLLAPGmAGELYLGG--EGLARGYLNrpglTAE 2368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 483 RYV-NTYWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVpDDVKGEVC 558
Cdd:PRK12316 2369 RFVpDPFSASGERLYRTGDLARYraDGVvEYL--GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQL 2445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446729151 559 HCFVVLRDNVT-FSGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK12316 2446 VAYVVPDDAAEdLLAELRAWLAARLPAY----MVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
264-611 |
1.13e-20 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 93.72 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 264 LIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGmNIKQGDRVLWVTdmgwmmgPFL-LFG-------SLINGATmVMYEGV 335
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCA-DLTEDDRYLIIN-------PFFhTFGykagivaCLLTGAT-VVPVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 336 PDfpeADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEvFASTGEPWNPdpwMWLFETVgKSNVPICNYS 415
Cdd:cd17638 76 FD---VDAILEAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLR-AAVTGAATVP---VELVRRM-RSELGFETVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 416 ---GGTEISGGifgnVLIKPIAPISFNAS-----LPGMAAVVLDDqgnpirdevGELCLEKPWVgmTKSFWEDDEryvNT 487
Cdd:cd17638 146 tayGLTEAGVA----TMCRPGDDAETVATtcgraCPGFEVRIADD---------GEVLVRGYNV--MQGYLDDPE---AT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 488 YWSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLR 565
Cdd:cd17638 208 AEAIDADGWLHtGDVGELDERGYLrITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446729151 566 DNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17638 288 PGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
83-546 |
1.27e-20 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 97.04 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 83 VVESVLSRWLADDETRT--QPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVM 160
Cdd:PRK10252 455 IPETTLSALVAQQAAKTpdAPALADARY-----QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIV 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 161 KIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRgkvvslkdevdkacehcptvekvvivRHAGNDFTPHNYDfS 240
Cdd:PRK10252 530 EAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPR--------------------------FADVPDLTSLCYN-A 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 241 WSTLEKEKPFVHAeemHSDDPLMLIYTSGTTGKPKGTVHTHAG-----------FPLKAAfdagfgmnikqgDRVLWVTD 309
Cdd:PRK10252 583 PLAPQGAAPLQLS---QPHHTAYIIFTSGSTGRPKGVMVGQTAivnrllwmqnhYPLTAD------------DVVLQKTP 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 310 MGWMMGPFLLFGSLINGATMVMYEgvpdfPEADR----LWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSL-EV 384
Cdd:PRK10252 648 CSFDVSVWEFFWPFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLrQV 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 385 FAStGEPWNP---DPWMWLFetvgksNVPICNYSGGTEI---------SGGIFGNVLIKPIaPISF---NASLpgmaaVV 449
Cdd:PRK10252 723 FCS-GEALPAdlcREWQQLT------GAPLHNLYGPTEAavdvswypaFGEELAAVRGSSV-PIGYpvwNTGL-----RI 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 450 LDDQGNPIRDEV-GELC-----LEKPWVGmtksfwEDD---ERYVNTYWSRFENKWVHGDWVVY--DGE-QYIitGRSDD 517
Cdd:PRK10252 790 LDARMRPVPPGVaGDLYltgiqLAQGYLG------RPDltaSRFIADPFAPGERMYRTGDVARWldDGAvEYL--GRSDD 861
|
490 500
....*....|....*....|....*....
gi 446729151 518 TLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:PRK10252 862 QLKIRGQRIELGEIDRAMQALPDVEQAVT 890
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
115-611 |
1.88e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 95.47 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD 194
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 GFSRRGKVVSLKDEVDKACEHCPtvekvVIVRHAgNDFT--PHNYDFSWSTL-EKEKP---------FVHAEEmhsdDPL 262
Cdd:PLN03102 120 SFEPLAREVLHLLSSEDSNLNLP-----VIFIHE-IDFPkrPSSEELDYECLiQRGEPtpslvarmfRIQDEH----DPI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 263 MLIYTSGTTGKPKGTVHTHAGFPLkAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVpdfpEAD 342
Cdd:PLN03102 190 SLNYTSGTTADPKGVVISHRGAYL-STLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHV----TAP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 343 RLWETVDKYEITHLGISPTLIRALMaKGDEYVNKHslKSLEVFASTGepwNPDPWMWLFETVGKSNVPICNYSGGTEISG 422
Cdd:PLN03102 265 EIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSP--RSGPVHVLTG---GSPPPAALVKKVQRLGFQVMHAYGLTEATG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 423 gifgnvlikpiaPISFNA------SLP-----------GMAAVVLDD--------QGNPIRD--EVGELCLEKPwvGMTK 475
Cdd:PLN03102 339 ------------PVLFCEwqdewnRLPenqqmelkarqGVSILGLADvdvknketQESVPRDgkTMGEIVIKGS--SIMK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 476 SFWEDDEryvnTYWSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDV 553
Cdd:PLN03102 405 GYLKNPK----ATSEAFKHGWLNtGDVGVIHPDGHVeIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446729151 554 KGEVCHCFVVLRDNVTFSGEL-------KKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PLN03102 481 WGETPCAFVVLEKGETTKEDRvdklvtrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILK 545
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
129-621 |
2.26e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 95.12 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 129 NGLKhagIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRrgkvvSLKDE 208
Cdd:PRK08974 67 NGLG---LKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAH-----TLEKV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 209 VDKACehcptVEKVVIVRhAGN----------DFT-------------PHNYDFSwSTLEKEK--PFVHAEeMHSDDPLM 263
Cdd:PRK08974 139 VFKTP-----VKHVILTR-MGDqlstakgtlvNFVvkyikrlvpkyhlPDAISFR-SALHKGRrmQYVKPE-LVPEDLAF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 264 LIYTSGTTGKPKGTVHTHAGFPlkaafdagfgMNIKQGDrvlwvtdmgWMMGPFL---------------LFGSLIN--- 325
Cdd:PRK08974 211 LQYTGGTTGVAKGAMLTHRNML----------ANLEQAK---------AAYGPLLhpgkelvvtalplyhIFALTVNcll 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 326 ----GATMVMYEGVPDFPEadrLWETVDKYEITHLGISPTLIRALMAKGD-EYVNKHSLK-----SLEVFASTGEPWnpd 395
Cdd:PRK08974 272 fielGGQNLLITNPRDIPG---FVKELKKYPFTAITGVNTLFNALLNNEEfQELDFSSLKlsvggGMAVQQAVAERW--- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 396 pwmwlfETVGKSNVpICNYsGGTEISGGIFGNvlikPIAPISFNASL----PGMAAVVLDDQGNPI-RDEVGELCLEKPW 470
Cdd:PRK08974 346 ------VKLTGQYL-LEGY-GLTECSPLVSVN----PYDLDYYSGSIglpvPSTEIKLVDDDGNEVpPGEPGELWVKGPQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 471 VgMtKSFWEDDERYVNTywsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:PRK08974 414 V-M-LGYWQRPEATDEV----IKDGWLAtGDIAVMDEEGFLrIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVG 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446729151 549 VPDDVKGEVCHCFVVLRDNvtfsGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGK 621
Cdd:PRK08974 488 VPSEVSGEAVKIFVVKKDP----SLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
264-616 |
5.44e-20 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 93.21 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 264 LIYTSGTTGKPKGTVHTHAGFPLKAA--FDAGFGMNIKQGDRVLWVTDM------GWMMGpfllfgSLINGATMVmyeGV 335
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDtlMAAALGFGPGADSVYLSPAPLyhaapfRWSMT------ALFMGGTLV---LM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 336 PDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEP---WNPDPWM-WLFETvgksnvpI 411
Cdd:cd05929 201 EKF-DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPcppWVKEQWIdWGGPI-------I 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 412 CNYSGGTEISGGIF----------GNVlikpiapisfnaslpGMAAV----VLDDQGNPI-RDEVGELCLEKPwvgmtkS 476
Cdd:cd05929 273 WEYYGGTEGQGLTIingeewlthpGSV---------------GRAVLgkvhILDEDGNEVpPGEIGEVYFANG------P 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 477 FWEDDERYVNTYWSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVK 554
Cdd:cd05929 332 GFEYTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLyLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEEL 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729151 555 GEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05929 412 GQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
114-612 |
5.86e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 93.52 E-value: 5.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:PRK13383 60 ALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVAD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 DGFSRR----GKVVSLKDEVDKACEHCPTvekvvivrhagndftphnydfswstlekeKPFVHAEEMhsddplMLIYTSG 269
Cdd:PRK13383 140 NEFAERiagaDDAVAVIDPATAGAEESGG-----------------------------RPAVAAPGR------IVLLTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 270 TTGKPKGTvhthagfPLKAAFDAGFGMNI--------KQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVpdfpEA 341
Cdd:PRK13383 185 TTGKPKGV-------PRAPQLRSAVGVWVtildrtrlRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHF----DA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 342 DRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKSnvpICNYSGGTEIS 421
Cdd:PRK13383 254 EAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI---LYNGYGSTEVG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 422 GGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRDEV-------GELCLEKPWVGMTKSFwedderyVNTYWSRfen 494
Cdd:PRK13383 331 IGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVtgrifvgGELAGTRYTDGGGKAV-------VDGMTST--- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 495 kwvhGDWVVYD--GEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNvtfSG 572
Cdd:PRK13383 401 ----GDMGYLDnaGRLFIV-GREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG---SG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446729151 573 ELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK13383 473 VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRK 512
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
115-617 |
6.95e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 93.47 E-value: 6.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 115 FTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD 194
Cdd:PRK08162 44 RTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 GFSrrgkvvslkDEVDKACEHCPTVEKVVI---------VRHAGN----DFTPH-NYDFSWSTLEKEKpfvhaeemhsdD 260
Cdd:PRK08162 124 EFA---------EVAREALALLPGPKPLVIdvddpeypgGRFIGAldyeAFLASgDPDFAWTLPADEW-----------D 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 261 PLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDA-GFGMniKQGDRVLWVTDM----GWMMgPFLLfgsLINGATMVMYEGV 335
Cdd:PRK08162 184 AIALNYTSGTTGNPKGVVYHHRGAYLNALSNIlAWGM--PKHPVYLWTLPMfhcnGWCF-PWTV---AARAGTNVCLRKV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 336 pdfpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPwnpdPWMWLFETVGKSNVPICNYS 415
Cdd:PRK08162 258 ----DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEW--RAGIDHPVHAMVAGAA----PPAAVIAKMEEIGFDLTHVY 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 416 GGTEISGgifgnvlikpiaPISFNASLPGMAAVVLDDQGN---------PIRDEVG----ELCLEKPWVGMT-------- 474
Cdd:PRK08162 328 GLTETYG------------PATVCAWQPEWDALPLDERAQlkarqgvryPLQEGVTvldpDTMQPVPADGETigeimfrg 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 475 ----KSFWEDDERYVNTywsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:PRK08162 396 nivmKGYLKNPKATEEA----FAGGWFHtGDLAVLHPDGYIkIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVA 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446729151 549 VPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIhVVEDLPKTRNSK----VMRRVIKAA 617
Cdd:PRK08162 472 KPDPKWGEVPCAFVELKDGASATEE---EIIAHCREHLAGFKVPKAV-VFGELPKTSTGKiqkfVLREQAKSL 540
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
116-628 |
1.04e-19 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 93.56 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispifsGFASDAVMTRVQAA------GSKM 189
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM------AFLANPELHRDDHAlaarntEPAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 190 IITADGFSRRGKVVSLKDEVDKACEhcptvekvvIVRHAGNDFTPHNYD-FSWSTlekekpfvhaeemhsddplmliYTS 268
Cdd:PRK06060 106 VVTSDALRDRFQPSRVAEAAELMSE---------AARVAPGGYEPMGGDaLAYAT----------------------YTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 269 GTTGKPKGTVHTHAG-FPLKAAFDAGfGMNIKQGDRVLWVTDM--GWMMGPFLLFgSLINGATMVMyEGVPDFPEADRLW 345
Cdd:PRK06060 155 GTTGPPKAAIHRHADpLTFVDAMCRK-ALRLTPEDTGLCSARMyfAYGLGNSVWF-PLATGGSAVI-NSAPVTPEAAAIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 346 ETvdKYEITHL-GISPTLIRALMAkgdeyVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksNVPICNYSGGTEIsGGI 424
Cdd:PRK06060 232 SA--RFGPSVLyGVPNFFARVIDS-----CSPDSFRSLRCVVSAGEALELGLAERLMEFFG--GIPILDGIGSTEV-GQT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 425 FGNVLIKPIAPISFNASLPGMAAVVLDDQGNpirdEVGElclekpwvGMTKSFWEDDERYVNTYWSRFENKWVHGDW--- 501
Cdd:PRK06060 302 FVSNRVDEWRLGTLGRVLPPYEIRVVAPDGT----TAGP--------GVEGDLWVRGPAIAKGYWNRPDSPVANEGWldt 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 502 ---VVYDGEQYIITG-RSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKE 577
Cdd:PRK06060 370 rdrVCIDSDGWVTYRcRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRD 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446729151 578 LMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSS 628
Cdd:PRK06060 450 LHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSL 500
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
116-613 |
1.75e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 92.11 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADG 195
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 FsRRGKVVSLKDEVDKACEhcPTVEKVVIVRHAGNDfTPHNYDFSWSTL----EKEKPFVHAEEMHSDDPLMLIY-TSGT 270
Cdd:PRK06164 117 F-KGIDFAAILAAVPPDAL--PPLRAIAVVDDAADA-TPAPAPGARVQLfalpDPAPPAAAGERAADPDAGALLFtTSGT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 271 TGKPKGTVHTHAGFPLKAAFDA-GFGMNikQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyEGVPDFPEADRLwetVD 349
Cdd:PRK06164 193 TSGPKLVLHRQATLLRHARAIArAYGYD--PGAVLLAALPFCGVFGFSTLLGALAGGAPLVC-EPVFDAARTARA---LR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 350 KYEITHLGISPTLIRALMAKGDEyvnKHSLKSLEV--FASTGEPWNPdpwmwLFETVGKSNVPICNYSGGTEisggIFGN 427
Cdd:PRK06164 267 RHRVTHTFGNDEMLRRILDTAGE---RADFPSARLfgFASFAPALGE-----LAALARARGVPLTGLYGSSE----VQAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 428 VLIKPIAPISFNASLPGMAAV-------VLDDQGNPI--RDEVGELCLEKPWV---------GMTKSFWEDDerYVNTyw 489
Cdd:PRK06164 335 VALQPATDPVSVRIEGGGRPAspearvrARDPQDGALlpDGESGEIEIRAPSLmrgyldnpdATARALTDDG--YFRT-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 490 srfenkwvhGDWVVYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKgEVCHCFVVLRDNV 568
Cdd:PRK06164 411 ---------GDLGYTRGDgQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGK-TVPVAFVIPTDGA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446729151 569 TFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTR--NSKVMRRV 613
Cdd:PRK06164 481 SPDEA---GLMAACREALAGFKVPARVQVVEAFPVTEsaNGAKIQKH 524
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
113-617 |
1.93e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 92.25 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGL-KHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 TADGFSrrgkvvslkDEVDKACEHCPtVEKVV------------------IVRHAgNDFTPhNYDFSWSTLEKE------ 247
Cdd:PRK08751 129 VIDNFG---------TTVQQVIADTP-VKQVIttglgdmlgfpkaalvnfVVKYV-KKLVP-EYRINGAIRFREalalgr 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 248 KPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTH----AGFPLKAAFDAGFGmNIKQGDRVLWVTdmgwmMGPFLLFGSL 323
Cdd:PRK08751 197 KHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHrnlvANMQQAHQWLAGTG-KLEEGCEVVITA-----LPLYHIFALT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 324 INGATMVMYEGVPDFPEADR----LWETVDKYEITHLGISPTLIRALM-AKGDEYVNKHSLK-----SLEVFASTGEPWN 393
Cdd:PRK08751 271 ANGLVFMKIGGCNHLISNPRdmpgFVKELKKTRFTAFTGVNTLFNGLLnTPGFDQIDFSSLKmtlggGMAVQRSVAERWK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 394 pdpwmwlfETVGksnVPICNYSGGTEISGGifgnVLIKPIAPISFNASL----PGMAAVVLDDQGNPIR-DEVGELCLEK 468
Cdd:PRK08751 351 --------QVTG---LTLVEAYGLTETSPA----ACINPLTLKEYNGSIglpiPSTDACIKDDAGTVLAiGEIGELCIKG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 469 PWVgmTKSFWEDDERyvnTYWSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:PRK08751 416 PQV--MKGYWKRPEE---TAKVMDADGWLHtGDIARMDEQGFVyIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAA 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729151 547 IGVPDDVKGEVCHCFVVLRDNVTFSGELKKElmslVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAA 617
Cdd:PRK08751 491 VGVPDEKSGEIVKVVIVKKDPALTAEDVKAH----ARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDA 557
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
111-615 |
4.22e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 90.84 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 111 TSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:PRK13390 21 TGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 191 ITAdgfsrrgkvVSLKDEVDKACEHCPtvekvviVRHAGNDFTPHNYDFSwSTLEKEKPFVhaeemhSDDPL--MLIYTS 268
Cdd:PRK13390 101 VAS---------AALDGLAAKVGADLP-------LRLSFGGEIDGFGSFE-AALAGAGPRL------TEQPCgaVMLYSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 269 GTTGKPKGTVHTHAGFPLKAAFD-----AGFGMNIKQGDrVLWVTDMGWMMGPfLLFGSLIN--GATMVMYEgvpDFPEA 341
Cdd:PRK13390 158 GTTGFPKGIQPDLPGRDVDAPGDpivaiARAFYDISESD-IYYSSAPIYHAAP-LRWCSMVHalGGTVVLAK---RFDAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 342 DRLwETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGksnvPIC-NYSGGTEI 420
Cdd:PRK13390 233 ATL-GHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG----PIVyEYYSSTEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 421 SGGIFGNVLIKPIAPISFNASLPGMAAVVlDDQGNPI-RDEVGELCLEKPwvGMTKSFWEDDERYV------NTYWSRFe 493
Cdd:PRK13390 308 HGMTFIDSPDWLAHPGSVGRSVLGDLHIC-DDDGNELpAGRIGTVYFERD--RLPFRYLNDPEKTAaaqhpaHPFWTTV- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 494 nkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSG 572
Cdd:PRK13390 384 -----GDLGSVDEDGYLyLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446729151 573 ELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK13390 459 ELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
96-612 |
1.54e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.61 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 96 ETRTQPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFAS 175
Cdd:PRK12467 524 QHPERPALVFGEQ-----VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 176 DAVMTRVQAAGSKMIITADGFSRRGKV-----VSLKDEVDKACEHCPTVekvvivrHAGNDFTPHNYDFswstlekekpf 250
Cdd:PRK12467 599 DRLAYMLDDSGVRLLLTQSHLLAQLPVpaglrSLCLDEPADLLCGYSGH-------NPEVALDPDNLAY----------- 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 251 vhaeemhsddplmLIYTSGTTGKPKGTVHTHAGFP-LKAAFDAGFGMNIKqgDRVLWVTDMGWMMGPFLLFGSLINGATM 329
Cdd:PRK12467 661 -------------VIYTSGSTGQPKGVAISHGALAnYVCVIAERLQLAAD--DSMLMVSTFAFDLGVTELFGALASGATL 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 330 VM--YEGVPDfpeADRLWETVDKYEITHLGISPTLIRALM--AKGDEYVNKHSLksleVFASTGEPWN-PDPWMWLfetv 404
Cdd:PRK12467 726 HLlpPDCARD---AEAFAALMADQGVTVLKIVPSHLQALLqaSRVALPRPQRAL----VCGGEALQVDlLARVRAL---- 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 405 gKSNVPICNYSGGTEISGGifgnVLIKPI--APISFNAS-----LPGMAAVVLDDQGNPIRDEV-GELC-----LEKPWV 471
Cdd:PRK12467 795 -GPGARLINHYGPTETTVG----VSTYELsdEERDFGNVpigqpLANLGLYILDHYLNPVPVGVvGELYiggagLARGYH 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 472 G---------MTKSFWEDDERYVNTywsrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDV 541
Cdd:PRK12467 870 RrpaltaerfVPDPFGADGGRLYRT-----------GDLARYRADGVIeYLGRMDHQVKIRGFRIELGEIEARLLAQPGV 938
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 542 IEAAAIGVPDDVKGE-VCHCFVVLRDNVT----FSGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK12467 939 REAVVLAQPGDAGLQlVAYLVPAAVADGAehqaTRDELKAQLRQVLPDY----MVPAHLLLLDSLPLTPNGKLDRK 1010
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
24-617 |
1.86e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.61 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 24 SLGYEDyETFYKKSIEETAWFWGEAEKAVGYQWMKPYTEV---------LDLENGTPFAQWYNGGTCnvVESVLSRWLAd 94
Cdd:PRK12467 1510 SLTYAT-DLFEASTIERLAGHWLNLLQGLVADPERRLGELdlldeaerrQILEGWNATHTGYPLARL--VHQLIEDQAA- 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 95 dETRTQPALQYEGEngtskSFTYEELDswvsRVANGLKHAGIEKG----DRVTIYMPMIPETVVAMLAVMKIGAIISPIF 170
Cdd:PRK12467 1586 -ATPEAVALVFGEQ-----ELTYGELN----RRANRLAHRLIALGvgpeVLVGIAVERSLEMVVGLLAILKAGGAYVPLD 1655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 171 SGFASDAVMTRVQAAGSKMIITADgfsrrgkvvslkdevdKACEHCPTVEKV-VIVRHAGNDftphnydfsWstLEKEKP 249
Cdd:PRK12467 1656 PEYPRERLAYMIEDSGIELLLTQS----------------HLQARLPLPDGLrSLVLDQEDD---------W--LEGYSD 1708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 250 FVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAgfPLKAAFDA---GFGMNikQGDRVLWVTDMGWMMGPFLLFGSLING 326
Cdd:PRK12467 1709 SNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHG--ALVNRLCAtqeAYQLS--AADVVLQFTSFAFDVSVWELFWPLING 1784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 327 ATMVMYE-GVPDFPEadRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLeVFAstGEPWNPDPWMWLFETVG 405
Cdd:PRK12467 1785 ARLVIAPpGAHRDPE--QLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRV-VCG--GEALEVEALRPWLERLP 1859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 406 ksNVPICNYSGGTEISggifGNVLIKPI----------APISfnASLPGMAAVVLDDQGNPI-RDEVGELCLEKpwVGMT 474
Cdd:PRK12467 1860 --DTGLFNLYGPTETA----VDVTHWTCrrkdlegrdsVPIG--QPIANLSTYILDASLNPVpIGVAGELYLGG--VGLA 1929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 475 KSFWE----DDERYVNTYWSRFENK-WVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:PRK12467 1930 RGYLNrpalTAERFVADPFGTVGSRlYRTGDLARYRADGVIeYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA 2009
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 549 VpDDVKGEVCHCFVVLRD---------NVTFSGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRRVIKAA 617
Cdd:PRK12467 2010 Q-DGANGKQLVAYVVPTDpglvdddeaQVALRAILKNHLKASLPEY----MVPAHLVFLARMPLTPNGKLDRKALPAP 2082
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
114-612 |
2.10e-18 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. 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: 341311 [Multi-domain] Cd Length: 479 Bit Score: 88.69 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITa 193
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 dgfsrrgkvvslkdevdkaCEHCPTvekvvivrhagndftphNYDFSWSTLEKEKPFVHAE-------EMHSDDPLMLIY 266
Cdd:cd17656 92 -------------------QRHLKS-----------------KLSFNKSTILLEDPSISQEdtsnidyINNSDDLLYIIY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 267 TSGTTGKPKGTVHTHAGFP--LKAAFDAgfgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATM--VMYEGVPDFPEad 342
Cdd:cd17656 136 TSGTTGKPKGVQLEHKNMVnlLHFEREK---TNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyiIREETKRDVEQ-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 343 rLWETVDKYEITHLgISPTLIRALMAKGDEYVN------KHSLKSLEVFASTGEpwnpdpwmwLFETVGKSNVPICNYSG 416
Cdd:cd17656 211 -LFDLVKRHNIEVV-FLPVAFLKFIFSEREFINrfptcvKHIITAGEQLVITNE---------FKEMLHEHNVHLHNHYG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 417 GTEISggIFGNVLIKPIAPISfnaSLP--GMAAV-----VLDDQGNPI-RDEVGELCLEKpwVGMTKSFWEDD----ERY 484
Cdd:cd17656 280 PSETH--VVTTYTINPEAEIP---ELPpiGKPISntwiyILDQEQQLQpQGIVGELYISG--ASVARGYLNRQeltaEKF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 485 VNTYWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCF 561
Cdd:cd17656 353 FPDPFDPNERMYRTGDLARYlpDGNiEFL--GRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAY 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446729151 562 VVLRDNVTFSgelkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17656 431 FVMEQELNIS-----QLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
103-611 |
2.21e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 88.27 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 103 LQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRV 182
Cdd:cd05914 1 LYYGGE-----PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 183 QAAGSKMIITADgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhSDDPL 262
Cdd:cd05914 76 NHSEAKAIFVSD---------------------------------------------------------------EDDVA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 263 MLIYTSGTTGKPKGTVHTHAGfpLKAAFDAGFGMNI-KQGDRVLWVTDMGWMMGpfLLFGSLI---NGATMVMYEGVPDf 338
Cdd:cd05914 93 LINYTSGTTGNSKGVMLTYRN--IVSNVDGVKEVVLlGKGDKILSILPLHHIYP--LTFTLLLpllNGAHVVFLDKIPS- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 339 PEADRLwetvDKYEITHLGISPTL-------IRALMAKGDEYVNKHSLKS----------------------LEVFASTG 389
Cdd:cd05914 168 AKIIAL----AFAQVTPTLGVPVPlviekifKMDIIPKLTLKKFKFKLAKkinnrkirklafkkvheafggnIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 390 EPWNPDpwmwLFETVGKSNVPICNYSGGTEISggifgnvlikPIapISFNaslpGMAAVVLDDQGNPIRD-EV------- 461
Cdd:cd05914 244 AKINPD----VEEFLRTIGFPYTIGYGMTETA----------PI--ISYS----PPNRIRLGSAGKVIDGvEVridspdp 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 462 ----GELCLEKPwvGMTKSFWEDDERYVNTYwsrFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNI-AGKRIGPAEYESI 534
Cdd:cd05914 304 atgeGEIIVRGP--NVMKGYYKNPEATAEAF---DKDGWFHtGDLGKIDAEGYLyIRGRKKEMIVLsSGKNIYPEEIEAK 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 535 LVKHNDVIE-----------AAAIGVPD--DVKGEvchcfvvlrDNVTFSGELKKELMSLVNShigKALCPKDIHVV--- 598
Cdd:cd05914 379 INNMPFVLEslvvvqekklvALAYIDPDflDVKAL---------KQRNIIDAIKWEVRDKVNQ---KVPNYKKISKVkiv 446
|
570
....*....|....
gi 446729151 599 -EDLPKTRNSKVMR 611
Cdd:cd05914 447 kEEFEKTPKGKIKR 460
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
114-612 |
4.15e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 87.96 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 114 SFTYEELDSWVSRVANGL-KHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIT 192
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLqQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 193 ADGFSRRGKVVSLKDEVD-----KACEHCPT------------VEKVVIVRHagndfTPHNYDFSWSTLEKEKPFVHAEE 255
Cdd:PRK12492 129 LNMFGKLVQEVLPDTGIEylieaKMGDLLPAakgwlvntvvdkVKKMVPAYH-----LPQAVPFKQALRQGRGLSLKPVP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 256 MHSDDPLMLIYTSGTTGKPKGTVHTHAGF-----PLKAAF---DAGFGMNIKQGDRVlwvtdmgwMMGPFLLFG------ 321
Cdd:PRK12492 204 VGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanmlQVRACLsqlGPDGQPLMKEGQEV--------MIAPLPLYHiyafta 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 322 ----SLINGATMVMYEGVPDFPEadrLWETVDKYEITHLGISPTLIRALMAkgdeyvnkhslkslevfastgepwNPDpw 397
Cdd:PRK12492 276 ncmcMMVSGNHNVLITNPRDIPG---FIKELGKWRFSALLGLNTLFVALMD------------------------HPG-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 398 mwlFETVGKSNVPICNySGGT-----------EISGGI----FGNVLIKPIA---PISFNASL-------PGMAAVVLDD 452
Cdd:PRK12492 327 ---FKDLDFSALKLTN-SGGTalvkataerweQLTGCTivegYGLTETSPVAstnPYGELARLgtvgipvPGTALKVIDD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 453 QGNPIR-DEVGELCLEKPWVgmTKSFWEDDERyvnTYWSRFENKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPA 529
Cdd:PRK12492 403 DGNELPlGERGELCIKGPQV--MKGYWQQPEA---TAEALDAEGWFKtGDIAVIDPDGFVrIVDRKKDLIIVSGFNVYPN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 530 EYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDnvtfSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:PRK12492 478 EIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARD----PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKI 553
|
...
gi 446729151 610 MRR 612
Cdd:PRK12492 554 LRR 556
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
116-615 |
1.08e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 86.73 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADG 195
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 FsrrgkvVSLkdeVDKACEHCPTVEKVVIVrhAGNDFTP----------------HNYDFSWSTLEKekpfvhaeemhsD 259
Cdd:PRK06018 121 F------VPI---LEKIADKLPSVERYVVL--TDAAHMPqttlknavayeewiaeADGDFAWKTFDE------------N 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFG-MNIKQGDRVLWVTDM----GWMMGpfllFGSLINGATMVMyeg 334
Cdd:PRK06018 178 TAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDaLGTSAADTMLPVVPLfhanSWGIA----FSAPSMGTKLVM--- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 335 vpdfPEAD----RLWETVDKYEITHLGISPTLIRALMakgdEYVNKHSLK--SLEVFASTGEPWnPDPWMWLFETVGksn 408
Cdd:PRK06018 251 ----PGAKldgaSVYELLDTEKVTFTAGVPTVWLMLL----QYMEKEGLKlpHLKMVVCGGSAM-PRSMIKAFEDMG--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 409 VPICNYSGGTEISG-GIFGnVLIKPIAPISFNASLPgmaavVLDDQGNP-------IRDEVGElclEKPWVGMT------ 474
Cdd:PRK06018 319 VEVRHAWGMTEMSPlGTLA-ALKPPFSKLPGDARLD-----VLQKQGYPpfgvemkITDDAGK---ELPWDGKTfgrlkv 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 475 ------KSFWE------DDERYVNTywsrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDV 541
Cdd:PRK06018 390 rgpavaAAYYRvdgeilDDDGFFDT-----------GDVATIDAYGYMrITDRSKDVIKSGGEWISSIDLENLAVGHPKV 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446729151 542 IEAAAIGVPDDVKGEVCHCFVVLRDNVTFSgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK06018 459 AEAAVIGVYHPKWDERPLLIVQLKPGETAT---REEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
113-612 |
2.13e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 85.84 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIG-------------------------AIIs 167
Cdd:PRK07059 47 KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGyvvvnvnplytprelehqlkdsgaeAIV- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 168 pIFSGFAS--DAVMTRVQAagsKMIITA---DGFSRRGKVVSLkdevdkacehcpTVEKVVIVRHAGNdfTPHNYDFSWS 242
Cdd:PRK07059 126 -VLENFATtvQQVLAKTAV---KHVVVAsmgDLLGFKGHIVNF------------VVRRVKKMVPAWS--LPGHVRFNDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 243 TLEKEKPFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFP---------LKAAFDAGfgmniKQGDRVLWVTDMgwm 313
Cdd:PRK07059 188 LAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvlqmeawLQPAFEKK-----PRPDQLNFVCAL--- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 314 mgPFLLFGSLINGATMVMYEG-----VPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFAST 388
Cdd:PRK07059 260 --PLYHIFALTVCGLLGMRTGgrnilIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIVANGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 389 G--------EPWNPDPWMWLFETVGKSN---VPICNYSGGTEISGGIfgnvlikpiapisfNASLPGMAAVVLDDQGN-- 455
Cdd:PRK07059 336 GmavqrpvaERWLEMTGCPITEGYGLSEtspVATCNPVDATEFSGTI--------------GLPLPSTEVSIRDDDGNdl 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 456 PIrDEVGELCLEKPWVgMtKSFWE--DDERYVNTYWSRFENkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYE 532
Cdd:PRK07059 402 PL-GEPGEICIRGPQV-M-AGYWNrpDETAKVMTADGFFRT----GDVGVMDERGYTkIVDRKKDMILVSGFNVYPNEIE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 533 SILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRD-NVTfsgelKKELmslvnshigKALC---------PKDIHVVEDLP 602
Cdd:PRK07059 475 EVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDpALT-----EEDV---------KAFCkerltnykrPKFVEFRTELP 540
|
570
....*....|
gi 446729151 603 KTRNSKVMRR 612
Cdd:PRK07059 541 KTNVGKILRR 550
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
99-586 |
2.94e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.34 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 99 TQPALQYEGENGTSKSFTYE-----ELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI---ISPif 170
Cdd:PRK09274 21 DQLAVAVPGGRGADGKLAYDelsfaELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVpvlVDP-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 171 sGFASDAVMTRVQAAGSKMIITadgfsrrgkvvslkdeVDKAceH---------CPTVEKVVIVrhAGNDFTPhnyDFSW 241
Cdd:PRK09274 99 -GMGIKNLKQCLAEAQPDAFIG----------------IPKA--HlarrlfgwgKPSVRRLVTV--GGRLLWG---GTTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 242 STLEKEKPfVHAEEMH---SDDPLMLIYTSGTTGKPKGTVHTHAGF-----PLKAAFDagfgmnIKQGDRvlwvtDMGwM 313
Cdd:PRK09274 155 ATLLRDGA-AAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFeaqieALREDYG------IEPGEI-----DLP-T 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 314 MGPFLLFG-SLinGATMVmyegVPDF---------PeaDRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLE 383
Cdd:PRK09274 222 FPLFALFGpAL--GMTSV----IPDMdptrpatvdP--AKLFAAIERYGVTNLFGSPALLERLGRYGEA--NGIKLPSLR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 384 VFASTGEPWNPDPWMwLFETVGKSNVPICNYSGGTEisggifgnVLikPIAPISFNASL-------------------PG 444
Cdd:PRK09274 292 RVISAGAPVPIAVIE-RFRAMLPPDAEILTPYGATE--------AL--PISSIESREILfatraatdngagicvgrpvDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 445 MAAVVLDDQGNPI----------RDEVGELCLEKPWVgmTKSFWEDDE--------RYVNTYWSRFenkwvhGDwVVY-D 505
Cdd:PRK09274 361 VEVRIIAISDAPIpewddalrlaTGEIGEIVVAGPMV--TRSYYNRPEatrlakipDGQGDVWHRM------GD-LGYlD 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 506 GEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNS 584
Cdd:PRK09274 432 AQGRLwFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGAQRPVLCVELEPGVACSKSALYQELRALAAA 511
|
..
gi 446729151 585 HI 586
Cdd:PRK09274 512 HP 513
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
116-549 |
1.45e-16 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 82.86 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITadg 195
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 fsrrgkvvSLKDEVDKACEHCPtvEKVVIVRHagndftphnydfswstlekekpfvhaeemhsDDPLMLIYTSGTTGKPK 275
Cdd:cd05939 82 --------NLLDPLLTQSSTEP--PSQDDVNF-------------------------------RDKLFYIYTSGTTGLPK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 276 GTVHTHAGFPLKAAFdAGFGMNIKQGDRV-----LWVTDMGWM-MGPFLLFGSlingaTMVMYEGVpdfpEADRLWETVD 349
Cdd:cd05939 121 AAVIVHSRYYRIAAG-AYYAFGMRPEDVVydclpLYHSAGGIMgVGQALLHGS-----TVVIRKKF----SASNFWDDCV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 350 KYEITHLGISPTLIRALMA-KGDEYVNKHSLKSLevfasTGEPWNPDPWMwlfETVGKSNVP-ICNYSGGTEISGGIfGN 427
Cdd:cd05939 191 KYNCTIVQYIGEICRYLLAqPPSEEEQKHNVRLA-----VGNGLRPQIWE---QFVRRFGIPqIGEFYGATEGNSSL-VN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 428 VLIKpIAPISFNA-SLPGMAAVVL----DDQGNPIRDEVGeLCLE----KPWVGMTKSFWEDDERYVNTYWSRFENK--- 495
Cdd:cd05939 262 IDNH-VGACGFNSrILPSVYPIRLikvdEDTGELIRDSDG-LCIPcqpgEPGLLVGKIIQNDPLRRFDGYVNEGATNkki 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 496 -----------WVHGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGV 549
Cdd:cd05939 340 ardvfkkgdsaFLSGDVLVMDELGYLyFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV 405
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
139-603 |
3.20e-16 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 81.61 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 139 GDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKVVSLKDE--------VD 210
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKLHHLFDVeydarivyLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 211 KACEHCPTVEKVVIVRHAgnDFTPhnydfSWSTLEKekpFVHAEEmhSDDPLMLIYTSGTTGKPKGTVHTHAGF-----P 285
Cdd:cd05909 111 DLRAKISKADKCKAFLAG--KFPP-----KWLLRIF---GVAPVQ--PDDPAVILFTSGSEGLPKGVVLSHKNLlanveQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 286 LKAAFDAgfgmniKQGDRVLWVtdmgwmMGPFLLFG-------SLINGATMVMYegvPDFPEADRLWETVDKYEITHLGI 358
Cdd:cd05909 179 ITAIFDP------NPEDVVFGA------LPFFHSFGltgclwlPLLSGIKVVFH---PNPLDYKKIPELIYDKKATILLG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 359 SPTLIRALMakgdEYVNKHSLKSLEVFASTGEPWNP---DPWMWLFetvgksNVPICNYSGGTEISGGIFGNVLIKPIAP 435
Cdd:cd05909 244 TPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDtlrQEFQEKF------GIRILEGYGTTECSPVISVNTPQSPNKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 436 ISFNASLPGMAAVVLDDQGN-PIRDEVGELCLEKPwVGMTKSFWEDDERYVntywSRFENKW-VHGDWVVYDGEQYI-IT 512
Cdd:cd05909 314 GTVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRG-PNVMLGYLNEPELTS----FAFGDGWyDTGDIGKIDGEGFLtIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 513 GRSDDTLNIAGKRIGPAEYESILVKH--NDViEAAAIGVPDDVKGEVchcfVVLrdnVTFSGELKKELMS--LVNSHIGK 588
Cdd:cd05909 389 GRLSRFAKIAGEMVSLEAIEDILSEIlpEDN-EVAVVSVPDGRKGEK----IVL---LTTTTDTDPSSLNdiLKNAGISN 460
|
490
....*....|....*
gi 446729151 589 ALCPKDIHVVEDLPK 603
Cdd:cd05909 461 LAKPSYIHQVEEIPL 475
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
106-618 |
9.92e-16 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 80.54 E-value: 9.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 106 EGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAA 185
Cdd:cd17641 3 EKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 186 GSKMIITADgfsrrgkvvslKDEVDKACEH---CPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFVHAE-------- 254
Cdd:cd17641 83 GARVVIAED-----------EEQVDKLLEIadrIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRdpglyere 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 255 --EMHSDDPLMLIYTSGTTGKPKGTVHTHAGFplkaafdAGFGMNIKQ------GDRVLWVTDMGWMM------GPFLLF 320
Cdd:cd17641 152 vaAGKGEDVAVLCTTSGTTGKPKLAMLSHGNF-------LGHCAAYLAadplgpGDEYVSVLPLPWIGeqmysvGQALVC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 321 GSLIN----GATMV--MYEGVPDFP-EADRLWETVD-------------KYEITHLGIS---------------PTLIRA 365
Cdd:cd17641 225 GFIVNfpeePETMMedLREIGPTFVlLPPRVWEGIAadvrarmmdatpfKRFMFELGMKlglraldrgkrgrpvSLWLRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 366 LMAKGDEYV-----NKHSLKSLEVFASTGEPWNPDPWMWlFETVGksnVPICNYSGGTEISGGIFgnvlIKPIAPISFNA 440
Cdd:cd17641 305 ASWLADALLfrplrDRLGFSRLRSAATGGAALGPDTFRF-FHAIG---VPLKQLYGQTELAGAYT----VHRDGDVDPDT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 441 SLPGMAavvlddqGNPIR-DEVGELCLEKPwvGMTKSFWEDDERYVNTYwsrFENKWVH-GDWVVYDGE-QYIITGRSDD 517
Cdd:cd17641 377 VGVPFP-------GTEVRiDEVGEILVRSP--GVFVGYYKNPEATAEDF---DEDGWLHtGDAGYFKENgHLVVIDRAKD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 518 TLNIA-GKRIGPAEYESILVKHNDVIEAAAIGvpddvKG-EVCHCFVVLR----------DNVTFSG----ELKKELMSL 581
Cdd:cd17641 445 VGTTSdGTRFSPQFIENKLKFSPYIAEAVVLG-----AGrPYLTAFICIDyaivgkwaeqRGIAFTTytdlASRPEVYEL 519
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 446729151 582 VNSHIGK--------------ALCPKDIHvVEDLPKTRNSKVMRRVIKAAY 618
Cdd:cd17641 520 IRKEVEKvnaslpeaqrirrfLLLYKELD-ADDGELTRTRKVRRGVIAEKY 569
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
260-604 |
1.19e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. 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: 341291 [Multi-domain] Cd Length: 331 Bit Score: 78.50 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDM---GWMMGpflLFGSLINGATMVMyegVP 336
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQAL-LAQALVLAVLQAIDEGTVFLNSGPLfhiGTLMF---TLATFHAGGTNVF---VR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 337 DFpEADRLWETVDKYEITHLGI-SPTL--IRALMAKGdeyvnKHSLKSLEVFASTgEPWN----PDPWMWlfetvgksnv 409
Cdd:cd17636 74 RV-DAEEVLELIEAERCTHAFLlPPTIdqIVELNADG-----LYDLSSLRSSPAA-PEWNdmatVDTSPW---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 410 piCNYSGG---TEISGGIFGNVLIKPIAPISFNASlPGMAAVVLDDQGNPIRD-EVGELCLEKPWVGmtKSFWEDDEryV 485
Cdd:cd17636 137 --GRKPGGygqTEVMGLATFAALGGGAIGGAGRPS-PLVQVRILDEDGREVPDgEVGEIVARGPTVM--AGYWNRPE--V 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 486 NTywSRFENKWVH-GDwvvydgeqyiiTGR--SDDTLNIAGKR----------IGPAEYESILVKHNDVIEAAAIGVPDD 552
Cdd:cd17636 210 NA--RRTRGGWHHtND-----------LGRrePDGSLSFVGPKtrmiksgaenIYPAEVERCLRQHPAVADAAVIGVPDP 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446729151 553 VKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKT 604
Cdd:cd17636 277 RWAQSVKAIVVLKPGASVTEA---ELIEHCRARIASYKKPKSVEFADALPRT 325
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
116-604 |
9.67e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 77.52 E-value: 9.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIItAD 194
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV-AD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 GfsrrgkvvSLKDEVDKACEHCPTVEKVVIV---------RHAGNDFTPHNY---------DFSWSTLEKekpfvhaeem 256
Cdd:PRK05620 119 P--------RLAEQLGEILKECPCVRAVVFIgpsdadsaaAHMPEGIKVYSYealldgrstVYDWPELDE---------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 257 hsDDPLMLIYTSGTTGKPKGTVHTHAGFPLKaafdagfGMNIKQGDRvLWVTD-------------MGWMMgPFLLFGSl 323
Cdd:PRK05620 181 --TTAAAICYSTGTTGAPKGVVYSHRSLYLQ-------SLSLRTTDS-LAVTHgesflccvpiyhvLSWGV-PLAAFMS- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 324 inGATMVmyegvpdFPEADRLWETVDKYEITHL-----GIsPTLIRALMAkgdEYVNKH----SLKSLEVFASTGEPWNP 394
Cdd:PRK05620 249 --GTPLV-------FPGPDLSAPTLAKIIATAMprvahGV-PTLWIQLMV---HYLKNPpermSLQEIYVGGSAVPPILI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 395 DPW----------MW-LFET--VGKSNVPICNYSGGT----EISGGIFgnvlikpiaPISFNASlpgmaaVVLDDQGNPI 457
Cdd:PRK05620 316 KAWeerygvdvvhVWgMTETspVGTVARPPSGVSGEArwayRVSQGRF---------PASLEYR------IVNDGQVMES 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 458 RDE-VGELCLEKPWVgmTKSFWEDD------------ERYVNTYWSRF-ENKWVH-GD--WVVYDGeQYIITGRSDDTLN 520
Cdd:PRK05620 381 TDRnEGEIQVRGNWV--TASYYHSPteegggaastfrGEDVEDANDRFtADGWLRtGDvgSVTRDG-FLTIHDRARDVIR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 521 IAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKALCPKDIHVVED 600
Cdd:PRK05620 458 SGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDE 537
|
....
gi 446729151 601 LPKT 604
Cdd:PRK05620 538 IDKT 541
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
264-612 |
1.10e-14 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. 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: 341299 [Multi-domain] Cd Length: 465 Bit Score: 76.70 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 264 LIYTSGTTGKPKGTVHTHAGF-----PLKAAFDagfgmnIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyegVPD- 337
Cdd:cd17644 111 VIYTSGSTGKPKGVMIEHQSLvnlshGLIKEYG------ITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVL---RPEe 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 338 -FPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKhSLKSLEVFASTGEPWNPDPWMWLFETVGKsNVPICNYSG 416
Cdd:cd17644 182 mRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTID-LPSSLRLVIVGGEAVQPELVRQWQKNVGN-FIQLINVYG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 417 GTEIS-GGIFGNVL---IKPIAPISFNASLPGMAAVVLDDQGNPIRDEV-GELCLEKpwVGMTKSFWEDD----ERYVNT 487
Cdd:cd17644 260 PTEATiAATVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVpGELHIGG--VGLARGYLNRPeltaEKFISH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 488 --YWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFV 562
Cdd:cd17644 338 pfNSSESERLYKTGDLARYlpDGNiEYL--GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYI 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446729151 563 VLRDNVTFSGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17644 416 VPHYEESPSTV---ELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
102-615 |
1.89e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 76.36 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 102 ALQYEgengtSKSFTYEELDSWVSRVANGLkHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTR 181
Cdd:PRK07638 19 AIKEN-----DRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 182 VQAAGSKMIITADGFSRrgkvvslkdevDKACEHCPtvekVVIVRHagndftphnydfsW-STLEKEKPFVHAEEMHSDD 260
Cdd:PRK07638 93 LAISNADMIVTERYKLN-----------DLPDEEGR----VIEIDE-------------WkRMIEKYLPTYAPIENVQNA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 261 PLMLIYTSGTTGKPKGTVHTHAGFplKAAFDAG---FGMniKQGDRVLWVtdmGWMMGPFLLFG---SLINGATMVMyeg 334
Cdd:PRK07638 145 PFYMGFTSGSTGKPKAFLRAQQSW--LHSFDCNvhdFHM--KREDSVLIA---GTLVHSLFLYGaisTLYVGQTVHL--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 335 VPDFPEADRLwETVDKYEITHLGISPTLIRALmAKGDEYVNkHSLKSLevfaSTGEPW---------NPDPWMWLFETVG 405
Cdd:PRK07638 215 MRKFIPNQVL-DKLETENISVMYTVPTMLESL-YKENRVIE-NKMKII----SSGAKWeaeakekikNIFPYAKLYEFYG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 406 KS---------------------------NVPICNySGGTEISGGIFGNVLIKpiAPISFNASLPGMAAVV-LDDQGNPI 457
Cdd:PRK07638 288 ASelsfvtalvdeeserrpnsvgrpfhnvQVRICN-EAGEEVQKGEIGTVYVK--SPQFFMGYIIGGVLAReLNADGWMT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 458 RDEVGelclekpwvgmtksfWEDDERYVntywsrfenkwvhgdwvvydgeqYIItGRSDDTLNIAGKRIGPAEYESILVK 537
Cdd:PRK07638 365 VRDVG---------------YEDEEGFI-----------------------YIV-GREKNMILFGGINIFPEEIESVLHE 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 538 HNDVIEAAAIGVPDDVKGEVCHCFVVLRDNvtfsgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK07638 406 HPAVDEIVVIGVPDSYWGEKPVAIIKGSAT-------KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
247-609 |
2.89e-14 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. 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: 341309 [Multi-domain] Cd Length: 449 Bit Score: 75.59 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 247 EKPFVHAEEMHSDDPL-----MLIYTSGTTGKPKGTVHTHAGF-PLKAAFDAGFGM---NIKQGDRVLwVTDmgwmmgPF 317
Cdd:cd17654 101 APLSFTPEHRHFNIRTdeclaYVIHTSGTTGTPKIVAVPHKCIlPNIQHFRSLFNItseDILFLTSPL-TFD------PS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 318 L--LFGSLINGATMVMyegVPDF--PEADRLWETVDK-YEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPW 392
Cdd:cd17654 174 VveIFLSLSSGATLLI---VPTSvkVLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 393 NPD----PWMwlfetvGKSN-VPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRdevGELCLE 467
Cdd:cd17654 251 PSLvilsSWR------GKGNrTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGT---GQVFLG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 468 kpwvGMTKSFWEDDerYVNTYWSRFENKwvhGDWV-VYDGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDViEAAA 546
Cdd:cd17654 322 ----GLNRVCILDD--EVTVPKGTMRAT---GDFVtVKDGELFFL-GRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCA 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446729151 547 IGVPDDvkgEVCHCFVVLRDNvtfSGELKKEL-MSLVNSHIgkalCPKDIHVVEDLPKTRNSKV 609
Cdd:cd17654 391 VTLSDQ---QRLIAFIVGESS---SSRIHKELqLTLLSSHA----IPDTFVQIDKLPLTSHGKV 444
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
249-616 |
2.90e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 75.87 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 249 PFVHAEEMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAG-FGMNikqGDRVLWVTdMGWMMGPFLLFG---SLI 324
Cdd:PRK07867 142 AEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQrFGLG---PDDVCYVS-MPLFHSNAVMAGwavALA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 325 NGATMVMYegvPDFpEADRLWETVDKYEITHLgisptliralmakgdEYVNKhslkSLEVFASTgePWNPD----PWMWL 400
Cdd:PRK07867 218 AGASIALR---RKF-SASGFLPDVRRYGATYA---------------NYVGK----PLSYVLAT--PERPDdadnPLRIV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 401 FETVGKS----------NVPICNYSGGTEisggifGNVLIKPiAPISFNASL----PGMAAV-----------VLDDQGN 455
Cdd:PRK07867 273 YGNEGAPgdiarfarrfGCVVVDGFGSTE------GGVAITR-TPDTPPGALgplpPGVAIVdpdtgtecppaEDADGRL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 456 PIRDE-VGELC-LEKPwvGMTKSFWEDDE----RYVN-TYWSrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIG 527
Cdd:PRK07867 346 LNADEaIGELVnTAGP--GGFEGYYNDPEadaeRMRGgVYWS--------GDLAYRDADGYAyFAGRLGDWMRVDGENLG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 528 PAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSlVNSHIGKALCPKDIHVVEDLPKTRNS 607
Cdd:PRK07867 416 TAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTATF 494
|
....*....
gi 446729151 608 KVMRRVIKA 616
Cdd:PRK07867 495 KVLKRQLSA 503
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
113-609 |
5.75e-14 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 74.36 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAGIEKGD-RVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:cd17648 11 KRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 TAdgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhSDDPLMLIYTSGTT 271
Cdd:cd17648 91 TN----------------------------------------------------------------STDLAYAIYTSGTT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 272 GKPKGTVHTHAG-FPLKAAFDAGFGMNIKQGDRVLWVTDmgWMMGPFL--LFGSLINGATMVMYEGvPDFPEADRLWETV 348
Cdd:cd17648 107 GKPKGVLVEHGSvVNLRTSLSERYFGRDNGDEAVLFFSN--YVFDFFVeqMTLALLNGQKLVVPPD-EMRFDPDRFYAYI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 349 DKYEITHLGISPTLIralmakgdEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKsnvPICNYSGGTEISggiFGNV 428
Cdd:cd17648 184 NREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAG---LIINAYGPTETT---VTNH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 429 LIKPIAPISFNASL----PGMAAVVLDD--QGNPIrDEVGELCLEKpwVGMTKSFWEDD----ERYV-NTYWS------- 490
Cdd:cd17648 250 KRFFPGDQRFDKSLgrpvRNTKCYVLNDamKRVPV-GAVGELYLGG--DGVARGYLNRPeltaERFLpNPFQTeqerarg 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 491 RFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPD-DVKGEVCHCFVV--- 563
Cdd:cd17648 327 RNARLYKTGDLVRWlpSGElEYL--GRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDaSQAQSRIQKYLVgyy 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446729151 564 LRDNVTFSgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:cd17648 405 LPEPGHVP---ESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
442-612 |
6.11e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 74.64 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 442 LPGMAAVVLDDQGNPIR---DEVGELCLEKPWVgmtksFWEdderYVN----TYWSRFENKWVH-GDWVVYDGEQYI-IT 512
Cdd:PRK07787 299 LAGVETRLVDEDGGPVPhdgETVGELQVRGPTL-----FDG----YLNrpdaTAAAFTADGWFRtGDVAVVDPDGMHrIV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 513 GR-SDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTfsgelKKELMSLVNSHIGKALC 591
Cdd:PRK07787 370 GReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA-----ADELIDFVAQQLSVHKR 444
|
170 180
....*....|....*....|.
gi 446729151 592 PKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK07787 445 PREVRFVDALPRNAMGKVLKK 465
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
124-571 |
1.26e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 74.06 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 124 VSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPI---FSGFASDAVMTRVQAAgskMIITADGfsrrg 200
Cdd:PLN02860 42 VLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLnyrWSFEEAKSAMLLVRPV---MLVTDET----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 201 kVVSLKDEVDKacEHCPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFVHAEEMHS---DDPLMLIYTSGTTGKPKGT 277
Cdd:PLN02860 114 -CSSWYEELQN--DRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDYAwapDDAVLICFTSGTTGRPKGV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 278 VHTHAGFPL----KAAFdAGFGmnikqGDRVLWVTdmgwmmGPFLLFGSLINGATMVMYEG----VPDFpEADRLWETVD 349
Cdd:PLN02860 191 TISHSALIVqslaKIAI-VGYG-----EDDVYLHT------APLCHIGGLSSALAMLMVGAchvlLPKF-DAKAALQAIK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 350 KYEITHLGISPTLIRALMAKGDEYVNKHSlkslevfastgepwnpdpwmwlFETVGKsnvpICNySGGTEISGGIFGNVL 429
Cdd:PLN02860 258 QHNVTSMITVPAMMADLISLTRKSMTWKV----------------------FPSVRK----ILN-GGGSLSSRLLPDAKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 430 IKPIAPIsFNA--------SLPGMA---------AVVLDDQGNPIRDEVGEL---CLEKP------WVGMTKS------- 476
Cdd:PLN02860 311 LFPNAKL-FSAygmteacsSLTFMTlhdptlespKQTLQTVNQTKSSSVHQPqgvCVGKPaphvelKIGLDESsrvgril 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 477 ---------FWEDDeryVNTYWSRFENKWVH-GD--WVVYDGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEA 544
Cdd:PLN02860 390 trgphvmlgYWGQN---SETASVLSNDGWLDtGDigWIDKAGNLWLI-GRSNDRIKTGGENVYPEEVEAVLSQHPGVASV 465
|
490 500
....*....|....*....|....*..
gi 446729151 545 AAIGVPDDVKGEVCHCFVVLRDNVTFS 571
Cdd:PLN02860 466 VVVGVPDSRLTEMVVACVRLRDGWIWS 492
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
97-614 |
1.38e-13 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 73.36 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 97 TRTQPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD 176
Cdd:cd17645 11 TPDHVAVVDRGQ-----SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 177 AVMTRVQAAGSKMIITadgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeem 256
Cdd:cd17645 86 RIAYMLADSSAKILLT---------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 257 HSDDPLMLIYTSGTTGKPKGT-VHTHAGFPLKAAFDAGFGMNikQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyegv 335
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVmIEHHNLVNLCEWHRPYFGVT--PADKSLVYASFSFDASAWEIFPHLTAGAALHV---- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 336 pdFPEADRL-WETVDKYEITHlGISPTLIRALMAKGDEYVNKHSLKsleVFASTGEPWNpdpwmwlfeTVGKSNVPICNY 414
Cdd:cd17645 176 --VPSERRLdLDALNDYFNQE-GITISFLPTGAAEQFMQLDNQSLR---VLLTGGDKLK---------KIERKGYKLVNN 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 415 SGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLdDQGNPIRDE--VGELCLEKPwvGMTKSFW----EDDERYVNTY 488
Cdd:cd17645 241 YGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYIL-DEALQLQPIgvAGELCIAGE--GLARGYLnrpeLTAEKFIVHP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 489 WSRFENKWVHGD---WVVYDGEQYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLR 565
Cdd:cd17645 318 FVPGERMYRTGDlakFLPDGNIEFL--GRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446729151 566 DNVTFsgelkKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:cd17645 396 EEIPH-----EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
113-609 |
1.90e-13 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 73.10 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIG-AIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:PRK10946 47 RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGvAPVNALFSHQRSELNAYASQIEPALLIA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 tadgfSRRGKVVSLKDEVDKACEHCPTVEkVVIVRHagndftpHNYDFSWST-LEKEKPFVHAEEMHSDDPLMLIYTSGT 270
Cdd:PRK10946 127 -----DRQHALFSDDDFLNTLVAEHSSLR-VVLLLN-------DDGEHSLDDaINHPAEDFTATPSPADEVAFFQLSGGS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 271 TGKPKGTVHTHAGF--PLKAAFD-AGFGMNIkqgdRVLWVTDMG--WMMGPFLLFGSLINGATMVMyegVPDfPEADRLW 345
Cdd:PRK10946 194 TGTPKLIPRTHNDYyySVRRSVEiCGFTPQT----RYLCALPAAhnYPMSSPGALGVFLAGGTVVL---APD-PSATLCF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 346 ETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPwnpdpwmwLFETVGKsNVP--------------- 410
Cdd:PRK10946 266 PLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGAR--------LSETLAR-RIPaelgcqlqqvfgmae 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 411 -ICNYSGGTEISGGIF---GNvlikpiaPISfnaslPGMAAVVLDDQGNPI-RDEVGELCLEKPWV--GMTKS------- 476
Cdd:PRK10946 337 gLVNYTRLDDSDERIFttqGR-------PMS-----PDDEVWVADADGNPLpQGEVGRLMTRGPYTfrGYYKSpqhnasa 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 477 FweDDERYvntYWSrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKG 555
Cdd:PRK10946 405 F--DANGF---YCS--------GDLVSIDPDGYItVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446729151 556 EVCHCFVVLRDNVTfSGELKKELMSLvnsHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:PRK10946 472 EKSCAFLVVKEPLK-AVQLRRFLREQ---GIAEFKLPDRVECVDSLPLTAVGKV 521
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
86-624 |
2.09e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 73.12 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 86 SVLSRWLADDETRTQpALQYEGENGTSkSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI 165
Cdd:PRK05857 15 TVLDRVFEQARQQPE-AIALRRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 166 iSPIFSGFASDAVMTRV-QAAGSKMIITADGfsrrGKVVSlkdevDKACEHCPTVEKVVIVRHAGNDFTPHNYDFSWSTL 244
Cdd:PRK05857 93 -AVMADGNLPIAAIERFcQITDPAAALVAPG----SKMAS-----SAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 245 EKEkpfvhaeeMHSDDPLMLIYTSGTTGKPKGTVHTHAGFplkaafdagFGM-NIKQGDRVLWVTdmgWMMG-------P 316
Cdd:PRK05857 163 NAD--------QGSEDPLAMIFTSGTTGEPKAVLLANRTF---------FAVpDILQKEGLNWVT---WVVGettysplP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 317 FLLFGSLINGATMVMYEG--VPDFPEADRLWETVDKYEITHLGISPTLIRALMAKgdeyvnkhsLKslevFASTGEPwnp 394
Cdd:PRK05857 223 ATHIGGLWWILTCLMHGGlcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSE---------LK----SANATVP--- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 395 dpwmwlfetvgksNVPICNYSGGTEISGGI-FGNVLIKPIAPIsFNASLPGMAAVVL-DDQGNPIRDEVGELCLEKPWV- 471
Cdd:PRK05857 287 -------------SLRLVGYGGSRAIAADVrFIEATGVRTAQV-YGLSETGCTALCLpTDDGSIVKIEAGAVGRPYPGVd 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 472 ----------------GMTKSF---WEDDERYVNTYWSRFE-------NKWVH-GDWVVY--DGEQYiITGRSDDTLNIA 522
Cdd:PRK05857 353 vylaatdgigptapgaGPSASFgtlWIKSPANMLGYWNNPErtaevliDGWVNtGDLLERreDGFFY-IKGRSSEMIICG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 523 GKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSG--ELKKELMSLVNSHIGKALCPKDIHVVED 600
Cdd:PRK05857 432 GVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAarALKHTIAARFRRESEPMARPSTIVIVTD 511
|
570 580
....*....|....*....|....
gi 446729151 601 LPKTRNSKVMRRVIKAAYLGKELG 624
Cdd:PRK05857 512 IPRTQSGKVMRASLAAAATADKAR 535
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
30-85 |
3.87e-13 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 64.03 E-value: 3.87e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 30 YETFYKKSIEETAWFWGEAEKAVgyQWMKPYTEVLDLENGtPFAQWYNGGTCNVVE 85
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKEL--DWFKPFDKVLDGSNG-PFAKWFVGGKLNVCY 53
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
105-573 |
4.74e-12 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 68.86 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 105 YEGEngtskSFTYEELDSWVSRVANGLK-HAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQ 183
Cdd:cd05938 1 FEGE-----TYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 184 AAGSKMIITADgfsrrgkvvSLKDEVDkacEHCPTV-EKVVIVRHAGNDFTPHNYDfswSTLEKEK-------PFVHAEE 255
Cdd:cd05938 76 CCGAKVLVVAP---------ELQEAVE---EVLPALrADGVSVWYLSHTSNTEGVI---SLLDKVDaasdepvPASLRAH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 256 MHSDDPLMLIYTSGTTGKPKGTVHTHagfpLKAAFDAGFGMNIK-QGDRVLWVT-----DMGWMMGpflLFGSLINGATM 329
Cdd:cd05938 141 VTIKSPALYIYTSGTTGLPKAARISH----LRVLQCSGFLSLCGvTADDVIYITlplyhSSGFLLG---IGGCIELGATC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 330 VMYegvPDFpEADRLWETVDKYEITHLGISPTLIRAL--MAKGDEYVNkHSlksleVFASTGEPWNPDPWMWLFETVGks 407
Cdd:cd05938 214 VLK---PKF-SASQFWDDCRKHNVTVIQYIGELLRYLcnQPQSPNDRD-HK-----VRLAIGNGLRADVWREFLRRFG-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 408 NVPICNYSGGTEISGGIF-----------GNVLIKPIAPISFNASLPGMAAVVLDDQGNPIRDEVGE--LCLEK-----P 469
Cdd:cd05938 282 PIRIREFYGSTEGNIGFFnytgkigavgrVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEpgLLVAKitqqsP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 470 WVGMTKS------------FWEDDeRYVNTywsrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILV 536
Cdd:cd05938 362 FLGYAGDkeqtekkllrdvFKKGD-VYFNT-----------GDLLVQDQQNFLyFHDRVGDTFRWKGENVATTEVADVLG 429
|
490 500 510
....*....|....*....|....*....|....*...
gi 446729151 537 KHNDVIEAAAIGVP-DDVKGEVCHCFVVLRDNVTFSGE 573
Cdd:cd05938 430 LLDFLQEVNVYGVTvPGHEGRIGMAAVKLKPGHEFDGK 467
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
253-616 |
4.53e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 65.82 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 253 AEEMHSDDPLMLIYTSGTTGKPKGTVHTHaGFPLKAAFDAGFGMNIKQGDrVLWVTdMGWMMGPFLLFG---SLINGATM 329
Cdd:PRK13388 144 HREVDAMDPFMLIFTSGTTGAPKAVRCSH-GRLAFAGRALTERFGLTRDD-VCYVS-MPLFHSNAVMAGwapAVASGAAV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 330 VMyegVPDFpEADRLWETVDKYEITHL---GISPTLIRALMAKGDE--------YVNKHSLKSLEVFAStgepwnpdpwm 398
Cdd:PRK13388 221 AL---PAKF-SASGFLDDVRRYGATYFnyvGKPLAYILATPERPDDadnplrvaFGNEASPRDIAEFSR----------- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 399 wlfetvgKSNVPICNYSGGTEisGGifGNVLIKPIAPI-SFNASLPGMAAV-----------VLDDQG---NPirDE-VG 462
Cdd:PRK13388 286 -------RFGCQVEDGYGSSE--GA--VIVVREPGTPPgSIGRGAPGVAIYnpetltecavaRFDAHGallNA--DEaIG 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 463 ELcLEKPWVGMTKSFWEDD----ERYVN-TYWSrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILV 536
Cdd:PRK13388 353 EL-VNTAGAGFFEGYYNNPeataERMRHgMYWS--------GDLAYRDADGWIyFAGRTADWMRVDGENLSAAPIERILL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 537 KHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFS-GELKKELMSlvNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK13388 424 RHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDpDAFAAFLAA--QPDLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
.
gi 446729151 616 A 616
Cdd:PRK13388 502 A 502
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
113-548 |
1.30e-10 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 63.92 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispifsgfasDAVmtrvqaagskmiit 192
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV----------DVV-------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 193 adgfsrRGKVVSLKdevdkacehcptvEKVVIVRHAGNDFTphnydfswstlekekpFVhaeEMHSDDPLMLIYTSGTTG 272
Cdd:cd17640 60 ------RGSDSSVE-------------ELLYILNHSESVAL----------------VV---ENDSDDLATIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 273 KPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMgWMMGPFLLFGSLINGATMVMYEGVPDFPE------------ 340
Cdd:cd17640 102 NPKGVMLTHANL-LHQIRSLSDIVPPQPGDRFLSILPI-WHSYERSAEYFIFACGCSQAYTSIRTLKDdlkrvkphyivs 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 341 ADRLWETVDKYEITHLGISPTLIRALMakgdeyvnkHSLKSLE--VFASTGEPWNPDPWMWLFETVGksnVPICNYSGGT 418
Cdd:cd17640 180 VPRLWESLYSGIQKQVSKSSPIKQFLF---------LFFLSGGifKFGISGGGALPPHVDTFFEAIG---IEVLNGYGLT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 419 EISGGIFGNVLIKPIAPiSFNASLPGMAAVVLDDQGNPI--RDEVGELCLEKPWVgmTKSFWEDDERyvnTYWSRFENKW 496
Cdd:cd17640 248 ETSPVVSARRLKCNVRG-SVGRPLPGTEIKIVDPEGNVVlpPGEKGIVWVRGPQV--MKGYYKNPEA---TSKVLDSDGW 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446729151 497 VH-GD--WVVYDGEqYIITGRSDDTLNIA-GKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:cd17640 322 FNtGDlgWLTCGGE-LVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
100-282 |
1.45e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 64.15 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 100 QPALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIG-AIIsPIFSGFASDAV 178
Cdd:PRK04813 18 FPAYDYLGE-----KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhAYI-PVDVSSPAERI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 179 MTRVQAAGSKMIITADGFsrrgkvvslkdevDKACEHCPTVEKVVIVRHAGNDFTphnYDFSwstlekekpfvHAeeMHS 258
Cdd:PRK04813 92 EMIIEVAKPSLIIATEEL-------------PLEILGIPVITLDELKDIFATGNP---YDFD-----------HA--VKG 142
|
170 180
....*....|....*....|....
gi 446729151 259 DDPLMLIYTSGTTGKPKGTVHTHA 282
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHD 166
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
116-611 |
1.61e-10 |
|
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: 63.63 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIisPIFSgfasDAVMTRvqaagskmiitadg 195
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV--PVLI----DPGMGR-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 fsrrgkvvslkdevdKACEHCptvekvvivrhagndftphnydfswstLEKEKPFVHAEEMHSDDPLMLIYTSGTTGKPK 275
Cdd:cd05910 64 ---------------KNLKQC---------------------------LQEAEPDAFIGIPKADEPAAILFTSGSTGTPK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 276 GTVHTHAGFplKAAFDA-GFGMNIKQGDRVLWVtdmgwmMGPFLLFGSLInGATMVMYEGVPDFP-EAD--RLWETVDKY 351
Cdd:cd05910 102 GVVYRHGTF--AAQIDAlRQLYGIRPGEVDLAT------FPLFALFGPAL-GLTSVIPDMDPTRPaRADpqKLVGAIRQY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 352 EITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWnPDPWMWLFETVGKSNVPICNYSGGTE---ISgGIFGNV 428
Cdd:cd05910 173 GVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPV-PIALAARLRKMLSDEAEILTPYGATEalpVS-SIGSRE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 429 LIKPIAPISFNAS-------LPGMAAVVLDDQGNPIRD----------EVGELCLEKPWV-----------GMTKSfWED 480
Cdd:cd05910 249 LLATTTAATSGGAgtcvgrpIPGVRVRIIEIDDEPIAEwddtlelprgEIGEITVTGPTVtptyvnrpvatALAKI-DDN 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 481 DERyvntYWSRFenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCH 559
Cdd:cd05910 328 SEG----FWHRM------GDLGYLDDEGRLwFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729151 560 CFVVLRDNVTFSGELKKELMSLVNSH-----IGKALC----PKDIHvvedlpktRNSKVMR 611
Cdd:cd05910 398 CVEPLPGTITPRARLEQELRALAKDYphtqrIGRFLIhpsfPVDIR--------HNAKIFR 450
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
113-615 |
2.66e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 63.22 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 113 KSFTYEELDSWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:cd05937 4 KTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 192 TADgfsrrgkvvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfvhaeemhsDDPLMLIYTSGTT 271
Cdd:cd05937 84 VDP----------------------------------------------------------------DDPAILIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 272 GKPKGTVHThAGFPLKAAFDAGFGMNIKQGDRvlWVTDMGWMMGPFLLFG---SLINGATMVMyegVPDFpEADRLWETV 348
Cdd:cd05937 100 GLPKAAAIS-WRRTLVTSNLLSHDLNLKNGDR--TYTCMPLYHGTAAFLGacnCLMSGGTLAL---SRKF-SASQFWKDV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 349 DKYEITHLGISPTLIRALMAKGDE-YVNKHSLKslevfASTGEPWNPDPWMWLFEtvgKSNVP-ICNYSGGTEisgGIFG 426
Cdd:cd05937 173 RDSGATIIQYVGELCRYLLSTPPSpYDRDHKVR-----VAWGNGLRPDIWERFRE---RFNVPeIGEFYAATE---GVFA 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 427 --NVLIKP--IAPISFNASL------PGMAAVVLD-DQGNPIRD------------EVGELCLEKPW--VGMTKSFWEDD 481
Cdd:cd05937 242 ltNHNVGDfgAGAIGHHGLIrrwkfeNQVVLVKMDpETDDPIRDpktgfcvrapvgEPGEMLGRVPFknREAFQGYLHNE 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 482 E----RYVNTYWSRFENKWVHGDWVVYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGV--PDDvK 554
Cdd:cd05937 322 DatesKLVRDVFRKGDIYFRTGDLLRQDADgRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvPGH-D 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729151 555 GEVCHCFVVLRDNVTFSGELKK-ELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05937 401 GRAGCAAITLEESSAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
75-281 |
2.79e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 63.46 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 75 WYNGGTC-------------------NVVESVLSRWLADDETRTQPaLQYEGENGTsKSFTYEELDSWVSRVANGLKHAG 135
Cdd:PTZ00216 65 WYYGPNFlqrlerickergdrralayRPVERVEKEVVKDADGKERT-MEVTHFNET-RYITYAELWERIVNFGRGLAELG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 136 IEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITadGFSRRGKVVSLKDEvdKACEH 215
Cdd:PTZ00216 143 LTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC--NGKNVPNLLRLMKS--GGMPN 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729151 216 CPtvekVVIVRHAGNDFTPHNYD-FSWSTLEKEKPFVHAEEMHS----DDPLMLI-YTSGTTGKPKGTVHTH 281
Cdd:PTZ00216 219 TT----IIYLDSLPASVDTEGCRlVAWTDVVAKGHSAGSHHPLNipenNDDLALImYTSGTTGDPKGVMHTH 286
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
209-611 |
4.80e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.42 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 209 VDKACEHCPTVEKVVIV---RHAGNDFTP----------HNYDFSWSTLEkekpfvhaEEMHSDdplmLIYTSGTTGKPK 275
Cdd:PRK07008 125 VDALAPQCPNVKGWVAMtdaAHLPAGSTPllcyetlvgaQDGDYDWPRFD--------ENQASS----LCYTSGTTGNPK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 276 GTVHTHAGFPLKAaFDAGF--GMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVmyegvpdFPEAD----RLWETVD 349
Cdd:PRK07008 193 GALYSHRSTVLHA-YGAALpdAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLV-------LPGPDldgkSLYELIE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 350 KYEITHLGISPTLIRALMakgdEYVNKHSLKsLEVFAST--GEPWNPDPWMWLFETVgkSNVPICNYSGGTEISG-GIFG 426
Cdd:PRK07008 265 AERVTFSAGVPTVWLGLL----NHMREAGLR-FSTLRRTviGGSACPPAMIRTFEDE--YGVEVIHAWGMTEMSPlGTLC 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 427 NVLIKpiapisfNASLPGMAAV-VLDDQGNPI----RDEVGELCLEKPWVGmtKSF--------WEDDeRYVNTYWSRFE 493
Cdd:PRK07008 338 KLKWK-------HSQLPLDEQRkLLEKQGRVIygvdMKIVGDDGRELPWDG--KAFgdlqvrgpWVID-RYFRGDASPLV 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 494 NKWVH-GDWVVYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFS 571
Cdd:PRK07008 408 DGWFPtGDVATIDADGFMqITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT 487
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446729151 572 GElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PRK07008 488 RE---ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQK 524
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
101-616 |
4.88e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.26 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 101 PALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK05691 2205 PALTFAGQ-----TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHY 2279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 181 RVQAAGSKMIIT-ADGFSRRGKvvsLKDEVDKACehcptvekvvivrhagndftphnydfswstLEKEKPFVHAeemHSD 259
Cdd:PRK05691 2280 MIEDSGIGLLLSdRALFEALGE---LPAGVARWC------------------------------LEDDAAALAA---YSD 2323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 260 DPL----------MLIYTSGTTGKPKGTVHTHAGFPLK-AAFDAGFGMniKQGDRVLWVTDMGWMMGPFLLFGSLINGAT 328
Cdd:PRK05691 2324 APLpflslpqhqaYLIYTSGSTGKPKGVVVSHGEIAMHcQAVIERFGM--RADDCELHFYSINFDAASERLLVPLLCGAR 2401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 329 MVMY-EGVPDfpeADRLWETVDKYEITHLGISPT----LIRALMAKGDEYVNKHSLKSLEvfASTGEPWnpdpwmwlfET 403
Cdd:PRK05691 2402 VVLRaQGQWG---AEEICQLIREQQVSILGFTPSygsqLAQWLAGQGEQLPVRMCITGGE--ALTGEHL---------QR 2467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 404 VGKSNVP--ICNYSGGTEisggifgnVLIKPIAPISFN------ASLP------GMAAVVLDDQGNPI-RDEVGELCL-- 466
Cdd:PRK05691 2468 IRQAFAPqlFFNAYGPTE--------TVVMPLACLAPEqleegaASVPigrvvgARVAYILDADLALVpQGATGELYVgg 2539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 467 --------EKPwvGMTKsfweddERYV-NTYWSRFENKWVHGDWVVY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESI 534
Cdd:PRK05691 2540 aglaqgyhDRP--GLTA------ERFVaDPFAADGGRLYRTGDLVRLraDGLvEYV--GRIDHQVKIRGFRIELGEIESR 2609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 535 LVKHNDVIEAA--AIGVPD--DVKGEVChCFVVLRDNVTfSGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVM 610
Cdd:PRK05691 2610 LLEHPAVREAVvlALDTPSgkQLAGYLV-SAVAGQDDEA-QAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLD 2687
|
....*.
gi 446729151 611 RRVIKA 616
Cdd:PRK05691 2688 RRALPA 2693
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
62-555 |
5.74e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.88 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 62 EVLDLENGTPFAQWyNGGTCNVVESVLSRWLaDDETRTQP---ALQYEGEngtskSFTYEELDSWVSRVANGLKHAGIEK 138
Cdd:PRK05691 1108 QLLDAAERAQLAQW-GQAPCAPAQAWLPELL-NEQARQTPeriALVWDGG-----SLDYAELHAQANRLAHYLRDKGVGP 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 139 GDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGfsrrgkvvslkdevdkACEHCPT 218
Cdd:PRK05691 1181 DVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSH----------------LLERLPQ 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 219 VEKVVIVRHAGNDFTphnydfSWSTlekEKPFVHaeeMHSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAF-DAGFGMN 297
Cdd:PRK05691 1245 AEGVSAIALDSLHLD------SWPS---QAPGLH---LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWmQATYALD 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 298 ikQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEyVNKH 377
Cdd:PRK05691 1313 --DSDVLMQKAPISFDVSVWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA-AACT 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 378 SLKSLevFaSTGEPWNPD---------PWMWLFETVGKSNVPI------CNYSGGtEIS--GGIFGNVLIKpiapisfna 440
Cdd:PRK05691 1389 SLRRL--F-SGGEALPAElrnrvlqrlPQVQLHNRYGPTETAInvthwqCQAEDG-ERSpiGRPLGNVLCR--------- 1455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 441 slpgmaavVLDDQGNPI-RDEVGELCLEKpwVGMTKSFW----EDDERYV-NTYWSRFENKWVHGD---WVVYDGEQYIi 511
Cdd:PRK05691 1456 --------VLDAELNLLpPGVAGELCIGG--AGLARGYLgrpaLTAERFVpDPLGEDGARLYRTGDrarWNADGALEYL- 1524
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729151 512 tGRSDDTLNIAGKRIGPAEYESILVKHnDVIEAAAIGVPDDVKG 555
Cdd:PRK05691 1525 -GRLDQQVKLRGFRVEPEEIQARLLAQ-PGVAQAAVLVREGAAG 1566
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
85-618 |
9.49e-10 |
|
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: 61.53 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 85 ESVLSRWLADDETRTqpaLQYEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGA 164
Cdd:cd05906 13 LELLLRAAERGPTKG---ITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 165 I--ISPIFSgfASDAVMTRV-------QAAGSKMIITADgfsrrgkvvSLKDEVDKACEHCPTVEKVVIVRHAGNDFtph 235
Cdd:cd05906 90 VpaPLTVPP--TYDEPNARLrklrhiwQLLGSPVVLTDA---------ELVAEFAGLETLSGLPGIRVLSIEELLDT--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 236 nydfswstlEKEKPFVHAEemhSDDPLMLIYTSGTTGKPKGTVHTHAGfpLKAAFDAGFGMNIKQGDRVLwvtdMGWMmg 315
Cdd:cd05906 156 ---------AADHDLPQSR---PDDLALLMLTSGSTGFPKAVPLTHRN--ILARSAGKIQHNGLTPQDVF----LNWV-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 316 PFLLFGSLINGATMVMYEG-----VP--DFPEADRLW-ETVDKYEITHlGISP----TLIRALMAKGDEYvnKHSLKSLE 383
Cdd:cd05906 216 PLDHVGGLVELHLRAVYLGcqqvhVPteEILADPLRWlDLIDRYRVTI-TWAPnfafALLNDLLEEIEDG--TWDLSSLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 384 VFASTGEPWNPDPWMWLFETVGKSNVP---ICNYSGGTEI-SGGIFGNVLIKPIAP-----ISFNASLPGMAAVVLDDQG 454
Cdd:cd05906 293 YLVNAGEAVVAKTIRRLLRLLEPYGLPpdaIRPAFGMTETcSGVIYSRSFPTYDHSqalefVSLGRPIPGVSMRIVDDEG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 455 NPI-RDEVGELCLEKPWVgmTKSFWEDD----ERYVNTYWsrFENkwvhGDW-VVYDGEQYiITGRSDDTLNIAGKRIGP 528
Cdd:cd05906 373 QLLpEGEVGRLQVRGPVV--TKGYYNNPeanaEAFTEDGW--FRT----GDLgFLDNGNLT-ITGRTKDTIIVNGVNYYS 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 529 AEYESILVKHNDVIE----AAAIGVPDDVKGEVCHCFVVLRDNVTFSGELKKELMSLVNSHIGKALcpkdIHVV----ED 600
Cdd:cd05906 444 HEIEAAVEEVPGVEPsftaAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVGVSP----AYLIplpkEE 519
|
570
....*....|....*...
gi 446729151 601 LPKTRNSKVMRRVIKAAY 618
Cdd:cd05906 520 IPKTSLGKIQRSKLKAAF 537
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
98-618 |
9.73e-10 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 61.43 E-value: 9.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 98 RTQPALqyegENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPI-------- 169
Cdd:PRK07514 16 RDAPFI----ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLntaytlae 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 170 ---FSGFASDAVM-----------TRVQAAGSKMIITADGfSRRGkvvSLKDEVDKACEHCPTVEKvvivrhagndftph 235
Cdd:PRK07514 92 ldyFIGDAEPALVvcdpanfawlsKIAAAAGAPHVETLDA-DGTG---SLLEAAAAAPDDFETVPR-------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 236 nydfswstlekekpfvhaeemHSDDPLMLIYTSGTTGKPKGTVHTHAgfplkaafdagfgmNIKQGDRVL---WvtdmGW 312
Cdd:PRK07514 154 ---------------------GADDLAAILYTSGTTGRSKGAMLSHG--------------NLLSNALTLvdyW----RF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 313 MMGPFL-----------LF----GSLINGATMV------------------MYEGVPDFpeadrlwetvdkYeiTHLGIS 359
Cdd:PRK07514 195 TPDDVLihalpifhthgLFvatnVALLAGASMIflpkfdpdavlalmpratVMMGVPTF------------Y--TRLLQE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 360 PTLIRALMAKGDEYVNKHSLKSLEVF----ASTGEPwnpdpwmwLFETVGKS--NVPICN-YSGgtEISGGIFGnvliKP 432
Cdd:PRK07514 261 PRLTREAAAHMRLFISGSAPLLAETHrefqERTGHA--------ILERYGMTetNMNTSNpYDG--ERRAGTVG----FP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 433 iapisfnasLPGMAAVVLD-DQGNPI-RDEVGELCLEKPWVgmTKSFWEDDERyvnTYWSRFENKW-VHGDWVVYDGEQY 509
Cdd:PRK07514 327 ---------LPGVSLRVTDpETGAELpPGEIGMIEVKGPNV--FKGYWRMPEK---TAEEFRADGFfITGDLGKIDERGY 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 510 I-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGK 588
Cdd:PRK07514 393 VhIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEA---AILAALKGRLAR 469
|
570 580 590
....*....|....*....|....*....|..
gi 446729151 589 ALCPKDIHVVEDLPktRNS--KVMRRVIKAAY 618
Cdd:PRK07514 470 FKQPKRVFFVDELP--RNTmgKVQKNLLREQY 499
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
116-282 |
1.92e-09 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 60.31 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIE--KGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 194 DGFsrrgKVVSLKDEVDKACEHcptvekvvIVRHagndftphnydfswstlEKEKPfvhaeemhsDDPLMLIYTSGTTGK 273
Cdd:cd05927 87 AGV----KVYSLEEFEKLGKKN--------KVPP-----------------PPPKP---------EDLATICYTSGTTGN 128
|
....*....
gi 446729151 274 PKGTVHTHA 282
Cdd:cd05927 129 PKGVMLTHG 137
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
116-328 |
3.74e-09 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 59.78 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLK-HAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI---- 190
Cdd:cd17632 69 TYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLavsa 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 191 --------ITADGFSRRGKVV--------SLKDEVDKACEHCPTVEKVVIVRHAGNDftphnydfSWSTLEKEKPFvhAE 254
Cdd:cd17632 149 ehldlaveAVLEGGTPPRLVVfdhrpevdAHRAALESARERLAAVGIPVTTLTLIAV--------RGRDLPPAPLF--RP 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446729151 255 EMHSDDPLMLIYTSGTTGKPKGTVHTHagfplKAAFDAGFGMNIKQGDR-----VLWVTDMGWMMGPFLLFGSLINGAT 328
Cdd:cd17632 219 EPDDDPLALLIYTSGSTGTPKGAMYTE-----RLVATFWLKVSSIQDIRppasiTLNFMPMSHIAGRISLYGTLARGGT 292
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
97-299 |
1.00e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 58.19 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 97 TRTQPalqyEGENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD 176
Cdd:PLN02736 65 TRIRV----DGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 177 AVMTRVQAAGSKMI-ITADGFSrrgKVVSLKDEvdkacehCPTVEKVVIVRHAGNDFTPHNYD-----FSWSTLEKE--- 247
Cdd:PLN02736 141 AVKFIVNHAEVAAIfCVPQTLN---TLLSCLSE-------IPSVRLIVVVGGADEPLPSLPSGtgveiVTYSKLLAQgrs 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446729151 248 --KPFVHAEEmhsDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAafdAGFGMNIK 299
Cdd:PLN02736 211 spQPFRPPKP---EDVATICYTSGTTGTPKGVVLTHGNLIANV---AGSSLSTK 258
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
513-617 |
5.32e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 55.43 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 513 GRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGE-VCHCFVVlrDNVTFSGELKKELMSLVNSHigkaLC 591
Cdd:PRK08308 311 GRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKVIS--HEEIDPVQLREWCIQHLAPY----QV 384
|
90 100
....*....|....*....|....*.
gi 446729151 592 PKDIHVVEDLPKTRNSKVMRRVIKAA 617
Cdd:PRK08308 385 PHEIESVTEIPKNANGKVSRKLLELG 410
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
116-281 |
8.76e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 55.30 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIItadg 195
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 fsrrgkvvslkdevdkaCEHCPtvekvvivrhagndftphnydfswstlekekpfvhaeemhsDDPLMLIYTSGTTGKPK 275
Cdd:cd17639 83 -----------------TDGKP-----------------------------------------DDLACIMYTSGSTGNPK 104
|
....*.
gi 446729151 276 GTVHTH 281
Cdd:cd17639 105 GVMLTH 110
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
116-282 |
4.74e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 53.20 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM-----TRVQA--AGSK 188
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALChslneTEVTTviCDSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 189 MIitadgfsrrGKVVSLKDEVDkacehcpTVEKVVIVRHAGNDFTPHNYD------FSWSTLEK---EKPfVHAEEMHSD 259
Cdd:PLN02387 188 QL---------KKLIDISSQLE-------TVKRVIYMDDEGVDSDSSLSGssnwtvSSFSEVEKlgkENP-VDPDLPSPN 250
|
170 180
....*....|....*....|...
gi 446729151 260 DPLMLIYTSGTTGKPKGTVHTHA 282
Cdd:PLN02387 251 DIAVIMYTSGSTGLPKGVMMTHG 273
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
511-620 |
4.87e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 52.35 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 511 ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVVLRDNVTFSGElkkELMSLVNSHIGKAL 590
Cdd:PRK07824 251 VLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE---ALRAHVARTLDRTA 327
|
90 100 110
....*....|....*....|....*....|
gi 446729151 591 CPKDIHVVEDLPKTRNSKVMRRVIKAAYLG 620
Cdd:PRK07824 328 APRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
116-282 |
6.60e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 52.54 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAV----------MTRVQAA 185
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVefiinhaevsIAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 186 GSKMIITA--------DGFSRRGKVVS-LKDEVDKACEHCptvekvvivrhagndftphnydFSWS------TLEKEKPf 250
Cdd:PLN02861 159 KISSILSClpkcssnlKTIVSFGDVSSeQKEEAEELGVSC----------------------FSWEefslmgSLDCELP- 215
|
170 180 190
....*....|....*....|....*....|..
gi 446729151 251 vhaeEMHSDDPLMLIYTSGTTGKPKGTVHTHA 282
Cdd:PLN02861 216 ----PKQKTDICTIMYTSGTTGEPKGVILTNR 243
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
488-611 |
5.77e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 49.22 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 488 YWSRFEN---KWVHGDWVVYDGEQY-IITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDDVKGEVCHCFVV 563
Cdd:PRK07445 315 YYPQILDsqgIFETDDLGYLDAQGYlHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV 394
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446729151 564 LRDNVTFSGELKkelmSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PRK07445 395 PKDPSISLEELK----TAIKDQLSPFKQPKHWIPVPQLPRNPQGKINR 438
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
116-278 |
8.33e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 48.86 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIitadg 195
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIV----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 196 FSRRGKVVSLKDEVDKACEHCPTV--------------EKVVIVRHAGNDFTP----HNYDfswstLEKEKPfvhaeemh 257
Cdd:PLN02614 156 FVEEKKISELFKTCPNSTEYMKTVvsfggvsreqkeeaETFGLVIYAWDEFLKlgegKQYD-----LPIKKK-------- 222
|
170 180
....*....|....*....|.
gi 446729151 258 sDDPLMLIYTSGTTGKPKGTV 278
Cdd:PLN02614 223 -SDICTIMYTSGTTGDPKGVM 242
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
112-169 |
1.10e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 48.91 E-value: 1.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446729151 112 SKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPI 169
Cdd:TIGR03443 268 TRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVI 325
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
107-186 |
2.30e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 47.51 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 107 GENGTSKSFTYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGA---IISP--------IFSGFAS 175
Cdd:cd17647 13 LNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGAtfsVIDPaypparqnIYLGVAK 92
|
90
....*....|.
gi 446729151 176 DAVMTRVQAAG 186
Cdd:cd17647 93 PRGLIVIRAAG 103
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
257-603 |
4.13e-05 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 46.84 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 257 HSDDPLMLIYTSGTTGKPKGTVHTHagFPLKAafdagfgmNIKQGDRVLWVTDMGWMMG--PFL--------LFGSLING 326
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSH--HNILS--------NIEQISDVFNLRNDDVILSslPFFhsfgltvtLWLPLLEG 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 327 ATMVMyegVPDFPEADRLWETVDKYEITHLGISPTLIRAlmakgdeYVNKHSLKSLEvFAS-----TG-EPWNPDpwmwL 400
Cdd:PRK08633 850 IKVVY---HPDPTDALGIAKLVAKHRATILLGTPTFLRL-------YLRNKKLHPLM-FASlrlvvAGaEKLKPE----V 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 401 ---FETvgKSNVPICNYSGGTEISGGIFGN---VLIKPIAPISFNAS------LPGMAAVVLD-DQGNPIRD-EVGELCL 466
Cdd:PRK08633 915 adaFEE--KFGIRILEGYGATETSPVASVNlpdVLAADFKRQTGSKEgsvgmpLPGVAVRIVDpETFEELPPgEDGLILI 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 467 EKPWVgMtKSFWEDDE------------RYVNTywsrfenkwvhGDWVVYDGEQYI-ITGRSDDTLNIAGKRI--GPAEY 531
Cdd:PRK08633 993 GGPQV-M-KGYLGDPEktaevikdidgiGWYVT-----------GDKGHLDEDGFLtITDRYSRFAKIGGEMVplGAVEE 1059
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729151 532 ESILVKHNDVIEAAAIGVPDDVKGEVchcFVVLRDNVTFSGELKKELMSlvNSHIGKALCPKDIHVVEDLPK 603
Cdd:PRK08633 1060 ELAKALGGEEVVFAVTAVPDEKKGEK---LVVLHTCGAEDVEELKRAIK--ESGLPNLWKPSRYFKVEALPL 1126
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
116-281 |
2.10e-04 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 44.27 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVmtRVQAAGSKM-IITAD 194
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEAC--QYVAETSEAnILVVE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 195 GFSRRGKVVSLKDEVdkacehcPTVEKVVIVRhagNDFTPH--NYdFSWSTLEkekpfvhaeEMHSDDPL---------- 262
Cdd:cd05933 88 NQKQLQKILQIQDKL-------PHLKAIIQYK---EPLKEKepNL-YSWDEFM---------ELGRSIPDeqldaiissq 147
|
170 180
....*....|....*....|....*
gi 446729151 263 ------MLIYTSGTTGKPKGTVHTH 281
Cdd:cd05933 148 kpnqccTLIYTSGTTGMPKGVMLSH 172
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
116-281 |
2.05e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 41.02 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIG---AIISPIFSGFASD-----AVMTRVQAAgs 187
Cdd:PRK08180 71 TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGvpyAPVSPAYSLVSQDfgklrHVLELLTPG-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729151 188 kMIITADG--FSRrgkvvSLKDEVDKACEhcptvekVVIVRHAGNDFTPHnydfSWSTLEKEKPFVHAEEMHS----DDP 261
Cdd:PRK08180 149 -LVFADDGaaFAR-----ALAAVVPADVE-------VVAVRGAVPGRAAT----PFAALLATPPTAAVDAAHAavgpDTI 211
|
170 180
....*....|....*....|
gi 446729151 262 LMLIYTSGTTGKPKGTVHTH 281
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTH 231
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
116-165 |
4.84e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 40.09 E-value: 4.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446729151 116 TYEELDSWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI 165
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAV 523
|
|
| |
