|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
54-559 |
0e+00 |
|
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: 1065.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 54 IPEYFNFAKDVLDQWTDKEKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW 133
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 134 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMK 213
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 214 HASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWI 293
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 294 QGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY 373
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 374 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLR 453
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 454 GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSH 533
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500
....*....|....*....|....*.
gi 1034595494 534 DQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKV 506
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
95-559 |
0e+00 |
|
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: 591.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 95 WSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 175 DvlapavdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSsFGL 254
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHS-YPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLV 334
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 335 QNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNG 414
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 415 NVLPPGQEGDIGIQVLPNrpfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVE 494
Cdd:cd05972 268 RELPPGEEGDIAIKLPPP---GLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034595494 495 NALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREI 407
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
54-559 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 564.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 54 IPEYFNFAKDVLDQWtdkekAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEW 133
Cdd:COG0365 4 VGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANAL-RALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 134 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAVASKCENLHSKLIV----SEN 200
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 201 SREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGW 280
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 281 AKSAWSSVFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEP 355
Cdd:COG0365 238 ATGHSYIVYGPLLNGATVVLYEgRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 356 ITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnRP 434
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK----GP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 435 F-GLFTHYVDNPSKTASTLRGNF---YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVS 510
Cdd:COG0365 394 WpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034595494 511 SPDPIRGEVVKAFVVLNPDYKSHDqeQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:COG0365 474 VPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREI 520
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
43-559 |
0e+00 |
|
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: 560.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 43 YESMKQDFKLGIPEYFNFAKDVLDQWtdkekAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDR 122
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAM-----AKEYPDKLALVWCDDAGEERIFTFAELADYSDKTANFF-KAMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 123 VILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS--KANCIITNDVLAPAVDAVASKCENLHSKLIVSEN 200
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESAdiKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 201 SREGWGNLKELMKHASDS----HTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSsFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 277 DTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPI 356
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 357 TPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFG 436
Cdd:cd05970 314 NPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 437 LFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIR 516
Cdd:cd05970 394 LFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIR 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1034595494 517 GEVVKAFVVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05970 474 GQVVKATIVLAKGYEP--SEELKKELQDHVKKVTAPYKYPRIV 514
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-561 |
1.49e-132 |
|
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: 394.63 E-value: 1.49e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAnciitnd 175
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLAPAVDAVaskcenlhsklivsensregwgnlkelmkHASDShtcvktkhneiMAIFFTSGTSGYPKMTAHTHSSFGLG 255
Cdd:cd05974 74 VYAAVDENT-----------------------------HADDP-----------MLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 256 lSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQ 335
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 336 NDITSYKFKsLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGN 415
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 416 vlpPGQEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVEN 495
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034595494 496 ALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKVGI 561
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE--PSPETALEIFRFSRERLAPYKRIRRLEF 412
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
35-557 |
6.76e-132 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 397.73 E-value: 6.76e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 35 ATPQNFSnYESMKQDFKLGIPEYFNFAKDVLDQWTDKEKAGKkpsnPAFWWINRNGEEmRWSFEELGSLSRKFANILSEA 114
Cdd:PRK04319 20 ETYATFS-WEEVEKEFSWLETGKVNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELSNKFANVLKEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 115 cSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVdaVASKCENLHSK 194
Cdd:PRK04319 94 -GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 195 LIVSENSREGWG--NLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVM 272
Cdd:PRK04319 171 LLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKYVLDLHEDDVY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 273 WNTSDTGWAKSAWSSVFSPWIQGA--CVFThhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLK 347
Cdd:PRK04319 250 WCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddlVKKYDLSSLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 348 HCVSAGEPITPDVTeKWRNKT-GLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGD 424
Cdd:PRK04319 327 HILSVGEPLNPEVV-RWGMKVfGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 425 IGIQvlPNRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVA 504
Cdd:PRK04319 405 LAIK--KGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVA 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034595494 505 ESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPR 557
Cdd:PRK04319 482 EAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVKKGLGAHAAPR 532
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
95-559 |
9.93e-117 |
|
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: 354.12 E-value: 9.93e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 175 DVLAPavdavaskcenlhsklivsensregwgnlkelmkhasdshtcvKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgL 254
Cdd:cd05969 80 EELYE-------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHlPRFEPTSILQTLSKYPITVFCSAPTVYRMLV 334
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 335 QNDI---TSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKI 409
Cdd:cd05969 195 KEGDelaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 410 VDVNGNVLPPGQEGDIGIQvlPNRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIG 489
Cdd:cd05969 274 VDENGNELPPGTKGILALK--PGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 490 PFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEP--SDELKEEIINFVRQKLGAHVAPREI 418
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
63-559 |
3.64e-112 |
|
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: 342.56 E-value: 3.64e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 63 DVLDQWtdkekAGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG0318 3 DLLRRA-----AARHPDRPALVFGGR-----RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITndvlapavdavaskcenlhsklivsensregwgnlkelmkhasdshtcv 222
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 223 ktkhneiMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTS----DTGWaksaWSSVFSPWIQGACV 298
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 299 ftHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYG 377
Cdd:COG0318 171 --VLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 378 QTET-VLICGNFKGMK-IKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGN 455
Cdd:COG0318 249 LTETsPVVTVNPEDPGeRRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 456 FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQ 535
Cdd:COG0318 324 WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDA 402
|
490 500
....*....|....*....|....
gi 1034595494 536 EQLIKEIQEHVkkttAPYKYPRKV 559
Cdd:COG0318 403 EELRAFLRERL----ARYKVPRRV 422
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
89-559 |
4.70e-109 |
|
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: 334.40 E-value: 4.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 89 NGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 169 NCIITNDVLAPAVdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimaIFFTSGTSGYPKMTAHT 248
Cdd:cd05971 80 SALVTDGSDDPAL--------------------------------------------------IIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 249 HSsFGLGLSVNGRFWLDLTP--SDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSA 326
Cdd:cd05971 110 HR-VLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 327 PTVYRML-VQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSPA 404
Cdd:cd05971 189 PTALKMMrQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 405 FDVKIVDVNGNVLPPGQEGDIGIQvLPNrPFGLFThYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSS 484
Cdd:cd05971 269 HRVAIVDDNGTPLPPGEVGEIAVE-LPD-PVAFLG-YWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034595494 485 GYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05971 346 GYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREI 418
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-559 |
6.36e-98 |
|
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: 305.60 E-value: 6.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNd 175
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 vlapavdavaskCENLHsklivsensregwgnlkelmKHASDshtcvktkhneIMAIFFTSGTSGYPKMTAHTHSSFgLG 255
Cdd:cd05973 80 ------------AANRH--------------------KLDSD-----------PFVMMFTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQ 335
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 336 NDITSYKFK--SLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMK--IKPGSMGKPSPAFDVKIVD 411
Cdd:cd05973 195 AGAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVLD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 412 VNGNVLPPGQEGDIGIQVlPNRPFGLFTHYVDNPSKTAStlrGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPF 491
Cdd:cd05973 275 DDGDELGPGEPGRLAIDI-ANSPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPF 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034595494 492 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05973 351 DVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEG--TPALADELQLHVKKRLSAHAYPRTI 416
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
228-559 |
2.16e-97 |
|
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: 300.36 E-value: 2.16e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 228 EIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFTHhlPRFE 307
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 PTSILQTLSKYPITVFCSAPTVYRMLVQND-ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--VLI 384
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPeSAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 385 CGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFGlfthYVDNPSKTASTLRGNFYITGDRGY 464
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-GPSVMKG----YWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 465 MDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdykshDQEQLIKEIQE 544
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRA 306
|
330
....*....|....*
gi 1034595494 545 HVKKTTAPYKYPRKV 559
Cdd:cd04433 307 HVRERLAPYKVPRRV 321
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
63-559 |
3.30e-96 |
|
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: 302.17 E-value: 3.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 63 DVLDqwtdkEKAGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:cd05936 3 DLLE-----EAARRFPDKTALIFMGR-----KLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIIT----NDVLAPAvDAVASKCENlhsklivsensregwgnlkelmkHASDs 218
Cdd:cd05936 72 AGAVVVPLNPLYTPRELEHILNDSGAKALIVavsfTDLLAAG-APLGERVAL-----------------------TPED- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 219 htcvktkhneIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNgRFWL--DLTPSDVMWNT-------SDTgwaksawSSVF 289
Cdd:cd05936 127 ----------VAVLQYTSGTTGVPKGAMLTHRNLVANALQI-KAWLedLLEGDDVVLAAlplfhvfGLT-------VALL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 290 SPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKT 368
Cdd:cd05936 189 LPLALGATIVL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 369 GLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFTHYVDN 444
Cdd:cd05936 267 GVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELwvrGPQV--------MKGYWNR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 445 PSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFV 524
Cdd:cd05936 339 PEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFV 418
|
490 500 510
....*....|....*....|....*....|....*.
gi 1034595494 525 VLNPDykshdqEQLIK-EIQEHVKKTTAPYKYPRKV 559
Cdd:cd05936 419 VLKEG------ASLTEeEIIAFCREQLAGYKVPRQV 448
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
56-559 |
4.11e-95 |
|
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: 300.44 E-value: 4.11e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 56 EYFNFAKDVLDQwTDKEKAGKkpsnPAFwwINRNGEemrWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWL 135
Cdd:cd05959 1 EKYNAATLVDLN-LNEGRGDK----TAF--IDDAGS---LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 136 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSRE--GWGNLKELMK 213
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 214 HASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSP-W 292
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPlS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 293 IQGACVFthhLP-RFEPTSILQTLSKYPITVFCSAPTVYR-MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL 370
Cdd:cd05959 230 VGATTVL---MPeRPTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 371 DIYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTA 449
Cdd:cd05959 307 DILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYV-----RGPSSATMYWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 450 STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 529
Cdd:cd05959 381 DTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPG 460
|
490 500 510
....*....|....*....|....*....|
gi 1034595494 530 YKshDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05959 461 YE--DSEALEEELKEFVKDRLAPYKYPRWI 488
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
92-559 |
1.03e-86 |
|
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: 276.28 E-value: 1.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 92 EMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQsskaNCI 171
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 172 ITNDVLAPAVDAVaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSS 251
Cdd:cd05958 84 ITVALCAHALTAS------------------------------------------DDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 252 FGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYR 331
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 332 -MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIV 410
Cdd:cd05958 200 aMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 411 DVNGNVLPPGQEGDIGIQvlpnRPFGLftHYVDNPSKtASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGP 490
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVR----GPTGC--RYLADKRQ-RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAP 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034595494 491 FEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05958 353 PEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAI 419
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
62-559 |
3.60e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 269.75 E-value: 3.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 62 KDVLDQWtdkekAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACL 141
Cdd:PRK06187 9 GRILRHG-----ARKHPDKEAVYF-----DGRRTTYAELDERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 142 RTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREG----WGNLKELMKHASD 217
Cdd:PRK06187 78 KIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 218 SHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGWAksawssvFSP 291
Cdd:PRK06187 158 TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL-FLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLP-------YLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 292 WIQGAcvfTHHLP-RFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITS-YKFKSLKHCVSAGEPITPDVTEKWRNKTG 369
Cdd:PRK06187 230 LMAGA---KQVIPrRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 370 LDIYEGYGQTETV-LICGNF-----KGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGqEGDIG-IQVL-PNRPFGlfthY 441
Cdd:PRK06187 307 IDLVQGYGMTETSpVVSVLPpedqlPGQWTKRRSAGRPLPGVEARIVDDDGDELPPD-GGEVGeIIVRgPWLMQG----Y 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 442 VDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVK 521
Cdd:PRK06187 382 WNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPV 461
|
490 500 510
....*....|....*....|....*....|....*...
gi 1034595494 522 AFVVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKV 559
Cdd:PRK06187 462 AVVVLKPG-ATLDAKELRAFLRGRL----AKFKLPKRI 494
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
72-484 |
3.24e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 251.08 E-value: 3.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPAFwwinRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:pfam00501 3 RQAARTPDKTAL----EVGEGRRLTYRELDERANRLAAGL-RALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 152 TQLTQKDILYRLQSSKANCIITNDVL-APAVDAVASKCENLHSKLIVS-ENSREGWGNLKELMKHASDSHTCVKTKHNEI 229
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDrDPVLKEEPLPEEAKPADVPPPPPPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 230 MAIFFTSGTSGYPKMTAHTH---SSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVFTHHLPR 305
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 306 FEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--- 381
Cdd:pfam00501 238 LDPAALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 382 VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDI---GIQVLPnrpfGlfthYVDNPSKTASTL-RGNF 456
Cdd:pfam00501 318 VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELcvrGPGVMK----G----YLNDPELTAEAFdEDGW 389
|
410 420
....*....|....*....|....*...
gi 1034595494 457 YITGDRGYMDKDGYFWFVARADDVILSS 484
Cdd:pfam00501 390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
59-559 |
1.47e-74 |
|
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: 249.40 E-value: 1.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 59 NFAKDVLDQWtdkekAGKKPSNPAFWWINRNGEEMR-WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLAN 137
Cdd:cd05966 53 NISYNCLDRH-----LKERGDKVAIIWEGDEPDQSRtITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 138 VACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND---------VLAPAVDAVASKCENLHsKLIVSENS---- 201
Cdd:cd05966 127 LACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRTggev 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 202 -----REGWGNlkELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTS 276
Cdd:cd05966 203 pmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 277 DTGWAKSAWSSVFSPWIQGACVFThhlprFE--PT--------SILQtlsKYPITVFCSAPTVYRMLVQ---NDITSYKF 343
Cdd:cd05966 281 DIGWITGHSYIVYGPLANGATTVM-----FEgtPTypdpgrywDIVE---KHKVTIFYTAPTAIRALMKfgdEWVKKHDL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 344 KSLKHCVSAGEPITPdvtEKWR---NKTG---LDIYEGYGQTETVLIC-----GnfkGMKIKPGSMGKPSPAFDVKIVDV 412
Cdd:cd05966 353 SSLRVLGSVGEPINP---EAWMwyyEVIGkerCPIVDTWWQTETGGIMitplpG---ATPLKPGSATRPFFGIEPAILDE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 413 NGNVLPPGQEGDIGIQvlpnRPFglfthyvdnPSkTASTLRGN--------------FYITGDRGYMDKDGYFWFVARAD 478
Cdd:cd05966 427 EGNEVEGEVEGYLVIK----RPW---------PG-MARTIYGDheryedtyfskfpgYYFTGDGARRDEDGYYWITGRVD 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 479 DVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDqeQLIKEIQEHVKKTTAPYKYPRK 558
Cdd:cd05966 493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDK 570
|
.
gi 1034595494 559 V 559
Cdd:cd05966 571 I 571
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
74-559 |
1.60e-74 |
|
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: 244.44 E-value: 1.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 74 AGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:cd17631 5 ARRHPDRTALVFGGR-----SLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 154 LTQKDILYRLQSSKAnciitndvlapavdavaskcenlhsKLIVSENSRegwgnlkelmkhasdshtcvktkhneimaIF 233
Cdd:cd17631 79 LTPPEVAYILADSGA-------------------------KVLFDDLAL-----------------------------LM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGwaksawssVFSPWIQGACVFTHHLPRFE 307
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNL-LWNAVNALAALDLGPDDVllvvapLFHIGGLG--------VFTLPTLLRGGTVVILRKFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETV-LIC 385
Cdd:cd17631 176 PETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSpGVT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 386 GNFKGMKI-KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTASTLRGNFYITGDRGY 464
Cdd:cd17631 255 FLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRG-PH----VMAGYWNRPEATAAAFRDGWFHTGDLGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 465 MDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIkeiqE 544
Cdd:cd17631 330 LDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG-AELDEDELI----A 404
|
490
....*....|....*
gi 1034595494 545 HVKKTTAPYKYPRKV 559
Cdd:cd17631 405 HCRERLARYKIPKSV 419
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
96-562 |
5.29e-73 |
|
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: 240.44 E-value: 5.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 vlapavDAVASkcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimaIFFTSGTSGYPKMTAHTHSSFGLG 255
Cdd:cd05919 91 ------DDIAY---------------------------------------------LLYSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLPRfEPTSILQTLSKYPITVFCSAPTVY-RMLV 334
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 335 QNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNG 414
Cdd:cd05919 199 SCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 415 NVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVE 494
Cdd:cd05919 279 HTIPPGEEGDLLV-----RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034595494 495 NALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShdQEQLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:cd05919 354 SLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP--QESLARDIHRHLLERLSAHKVPRRIAFV 419
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
74-562 |
5.60e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 242.50 E-value: 5.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 74 AGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK07656 15 ARRFGDKEAYVF-----GDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIV----SENSREGWGNLKELMKHASDSHTCVKTKHNEI 229
Cdd:PRK07656 89 YTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 230 MAIFFTSGTSGYPK--MTAHTHSsfglgLSvNGRFW---LDLTPSD---------------VMWNTsdtgwaksawssvf 289
Cdd:PRK07656 169 ADILFTSGTTGRPKgaMLTHRQL-----LS-NAADWaeyLGLTEGDrylaanpffhvfgykAGVNA-------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 290 sPWIQGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKT 368
Cdd:PRK07656 229 -PLMRGATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 369 GLDIY-EGYGQTE---TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDN 444
Cdd:PRK07656 306 GVDIVlTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV-----RGPNVMKGYYDD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 445 PSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:PRK07656 381 PEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAY 460
|
490 500 510
....*....|....*....|....*....|....*....
gi 1034595494 524 VVLNPDyKSHDQEQLIKEIQEHVkkttAPYKYPRKVGIL 562
Cdd:PRK07656 461 VVLKPG-AELTEEELIAYCREHL----AKYKVPRSIEFL 494
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
95-559 |
1.05e-72 |
|
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: 244.02 E-value: 1.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17634 85 ISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 175 D----------VLAPAVDAVASKCENLHSKLIVSensREG---------WGNLKELMKHASDSHTCVKTKHNEIMAIFFT 235
Cdd:cd17634 164 DggvragrsvpLKKNVDDALNPNVTSVEHVIVLK---RTGsdidwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 236 SGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHH-LPRF-EPTSILQ 313
Cdd:cd17634 241 SGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 314 TLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEPITPDVTE-KWR--NKTGLDIYEGYGQTETV-LICG 386
Cdd:cd17634 321 VVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPINPEAYEwYWKkiGKEKCPVVDTWWQTETGgFMIT 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 387 NFKGM-KIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQV-LPNRPFGLFThyvDNPSKTASTLR--GNFYITGDR 462
Cdd:cd17634 401 PLPGAiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDpWPGQTRTLFG---DHERFEQTYFStfKGMYFSGDG 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 463 GYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQEQLIKEI 542
Cdd:cd17634 478 ARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAEL 555
|
490
....*....|....*..
gi 1034595494 543 QEHVKKTTAPYKYPRKV 559
Cdd:cd17634 556 RNWVRKEIGPLATPDVV 572
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
80-557 |
3.19e-71 |
|
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: 237.81 E-value: 3.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 80 NPAFWWINRNGEEMR------------WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:TIGR02262 4 NAAEDLLDRNVVEGRggktafiddissLSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSkLIVSENSREGWGNLKELMKHASDSHTCVKTKHN 227
Cdd:TIGR02262 83 VALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATESEQFKPAATQAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 228 EIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHlPRFE 307
Cdd:TIGR02262 162 DPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMG-ERPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 PTSILQTLSKYPITVFCSAPTVYR-MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICG 386
Cdd:TIGR02262 241 PDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 387 NFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfthYVDNPSKTASTLRGNFYITGDRGYMD 466
Cdd:TIGR02262 321 SNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISG-PSSATM----YWNNRAKSRDTFQGEWTRSGDKYVRN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 467 KDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShdqeqLIKEIQEHV 546
Cdd:TIGR02262 396 DDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-----LETELKEHV 470
|
490
....*....|.
gi 1034595494 547 KKTTAPYKYPR 557
Cdd:TIGR02262 471 KDRLAPYKYPR 481
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
95-567 |
7.38e-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: 233.64 E-value: 7.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 95 WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT- 173
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 NDVLAPAVDAVasKCENLHSKLIVSENSREGWGNLKELMK---HASDSH--TCVKTKHNEIMAIFFTSGTSGYPKMTAHT 248
Cdd:cd05911 90 PDGLEKVKEAA--KELGPKDKIIVLDDKPDGVLSIEDLLSptlGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 249 HSSFGLGL-SVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWiQGACVFTHhlPRFEPTSILQTLSKYPITVFCSAP 327
Cdd:cd05911 168 HRNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIM--PKFDSELFLDLIEKYKITFLYLVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 328 TVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAF 405
Cdd:cd05911 245 PIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 406 DVKIVDVNGN-VLPPGQEGDI---GIQVLPnrpfGlfthYVDNPSKTASTL-RGNFYITGDRGYMDKDGYFWFVARADDV 480
Cdd:cd05911 325 EAKIVDDDGKdSLGPNEPGEIcvrGPQVMK----G----YYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 481 ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDqeqliKEIQEHVKKTTAPYKYPRKvG 560
Cdd:cd05911 397 IKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASYKQLRG-G 470
|
....*..
gi 1034595494 561 ILIITNI 567
Cdd:cd05911 471 VVFVDEI 477
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
96-559 |
1.38e-68 |
|
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: 228.52 E-value: 1.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnd 175
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 vlapavdavaskcenlHSKLivsensregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTHSSFgLG 255
Cdd:cd05935 80 ----------------GSEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 256 LSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQ 335
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 336 N-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDV-N 413
Cdd:cd05935 190 TpEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIeT 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 414 GNVLPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTAS---TLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIG 489
Cdd:cd05935 270 GRELPPNEVGEIVVRG-PQ----IFKGYWNRPEETEEsfiEIKGRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 490 PFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQlikEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREV 411
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
78-559 |
1.20e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 229.46 E-value: 1.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 78 PSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:PRK08314 24 PDKTAIVFYGR-----AISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 158 DILYRLQSSKANCIITNDVLAPAV------------------DAVASKCE-----NLHSKLIVSENSREGWGNLKELMK- 213
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAPGGVVAWKEALAa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 214 -HASDSHTcvkTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSD----TGWAKSAWSSV 288
Cdd:PRK08314 179 gLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfhvTGMVHSMNAPI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 289 FSpwiqGACVFThhLPRFEPTSILQTLSKYPITVFCSAPTvyrMLV----QNDITSYKFKSLKHCVSAGEPITPDVTEKW 364
Cdd:PRK08314 255 YA----GATVVL--MPRWDREAAARLIERYRVTHWTNIPT---MVVdflaSPGLAERDLSSLRYIGGGGAAMPEAVAERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 365 RNKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDI---GIQVlpnrpfglFT 439
Cdd:PRK08314 326 KELTGLDYVEGYGLTETMaQTHSNPPD-RPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIvvhGPQV--------FK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 440 HYVDNPSKTAS---TLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPI 515
Cdd:PRK08314 397 GYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPR 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1034595494 516 RGEVVKAFVVLNPDYKSHDQEQlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08314 477 RGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIV 517
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
90-559 |
2.80e-65 |
|
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: 224.89 E-value: 2.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 90 GEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTV--LIPG---TTQLTQkdilyRLQ 164
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfaAKELAS-----RID 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 165 SSKANCIITNDV---------LAPAVD-AVASKCENLHSKLIVSENSRE-------GWGNLKELMKHASdSHTCVKTKHN 227
Cdd:cd05967 152 DAKPKLIVTASCgiepgkvvpYKPLLDkALELSGHKPHHVLVLNRPQVPadltkpgRDLDWSELLAKAE-PVDCVPVAAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 228 EIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVFTHHLPRF 306
Cdd:cd05967 231 DPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGAtTVLYEGKPVG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 307 --EPTSILQTLSKYPITVFCSAPTVYRMLVQND-----ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQT 379
Cdd:cd05967 311 tpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 380 ET----VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFGLFTHYVDNP---SKTASTL 452
Cdd:cd05967 391 ETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK-LPLPPGCLLTLWKNDErfkKLYLSKF 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 453 RGnFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKS 532
Cdd:cd05967 470 PG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKI 548
|
490 500
....*....|....*....|....*..
gi 1034595494 533 hDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05967 549 -TAEELEKELVALVREQIGPVAAFRLV 574
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
94-562 |
4.15e-64 |
|
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: 216.39 E-value: 4.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 ndvlAPAvdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimAIFFTSGTSGYPKMTAHTHSSFG 253
Cdd:cd05934 82 ----DPA--------------------------------------------------SILYTSGTTGPPKGVVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 254 LGLSVNGRfWLDLTPSDVMW--------NTSDTGWAkSAWSSvfspwiQGACVFthhLPRFEPTSILQTLSKYPITVFCS 325
Cdd:cd05934 108 FAGYYSAR-RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL---LPRFSASRFWSDVRRYGATVTNY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 326 APTVYRMLVQNDItsyKFKSLKHCVSA--GEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP 403
Cdd:cd05934 177 LGAMLSYLLAQPP---SPDDRAHRLRAayGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 404 AFDVKIVDVNGNVLPPGQEGDIGIQvlPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILS 483
Cdd:cd05934 254 GYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRR 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 484 SGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYK-SHDqeqlikEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:cd05934 332 RGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETlDPE------ELFAFCEGQLAYFKVPRYIRFV 405
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
106-559 |
9.28e-62 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 215.77 E-value: 9.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 106 KFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPGttqLTQKDILYRLQSSKANCIITND------- 175
Cdd:PRK00174 110 RFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAEALADRIIDAGAKLVITADegvrggk 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 --VLAPAVDAVASKCENLHSKLIVS--------ENSREGWGNlkELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMT 245
Cdd:PRK00174 186 piPLKANVDEALANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 246 AHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVF 323
Cdd:PRK00174 264 LHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEgVPNYpDPGRFWEVIDKHKVTIF 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 324 CSAPTVYRMLVQ---NDITSYKFKSLKHCVSAGEPITPdvtEKWR---NKTGLD---IYEGYGQTET--VLIC---Gnfk 389
Cdd:PRK00174 344 YTAPTAIRALMKegdEHPKKYDLSSLRLLGSVGEPINP---EAWEwyyKVVGGErcpIVDTWWQTETggIMITplpG--- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 390 GMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpNRPFglfthyvdnPS-------------KTA-STLRGN 455
Cdd:PRK00174 418 ATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVI----KDPW---------PGmmrtiygdherfvKTYfSTFKGM 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 456 fYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDq 535
Cdd:PRK00174 485 -YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD- 562
|
490 500
....*....|....*....|....
gi 1034595494 536 eQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK00174 563 -ELRKELRNWVRKEIGPIAKPDVI 585
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
94-559 |
1.13e-60 |
|
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: 207.91 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCiit 173
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 ndVLAPAVdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimaIFFTSGTSGYPKMTAHTHSSFG 253
Cdd:cd05941 88 --VLDPAL--------------------------------------------------ILYTSGTTGRPKGVVLTHANLA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 254 LGLSVNGRFWlDLTPSDV------------MWNtsdtgwaksawsSVFSPWIQGACVftHHLPRFEPTSILQTLSKYPIT 321
Cdd:cd05941 116 ANVRALVDAW-RWTEDDVllhvlplhhvhgLVN------------ALLCPLFAGASV--EFLPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 322 VFCSAPTVYRMLVQ---------NDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGN-FKGm 391
Cdd:cd05941 181 VFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpLDG- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 392 KIKPGSMGKPSPAFDVKIVDVNGNvlPPGQEGDIG-IQVlpnRPFGLFTHYVDNPSKTASTLRG-NFYITGDRGYMDKDG 469
Cdd:cd05941 260 ERRPGTVGMPLPGVQARIVDEETG--EPLPRGEVGeIQV---RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 470 YFWFVAR-ADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIkeiqEHVKK 548
Cdd:cd05941 335 YYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EWAKQ 410
|
490
....*....|.
gi 1034595494 549 TTAPYKYPRKV 559
Cdd:cd05941 411 RLAPYKRPRRL 421
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
59-552 |
5.67e-60 |
|
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: 210.42 E-value: 5.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 59 NFAKDVLDQWTdkekaGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANV 138
Cdd:cd05968 61 NIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 139 ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAVASKCENLHSKLIVSENSRE-GWGNL 208
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVVVVRHLGNDfTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 209 KELMKH---ASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAW 285
Cdd:cd05968 215 RDLSYDeekETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPW 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 286 sSVFSPWIQGACVFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVYRMLV---QNDITSYKFKSLKHCVSAGEPITPdv 360
Cdd:cd05968 295 -LIFGGLILGATMVLYDgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNP-- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 361 tEKW------RNKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPgQEGDIGIQ-VLPN 432
Cdd:cd05968 372 -EPWnwlfetVGKGRNPIINYSGGTEISgGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLaPWPG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 433 RPFGLF---THYVDnpskTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:cd05968 450 MTRGFWrdeDRYLE----TYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAI 525
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1034595494 510 SSPDPIRGEVVKAFVVLNPDYKSHD--QEQLIKEIQEHVKKTTAP 552
Cdd:cd05968 526 GVPHPVKGEAIVCFVVLKPGVTPTEalAEELMERVADELGKPLSP 570
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
96-557 |
2.63e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 207.58 E-value: 2.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK06710 51 TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLAPAVDAV--ASKCENL-----------------------HSKLIVSENSREG---WGNLKELMKHASDShTCvkTKHN 227
Cdd:PRK06710 130 LVFPRVTNVqsATKIEHVivtriadflpfpknllypfvqkkQSNLVVKVSESETihlWNSVEKEVNTGVEV-PC--DPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 228 EIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLD--LTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPR 305
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWLYncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL--IPK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 306 FEPTSILQTLSKYPITVFCSAPTVYRMLVQNDI-TSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLI 384
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 385 C-GNFKGMKIKPGSMGKPSPAFDVKIVDV-NGNVLPPGQEGDI---GIQVLPNrpfglfthYVDNPSKTASTLRGNFYIT 459
Cdd:PRK06710 364 ThSNFLWEKRVPGSIGVPWPDTEAMIMSLeTGEALPPGEIGEIvvkGPQIMKG--------YWNKPEETAAVLQDGWLHT 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 460 GDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQeqli 539
Cdd:PRK06710 436 GDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEE---- 511
|
490
....*....|....*...
gi 1034595494 540 kEIQEHVKKTTAPYKYPR 557
Cdd:PRK06710 512 -ELNQFARKYLAAYKVPK 528
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
95-559 |
7.89e-57 |
|
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: 199.08 E-value: 7.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 95 WSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT- 173
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 NDVLAPAVDAvASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKH---NEIMAIFFTSGTSGYPKMTAHTHS 250
Cdd:cd05926 94 KGELGPASRA-ASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVplpDDLALILHTSGTTGRPKGVPLTHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 251 SfgLGLSV-NGRFWLDLTPSD----VMWNTSDTGWAKSAWSSVFSpwiQGACVFThhlPRFEPTSILQTLSKYPITVFCS 325
Cdd:cd05926 173 N--LAASAtNITNTYKLTPDDrtlvVMPLFHVHGLVASLLSTLAA---GGSVVLP---PRFSASTFWPDVRDYNATWYTA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 326 APTVYRMLVQNDITSY--KFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV--LICGNFKGMKIKPGSMGKP 401
Cdd:cd05926 245 VPTIHQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 402 SPAfDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfthYVDNPSKTA-STLRGNFYITGDRGYMDKDGYFWFVARADDV 480
Cdd:cd05926 325 VGV-EVRILDEDGEILPPGVVGEICLRG-PNVTRG----YLNNPEANAeAAFKDGWFRTGDLGYLDADGYLFLTGRIKEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034595494 481 ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShdqeqLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05926 399 INRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV-----TEEELRAFCRKHLAAFKVPKKV 472
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
91-559 |
4.44e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 197.46 E-value: 4.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDVLAPAVDAVASKCENLHSKLIVSENSRE---GWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 248 THSSFgLGLSVNGRFWLDLTPSDVMWNtsdtgwA----KSAWSSVF-SPWIQ-GACvfTHHLPRFEPTSILQTLSKYPIT 321
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDVFlGPYLYvGAT--NVILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 322 VFCSAPTVYRMLVQN-DITSYKFKSLKHCVSaGEPITP-DVTEKWRNK-TGLDIYEGYGQTE-----TVLicgNFKGMKI 393
Cdd:PRK08316 263 SFFAPPTVWISLLRHpDFDTRDLSSLRKGYY-GASIMPvEVLKELRERlPGLRFYNCYGQTEiaplaTVL---GPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 394 KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqvlPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWF 473
Cdd:PRK08316 339 RPGSAGRPVLNVETRVVDDDGNDVAPGEVGEI-----VHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 474 VARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIkeiqEHVKKTTAPY 553
Cdd:PRK08316 414 VDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG-ATVTEDELI----AHCRARLAGF 488
|
....*.
gi 1034595494 554 KYPRKV 559
Cdd:PRK08316 489 KVPKRV 494
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
94-559 |
4.76e-56 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 197.02 E-value: 4.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK07514 28 RYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 NDVLAPAVDAVASKCENLHskliVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPK--MTAHTH-S 250
Cdd:PRK07514 107 DPANFAWLSKIAAAAGAPH----VETLDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMLSHGNlL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 251 SFGLGLSVNGRFwldlTPSDVMwntsdtgwaksawssvfspwIQGACVFTHH------------------LPRFEPTSIL 312
Cdd:PRK07514 183 SNALTLVDYWRF----TPDDVL--------------------IHALPIFHTHglfvatnvallagasmifLPKFDPDAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 313 QTLSKypITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGN-FKG 390
Cdd:PRK07514 239 ALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNpYDG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 391 MKIkPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTASTLRGN-FYITGDRGYMDKD 468
Cdd:PRK07514 317 ERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKG-PN----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDER 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 469 GYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHVkk 548
Cdd:PRK07514 391 GYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL-- 467
|
490
....*....|.
gi 1034595494 549 ttAPYKYPRKV 559
Cdd:PRK07514 468 --ARFKQPKRV 476
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
72-559 |
1.98e-55 |
|
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: 195.53 E-value: 1.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPAFwwIN-RNGEEMrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:cd05904 13 LFASAHPSRPAL--IDaATGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 151 TTQLTQKDILYRLQSSKANCIITndvlapaVDAVASKCENLHSKLIVSENSR-EGWGNLKELMKHASDSHTCVKTKHNEI 229
Cdd:cd05904 88 NPLSTPAEIAKQVKDSGAKLAFT-------TAELAEKLASLALPVVLLDSAEfDSLSFSDLLFEADEAEPPVVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 230 MAIFFTSGTSGYPKMTAHTHSSF-GLGLSVNGRFWLDLTPSDVMWntsdtgwaksawssVFSPW--IQGACVFTHH---- 302
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLiAMVAQFVAGEGSNSDSEDVFL--------------CVLPMfhIYGLSSFALGllrl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 303 ------LPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDIT-SYKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYE 374
Cdd:cd05904 227 gatvvvMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 375 GYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTAS 450
Cdd:cd05904 307 GYGMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPEtGESLPPNQTGELWI-----RGPSIMKGYLNNPEATAA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 451 TLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 529
Cdd:cd05904 382 TIDKEGWLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG 461
|
490 500 510
....*....|....*....|....*....|
gi 1034595494 530 ykSHDQEQlikEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05904 462 --SSLTED---EIMDFVAKQVAPYKKVRKV 486
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
90-562 |
4.96e-51 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 183.14 E-value: 4.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 90 GEEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 170 CIITNDVLAPAVDAVASKCENLHSKLIVSensregwgnLKELMKHASDShtCVKTKHNEIMAIFFTSGTSGYPKMTAHTH 249
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITS---------LKEIEDRKIDN--FVEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 250 SSFGLGlSVNGRFWLDLTPSDV------MWNTSDTGWAksawssVFSPWIQGACVFTHHlpRFEPTSILQTLSKYPITVF 323
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF------AFPTLFAGGVIIVPR--KFEPTKALSMIEKHKVTVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 324 CSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTET-----VLICGNFKGmkiKPGS 397
Cdd:PRK06839 243 MGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 398 MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARA 477
Cdd:PRK06839 319 IGKPVLFCDYELIDENKNKVEVGEVGELLIRG-PN----VMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 478 DDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDqeqliKEIQEHVKKTTAPYKYPR 557
Cdd:PRK06839 394 KEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPK 468
|
....*
gi 1034595494 558 KVGIL 562
Cdd:PRK06839 469 EIVFL 473
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
76-559 |
7.85e-51 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 185.54 E-value: 7.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 76 KKPSNPAFWWIN-RNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIPG- 150
Cdd:PRK10524 65 KRPEQLALIAVStETDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 151 -TTQLTQkdilyRLQSSKANCIITND-------VLA--PAVDAVASKCENLHSK-LIVS-----ENSREG----WGNLKE 210
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADagsrggkVVPykPLLDEAIALAQHKPRHvLLVDrglapMARVAGrdvdYATLRA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 211 lmKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFS 290
Cdd:PRK10524 219 --QHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 291 PWIQG-ACVFTHHLP-RFEPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEPITpDVTEKWR 365
Cdd:PRK10524 297 PLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALFLAGEPLD-EPTASWI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 366 NKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQV-LPnrPFGLF 438
Cdd:PRK10524 376 SEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGpLP--PGCMQ 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 439 THYVDNP---SKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPI 515
Cdd:PRK10524 454 TVWGDDDrfvKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDAL 533
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1034595494 516 RGEVVKAFVVLNPDYKSHDQEQ---LIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK10524 534 KGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARV 580
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
90-559 |
1.14e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 179.71 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 90 GEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 170 CIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEiMAifFTSGTSGYPK------ 243
Cdd:PRK08276 86 VLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGAD-ML--YSSGTTGRPKgikrpl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 244 MTAHTHSSFGLGLSVNGrFWLDLTPSDV------MWNTSDTGWAKSAwssvfspwiqgacvftHHL-------PRFEPTS 310
Cdd:PRK08276 163 PGLDPDEAPGMMLALLG-FGMYGGPDSVylspapLYHTAPLRFGMSA----------------LALggtvvvmEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 311 ILQTLSKYPITVFCSAPTVY-RML-----VQNditSYKFKSLKHCVSAGEPITPDVTEK----WrnktGLDIYEGYGQTE 380
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFvRMLklpeeVRA---RYDVSSLRVAIHAAAPCPVEVKRAmidwW----GPIIHEYYASSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 381 ----TVLICGNFKGmkiKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFglftHYVDNPSKTASTLRGNF 456
Cdd:PRK08276 299 gggvTVITSEDWLA---HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPF----EYHNDPEKTAAARNPHG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 457 YIT-GDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKshDQ 535
Cdd:PRK08276 370 WVTvGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD--AG 447
|
490 500
....*....|....*....|....
gi 1034595494 536 EQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08276 448 DALAAELIAWLRGRLAHYKCPRSI 471
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
63-556 |
4.42e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 179.47 E-value: 4.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 63 DVLDQWtdkekAGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK06178 37 EYLRAW-----ARERPQRPAIIFYGH-----VITYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLH------SKLIVSENSR-------------E 203
Cdd:PRK06178 106 LGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHvivtslADVLPAEPTLplpdslraprlaaA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 204 GWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS 283
Cdd:PRK06178 186 GAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 284 AWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVfcsapTVyrMLVQN--------DITSYKFKSLKH--CVSAG 353
Cdd:PRK06178 266 ENFGLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTR-----TV--MLVDNavelmdhpRFAEYDLSSLRQvrVVSFV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 354 EPITPDVTEKWRNKTGLDIYEG-YGQTETvLICGNF-KGM-------KIKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEG 423
Cdd:PRK06178 337 KKLNPDYRQRWRALTGSVLAEAaWGMTET-HTCDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 424 DIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSV 503
Cdd:PRK06178 416 EIVV-----RTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAV 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034595494 504 AESAVVSSPDPIRGEVVKAFVVLNPDyksHDQEQliKEIQEHVKKTTAPYKYP 556
Cdd:PRK06178 491 LGSAVVGRPDPDKGQVPVAFVQLKPG---ADLTA--AALQAWCRENMAVYKVP 538
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
63-559 |
1.64e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 177.88 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 63 DVLDqwtdkEKAGKKPSNPAFWWInrnGEEMrwSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK05605 36 DLYD-----NAVARFGDRPALDFF---GATT--TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 143 TGTVLIPGTTQLTQKDILYRLQSSKANCIItndvlapAVDAVASKCENLHSKL----IVSEN------------------ 200
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAI-------VWDKVAPTVERLRRTTpletIVSVNmiaampllqrlalrlpip 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 201 ----SREG----------WgnlKELMKHA----SDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSsfglGLSVN--- 259
Cdd:PRK05605 178 alrkARAAltgpapgtvpW---ETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHR----NLFANaaq 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 260 GRFWLDLTPSD----------------VMWNTsdtgwaksawssvFSPWIQGACVFthhLPRFEPTSILQTLSKYPITVF 323
Cdd:PRK05605 251 GKAWVPGLGDGpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMKKHPPTWL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 324 CSAPTVYRMLVQN------DITSykfksLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIKPG 396
Cdd:PRK05605 315 PGVPPLYEKIAEAaeergvDLSG-----VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 397 SMGKPSPAFDVKIVDVN--GNVLPPGQEGDI---GIQVlpnrpfglFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYF 471
Cdd:PRK05605 390 YVGVPFPDTEVRIVDPEdpDETMPDGEEGELlvrGPQV--------FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 472 WFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLikeiQEHVKKTTA 551
Cdd:PRK05605 462 RIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEGL----RAYCREHLT 536
|
....*...
gi 1034595494 552 PYKYPRKV 559
Cdd:PRK05605 537 RYKVPRRF 544
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
77-562 |
5.63e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 175.74 E-value: 5.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 77 KPSNPAFWWInrnGEEMRWSfeELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQ 156
Cdd:PRK07786 30 QPDAPALRFL---GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 157 KDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTS 236
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 237 GTSGYPKMTAHTHSSFGlGLSVNG-RFWLDLTPSDVMWNTSDTgWAKSAWSSVFSPWIQGACVFTHHLPRFEPTSILQTL 315
Cdd:PRK07786 184 GTTGRPKGAVLTHANLT-GQAMTClRTNGADINSDVGFVGVPL-FHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 316 SKYPIT-VFCsAPTVYRMLVQNDITSYKFKSLKhCVSAGEPITPDVTEKWRNKT--GLDIYEGYGQTE----TVLICGNF 388
Cdd:PRK07786 262 EAEKVTgIFL-VPAQWQAVCAEQQARPRDLALR-VLSWGAAPASDTLLRQMAATfpEAQILAAFGQTEmspvTCMLLGED 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 389 KGMKIkpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqvlPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKD 468
Cdd:PRK07786 340 AIRKL--GSVGKVIPTVAARVVDENMNDVPVGEVGEI-----VYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 469 GYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDykshDQEQLIKEIQEHVKK 548
Cdd:PRK07786 413 GYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND----DAALTLEDLAEFLTD 488
|
490
....*....|....
gi 1034595494 549 TTAPYKYPRKVGIL 562
Cdd:PRK07786 489 RLARYKHPKALEIV 502
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
96-508 |
4.50e-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: 170.14 E-value: 4.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKA 168
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 169 NCIITNDVLAPAVDAVAskcenlhsKLIVSENSREGWgnlkELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHT 248
Cdd:TIGR01733 74 RLLLTDSALASRLAGLV--------LPVILLDPLELA----ALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 249 HSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWsSVFSPWIQGACVF--THHLPRFEPTSILQTLSKYPITVFCSA 326
Cdd:TIGR01733 142 HRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVvpPEDEERDDAALLAALIAEHPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 327 PTVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVLICgnfkGMKIKPGSM------- 398
Cdd:TIGR01733 220 PSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWS----TATLVDPDDaprespv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 399 --GKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTA---------STLRGNFYITGDRGYMDK 467
Cdd:TIGR01733 294 piGRPLANTRLYVLDDDLRPVPVGVVGELYI-----GGPGVARGYLNRPELTAerfvpdpfaGGDGARLYRTGDLVRYLP 368
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1034595494 468 DGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV 508
Cdd:TIGR01733 369 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
74-559 |
5.87e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 172.92 E-value: 5.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 74 AGKKPSNPAFWWinrnGEEmRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK07470 17 ARRFPDRIALVW----GDR-SWTWREIDARVDALAAAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKlIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIF 233
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHV-VAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHSSfgLGLSVNGRFwLDLTPsdvmwntsdtGWAKSAWSSVFSPWIQGACVftHHL---------- 303
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQ--MAFVITNHL-ADLMP----------GTTEQDASLVVAPLSHGAGI--HQLcqvargaatv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 304 ----PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQ 378
Cdd:PRK07470 235 llpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHpAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 379 TE-----TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFTHYVDNPSK 447
Cdd:PRK07470 315 GEvtgniTVLpPALHDaeDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEIcviGPAV--------FAGYYNNPEA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 448 TASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLN 527
Cdd:PRK07470 387 NAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR 466
|
490 500 510
....*....|....*....|....*....|..
gi 1034595494 528 pDYKSHDQEqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK07470 467 -DGAPVDEA----ELLAWLDGKVARYKLPKRF 493
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
303-559 |
1.01e-46 |
|
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: 167.06 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 303 LPRFEPTSILQTLSKYPITVFCS-APTVYRMLVQNDITSYKFKSLKHcVSAGEpiTPDVTEKWRNKTGLDIYEGYGQTET 381
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 382 ---VLICGNFKgmkiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYI 458
Cdd:cd17637 149 sglVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV-----RGPLVFQGYWNLPELTAYTFRNGWHH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 459 TGDRGYMDKDGYFWFVAR--ADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQE 536
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG-ATLTAD 298
|
250 260
....*....|....*....|...
gi 1034595494 537 QLIkeiqEHVKKTTAPYKYPRKV 559
Cdd:cd17637 299 ELI----EFVGSRIARYKKPRYV 317
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
95-559 |
1.04e-46 |
|
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: 169.45 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 95 WSFEEL----GSLSRKFANIlseacSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05912 2 YTFAELfeevSRLAEHLAAL-----GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 iitndvlapavdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPK---MTAH 247
Cdd:cd05912 77 --------------------------------------------------------DDIATIMYTSGTTGKPKgvqQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 248 TH------SSFGLGLSVNGRfWLDLTPsdvMWNTSdtgwaksAWSSVFSPWIQGACVFTHhlPRFEPTSILQTLSKYPIT 321
Cdd:cd05912 101 NHwwsaigSALNLGLTEDDN-WLCALP---LFHIS-------GLSILMRSVIYGMTVYLV--DKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 322 VFCSAPTVYRMLVQNDITSYKfKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTETV--LICGNFKGMKIKPGSMG 399
Cdd:cd05912 168 IISVVPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSAG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 400 KPSPAFDVKIVDVNGnvlPPGQEGDIGIQVlPNRPFGlfthYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADD 479
Cdd:cd05912 246 KPLFPVELKIEDDGQ---PPYEVGEILLKG-PNVTKG----YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSD 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 480 VILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYkshDQEQLIKEIQEHVKKttapYKYPRKV 559
Cdd:cd05912 318 LIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKLAK----YKVPKKI 390
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
78-557 |
5.47e-46 |
|
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: 168.09 E-value: 5.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 78 PSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:cd05930 1 PDAVAVVDGDQ-----SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 158 DILYRLQSSKANCIITNdvlapavdavaskcenlhsklivsensregwgnlkelmkhasdshtcvktkHNEIMAIFFTSG 237
Cdd:cd05930 75 RLAYILEDSGAKLVLTD---------------------------------------------------PDDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 238 TSGYPKMTAHTHSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVftHHLP---RFEPTS 310
Cdd:cd05930 104 STGKPKGVMVEHRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATL--VVLPeevRKDPEA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 311 ILQTLSKYPITVFCSAPTVYRMLVQNDITSyKFKSLKHCVSAGEPITPDVTEKWR-NKTGLDIYEGYGQTETVLICGNF- 388
Cdd:cd05930 176 LADLLAEEGITVLHLTPSLLRLLLQELELA-ALPSLRLVLVGGEALPPDLVRRWReLLPGARLVNLYGPTEATVDATYYr 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 389 -KGMKIKPGSM--GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpNRpfGlfthYVDNPSKTASTLRGN------- 455
Cdd:cd05930 255 vPPDDEEDGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELyigGAGL--AR--G----YLNRPELTAERFVPNpfgpger 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 456 FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdykshDQ 535
Cdd:cd05930 327 MYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE-----GG 401
|
490 500
....*....|....*....|..
gi 1034595494 536 EQLIKEIQEHVKKTTAPYKYPR 557
Cdd:cd05930 402 ELDEEELRAHLAERLPDYMVPS 423
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
94-562 |
7.37e-46 |
|
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: 167.56 E-value: 7.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILSEAcSLQRGDRVILILPrvpEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLP---NWWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDVlapavdavaskcenlhsklivsensregWGNlkelMKHASDShtcvktkhNEIMAIFFTSGTSGYPKMTAHTHS 250
Cdd:cd05903 77 FVVPER----------------------------FRQ----FDPAAMP--------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 251 SfglgLSVNGRFW---LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVftHHLPRFEPTSILQTLSKYPITVFCSAP 327
Cdd:cd05903 117 T----LSASIRQYaerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 328 T-VYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLICGNfkgmkIKPG-------SMG 399
Cdd:cd05903 191 PfLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPApedrrlyTDG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 400 KPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADD 479
Cdd:cd05903 266 RPLPGVEIKVVDDTGATLAPGVEGELLS-----RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 480 VILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdykshDQEQLIKEIQEHV-KKTTAPYKYPRK 558
Cdd:cd05903 341 IIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKS-----GALLTFDELVAYLdRQGVAKQYWPER 415
|
....
gi 1034595494 559 VGIL 562
Cdd:cd05903 416 LVHV 419
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
92-562 |
8.43e-46 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 169.94 E-value: 8.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 92 EMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 172 ITNDVLAPAVDAVASKCENLHSKLIVSENSRE----GWGNLKelMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVsvpaGWSTAP--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 248 THSSFglglsvngrFW--------LDLTPSDVMWNTSDTgWAKSAWSSVFSPWIQGAcvfTHHL-PRFEPTSILQTLSKY 318
Cdd:PRK06155 201 PHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALNAFFQALLAGA---TYVLePRFSASGFWPAVRRH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 319 PITVFCSAPTVYRMLVQNDIT-SYKFKSLKHCVSAGEPitPDVTEKWRNKTGLDIYEGYGQTETVLICGNFKGMKiKPGS 397
Cdd:PRK06155 268 GATVTYLLGAMVSILLSQPAReSDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 398 MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARA 477
Cdd:PRK06155 345 MGRLAPGFEARVVDEHDQELPDGEPGELLLRA--DEPFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 478 DDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIkeiqEHVKKTTAPYKYPR 557
Cdd:PRK06155 423 KDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEPVALV----RHCEPRLAYFAVPR 497
|
....*
gi 1034595494 558 KVGIL 562
Cdd:PRK06155 498 YVEFV 502
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-559 |
1.39e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 167.83 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDVLAPAVDAVASkcenlhskLIVSEnsregwgnlkeLMKHASDSHTCVKTKH-NEIMAIFFTSGTSGYPK---MTA 246
Cdd:PRK03640 103 LITDDDFEAKLIPGIS--------VKFAE-----------LMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPKgviQTY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 247 HTH------SSFGLGLSVNGRfWLDLTPsdvMWNTSdtgwaksAWSSVFSPWIQGACVFTHhlPRFEPTSILQTLSKYPI 320
Cdd:PRK03640 164 GNHwwsavgSALNLGLTEDDC-WLAAVP---IFHIS-------GLSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 321 TVFCSAPT-VYRMLVQNDITSYKfKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTETV-LICG-NFKGMKIKPGS 397
Cdd:PRK03640 231 TIISVVSTmLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsQIVTlSPEDALTKLGS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 398 MGKPSPAFDVKIVDvNGNVLPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARA 477
Cdd:PRK03640 309 AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKG-PN----VTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 478 DDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpdyKSHDQEQLIKEIQEHVkkttAPYKYPR 557
Cdd:PRK03640 383 SDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS---GEVTEEELRHFCEEKL----AKYKVPK 455
|
..
gi 1034595494 558 KV 559
Cdd:PRK03640 456 RF 457
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
72-559 |
1.47e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 169.46 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKK-PSNPAFwwINRnGEEMrwSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK08974 30 EQAVARyADQPAF--INM-GEVM--TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 151 TTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLI-VSENSREGWGNL--------KELMK--HASDSH 219
Cdd:PRK08974 105 NPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTrMGDQLSTAKGTLvnfvvkyiKRLVPkyHLPDAI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 220 TCVKTKH-------------NEIMAIF-FTSGTSGYPKMTAHTHSsfglglsvngrfwldltpsDVMWNTSDTGWAKSAW 285
Cdd:PRK08974 185 SFRSALHkgrrmqyvkpelvPEDLAFLqYTGGTTGVAKGAMLTHR-------------------NMLANLEQAKAAYGPL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 286 SSVFSPWIQGA------------CVFTHHL---------PRFEPTSIlQTLSKYPITVFCSAPTVYRMLVQN-DITSYKF 343
Cdd:PRK08974 246 LHPGKELVVTAlplyhifaltvnCLLFIELggqnllitnPRDIPGFV-KELKKYPFTAITGVNTLFNALLNNeEFQELDF 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 344 KSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQE 422
Cdd:PRK08974 325 SSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 423 GDI---GIQVLPNrpfglfthYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNE 499
Cdd:PRK08974 405 GELwvkGPQVMLG--------YWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVML 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 500 HPSVAESAVVSSPDPIRGEVVKAFVVLNPdyKSHDQEQLIKEIQEHVkkttAPYKYPRKV 559
Cdd:PRK08974 477 HPKVLEVAAVGVPSEVSGEAVKIFVVKKD--PSLTEEELITHCRRHL----TGYKVPKLV 530
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
78-559 |
5.23e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 167.09 E-value: 5.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 78 PSNPAFWWINRngeemRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTG---TVLIP-GTTQ 153
Cdd:PRK06188 26 PDRPALVLGDT-----RLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrTALHPlGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 154 ltqkDILYRLQSSKANCIITNDvlAPAVD---AVASKCENLhsKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIM 230
Cdd:PRK06188 100 ----DHAYVLEDAGISTLIVDP--APFVEralALLARVPSL--KHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 231 AIFFTSGTSGYPKMTAHTHSSFG---------LGLSVNGRFwLDLTPsdvmwnTSDTGWAKsawssvFSPWIQ-GACVft 300
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIAtmaqiqlaeWEWPADPRF-LMCTP------LSHAGGAF------FLPTLLrGGTV-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 301 HHLPRFEPTSILQTLSKYPITVFCSAPT-VYRMLVQNDITSYKFKSLKHCVSAGEPITPDvtekwRNKTGLDIY-----E 374
Cdd:PRK06188 237 IVLAKFDPAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSPV-----RLAEAIERFgpifaQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 375 GYGQTE-----TVLICGNFKGMKIKP-GSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKT 448
Cdd:PRK06188 312 YYGQTEapmviTYLRKRDHDPDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICV-----RGPLVMDGYWNRPEET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 449 ASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNP 528
Cdd:PRK06188 387 AEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRP 466
|
490 500 510
....*....|....*....|....*....|.
gi 1034595494 529 DyKSHDQEqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK06188 467 G-AAVDAA----ELQAHVKERKGSVHAPKQV 492
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
72-561 |
5.70e-45 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 167.17 E-value: 5.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANiLSEACSLQRGDRVILILPRVPEW---WLAnVACLrtGTVLI 148
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 149 PGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCEN-LHSKLIVSENSRE--GWGNLKELMKHASDSHTCVKTK 225
Cdd:PRK08008 91 PINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATpLRHICLTRVALPAddGVSSFTQLKAQQPATLCYAPPL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 226 HNEIMA-IFFTSGTSGYPKMTAHTHSsfglglsvNGRF------W-LDLTPSDVMWNTSdtgwaksawssvfsPWIQGAC 297
Cdd:PRK08008 171 STDDTAeILFTSGTTSRPKGVVITHY--------NLRFagyysaWqCALRDDDVYLTVM--------------PAFHIDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 298 VFTHHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGE------------PITPDVTEKWR 365
Cdd:PRK08008 229 QCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDrqhclrevmfylNLSDQEKDAFE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 366 NKTGLDIYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRPfgLFTHYVDN 444
Cdd:PRK08008 309 ERFGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKT--IFKEYYLD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 445 PSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:PRK08008 387 PKATAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAF 466
|
490 500 510
....*....|....*....|....*....|....*....
gi 1034595494 524 VVLNPDykshdqEQL-IKEIQEHVKKTTAPYKYPRKVGI 561
Cdd:PRK08008 467 VVLNEG------ETLsEEEFFAFCEQNMAKFKVPSYLEI 499
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
74-558 |
1.13e-43 |
|
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: 162.03 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 74 AGKKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEACsLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:cd05945 1 AAANPDRPAVVEGGR-----TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 154 LTQKdilyRLQSskancIItnDVLAPAVdavaskcenlhskLIVSENsregwgnlkelmkhasdshtcvktkhnEIMAIF 233
Cdd:cd05945 75 SPAE----RIRE-----IL--DAAKPAL-------------LIADGD---------------------------DNAYII 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHS---SFGLGLsvNGRFwlDLTPSDVMWNTSDtgwaksaWS---SVFS---PWIQGACVFThhLP 304
Cdd:cd05945 104 FTSGSTGRPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGATLVP--VP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 305 RFE---PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQT 379
Cdd:cd05945 171 RDAtadPKQLFRFLAEHGITVWVSTPSFAAMCLLSpTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 380 ETVLICgnfKGMKIKPGSM--------GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVlpnrpfglFTHYVDNPSKT 448
Cdd:cd05945 251 EATVAV---TYIEVTPEVLdgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELvisGPSV--------SKGYLNNPEKT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 449 ASTLRGNF----YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFV 524
Cdd:cd05945 320 AAAFFPDEgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFV 399
|
490 500 510
....*....|....*....|....*....|....
gi 1034595494 525 VLNPdyksHDQEQLIKEIQEHVKKTTAPYKYPRK 558
Cdd:cd05945 400 VPKP----GAEAGLTKAIKAELAERLPPYMIPRR 429
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
78-559 |
1.43e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 160.17 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 78 PSNPAFWwINRNGEEMrwSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:PRK13390 11 PDRPAVI-VAETGEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 158 DILYRLQSSKANCIitndVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTcvKTKHNEIMaiFFTSG 237
Cdd:PRK13390 87 EADYIVGDSGARVL----VASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLT--EQPCGAVM--LYSSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 238 TSGYPK-----MTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKS-AWSSVFSPwIQGACVFTHhlpRFEPTSI 311
Cdd:PRK13390 159 TTGFPKgiqpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 312 LQTLSKYPITVFCSAPTVY-RMLVQND--ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE----TVLI 384
Cdd:PRK13390 235 LGHVERYRITVTQMVPTMFvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFID 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 385 CGNFKGmkiKPGSMGKpSPAFDVKIVDVNGNVLPPGQEGDIGIQ--VLPNRpfglfthYVDNPSKTASTLRGN--FYIT- 459
Cdd:PRK13390 315 SPDWLA---HPGSVGR-SVLGDLHICDDDGNELPAGRIGTVYFErdRLPFR-------YLNDPEKTAAAQHPAhpFWTTv 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 460 GDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKShdQEQLI 539
Cdd:PRK13390 384 GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG--SDELA 461
|
490 500
....*....|....*....|
gi 1034595494 540 KEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK13390 462 RELIDYTRSRIAHYKAPRSV 481
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
96-559 |
4.68e-42 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 159.42 E-value: 4.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLAPAVDAVASKCE--------------------NL---HSKLIVSENSREGWGNLKE-LMKHASDSHTCVKTKHNEIMA 231
Cdd:PRK07059 129 NFATTVQQVLAKTAvkhvvvasmgdllgfkghivNFvvrRVKKMVPAWSLPGHVRFNDaLAEGARQTFKPVKLGPDDVAF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKMTAHTHSSFglglsvngrfwldltPSDVMWNTSdtgWAKSAWSSvfsPWIQGACVFTHHLP------- 304
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRNI---------------VANVLQMEA---WLQPAFEK---KPRPDQLNFVCALPlyhifal 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 305 --------RFEPTSIL-----------QTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKW 364
Cdd:PRK07059 268 tvcgllgmRTGGRNILipnprdipgfiKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAERW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 365 RNKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglft 439
Cdd:PRK07059 348 LEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEIcirGPQVMAG------- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 440 hYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGE 518
Cdd:PRK07059 420 -YWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGE 498
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1034595494 519 VVKAFVVlnpdykSHDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK07059 499 AVKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFV 533
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
96-559 |
8.21e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 158.55 E-value: 8.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEACSlqRGDRVILILPRVPEWW-LANVACLRTGTVLI-----PGTTQLtqKDILYRLqssKAN 169
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGV--RAGDGVAVLARNHRGFvLALYAAGKVGARIIllntgFSGPQL--AEVAARE---GVK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 170 CIITNDVLAPAVDAVASKCENLHSKLIVSEN---SREGWGNLKELMKHASDSHTCVKTKHNEImaIFFTSGTSGYPKMTA 246
Cdd:PRK07788 149 ALVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLIAGSSTAPLPKPPKPGGI--VILTSGTTGTPKGAP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 247 HTHSSfglGLSVNGRFwLDLTP---SDVMWNTS----DTGWAKSAWSSVFspwiqGACVFTHHlpRFEPTSILQTLSKYP 319
Cdd:PRK07788 227 RPEPS---PLAPLAGL-LSRVPfraGETTLLPApmfhATGWAHLTLAMAL-----GSTVVLRR--RFDPEATLEDIAKHK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 320 ITVFCSAPT-VYRML--VQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE----TVlicGNFKGMK 392
Cdd:PRK07788 296 ATALVVVPVmLSRILdlGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvafaTI---ATPEDLA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 393 IKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKtaSTLRGnFYITGDRGYMDKDGYfW 472
Cdd:PRK07788 373 EAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV-----GNGFPFEGYTDGRDK--QIIDG-LLSSGDVGYFDEDGL-L 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 473 FVA-RADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEqlikEIQEHVKKTTA 551
Cdd:PRK07788 444 FVDgRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG-AALDED----AIKDYVRDNLA 518
|
....*...
gi 1034595494 552 PYKYPRKV 559
Cdd:PRK07788 519 RYKVPRDV 526
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-557 |
2.95e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 157.24 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDV------------LAPAV---DAVASKCENL-HSKLIVS--ENSREGWGNLKELMKHA---SDSHTCVKT---KH 226
Cdd:PRK12583 121 VICADAfktsdyhamlqeLLPGLaegQPGALACERLpELRGVVSlaPAPPPGFLAWHELQARGetvSREALAERQaslDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 227 NEIMAIFFTSGTSGYPKMTAHTHSSfglgLSVNGRF---WLDLTPSDVM------WNTSDTGWAKSAWSSVfspwiqGAC 297
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLcvpvplYHCFGMVLANLGCMTV------GAC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 298 VFthhLPR--FEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL-DIY 373
Cdd:PRK12583 271 LV---YPNeaFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 374 EGYGQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDigiqvLPNRPFGLFTHYVDNPSKTAS 450
Cdd:PRK12583 348 IAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGE-----LCTRGYSVMKGYWNNPEATAE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 451 TLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 529
Cdd:PRK12583 423 SIDEDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPG 502
|
490 500
....*....|....*....|....*...
gi 1034595494 530 YKSHDQeqlikEIQEHVKKTTAPYKYPR 557
Cdd:PRK12583 503 HAASEE-----ELREFCKARIAHFKVPR 525
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
83-554 |
3.61e-41 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 158.52 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 83 FWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYR 162
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 163 LQSSKANCIIT-NDV--------LAPAVDAVASKCENLHSKL---IVSENS----REG--WGNLKELMKHasDSHTCVKT 224
Cdd:PLN02654 188 IVDCKPKVVITcNAVkrgpktinLKDIVDAALDESAKNGVSVgicLTYENQlamkREDtkWQEGRDVWWQ--DVVPNYPT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 225 K-------HNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGAC 297
Cdd:PLN02654 266 KcevewvdAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGAT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 298 VFTHH-LPRF-EPTSILQTLSKYPITVFCSAPTVYRMLVQND---ITSYKFKSLKHCVSAGEPITPDVTEKWRNKTG--- 369
Cdd:PLN02654 346 VLVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsr 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 370 LDIYEGYGQTETvlicGNFKGMKI------KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlPNRPFGLFTHYVD 443
Cdd:PLN02654 426 CPISDTWWQTET----GGFMITPLpgawpqKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVK--KSWPGAFRTLYGD 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 444 NPSKTASTLR--GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVK 521
Cdd:PLN02654 500 HERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIY 579
|
490 500 510
....*....|....*....|....*....|....*
gi 1034595494 522 AFVVLNP--DYKSHDQEQLIKEIQEHVKKTTAPYK 554
Cdd:PLN02654 580 AFVTLVEgvPYSEELRKSLILTVRNQIGAFAAPDK 614
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
74-546 |
4.30e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 157.81 E-value: 4.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 74 AGKKPSNPAFWWI---NRNGEEMRWSFEELgsLSR--KFANILSeACSLQRGDRVILILPRVPE----WW---LANVAC- 140
Cdd:PRK07529 35 AARHPDAPALSFLldaDPLDRPETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPEthfaLWggeAAGIANp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 141 -------------LR-TGT-VLI-----PGTtqltqkDILYRLQSSKAnciitndvLAPAVDAV----ASKCENLHSKLI 196
Cdd:PRK07529 112 inpllepeqiaelLRaAGAkVLVtlgpfPGT------DIWQKVAEVLA--------ALPELRTVvevdLARYLPGPKRLA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 197 VSENSREG----WGNLKELMKHASDSHTCVKTKHNEIMAIFF-TSGTSGYPKMTAHTHSsfglGLSVNGrfW-----LDL 266
Cdd:PRK07529 178 VPLIRRKAhariLDFDAELARQPGDRLFSGRPIGPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WlgallLGL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 267 TPSDVMW--------NTSDTGwaksawssVFSPWIQGACVFThhlprfePTS-----------ILQTLSKYPITVFCSAP 327
Cdd:PRK07529 252 GPGDTVFcglplfhvNALLVT--------GLAPLARGAHVVL-------ATPqgyrgpgvianFWKIVERYRINFLSGVP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 328 TVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFD 406
Cdd:PRK07529 317 TVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 407 VKIV--DVNGNVLPPGQEGDIGIQVLPNrPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSS 484
Cdd:PRK07529 397 VRVVilDDAGRYLRDCAVDEVGVLCIAG-P-NVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRG 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034595494 485 GYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHV 546
Cdd:PRK07529 475 GHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPG-ASATEAELLAFARDHI 535
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
92-559 |
1.12e-40 |
|
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: 154.38 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 92 EMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 172 ItndvlapaVDAvaskcENLHSKLIVSENSREGWgnlkelmkhasdshTCVKTKHNEImAIFFTSGTSGYPKMTAHTHSS 251
Cdd:cd12118 106 F--------VDR-----EFEYEDLLAEGDPDFEW--------------IPPADEWDPI-ALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 252 FGLGLSVNGRFWlDLTPSDV-MWNTSD---TGWAksawssvfSPWIQGACVFTHH-LPRFEPTSILQTLSKYPITVFCSA 326
Cdd:cd12118 158 AYLNALANILEW-EMKQHPVyLWTLPMfhcNGWC--------FPWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 327 PTVYRMLVqNDITSYKfKSLKHCVS---AGEPITPDVTEKWRNKtGLDIYEGYGQTET---VLICgnfkgmKIKPGSMGK 400
Cdd:cd12118 229 PTVLNMLA-NAPPSDA-RPLPHRVHvmtAGAPPPAAVLAKMEEL-GFDVTHVYGLTETygpATVC------AWKPEWDEL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 401 PSP---------------AFDVKIVDVNGNVLPPGQEGDIGIQVLpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYM 465
Cdd:cd12118 300 PTEerarlkarqgvryvgLEEVDVLDPETMKPVPRDGKTIGEIVF--RGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 466 DKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQeqlikEIQEH 545
Cdd:cd12118 378 HPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE-----EIIAF 452
|
490
....*....|....
gi 1034595494 546 VKKTTAPYKYPRKV 559
Cdd:cd12118 453 CREHLAGFMVPKTV 466
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-562 |
1.67e-40 |
|
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: 151.09 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 226 HNEIMAIFFTSGTSGYPKMTAHTHSsfglGLSVNGrfW-----LDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGA-CVF 299
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHS----NEVYNA--WmlalnSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAhVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 300 THHLPRFEPT---SILQTLSKYPITVFCSAPTVYRMLVQNDITSyKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 376
Cdd:cd05944 75 AGPAGYRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 377 GQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIV--DVNGNVLPPGQEGDIGIQVLPNRpfGLFTHYVDNPSKTASTLR 453
Cdd:cd05944 154 GLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDEVGEICVAGP--GVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 454 GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSh 533
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVV- 310
|
330 340
....*....|....*....|....*....
gi 1034595494 534 DQEQLIKEIQEHVKKTTApykYPRKVGIL 562
Cdd:cd05944 311 EEEELLAWARDHVPERAA---VPKHIEVL 336
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
94-562 |
2.76e-40 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 154.52 E-value: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 NDVLA-----PAVDAVASKCENLHSKLIVSENSREGWG-NLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PRK06087 128 PTLFKqtrpvDLILPLQNQLPQLQQIVGVDKLAPATSSlSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVML 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 248 THSSFGLG-LSVNGRfwLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFThhLPRFEPTSILQTLSKYPITVFCSA 326
Cdd:PRK06087 208 THNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL--LDIFTPDACLALLEQQRCTCMLGA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 327 -PTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEK-WRNktGLDIYEGYGQTETV--LICGNFKGMKIKPGSMGKPS 402
Cdd:PRK06087 284 tPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVAREcQQR--GIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 403 PAFDVKIVDVNGNVLPPGQEGDiGIQVLPNrpfgLFTHYVDNPSKTASTL--RGNFYiTGDRGYMDKDGYFWFVARADDV 480
Cdd:PRK06087 362 AGVEIKVVDEARKTLPPGCEGE-EASRGPN----VFMGYLDEPELTARALdeEGWYY-SGDLCRMDEAGYIKITGRKKDI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 481 ILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQLIKEIQEhvkKTTAPYKYPRKVG 560
Cdd:PRK06087 436 IVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFSR---KRVAKYKYPEHIV 512
|
..
gi 1034595494 561 IL 562
Cdd:PRK06087 513 VI 514
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
232-562 |
4.34e-40 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 153.76 E-value: 4.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKMTAHTHSSFGLGLSVngrfWLDLTPsdvmWNTSDTGWAKSAwssVFSPWIQGACVFTHHLP------- 304
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKA----ILDRTP----WRAEEPTVIVAP---MFHAWGFSQLVLAASLActivtrr 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 305 RFEPTSILQTLSKYPITVFCSAPTVYRM---LVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET 381
Cdd:PRK13382 270 RFDPEATLDLIDRHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 382 VLIC-GNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGdiGIQVLPNRPFGLFThyvdnPSKTASTLRGnFYITG 460
Cdd:PRK13382 350 GMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVG--TIFVRNDTQFDGYT-----SGSTKDFHDG-FMASG 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 461 DRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdykshDQEQLIK 540
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GASATPE 496
|
330 340
....*....|....*....|..
gi 1034595494 541 EIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVL 518
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
90-548 |
4.53e-40 |
|
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: 153.17 E-value: 4.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 90 GEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEWWLAnVAClrTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYA-VPG--MGAVLHTINPRLFPEQIAYIINHA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 167 KANCIITNDVLAPAVDAVASKCENLHSKLIVSENSR------EGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSG 240
Cdd:cd12119 97 EDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 241 YPKMTAHTHSSFGLG-LSVNGRFWLDLTPSDV------MWNTSdtgwaksAWSSVFSPWIQGAC-VFTHhlPRFEPTSIL 312
Cdd:cd12119 177 NPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHVN-------AWGLPYAAAMVGAKlVLPG--PYLDPASLA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 313 QTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTET--VLICGnfk 389
Cdd:cd12119 248 ELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETspLGTVA--- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 390 gmKIKPG--------------SMGKPSPAFDVKIVDVNGNVLP--PGQEGDIgiQVlpnR-PFgLFTHYVDNPSKTASTL 452
Cdd:cd12119 324 --RPPSEhsnlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGEL--QV---RgPW-VTKSYYKNDEESEALT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 453 RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKS 532
Cdd:cd12119 396 EDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEG-AT 474
|
490
....*....|....*.
gi 1034595494 533 HDQEQLIKEIQEHVKK 548
Cdd:cd12119 475 VTAEELLEFLADKVAK 490
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
301-559 |
1.31e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 150.91 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 301 HHLPRFEPTSILQTLSKyPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE 380
Cdd:PRK07787 199 VHTGRPTPEAYAQALSE-GGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 381 TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlpnRPFGLFTHYVDNPSKTASTLRGN-FYIT 459
Cdd:PRK07787 278 TLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV---RGPTLFDGYLNRPDATAAAFTADgWFRT 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 460 GDRGYMDKDGYFWFVAR-ADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYkshDQEQL 538
Cdd:PRK07787 355 GDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV---AADEL 431
|
250 260
....*....|....*....|.
gi 1034595494 539 IkeiqEHVKKTTAPYKYPRKV 559
Cdd:PRK07787 432 I----DFVAQQLSVHKRPREV 448
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
78-559 |
2.24e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 151.00 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 78 PSNPAFWwINRNGEEMrwSFEELGSLSRKFANILSEAcSLQRGDRVILIL---PRVPEwwlANVACLRTGTVLIPGTTQL 154
Cdd:PRK13391 11 PDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 155 TQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIV-SENSREGWGNLKELMKHASDShtcVKTKHNEIMAIF 233
Cdd:PRK13391 84 TPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPAT---PIADESLGTDML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPK----------------MTAHTHSSFGLGlsvNGRFWLDLTPsdvMWNTsdtgwAKSAWSSVfspwIQ--G 295
Cdd:PRK13391 161 YSSGTTGRPKgikrplpeqppdtplpLTAFLQRLWGFR---SDMVYLSPAP---LYHS-----APQRAVML----VIrlG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 296 ACVFThhLPRFEPTSILQTLSKYPITVFCSAPTVY-RML-VQNDI-TSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDI 372
Cdd:PRK13391 226 GTVIV--MEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLkLPEEVrDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPII 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 373 YEGYGQTETVLICG-NFKGMKIKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIGIQvlPNRPFglftHYVDNPSKTAST 451
Cdd:PRK13391 304 HEYYAATEGLGFTAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFE--GGRPF----EYLNDPAKTAEA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 452 L--RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNP- 528
Cdd:PRK13391 377 RhpDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDg 456
|
490 500 510
....*....|....*....|....*....|..
gi 1034595494 529 -DYKSHDQEQLIKEIQEHVkkttAPYKYPRKV 559
Cdd:PRK13391 457 vDPGPALAAELIAFCRQRL----SRQKCPRSI 484
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
96-559 |
4.46e-39 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 151.18 E-value: 4.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLAPAVDAVASKCE---------------------NL---HSKLIVSENSREGWGNLKELMKHASdSHTC--VKTKHNEI 229
Cdd:PRK08751 132 NFGTTVQQVIADTPvkqvittglgdmlgfpkaalvNFvvkYVKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 230 MAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRfWLDLTpsdvmwNTSDTG-------------WAKSAWSSVFSPWiqGA 296
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAGT------GKLEEGcevvitalplyhiFALTANGLVFMKI--GG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 297 CvftHHL---PRFEPTSIlQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDI 372
Cdd:PRK08751 282 C---NHLisnPRDMPGFV-KELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 373 YEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfthYVDNPSKT 448
Cdd:PRK08751 358 VEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELcikGPQVMKG--------YWKRPEET 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 449 ASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVln 527
Cdd:PRK08751 430 AKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV-- 507
|
490 500 510
....*....|....*....|....*....|..
gi 1034595494 528 pdykSHDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08751 508 ----KKDPALTAEDVKAHARANLTGYKQPRII 535
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
94-561 |
7.45e-39 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 149.46 E-value: 7.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 N-DVLAPAVDAVASKCENLH--------SKLIVSENSR---------EGWgnlkeLMKHASDSHTCVKTKHNEImaifFT 235
Cdd:PRK12406 90 HaDLLHGLASALPAGVTVLSvptppeiaAAYRISPALLtppagaidwEGW-----LAQQEPYDGPPVPQPQSMI----YT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 236 SGTSGYPK------MTAHTHSSFGL------GLSVNGRFWLdltpSDVMWNTSDTGWAksawssVFSPWIQGACVFthhL 303
Cdd:PRK12406 161 SGTTGHPKgvrraaPTPEQAAAAEQmraliyGLKPGIRALL----TGPLYHSAPNAYG------LRAGRLGGVLVL---Q 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 304 PRFEPTSILQTLSKYPITVFCSAPTVY-RML-----VQNditSYKFKSLKHCVSAGEPITPDVT----EKWrnktGLDIY 373
Cdd:PRK12406 228 PRFDPEELLQLIERHRITHMHMVPTMFiRLLklpeeVRA---KYDVSSLRHVIHAAAPCPADVKramiEWW----GPVIY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 374 EGYGQTET--VLICGNFKGMKiKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNrpfGLFThYVDNPSKTAST 451
Cdd:PRK12406 301 EYYGSTESgaVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGN---PDFT-YHNKPEKRAEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 452 LRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyK 531
Cdd:PRK12406 376 DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-A 454
|
490 500 510
....*....|....*....|....*....|
gi 1034595494 532 SHDQEqlikEIQEHVKKTTAPYKYPRKVGI 561
Cdd:PRK12406 455 TLDEA----DIRAQLKARLAGYKVPKHIEI 480
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
303-559 |
1.97e-38 |
|
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: 147.91 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 303 LPRFEPTSILQTLSKYPITVFCSAPTVY-RML-----VQNditSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 376
Cdd:cd05929 200 MEKFDPEEFLRLIERYRVTFAQFVPTMFvRLLklpeaVRN---AYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 377 GQTETV-LICGNFKGMKIKPGSMGKPSPAfDVKIVDVNGNVLPPGQEGDIgiQVLPNRPFglftHYVDNPSKTA-STLRG 454
Cdd:cd05929 277 GGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEV--YFANGPGF----EYTNDPEKTAaARNEG 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 455 NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAfvVLNPDYKSHD 534
Cdd:cd05929 350 GWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADA 427
|
250 260
....*....|....*....|....*
gi 1034595494 535 QEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05929 428 GTALAEELIAFLRDRLSRYKCPRSI 452
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-562 |
3.01e-38 |
|
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: 146.82 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 117 LQRGDRVILILPRVPE--WWLANV--ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENlh 192
Cdd:cd05922 15 GVRGERVVLILPNRFTyiELSFAVayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 193 SKLIVSEnsrEGWgnlkelmKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRfwLDLTPSDV 271
Cdd:cd05922 93 PGTVLDA---DGI-------RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArSIAEY--LGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 272 MWNTSDTGWAkSAWSSVFSPWIQGACVFTHHLPRFePTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVS 351
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVL-DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 352 AGEPITPDVTEKWRNK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSPAFDVKIVDVNGNVLPPGQE 422
Cdd:cd05922 239 AGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 423 GDIGiqvlPNRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPS 502
Cdd:cd05922 313 GEIV----HRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 503 VAESAVVSSPDPIrGEVVKAFVVLNPDYKSHDqeqlikeIQEHVKKTTAPYKYPRKVGIL 562
Cdd:cd05922 389 IIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVV 440
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-548 |
3.04e-38 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 149.10 E-value: 3.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 74 AGKKPSNPAFWWiNRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:COG1022 21 AARFPDRVALRE-KEDGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 154 LTQKDILYRLQSSKANCIIT-NDVLAPAVDAVASKCENLhsKLIVSENSREGWG-----NLKELMKHASDSHT------- 220
Cdd:COG1022 99 SSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDdprllSLDELLALGREVADpaelear 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 221 CVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDV------MWNTSDTGWaksawsSVFSpWIQ 294
Cdd:COG1022 177 RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsflpLAHVFERTV------SYYA-LAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 295 GACVftHHLPRfePTSILQTLSKYPITVFCSAPTVYRMlVQNDITS---------------------------------- 340
Cdd:COG1022 249 GATV--AFAES--PDTLAEDLREVKPTFMLAVPRVWEK-VYAGIQAkaeeagglkrklfrwalavgrryararlagksps 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 341 --YKFK------------------SLKHCVSAGEPITPDVTEKWRNkTGLDIYEGYGQTET-VLICGNFKGmKIKPGSMG 399
Cdd:COG1022 324 llLRLKhaladklvfsklrealggRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETsPVITVNRPG-DNRIGTVG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 400 KPSPAFDVKIvdvngnvlppGQEGDI---GIQVlpnrpfglFTHYVDNPSKTASTLR--GNFYiTGDRGYMDKDGYFWFV 474
Cdd:COG1022 402 PPLPGVEVKI----------AEDGEIlvrGPNV--------MKGYYKNPEATAEAFDadGWLH-TGDIGELDEDGFLRIT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 475 ARADDVI-LSSGYRIGPFEVENALNEHPSVAESAVVsspdpirGE----VVkAFVVLNPD------------YKSHDQ-- 535
Cdd:COG1022 463 GRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEalgewaeenglpYTSYAEla 534
|
570
....*....|....*
gi 1034595494 536 --EQLIKEIQEHVKK 548
Cdd:COG1022 535 qdPEVRALIQEEVDR 549
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
72-559 |
3.13e-38 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 148.20 E-value: 3.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPAFwwIN-RNGEEMrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PLN02246 31 ERLSEFSDRPCL--IDgATGRVY--TYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 151 TTQLTQKDILYRLQSSKANCIITndvLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIM 230
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 231 AIFFTSGTSGYPKMTAHTHSsfGLGLSV---------NgrfwLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTh 301
Cdd:PLN02246 183 ALPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN----LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 302 hLPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDIT-SYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIY-EGYGQT 379
Cdd:PLN02246 256 -MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVeKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 380 E--TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTL- 452
Cdd:PLN02246 335 EagPVLaMCLAFakEPFPVKSGSCGTVVRNAELKIVDPEtGASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTId 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 453 RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYK- 531
Cdd:PLN02246 410 KDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEi 489
|
490 500
....*....|....*....|....*...
gi 1034595494 532 SHDqeqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PLN02246 490 TED------EIKQFVAKQVVFYKRIHKV 511
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
96-571 |
9.45e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 147.22 E-value: 9.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLAPAVDAVASKCENLHskLIVSENSrEGWGNLKELMKHASDSH----------------------------TCVKTKHN 227
Cdd:PRK05677 131 NMAHLAEKVLPKTGVKH--VIVTEVA-DMLPPLKRLLINAVVKHvkkmvpayhlpqavkfndalakgagqpvTEANPQAD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 228 EIMAIFFTSGTSGYPKMTAHTHSSfglgLSVNgrfWLDLTP--SDVMWNTSDTGWAKSAWSSVFSpwiqgacvFTHHL-- 303
Cdd:PRK05677 208 DVAVLQYTGGTTGVAKGAMLTHRN----LVAN---MLQCRAlmGSNLNEGCEILIAPLPLYHIYA--------FTFHCma 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 304 -------------PRFEPtSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTG 369
Cdd:PRK05677 273 mmlignhnilisnPRDLP-AMVKELGKWKFSGFVGLNTLFVALCNNeAFRKLDFSALKLTLSGGMALQLATAERWKEVTG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 370 LDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfthYVDNP 445
Cdd:PRK05677 352 CAICEGYGMTETSpVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELcvkGPQVMKG--------YWQRP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 446 SKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFV 524
Cdd:PRK05677 423 EATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFV 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1034595494 525 VLNPDykshdqEQLIKE-IQEHVKKTTAPYKYPRKV---GILIITNICSVL 571
Cdd:PRK05677 503 VVKPG------ETLTKEqVMEHMRANLTGYKVPKAVefrDELPTTNVGKIL 547
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-559 |
9.61e-38 |
|
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: 142.80 E-value: 9.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKMTAHTHSSFglgLSvNGRF---WLDLTPSDVM----------------WNTSDTGwaksawssvfspw 292
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI---VN-NGYFigeRLGLTEQDRLcipvplfhcfgsvlgvLACLTHG------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 293 iqGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGL- 370
Cdd:cd05917 70 --ATMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 371 DIYEGYGQTETVLICgnFKGMKIKP-----GSMGKPSPAFDVKIVDVNGNVLPP-GQEGDIGIqvlpnRPFGLFTHYVDN 444
Cdd:cd05917 146 DVTIAYGMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCI-----RGYSVMKGYWND 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 445 PSKTASTLRG-NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:cd05917 219 PEKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAW 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 1034595494 524 VVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05917 299 IRLKEGAELTEE-----DIKAYCKGKIAHYKVPRYV 329
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
74-559 |
1.77e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 145.41 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 74 AGKKPSNPAfwwINRNGEEMrwSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQ 153
Cdd:PRK06145 12 ARRTPDRAA---LVYRDQEI--SYAEFHQRILQAAGMLH-ARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 154 LTQKDILYRLQSSKANCIITNDVLAPAVDAVASKC-ENLHSKlivSENSREGWGNLKELMKHASdshtcvktKHNEIMAI 232
Cdd:PRK06145 86 LAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIvIDAAAQ---ADSRRLAQGGLEIPPQAAV--------APTDLVRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 233 FFTSGTSGYPKMTAHTHSSF---------GLGLSVNGRFW----------LDLTPSDVMWntsdtgwaksawssvfspwi 293
Cdd:PRK06145 155 MYTSGTTDRPKGVMHSYGNLhwksidhviALGLTASERLLvvgplyhvgaFDLPGIAVLW-------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 294 QGACVFTHHlpRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPiTP-----DVTEKWRNK 367
Cdd:PRK06145 215 VGGTLRIHR--EFDPEAVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEK-TPesrirDFTRVFTRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 368 TGLDiyeGYGQTETvliCGNFKGMKI-----KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfthYV 442
Cdd:PRK06145 292 RYID---AYGLTET---CSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRG-PKVTKG----YW 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 443 DNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKA 522
Cdd:PRK06145 361 KDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITA 440
|
490 500 510
....*....|....*....|....*....|....*..
gi 1034595494 523 FVVLNPdykshDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK06145 441 VVVLNP-----GATLTLEALDRHCRQRLASFKVPRQL 472
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
295-559 |
8.50e-37 |
|
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: 139.74 E-value: 8.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 295 GACVFthhLPRFEPTSILQTLSKYPIT-VFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGE---PITPDVTEkWRNKTGl 370
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwndMATVDTSP-WGRKPG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 371 diyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTA 449
Cdd:cd17636 142 ----GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 450 STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 529
Cdd:cd17636 212 RRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG 291
|
250 260 270
....*....|....*....|....*....|
gi 1034595494 530 yKSHDQEQLIkeiqEHVKKTTAPYKYPRKV 559
Cdd:cd17636 292 -ASVTEAELI----EHCRARIASYKKPKSV 316
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
221-570 |
4.95e-36 |
|
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: 141.31 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 221 CVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGL-SVNGRFwlDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVF 299
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 300 THHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQNdITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQT 379
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 380 ETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNV-LPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTASTLRGNFY 457
Cdd:cd05909 297 ECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRG-PN----VMLGYLNEPELTSFAFGDGWY 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 458 ITGDRGYMDKDGYFWFVARaddviLSSGYRIG----PFE-VENALNEH-PSVAESAVVSSPDPIRGEVVKAFVVLnpdyk 531
Cdd:cd05909 372 DTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTT----- 441
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034595494 532 sHDQEQLikEIQEHVKKTTAPykyprkvGILIITNICSV 570
Cdd:cd05909 442 -TDTDPS--SLNDILKNAGIS-------NLAKPSYIHQV 470
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
92-557 |
8.02e-36 |
|
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: 141.13 E-value: 8.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 92 EMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI 171
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKY-GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 172 ITNDVLAPAVDAVASKceNLHSKLIVSENSREGWGNLKELMK----------HASDSHTCVKTKHNEIMAIFFTSGTSGY 241
Cdd:cd17642 121 FCSKKGLQKVLNVQKK--LKIIKTIIILDSKEDYKGYQCLYTfitqnlppgfNEYDFKPPSFDRDEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 242 PKMTAHTHssfglgLSVNGRFWLDLTPSDVMWNTSDTgwaksAWSSVFsPWIQGACVFTH-----------HLPRFEPTS 310
Cdd:cd17642 199 PKGVQLTH------KNIVARFSHARDPIFGNQIIPDT-----AILTVI-PFHHGFGMFTTlgylicgfrvvLMYKFEEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 311 ILQTLSKYPITVFCSAPTVYRMLVQNDITS-YKFKSLKHCVSAGEPITPDVTEKWRNKTGLD-IYEGYGQTET---VLIC 385
Cdd:cd17642 267 FLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETtsaILIT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 386 GNfkgMKIKPGSMGKPSPAFDVKIVDVN-GNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRG 463
Cdd:cd17642 347 PE---GDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCV-----KGPMIMKGYVNNPEATKALIDKDGWLhSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 464 YMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLnpdykSHDQEQLIKEIQ 543
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL-----EAGKTMTEKEVM 493
|
490
....*....|....
gi 1034595494 544 EHVKKTTAPYKYPR 557
Cdd:cd17642 494 DYVASQVSTAKRLR 507
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
67-562 |
1.98e-35 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 140.19 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 67 QWTDK-------EKAGKKPSNPAFWWINRNGEEM-RWSFEELGSLSRKFANILSEaCSLQRGDRVILilpRVPEWWLANV 138
Cdd:PRK13295 20 HWHDRtinddldACVASCPDKTAVTAVRLGTGAPrRFTYRELAALVDRVAVGLAR-LGVGRGDVVSC---QLPNWWEFTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 139 ---ACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVL-----APAVDAVASKCENLHSKLIVSENSREGWGNL-- 208
Cdd:PRK13295 96 lylACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFrgfdhAAMARRLRPELPALRHVVVVGGDGADSFEALli 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 209 ---KELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSS-FGLGLSVNGRfwLDLTPSDVMWNTS----DTGW 280
Cdd:PRK13295 176 tpaWEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTlMANIVPYAER--LGLGADDVILMASpmahQTGF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 281 AKSAwssvFSPWIQGACVFTHHLprFEPTSILQTLSKYPITvFCSAPTVYRM-LVQN-DITSYKFKSLKHCVSAGEPITP 358
Cdd:PRK13295 254 MYGL----MMPVMLGATAVLQDI--WDPARAAELIRTEGVT-FTMASTPFLTdLTRAvKESGRPVSSLRTFLCAGAPIPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 359 DVTEKWRNKTGLDIYEGYGQTETVLICGnfkgmkIKPG--------SMGKPSPAFDVKIVDVNGNVLPPGQEGDIgiQVl 430
Cdd:PRK13295 327 ALVERARAALGAKIVSAWGMTENGAVTL------TKLDdpderastTDGCPLPGVEVRVVDADGAPLPAGQIGRL--QV- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 431 pnRPFGLFTHYVDNPSKTASTLRGnFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVS 510
Cdd:PRK13295 398 --RGCSNFGGYLKRPQLNGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVA 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1034595494 511 SPDPIRGEVVKAFVVLNPDyKSHDQEQLIKEIQEHvkKTTAPYkYPRKVGIL 562
Cdd:PRK13295 475 YPDERLGERACAFVVPRPG-QSLDFEEMVEFLKAQ--KVAKQY-IPERLVVR 522
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
228-562 |
2.10e-35 |
|
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: 136.09 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 228 EIMAIFFTSGTSGYPK--MTAHTHSsfgLGLSVNgrfWldltpSDVMWNTSDTGWA-----------KSAWSSVFspwIQ 294
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 295 GACVFTHHLprFEPTSILQTLSKYPITVFCSAPTVYR-MLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLD-I 372
Cdd:cd17638 67 GATVVPVAV--FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 373 YEGYGQTE--TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDvNGNVLPPGqegdigiqvlPNRPFGlfthYVDNPSKTAS 450
Cdd:cd17638 145 LTAYGLTEagVATMCRPGDDAETVATTCGRACPGFEVRIAD-DGEVLVRG----------YNVMQG----YLDDPEATAE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 451 TLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 529
Cdd:cd17638 210 AIDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG 289
|
330 340 350
....*....|....*....|....*....|...
gi 1034595494 530 yKSHDQEQLIKEIQEHVkkttAPYKYPRKVGIL 562
Cdd:cd17638 290 -VTLTEEDVIAWCRERL----ANYKVPRFVRFL 317
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
95-559 |
2.54e-35 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 140.11 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 175 DvlapavdAVASKCENLHSKLIV-SENSREGWGNLKELMK---HASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTH- 249
Cdd:PLN02330 135 D-------TNYGKVKGLGLPVIVlGEEKIEGAVNWKELLEaadRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHr 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 250 --------SSFGLGLSVNGRF-WLDLTPSDVMWNtsdtgwaksawssvfspwIQGACVFTHH-------LPRFEPTSILQ 313
Cdd:PLN02330 208 nlvanlcsSLFSVGPEMIGQVvTLGLIPFFHIYG------------------ITGICCATLRnkgkvvvMSRFELRTFLN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 314 TLSKYPITVFCSAPTVYRMLVQN------DITSYKFKSLkhcVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTETVLICG 386
Cdd:PLN02330 270 ALITQEVSFAPIVPPIILNLVKNpiveefDLSKLKLQAI---MTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 387 NF----KGMKI-KPGSMGKPSPAFDVKIVDV-NGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYI-T 459
Cdd:PLN02330 347 THgdpeKGHGIaKKNSVGFILPNLEVKFIDPdTGRSLPKNTPGELCV-----RSQCVMQGYYNNKEETDRTIDEDGWLhT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 460 GDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQeqli 539
Cdd:PLN02330 422 GDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEE---- 497
|
490 500
....*....|....*....|
gi 1034595494 540 kEIQEHVKKTTAPYKYPRKV 559
Cdd:PLN02330 498 -DILNFVAANVAHYKKVRVV 516
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
72-556 |
4.90e-35 |
|
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: 138.18 E-value: 4.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:cd17646 6 EQAARTPDAPAVVD-----EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 152 TQLTQKDILYRLQSSKANCIITNDVLA---PAVDAVASKCEnlhsklivsensregwgnlkELMKHASDSHTCVKTKHNE 228
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAarlPAGGDVALLGD--------------------EALAAPPATPPLVPPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 229 IMAIFFTSGTSGYPKMTAHTHSSFglglsVNGRFWL----DLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFTHHL 303
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGI-----VNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVARPG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 304 PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQnDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET-- 381
Cdd:cd17646 214 GHRDPAYLAALIREHGVTTCHFVPSMLRVFLA-EPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAai 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 382 -VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQV---LPNRPfGLfT--HYVDNPSKTASTL 452
Cdd:cd17646 293 dVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELylgGVQLargYLGRP-AL-TaeRFVPDPFGPGSRM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 453 rgnfYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKS 532
Cdd:cd17646 371 ----YRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAG 446
|
490 500
....*....|....*....|....
gi 1034595494 533 HDQEQLikeiQEHVKKTTAPYKYP 556
Cdd:cd17646 447 PDTAAL----RAHLAERLPEYMVP 466
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
95-548 |
6.70e-35 |
|
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: 137.34 E-value: 6.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 95 WSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAnciitn 174
Cdd:cd05907 6 ITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 175 dvlapavdavaskcenlhsKLIVSENSregwgnlkelmkhasdSHTCVktkhneimaIFFTSGTSGYPKMTAHTHSSFgl 254
Cdd:cd05907 79 -------------------KALFVEDP----------------DDLAT---------IIYTSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 255 glsvngrfwldltpsdvMWN--TSDTGWAKSAWSSVFS----------------PWIQGACVFthHLPRFEptSILQTLS 316
Cdd:cd05907 113 -----------------LSNalALAERLPATEGDRHLSflplahvferraglyvPLLAGARIY--FASSAE--TLLDDLS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 317 KYPITVFCSAPTVYRML----VQNDITSYK--------FKSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETV-L 383
Cdd:cd05907 172 EVRPTVFLAVPRVWEKVyaaiKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFFR-ALGIPVYEGYGLTETSaV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 384 ICGNFKGmKIKPGSMGKPSPAFDVKIVDVNgnvlppgqEgdigIQVlpnRPFGLFTHYVDNPSKTA-STLRGNFYITGDR 462
Cdd:cd05907 251 VTLNPPG-DNRIGTVGKPLPGVEVRIADDG--------E----ILV---RGPNVMLGYYKNPEATAeALDADGWLHTGDL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 463 GYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALNEHPSVAESAVVSSPDPirgeVVKAFVVLNPDY-----KSHD-- 534
Cdd:cd05907 315 GEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEAleawaEEHGia 390
|
490 500
....*....|....*....|...
gi 1034595494 535 ---------QEQLIKEIQEHVKK 548
Cdd:cd05907 391 ytdvaelaaNPAVRAEIEAAVEA 413
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
117-562 |
7.71e-34 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 137.09 E-value: 7.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLapavdavaskCENLHSKLI 196
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDAL----------RDRFQPSRV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 197 V------SENSREGWGNLKELMKHASDSHTcvktkhneimaifFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSD 270
Cdd:PRK06060 122 AeaaelmSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPED 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 271 VMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHLP-RFEPTSILQTlsKYPITVFCSAPTVYRMLVqNDITSYKFKSLKHC 349
Cdd:PRK06060 189 TGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPvTPEAAAILSA--RFGPSVLYGVPNFFARVI-DSCSPDSFRSLRCV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 350 VSAGEPITPDVTEKWRNK-TGLDIYEGYGQTEtvlICGNFKGMKI---KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI 425
Cdd:PRK06060 266 VSAGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 426 GI------QVLPNRPFGLFTHyvdnpsktastlrGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNE 499
Cdd:PRK06060 343 WVrgpaiaKGYWNRPDSPVAN-------------EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIE 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034595494 500 HPSVAESAVVSSPDPIRGEVVKAFVVlnPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK06060 410 DEAVAEAAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVV 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
96-559 |
1.02e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 135.33 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLAPAVDAVASKCENLH---SKLIVSENSREGW---------------------GNLKELMKHASD-SHTCVKTKHNEIM 230
Cdd:PRK12492 131 MFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvntvvdkvkkmvpayhlpqaVPFKQALRQGRGlSLKPVPVGLDDIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 231 AIFFTSGTSGYPKMTAHTHSSfglgLSVN--------GRFWLDLTPsdVMWNTSDTGWAKSAWSSVFSPWIQGACVF--- 299
Cdd:PRK12492 211 VLQYTGGTTGLAKGAMLTHGN----LVANmlqvraclSQLGPDGQP--LMKEGQEVMIAPLPLYHIYAFTANCMCMMvsg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 300 THHLPRFEPTSI---LQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEG 375
Cdd:PRK12492 285 NHNVLITNPRDIpgfIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 376 YGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLPNrpfglfthYVDNPSKTAST 451
Cdd:PRK12492 365 YGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELcikGPQVMKG--------YWQQPEATAEA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 452 LRGN-FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVlnpdy 530
Cdd:PRK12492 437 LDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVV----- 511
|
490 500
....*....|....*....|....*....
gi 1034595494 531 kSHDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK12492 512 -ARDPGLSVEELKAYCKENFTGYKVPKHI 539
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
90-529 |
1.17e-33 |
|
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: 134.39 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 90 GEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 170 CIITNDVLAPAVDAVAskcenlhskLIVSENSREGWGNLkelmkhASDSHTCVKTKHNEIMAIFfTSGTSGYPKMTAHTH 249
Cdd:cd17651 95 LVLTHPALAGELAVEL---------VAVTLLDQPGAAAG------ADAEPDPALDADDLAYVIY-TSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 250 SSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfthHLP----RFEPTSILQTLSKYPIT 321
Cdd:cd17651 159 RSL-----ANLVAWQArassLGPGARTLQFAGLGFDVSVQE-IFSTLCAGATL---VLPpeevRTDPPALAAWLDEQRIS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 322 VfCSAPTVY--RMLVQNDITSYKFKSLKHCVSAGEP--ITPDVTEKWRNKTGLDIYEGYGQTE----TVLICGNFKGMKI 393
Cdd:cd17651 230 R-VFLPTVAlrALAEHGRPLGVRLAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTEthvvTALSLPGDPAAWP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 394 KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPfGLfTH--YVDNPSKTASTLrgnfYITGDRGYM 465
Cdd:cd17651 309 APPPIGRPIDNTRVYVLDAALRPVPPGVPGELyigGAGLARgylNRP-EL-TAerFVPDPFVPGARM----YRTGDLARW 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034595494 466 DKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 529
Cdd:cd17651 383 LPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE 446
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
117-535 |
2.60e-32 |
|
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: 130.32 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttqltqkdILYRLQSSKANCIITNDVLAPAVDAVASKcenlhskli 196
Cdd:cd05923 50 LRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL---------INPRLKAAELAELIERGEMTAAVIAVDAQ--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 197 VSENSREGWGNLKELMKHASDSHTCVKTKHNEIMA--------IFFTSGTSGYPK---------------MTAHTHSSFG 253
Cdd:cd05923 112 VMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPrepeqpafVFYTSGTTGLPKgavipqraaesrvlfMSTQAGLRHG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 254 LGLSVngrfwLDLTPsdvMWNTSdtgwaksAWSSVFSpwiqGACVF--THHLPR-FEPTSILQTLSKYPITVFCSAPTVY 330
Cdd:cd05923 192 RHNVV-----LGLMP---LYHVI-------GFFAVLV----AALALdgTYVVVEeFDPADALKLIEQERVTSLFATPTHL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 331 RMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVlicgNFKGMK-IKPGSMGKPSPAFDVK 408
Cdd:cd05923 253 DALAAAaEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM----NSLYMRdARTGTEMRPGFFSEVR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 409 IVDVNGNV---LPPGQEGDIGIQVLPNRPFglfTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSG 485
Cdd:cd05923 329 IVRIGGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGG 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1034595494 486 YRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQ 535
Cdd:cd05923 406 ENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADE 455
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
228-567 |
4.75e-32 |
|
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: 126.61 E-value: 4.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 228 EIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHlpRFE 307
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE--NTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 PTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAG--EPITPDVTEKWRNKTgLDIYEGYGQTET-VLI 384
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGgsRAIAADVRFIEATGL-TNTAQVYGLSETgTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 385 CGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNRPFGlfthYVDNPSKTASTLRGNFYITGDRGY 464
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS-PANMLG----YWNNPERTAEVLIDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 465 MDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpdykSHDQEQLIKEIQE 544
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----AELDENAIRALKH 309
|
330 340
....*....|....*....|...
gi 1034595494 545 HVKKTTAPYKYPRKvgILIITNI 567
Cdd:cd17635 310 TIRRELEPYARPST--IVIVTDI 330
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
94-559 |
5.51e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 129.54 E-value: 5.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILsEACSLQRGDRvILILPRVPEWWLA-NVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCII 172
Cdd:PRK09088 22 RWTYAELDALVGRLAAVL-RRRGCVDGER-LAVLARNSVWLVAlHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 173 TNDVLApavdavASKCENLhsklivsensregwgNLKELMKHAsDSHTCVKTKH---NEIMAIFFTSGTSGYPK--MTA- 246
Cdd:PRK09088 100 GDDAVA------AGRTDVE---------------DLAAFIASA-DALEPADTPSippERVSLILFTSGTSGQPKgvMLSe 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 247 ----HTHSSFGLGLSVNGR--FWLDlTPsdvMWNTsdTGWAksawSSVFSPWIQGACVFTHhlPRFEPTSILQTLS--KY 318
Cdd:PRK09088 158 rnlqQTAHNFGVLGRVDAHssFLCD-AP---MFHI--IGLI----TSVRPVLAVGGSILVS--NGFEPKRTLGRLGdpAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 319 PITVFCSAPTVYRML-VQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGYGQTE--TVLicgnfkGMKI-- 393
Cdd:PRK09088 226 GITHYFCVPQMAQAFrAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEagTVF------GMSVdc 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 394 -----KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTASTLRGN-FYITGDRGYMDK 467
Cdd:PRK09088 299 dviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRG-PN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 468 DGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdykshDQEQLIKEIQEHVK 547
Cdd:PRK09088 374 DGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD-----GAPLDLERIRSHLS 448
|
490
....*....|..
gi 1034595494 548 KTTAPYKYPRKV 559
Cdd:PRK09088 449 TRLAKYKVPKHL 460
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
91-559 |
3.19e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 127.76 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDVLAPAVDAVASKCENLhsKLIV--------SENSREGWGNLKELMKHAsDSHTCVKTKHNEIMAIF--FTSGTSG 240
Cdd:PRK08162 119 LIVDTEFAEVAREALALLPGP--KPLVidvddpeyPGGRFIGALDYEAFLASG-DPDFAWTLPADEWDAIAlnYTSGTTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 241 YPKMTAHTHSSFGLGLSVNGRFWlDLTPSDV-MW-------NtsdtGWAksawssvFsPWIQGACVFTH-HLPRFEPTSI 311
Cdd:PRK08162 196 NPKGVVYHHRGAYLNALSNILAW-GMPKHPVyLWtlpmfhcN----GWC-------F-PWTVAARAGTNvCLRKVDPKLI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 312 LQTLSKYPITVFCSAPTVYRMLVqNDITSYKfKSLKHCVS---AGEPITPDVTEKWRNkTGLDIYEGYGQTET---VLIC 385
Cdd:PRK08162 263 FDLIREHGVTHYCGAPIVLSALI-NAPAEWR-AGIDHPVHamvAGAAPPAAVIAKMEE-IGFDLTHVYGLTETygpATVC 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 386 --------------GNFKGMK------------IKPGSMgKPSPAFDVKI--VDVNGNVLPPGqegdigiqvlpnrpfgl 437
Cdd:PRK08162 340 awqpewdalplderAQLKARQgvryplqegvtvLDPDTM-QPVPADGETIgeIMFRGNIVMKG----------------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 438 fthYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRG 517
Cdd:PRK08162 402 ---YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWG 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1034595494 518 EVVKAFVVLNPDyKSHDQEqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08162 479 EVPCAFVELKDG-ASATEE----EIIAHCREHLAGFKVPKAV 515
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
72-556 |
1.11e-30 |
|
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: 125.52 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPA--FwwinrngEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIP 149
Cdd:cd17655 5 EQAEKTPDHTAvvF-------EDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 150 GTTQLTQKDILYRLQSSKANCIITNDVLAPAVDavaskcenlHSKLIVSENSREGwgnlkelmKHASDSHTCVKTKHNEI 229
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLTQSHLQPPIA---------FIGLIDLLDEDTI--------YHEESENLEPVSKSDDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 230 MAIFFTSGTSGYPKMTAHTHSSFglglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTH-HLP 304
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHRGV-----VNLVEWANkviyQGEHLRVALFASISFDASVTE-IFASLLSGNTLYIVrKET 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 305 RFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKW--RNKTGLDIYEGYGQTETV 382
Cdd:cd17655 214 VLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 383 LIC--GNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIGI------QVLPNRPFGLFTHYVDNPSKTAstl 452
Cdd:cd17655 292 VDAsiYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIggegvaRGYLNRPELTAEKFVDDPFVPG--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 453 rGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKs 532
Cdd:cd17655 369 -ERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP- 446
|
490 500
....*....|....*....|....
gi 1034595494 533 hdqeqlIKEIQEHVKKTTAPYKYP 556
Cdd:cd17655 447 ------VAQLREFLARELPDYMIP 464
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
90-565 |
1.87e-30 |
|
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: 124.48 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 90 GEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAn 169
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLL-KINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 170 ciitndvlapavdavaskcenlhSKLIVSENsregwgnlkelmkhasdshtcvktkhNEIMAIFFTSGTSGYPKMTAHTH 249
Cdd:cd05914 81 -----------------------KAIFVSDE--------------------------DDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 250 SSfgLGLSVNGRFWLD-LTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVftHHLPRFePTSILQTLSKYPITVFCSAPT 328
Cdd:cd05914 112 RN--IVSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKI-PSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 329 VYRM--------LVQNDITSYKFK------------------------SLKHCVSAGEPITPDVTEKWRnKTGLDIYEGY 376
Cdd:cd05914 187 PLVIekifkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLR-TIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 377 GQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKIVDVNgnvlPPGQEGDIgiQVlpnRPFGLFTHYVDNPSKTAS--TLR 453
Cdd:cd05914 266 GMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEI--IV---RGPNVMKGYYKNPEATAEafDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 454 GNFYiTGDRGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALNEHPSVAESAVVsspdpIRGEVVKAFVVLNPDY-- 530
Cdd:cd05914 336 GWFH-TGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFld 409
|
490 500 510
....*....|....*....|....*....|....*....
gi 1034595494 531 -KSHDQEQLIKEIQEHVKK---TTAPyKYPRKVGILIIT 565
Cdd:cd05914 410 vKALKQRNIIDAIKWEVRDkvnQKVP-NYKKISKVKIVK 447
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
91-556 |
2.56e-30 |
|
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: 124.62 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDVLAPAVDavaskcENLHSKLIVSENSREGWGNLKelmkHASDSHTCvktkhneimA-IFFTSGTSGYPKMTAHTH 249
Cdd:cd12117 98 LLTDRSLAGRAG------GLEVAVVIDEALDAGPAGNPA----VPVSPDDL---------AyVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 250 SSFgLGLsVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVF---THHLPRfePTSILQTLSKYPITV-FCS 325
Cdd:cd12117 159 RGV-VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTFE-IWGALLNGARLVlapKGTLLD--PDALGALIAEEGVTVlWLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 326 APtVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTE--TVLICGNFKGMKIKPGS--MGK 400
Cdd:cd12117 234 AA-LFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEntTFTTSHVVTELDEVAGSipIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 401 PSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFTHYVDNPSKTASTLrgnfYITGDRGYMDKDGYFWFV 474
Cdd:cd12117 311 PIANTRVYVLDEDGRPVPPGVPGELyvgGDGLALgylNRPALTAERFVADPFGPGERL----YRTGDLARWLPDGRLEFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 475 ARADDVILSSGYRIGPFEVENALNEHPSVAESAV-VSSPDPIRGEVVkAFVVLNPDyKSHDqeqlikEIQEHVKKTTAPY 553
Cdd:cd12117 387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVVAEGA-LDAA------ELRAFLRERLPAY 458
|
...
gi 1034595494 554 KYP 556
Cdd:cd12117 459 MVP 461
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
96-559 |
5.88e-30 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 124.18 E-value: 5.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLipgttqlTQKDILYRLQSSKANCIITND 175
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIV-------TTMNPSSSLGEIKKRVVDCSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLAPAVDAVASKCENLHSKLI-VSEN-----SREGWGNLKELMKhaSDSHTCVK--TKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PLN02574 141 GLAFTSPENVEKLSPLGVPVIgVPENydfdsKRIEFPKFYELIK--EDFDFVPKpvIKQDDVAAIMYSSGTTGASKGVVL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 248 THSSFGLGLSVNGRFwldltpsdvmwntSDTGWAKSAWSSVFSP-----WIQGACVFTHHL----------PRFEPTSIL 312
Cdd:PLN02574 219 THRNLIAMVELFVRF-------------EASQYEYPGSDNVYLAalpmfHIYGLSLFVVGLlslgstivvmRRFDASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 313 QTLSKYPITVFCSAPTVYRMLVQN--DITSYKFKSLKHCVSAGEPITPDVTEKW-RNKTGLDIYEGYGQTETVLICG--- 386
Cdd:PLN02574 286 KVIDRFKVTHFPVVPPILMALTKKakGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTESTAVGTrgf 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 387 NFKGMKiKPGSMGKPSPAFDVKIVD-VNGNVLPPGQEGDIGIQvlpnRPfGLFTHYVDNPSKTASTLRGNFYI-TGDRGY 464
Cdd:PLN02574 366 NTEKLS-KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ----GP-GVMKGYLNNPKATQSTIDKDGWLrTGDIAY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 465 MDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLIkeiqE 544
Cdd:PLN02574 440 FDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG-STLSQEAVI----N 514
|
490
....*....|....*
gi 1034595494 545 HVKKTTAPYKYPRKV 559
Cdd:PLN02574 515 YVAKQVAPYKKVRKV 529
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
217-556 |
6.27e-30 |
|
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: 122.86 E-value: 6.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 217 DS-HTCVKTKHNEIMA-IFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPSDVMWNTSDTGWaKSAWSSVFSPWIQ 294
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 295 GACVFTHHLPRFEPTSILQTL-SKYPITVFCSAPTVYRMLVQ--NDITSYKFKSLKHCVSAGEPITPDVTEKWRnKTGLD 371
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVLDLPPAYLQQLAEeaDRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 372 IYEGYGQTETVLICGNFK---GMKIKPGSM--GKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQVLP----NRPfGLfTH 440
Cdd:cd17649 239 LFNAYGPTEATVTPLVWKceaGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGEGLArgylGRP-EL-TA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 441 --YVDNPSKTAStlrGNFYITGD--RgYMDkDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIR 516
Cdd:cd17649 317 erFVPDPFGAPG---SRLYRTGDlaR-WRD-DGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGG 391
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1034595494 517 GEVVkAFVVLNPDYKshdQEQLIKEIQEHVKKTTAPYKYP 556
Cdd:cd17649 392 KQLV-AYVVLRAAAA---QPELRAQLRTALRASLPDYMVP 427
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
232-557 |
2.10e-29 |
|
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: 118.59 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKMTAHT-----HSSFG----LGLSVNGRfWLDLTPS------DVMWNtsdtgWAKSAWSSVFSPWIQGA 296
Cdd:cd17630 5 VILTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDS-WLLSLPLyhvgglAILVR-----SLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 297 cvfthhlprfeptsiLQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKtGLDIYEGY 376
Cdd:cd17630 79 ---------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 377 GQTETV-LICGNFKGMKiKPGSMGKPSPAFDVKIVDvngnvlppgqEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGN 455
Cdd:cd17630 143 GMTETAsQVATKRPDGF-GRGGVGVLLPGRELRIVE----------DGEIWV-----GGASLAMGYLRGQLVPEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 456 FYiTGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPdykSHDQ 535
Cdd:cd17630 207 FT-TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG---PADP 282
|
330 340
....*....|....*....|..
gi 1034595494 536 EQLIkeiqEHVKKTTAPYKYPR 557
Cdd:cd17630 283 AELR----AWLKDKLARFKLPK 300
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
58-559 |
9.40e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 120.38 E-value: 9.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 58 FNFAkDVLDQWTDKekagkKPSNPAFWWINRngeemRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLAN 137
Cdd:PRK07798 3 WNIA-DLFEAVADA-----VPDRVALVCGDR-----RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 138 VACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIV---SENSREGWGNLKELMKH 214
Cdd:PRK07798 71 LGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVedgSGNDLLPGAVDYEDALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 215 ASDSHTCVKTKHNEIMAIFFTSGTSGYPK--MTAHT---HSSFGLGLSVNGRF------------------WLDLTPsdV 271
Cdd:PRK07798 151 AGSPERDFGERSPDDLYLLYTGGTTGMPKgvMWRQEdifRVLLGGRDFATGEPiedeeelakraaagpgmrRFPAPP--L 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 272 MWNTSDtgWAksAWSSVFSpwiqGACVFTHHLPRFEPTSILQTLSKYPITV-FCSAPTVYRMLVQ--NDITSYKFKSLKH 348
Cdd:PRK07798 229 MHGAGQ--WA--AFAALFS----GQTVVLLPDVRFDADEVWRTIEREKVNViTIVGDAMARPLLDalEARGPYDLSSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 349 CVSAGEPITPDVTEKWR----NKTGLDiyeGYGQTETvlicgNFKGMKI-KPGSMGKPSPAF----DVKIVDVNGNVLPP 419
Cdd:PRK07798 301 IASGGALFSPSVKEALLellpNVVLTD---SIGSSET-----GFGGSGTvAKGAVHTGGPRFtigpRTVVLDEDGNPVEP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 420 GqEGDIG-IQVLPNRPFGlfthYVDNPSKTASTLR---GNFY-ITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVE 494
Cdd:PRK07798 373 G-SGEIGwIARRGHIPLG----YYKDPEKTAETFPtidGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVE 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034595494 495 NALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK07798 448 EALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAI 507
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
91-529 |
9.97e-29 |
|
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: 122.27 E-value: 9.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDVLAPAVDAVASKCENLHSKLIVSENSregwGNLKElmkHASDSHTCVktkhneimaIFFTSGTSGYPKMTAHTHS 250
Cdd:COG1020 577 VLTQSALAARLPELGVPVLALDALALAAEPA----TNPPV---PVTPDDLAY---------VIYTSGSTGRPKGVMVEHR 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 251 SFG-LGLSVNGRFwlDLTPSDVM-WNTS---DTgwakSAWSsVFSPWIQGACVfthHLP----RFEPTSILQTLSKYPIT 321
Cdd:COG1020 641 ALVnLLAWMQRRY--GLGPGDRVlQFASlsfDA----SVWE-IFGALLSGATL---VLAppeaRRDPAALAELLARHRVT 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 322 VFCSAPTVYRMLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTETVL--ICGNFKGMKIKPGSM 398
Cdd:COG1020 711 VLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVdsTYYEVTPPDADGGSV 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 399 --GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQV----LpNRPfGL----FthyVDNPSKTASTlRgnFYITGDRGYM 465
Cdd:COG1020 789 piGRPIANTRVYVLDAHLQPVPVGVPGELyigGAGLargyL-NRP-ELtaerF---VADPFGFPGA-R--LYRTGDLARW 860
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034595494 466 DKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 529
Cdd:COG1020 861 LPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG 924
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
63-556 |
1.77e-28 |
|
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: 119.48 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 63 DVLDQWtdkekAGKKPSNPAFwwInrnGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:COG1021 29 DLLRRR-----AERHPDRIAV--V---DGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 143 TGtvLIPGTT--QLTQKDILYRLQSSKANCIITNDV-----LAPAVDAVASKCENLhsKLIVSENSREGWGNLKELMKHA 215
Cdd:COG1021 98 AG--AIPVFAlpAHRRAEISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVPSL--RHVLVVGDAGEFTSLDALLAAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 216 SDSHTCvkTKHNEIMAIFFTS-GTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMW-------NtsdtgwakSAWSS 287
Cdd:COG1021 174 ADLSEP--RPDPDDVAFFQLSgGTTGLPKLIPRTHDDYLYSVRASAEIC-GLDADTVYLaalpaahN--------FPLSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 288 --VFSPWIQGACVFTHhlPRFEPTSILQTLSKYPITVFCSAPTVYRMLVQ-NDITSYKFKSLKHCVSAGEPITPDVTEKW 364
Cdd:COG1021 243 pgVLGVLYAGGTVVLA--PDPSPDTAFPLIERERVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPELARRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 365 RNKTGLDIYEGYG-------QT------ETVLicgnfkgmkikpGSMGKP-SPAFDVKIVDVNGNVLPPGQEGdigiqVL 430
Cdd:COG1021 321 RPALGCTLQQVFGmaeglvnYTrlddpeEVIL------------TTQGRPiSPDDEVRIVDEDGNPVPPGEVG-----EL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 431 PNRPFGLFTHYVDNPSKTAS--TLRGnFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV 508
Cdd:COG1021 384 LTRGPYTIRGYYRAPEHNARafTPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAV 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034595494 509 VSSPDPIRGEVVKAFVVLNpdykshDQEQLIKEIQEHVK-KTTAPYKYP 556
Cdd:COG1021 463 VAMPDEYLGERSCAFVVPR------GEPLTLAELRRFLReRGLAAFKLP 505
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
94-546 |
3.04e-28 |
|
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: 117.41 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd17653 22 SLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 NDvlapAVDAVAskcenlhsklivsensregwgnlkelmkhasdshtcvktkhneimAIFFTSGTSGYPKMTAHTHSSFg 253
Cdd:cd17653 101 TD----SPDDLA---------------------------------------------YIIFTSGSTGIPKGVMVPHRGV- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 254 LGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAcvfthHLPRFEPTSILQTLSKyPITVFCSAPTVYRML 333
Cdd:cd17653 131 LNYVSQPPARLDVGPGSRVAQVLSIAFDACIGE-IFSTLCNGG-----TLVLADPSDPFAHVAR-TVDALMSTPSILSTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 334 VQNDitsykFKSLKHCVSAGEPITPDVTEKWRNktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVN 413
Cdd:cd17653 204 SPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDAD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 414 GNVLPPGQEGDI---GIQVLPNrpfglfthYVDNPSKTASTLRGN-------FYITGDRGYMDKDGYFWFVARADDVILS 483
Cdd:cd17653 277 LQPVPEGVVGEIcisGVQVARG--------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGREDNQVKV 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034595494 484 SGYRIGPFEVENALNEHPSVAESAVVSSpdpIRGEVVkAFVVlnPDykSHDQEQLIKEIQEHV 546
Cdd:cd17653 349 RGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PE--TVDVDGLRSELAKHL 403
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
90-528 |
7.69e-28 |
|
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: 117.04 E-value: 7.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 90 GEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 170 CIITNDVLAPavdavaskcenlhsklivsensregwgnlkelMKHASDSHTcVKTKHNEIMAIFFTSGTSGYPKMTAHTH 249
Cdd:cd05920 115 AYIVPDRHAG--------------------------------FDHRALARE-LAESIPEVALFLLSGGTTGTPKLIPRTH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 250 SSFGLGLSvngrfwldlTPSDVMWNTSDT----------GWAKSAWSSVFSPWIQGACVFThhlPRFEPTSILQTLSKYP 319
Cdd:cd05920 162 NDYAYNVR---------ASAEVCGLDQDTvylavlpaahNFPLACPGVLGTLLAGGRVVLA---PDPSPDAAFPLIEREG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 320 ITVFCSAPTVYRMLVQNDITS-YKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLicgNFKGM----KIK 394
Cdd:cd05920 230 VTVTALVPALVSLWLDAAASRrADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL---NYTRLddpdEVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 395 PGSMGKP-SPAFDVKIVDVNGNVLPPGQEGdigiQVLPNRPFgLFTHYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFW 472
Cdd:cd05920 307 IHTQGRPmSPDDEIRVVDEEGNPVPPGEEG----ELLTRGPY-TIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLV 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034595494 473 FVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNP 528
Cdd:cd05920 382 VEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD 437
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
91-545 |
1.14e-27 |
|
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: 116.24 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDVLapavdavaskCENLHSKLIVSEnsregwgnLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHS 250
Cdd:cd12116 88 VLTDDAL----------PDRLPAGLPVLL--------LALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 251 SF-GLGLSVNGRfwLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVftHHLPR---FEPTSILQTLSKYPITVFCSA 326
Cdd:cd12116 150 NLvNFLHSMRER--LGLGPGDRLLAVTTYAFDISLLE-LLLPLLAGARV--VIAPRetqRDPEALARLIEAHSITVMQAT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 327 PTVYRMLVQNDitsykFKSLKH----CvsAGEPITPDVTEKWRNKTGlDIYEGYGQTETVL------ICGNFKGMKIkpg 396
Cdd:cd12116 225 PATWRMLLDAG-----WQGRAGltalC--GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 397 smGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFTHYVDNPSKTAstlRGNFYITGDRGYMDKDGY 470
Cdd:cd12116 294 --GRPLANTQVYVLDAALRPVPPGVPGELyigGDGVAQgylGRPALTAERFVPDPFAGP---GSRLYRTGDLVRRRADGR 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034595494 471 FWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVkAFVVLnPDYKSHDQEQLIKEIQEH 545
Cdd:cd12116 369 LEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALRAHLRAT 441
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
105-559 |
1.48e-27 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 117.25 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 105 RKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAP----A 180
Cdd:PLN02479 56 RRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTlaeeA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 181 VDAVASKCENLHSK--LIVSENSREGWGNLKE-LMKHASDSHTCVKTKHNEI-----------MAIFFTSGTSGYPKmta 246
Cdd:PLN02479 135 LKILAEKKKSSFKPplLIVIGDPTCDPKSLQYaLGKGAIEYEKFLETGDPEFawkppadewqsIALGYTSGTTASPK--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 247 hthssfGLGLSVNGRFWLDLTpSDVMWNTSD-------------TGWAKSaWSsvfspwIQGACVFTHHLPRFEPTSILQ 313
Cdd:PLN02479 212 ------GVVLHHRGAYLMALS-NALIWGMNEgavylwtlpmfhcNGWCFT-WT------LAALCGTNICLRQVTAKAIYS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 314 TLSKYPITVFCSAPTVYRMLVqNDITSYKFKSLKHCV---SAGEPITPDVTEKWrNKTGLDIYEGYGQTETVlicgnfkg 390
Cdd:PLN02479 278 AIANYGVTHFCAAPVVLNTIV-NAPKSETILPLPRVVhvmTAGAAPPPSVLFAM-SEKGFRVTHTYGLSETY-------- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 391 mkiKPGSMGKPSPAFD-----------------------VKIVDVNGNVLPPGQEGDIGIQVLpnRPFGLFTHYVDNPSK 447
Cdd:PLN02479 348 ---GPSTVCAWKPEWDslppeeqarlnarqgvryiglegLDVVDTKTMKPVPADGKTMGEIVM--RGNMVMKGYLKNPKA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 448 TASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLN 527
Cdd:PLN02479 423 NEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLK 502
|
490 500 510
....*....|....*....|....*....|..
gi 1034595494 528 PDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PLN02479 503 PGVDKSDEAALAEDIMKFCRERLPAYWVPKSV 534
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
94-559 |
2.22e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 116.45 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS--KANCI 171
Cdd:PRK08315 43 RWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSgcKALIA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 172 I----TNDVLApAVDAVASKCE-----NLHSK--------LIVSENSREGWGNLKELMKHASDSHtcvKTKHNEIMA--- 231
Cdd:PRK08315 122 AdgfkDSDYVA-MLYELAPELAtcepgQLQSArlpelrrvIFLGDEKHPGMLNFDELLALGRAVD---DAELAARQAtld 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 ------IFFTSGTSGYPKMTAHTHSSFGLglsvNGRF---WLDLTPSD--------------VMWNTsdtgwaksawssv 288
Cdd:PRK08315 198 pddpinIQYTSGTTGFPKGATLTHRNILN----NGYFigeAMKLTEEDrlcipvplyhcfgmVLGNL------------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 289 fspwiqgACVfTHH------LPRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVT 361
Cdd:PRK08315 261 -------ACV-THGatmvypGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLRTGIMAGSPCPIEVM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 362 EKWRNKTGL-DIYEGYGQTETvlicgnfkgmkiKPGSM---------------GKPSPAFDVKIVD-VNGNVLPPGQEGD 424
Cdd:PRK08315 333 KRVIDKMHMsEVTIAYGMTET------------SPVSTqtrtddplekrvttvGRALPHLEVKIVDpETGETVPRGEQGE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 425 igiqvLPNRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSV 503
Cdd:PRK08315 401 -----LCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKI 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034595494 504 AESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQeqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK08315 476 QDVQVVGVPDEKYGEEVCAWIILRPGATLTEE-----DVRDFCRGKIAHYKIPRYI 526
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
232-557 |
3.79e-27 |
|
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: 114.71 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA--CVFTHHLPRfEPT 309
Cdd:cd17643 98 VIYTSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWE-IWGALLHGGrlVVVPYEVAR-SPE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 310 SILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFK-SLKHCVSAGEPITPDVTEKWRNKTGL---DIYEGYGQTET-VLI 384
Cdd:cd17643 175 DFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 385 cgNFKGMK---IKPGSM---GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFTHYVDNPsKTASTL 452
Cdd:cd17643 255 --TFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELyvsGAGVARgylGRPELTAERFVANP-FGGPGS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 453 RGnfYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpdyks 532
Cdd:cd17643 332 RM--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD----- 404
|
330 340
....*....|....*....|....*
gi 1034595494 533 HDQEQLIKEIQEHVKKTTAPYKYPR 557
Cdd:cd17643 405 DGAAADIAELRALLKELLPDYMVPA 429
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-556 |
4.44e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 117.37 E-value: 4.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILseacsLQRG----DRVILILPRVPEWWLANVACLRTGTVL 147
Cdd:PRK12316 4559 ERARMTPDAVAVVF-----DEEKLTYAELNRRANRLAHAL-----IARGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 148 IPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASkcenLHSKLIVSENSREGWgnlkelmkhaSDSHTCVKTKHN 227
Cdd:PRK12316 4629 VPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDG----LASLALDRDEDWEGF----------PAHDPAVRLHPD 4694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 228 EIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTHHLPRFE 307
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWD 4772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 PTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPD-VTEKWRNKTGLDIYEGYGQTETVLICG 386
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQAsYDLAWRALKPVYLFNGYGPTETTVTVL 4852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 387 NFKGMK-IKPGS----MGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQvlpnrpfGLFTHYVDNPSKTASTL------- 452
Cdd:PRK12316 4853 LWKARDgDACGAaympIGTPLGNRSGYVLDGQLNPLPVGVAGElyLGGE-------GVARGYLERPALTAERFvpdpfga 4925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 453 -RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYK 531
Cdd:PRK12316 4926 pGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALA 5005
|
490 500
....*....|....*....|....*..
gi 1034595494 532 SHDQEQ--LIKEIQEHVKKTTAPYKYP 556
Cdd:PRK12316 5006 DADEAQaeLRDELKAALRERLPEYMVP 5032
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
234-559 |
4.65e-27 |
|
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: 111.73 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHSSfglglsvngrfWLDLTPSDVMwntsdtGWAKSAWSSVFSPwiqGACVFTHHL---------- 303
Cdd:cd17633 7 FTSGTTGLPKAYYRSERS-----------WIESFVCNED------LFNISGEDAILAP---GPLSHSLFLygaisalylg 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 304 ------PRFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLkhcVSAGEPITPDVTEKWRNKT-GLDIYEGY 376
Cdd:cd17633 67 gtfigqRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 377 GQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlppgqegdIG-IQVLPNRpfgLFTHYVDNPSKTAstlrGN 455
Cdd:cd17633 144 GTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGE--------IGkIFVKSEM---VFSGYVRGGFSNP----DG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 456 FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpdyKSHDQ 535
Cdd:cd17633 209 WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---KLTYK 285
|
330 340
....*....|....*....|....
gi 1034595494 536 EQLIKeiqehVKKTTAPYKYPRKV 559
Cdd:cd17633 286 QLKRF-----LKQKLSRYEIPKKI 304
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
89-574 |
1.45e-26 |
|
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: 113.72 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 89 NGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 168
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 169 NCIIT-----NDVLAPAV-DAVASKCENLHSKLivseNSREGWgnlKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYP 242
Cdd:cd05932 80 KALFVgklddWKAMAPGVpEGLISISLPPPSAA----NCQYQW---DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 243 KMTAHTHSSFGLGLSvNGRFWLDLTPSDVMWntSDTGWAKSAWSS-VFSPWIQGACV--FTHHLPRFeptsiLQTLSKYP 319
Cdd:cd05932 153 KGVMLTFGSFAWAAQ-AGIEHIGTEENDRML--SYLPLAHVTERVfVEGGSLYGGVLvaFAESLDTF-----VEDVQRAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 320 ITVFCSAP---TVYRMLVQNDITSYKFKSL----------KHCVSAG-------------EPITPDVTEkWRNKTGLDIY 373
Cdd:cd05932 225 PTLFFSVPrlwTKFQQGVQDKIPQQKLNLLlkipvvnslvKRKVLKGlgldqcrlagcgsAPVPPALLE-WYRSLGLNIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 374 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIvdvngnvlppGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLR 453
Cdd:cd05932 304 EAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILV-----RSPALMMGYYKDPEATAEAFT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 454 GN-FYITGDRGYMDKDGYFWFVARADDVILSS-GYRIGPFEVENALNEHPSVAESAVVSS--PDPIRGEVVKAFVVLNPD 529
Cdd:cd05932 369 ADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRAD 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1034595494 530 ykSHDQEQLIKEIQEHVKKTTAPY-KYPRKVGILIITNIcsvlWTI 574
Cdd:cd05932 449 --AFARAELEASLRAHLARVNSTLdSHEQLAGIVVVKDP----WSI 488
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
96-545 |
3.49e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 112.68 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKANCII 172
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 173 TNDvLApavdAVAS-----KCENLHSKLIVSenSREGWGN--LKELMKHASD-SHTCVKTKHNEIMAIFFTSGTSGYPKM 244
Cdd:PRK09274 119 GIP-KA----HLARrlfgwGKPSVRRLVTVG--GRLLWGGttLATLLRDGAAaPFPMADLAPDDMAAILFTSGSTGTPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 245 TAHTHSSF---------GLGLSVNGRfwlDLTPSDVMwntsdtgwaksawsSVFSPWIQGACVfthhLPRFEPT------ 309
Cdd:PRK09274 192 VVYTHGMFeaqiealreDYGIEPGEI---DLPTFPLF--------------ALFGPALGMTSV----IPDMDPTrpatvd 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 310 --SILQTLSKYPITVFCSAPTVYRML----VQNDItsyKFKSLKHCVSAGEPITPDVTEKWRN--KTGLDIYEGYGQTET 381
Cdd:PRK09274 251 paKLFAAIERYGVTNLFGSPALLERLgrygEANGI---KLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 382 VLICgnfkgmKIkpGS------------------MGKPSPAFDVKIVDVNGN---------VLPPGQEGDI---GIQVLP 431
Cdd:PRK09274 328 LPIS------SI--ESreilfatraatdngagicVGRPVDGVEVRIIAISDApipewddalRLATGEIGEIvvaGPMVTR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 432 NrpfglfthYVDNPSKTA-----STLRGNFYITGDRGYMDKDGYFWFVAR-ADDVILSSGyRIGPFEVENALNEHPSVAE 505
Cdd:PRK09274 400 S--------YYNRPEATRlakipDGQGDVWHRMGDLGYLDAQGRLWFCGRkAHRVETAGG-TLYTIPCERIFNTHPGVKR 470
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1034595494 506 SAVVSSPDPirGEVVKAFVV-LNPDyKSHDQEQLIKEIQEH 545
Cdd:PRK09274 471 SALVGVGVP--GAQRPVLCVeLEPG-VACSKSALYQELRAL 508
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
94-509 |
5.86e-26 |
|
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: 111.30 E-value: 5.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKanciit 173
Cdd:cd17640 5 RITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSE------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 ndvlapavdavaskcenlhSKLIVSENSregwgnlkelmkhasdshtcvktkHNEIMAIFFTSGTSGYPKMTAHTHSSF- 252
Cdd:cd17640 78 -------------------SVALVVEND------------------------SDDLATIIYTSGTTGNPKGVMLTHANLl 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 253 --------GLGLSVNGRFwLDLTPSdvmWNTSDtgwaKSAWSSVFSpwiQG-ACVFThhlprfEPTSILQTLSKYPITVF 323
Cdd:cd17640 115 hqirslsdIVPPQPGDRF-LSILPI---WHSYE----RSAEYFIFA---CGcSQAYT------SIRTLKDDLKRVKPHYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 324 CSAPTVYRMLVQNDITSYKFKS---------------LKHCVSAGEPITPDVtEKWRNKTGLDIYEGYGQTET--VLICG 386
Cdd:cd17640 178 VSVPRLWESLYSGIQKQVSKSSpikqflflfflsggiFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETspVVSAR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 387 NFKGMKIkpGSMGKPSPAFDVKIVDVNGN-VLPPGQEGDI---GIQVLPNrpfglfthYVDNPSKTASTLRGN-FYITGD 461
Cdd:cd17640 257 RLKCNVR--GSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVwvrGPQVMKG--------YYKNPEATSKVLDSDgWFNTGD 326
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034595494 462 RGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:cd17640 327 LGWLTCGGELVLTGRAKDTIvLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
105-559 |
7.23e-26 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 112.03 E-value: 7.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 105 RKFANILSeaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAV 184
Cdd:PLN03102 51 RLAASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 185 ----ASKCENLHSKLIV------------SENSREGWGNLKELMKHASDSHTCVKTKHNEImAIFFTSGTSGYPKMTAHT 248
Cdd:PLN03102 129 lhllSSEDSNLNLPVIFiheidfpkrpssEELDYECLIQRGEPTPSLVARMFRIQDEHDPI-SLNYTSGTTADPKGVVIS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 249 HSSFGL-GLSVNGRFWLDLTPSdVMWNTSD---TGWAKSaWSSVFSpwiQGACVFTHHLPRFEptsILQTLSKYPITVFC 324
Cdd:PLN03102 208 HRGAYLsTLSAIIGWEMGTCPV-YLWTLPMfhcNGWTFT-WGTAAR---GGTSVCMRHVTAPE---IYKNIEMHNVTHMC 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 325 SAPTVYRMLVQNDITSYKFKSLK-HCVSAGEPiTPDVTEKWRNKTGLDIYEGYGQTET---VLIC-----------GNFK 389
Cdd:PLN03102 280 CVPTVFNILLKGNSLDLSPRSGPvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCewqdewnrlpeNQQM 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 390 GMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQE-GDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKD 468
Cdd:PLN03102 359 ELKARQGVSILGLADVDVKNKETQESVPRDGKTmGEIVI-----KGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 469 GYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVL--NPDYKSHDQEQLI---KEIQ 543
Cdd:PLN03102 434 GHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLVtreRDLI 513
|
490
....*....|....*.
gi 1034595494 544 EHVKKTTAPYKYPRKV 559
Cdd:PLN03102 514 EYCRENLPHFMCPRKV 529
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
91-558 |
9.89e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 110.64 E-value: 9.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSEACSLQRgdRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK07638 23 NDRVLTYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDVLApavdavaskcenlhSKLIVSENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHS 250
Cdd:PRK07638 101 IVTERYKL--------------NDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 251 SfglglsvngrfWL---DLTPSDV-MWNTSDTGWAKSAWSSVF-----SPWIQGACVftHHLPRFEPTSILQTLSKYPIT 321
Cdd:PRK07638 167 S-----------WLhsfDCNVHDFhMKREDSVLIAGTLVHSLFlygaiSTLYVGQTV--HLMRKFIPNQVLDKLETENIS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 322 VFCSAPTVYRMLVQndITSYKFKSLKhCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTE----TVLICGNFKgmkIKPG 396
Cdd:PRK07638 234 VMYTVPTMLESLYK--ENRVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASElsfvTALVDEESE---RRPN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 397 SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpNRPFgLFTHYVdNPSKTASTLRGNFYIT-GDRGYMDKDGYFWFVA 475
Cdd:PRK07638 308 SVGRPFHNVQVRICNEAGEEVQKGEIGTVYV----KSPQ-FFMGYI-IGGVLARELNADGWMTvRDVGYEDEEGFIYIVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 476 RADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVvlnpdykshDQEQLIKEIQEHVKKTTAPYKY 555
Cdd:PRK07638 382 REKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKI 452
|
...
gi 1034595494 556 PRK 558
Cdd:PRK07638 453 PKE 455
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
227-557 |
1.08e-25 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 111.43 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 227 NEIMAIFFTSGTSGYPKMTAHTHSSF---GLG-LSVNGrfwldLTPSDVMWNTS---DTGwaksAWSSVFSPWIQGAC-V 298
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALivqSLAkIAIVG-----YGEDDVYLHTAplcHIG----GLSSALAMLMVGAChV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 299 FthhLPRFEPTSILQTLSKYPITVFCSAPTVYRMLV---QNDITSYKFKSLKHCVSAGEPIT----PDVTEKWRNKtglD 371
Cdd:PLN02860 243 L---LPKFDAKAALQAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSsrllPDAKKLFPNA---K 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 372 IYEGYGQTET----------VLICGNFK-----GMKIKPGS--------MGKPSPAFDVKIvdvngnvlppGQEGDIGIQ 428
Cdd:PLN02860 317 LFSAYGMTEAcssltfmtlhDPTLESPKqtlqtVNQTKSSSvhqpqgvcVGKPAPHVELKI----------GLDESSRVG 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 429 VLPNRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESA 507
Cdd:PLN02860 387 RILTRGPHVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVV 466
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 508 VVSSPDPIRGEVVKAFVVLNPDYK-SHDQEQLIK--------EIQEHV-KKTTAPYKYPR 557
Cdd:PLN02860 467 VVGVPDSRLTEMVVACVRLRDGWIwSDNEKENAKknltlsseTLRHHCrEKNLSRFKIPK 526
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
221-552 |
1.16e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 112.71 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 221 CVKTKHNE-IMAIFFTSGTSGYPK--MTAHT----------------------------HSsfgLGLSVNgrFWLdltps 269
Cdd:PRK08633 775 YGPTFKPDdTATIIFSSGSEGEPKgvMLSHHnilsnieqisdvfnlrnddvilsslpffHS---FGLTVT--LWL----- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 270 dvmwntsdtgwaksawssvfsPWIQGACVFTHHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQND-ITSYKFKSLKH 348
Cdd:PRK08633 845 ---------------------PLLEGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRL 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 349 CVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFDVKIVD-VNGNVL 417
Cdd:PRK08633 903 VVAGAEKLKPEVADAFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEEL 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 418 PPGQEGDI---GIQVLpnrpfglfTHYVDNPSKTASTLR----GNFYITGDRGYMDKDGYFWFVARaddviLSSGYRIG- 489
Cdd:PRK08633 983 PPGEDGLIligGPQVM--------KGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGg 1049
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 490 ---PF-EVENALNE--HPSVAESAVVSSPDPIRGEVVkafVVLnpdyksHDQEQL-IKEIQEHVKKTTAP 552
Cdd:PRK08633 1050 emvPLgAVEEELAKalGGEEVVFAVTAVPDEKKGEKL---VVL------HTCGAEdVEELKRAIKESGLP 1110
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
232-567 |
1.26e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 111.76 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSDVMWNTSDTGWAKsawssvFSPWIQGACVFTHHLPRFE---- 307
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS------FHGFLYGSLSLGNTFVMFEggii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 -----PTSILQTLSKYPITVFCSAPTVYRMLVQND-----ITS-YKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGY 376
Cdd:PTZ00237 333 knkhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiIRSkYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 377 GQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvLPNRPFGLFTHYV-DNPSKTASTLRG 454
Cdd:PTZ00237 413 GQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK-LPMPPSFATTFYKnDEKFKQLFSKFP 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 455 NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSH- 533
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQs 571
|
330 340 350
....*....|....*....|....*....|....*
gi 1034595494 534 -DQEQLIKEIQEHVKKTTAPYKYPRKvgILIITNI 567
Cdd:PTZ00237 572 iDLNKLKNEINNIITQDIESLAVLRK--IIIVNQL 604
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
96-556 |
1.70e-25 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 110.75 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITnD 175
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI-D 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLAPAVDAVAS-KCENLhsKLIVSENSREGWGNLKELMKHASDSHTCVKT----KHNEIMaIFFTSGTSGYPKMTAHTHS 250
Cdd:PRK05852 123 ADGPHDRAEPTtRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglRPDDAM-IMFTGGTTGLPKMVPWTHA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 251 SfgLGLSVNGRFW-LDLTPSD----VMWNTSDTGWAKSAWSSVFSpwiqGACVFTHHLPRFEPTSILQTLSKYPITVFCS 325
Cdd:PRK05852 200 N--IASSVRAIITgYRLSPRDatvaVMPLYHGHGLIAALLATLAS----GGAVLLPARGRFSAHTFWDDIKAVGATWYTA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 326 APTVYRMLVQNDITSY---KFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET--------VLICGNFKGMKIK 394
Cdd:PRK05852 274 VPTIHQILLERAATEPsgrKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqIEGIGQTENPVVS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 395 PGSMGKpSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFV 474
Cdd:PRK05852 354 TGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWL-----RGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 475 ARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVlnPDYKSHDQEQlikEIQEHVKKTTAPYK 554
Cdd:PRK05852 428 GRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTAE---ELVQFCRERLAAFE 502
|
..
gi 1034595494 555 YP 556
Cdd:PRK05852 503 IP 504
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
80-529 |
1.31e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 107.84 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 80 NPAFWWinrngEEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIP-GTTQL---T 155
Cdd:PRK07867 19 DRGLYF-----EDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGlNPTRRgaaL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 156 QKDILyrlqssKANC--IITNDVLAPAVDAVASKCEnlhsklIVSENSREgWGNlkELMKHASDSHTCVKTKHNEIMAIF 233
Cdd:PRK07867 94 ARDIA------HADCqlVLTESAHAELLDGLDPGVR------VINVDSPA-WAD--ELAAHRDAEPPFRVADPDDLFMLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHSSF-GLGLSVNGRFwlDLTPSDVMWntsdtgwaksawssVFSPWIQGACVFTHHLP-------- 304
Cdd:PRK07867 159 FTSGTSGDPKAVRCTHRKVaSAGVMLAQRF--GLGPDDVCY--------------VSMPLFHSNAVMAGWAValaagasi 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 305 ----RFEPTSILQTLSKYPITVFcsaptvyrmlvqnditSYKFKSLKHCVSA---------------GEPITPDVTEKWR 365
Cdd:PRK07867 223 alrrKFSASGFLPDVRRYGATYA----------------NYVGKPLSYVLATperpddadnplrivyGNEGAPGDIARFA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 366 NKTGLDIYEGYGQTETvlicgnfkGMKIK------PGSMGKPSPafDVKIVDVN-GNVLPPGQEGD---------IGIQV 429
Cdd:PRK07867 287 RRFGCVVVDGFGSTEG--------GVAITrtpdtpPGALGPLPP--GVAIVDPDtGTECPPAEDADgrllnadeaIGELV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 430 LPNRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:PRK07867 357 NTAGP-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVY 435
|
490 500
....*....|....*....|
gi 1034595494 510 SSPDPIRGEVVKAFVVLNPD 529
Cdd:PRK07867 436 AVPDPVVGDQVMAALVLAPG 455
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
86-546 |
7.72e-24 |
|
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: 105.44 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 86 INRNGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPR----VPEWWlanvACLRTGTVLIPGTTQLTqkdilY 161
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPT-----Y 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 162 RLQSSKAN------------CIITNDVLAPAVDAVASKCENLHSKLIVSENSREGwgnLKELMKHASDSHTcvktkhneI 229
Cdd:cd05906 101 DEPNARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDT---AADHDLPQSRPDD--------L 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 230 MAIFFTSGTSGYPKMTAHTHSSF---GLGLSVNGRFwldlTPSDVMWNtsdtgwaksawssvfspWIQ----GACVFTHH 302
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTHRNIlarSAGKIQHNGL----TPQDVFLN-----------------WVPldhvGGLVELHL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 303 LPRF---------------EPTSILQTLSKYPITV-FcsAPT-VYRMLVQ----NDITSYKFKSLKHCVSAGEPITPDVT 361
Cdd:cd05906 229 RAVYlgcqqvhvpteeilaDPLRWLDLIDRYRVTItW--APNfAFALLNDlleeIEDGTWDLSSLRYLVNAGEAVVAKTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 362 EKWRN---KTGLD---IYEGYGQTET---VLICGNFKGMKIKPG----SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQ 428
Cdd:cd05906 307 RRLLRllePYGLPpdaIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 429 VLPnrpfgLFTHYVDNPSKTASTLR-GNFYITGDRGYMDkDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAES- 506
Cdd:cd05906 387 GPV-----VTKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSf 460
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1034595494 507 -AVVSSPDPIRGEVVKAfVVLNPDYKSHDQ-EQLIKEIQEHV 546
Cdd:cd05906 461 tAAFAVRDPGAETEELA-IFFVPEYDLQDAlSETLRAIRSVV 501
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
91-556 |
1.01e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 106.78 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANC 170
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNDVLA---PAVDAVASKCENLhsklivsensregwgnLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PRK12467 613 LLTQSHLLaqlPVPAGLRSLCLDE----------------PADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAI 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 248 THSSFGLGLSVNGRfWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVftHHLPR---FEPTSILQTLSKYPITVFC 324
Cdd:PRK12467 677 SHGALANYVCVIAE-RLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLK 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 325 SAPTVYRMLVQnDITSYKFKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTETVLICGNFK----GMKIKPGSMG 399
Cdd:PRK12467 753 IVPSHLQALLQ-ASRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdeERDFGNVPIG 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 400 KPSPAFDVKIVDVNGNVLPPGQEGD--IGIQVLPN----RPFGLFTHYVDNPSKTAStlrGNFYITGDRGYMDKDGYFWF 473
Cdd:PRK12467 832 QPLANLGLYILDHYLNPVPVGVVGElyIGGAGLARgyhrRPALTAERFVPDPFGADG---GRLYRTGDLARYRADGVIEY 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 474 VARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVkAFVVlnPDYKSHDQEQLIK--EIQEHVKKTTA 551
Cdd:PRK12467 909 LGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLV--PAAVADGAEHQATrdELKAQLRQVLP 985
|
....*
gi 1034595494 552 PYKYP 556
Cdd:PRK12467 986 DYMVP 990
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
96-562 |
1.08e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 105.21 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCI---- 171
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLvvwp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 172 -------------ITNDVL--APAVDAVASKCENLHSKLivsensREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFT- 235
Cdd:PRK06164 116 gfkgidfaailaaVPPDALppLRAIAVVDDAADATPAPA------PGARVQLFALPDPAPPAAAGERAADPDAGALLFTt 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 236 SGTSGYPKMTAHTHSSF---------GLGLSVNGRFWLDLTPSDVMwntsdtgwaksAWSSVFSPWIQGACVftHHLPRF 306
Cdd:PRK06164 190 SGTTSGPKLVLHRQATLlrharaiarAYGYDPGAVLLAALPFCGVF-----------GFSTLLGALAGGAPL--VCEPVF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 307 EPTSILQTLSKYPIT-VFCSAPTVYRMLVQNDiTSYKFKSLKHC-VSAGEPITPDVTEkWRNKTGLDIYEGYGQTE--TV 382
Cdd:PRK06164 257 DAARTARALRRHRVThTFGNDEMLRRILDTAG-ERADFPSARLFgFASFAPALGELAA-LARARGVPLTGLYGSSEvqAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 383 LICGNFK---GMKIKPGsmGKP-SPAFDVKIVDV-NGNVLPPGQEGDIGIQVlPNrpfgLFTHYVDNPSKTASTLRGN-F 456
Cdd:PRK06164 335 VALQPATdpvSVRIEGG--GRPaSPEARVRARDPqDGALLPDGESGEIEIRA-PS----LMRGYLDNPDATARALTDDgY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 457 YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSpdPIRGE-VVKAFVVLNpDYKSHDQ 535
Cdd:PRK06164 408 FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPT-DGASPDE 484
|
490 500
....*....|....*....|....*..
gi 1034595494 536 EQLIKeiqeHVKKTTAPYKYPRKVGIL 562
Cdd:PRK06164 485 AGLMA----ACREALAGFKVPARVQVV 507
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-559 |
2.09e-23 |
|
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: 102.08 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKMTAHTHSSFGLGLS-----VNGRFWLDLTPSDVMWNTSDTGW--------AKSAWSSVFSPWIQGACV 298
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMggadfGTGEFTPSEDAHKAAAAAAGTVMfpapplmhGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 299 FthHLPRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQ--NDITSYKFKSLKHCVSAGEPITPDVTEKW-RNKTGLDIYE 374
Cdd:cd05924 88 L--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDalRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 375 GYGQTET-VLICGNFKGMKIKPGSMGKPSPafDVKIVDVNGNVLPPGQEGDIGIQVLPNRPFGlfthYVDNPSKTASTLR 453
Cdd:cd05924 166 AFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGGVGWIARRGHIPLG----YYGDEAKTAETFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 454 ---GNFY-ITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPD 529
Cdd:cd05924 240 evdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREG 319
|
330 340 350
....*....|....*....|....*....|
gi 1034595494 530 YKSHDQeqlikEIQEHVKKTTAPYKYPRKV 559
Cdd:cd05924 320 AGVDLE-----ELREHCRTRIARYKLPKQV 344
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
78-562 |
3.78e-23 |
|
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: 102.33 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 78 PSNPAfwwINRNGEEMrwSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQK 157
Cdd:cd17652 1 PDAPA---VVFGDETL--TYAELNARANRLARLLAA-RGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 158 DILYRLQSSKANCIITndvlapavdavaskcenlhsklivsensregwgnlkelmkHASDshtcvktkhneIMAIFFTSG 237
Cdd:cd17652 75 RIAYMLADARPALLLT----------------------------------------TPDN-----------LAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 238 TSGYPKMTAHTHSSFGlGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVfthHLPRFEPTS----ILQ 313
Cdd:cd17652 104 STGRPKGVVVTHRGLA-NLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATL---VLAPAEELLpgepLAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 314 TLSKYPITVFCSAPTVYRMLVQNDITSykfksLKHCVSAGEPITPDVTEKWrnKTGLDIYEGYGQTETVL---ICGNFKG 390
Cdd:cd17652 179 LLREHRITHVTLPPAALAALPPDDLPD-----LRTLVVAGEACPAELVDRW--APGRRMINAYGPTETTVcatMAGPLPG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 391 MKIKPgsMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFTHYVDNPSKTA--------STLRGNFYIT 459
Cdd:cd17652 252 GGVPP--IGRPVPGTRVYVLDARLRPVPPGVPGELyiaGA--------GLARGYLNRPGLTAerfvadpfGAPGSRMYRT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 460 GDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDyKSHDQEQLi 539
Cdd:cd17652 322 GDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPG-AAPTAAEL- 399
|
490 500
....*....|....*....|...
gi 1034595494 540 keiQEHVKKTTAPYKYPRKVGIL 562
Cdd:cd17652 400 ---RAHLAERLPGYMVPAAFVVL 419
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
295-562 |
9.71e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 102.00 E-value: 9.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 295 GACVFTHHlpRFEPTSILQTLSKYPITVFCSAPTVY-RMLVQNDITSYK--FKSLKHCVSAGEPITPDVTEKWRNKTGLD 371
Cdd:PRK13383 242 GGTVLTHR--HFDAEAALAQASLHRADAFTAVPVVLaRILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 372 IYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLPNRpfglfTHYVDNPSKtaS 450
Cdd:PRK13383 320 LYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAG-----TRYTDGGGK--A 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 451 TLRGnFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDy 530
Cdd:PRK13383 393 VVDG-MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG- 470
|
250 260 270
....*....|....*....|....*....|..
gi 1034595494 531 KSHDQEQlikeIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK13383 471 SGVDAAQ----LRDYLKDRVSRFEQPRDINIV 498
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
63-513 |
6.95e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 99.95 E-value: 6.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 63 DVLDQWTDKekagkKPSNPAFwwinrNGEEMRWSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLR 142
Cdd:PRK08279 41 DVFEEAAAR-----HPDRPAL-----LFEDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 143 TGTV--LIpgTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHT 220
Cdd:PRK08279 110 LGAVvaLL--NTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 221 CVKTKHNEIMA---IF--FTSGTSGYPKMTAHTH-----SSFGLGLSvngrfwLDLTPSDVMWNT----SDTGwAKSAWS 286
Cdd:PRK08279 188 TNPASRSGVTAkdtAFyiYTSGTTGLPKAAVMSHmrwlkAMGGFGGL------LRLTPDDVLYCClplyHNTG-GTVAWS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 287 SVFSPwiqGACV-----FThhLPRFEPTSIlqtlsKYPITVFCSAPTVYRMLVQNDITSY-KFKSLKHCVSAGepITPDV 360
Cdd:PRK08279 261 SVLAA---GATLalrrkFS--ASRFWDDVR-----RYRATAFQYIGELCRYLLNQPPKPTdRDHRLRLMIGNG--LRPDI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 361 TEKWRNKTGLD-IYEGYGQTE--TVLIcgNFKGmkiKPGSMGKpSPAFDVK---IV-----------DVNGNVLP--PGQ 421
Cdd:PRK08279 329 WDEFQQRFGIPrILEFYAASEgnVGFI--NVFN---FDGTVGR-VPLWLAHpyaIVkydvdtgepvrDADGRCIKvkPGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 422 EGD-IGiQVLPNRPfglFTHYVDnPSKT-ASTLRGNF------YITGDRGYMDKDGYFWFVARADDVilssgYR-----I 488
Cdd:PRK08279 403 VGLlIG-RITDRGP---FDGYTD-PEASeKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDT-----FRwkgenV 472
|
490 500
....*....|....*....|....*..
gi 1034595494 489 GPFEVENALNEHPSVAESAV--VSSPD 513
Cdd:PRK08279 473 ATTEVENALSGFPGVEEAVVygVEVPG 499
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
96-552 |
8.77e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 99.47 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWW--LANVACLrtGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 NDVLAPAVDAVASKCENLHSKLIVSENS-REGWGNLKELMKHAS-----DSHTCV----KTKHNEIMAIFFTSGTSGYPK 243
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPSDaDSAAAHMPEGIKVYSyeallDGRSTVydwpELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 244 MTAHTHSSFGLGLsvngrfwLDLTPSDVMWNTSDTG-------WAKSAWSSVFSPWIQGA-CVFTHHlpRFEPTSILQTL 315
Cdd:PRK05620 198 GVVYSHRSLYLQS-------LSLRTTDSLAVTHGESflccvpiYHVLSWGVPLAAFMSGTpLVFPGP--DLSAPTLAKII 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 316 SKYPITVFCSAPTVY-RMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLIcgnfkGMKIK 394
Cdd:PRK05620 269 ATAMPRVAHGVPTLWiQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPV-----GTVAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 395 PG-------------SMGKPSPAFDVKIVDvNGNVLPPGQEGDIGIQVLPNRpfgLFTHYVDNPSKT----ASTLRGN-- 455
Cdd:PRK05620 344 PPsgvsgearwayrvSQGRFPASLEYRIVN-DGQVMESTDRNEGEIQVRGNW---VTASYYHSPTEEgggaASTFRGEdv 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 456 -----------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFV 524
Cdd:PRK05620 420 edandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVT 499
|
490 500 510
....*....|....*....|....*....|
gi 1034595494 525 VLNPDYKSHDQ--EQLIKEIQEHVKKTTAP 552
Cdd:PRK05620 500 VLAPGIEPTREtaERLRDQLRDRLPNWMLP 529
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
95-528 |
4.47e-21 |
|
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: 97.11 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 95 WSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 175 DvlAPAVDAVASKCENLHS--KLIVSE-----NSREGW----GNLKELMKHASDSHTCV------KTKHNEIMAIFFTSG 237
Cdd:cd17641 91 D--EEQVDKLLEIADRIPSvrYVIYCDprgmrKYDDPRlisfEDVVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 238 TSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVfthHLPRfEPTSILQTLSK 317
Cdd:cd17641 169 TTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV---NFPE-EPETMMEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 318 YPITVFCSAPTVYRMLVQN------DITSYK------------------------------------------------F 343
Cdd:cd17641 244 IGPTFVLLPPRVWEGIAADvrarmmDATPFKrfmfelgmklglraldrgkrgrpvslwlrlaswladallfrplrdrlgF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 344 KSLKHCVSAGEPITPDVTEKWRnKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVnGNVLPPGQeg 423
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV-GEILVRSP-- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 424 digiqvlpnrpfGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDKDGYFWFVARADDV-ILSSGYRIGPFEVENALNEHP 501
Cdd:cd17641 400 ------------GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFSP 467
|
490 500
....*....|....*....|....*..
gi 1034595494 502 SVAESAVVSSPDPIrgevVKAFVVLNP 528
Cdd:cd17641 468 YIAEAVVLGAGRPY----LTAFICIDY 490
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
72-567 |
1.87e-20 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 95.08 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPAfwwINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PRK05857 22 EQARQQPEAIA---LRRCDGTSALRYRELVAEVGGLAADL-RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 152 TQLTQKDILYRLQSSKANCIITNDvlAPAVDAvASKCENLHSKLIVSENSREGWGNlkelMKHASDSH---TCVKTKHNE 228
Cdd:PRK05857 98 GNLPIAAIERFCQITDPAAALVAP--GSKMAS-SAVPEALHSIPVIAVDIAAVTRE----SEHSLDAAslaGNADQGSED 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 229 IMAIFFTSGTSGYPKMTAHTHSSFGLG---LSVNGRFWLDltpsdvmWNTSDTGWAKSAWSSVFSPW------IQGACVF 299
Cdd:PRK05857 171 PLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNWVT-------WVVGETTYSPLPATHIGGLWwiltclMHGGLCV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 300 THHlprfEPT-SILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAG-EPITPDVteKWRNKTGLDIYEGY 376
Cdd:PRK05857 244 TGG----ENTtSLLEILTTNAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGsRAIAADV--RFIEATGVRTAQVY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 377 GQTET-----VLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNG---NVLPPGQEGDIGIQVL--PNRPFGlfthYVDNPS 446
Cdd:PRK05857 318 GLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGigpTAPGAGPSASFGTLWIksPANMLG----YWNNPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 447 KTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVL 526
Cdd:PRK05857 394 RTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1034595494 527 NPDYKSHDQEQLIKEIQEHVKKTTAPYKYPRKvgILIITNI 567
Cdd:PRK05857 474 SAELDESAARALKHTIAARFRRESEPMARPST--IVIVTDI 512
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
492-559 |
2.10e-20 |
|
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: 85.29 E-value: 2.10e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034595494 492 EVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYkshdqEQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEV 63
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
234-529 |
5.53e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 93.55 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHSSFG-LGLSVNGRFwlDLTPSDVMW--------NTSDTGWAKSAwssvfspwIQGACVFTHhlP 304
Cdd:PRK13388 157 FTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplfhsNAVMAGWAPAV--------ASGAAVALP--A 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 305 RFEPTSILQTLSKYPITVF--CSAPTVYRMLV-------QNDITsykfkslkhcVSAGEPITPDVTEKWRNKTGLDIYEG 375
Cdd:PRK13388 225 KFSASGFLDDVRRYGATYFnyVGKPLAYILATperpddaDNPLR----------VAFGNEASPRDIAEFSRRFGCQVEDG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 376 YGQTETVLICGNFKGMKikPGSMGKPSPafDVKIVDV-------------NGNVLPPgqegDIGIQVLPNRP-FGLFTHY 441
Cdd:PRK13388 295 YGSSEGAVIVVREPGTP--PGSIGRGAP--GVAIYNPetltecavarfdaHGALLNA----DEAIGELVNTAgAGFFEGY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 442 VDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVK 521
Cdd:PRK13388 367 YNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVM 446
|
....*...
gi 1034595494 522 AFVVLNPD 529
Cdd:PRK13388 447 AALVLRDG 454
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
71-526 |
2.69e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 92.71 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 71 KEKAGKKPSNPAFwwinRNGEEmRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK12316 518 EEQVERTPEAPAL----AFGEE-TLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 151 TTQLTQKDILYRLQSSKANCIITNDVLAPAVDaVASKCENLHSKLIVSENSREGWGNLKelmkhasdshTCVktkHNEIM 230
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLLSQSHLGRKLP-LAAGVQVLDLDRPAAWLEGYSEENPG----------TEL---NPENL 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 231 A-IFFTSGTSGYPKMTAHTHSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGA-CVFTHHLP 304
Cdd:PRK12316 658 AyVIYTSGSTGKPKGAGNRHRAL-----SNRLCWmqqaYGLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGD 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 305 RFEPTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSykFKSLKHCVSAGEPITPDVTEK-WRNKTGLDIYEGYGQTETV 382
Cdd:PRK12316 732 HRDPAKLVELINREGVDTLHFVPSMLQAFLQDeDVAS--CTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAA 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 383 LICGNFKGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIgiqVLPNRpfGLFTHYVDNPSKTASTLRGN----- 455
Cdd:PRK12316 810 IDVTHWTCVEEGGDSvpIGRPIANLACYILDANLEPVPVGVLGEL---YLAGR--GLARGYHGRPGLTAERFVPSpfvag 884
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034595494 456 --FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSspdpIRGEVVKAFVVL 526
Cdd:PRK12316 885 erMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL 953
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
94-538 |
3.21e-19 |
|
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: 90.79 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIIT 173
Cdd:cd12114 12 TLTYGELAERARRVAGAL-KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 174 NDVLAPAVDAVASKcenlhskLIVSENSREGWgnlKELMKHASDSHTcvktkhneiMA-IFFTSGTSGYPKMTAHTHSS- 251
Cdd:cd12114 91 DGPDAQLDVAVFDV-------LILDLDALAAP---APPPPVDVAPDD---------LAyVIFTSGSTGTPKGVMISHRAa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 252 FGLGLSVNGRFwlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGAC-VFTHHLPRFEPTSILQTLSKYPITVFCSAPTVY 330
Cdd:cd12114 152 LNTILDINRRF--AVGPDDRVLALSSLSFDLSVYD-IFGALSAGATlVLPDEARRRDPAHWAELIERHGVTLWNSVPALL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 331 RMLV----QNDITSykfKSLKHCVSAGEPITPDVTEKWRNKT-GLDIYEGYGQTETVlICGNFkgMKIKPGSM------- 398
Cdd:cd12114 229 EMLLdvleAAQALL---PSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIY--HPIDEVPPdwrsipy 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 399 GKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFTHYVDNPSKTAS-----TLRGNFYITGDRGYMDKDGY 470
Cdd:cd12114 303 GRPLANQRYRVLDPRGRDCPDWVPGELwigGR--------GVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGT 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034595494 471 FWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPiRGEVVKAFVVLNPDYKSHDQEQL 538
Cdd:cd12114 375 LEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDAL 441
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
224-556 |
3.40e-19 |
|
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: 90.57 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 224 TKHNEIMAIFFTSGTSGYPKMTAHTHSS---FGLGLSVNgrfwLDLTPSDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VF 299
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVMIEHQSlvnLSHGLIKE----YGITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 300 THHLPRFEPTSILQTLSKYPITVFCSAPTVYRMLV----QNDITSykFKSLKHCVSAGEPITPDVTEKWRNKTGLDI--Y 373
Cdd:cd17644 178 RPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVlellLSTIDL--PSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 374 EGYGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFTHYVDNPSKT 448
Cdd:cd17644 256 NVYGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV-----GLARGYLNRPELT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 449 ASTLRGN---------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEV 519
Cdd:cd17644 331 AEKFISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKR 410
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034595494 520 VKAFVVlnPDYkshDQEQLIKEIQEHVKKTTAPYKYP 556
Cdd:cd17644 411 LVAYIV--PHY---EESPSTVELRQFLKAKLPDYMIP 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
71-556 |
6.29e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.56 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 71 KEKAGKKPSNPAFWWinrNGEEMrwSFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:PRK12316 3064 EEQVERTPDAVALAF---GEQRL--SYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 151 TTQLTQKDILYRLQSSKANCIITNDVLA-PAVDAVASKCENLHSKLIVSENSRegwgnlkelmkhasdshtcVKTKHNEI 229
Cdd:PRK12316 3138 DPEYPEERLAYMLEDSGAQLLLSQSHLRlPLAQGVQVLDLDRGDENYAEANPA-------------------IRTMPENL 3198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 230 MAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTHHLPRF-EP 308
Cdd:PRK12316 3199 AYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEE-LFWPLMSGARVVLAGPEDWrDP 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 309 TSILQTLSKYPITVFCSAPTVYRMLVQnDITSYKFKSLKHCVSAGEPITPDVTEKWrnKTGLDIYEGYGQTETVLICGNF 388
Cdd:PRK12316 3277 ALLVELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHW 3353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 389 KGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGD--IGIQVLP----NRPFGLFTHYVDNPSKTASTLrgnfYITG 460
Cdd:PRK12316 3354 QCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGElyLGGEGLArgyhNRPGLTAERFVPDPFVPGERL----YRTG 3429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 461 DRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSspdpIRGEVVKAFVVLnpdykSHDQEQLIK 540
Cdd:PRK12316 3430 DLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVP-----EDEAGDLRE 3500
|
490
....*....|....*.
gi 1034595494 541 EIQEHVKKTTAPYKYP 556
Cdd:PRK12316 3501 ALKAHLKASLPEYMVP 3516
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
313-558 |
7.04e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 89.95 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 313 QTLSKYPITVFCSAPTVYRM-LVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQTE-TVLIcgnfK 389
Cdd:PRK04813 228 ETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERfPSATIYNTYGPTEaTVAV----T 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 390 GMKI--------KPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqVLPNRPFGlfthYVDNPSKTAS---TLRGN-FY 457
Cdd:PRK04813 304 SIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SGPSVSKG----YLNNPEKTAEaffTFDGQpAY 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 458 ITGDRGYMDkDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVsspdPI-RGEVVK---AFVVLNPdyksH 533
Cdd:PRK04813 379 HTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV----PYnKDHKVQyliAYVVPKE----E 449
|
250 260
....*....|....*....|....*...
gi 1034595494 534 DQE---QLIKEIQEHVKKTTAPYKYPRK 558
Cdd:PRK04813 450 DFErefELTKAIKKELKERLMEYMIPRK 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
225-553 |
7.13e-19 |
|
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: 89.91 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 225 KHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFwLDLTPS-----------DVMWNtsdtgwaksawsSVFSPWI 293
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRA-LGLTSEsrvlqfasytfDVSIL------------EIFTTLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 294 QGACVFT-------HHLPRFeptsilqtLSKYPITVFCSAPTVYRMLVQNDITSykfksLKHCVSAGEPITPDVTEKWRN 366
Cdd:cd05918 171 AGGCLCIpseedrlNDLAGF--------INRLRVTWAFLTPSVARLLDPEDVPS-----LRTLVLGGEALTQSDVDTWAD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 367 KTGLdiYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFdVKIVDVNGN--VLPPGQEGDI---GIQVLPnrpfGlfth 440
Cdd:cd05918 238 RVRL--INAYGPAEcTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNHdrLVPIGAVGELlieGPILAR----G---- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 441 YVDNPSKTA--------------STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAES 506
Cdd:cd05918 307 YLNDPEKTAaafiedpawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKE 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034595494 507 AVVSSPDPIRGEVVK---AFVVLNPDYKSHDQEQ------------LIKEIQEHVKKTTAPY 553
Cdd:cd05918 387 VVVEVVKPKDGSSSPqlvAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSY 448
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
232-562 |
1.26e-18 |
|
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: 88.91 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKMTAHTHSSfglglSVNGRFWLDLT-PSD----VMWNTSdTGWAKSAWSsVFSPWIQGACVFT------ 300
Cdd:cd12115 110 VIYTSGSTGRPKGVAIEHRN-----AAAFLQWAAAAfSAEelagVLASTS-ICFDLSVFE-LFGPLATGGKVVLadnvla 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 301 -HHLPRFEPTSILQTLskypitvfcsaPTVYRMLVQNDITSykfKSLKHCVSAGEPITPD-VTEKWRNKTGLDIYEGYGQ 378
Cdd:cd12115 183 lPDLPAAAEVTLINTV-----------PSAAAELLRHDALP---ASVRVVNLAGEPLPRDlVQRLYARLQVERVVNLYGP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 379 TE-----TVLICGnfKGMKIKPgSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIqvlpnrpfGLFTHYVDNPSKTAS 450
Cdd:cd12115 249 SEdttysTVAPVP--PGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELyigGA--------GVARGYLGRPGLTAE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 451 TLRGN-------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAF 523
Cdd:cd12115 318 RFLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAY 397
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034595494 524 VVLNPDYKShdqeqLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:cd12115 398 IVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRL 431
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
91-562 |
1.36e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 90.61 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILseacsLQRG---DRVI-LILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:PRK12467 3117 GDQQLSYAELNRRANRLAHRL-----IAIGvgpDVLVgVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDS 3191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 167 KANCIITNDVLAPAVDAVASkcenLHSKLIvsenSREGWGNLKElmkHASDSHTcvktkHNEIMA-IFFTSGTSGYPKMT 245
Cdd:PRK12467 3192 GVKLLLTQAHLLEQLPAPAG----DTALTL----DRLDLNGYSE---NNPSTRV-----MGENLAyVIYTSGSTGKPKGV 3255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 246 AHTHSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCS 325
Cdd:PRK12467 3256 GVRHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACF 3333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 326 APTVYRMLVQN-DITSYKfkSLKHCVSAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVLI-----CGNFKGMKIKPGSM 398
Cdd:PRK12467 3334 PPAYLQQFAEDaGGADCA--SLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTvtlwkCGGDAVCEAPYAPI 3411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 399 GKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDKDGY 470
Cdd:PRK12467 3412 GRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLARYRADGV 3486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 471 FWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSpDPIRGEVVKAFVVLNPdykshDQEQLIKEIQEHVKKTT 550
Cdd:PRK12467 3487 IEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD-----PQGDWRETLRDHLAASL 3560
|
490
....*....|..
gi 1034595494 551 APYKYPRKVGIL 562
Cdd:PRK12467 3561 PDYMVPAQLLVL 3572
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
71-556 |
1.37e-18 |
|
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: 88.77 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 71 KEKAGKKPSNPAfwwINRNGEemRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPG 150
Cdd:cd17645 5 EEQVERTPDHVA---VVDRGQ--SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 151 TTQLTQKDILYRLQSSKANCIITNDvlapavdavaskcenlhsklivsensregwGNLKELMkhasdshtcvktkhneim 230
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLTNP------------------------------DDLAYVI------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 231 aifFTSGTSGYPKMTAHTHSSFglglsVNGRFW----LDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVftHHLP-- 304
Cdd:cd17645 111 ---YTSGSTGLPKGVMIEHHNL-----VNLCEWhrpyFGVTPADKSLVYASFSFDASAWE-IFPHLTAGAAL--HVVPse 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 305 -RFEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSykfksLKHCVSAGepitpDVTEKWRNKtGLDIYEGYGQTETVL 383
Cdd:cd17645 180 rRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQS-----LRVLLTGG-----DKLKKIERK-GYKLVNNYGPTENTV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 384 ICGNFKGMKIKPG-SMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFTHYVDNPSKTASTLRGN------- 455
Cdd:cd17645 249 VATSFEIDKPYANiPIGKPIDNTRVYILDEALQLQPIGVAGELCIA-----GEGLARGYLNRPELTAEKFIVHpfvpger 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 456 FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLnpdykshDQ 535
Cdd:cd17645 324 MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------PE 396
|
490 500
....*....|....*....|.
gi 1034595494 536 EQLIKEIQEHVKKTTAPYKYP 556
Cdd:cd17645 397 EIPHEELREWLKNDLPDYMIP 417
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
92-562 |
2.30e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.02 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 92 EMRWSFEELGSLSRKFANILseacsLQRG----DRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 167
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRL-----RARGvgpeVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSG 2100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 168 ANCIITNDVLAPAVDAVASkcenlhskLIVSENSREGWgnlkelMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:PRK12316 2101 AALLLTQRHLLERLPLPAG--------VARLPLDRDAE------WADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAV 2166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 248 THSSFGLGLSVNGRFWlDLTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPITVFCSAP 327
Cdd:PRK12316 2167 SHGALVAHCQAAGERY-ELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPP 2244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 328 TVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEK-WRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGS-----MGKP 401
Cdd:PRK12316 2245 VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRA 2324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 402 SPAFDVKIVDVNGNVLPPGQEGD--IGIQvlpnrpfGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDKDGYF 471
Cdd:PRK12316 2325 LGNRRAYILDADLNLLAPGMAGElyLGGE-------GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVV 2397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 472 WFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSpDPIRGEVVKAFVVlnPDyksHDQEQLIKEIQEHVKKTTA 551
Cdd:PRK12316 2398 EYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PD---DAAEDLLAELRAWLAARLP 2471
|
490
....*....|.
gi 1034595494 552 PYKYPRKVGIL 562
Cdd:PRK12316 2472 AYMVPAHWVVL 2482
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
122-556 |
4.96e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.68 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 122 RVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVaskcENLHSKLIVSENS 201
Cdd:PRK12467 1626 LVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLP----DGLRSLVLDQEDD 1701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 202 regWgnlkelMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWA 281
Cdd:PRK12467 1702 ---W------LEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADVVLQFTSFAFD 1771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 282 KSAWSsVFSPWIQGACV----FTHHLprfEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPIT 357
Cdd:PRK12467 1772 VSVWE-LFWPLINGARLviapPGAHR---DPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALE 1847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 358 PDVTEKWRNKTG-LDIYEGYGQTETVL-----IC--GNFKGMKIKPgsMGKPSPAFDVKIVDVNGNVLPPGQEGD--IGI 427
Cdd:PRK12467 1848 VEALRPWLERLPdTGLFNLYGPTETAVdvthwTCrrKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGElyLGG 1925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 428 QVLP----NRPFGLFTHYVDNPSktaSTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSV 503
Cdd:PRK12467 1926 VGLArgylNRPALTAERFVADPF---GTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGV 2002
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034595494 504 AESAVVSSpDPIRGEVVKAFVV-LNPDYKSHDQEQ--LIKEIQEHVKKTTAPYKYP 556
Cdd:PRK12467 2003 REAVVIAQ-DGANGKQLVAYVVpTDPGLVDDDEAQvaLRAILKNHLKASLPEYMVP 2057
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
91-558 |
7.98e-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: 86.37 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSeaCSLQRGDRVILI-LPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN 169
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLR--EKGVKKDSIVAImMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 170 CIITndvlapavdavaskCENLHSKLivsenSREGWGNLKE--LMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAH 247
Cdd:cd17656 88 VVLT--------------QRHLKSKL-----SFNKSTILLEdpSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 248 THSSFGLGLSVNGRFWLDLTPSDVMWNTSDTgwAKSAWSSVFSPWIQGAcvfTHHLPRFEPTSILQTL----SKYPITVF 323
Cdd:cd17656 149 EHKNMVNLLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLLSGG---TLYIIREETKRDVEQLfdlvKRHNIEVV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 324 cSAPTVYRMLVQNDITSYK--FKSLKHCVSAGEP--ITPDVTEKWRNKtGLDIYEGYGQTETVLIcgnfKGMKIKPGS-- 397
Cdd:cd17656 224 -FLPVAFLKFIFSEREFINrfPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSETHVV----TTYTINPEAei 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 398 -----MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFTHYVDNPSKTASTLRGN-------FYITGDRGYM 465
Cdd:cd17656 298 pelppIGKPISNTWIYILDQEQQLQPQGIVGELYISGA-----SVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 466 DKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLnpdykshDQEQLIKEIQEH 545
Cdd:cd17656 373 LPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-------EQELNISQLREY 445
|
490
....*....|...
gi 1034595494 546 VKKTTAPYKYPRK 558
Cdd:cd17656 446 LAKQLPEYMIPSF 458
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
74-546 |
1.43e-17 |
|
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: 86.14 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 74 AGKKPSNPAFWWINR-NGEEMRWSFEELGSLSRKFANILSEACslQRGDRVILILPRVPEWWLANVACLRTGTV---LIP 149
Cdd:cd05931 3 AAARPDRPAYTFLDDeGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 150 GTTQLTQKDILYRLQSSKANCIITNDVLAPAVDAVASK-CENLHSKLIVSENSREGwgnlkelmkhASDSHTCVKTKHNE 228
Cdd:cd05931 81 PTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASrPAAGTPRLLVVDLLPDT----------SAADWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 229 IMAIFFTSGTSGYPK--MTAHT--HSSFGLGLSVngrfwLDLTPSDVMWNtsdtgwaksaW----------SSVFSPWIQ 294
Cdd:cd05931 151 IAYLQYTSGSTGTPKgvVVTHRnlLANVRQIRRA-----YGLDPGDVVVS----------WlplyhdmgliGGLLTPLYS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 295 GA-CVFTHhlPR-F--EPTSILQTLSKYPITvFCSAPT-VYRMLVQ----NDITSYKFKSLKHCVSAGEPITPDVTEKWR 365
Cdd:cd05931 216 GGpSVLMS--PAaFlrRPLRWLRLISRYRAT-ISAAPNfAYDLCVRrvrdEDLEGLDLSSWRVALNGAEPVRPATLRRFA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 366 NK---TGLD---IYEGYGQTE-TVLICGNFKG------------------MKIKPG-------SMGKPSPAFDVKIVDVN 413
Cdd:cd05931 293 EAfapFGFRpeaFRPSYGLAEaTLFVSGGPPGtgpvvlrvdrdalagravAVAADDpaarelvSCGRPLPDQEVRIVDPE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 414 GN-VLPPGQEGDIGIQVlPNRPFGlfthYVDNPSKTASTLR-------GNFYITGDRGYMdKDGYFWFVARADDVILSSG 485
Cdd:cd05931 373 TGrELPDGEVGEIWVRG-PSVASG----YWGRPEATAETFGalaatdeGGWLRTGDLGFL-HDGELYITGRLKDLIIVRG 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034595494 486 YRIGPFEVENAL-NEHPSVAES--AVVSSPDPIRGEVVkAFVVLNPDYKSHDQEQLIKEIQEHV 546
Cdd:cd05931 447 RNHYPQDIEATAeEAHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAV 509
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
376-558 |
3.36e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 84.28 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 376 YGQTETV-LICgnfkgmKIKPG-------SMGKPSPAFDVKIVdvngnvlpPGQEGDIGIQVlPNRPFGLFTHYVDNPsk 447
Cdd:PRK07445 261 YGMTETAsQIA------TLKPDdflagnnSSGQVLPHAQITIP--------ANQTGNITIQA-QSLALGYYPQILDSQ-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 448 tastlrgNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVln 527
Cdd:PRK07445 324 -------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV-- 394
|
170 180 190
....*....|....*....|....*....|.
gi 1034595494 528 PDYKSHDQEqlikEIQEHVKKTTAPYKYPRK 558
Cdd:PRK07445 395 PKDPSISLE----ELKTAIKDQLSPFKQPKH 421
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
96-509 |
7.58e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 84.71 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEAcSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLA---PAVDAVASKCENlhSKLIVSENSREGWGnlkelmkhaSDSHTCVktkhneimaIFFTSGTSGYPKMTAHTHSSF 252
Cdd:PRK10252 564 DQLprfADVPDLTSLCYN--APLAPQGAAPLQLS---------QPHHTAY---------IIFTSGSTGRPKGVMVGQTAI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 253 glglsVNGRFWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQGACVF-----THHlprfEPTSILQTLSKYPITV- 322
Cdd:PRK10252 624 -----VNRLLWMQnhypLTADDVVLQKTPCSFDVSVWE-FFWPFIAGAKLVmaepeAHR----DPLAMQQFFAEYGVTTt 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 323 ---------FCSAPTVyrmlvqnDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTET-VLICGNFKGMK 392
Cdd:PRK10252 694 hfvpsmlaaFVASLTP-------EGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAaVDVSWYPAFGE 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 393 IKPGSMGKPSP-AFDV-----KIVDVNGNVLPPGQEGDI---GIQvlpnrpfgLFTHYVDNPSKTASTLRGN-------F 456
Cdd:PRK10252 767 ELAAVRGSSVPiGYPVwntglRILDARMRPVPPGVAGDLyltGIQ--------LAQGYLGRPDLTASRFIADpfapgerM 838
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1034595494 457 YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:PRK10252 839 YRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
399-562 |
7.97e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 83.50 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 399 GKP-SPAFDVKIVDVNGNVLPPGQEGdigiqVLPNR-PFgLFTHYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWFVA 475
Cdd:PRK10946 356 GRPmSPDDEVWVADADGNPLPQGEVG-----RLMTRgPY-TFRGYYKSPQHNASAFDANgFYCSGDLVSIDPDGYITVVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 476 RADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKS-----HDQEQLIkeiqehvkktt 550
Cdd:PRK10946 430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAvqlrrFLREQGI----------- 498
|
170
....*....|..
gi 1034595494 551 APYKYPRKVGIL 562
Cdd:PRK10946 499 AEFKLPDRVECV 510
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
232-514 |
1.62e-16 |
|
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: 82.45 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPK--MTAHtHSSFGLGLSVNGRFWLDLTPSDVMWNTSdtgwaksawSSVFSPWIQGAC--VFTHH----L 303
Cdd:cd17648 99 AIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAVLFFS---------NYVFDFFVEQMTlaLLNGQklvvP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 304 P---RFEPTSILQTLSKYPITVFCSAPTVyrmLVQNDITSykFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTE 380
Cdd:cd17648 169 PdemRFDPDRFYAYINREKVTYLSGTPSV---LQQYDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 381 TVL--ICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVLPPGQEGDI---GIQVLP---NRPFGLFTHYVDNPSKTAS-T 451
Cdd:cd17648 244 TTVtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELylgGDGVARgylNRPELTAERFLPNPFQTEQeR 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034595494 452 LRGNF---YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP 514
Cdd:cd17648 324 ARGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDA 389
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
231-538 |
3.16e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 81.72 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 231 AIFFTSGTSGYPKMTAHTHSSFGL-GLSVNGRFWLDLTPSDVMWNTSDTGWAkSAWSSVFSPWIQGACVFthhLP--RFE 307
Cdd:PRK06018 181 GMCYTSGTTGDPKGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLD 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPItPDVTEKWRNKTGLDIYEGYGQTETVLI-- 384
Cdd:PRK06018 257 GASVYELLDTEKVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPLgt 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 385 CGNFKG----------MKIKPgSMGKPSPAFDVKIVDVNGNVLPpgQEGdigiqvlpnRPFGLFThyVDNPSKTASTLRG 454
Cdd:PRK06018 336 LAALKPpfsklpgdarLDVLQ-KQGYPPFGVEMKITDDAGKELP--WDG---------KTFGRLK--VRGPAVAAAYYRV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 455 N--------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVL 526
Cdd:PRK06018 402 DgeildddgFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQL 481
|
330
....*....|..
gi 1034595494 527 NPDYKSHDQEQL 538
Cdd:PRK06018 482 KPGETATREEIL 493
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
131-530 |
3.25e-16 |
|
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: 81.88 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIItndvlapavdavASKCENLHSklivsensregwgnLKE 210
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF------------CDAGVKVYS--------------LEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 211 LMK-HASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLtpsdVMWNTSDTGWAKSAWSSVF 289
Cdd:cd05927 97 FEKlGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEIL----NKINPTDVYISYLPLAHIF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 290 SPWIQ------GACV-FTHHLPRfEPTSILQTLSkyPiTVFCSAPTVY-RML--VQNDI--------------TSYKFKS 345
Cdd:cd05927 173 ERVVEalflyhGAKIgFYSGDIR-LLLDDIKALK--P-TVFPGVPRVLnRIYdkIFNKVqakgplkrklfnfaLNYKLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 346 LKH---------------------------CVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETV-LICGNFKGMKIkPGS 397
Cdd:cd05927 249 LRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTaGATLTLPGDTS-VGH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 398 MGKPSPAFDVKIVDV---NGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLRGN-FYITGDRGYMDKDGYFWF 473
Cdd:cd05927 328 VGGPLPCAEVKLVDVpemNYDAKDPNPRGEVCI-----RGPNVFSGYYKDPEKTAEALDEDgWLHTGDIGEWLPNGTLKI 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034595494 474 VARADDVI-LSSGYRIGPFEVENALNEHPSVAESAVvsspdpiRGEVVKAF----VVLNPDY 530
Cdd:cd05927 403 IDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV-------YGDSLKSFlvaiVVPDPDV 457
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
224-509 |
3.60e-16 |
|
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: 81.35 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 224 TKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNgRFWLDLTPSDVMWntsdtgwAKSAWSSVFSPWIQGACV---FT 300
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL-RQLYGIRPGEVDL-------ATFPLFALFGPALGLTSVipdMD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 301 HHLP-RFEPTSILQTLSKYPITVFCSAPTVYRML----VQNDITsykFKSLKHCVSAGEPITPDVTEKWRN--KTGLDIY 373
Cdd:cd05910 154 PTRPaRADPQKLVGAIRQYGVSIVFGSPALLERVarycAQHGIT---LPSLRRVLSAGAPVPIALAARLRKmlSDEAEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 374 EGYGQTETVLICG-------NFKGMKIKPGS---MGKPSPAFDVKIVDVN---------GNVLPPGQEGDI---GIQVLP 431
Cdd:cd05910 231 TPYGATEALPVSSigsrellATTTAATSGGAgtcVGRPIPGVRVRIIEIDdepiaewddTLELPRGEIGEItvtGPTVTP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 432 NrpfglfthYVDNPSKTA----STLRGNF-YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAES 506
Cdd:cd05910 311 T--------YVNRPVATAlakiDDNSEGFwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRS 382
|
...
gi 1034595494 507 AVV 509
Cdd:cd05910 383 ALV 385
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
87-559 |
6.05e-16 |
|
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. 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, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 80.94 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 87 NRNGEEMRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS 166
Cdd:cd05915 17 LHTGEVHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 167 KANCIITNDVLApavdAVASKCENLHSKLIVSENSREGWGNLKELMKHASDSHTCVK-TKHNEIMAIFFTSGTSGYPKMT 245
Cdd:cd05915 96 EDKVLLFDPNLL----PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTGTTGLPKGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 246 AHTHSSFGLGLSVNGRF-WLDLTPSDVMWNTSDTgWAKSAWSSVFS-PWIQGACVFTHHLPRFEptSILQTLSKYPITVF 323
Cdd:cd05915 172 VYSHRALVLHSLAASLVdGTALSEKDVVLPVVPM-FHVNAWCLPYAaTLVGAKQVLPGPRLDPA--SLVELFDGEGVTFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 324 CSAPTVYRMLVQ-NDITSYKFKSLKHCVSAGEPiTPDVTEKWRNKTGLDIYEGYGQTETVLI------------CGNFKG 390
Cdd:cd05915 249 AGVPTVWLALADyLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTETSPVvvqnfvkshlesLSEEEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 391 MKIK----------------PGSMGKPSPAFDVKIVDVNGNVLPPGqegdigiqvlpnrpfglftHYVDNPSKTASTLRG 454
Cdd:cd05915 328 LTLKaktglpiplvrlrvadEEGRPVPKDGKALGEVQLKGPWITGG-------------------YYGNEEATRSALTPD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 455 NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNpdykshD 534
Cdd:cd05915 389 GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR------G 462
|
490 500
....*....|....*....|....*.
gi 1034595494 535 QEQLIKEIQEHVKKTTAPYKY-PRKV 559
Cdd:cd05915 463 EKPTPEELNEHLLKAGFAKWQlPDAY 488
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
178-514 |
5.94e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 77.82 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 178 APAVDAVASKCENLHSKLIVSENSREGWGNL-----KELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSS- 251
Cdd:PRK07008 122 LPLVDALAPQCPNVKGWVAMTDAAHLPAGSTpllcyETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRSt 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 252 ----FGLGLSVNgrfwLDLTPSDV------MWNTSdtgwaksAWSSVFSPWIQGA-CVFTHhlPRFEPTSILQTLSKYPI 320
Cdd:PRK07008 202 vlhaYGAALPDA----MGLSARDAvlpvvpMFHVN-------AWGLPYSAPLTGAkLVLPG--PDLDGKSLYELIEAERV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 321 TVFCSAPTVYRMLVQN-DITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLIcGNFKGMKIKPGSM- 398
Cdd:PRK07008 269 TFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPL-GTLCKLKWKHSQLp 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 399 -----------GKPSPAFDVKIVDVNGNVLP-PGQE-GDIgiQVlpnRPFGLFTHYVDNpskTASTLRGNFYITGDRGYM 465
Cdd:PRK07008 348 ldeqrkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGDL--QV---RGPWVIDRYFRG---DASPLVDGWFPTGDVATI 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1034595494 466 DKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDP 514
Cdd:PRK07008 420 DADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHP 468
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
91-557 |
1.69e-14 |
|
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: 76.18 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 91 EEMRWSFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSK 167
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 168 ANCIITNDVLAPAVDAV--ASKCENLHSKLIVSENSREGWGNLKELMKHASD--------SHTCVKTKhneimAIF-FTS 236
Cdd:cd05938 79 AKVLVVAPELQEAVEEVlpALRADGVSVWYLSHTSNTEGVISLLDKVDAASDepvpaslrAHVTIKSP-----ALYiYTS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 237 GTSGYPKMTAHTHSSFglgLSVNGRFWL-DLTPSDVMWNTSDTgWAKSAWSSVFSPWIQ-GA-CVFThhlPRFEPTSILQ 313
Cdd:cd05938 154 GTTGLPKAARISHLRV---LQCSGFLSLcGVTADDVIYITLPL-YHSSGFLLGIGGCIElGAtCVLK---PKFSASQFWD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 314 TLSKYPITVFCSAPTVYRMLVQndiTSYKFKSLKHCV--SAGEPITPDVTEKWRNKTG-LDIYEGYGQTETVLICGNFKG 390
Cdd:cd05938 227 DCRKHNVTVIQYIGELLRYLCN---QPQSPNDRDHKVrlAIGNGLRADVWREFLRRFGpIRIREFYGSTEGNIGFFNYTG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 391 mkiKPGSMGKPS-------P----AFDVK----IVDVNGNVLP--PGQEGDIGIQVLPNRPfglFTHYVDNPSKTASTL- 452
Cdd:cd05938 304 ---KIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQSP---FLGYAGDKEQTEKKLl 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 453 -----RGNFYI-TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV--VSSPDpIRGEVVKAFV 524
Cdd:cd05938 378 rdvfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-HEGRIGMAAV 456
|
490 500 510
....*....|....*....|....*....|...
gi 1034595494 525 VLNPDYkSHDQEQLIkeiqEHVKKTTAPYKYPR 557
Cdd:cd05938 457 KLKPGH-EFDGKKLY----QHVREYLPAYARPR 484
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
298-556 |
9.73e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 73.53 E-value: 9.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 298 VFTHHLPRFeptsILQTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLkhcVSAGEPITPDVTEKWRNKTgLDIYEGYG 377
Cdd:PRK08308 173 IITNKNPKF----ALNILRNTPQHILYAVPLMLHILGRLLPGTFQFHAV---MTSGTPLPEAWFYKLRERT-TYMMQQYG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 378 QTET--VLICGNFKgmkiKPGSMGKPSPAFDVKIvdvngnvlppGQEgdigiqvlpnrpfglfthyVDNPSKTASTLRGN 455
Cdd:PRK08308 245 CSEAgcVSICPDMK----SHLDLGNPLPHVSVSA----------GSD-------------------ENAPEEIVVKMGDK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 456 FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVlnpdykSHDQ 535
Cdd:PRK08308 292 EIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI------SHEE 365
|
250 260
....*....|....*....|.
gi 1034595494 536 EQLIkEIQEHVKKTTAPYKYP 556
Cdd:PRK08308 366 IDPV-QLREWCIQHLAPYQVP 385
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
232-513 |
1.20e-13 |
|
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: 73.27 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKMTAHTHSSFG-LGLSVNGRFWLDLTPSDVMWNTS---DTGWAKSAWSSVFSpwiqGACVFTHHLPRFE 307
Cdd:cd17650 98 VIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQMASfsfDVFAGDFARSLLNG----GTLVICPDEVKLD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 PTSILQTLSKYPITVFCSAPTVYRMLVQN-DITSYKFKSLKHCV--SAGEPITPDVTEKWRNKTGLDIYEGYGQTETVLI 384
Cdd:cd17650 174 PAALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIvgSDGCKAQDFKTLAARFGQGMRIINSYGVTEATID 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 385 CGNFK-GMKIKPGS----MGKPSPAFDVKIVDVNGNVLPPGQEGDIGI------QVLPNRPFGLFTHYVDNPSKTAstlr 453
Cdd:cd17650 254 STYYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIggagvaRGYLNRPELTAERFVENPFAPG---- 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 454 GNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPD 513
Cdd:cd17650 330 ERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRED 389
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
96-508 |
5.61e-13 |
|
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: 71.35 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEacSLQRGDRVI-LILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITN 174
Cdd:cd17654 18 SYADLAEKISNLSNFLRK--KFQTEERAIgLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 175 dvlapavdavaskCENLHSKLIvsensregwgnlkelmKHASDSHTCVKTKHNEIMAIFfTSGTSGYPKMTAHTHSSFgL 254
Cdd:cd17654 96 -------------KELDNAPLS----------------FTPEHRHFNIRTDECLAYVIH-TSGTTGTPKIVAVPHKCI-L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 255 GLSVNGRFWLDLTPSDVMWNTSDTGWAKSAwSSVFSPWIQGAC-VFTHHLPRFEPTSILQTLSKYP-ITVFCSAPTVYRM 332
Cdd:cd17654 145 PNIQHFRSLFNITSEDILFLTSPLTFDPSV-VEIFLSLSSGATlLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 333 LVQNDITSY---KFKSLKHCVSAGEPITPDVTEK-WRNK-TGLDIYEGYGQTETVlICGNFKGMKIKPGSMGKPSPAFDV 407
Cdd:cd17654 224 FGSQSIKSTvlsATSSLRVLALGGEPFPSLVILSsWRGKgNRTRIFNIYGITEVS-CWALAYKVPEEDSPVQLGSPLLGT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 408 KI--VDVNGNVlPPGQEGDIGIqvlpNRpFGLFTHYVDNPsktastlRGNFYITGDRGYMdKDGYFWFVARADDVILSSG 485
Cdd:cd17654 303 VIevRDQNGSE-GTGQVFLGGL----NR-VCILDDEVTVP-------KGTMRATGDFVTV-KDGELFFLGRKDSQIKRRG 368
|
410 420
....*....|....*....|...
gi 1034595494 486 YRIGPFEVENALNEHPSVAESAV 508
Cdd:cd17654 369 KRINLDLIQQVIESCLGVESCAV 391
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-509 |
7.85e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.12 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPAFWWinrngEEMRWSFEELGSLSRKFANILSEaCSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGT 151
Cdd:PRK05691 1139 EQARQTPERIALVW-----DGGSLDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 152 TQLTQKDILYRLQSSKANCIITNDVL---APAVDAVASKC-ENLHSklivsensrEGWGNlkelmkHASDSHTcvktkHN 227
Cdd:PRK05691 1213 PDYPAERLAYMLADSGVELLLTQSHLlerLPQAEGVSAIAlDSLHL---------DSWPS------QAPGLHL-----HG 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 228 EIMA-IFFTSGTSGYPKMTAHTHSSFGLGLSvngrfWLD----LTPSDVMWNTSDTGWAKSAWSsVFSPWIQG-----AC 297
Cdd:PRK05691 1273 DNLAyVIYTSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVLMQKAPISFDVSVWE-CFWPLITGcrlvlAG 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 298 VFTHHlprfEPTSILQTLSKYPITVFCSAPTVYRMLVQNDITSyKFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGY 376
Cdd:PRK05691 1347 PGEHR----DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAELRNRVLQRlPQVQLHNRY 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 377 GQTETVL-----ICGNFKGMKikpGSMGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFTHYVDNPSKTA-- 449
Cdd:PRK05691 1422 GPTETAInvthwQCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGA-----GLARGYLGRPALTAer 1493
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034595494 450 ------STLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:PRK05691 1494 fvpdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL 1559
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
94-508 |
1.11e-12 |
|
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: 70.53 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 94 RWSFEELGSLSRKFANILSeACSLQRGDRVILILPRVPEW---WLAnVACLRTGTVLIpgTTQLTQKDILYRLQSSKANC 170
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQ-AQGYRSGDVVALFMENRLEFvalWLG-LAKIGVETALI--NSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 171 IITNdvlapavdavaskcenlhsklivsensregwgnLKELMKHASDSH--TCVKTKHNEIMAIFFTSGTSGYPKMTAHT 248
Cdd:cd05939 79 LIFN---------------------------------LLDPLLTQSSTEppSQDDVNFRDKLFYIYTSGTTGLPKAAVIV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 249 HSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTHHlpRFEPTSILQTLSKYPITVFCSAPT 328
Cdd:cd05939 126 HSRY-YRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRK--KFSASNFWDDCVKYNCTIVQYIGE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 329 VYRMLVQndiTSYKFKSLKHCV--SAGEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICGNFKG------------MKI 393
Cdd:cd05939 203 ICRYLLA---QPPSEEEQKHNVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLVNIDNhvgacgfnsrilPSV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 394 KPGSMGKPSPAFDVKIVDVNGNVLP--PGQEGDIGIQVLPNRPFGLFTHYVDNPSKTASTLRGNF------YITGDRGYM 465
Cdd:cd05939 280 YPIRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFkkgdsaFLSGDVLVM 359
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1034595494 466 DKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV 508
Cdd:cd05939 360 DELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVV 402
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
231-518 |
9.50e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 68.07 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 231 AIFFTSGTSGYPKMTAHTHSSFglgLS----VNGRfwLDLTPSDVMWNTsdtgwaksawssvfspwiqgacvfthhLPRF 306
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLSHRNL---LAnraqVAAR--IDFSPEDKVFNA---------------------------LPVF 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 307 EP---TS--ILQTLSKYPITVFCSaPTVYR----MLVQNDIT-----------------SYKFKSLKHCVSAGEPITPDV 360
Cdd:PRK06814 845 HSfglTGglVLPLLSGVKVFLYPS-PLHYRiipeLIYDTNATilfgtdtflngyaryahPYDFRSLRYVFAGAEKVKEET 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 361 TEKWRNKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFDVKIVDVngnvlpPGQEGDIGIQVL-PNRPFGl 437
Cdd:PRK06814 924 RQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEYRLEPV------PGIDEGGRLFVRgPNVMLG- 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 438 fthYV--DNPSkTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPI 515
Cdd:PRK06814 995 ---YLraENPG-VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDAR 1070
|
...
gi 1034595494 516 RGE 518
Cdd:PRK06814 1071 KGE 1073
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
127-552 |
1.18e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 67.15 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 127 LPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITNDVLA------PAVDAVASKCENLHSKLIVSEN 200
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 201 S-----REGWGNLKELMKHASDSH-------TCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSfGLGLSVNGRFWLDLTP 268
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAQGsvggneySPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 269 SDVM-WNTSdTGWAKSAWsSVFSPWIQGACVFTHHlprFEPTS--ILQTLSKYPITVFCSAPTV---YRMLVQNDITSYK 342
Cdd:PLN03051 160 GDVVcWPTN-LGWMMGPW-LLYSAFLNGATLALYG---GAPLGrgFGKFVQDAGVTVLGLVPSIvkaWRHTGAFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 343 FKSLKHCVSAGEPITPDvTEKWRNKT------------GLDIYEGYGQTETVLICGnfkgmkikPGSMGKPSPAFDVKIV 410
Cdd:PLN03051 235 WSKLRVFASTGEASAVD-DVLWLSSVrgyykpvieycgGTELASGYISSTLLQPQA--------PGAFSTASLGTRFVLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 411 DVNGNVLPPGQE--GDIGI--------QVLPNRPFGLfTHYVDNP--SKTASTLRGNfyitGDRGYMDKDGYFWFVARAD 478
Cdd:PLN03051 306 NDNGVPYPDDQPcvGEVALappmlgasDRLLNADHDK-VYYKGMPmyGSKGMPLRRH----GDIMKRTPGGYFCVQGRAD 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034595494 479 DVILSSGYRIGPFEVENALNE-HPSVAESAVVSSPDPIRGE----VVKAFVVLNPDYKSHDQEQLIKEIQEHVKKTTAP 552
Cdd:PLN03051 381 DTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNP 459
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
222-545 |
1.21e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 67.43 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 222 VKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFgLGLSVNGRFWLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTh 301
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 302 hlprfeptsilqtlskYPitvfcsAPTVYRM---LV--QNDI----TS------------YKFKSLKHCVSAGEPITPDV 360
Cdd:PRK08043 438 ----------------YP------SPLHYRIvpeLVydRNCTvlfgTStflgnyarfanpYDFARLRYVVAGAEKLQEST 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 361 TEKWRNKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVngnvlpPGQEGDIGIQVL-PNRPFGLFT 439
Cdd:PRK08043 496 KQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSV------PGIEQGGRLQLKgPNIMNGYLR 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 440 hyVDNPSK----TASTLRG----NFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSS 511
Cdd:PRK08043 570 --VEKPGVlevpTAENARGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIK 647
|
330 340 350
....*....|....*....|....*....|....
gi 1034595494 512 PDPIRGEvvkAFVVLNPDyKSHDQEQLIKEIQEH 545
Cdd:PRK08043 648 SDASKGE---ALVLFTTD-SELTREKLQQYAREH 677
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
72-552 |
2.91e-11 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 66.26 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 72 EKAGKKPSNPAFWWINRNGEEM---RWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLI 148
Cdd:PLN03052 183 PKPSKTDDSIAIIWRDEGSDDLpvnRMTLSELRSQVSRVANAL-DALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 149 PGTTQLTQKDILYRLQSSKANCIITNDVL-----------------APAVDAVASKCENLHSKLivsensREG---WGNL 208
Cdd:PLN03052 262 SIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplysrvveakAPKAIVLPADGKSVRVKL------REGdmsWDDF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 209 KELMKHAS--DSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSfGLGLSVNGRFWLDLTPSDVM-WNTsDTGWAKSAW 285
Cdd:PLN03052 336 LARANGLRrpDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDIVcWPT-NLGWMMGPW 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 286 sSVFSPWIQGACvfthhLPRFEPTSILQTLSKY----PITVFCSAPTVYRMLVQNDITS-YKFKSLKHCVSAGEPITPD- 359
Cdd:PLN03052 414 -LVYASLLNGAT-----LALYNGSPLGRGFAKFvqdaKVTMLGTVPSIVKTWKNTNCMAgLDWSSIRCFGSTGEASSVDd 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 360 ---VTEKWRNKTgldIYEGYGQTEtvlICGNF-KGMKIKPGSMGK---PSPAFDVKIVDVNGNVLPPGQEGdIGIQVLPN 432
Cdd:PLN03052 488 ylwLMSRAGYKP---IIEYCGGTE---LGGGFvTGSLLQPQAFAAfstPAMGCKLFILDDSGNPYPDDAPC-TGELALFP 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 433 RPFGLFT----------HYVDNPSKTASTLRGNfyitGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNE-HP 501
Cdd:PLN03052 561 LMFGASStllnadhykvYFKGMPVFNGKILRRH----GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDE 636
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034595494 502 SVAESAVVSSPDPIRG--EVVKAFVVLNPDYKSHDQEQLIKEIQEHVKKTTAP 552
Cdd:PLN03052 637 SVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNP 689
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
55-564 |
7.45e-11 |
|
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: 64.98 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 55 PEYF-----NFAKDVLdqwtdkekAGKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPR 129
Cdd:cd05943 62 ARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAGYLPN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 130 VPEwwlANVACLRT---GTVLIPGTTQLTQKDILYRLQSSKANCIITNDV---------LAPAVDAVASKCENLHSKLIV 197
Cdd:cd05943 133 IPE---AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPSLLAVVVV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 198 SENSREGWGNLKELMKHASDSHTCVKTKHNEI----------MAIFFTSGTSGYPKmtAHTHSSFGLGLSVNGRFWL--D 265
Cdd:cd05943 210 PYTVAAGQPDLSKIAKALTLEDFLATGAAGELefeplpfdhpLYILYSSGTTGLPK--CIVHGAGGTLLQHLKEHILhcD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 266 LTPSDVM-WNTSdTGWAksAWSSVFSPWIQGACVFTHHLPRFEPTS--ILQTLSKYPITVFCSAPTVYRMLVQNDI---T 339
Cdd:cd05943 288 LRPGDRLfYYTT-CGWM--MWNWLVSGLAVGATIVLYDGSPFYPDTnaLWDLADEEGITVFGTSAKYLDALEKAGLkpaE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 340 SYKFKSLKHCVSAGEPITPD----VTEKWrnKTGLDIYEGYGQTEtvlICGNFKGMK----IKPGSMGKPSPAFDVKIVD 411
Cdd:cd05943 365 THDLSSLRTILSTGSPLKPEsfdyVYDHI--KPDVLLASISGGTD---IISCFVGGNpllpVYRGEIQCRGLGMAVEAFD 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 412 VNGNVLPpGQEGDIGI-QVLPNRPfglfTHYVDNPSktASTLRGNFYIT-------GDRGYMDKDGYFWFVARADDVILS 483
Cdd:cd05943 440 EEGKPVW-GEKGELVCtKPFPSMP----VGFWNDPD--GSRYRAAYFAKypgvwahGDWIEITPRGGVVILGRSDGTLNP 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 484 SGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDykshdqEQLIKEIQEHVKKTTAPYKYPRKVGILI 563
Cdd:cd05943 513 GGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDELRKRIRSTIRSALSPRHVPAKI 586
|
.
gi 1034595494 564 I 564
Cdd:cd05943 587 I 587
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
234-556 |
1.01e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHSSFGLGL-SVNGRFwlDLTPSDVMWNTSDTGWaKSAWSSVFSPWIQGACVFTHHLPRFEPTSIL 312
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGEIAMHCqAVIERF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQGQWGAEEIC 2416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 313 QTLSKYPITVFCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRNKTGLD-IYEGYGQTETV---LICGNF 388
Cdd:PRK05691 2417 QLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTETVvmpLACLAP 2496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 389 KGMKIKPGS--MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQVLpnrpfGLFTHYVDNPSKTA--------STLRGNFYI 458
Cdd:PRK05691 2497 EQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRLYR 2571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 459 TGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDYKSHDQEQL 538
Cdd:PRK05691 2572 TGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQAAL 2651
|
330
....*....|....*...
gi 1034595494 539 IKEIQEHVKKTTAPYKYP 556
Cdd:PRK05691 2652 REALKAHLKQQLPDYMVP 2669
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
234-513 |
1.13e-10 |
|
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: 63.91 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHSSFGLGLSVNGrFWLDLTPSDVMWNT----SDTGwAKSAWSSVFspwIQGACVFTHHlpRFEPT 309
Cdd:cd05940 88 YTSGTTGLPKAAIISHRRAWRGGAFFA-GSGGALPSDVLYTClplyHSTA-LIVGWSACL---ASGATLVIRK--KFSAS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 310 SILQTLSKYPITVFCSAPTVYRMLVQndiTSYKFKSLKHCVSA--GEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICG 386
Cdd:cd05940 161 NFWDDIRKYQATIFQYIGELCRYLLN---QPPKPTERKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 387 NFKGmkiKPGSMGKPSP----AFDVKIV-----------DVNGNV--LPPGQEGDIGIQVLPNRPFglfTHYVDNPSKTA 449
Cdd:cd05940 238 NFFG---KPGAIGRNPSllrkVAPLALVkydlesgepirDAEGRCikVPRGEPGLLISRINPLEPF---DGYTDPAATEK 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034595494 450 STLRGNF------YITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAV--VSSPD 513
Cdd:cd05940 312 KILRDVFkkgdawFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG 383
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
232-556 |
2.11e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 232 IFFTSGTSGYPKmtahthssfglGLSVNGRF----------WLDLTPSDVMWNTSDTGWAKSAWSSVFSPWIQGACVFTH 301
Cdd:PRK05691 3874 VIYTSGSTGLPK-----------GVMVEQRGmlnnqlskvpYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVP 3942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 302 HLPRFEPTSILQTLSKYPITVFCSAPT-VYRMLVQNDITsykFKSLKHCVSAGEPITPDVTEKWRNK-TGLDIYEGYGQT 379
Cdd:PRK05691 3943 NAIAHDPQGLLAHVQAQGITVLESVPSlIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRyPQIGLVNAYGPA 4019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 380 ETVLICGNFK-GMKIKPGS---MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIQvlpnrPFGLFTHYVDNPSKTASTLRGN 455
Cdd:PRK05691 4020 ECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTALAFVPH 4094
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 456 --------FYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPiRGEVVKAFVVln 527
Cdd:PRK05691 4095 pfgapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLVGYLV-- 4171
|
330 340
....*....|....*....|....*....
gi 1034595494 528 PDYKSHDQEQLIKEIQEHVKKTTAPYKYP 556
Cdd:PRK05691 4172 PHQTVLAQGALLERIKQRLRAELPDYMVP 4200
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
227-550 |
3.02e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 59.42 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 227 NEIMAIFFTSGTSGYPKMTAHTHSSFGLG-LSVNGRFWLDLTPSDVMWN--TSDTGWAksawSSVFSPWIQGACVFTHHL 303
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNmFAILNSTEWKTKDRILSWMplTHDMGLI----AFHLAPLIAGMNQYLMPT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 304 PRF--EPTSILQTLSKYPITVFCSAPTVYRMLVQ----NDITSYKFKSLKHCVSAGEPITPDVTE---KWRNKTGLD--- 371
Cdd:cd05908 182 RLFirRPILWLKKASEHKATIVSSPNFGYKYFLKtlkpEKANDWDLSSIRMILNGAEPIDYELCHeflDHMSKYGLKrna 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 372 IYEGYGQTE-TVLICGNFKGMKIKPGSM-------GKPSPAFD--------------------VKIVDVNGNVLPPGQEG 423
Cdd:cd05908 262 ILPVYGLAEaSVGASLPKAQSPFKTITLgrrhvthGEPEPEVDkkdsecltfvevgkpidetdIRICDEDNKILPDGYIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 424 DI---GIQVLPNrpfglfthYVDNPSKTASTLRGN-FYITGDRGYMdKDGYFWFVARADDVILSSGYRIGPFEVENALNE 499
Cdd:cd05908 342 HIqirGKNVTPG--------YYNNPEATAKVFTDDgWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEE 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034595494 500 HPSVAESAVVS---SPDPIRGEVVKAFVVLNpdyKSHDQ-EQLIKEIQEHVKKTT 550
Cdd:cd05908 413 LEGVELGRVVAcgvNNSNTRNEEIFCFIEHR---KSEDDfYPLGKKIKKHLNKRG 464
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
234-529 |
5.31e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 58.98 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTPSD-VMWNtsdtgWAksAWSSVFSpwiqGACVF--------THHLP 304
Cdd:cd05921 172 FTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVD-----WL--PWNHTFG----GNHNFnlvlynggTLYID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 305 RFEPT-----SILQTLSKYPITVFCSAPTVYRMLVQ---NDITSYK--FKSLKHCVSAGEPITPDVTEKWRN----KTGL 370
Cdd:cd05921 241 DGKPMpggfeETLRNLREISPTVYFNVPAGWEMLVAaleKDEALRRrfFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 371 DI--YEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlppgqEGDI-GIQVLPNrpfglfthYVDNPSK 447
Cdd:cd05921 321 RIpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSGGKY-----EVRVkGPNVTPG--------YWRQPEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 448 TASTL-RGNFYITGDRGYM----DKDGYFWFVAR-ADDVILSSG--YRIGPFEVEnALNEHPSVAESAVVSSPDpirGEV 519
Cdd:cd05921 388 TAQAFdEEGFYCLGDAAKLadpdDPAKGLVFDGRvAEDFKLASGtwVSVGPLRAR-AVAACAPLVHDAVVAGED---RAE 463
|
330
....*....|
gi 1034595494 520 VKAFVVLNPD 529
Cdd:cd05921 464 VGALVFPDLL 473
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
308-496 |
5.78e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 58.85 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 PTSILQTLSKYPITV-----FCSAPTVYRMLVQNDITSYKFKSLKHCVSAGEPITPDVTEKWRN---KTGLD---IYEGY 376
Cdd:PRK07768 235 PLLWAELISKYRGTMtaapnFAYALLARRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDagaRFGLRpeaILPAY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 377 GQTETVLI-----CGNfkGMKI------------------KPG-----SMGKPSPAFDVKIVDVNGNVLPPGQEGDI--- 425
Cdd:PRK07768 315 GMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKGNtrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIelr 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034595494 426 GIQVLPnrpfglftHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENA 496
Cdd:PRK07768 393 GESVTP--------GYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERA 455
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
131-499 |
1.01e-08 |
|
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: 58.14 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 131 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAN-CIITNDVLAPAVDAVASKCENLHSKLIVSENSRE------ 203
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANiLVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEkepnly 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 204 GWGNLKELMKHASDS--HTCVKT-KHNEIMAIFFTSGTSGYPK--MTAHTHSSFGLGLSVNGrfwLDLTPSDVMwntsdt 278
Cdd:cd05933 124 SWDEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKgvMLSHDNITWTAKAASQH---MDLRPATVG------ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 279 gwAKSAWS------------SVFSPWIQGACVFthhlprF-EPT----SILQTLSKYPITVFCSAPTVY-RML-----VQ 335
Cdd:cd05933 195 --QESVVSylplshiaaqilDIWLPIKVGGQVY------FaQPDalkgTLVKTLREVRPTAFMGVPRVWeKIQekmkaVG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 336 NDITSYKFK--------SLKH-------------------------------------CVSAGEPITPDVTEKWrnkTGL 370
Cdd:cd05933 267 AKSGTLKRKiaswakgvGLETnlklmggespsplfyrlakklvfkkvrkalgldrcqkFFTGAAPISRETLEFF---LSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 371 DI--YEGYGQTE-----TVLICGNFKgmkikPGSMGKPSPAFDVKIVDVNGNvlppGQeGDIGIqvlpnRPFGLFTHYVD 443
Cdd:cd05933 344 NIpiMELYGMSEtsgphTISNPQAYR-----LLSCGKALPGCKTKIHNPDAD----GI-GEICF-----WGRHVFMGYLN 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034595494 444 NPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADD-VILSSGYRIGPFEVENALNE 499
Cdd:cd05933 409 MEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVKK 466
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
117-547 |
1.35e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 57.71 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIP--GTTQLTQKDILYR-----LQSSKANCIITNDVLAPAVDAVAskce 189
Cdd:PRK09192 71 LKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlpLPMGFGGRESYIAqlrgmLASAQPAAIITPDELLPWVNEAT---- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 190 nlhsklivsENSREGW-GNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSSFGLGLSVNGRFWLDLTP 268
Cdd:PRK09192 147 ---------HGNPLLHvLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRP 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 269 SD--VMWNT--SDTGWAksawSSVFSPWiqgAC-VFTHHLPRFE----PTSILQTLSKYPITVFCSAPTVY-----RMLV 334
Cdd:PRK09192 218 GDrcVSWLPfyHDMGLV----GFLLTPV---ATqLSVDYLPTRDfarrPLQWLDLISRNRGTISYSPPFGYelcarRVNS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 335 QnDITSYkfkSLKHCVSAG---EPITPDVTEKWRNK--------------TGL----------DIYEGYgQTETV----L 383
Cdd:PRK09192 291 K-DLAEL---DLSCWRVAGigaDMIRPDVLHQFAEAfapagfddkafmpsYGLaeatlavsfsPLGSGI-VVEEVdrdrL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 384 IcgnFKGMKIKPGS----------MGKPSPAFDVKIVDVNGNVLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLR 453
Cdd:PRK09192 366 E---YQGKAVAPGAetrrvrtfvnCGKALPGHEIEIRNEAGMPLPERVVGHICV-----RGPSLMSGYFRDEESQDVLAA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 454 GNFYITGDRGYMdKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSV--AESAVVSSPDPiRGEVVKAFV---VLNP 528
Cdd:PRK09192 438 DGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDE 515
|
490
....*....|....*....
gi 1034595494 529 DykshDQEQLIKEIQEHVK 547
Cdd:PRK09192 516 E----RRGQLIHALAALVR 530
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
457-562 |
1.47e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.98 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 457 YITGDRGYMDkDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVlnpdyKSHDQE 536
Cdd:PRK07824 236 FRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV-----GDGGPA 309
|
90 100
....*....|....*....|....*.
gi 1034595494 537 QLIKEIQEHVKKTTAPYKYPRKVGIL 562
Cdd:PRK07824 310 PTLEALRAHVARTLDRTAAPRELHVV 335
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
96-511 |
2.24e-08 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 56.97 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 96 SFEELGSLSRKFANILSEACSLQRGDRVILILPRVPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKANCIITND 175
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 176 VLAP----AVDAVASKCENLHSKLIvsENSREGWGNLKELMKHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTHSS 251
Cdd:cd05905 96 ACLKglpkKLLKSKTAAEIAKKKGW--PKILDFVKIPKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 252 FgLGLSVNGRFWLDLTPSDVMWN----TSDTGWAKSAWSSVFSpwiqGACVFTHHLPRFE--PTSILQTLSKYPI-TVFC 324
Cdd:cd05905 174 L-LAHCRALKEACELYESRPLVTvldfKSGLGLWHGCLLSVYS----GHHTILIPPELMKtnPLLWLQTLSQYKVrDAYV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 325 SAPTVYRMLVQ--NDITSYK-----FKSLKHC-VSAGEPITPDVTEKWRN---KTGL----------------------- 370
Cdd:cd05905 249 KLRTLHWCLKDlsSTLASLKnrdvnLSSLRMCmVPCENRPRISSCDSFLKlfqTLGLspravstefgtrvnpficwqgts 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 371 -----DIY---------------EGYGQTETVLICGnfkgmKIKPGsmgkpspafdVKIVDVNGNVLPPGQEGDIG-IQV 429
Cdd:cd05905 329 gpepsRVYldmralrhgvvrldeRDKPNSLPLQDSG-----KVLPG----------AQVAIVNPETKGLCKDGEIGeIWV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 430 L-PNRPFGLFTHYVDN-------PSKTASTLRGN-FYI-TGDRGY----------MDKDGYFWFVARADDVILSSGYRIG 489
Cdd:cd05905 394 NsPANASGYFLLDGETndtfkvfPSTRLSTGITNnSYArTGLLGFlrptkctdlnVEEHDLLFVVGSIDETLEVRGLRHH 473
|
490 500
....*....|....*....|...
gi 1034595494 490 PFEVEN-ALNEHPSVAESAVVSS 511
Cdd:cd05905 474 PSDIEAtVMRVHPYRGRCAVFSI 496
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
222-500 |
3.05e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 56.36 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 222 VKTKHNEIMA-IFFTSGTSGYPKMTAHTHSSfglgLSVNGRFWLDL---TPSDVMWNTSDTGWAKSAWSSVFSPWIQGAC 297
Cdd:PRK06334 177 VSDKDPEDVAvILFTSGTEKLPKGVPLTHAN----LLANQRACLKFfspKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 298 VFTHHLPrFEPTSILQTLSKYPITVFCSAPTVYRMLVQndiTSYK----FKSLKHCVSAGEPITPDVTEK-WRNKTGLDI 372
Cdd:PRK06334 253 VVFAYNP-LYPKKIVEMIDEAKVTFLGSTPVFFDYILK---TAKKqescLPSLRFVVIGGDAFKDSLYQEaLKTFPHIQL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 373 YEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKIVDVNGNVlpPGQEGDIGIQVLpnRPFGLFTHYVDN-PSKTAS 450
Cdd:PRK06334 329 RQGYGTTEcSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKV--PVSSGETGLVLT--RGTSLFSGYLGEdFGQGFV 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034595494 451 TLRG-NFYITGDRGYMDKDGYFWFVARaddviLSSGYRIGPFEV-----ENALNEH 500
Cdd:PRK06334 405 ELGGeTWYVTGDLGYVDRHGELFLKGR-----LSRFVKIGAEMVslealESILMEG 455
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
346-549 |
5.15e-07 |
|
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: 52.60 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 346 LKHCVSAGEPITPDvTEKWRNKTGLDIYEGYGQTETvliCGNfkGMKIKPGSM-----GKPSPAFDVKIVDV----NGNV 416
Cdd:cd17639 252 LRYMLSGGAPLSAD-TQEFLNIVLCPVIQGYGLTET---CAG--GTVQDPGDLetgrvGPPLPCCEIKLVDWeeggYSTD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 417 LPPGQeGDIGIQvlpnRPFgLFTHYVDNPSKTASTLRGN--FYiTGDRGYMDKDGYFWFVARADD-VILSSGYRIGPFEV 493
Cdd:cd17639 326 KPPPR-GEILIR----GPN-VFKGYYKNPEKTKEAFDGDgwFH-TGDIGEFHPDGTLKIIDRKKDlVKLQNGEYIALEKL 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034595494 494 ENALNEHPSVAESAVVSspDPIRGEVVkAFVVLNpdykshdQEQLIKEIQEHVKKT 549
Cdd:cd17639 399 ESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPN-------EKHLTKLAEKHGVIN 444
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
347-509 |
5.93e-07 |
|
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: 52.05 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 347 KHCVSA--GEPITPDVTEKWRNKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP------AFDVKIVDVNGN-- 415
Cdd:cd05937 201 DHKVRVawGNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLirrwkfENQVVLVKMDPEtd 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 416 ------------VLPPGQEGDIgIQVLPNRPFGLFTHYVDNPSKTASTL------RGN-FYITGDRGYMDKDGYFWFVAR 476
Cdd:cd05937 281 dpirdpktgfcvRAPVGEPGEM-LGRVPFKNREAFQGYLHNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDR 359
|
170 180 190
....*....|....*....|....*....|...
gi 1034595494 477 ADDVILSSGYRIGPFEVENALNEHPSVAESAVV 509
Cdd:cd05937 360 LGDTFRWKSENVSTTEVADVLGAHPDIAEANVY 392
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
117-522 |
4.16e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 49.71 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 117 LQRGDRVILILPRVPEWWLANVACLRTGTVLIPgttqltqkdiLYRLQSSKANCIITNDVLAPAVDAVASKCENLHS--- 193
Cdd:PLN02736 100 IPKGACVGLYFINRPEWLIVDHACSAYSYVSVP----------LYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLScls 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 194 -----KLIVSensregWGNLKELM-------------------KHASDSHTCVKTKHNEIMAIFFTSGTSGYPKMTAHTH 249
Cdd:PLN02736 170 eipsvRLIVV------VGGADEPLpslpsgtgveivtyskllaQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTH 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 250 SSfgLGLSVNG-RFWLDLTPSDVmwNTSDTGWAKsawssVFSPWIQGACVFTHHLPRFEPTSILQTLSKYPI---TVFCS 325
Cdd:PLN02736 244 GN--LIANVAGsSLSTKFYPSDV--HISYLPLAH-----IYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAAlrpTIFCS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 326 APTVY-------------------RM------------------------LVQNDITSYKFKSLKHCVSAGEPITPDVTE 362
Cdd:PLN02736 315 VPRLYnriydgitnavkesgglkeRLfnaaynakkqalengknpspmwdrLVFNKIKAKLGGRVRFMSSGASPLSPDVME 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 363 KWRNKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFDVKIVDVngnvlP---------PGQEGDIGIqvlpn 432
Cdd:PLN02736 395 FLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVDV-----PemnytsedqPYPRGEICV----- 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 433 RPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALNEHPSVAESAV-- 508
Cdd:PLN02736 464 RGPIIFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCFVyg 543
|
490 500
....*....|....*....|...
gi 1034595494 509 ---------VSSPDPirgEVVKA 522
Cdd:PLN02736 544 dslnsslvaVVVVDP---EVLKA 563
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
234-556 |
5.46e-06 |
|
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: 49.05 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 234 FTSGTSGYPKMTAHTHSSFGLGLS-VNGRFwlDLTPSDVMwnTSDTGWAKSAWS-SVFSPWIQGACVFthhLPRFE---- 307
Cdd:cd17647 116 FTSGSEGIPKGVLGRHFSLAYYFPwMAKRF--NLSENDKF--TMLSGIAHDPIQrDMFTPLFLGAQLL---VPTQDdigt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 308 PTSILQTLSKYPITVFCSAPTVYRMLVQNDITSykFKSLKHCVSAGEPITP-DVTEKWRNKTGLDIYEGYGQTETVLICG 386
Cdd:cd17647 189 PGRLAEWMAKYGATVTHLTPAMGQLLTAQATTP--FPKLHHAFFVGDILTKrDCLRLQTLAENVRIVNMYGTTETQRAVS 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 387 NF--KGMKIKPG---SMGKPSPA----FDVKIVDVNGN----VLPPGQEGDIGIqvlpnRPFGLFTHYVDNPSKTASTLR 453
Cdd:cd17647 267 YFevPSRSSDPTflkNLKDVMPAgrgmLNVQLLVVNRNdrtqICGIGEVGEIYV-----RAGGLAEGYRGLPELNKEKFV 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 454 GNFYITGDR-GYMDKDG-----YFWF-----------------------VARADDVILSSGYRIGPFEVENALNEHPSVA 504
Cdd:cd17647 342 NNWFVEPDHwNYLDKDNnepwrQFWLgprdrlyrtgdlgrylpngdcecCGRADDQVKIRGFRIELGEIDTHISQHPLVR 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034595494 505 ES------------AVVS--SPDPIRGEVVKAFVVLNPDYKSHDQ--------EQLIKEIQEHVKKTTAPYKYP 556
Cdd:cd17647 422 ENitlvrrdkdeepTLVSyiVPRFDKPDDESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIP 495
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
350-529 |
8.17e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 48.66 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 350 VSAGEPITPDVTEKWRNKTGLDIYEGYGQTETvliCGnfkgmkikPGSMGKPSPAFDVKIVDVNG--NVLPPGQEGDIGI 427
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG--------PTTLGFPDEMCMLGTVGAPAvyNELRLEEVPEMGY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 428 QVLPNRPFG--------LFTHYVDNPSKTASTLRGNFYITGDRGYMDKDGYFWFVARADDVI-LSSGYRIGPFEVENALN 498
Cdd:PLN02430 458 DPLGEPPRGeicvrgkcLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYG 537
|
170 180 190
....*....|....*....|....*....|.
gi 1034595494 499 EHPSVAESAVVSspDPIRGEVVkAFVVLNPD 529
Cdd:PLN02430 538 QNPIVEDIWVYG--DSFKSMLV-AVVVPNEE 565
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
59-559 |
5.26e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 46.33 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 59 NFAKDVLDQwtdkekagKKPSNPAFWWINRNGEEMRWSFEELGSLSRKFANILsEACSLQRGDRVILILPRVPEwwlANV 138
Cdd:PRK03584 87 NYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 139 ACLRT--------------GT-------------VLIP-------GTTQ-LTQK--DILYRLQSSKANCIITNDVLAPAV 181
Cdd:PRK03584 155 AMLATaslgaiwsscspdfGVqgvldrfgqiepkVLIAvdgyrygGKAFdRRAKvaELRAALPSLEHVVVVPYLGPAAAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 182 DAVAskceNLHSklivsensregWGnlkELMKHASDSH-TCVKTKHNEIMAIFFTSGTSGYPKMTAHTHssfG------- 253
Cdd:PRK03584 235 AALP----GALL-----------WE---DFLAPAEAAElEFEPVPFDHPLWILYSSGTTGLPKCIVHGH---Ggillehl 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 254 --LGLSvngrfwLDLTPSD-VMWNTSdTGWAksAWSSVFSPWIQGACVFTHHLPRFEPTsiLQTL----SKYPITVFCSA 326
Cdd:PRK03584 294 keLGLH------CDLGPGDrFFWYTT-CGWM--MWNWLVSGLLVGATLVLYDGSPFYPD--PNVLwdlaAEEGVTVFGTS 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 327 PTVYRMLVQNDIT---SYKFKSLKHCVSAGEPITPDVTEkWrnktgldIYEGYGQ----------TEtvlICGNFKG--- 390
Cdd:PRK03584 363 AKYLDACEKAGLVpgeTHDLSALRTIGSTGSPLPPEGFD-W-------VYEHVKAdvwlasisggTD---ICSCFVGgnp 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 391 -MKIKPGSMGKPSPAFDVKIVDVNGN-VLppGQEGDIGI-QVLPNRPFGlFTHYVDNPSKTAS----------------- 450
Cdd:PRK03584 432 lLPVYRGEIQCRGLGMAVEAWDEDGRpVV--GEVGELVCtKPFPSMPLG-FWNDPDGSRYRDAyfdtfpgvwrhgdwiei 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 451 TLRGNFYITGdrgymdkdgyfwfvaRADDVILSSGYRIGPFEVENALNEHPSVAESAVVSSPDPIRGEVVKAFVVLNPDY 530
Cdd:PRK03584 509 TEHGGVVIYG---------------RSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGV 573
|
570 580
....*....|....*....|....*....
gi 1034595494 531 KSHDqeQLIKEIQEHVKKTTAPYKYPRKV 559
Cdd:PRK03584 574 TLDD--ALRARIRTTIRTNLSPRHVPDKI 600
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
453-556 |
2.20e-04 |
|
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: 44.29 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 453 RGNFYITGDRGYMDKDGYFWFVARADDVILSSGYRIGPFEVENALNEHPSVAE----------------SAVVSSPDPir 516
Cdd:TIGR03443 676 RDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeeptlvSYIVPQDKS-- 753
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034595494 517 gEVVKAFVVLNPDYKSHDQ--------EQLIKEIQEHVKKTTAPYKYP 556
Cdd:TIGR03443 754 -DELEEFKSEVDDEESSDPvvkglikyRKLIKDIREYLKKKLPSYAIP 800
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
345-510 |
1.55e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 41.29 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 345 SLKHCVSAGEPITPDVTEKWRNKT---GLD---IYEGYGQTE-----TVLICGNfkGMKIKPGSM------------GKP 401
Cdd:PRK05851 273 ALRVALNGGEPVDCDGFERFATAMapfGFDagaAAPSYGLAEstcavTVPVPGI--GLRVDEVTTddgsgarrhavlGNP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595494 402 SPAFDVKIVDVNGNVLPPGQE-GDIGIqvlpnRPFGLFTHYVDNPSKTastlRGNFYITGDRGYMdKDGYFWFVARADDV 480
Cdd:PRK05851 351 IPGMEVRISPGDGAAGVAGREiGEIEI-----RGASMMSGYLGQAPID----PDDWFPTGDLGYL-VDGGLVVCGRAKEL 420
|
170 180 190
....*....|....*....|....*....|
gi 1034595494 481 ILSSGYRIGPFEVENALNEHPSVAESAVVS 510
Cdd:PRK05851 421 ITVAGRNIFPTEIERVAAQVRGVREGAVVA 450
|
|
| |
