|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
48-578 |
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: 1060.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 48 IPEYFNFAKDVLDQWTNTEKTGKRLSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEW 127
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 128 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMK 207
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 208 YASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 287
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 288 QGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRsYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDI 367
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS-YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 368 YEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPDRPFGLFTHYVDNPSKTASTL 447
Cdd:cd05928 320 YEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 448 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 527
Cdd:cd05928 400 RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLS 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 564330613 528 HDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 578
Cdd:cd05928 480 HDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
89-574 |
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: 624.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 89 WSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 169 DtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSsFGL 248
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHS-YPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 249 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 329 QNDITrSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDEN 408
Cdd:cd05972 188 KQDLS-SYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 409 GTILPPGQEGDIAVQVlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEV 488
Cdd:cd05972 267 GRELPPGEEGDIAIKL---PPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 489 ESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 568
Cdd:cd05972 344 ESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421
|
....*.
gi 564330613 569 KRNELR 574
Cdd:cd05972 422 RRVELR 427
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
45-578 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 608.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 45 KIEIPEYFNFAKDVLDQWTNTEKtgkrlSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKI 124
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRG-----DKVALIWEGEDGEERTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLHSKLIV---- 191
Cdd:COG0365 75 PEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSLEHVIVVgrtg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 192 SQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSD 271
Cdd:COG0365 155 ADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 272 TGWAKSAWSSVFSPWTQGACVFAH-YLPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQNDIT--RSYKFNSLKHCVSA 347
Cdd:COG0365 235 IGWATGHSYIVYGPLLNGATVVLYeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEplKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 348 GEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlp 426
Cdd:COG0365 315 GEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVI---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 427 DRPF-GLFTHYVDNPSKTASTLRGNF---YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA 502
Cdd:COG0365 391 KGPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330613 503 VVSSPDPIRGEVVKAFIVLNPDYKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 578
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
37-577 |
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: 586.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 37 YESMKHDFKIEIPEYFNFAKDVLDQWTNTEKtgkrlSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILTeACSLQRGDR 116
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAMAKEYP-----DKLALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 117 VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD--DTLAPAVDIVAAKCENLHSKLIVSQH 194
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIaeDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 195 SREGWGNLKEMMKYASDS----HTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIASDVMWNTS 270
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 271 DTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRsYKFNSLKHCVSAGEP 350
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR-YDLSSLRYCTTAGEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 351 INPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPDRPF 430
Cdd:cd05970 313 LNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 431 GLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPI 510
Cdd:cd05970 393 GLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPI 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564330613 511 RGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 577
Cdd:cd05970 473 RGQVVKATIVLAKGYE--PSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
33-577 |
2.24e-149 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 442.03 E-value: 2.24e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 33 NFSNYESMKHDFKI-EIPEYF--------NFAKDVLDQWTNTEKTGKrlsnPAFWWVDGNGKEvRWSFEELGSLSRKFAN 103
Cdd:PRK04319 14 NLKDYEETYATFSWeEVEKEFswletgkvNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELSNKFAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 104 ILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAvdIVAAKCE 183
Cdd:PRK04319 89 VLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLER--KPADDLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 184 NLHSKLIVSQHSREGWG--NLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLI 261
Cdd:PRK04319 166 SLKHVLLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKYVLDLH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 262 ASDVMWNTSDTGWAKSAWSSVFSPWTQGA--CVFAhylPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYK 337
Cdd:PRK04319 245 EDDVYWCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGagDDLVKKYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 338 FNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPG 415
Cdd:PRK04319 322 LSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 416 QEGDIAVQvlPDRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEH 495
Cdd:PRK04319 401 RMGNLAIK--KGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 496 PSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:PRK04319 478 PAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
..
gi 564330613 576 KE 577
Cdd:PRK04319 556 WE 557
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-577 |
2.15e-147 |
|
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: 431.99 E-value: 2.15e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:cd05974 81 N-----------------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 250 lSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQ 329
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 330 NDITRSYKfnSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENG 409
Cdd:cd05974 193 QDLASFDV--KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 410 TilpPGQEGDIAVQVLPDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVE 489
Cdd:cd05974 271 A---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 490 SALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIeELPKTVSGKVK 569
Cdd:cd05974 348 SVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE--PSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIR 424
|
....*...
gi 564330613 570 RNELRRKE 577
Cdd:cd05974 425 RVELRRRE 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
89-577 |
4.39e-137 |
|
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: 405.73 E-value: 4.39e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 89 WSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 169 DTLAPAVDIvaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSSFgL 248
Cdd:cd05969 80 EELYERTDP-------------------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 249 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 329 QNDI--TRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFNVEI 404
Cdd:cd05969 195 KEGDelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 405 LDENGTILPPGQEGDIAVQvlPDRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIG 484
Cdd:cd05969 274 VDENGNELPPGTKGILALK--PGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 485 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTV 564
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE--PSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|...
gi 564330613 565 SGKVKRNELRRKE 577
Cdd:cd05969 429 SGKIMRRVLKAKE 441
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-575 |
6.54e-130 |
|
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: 387.56 E-value: 6.54e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 83 NGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 162
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 163 KCIITDDTLAPAVdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelmaIYFTSGTTGPPKMIGHT 242
Cdd:cd05971 80 SALVTDGSDDPAL--------------------------------------------------IIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 243 HSsFGLGLSVNGRFWLDLI--ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSA 320
Cdd:cd05971 110 HR-VLLGHLPGVQFPFNLFprDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 321 PTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMeQWKKKT-GLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSP 398
Cdd:cd05971 189 PTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELL-GWAREQfGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 399 AFNVEILDENGTILPPGQEGDIAVQvLPDrPFGLFThYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILS 478
Cdd:cd05971 268 GHRVAIVDDNGTPLPPGEVGEIAVE-LPD-PVAFLG-YWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 479 SGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIE 558
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVN 422
|
490
....*....|....*..
gi 564330613 559 ELPKTVSGKVKRNELRR 575
Cdd:cd05971 423 ELPRTATGKIRRRELRA 439
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
86-581 |
1.64e-124 |
|
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: 373.76 E-value: 1.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:COG0318 22 GRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITddtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:COG0318 101 VT--------------------------------------------------------ALILYTSGTTGRPKGVMLTHRN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 FgLGLSVNGRFWLDLIASDVMWNTS----DTGWaksaWSSVFSPWTQGACVfaHYLPRFDSTSILQTLSKFPITVFCSAP 321
Cdd:COG0318 125 L-LANAAAIAAALGLTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL--VLLPRFDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 322 TAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET-VLICGNFKGMK-IKPGSMGKPSPA 399
Cdd:COG0318 198 TMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETsPVVTVNPEDPGeRRPGSVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 400 FNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSS 479
Cdd:COG0318 278 VEVRIVDEDGRELPPGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 480 GYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQEHVkkttAPYKYPRKIEFIEE 559
Cdd:COG0318 353 GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAEL-DAEELRAFLRERL----ARYKVPRRVEFVDE 427
|
490 500
....*....|....*....|..
gi 564330613 560 LPKTVSGKVKRNELRRKEWTTT 581
Cdd:COG0318 428 LPRTASGKIDRRALRERYAAGA 449
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-575 |
9.83e-111 |
|
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: 337.95 E-value: 9.83e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDd 169
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 tlapavdivAAKCENLHSKLIVsqhsregwgnlkeMMkyasdshtcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFgLG 249
Cdd:cd05973 80 ---------AANRHKLDSDPFV-------------MM---------------------FTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG-ACVFAHylPRFDSTSILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLE--GGFSVESTWRVIERLGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 329 QNDITRSYKFN-SLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMK--IKPGSMGKPSPAFNVEIL 405
Cdd:cd05973 194 AAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 406 DENGTILPPGQEGDIAVQVlPDRPFGLFTHYVDNPSKTAStlrGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGP 485
Cdd:cd05973 274 DDDGDELGPGEPGRLAIDI-ANSPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 486 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVS 565
Cdd:cd05973 350 FDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHE--GTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPS 427
|
490
....*....|
gi 564330613 566 GKVKRNELRR 575
Cdd:cd05973 428 GKIQRFLLRR 437
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
66-574 |
3.65e-108 |
|
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: 332.61 E-value: 3.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 66 EKTGKRLSN-PAFWWvdgngKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:cd05936 6 EEAARRFPDkTALIF-----MGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 145 TTQLTQKDILYRLQSSKSKCIITDDTLApavdivaakcenlhsKLIVSQHSREGWgnlkemmkyasdshtCVDTKHnELM 224
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFT---------------DLLAAGAPLGER---------------VALTPE-DVA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 225 AIYFTSGTTGPPKMIGHTHSSfglgLSVNgrfwldliASDVMWNTSDTGWAKS------------AWS-SVFSPWTQGAC 291
Cdd:cd05936 129 VLQYTSGTTGVPKGAMLTHRN----LVAN--------ALQIKAWLEDLLEGDDvvlaalplfhvfGLTvALLLPLALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 292 VFahYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGY 371
Cdd:cd05936 197 IV--LIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVlpdrpfglFTHYVDNPSKTASTL 447
Cdd:cd05936 275 GLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVrgpQV--------MKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 448 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 527
Cdd:cd05936 347 VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASL 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 564330613 528 hdqeqLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd05936 427 -----TEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
222-569 |
1.19e-105 |
|
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: 321.16 E-value: 1.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 222 ELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFAHylPRFD 301
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 302 STSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--VLI 379
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 380 CGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGY 459
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVV-----RGPSVMKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 460 MDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQEQLKKEIQE 539
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRA 306
|
330 340 350
....*....|....*....|....*....|
gi 564330613 540 HVKKTTAPYKYPRKIEFIEELPKTVSGKVK 569
Cdd:cd04433 307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-574 |
3.13e-103 |
|
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: 321.24 E-value: 3.13e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 50 EYFNFAKDVLDQwtnteKTGKRLSNPAFwwVDGNGkevRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWL 129
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAF--IDDAG---SLTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 130 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSRE--GWGNLKEMMK 207
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 208 YASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 287
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 288 QGACVFahYLP-RFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD 366
Cdd:cd05959 230 VGATTV--LMPeRPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 367 IYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 445
Cdd:cd05959 308 ILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYV-----RGPSSATMYWNNRDKTRD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 446 TLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDY 525
Cdd:cd05959 382 TFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 564330613 526 KlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd05959 462 E--DSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
86-574 |
5.48e-96 |
|
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: 300.16 E-value: 5.48e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIvaakcenlhsklivsqhsregwgnlkemmkyasdshtCVdtkhnelmaIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd05958 88 LCAHALTASDDI-------------------------------------CI---------LAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 FGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFDSTSILQTLSKFPITVFCSAPTAYR 325
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 326 MLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEIL 405
Cdd:cd05958 200 AMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 406 DENGTILPPGQEGDIAVQvlpdRPFGLftHYVDNPSKtASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGP 485
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVR----GPTGC--RYLADKRQ-RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 486 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVS 565
Cdd:cd05958 353 PEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI--PGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTAT 430
|
....*....
gi 564330613 566 GKVKRNELR 574
Cdd:cd05958 431 GKLQRFALR 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
88-578 |
4.39e-95 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 300.18 E-value: 4.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:PRK06187 31 RTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 168 DDTLAPAVDIVAAKCENLHSKLIVSQHSREG----WGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK06187 110 DSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 244 SSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWAksawssvFSPWTQGACVFahYLPRFDSTSILQTLSKFPITVF 317
Cdd:PRK06187 190 RNL-FLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLP-------YLALMAGAKQV--IPRRFDPENLLDLIETERVTFF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 318 CSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNF-----KGMKIKPG 391
Cdd:PRK06187 260 FAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqlPGQWTKRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 392 SMGKPSPAFNVEILDENGTILPP--GQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFV 469
Cdd:PRK06187 340 SAGRPLPGVEARIVDDDGDELPPdgGEVGEIIV-----RGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYIT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 470 ARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyklhdqEQLK-KEIQEHVKKTTAPY 548
Cdd:PRK06187 415 DRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG------ATLDaKELRAFLRGRLAKF 488
|
490 500 510
....*....|....*....|....*....|
gi 564330613 549 KYPRKIEFIEELPKTVSGKVKRNELRRKEW 578
Cdd:PRK06187 489 KLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
33-574 |
2.69e-89 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 288.38 E-value: 2.69e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 33 NFSNYESMkHDFKIEIPEYF--NFAKDVLDqWTNTEKTGKRLSNPAF--WWVDG-------------------------- 82
Cdd:TIGR02188 3 NLEQYKEL-YEESIEDPDKFwaKLARELLD-WFKPFTKVLDWSFPPFykWFVGGelnvsyncvdrhlearpdkvaiiweg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 83 --NGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQKDILYRL 157
Cdd:TIGR02188 81 dePGEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGaihSVVFGG---FSAEALADRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 158 QSSKSKCIITDDT---------LAPAVDIVAAKCENLHSKLIVSQH----------SREGWGNlkEMMKYASDSHTCVDT 218
Cdd:TIGR02188 157 NDAGAKLVITADEglrggkvipLKAIVDEALEKCPVSVEHVLVVRRtgnpvvpwveGRDVWWH--DLMAKASAYCEPEPM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 219 KHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHY-L 297
Cdd:TIGR02188 235 DSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEgV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 298 PRFDSTS-ILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD---IYEGY 371
Cdd:TIGR02188 315 PTYPDPGrFWEIIEKHKVTIFYTAPTAIRALMRlgDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKErcpIVDTW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTET--VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILP-PGQEGDIAV-QVLPDRPFGLF---THYVDNPSKTA 444
Cdd:TIGR02188 395 WQTETggIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIkQPWPGMLRTIYgdhERFVDTYFSPF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 445 StlrgNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 524
Cdd:TIGR02188 475 P----GYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDG 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 564330613 525 YKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:TIGR02188 551 YEPDD--ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLR 598
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
53-574 |
3.80e-86 |
|
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: 279.45 E-value: 3.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 53 NFAKDVLDQwtNTEKTGKRlsnPAFWWvDGN--GKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLA 130
Cdd:cd05966 53 NISYNCLDR--HLKERGDK---VAIIW-EGDepDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 131 NVACLRTG---TVLIPGttqLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLHsKLIVSQHS--- 195
Cdd:cd05966 126 MLACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRTgge 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 196 ------REGWGNlkEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNT 269
Cdd:cd05966 202 vpmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 270 SDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFDSTSIL-QTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCV 345
Cdd:cd05966 280 ADIGWITGHSYIVYGPLANGAtTVMFEGTPTYPDPGRYwDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVLG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 346 SAGEPINPEVMEQWKKKTG---LDIYEGYGQTETVLIC-----GnfkGMKIKPGSMGKPSPAFNVEILDENGTILPPGQE 417
Cdd:cd05966 360 SVGEPINPEAWMWYYEVIGkerCPIVDTWWQTETGGIMitplpG---ATPLKPGSATRPFFGIEPAILDEEGNEVEGEVE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 418 GDIAVqvlpDRPFglfthyvdnPSkTASTLRGN--------------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRI 483
Cdd:cd05966 437 GYLVI----KRPW---------PG-MARTIYGDheryedtyfskfpgYYFTGDGARRDEDGYYWITGRVDDVINVSGHRL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 484 GPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKT 563
Cdd:cd05966 503 GTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDKIQFVPGLPKT 580
|
570
....*....|.
gi 564330613 564 VSGKVKRNELR 574
Cdd:cd05966 581 RSGKIMRRILR 591
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-574 |
3.08e-85 |
|
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: 272.03 E-value: 3.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 tlapavDIVAakcenlhsklivsqhsregwgnlkemmkYASdshtcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:cd05919 91 ------DDIA----------------------------YLL-----------------YSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPrfDSTSILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGAsAVLNPGWP--TAERVLATLARFRPTVLYGVPTFYANLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 329 QNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDEN 408
Cdd:cd05919 198 DSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 409 GTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEV 488
Cdd:cd05919 278 GHTIPPGEEGDLLV-----RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 489 ESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 568
Cdd:cd05919 353 ESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSP--AAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
|
....*.
gi 564330613 569 KRNELR 574
Cdd:cd05919 431 QRFKLR 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
86-568 |
8.91e-85 |
|
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: 270.64 E-value: 8.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd17631 18 GRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDdtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhneLMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd17631 97 FDD------------------------------------------------------LALLMYTSGTTGRPKGAMLTHRN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 FgLGLSVNGRFWLDLIASDV------MWNTSDTGwaksawssVFSPWT--QGACVfaHYLPRFDSTSILQTLSKFPITVF 317
Cdd:cd17631 123 L-LWNAVNALAALDLGPDDVllvvapLFHIGGLG--------VFTLPTllRGGTV--VILRKFDPETVLDLIERHRVTSF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 318 CSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTETV-LICGNFKGMKI-KPGSMGK 395
Cdd:cd17631 192 FLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 396 PSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDV 475
Cdd:cd17631 271 PVFFVEVRIVDPDGREVPPGEVGEIVV-----RGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 476 ILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIE 555
Cdd:cd17631 346 IISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDED-----ELIAHCRERLARYKIPKSVE 420
|
490
....*....|...
gi 564330613 556 FIEELPKTVSGKV 568
Cdd:cd17631 421 FVDALPRNATGKI 433
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
50-574 |
5.07e-82 |
|
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: 265.93 E-value: 5.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 50 EYFNFAKDVLDqwTNTEKtgKRLSNPAFwwVDGNGkevRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWL 129
Cdd:TIGR02262 1 EKYNAAEDLLD--RNVVE--GRGGKTAF--IDDIS---SLSYGELEAQVRRLAAAL-RRLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 130 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSkLIVSQHSREGWGNLKEMMKYA 209
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 210 SDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG 289
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 290 ACVFAhYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYE 369
Cdd:TIGR02262 230 ATTVL-MGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 370 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVlPDRPFGlfthYVDNPSKTASTLRG 449
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISG-PSSATM----YWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 450 NFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhd 529
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 564330613 530 qeqLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:TIGR02262 462 ---LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
53-568 |
2.00e-80 |
|
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: 264.05 E-value: 2.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 53 NFAKDVLDQwtNTEKTGKRLsnpAFWWVDGNGKEVR-WSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLAN 131
Cdd:cd17634 53 NLAANALDR--HLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 132 VACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVA-AKCENLHSKLIVSqhsREG--- 198
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvPLKKNVDDALnPNVTSVEHVIVLK---RTGsdi 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 199 ------WGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDT 272
Cdd:cd17634 204 dwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 273 GWAKSAWSSVFSPWTQGACVFAHY-LPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCVSAG 348
Cdd:cd17634 284 GWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAagDDAIEGTDRSSLRILGSVG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 349 EPINPEVMEQWKKKTGLD---IYEGYGQTETV-LICGNFKGM-KIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQ 423
Cdd:cd17634 364 EPINPEAYEWYWKKIGKEkcpVVDTWWQTETGgFMITPLPGAiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVIT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 424 V-LPDRPFGLFThyvDNPSKTASTLR--GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:cd17634 444 DpWPGQTRTLFG---DHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564330613 501 SAVVSSPDPIRGEVVKAFIVLNPDykLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 568
Cdd:cd17634 521 AAVVGIPHAIKGQAPYAYVVLNHG--VEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
76-574 |
2.58e-78 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 259.69 E-value: 2.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 76 AFWWVDGNGKEVR-WSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQK 151
Cdd:PRK00174 85 AIIWEGDDPGDSRkITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 152 DILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLHSKLIVS--------QHSREGWGNlkEMMKYASDSHT 214
Cdd:PRK00174 161 ALADRIIDAGAKLVITADegvrggkpiPLKANVDEALANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 215 CVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFA 294
Cdd:PRK00174 239 PEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLM 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 295 HY-LPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD---I 367
Cdd:PRK00174 319 FEgVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGErcpI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 368 YEGYGQTET--VLIC---GnfkGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpDRPFglfthyvdnPS- 441
Cdd:PRK00174 399 VDTWWQTETggIMITplpG---ATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVI----KDPW---------PGm 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 442 ------------KTA-STLRGNfYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPD 508
Cdd:PRK00174 463 mrtiygdherfvKTYfSTFKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPD 541
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330613 509 PIRGEVVKAFIVLNPDYKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK00174 542 DIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
66-574 |
4.68e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 255.60 E-value: 4.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 66 EKTGKRL-SNPAFwwVDGngkEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PRK07656 12 ARAARRFgDKEAY--VFG---DQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 145 TTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKH 220
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 221 NELMAIYFTSGTTGPPK--MIGHTHSsfglgLSvNGRFW---LDLIASD---------------VMWNTsdtgwaksaws 280
Cdd:PRK07656 166 DDVADILFTSGTTGRPKgaMLTHRQL-----LS-NAADWaeyLGLTEGDrylaanpffhvfgykAGVNA----------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 281 svfsPWTQGACVFAHylPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWK 360
Cdd:PRK07656 229 ----PLMRGATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 361 KKTGLDIY-EGYGQTE---TVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHY 436
Cdd:PRK07656 303 SELGVDIVlTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV-----RGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 437 VDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVV 515
Cdd:PRK07656 378 YDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 564330613 516 KAFIVLNPDYKLhDQEQLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK07656 458 KAYVVLKPGAEL-TEEELIAYCREHL----AKYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
83-568 |
6.68e-78 |
|
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: 254.44 E-value: 6.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 83 NGKEvrWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 162
Cdd:cd05911 7 TGKE--LTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 163 KCIITDDTLAPAVdIVAAKCENLHSKLIVSQHSREGWGNLKEMMK---YASDSH--TCVDTKHNELMAIYFTSGTTGPPK 237
Cdd:cd05911 84 KVIFTDPDGLEKV-KEAAKELGPKDKIIVLDDKPDGVLSIEDLLSptlGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 238 MIGHTHSSFGLGL-SVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWtQGACVfaHYLPRFDSTSILQTLSKFPITV 316
Cdd:cd05911 163 GVCLSHRNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATV--IIMPKFDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 317 FCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGK 395
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 396 PSPAFNVEILDENG-TILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSD 473
Cdd:cd05911 320 LLPNVEAKIVDDDGkDSLGPNEPGEICV-----RGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 474 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDqeqlkKEIQEHVKKTTAPYKYPRK 553
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASYKQLRG 469
|
490
....*....|....*.
gi 564330613 554 -IEFIEELPKTVSGKV 568
Cdd:cd05911 470 gVVFVDEIPKSASGKI 485
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
71-574 |
1.61e-77 |
|
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: 256.86 E-value: 1.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 71 RLSNPAFWWVDG-NGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTV--LIPG--- 144
Cdd:cd05967 64 RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfa 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 145 TTQLTQkdilyRLQSSKSKCIITDDTLAPAVDIVAAKcENLHSKLIVSQH------------------SREGWGNLKEMM 206
Cdd:cd05967 143 AKELAS-----RIDDAKPKLIVTASCGIEPGKVVPYK-PLLDKALELSGHkphhvlvlnrpqvpadltKPGRDLDWSELL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 207 KYASdSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPW 286
Cdd:cd05967 217 AKAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 287 TQGAcvfahylprfdsTSIL---------------QTLSKFPITVFCSAPTAYRMLIQND----ITRSYKFNSLKHCVSA 347
Cdd:cd05967 296 LHGA------------TTVLyegkpvgtpdpgafwRVIEKYQVNALFTAPTAIRAIRKEDpdgkYIKKYDLSSLRTLFLA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 348 GEPINPEVMEQWKKKTGLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQ 423
Cdd:cd05967 364 GERLDPPTLEWAENTLGVPVIDHWWQTETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 424 vLPDRPFGLFTHYVDNP---SKTASTLRGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:cd05967 444 -LPLPPGCLLTLWKNDErfkKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564330613 501 SAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd05967 522 CAVVGVRDELKGQVPLGLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-479 |
7.37e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 249.54 E-value: 7.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 82 GNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 161
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 162 SKCIITDDTL-APAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSH-TCVDTKHNELMAIYFTSGTTGPPKMI 239
Cdd:pfam00501 94 AKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPpPPPPPDPDDLAYIIYTSGTTGKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 240 GHTH---SSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFDSTSILQTLSKFPIT 315
Cdd:pfam00501 174 MLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 316 VFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET---VLICGNFKGMKIKPGS 392
Cdd:pfam00501 254 VLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgvVTTPLPLDEDLRSLGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 393 MGKPSPAFNVEILDEN-GTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVA 470
Cdd:pfam00501 334 VGRPLPGTEVKIVDDEtGEPVPPGEPGELCV-----RGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVG 408
|
....*....
gi 564330613 471 RSDDVILSS 479
Cdd:pfam00501 409 RKKDQIKLG 417
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
90-573 |
1.81e-75 |
|
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: 246.24 E-value: 1.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITdd 169
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 tlapavdivaakcenlHSKLivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSSFgLG 249
Cdd:cd05935 80 ----------------GSEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQ 329
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 330 NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILD-EN 408
Cdd:cd05935 190 TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 409 GTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIG 484
Cdd:cd05935 270 GRELPPNEVGEIVV-----RGPQIFKGYWNRPEETEEsfiEIKGRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 485 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTV 564
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDELPRSA 421
|
....*....
gi 564330613 565 SGKVKRNEL 573
Cdd:cd05935 422 SGKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
62-578 |
1.94e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 247.18 E-value: 1.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 62 WTNTEKTGKRLSNPAFWWVDGNgkevRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVL 141
Cdd:PRK08314 13 FHNLEVSARRYPDKTAIVFYGR----AISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 142 IPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVD-----------IVAAKCENLHSK-------LIVSQHSRE-----G 198
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSELAPKVApavgnlrlrhvIVAQYSDYLPAEpeiavpaWLRAEPPLQalapgG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 199 WGNLKEMMK--YASDSHTcvdTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSD----T 272
Cdd:PRK08314 169 VVAWKEALAagLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfhvT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 273 GWAKSAWSSVFSpwtqGACVFahYLPRFDSTSILQTLSKFPITVFCSAPTayrMLIQ---NDITRSYKFNSLKHCVSAGE 349
Cdd:PRK08314 245 GMVHSMNAPIYA----GATVV--LMPRWDREAAARLIERYRVTHWTNIPT---MVVDflaSPGLAERDLSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 350 PINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSpaFNVE--ILD-ENGTILPPGQEGDIAV--- 422
Cdd:PRK08314 316 AMPEAVAERLKELTGLDYVEGYGLTETMaQTHSNPPD-RPKLQCLGIPT--FGVDarVIDpETLEELPPGEVGEIVVhgp 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 423 QVlpdrpfglFTHYVDNPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSI 498
Cdd:PRK08314 393 QV--------FKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 499 AESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 578
Cdd:PRK08314 465 QEACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEK 541
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-574 |
6.00e-74 |
|
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: 242.20 E-value: 6.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 168 DdtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhneLMAIYFTSGTTGPPK--MIGHTHSS 245
Cdd:cd05934 82 D------------------------------------------------------PASILYTSGTTGPPKgvVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 FGLGLSVNgrfWLDLIASDVMW--------NTSDTGWAkSAWSSvfspwtQGACVFahyLPRFDSTSILQTLSKFPITVF 317
Cdd:cd05934 108 FAGYYSAR---RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL---LPRFSASRFWSDVRRYGATVT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 318 CSAPTAYRMLIQNDITRSYKFNSLKHCVSAgePINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPS 397
Cdd:cd05934 175 NYLGAMLSYLLAQPPSPDDRAHRLRAAYGA--PNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 398 PAFNVEILDENGTILPPGQEGDIAVQvlPDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVIL 477
Cdd:cd05934 253 PGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 478 SSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEqlkkEIQEHVKKTTAPYKYPRKIEFI 557
Cdd:cd05934 331 RRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETL-DPE----ELFAFCEGQLAYFKVPRYIRFV 405
|
490
....*....|....*..
gi 564330613 558 EELPKTVSGKVKRNELR 574
Cdd:cd05934 406 DDLPKTPTEKVAKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
88-575 |
3.06e-73 |
|
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: 240.65 E-value: 3.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIit 167
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 168 ddtLAPAVdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelmaIYFTSGTTGPPKMIGHTHSSfg 247
Cdd:cd05941 89 ---LDPAL--------------------------------------------------ILYTSGTTGRPKGVVLTHAN-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 248 lglsvngrfwldlIASDVMWNTSDTGWAKS--------------AWSSVFSP-WTQGACVFahyLPRFDSTSILQTLSKF 312
Cdd:cd05941 114 -------------LAANVRALVDAWRWTEDdvllhvlplhhvhgLVNALLCPlFAGASVEF---LPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 313 PITVFCSAPTAYRMLIQ--------NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGN-F 383
Cdd:cd05941 178 SITVFMGVPTIYTRLLQyyeahftdPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 384 KGmKIKPGSMGKPSPAFNVEILDENGT-ILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRG-NFYITGDRGYMD 461
Cdd:cd05941 258 DG-ERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQV-----RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 462 EDGYFWFVAR-SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLKkeiqEH 540
Cdd:cd05941 332 EDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EW 407
|
490 500 510
....*....|....*....|....*....|....*
gi 564330613 541 VKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
84-577 |
2.65e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 236.47 E-value: 2.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 84 GKEVrwSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:PRK06710 47 GKDI--TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 164 CIITDDTLAPAVDIV--AAKCENL-----------------------HSKLIV---SQHSREGWGNLKEmmkyasDSHTC 215
Cdd:PRK06710 124 VILCLDLVFPRVTNVqsATKIEHVivtriadflpfpknllypfvqkkQSNLVVkvsESETIHLWNSVEK------EVNTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 216 VDT---KHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLdliasdvmWNTSDTGWAKSAWSSVFSPWTQGAC- 291
Cdd:PRK06710 198 VEVpcdPENDLALLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWL--------YNCKEGEEVVLGVLPFFHVYGMTAVm 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 292 ---VFAHY----LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTG 364
Cdd:PRK06710 269 nlsIMQGYkmvlIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 365 LDIYEGYGQTETVLIC-GNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVQVlPDrpfgLFTHYVDNPSK 442
Cdd:PRK06710 349 GKLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKG-PQ----IMKGYWNKPEE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 443 TASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 522
Cdd:PRK06710 424 TAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 564330613 523 pdyklHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 577
Cdd:PRK06710 504 -----EGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
53-574 |
1.11e-68 |
|
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: 233.54 E-value: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 53 NFAKDVLDQWTNTEKTgkrlsNPAFWWVDGNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANV 132
Cdd:cd05968 61 NIVEQLLDKWLADTRT-----RPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 133 ACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLhSKLIVSQHSregwGNLK 203
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTV-EKVVVVRHL----GNDF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 204 EMMKYASDSHTCVDTKH----------NELMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTG 273
Cdd:cd05968 210 TPAKGRDLSYDEEKETAgdgaerteseDPLMIIY-TSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 274 WAKSAWsSVFSPWTQGACVFAHY-LPRFDSTSIL-QTLSKFPITVFCSAPTAYRMLI--QNDITRSYKFNSLKHCVSAGE 349
Cdd:cd05968 289 WMMGPW-LIFGGLILGATMVLYDgAPDHPKADRLwRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 350 PINPEVMeQWKKKTGLD----IYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPgQEGDIAVQ- 423
Cdd:cd05968 368 PWNPEPW-NWLFETVGKgrnpIINYSGGTEISgGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLa 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 424 VLPDRPFGLF---THYVDnpskTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:cd05968 446 PWPGMTRGFWrdeDRYLE----TYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564330613 501 SAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd05968 522 SAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
88-574 |
2.94e-66 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 223.98 E-value: 2.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:PRK07514 28 RYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 168 DDTLAPAVDIVAAKCENLHskliVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPK--M------- 238
Cdd:PRK07514 107 DPANFAWLSKIAAAAGAPH----VETLDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMlshgnll 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 239 -----------------------IGHTHssfGLGLSVNGRfwldLIAsdvmwntsdtgwaksawssvfspwtqGACVFah 295
Cdd:PRK07514 183 snaltlvdywrftpddvlihalpIFHTH---GLFVATNVA----LLA--------------------------GASMI-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 296 YLPRFDSTSILQTLSKfpITVFCSAPTAY-RMLIQNDITRsykfNSLKH---CVSAGEPINPEVMEQWKKKTGLDIYEGY 371
Cdd:PRK07514 228 FLPKFDPDAVLALMPR--ATVMMGVPTFYtRLLQEPRLTR----EAAAHmrlFISGSAPLLAETHREFQERTGHAILERY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTETVLICGN-FKGMKIkPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVQvlpdrpfG--LFTHYVDNPSKTASTL 447
Cdd:PRK07514 302 GMTETNMNTSNpYDGERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 448 RGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYK 526
Cdd:PRK07514 374 RADgFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAA 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 564330613 527 LhDQEQLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK07514 454 L-DEAAILAALKGRL----ARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
89-574 |
5.30e-65 |
|
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: 220.65 E-value: 5.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 89 WSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 169 D----------------TLAPAVDivAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDshtcvdtkhneLMAIYFTSGT 232
Cdd:cd05926 94 KgelgpasraasklglaILELALD--VGVLIRAPSAESLSNLLADKKNAKSEGVPLPDD-----------LALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 233 TGPPKMIGHTHssfgLGLSVNGRFwldlIASDVMWNTSDT-----------GWAKSAWSSVFSpwtQGACVFAhylPRFD 301
Cdd:cd05926 161 TGRPKGVPLTH----RNLAASATN----ITNTYKLTPDDRtlvvmplfhvhGLVASLLSTLAA---GGSVVLP---PRFS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 302 STSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYK-FNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV--L 378
Cdd:cd05926 227 ASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 379 ICGNFKGMKIKPGSMGKPspaFNVE--ILDENGTILPPGQEGDIAVQ---VlpdrpfglfTH-YVDNPSKTA-STLRGNF 451
Cdd:cd05926 307 TSNPLPPGPRKPGSVGKP---VGVEvrILDEDGEILPPGVVGEICLRgpnV---------TRgYLNNPEANAeAAFKDGW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 452 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqe 531
Cdd:cd05926 375 FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV---- 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 564330613 532 qLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd05926 451 -TEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
73-573 |
9.82e-64 |
|
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: 217.49 E-value: 9.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 73 SNPAFwwVDG-NGKEVrwSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQK 151
Cdd:cd05904 20 SRPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 152 DILYRLQSSKSKCIITDDTLAPavdivaaKCENLHSKLI-VSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTS 230
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELAE-------KLASLALPVVlLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 231 GTTGPPK--MIGH---------THSSFGLGLSVNGRFWLDLIASDVMwntsdtGWAKSAWSSVFSpwtqGACVFAhyLPR 299
Cdd:cd05904 168 GTTGRSKgvMLTHrnliamvaqFVAGEGSNSDSEDVFLCVLPMFHIY------GLSSFALGLLRL----GATVVV--MPR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 300 FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTET-- 376
Cdd:cd05904 236 FDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTEStg 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 377 -VLICGNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI- 453
Cdd:cd05904 316 vVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWI-----RGPSIMKGYLNNPEATAATIDKEGWLh 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 454 TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdQEQl 533
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSL--TED- 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 564330613 534 kkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd05904 468 --EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
85-574 |
3.53e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 216.34 E-value: 3.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 85 KEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKC 164
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 165 IITDDTLAPAVDIVAAKCENLHSKLIVS---QHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGH 241
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 242 THSSFgLGLSVNGRFWLDLIASDVMWNtsdtgwA----KSAWSSVF-SPWTQ-GACVfaHYLPRFDSTSILQTLSKFPIT 315
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDVFlGPYLYvGATN--VILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 316 VFCSAPTAYRMLIQNDITRSYKFNSLKHCVSaGEPINP-EVMEQWKKK-TGLDIYEGYGQTE-----TVLicgNFKGMKI 388
Cdd:PRK08316 263 SFFAPPTVWISLLRHPDFDTRDLSSLRKGYY-GASIMPvEVLKELRERlPGLRFYNCYGQTEiaplaTVL---GPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 389 KPGSMGKPspAFNVE--ILDENGTILPPGQEGDIAvqvlpDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYF 466
Cdd:PRK08316 339 RPGSAGRP--VLNVEtrVVDDDGNDVAPGEVGEIV-----HRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 467 WFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqLKKEIQEHVKKTTA 546
Cdd:PRK08316 412 TVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATV-----TEDELIAHCRARLA 486
|
490 500
....*....|....*....|....*...
gi 564330613 547 PYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK08316 487 GFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
80-578 |
9.30e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 212.07 E-value: 9.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 80 VDGNGKEvrWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:PRK08276 5 MAPSGEV--VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 160 SKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKE----MMKYASDSHTCVDtkhneLMAiyFTSGTTGP 235
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEalaaQPDTPIADETAGA-----DML--YSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 236 PKMI------GHTHSSFGLGLSVNGRFwldliasdvMWNTSDTGWAKSA--WSSVFSPWTQGACVFAH---YLPRFDSTS 304
Cdd:PRK08276 155 PKGIkrplpgLDPDEAPGMMLALLGFG---------MYGGPDSVYLSPAplYHTAPLRFGMSALALGGtvvVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 305 ILQTLSKFPITVFCSAPTAY-RMLIQNDITR-SYKFNSLKHCVSAGEPINPEVMEQ----WkkktGLDIYEGYGQTE--- 375
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFvRMLKLPEEVRaRYDVSSLRVAIHAAAPCPVEVKRAmidwW----GPIIHEYYASSEggg 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 376 -TVLICGNFKGmkiKPGSMGKPSPAfNVEILDENGTILPPGQEGDIAVQvLPDRPFglftHYVDNPSKTASTLRGNFYIT 454
Cdd:PRK08276 302 vTVITSEDWLA---HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPF----EYHNDPEKTAAARNPHGWVT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 455 -GDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQL 533
Cdd:PRK08276 373 vGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD--AGDAL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 564330613 534 KKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 578
Cdd:PRK08276 451 AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYW 495
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
86-581 |
2.52e-58 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 203.84 E-value: 2.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAKCENLHSKLIV----SQHSREGWGNLKemMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGH 241
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLdapaSVSVPAGWSTAP--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 242 THSSFglglsvngrFW--------LDLIASDVMWNTSDTgWAKSAWSSVFSPWTQGACVfaHYLPRFDSTSILQTLSKFP 313
Cdd:PRK06155 201 PHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALNAFFQALLAGATY--VLEPRFSASGFWPAVRRHG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 314 ITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPinPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKiKPGSM 393
Cdd:PRK06155 269 ATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 394 GKPSPAFNVEILDENGTILPPGQEGDIAVQVlpDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSD 473
Cdd:PRK06155 346 GRLAPGFEARVVDEHDQELPDGEPGELLLRA--DEPFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 474 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRK 553
Cdd:PRK06155 424 DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV-----ALVRHCEPRLAYFAVPRY 498
|
490 500
....*....|....*....|....*...
gi 564330613 554 IEFIEELPKTVSGKVKRNELRRKEWTTT 581
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLREQGVTAD 526
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
89-575 |
4.37e-58 |
|
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: 199.88 E-value: 4.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 89 WSFEEL----GSLSRKFANILTeacslQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKC 164
Cdd:cd05912 2 YTFAELfeevSRLAEHLAALGV-----RKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 165 iitDDTlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelMAIYFTSGTTGPPKMIGHT-- 242
Cdd:cd05912 77 ---DDI-----------------------------------------------------ATIMYTSGTTGKPKGVQQTfg 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 243 -H------SSFGLGLSVNGRfWLDLIAsdvMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFDSTSILQTLSKFPIT 315
Cdd:cd05912 101 nHwwsaigSALNLGLTEDDN-WLCALP---LFHIS-------GLSILMRSVIYGMTVYLV--DKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 316 VFCSAPTAYRMLIQnDITRSYKfNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTETV--LICGNFKGMKIKPGSM 393
Cdd:cd05912 168 IISVVPTMLQRLLE-ILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 394 GKPSPAFNVEILDENGtilPPGQEGDIAVQ---VLPDrpfglfthYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVA 470
Cdd:cd05912 245 GKPLFPVELKIEDDGQ---PPYEVGEILLKgpnVTKG--------YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 471 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYklhDQEQLKKEIQEHVKKttapYKY 550
Cdd:cd05912 314 RRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKLAK----YKV 386
|
490 500
....*....|....*....|....*
gi 564330613 551 PRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:cd05912 387 PKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
84-575 |
1.28e-57 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 200.86 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 84 GKEVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 164 CIITDDTLAPAVDIVAAKCENLHSKLIVSqhsregwgnLKEMMKYASDShtCVDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITS---------LKEIEDRKIDN--FVEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 244 SSFGLGlSVNGRFWLDLIASDV------MWNTSDTGWAksawssVFSPWTQGACVFahyLP-RFDSTSILQTLSKFPITV 316
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF------AFPTLFAGGVII---VPrKFEPTKALSMIEKHKVTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 317 FCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTET-----VLICGNFKGmkiKPG 391
Cdd:PRK06839 242 VMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 392 SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVAR 471
Cdd:PRK06839 318 SIGKPVLFCDYELIDENKNKVEVGEVGELLI-----RGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 472 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqLKKEIQEHVKKTTAPYKYP 551
Cdd:PRK06839 393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVL-----IEKDVIEHCRLFLAKYKIP 467
|
490 500
....*....|....*....|....
gi 564330613 552 RKIEFIEELPKTVSGKVKRNELRR 575
Cdd:PRK06839 468 KEIVFLKELPKNATGKIQKAQLVN 491
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
70-575 |
9.67e-57 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 201.33 E-value: 9.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 70 KRLSNPAFWWVDGN-GKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPG- 144
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 145 -TTQLTQkdilyRLQSSKSKCIITDDTLAPAVDIVAAK------CENLHSK----LIVSQhsregwgNLKEMMK------ 207
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADAGSRGGKVVPYKplldeaIALAQHKprhvLLVDR-------GLAPMARvagrdv 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 208 -YAS------DSHT-CVDTKHNELMAIYFTSGTTGPPKMI-----GHThssFGLGLSVNGRFwlDLIASDVMWNTSDTGW 274
Cdd:PRK10524 212 dYATlraqhlGARVpVEWLESNEPSYILYTSGTTGKPKGVqrdtgGYA---VALATSMDTIF--GGKAGETFFCASDIGW 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 275 AKSAWSSVFSPWTQG-ACVFAHYLP-RFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDIT--RSYKFNSLKHCVSAGEP 350
Cdd:PRK10524 287 VVGHSYIVYAPLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPAllRKHDLSSLRALFLAGEP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 351 INpEVMEQWKKKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFNVEILDEN-GTILPPGQEGDIAVQV 424
Cdd:PRK10524 367 LD-EPTASWISEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 425 -LPdrPFGLFTHYVDNP---SKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:PRK10524 446 pLP--PGCMQTVWGDDDrfvKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564330613 501 SAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQ---LKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVkrneLRR 575
Cdd:PRK10524 524 VAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKL----LRR 597
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
80-577 |
2.09e-56 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 197.11 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 80 VDGNGKevrWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:PRK03640 22 EFEEKK---VTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 160 SKSKCIITDDTLApavdivaakcenlhSKLIVSQHSRegwgnLKEMMKYASDSHTCVDTKH-NELMAIYFTSGTTGPPKM 238
Cdd:PRK03640 98 AEVKCLITDDDFE--------------AKLIPGISVK-----FAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 239 I-----GHTHSSFG----LGLSVNGRfWLdliASDVMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFDSTSILQTL 309
Cdd:PRK03640 159 ViqtygNHWWSAVGsalnLGLTEDDC-WL---AAVPIFHIS-------GLSILMRSVIYGMRVVLV--EKFDAEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 310 SKFPITVFCSAPTAYRMLIQNDITRSYKfNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTETV-LICG-NFKGMK 387
Cdd:PRK03640 226 QTGGVTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsQIVTlSPEDAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 388 IKPGSMGKPspAFNVEI-LDENGTILPPGQEGDIAVQ---VLPDrpfglfthYVDNPSKTASTLRGNFYITGDRGYMDED 463
Cdd:PRK03640 304 TKLGSAGKP--LFPCELkIEKDGVVVPPFEEGEIVVKgpnVTKG--------YLNREDATRETFQDGWFKTGDIGYLDEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 464 GYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpDYKLhDQEQLKKEIQEHVkk 543
Cdd:PRK03640 374 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEV-TEEELRHFCEEKL-- 448
|
490 500 510
....*....|....*....|....*....|....
gi 564330613 544 ttAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 577
Cdd:PRK03640 449 --AKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
90-573 |
1.10e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 197.19 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK06178 60 TYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPAVDIVAAKCEnLHSKLIVSQH--------------------SREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFT 229
Cdd:PRK06178 139 QLAPVVEQVRAETS-LRHVIVTSLAdvlpaeptlplpdslraprlAAAGAIDLLPALRACTAPVPLPPPALDALAALNYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 230 SGTTGPPKMIGHTH-------SSFGlGLSVNGRfwldliASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahYLPRFDS 302
Cdd:PRK06178 218 GGTTGMPKGCEHTQrdmvytaAAAY-AVAVVGG------EDSVFLSFLPEFWIAGENFGLLFPLFSGATLV--LLARWDA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 303 TSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKH--CVSAGEPINPEVMEQWKKKTGLDIYEG-YGQTETvLI 379
Cdd:PRK06178 289 VAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTET-HT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 380 CGNF-KGM-------KIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN 450
Cdd:PRK06178 368 CDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVV-----RTPSLLKGYWNKPEATAEALRDG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 451 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQ 530
Cdd:PRK06178 443 WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADL-TA 521
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 564330613 531 EQLKKEIQEHVkkttAPYKYPrKIEFIEELPKTVSGKVKRNEL 573
Cdd:PRK06178 522 AALQAWCRENM----AVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
86-574 |
2.35e-54 |
|
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: 191.74 E-value: 2.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLApavdivaakcenlHSKLIVSQHSREGWgnlkemmKYASDSHtcvdtkhnELMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd12118 106 FVDREFE-------------YEDLLAEGDPDFEW-------IPPADEW--------DPIALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 FglglsvngrfWLDLIASDVMWNTSD-------------TGWAksawssvfSPWTQGACVFAHY-LPRFDSTSILQTLSK 311
Cdd:cd12118 158 A----------YLNALANILEWEMKQhpvylwtlpmfhcNGWC--------FPWTVAAVGGTNVcLRKVDAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 312 FPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQwKKKTGLDIYEGYGQTET---VLICgnfkgmKI 388
Cdd:cd12118 220 HKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVC------AW 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 389 KPGSMGKPSP---------------AFNVEILDENGTILPP--GQE-GDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN 450
Cdd:cd12118 293 KPEWDELPTEerarlkarqgvryvgLEEVDVLDPETMKPVPrdGKTiGEIVF-----RGNIVMKGYLKNPEATAEAFRGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 451 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQ 530
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 564330613 531 eqlkkEIQEHVKKTTAPYKYPRKIEFiEELPKTVSGKVKRNELR 574
Cdd:cd12118 448 -----EIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLR 485
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
57-574 |
4.49e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 192.91 E-value: 4.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 57 DVLDQwtNTEKTGKRlsnPAFWWVdgnGKEVrwSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLR 136
Cdd:PRK05605 36 DLYDN--AVARFGDR---PALDFF---GATT--TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 137 TGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAP---------------AVDIVAA------------------KCE 183
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPtverlrrttpletivSVNMIAAmpllqrlalrlpipalrkARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 184 NLHSKL-------IVSQHSREGWGNLKEMMKYASDShtcvdtkhneLMAIYFTSGTTGPPKMIGHTHSsfglGLSVN--- 253
Cdd:PRK05605 185 ALTGPApgtvpweTLVDAAIGGDGSDVSHPRPTPDD----------VALILYTSGTTGKPKGAQLTHR----NLFANaaq 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 254 GRFWLDLIASD----------------VMWNTsdtgwaksawssvFSPWTQGACVFahyLPRFDSTSILQTLSKFPITVF 317
Cdd:PRK05605 251 GKAWVPGLGDGpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMKKHPPTWL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 318 CSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKP 396
Cdd:PRK05605 315 PGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 397 SPAFNVEILD-EN-GTILPPGQEGDIAV---QVlpdrpfglFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVAR 471
Cdd:PRK05605 395 FPDTEVRIVDpEDpDETMPDGEEGELLVrgpQV--------FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 472 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKkeiqEHVKKTTAPYKYP 551
Cdd:PRK05605 467 IKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAAL-DPEGLR----AYCREHLTRYKVP 541
|
570 580
....*....|....*....|...
gi 564330613 552 RKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK05605 542 RRFYHVDELPRDQLGKVRRREVR 564
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
90-574 |
6.12e-54 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 192.16 E-value: 6.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPAVD-----------IVAAKCENLHSK-LIVSQHSRegwgNLKEMM----------------KYASDSHTCVDTKHN 221
Cdd:PRK07059 129 NFATTVQqvlaktavkhvVVASMGDLLGFKgHIVNFVVR----RVKKMVpawslpghvrfndalaEGARQTFKPVKLGPD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 222 ELMAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSdtgWAKSAWSS---VFSPWTQGAC----VFA 294
Cdd:PRK07059 205 DVAFLQYTGGTTGVSKGATLLHRN---------------IVANVLQMEA---WLQPAFEKkprPDQLNFVCALplyhIFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 295 ---HYL--------------PRfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVME 357
Cdd:PRK07059 267 ltvCGLlgmrtggrnilipnPR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 358 QWKKKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLPDrpfgl 432
Cdd:PRK07059 346 RWLEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIrgpQVMAG----- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 433 fthYVDNPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 511
Cdd:PRK07059 420 ---YWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564330613 512 GEVVKAFIVLNpdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK07059 497 GEAVKLFVVKK------DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
80-573 |
1.08e-53 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 188.89 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 80 VDGNGkevRWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd05930 7 VDGDQ---SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 160 SKSKCIITDdtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkHNELMAIYFTSGTTGPPKMI 239
Cdd:cd05930 83 SGAKLVLTD---------------------------------------------------PDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 240 GHTHSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLP---RFDSTSILQTLSKF 312
Cdd:cd05930 112 MVEHRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATL--VVLPeevRKDPEALADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 313 PITVFCSAPTAYRMLIQNDITRSykFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTETVLICGNF--KGMKIK 389
Cdd:cd05930 184 GITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYYrvPPDDEE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 390 PGSM--GKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYM 460
Cdd:cd05930 262 DGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELYI-----GGAGLARGYLNRPELTAERFVPNpfgpgerMYRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 461 DEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqeqlKKEIQEH 540
Cdd:cd05930 337 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD-----EEELRAH 411
|
490 500 510
....*....|....*....|....*....|...
gi 564330613 541 VKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd05930 412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
297-570 |
1.73e-53 |
|
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: 185.17 E-value: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 297 LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHcVSAGEpiNPEVMEQWKKKTGLDIYEGYGQTET 376
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 377 ---VLICGNFKgmkiKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI 453
Cdd:cd17637 149 sglVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV-----RGPLVFQGYWNLPELTAYTFRNGWHH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 454 TGDRGYMDEDGYFWFVARS--DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqe 531
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLT--- 296
|
250 260 270
....*....|....*....|....*....|....*....
gi 564330613 532 qlKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 570
Cdd:cd17637 297 --ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-579 |
5.89e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 189.04 E-value: 5.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 73 SNPAFWWVDGngkevRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIP-GTTQl 148
Cdd:PRK06188 27 DRPALVLGDT-----RLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrTALHPlGSLD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 149 tqkDILYRLQSSKSKCIITDDT--LAPAVDIvAAKCENLHSKLIVSQhSREGWGNLKEMMKYASDSHTCVDTkHNELMAI 226
Cdd:PRK06188 100 ---DHAYVLEDAGISTLIVDPApfVERALAL-LARVPSLKHVLTLGP-VPDGVDLLAAAAKFGPAPLVAAAL-PPDIAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 227 YFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF----------AHY 296
Cdd:PRK06188 174 AYTGGTTGKPKGVMGTHRS---------------IATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFflptllrggtVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 297 LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE- 375
Cdd:PRK06188 239 LAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEa 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 376 ----TVLICGNFKGMKIKP-GSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN 450
Cdd:PRK06188 319 pmviTYLRKRDHDPDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICV-----RGPLVMDGYWNRPEETAEAFRDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 451 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlHDQ 530
Cdd:PRK06188 394 WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAA-VDA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 564330613 531 EqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWT 579
Cdd:PRK06188 473 A----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWE 517
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
67-574 |
6.43e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 188.71 E-value: 6.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 67 KTGKRLSN-PAFWWvdgngKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGT 145
Cdd:PRK07470 15 QAARRFPDrIALVW-----GDRSWTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 146 TQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKL-IVSQHSREGWGNLkeMMKYASDSHTCVDTKHNELM 224
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVaIGGARAGLDYEAL--VARHLGARVANAAVDHDDPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 225 AIYFTSGTTGPPKMIGHTHSSfgLGLSVNGRFwldliaSDVMWNTSDTGWaksawSSVFSPWTQGACVfaHYL------- 297
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLTHGQ--MAFVITNHL------ADLMPGTTEQDA-----SLVVAPLSHGAGI--HQLcqvarga 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 298 -------PRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEG 370
Cdd:PRK07470 232 atvllpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 371 YGQTE-----TVL-ICGNF--KGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPdrpfgLFTHYVDNPSK 442
Cdd:PRK07470 312 FGLGEvtgniTVLpPALHDaeDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPA-----VFAGYYNNPEA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 443 TASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 522
Cdd:PRK07470 387 NAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 564330613 523 PDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK07470 467 DGAPVDEA-----ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
84-576 |
8.24e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 188.83 E-value: 8.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 84 GKEVRWSfeELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:PRK07786 40 GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 164 CIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK07786 117 VVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 244 SSfglglsVNGRFwLDLIASDVMWNTSDTGWAKS------AWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPIT-V 316
Cdd:PRK07786 197 AN------LTGQA-MTCLRTNGADINSDVGFVGVplfhiaGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTgI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 317 FCsAPTAYRMLIQNDITRSYKFnSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTE----TVLICGNFKGMKIkpG 391
Cdd:PRK07786 270 FL-VPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEmspvTCMLLGEDAIRKL--G 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 392 SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVAR 471
Cdd:PRK07786 346 SVGKVIPTVAARVVDENMNDVPVGEVGEIVY-----RAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 472 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLKKEIQEHVkkttAPYKYP 551
Cdd:PRK07786 421 KKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRL----ARYKHP 496
|
490 500
....*....|....*....|....*
gi 564330613 552 RKIEFIEELPKTVSGKVKRNELRRK 576
Cdd:PRK07786 497 KALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
90-577 |
1.06e-52 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 189.11 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPAVDIVAAKCENLHSKL--IVSQHSReGWGNL--------KEMM-KY---ASDSHTCV------------DTKHNEL 223
Cdd:PRK08974 130 NFAHTLEKVVFKTPVKHVILtrMGDQLST-AKGTLvnfvvkyiKRLVpKYhlpDAISFRSAlhkgrrmqyvkpELVPEDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 224 MAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWntsdtgwAKSAWSSVFSPWTQGAC-------VFAHY 296
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRN---------------MLANLEQ-------AKAAYGPLLHPGKELVVtalplyhIFALT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 297 L-----------------PRfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQW 359
Cdd:PRK08974 267 VncllfielggqnllitnPR-DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERW 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 360 KKKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLpdrpfglfTH 435
Cdd:PRK08974 346 VKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVkgpQVM--------LG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 436 YVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVV 515
Cdd:PRK08974 418 YWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAV 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564330613 516 KAFIVLNpdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 577
Cdd:PRK08974 498 KIFVVKK------DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
88-574 |
7.64e-52 |
|
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: 183.74 E-value: 7.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKipeWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKSKC 164
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPN---WWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 165 IITDDTlapavdivaakcenlhsklivsqhsregWGNlkemMKYASDShtcvdtkhNELMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05903 77 FVVPER----------------------------FRQ----FDPAAMP--------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 245 SfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFDSTSILQTLSKFPITVFCSAP 321
Cdd:cd05903 117 T----LSASIRQYAERLGlgpGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 322 TayrmlIQNDITRSYKF-----NSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNfkgmkIKPG----- 391
Cdd:cd05903 191 P-----FLTDLLNAVEEageplSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPApedrr 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 392 --SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFV 469
Cdd:cd05903 261 lyTDGRPLPGVEIKVVDDTGATLAPGVEGELLS-----RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRIT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 470 ARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEqlkkEIQEHV-KKTTAPY 548
Cdd:cd05903 336 GRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALL-TFD----ELVAYLdRQGVAKQ 410
|
490 500
....*....|....*....|....*.
gi 564330613 549 KYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd05903 411 YWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
81-574 |
3.00e-51 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 184.12 E-value: 3.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 81 DGNGKEVRWSFEELGSLSRKFANiLTEACSLQRGDRVMVILPKIPEW---WLAnVACLrtGTVLIPGTTQLTQKDILYRL 157
Cdd:PRK08008 30 SSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMVPINARLLREESAWIL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 158 QSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSqhsREGWGNLKEMMKYAS--DSHTCVDTKHNELMA-----IYFTS 230
Cdd:PRK08008 106 QNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLT---RVALPADDGVSSFTQlkAQQPATLCYAPPLSTddtaeILFTS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 231 GTTGPPKMIGHTHSsfglglsvNGRF------W-LDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFDST 303
Cdd:PRK08008 183 GTTSRPKGVVITHY--------NLRFagyysaWqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL--LEKYSAR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 304 SILQTLSKFPITVFCSAPtayrMLIQNDITRSYKFNSLKHCVSagepinpEVM------EQWK----KKTGLDIYEGYGQ 373
Cdd:PRK08008 253 AFWGQVCKYRATITECIP----MMIRTLMVQPPSANDRQHCLR-------EVMfylnlsDQEKdafeERFGVRLLTSYGM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 374 TETVL-ICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPDRPfgLFTHYVDNPSKTASTLRGNFY 452
Cdd:PRK08008 322 TETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKT--IFKEYYLDPKATAKVLEADGW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 453 I-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQe 531
Cdd:PRK08008 400 LhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE- 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 564330613 532 qlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK08008 479 ----EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
90-574 |
4.38e-51 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 184.70 E-value: 4.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPAVDIVAAKCE---------------------NL---HSKLIVSQHSREGWGNLKEMMKYASdSHTC--VDTKHNEL 223
Cdd:PRK08751 132 NFGTTVQQVIADTPvkqvittglgdmlgfpkaalvNFvvkYVKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 224 MAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRfWLD-----------LIASDVMWNTsdtgWAKSAWSSVFSPWtqGACV 292
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAgtgkleegcevVITALPLYHI----FALTANGLVFMKI--GGCN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 293 FAHYLPRfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG 372
Cdd:PRK08751 284 HLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 373 QTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTASTLR 448
Cdd:PRK08751 363 LTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIkgpQVMKG--------YWKRPEETAKVMD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 449 GNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdykl 527
Cdd:PRK08751 435 ADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK----- 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 564330613 528 hDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK08751 510 -DPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
86-574 |
5.51e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 181.51 E-value: 5.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 I------TDDTLAPAVDIV---------AAKCENL-HSKLIVSQHSRE-----GWGNLKEMMKYASDSHTCVDT---KHN 221
Cdd:PRK12583 122 IcadafkTSDYHAMLQELLpglaegqpgALACERLpELRGVVSLAPAPppgflAWHELQARGETVSREALAERQaslDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 222 ELMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRF---WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahyLP 298
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLV---YP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 299 R--FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL-DIYEGYGQTE 375
Cdd:PRK12583 275 NeaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 376 T---VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFY 452
Cdd:PRK12583 355 TspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCT-----RGYSVMKGYWNNPEATAESIDEDGW 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 453 I-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQe 531
Cdd:PRK12583 430 MhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE- 508
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 564330613 532 qlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK12583 509 ----ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
90-579 |
1.11e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 179.50 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPAVDIVAAKCENLHSKLIVSQH-SREGWGNLKEMMKYASDshTCVDTKhNELMAIYFTSGTTGPPKMIGHTHSSFGL 248
Cdd:PRK13391 105 AKLDVARALLKQCPGVRHRLVLDGDgELEGFVGYAEAVAGLPA--TPIADE-SLGTDMLYSSGTTGRPKGIKRPLPEQPP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 249 GLSVNgrfWLDLIASdvMWN-TSDTGW---------AKSAWSSVfspwTQ--GACVFAhyLPRFDSTSILQTLSKFPITV 316
Cdd:PRK13391 182 DTPLP---LTAFLQR--LWGfRSDMVYlspaplyhsAPQRAVML----VIrlGGTVIV--MEHFDAEQYLALIEEYGVTH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 317 FCSAPTAY-RML-IQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICG-NFKGMKIKPGSM 393
Cdd:PRK13391 251 TQLVPTMFsRMLkLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTAcDSEEWLAHPGTV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 394 GKPSPAfNVEILDENGTILPPGQEGDIAVQvlPDRPFglftHYVDNPSKTASTL--RGNFYITGDRGYMDEDGYFWFVAR 471
Cdd:PRK13391 331 GRAMFG-DLHILDDDGAELPPGEPGTIWFE--GGRPF----EYLNDPAKTAEARhpDGTWSTVGDIGYVDEDGYLYLTDR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 472 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyKLHDQEQLKKEIQEHVKKTTAPYKYP 551
Cdd:PRK13391 404 AAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVD--GVDPGPALAAELIAFCRQRLSRQKCP 481
|
490 500
....*....|....*....|....*...
gi 564330613 552 RKIEFIEELPKTVSGKVKRNELRRKEWT 579
Cdd:PRK13391 482 RSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
87-577 |
2.60e-49 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 180.92 E-value: 2.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 87 VRWSFEELgsLSR--KFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVlIPGTTQLTQKDILYRLQSSKSKC 164
Cdd:PRK07529 57 ETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 165 IIT-----DDTLAPAVDIVAAKCENLhsKLIVSQHSREGWGNLK--------------------EMMKYASDSHTCVDTK 219
Cdd:PRK07529 133 LVTlgpfpGTDIWQKVAEVLAALPEL--RTVVEVDLARYLPGPKrlavplirrkaharildfdaELARQPGDRLFSGRPI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 220 HNELMAIYF-TSGTTGPPKMIGHTHSsfglGLSVNGrfWLdlIASDVMWNTSDTGWA-------KSAWSSVFSPWTQGA- 290
Cdd:PRK07529 211 GPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WL--GALLLGLGPGDTVFCglplfhvNALLVTGLAPLARGAh 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 291 CVFA--------HYLPRFdsTSILQtlsKFPITVFCSAPTAYRMLIQ-----NDITrsykfnSLKHCVSAGEPINPEVME 357
Cdd:PRK07529 283 VVLAtpqgyrgpGVIANF--WKIVE---RYRINFLSGVPTVYAALLQvpvdgHDIS------SLRYALCGAAPLPVEVFR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 358 QWKKKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFNVEI--LDENGTIL---PPGQEGDIAVQvlpdRPfG 431
Cdd:PRK07529 352 RFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVviLDDAGRYLrdcAVDEVGVLCIA----GP-N 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 432 LFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 511
Cdd:PRK07529 427 VFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHA 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330613 512 GEVVKAFIVLNPDYKLhDQEQLKKEIQEHVKKTTApykYPRKIEFIEELPKTVSGKVKRNELRRKE 577
Cdd:PRK07529 507 GELPVAYVQLKPGASA-TEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
53-577 |
3.86e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 179.19 E-value: 3.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 53 NFAKDV----------LDQWTNT----EKTGKRLSN-PAFWWVdgnGKEVRWSfeELGSLSRKFANILTEACSLQRGDRV 117
Cdd:PRK05677 4 NFWKDKypagiaaeinPDEYPNIqavlKQSCQRFADkPAFSNL---GKTLTYG--ELYKLSGAFAAWLQQHTDLKPGDRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 118 MVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLA-------PAVDI---VAAKCENLHS 187
Cdd:PRK05677 79 AVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAhlaekvlPKTGVkhvIVTEVADMLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 188 ---------------KLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSsfglglsv 252
Cdd:PRK05677 159 plkrllinavvkhvkKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHR-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 253 ngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSP--------WTQGaCVF-----AHYL----PRfDSTSILQTLSKFPIT 315
Cdd:PRK05677 231 ------NLVANMLQCRALMGSNLNEGCEILIAPlplyhiyaFTFH-CMAmmligNHNIlisnPR-DLPAMVKELGKWKFS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 316 VFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMG 394
Cdd:PRK05677 303 GFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQ-AIQVGTIG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 395 KPSPAFNVEILDENGTILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVA 470
Cdd:PRK05677 382 IPVPSTLCKVIDDDGNELPLGEVGELCVkgpQVMKG--------YWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 471 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKkeiqEHVKKTTAPYKY 550
Cdd:PRK05677 454 RKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETL-TKEQVM----EHMRANLTGYKV 528
|
570 580
....*....|....*....|....*..
gi 564330613 551 PRKIEFIEELPKTVSGKVKRNELRRKE 577
Cdd:PRK05677 529 PKAVEFRDELPTTNVGKILRRELRDEE 555
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-574 |
5.00e-49 |
|
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: 173.62 E-value: 5.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHTHSSFglglsVNGRFwldlIASDVMWNTSDT------------GWAKSAWSSVfspwTQGA-CV 292
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI-----VNNGY----FIGERLGLTEQDrlcipvplfhcfGSVLGVLACL----THGAtMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 293 FAHylPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL-DIYEGY 371
Cdd:cd05917 74 FPS--PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTETVLICgnFKGMKIKP-----GSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 445
Cdd:cd05917 152 GMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCI-----RGYSVMKGYWNDPEKTAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 446 TLRG-NFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 524
Cdd:cd05917 225 AIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 564330613 525 YKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd05917 305 AELTEE-----DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-574 |
1.34e-48 |
|
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: 176.67 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 81 DGNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILpkipeW--------WLAnVAClrTGTVLIPGTTQLTQKD 152
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLA-----WnthrhlelYYA-VPG--MGAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 153 ILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSR------EGWGNLKEMMKYASDSHTCVDTKHNELMAI 226
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 227 YFTSGTTGPPKMIGHTHSSFGLG-LSVNGRFWLDLIASDV------MWNTSdtgwaksAWSSVFSPWTQGACvfaHYLP- 298
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHVN-------AWGLPYAAAMVGAK---LVLPg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 299 -RFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTET- 376
Cdd:cd12119 239 pYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETs 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 377 -VLICGnfkgmKIKPG--------------SMGKPSPAFNVEILDENGTILP--PGQEGDIAVQvlpdRPFgLFTHYVDN 439
Cdd:cd12119 318 pLGTVA-----RPPSEhsnlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVR----GPW-VTKSYYKN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 440 PSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 519
Cdd:cd12119 388 DEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVV 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 564330613 520 VLNPdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd12119 468 VLKE-----GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
90-574 |
2.36e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 175.97 E-value: 2.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITdd 169
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 tlAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTcvDTKHNELMaiYFTSGTTGPPKMI-----GHTHS 244
Cdd:PRK13390 103 --SAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLT--EQPCGAVM--LYSSGTTGFPKGIqpdlpGRDVD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 245 SFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKS-AWSSVFSPwTQGACVFAHylpRFDSTSILQTLSKFPITVFCSAPTA 323
Cdd:PRK13390 177 APGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQATLGHVERYRITVTQMVPTM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 324 Y-RMLIQNDITRS-YKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE----TVLICGNFKGmkiKPGSMGKpS 397
Cdd:PRK13390 253 FvRLLKLDADVRTrYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA---HPGSVGR-S 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 398 PAFNVEILDENGTILPPGQEGDIAVQvlPDR-PFglftHYVDNPSKTASTLRGN--FYIT-GDRGYMDEDGYFWFVARSD 473
Cdd:PRK13390 329 VLGDLHICDDDGNELPAGRIGTVYFE--RDRlPF----RYLNDPEKTAAAQHPAhpFWTTvGDLGSVDEDGYLYLADRKS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 474 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykLHDQEQLKKEIQEHVKKTTAPYKYPRK 553
Cdd:PRK13390 403 FMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEG--IRGSDELARELIDYTRSRIAHYKAPRS 480
|
490 500
....*....|....*....|.
gi 564330613 554 IEFIEELPKTVSGKVKRNELR 574
Cdd:PRK13390 481 VEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
226-576 |
2.73e-48 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 176.49 E-value: 2.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKmiGHTHSSFGlGLSVngrfwldliASDVMwntSDTGWAKSAWSSVFSP----WTQGACVFAHYLP--- 298
Cdd:PRK13382 201 ILLTSGTTGTPK--GARRSGPG-GIGT---------LKAIL---DRTPWRAEEPTVIVAPmfhaWGFSQLVLAASLActi 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 299 ----RFDSTSILQTLSKFPITVFCSAPTAYR--MLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG 372
Cdd:PRK13382 266 vtrrRFDPEATLDLIDRHRATGLAVVPVMFDriMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYN 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 373 QTETVLIC-GNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVdnPSKTASTLRGnF 451
Cdd:PRK13382 346 ATEAGMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFV-----RNDTQFDGYT--SGSTKDFHDG-F 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 452 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqe 531
Cdd:PRK13382 418 MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASA---- 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 564330613 532 qLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 576
Cdd:PRK13382 494 -TPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
88-578 |
7.52e-48 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 175.32 E-value: 7.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 168 D-------------------DTLAPAVDIVAAKCEnlHSKLIVSQhsregwgnlkEMMKYASDSHTCvDTKHNELMAIYF 228
Cdd:PRK06087 128 PtlfkqtrpvdlilplqnqlPQLQQIVGVDKLAPA--TSSLSLSQ----------IIADYEPLTTAI-TTHGDELAAVLF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 229 TSGTTGPPKMIGHTHSSFGLG-LSVNGRfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahYLPRFDSTSILQ 307
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDACLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 308 TLSKFPITVFCSA-PTAYRML--IQNDitrSYKFNSLKHCVSAGEPInPEVMEQWKKKTGLDIYEGYGQTETV--LICGN 382
Cdd:PRK06087 271 LLEQQRCTCMLGAtPFIYDLLnlLEKQ---PADLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSphAVVNL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 383 FKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAvqvlpDRPFGLFTHYVDNPSKTASTL--RGNFYiTGDRGYM 460
Cdd:PRK06087 347 DDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEA-----SRGPNVFMGYLDEPELTARALdeEGWYY-SGDLCRM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 461 DEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEqlkkEIQEH 540
Cdd:PRK06087 421 DEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLE----EVVAF 496
|
490 500 510
....*....|....*....|....*....|....*....
gi 564330613 541 V-KKTTAPYKYPRKIEFIEELPKTVSGKVKRNELrRKEW 578
Cdd:PRK06087 497 FsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL-RKDI 534
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-574 |
3.69e-47 |
|
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: 171.47 E-value: 3.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 111 LQRGDRVMVILPKIPE--WWLANV--ACLRTGTVLIPGTTQLTQKDILYrlqsskskcIITDdtLAPAVDIVAAKCENlH 186
Cdd:cd05922 15 GVRGERVVLILPNRFTyiELSFAVayAGGRLGLVFVPLNPTLKESVLRY---------LVAD--AGGRIVLADAGAAD-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 187 SKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRfwLDLIASDV 265
Cdd:cd05922 83 LRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArSIAEY--LGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 266 MWNTSDTGWAkSAWSSVFSPWTQGACVFAHYLPRFDSTsILQTLSKFPITVFCSAPTAYRMLIQNDITRSyKFNSLKHCV 345
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVLDDA-FWEDLREHGATGLAGVPSTYAMLTRLGFDPA-KLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 346 SAGEPINPEVMEQWKKK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSPAFNVEILDENGTILPPGQ 416
Cdd:cd05922 238 QAGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 417 EGDIAVQvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHP 496
Cdd:cd05922 312 PGEIVHR----GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564330613 497 SIAESAVVSSPDPIrGEVVKAFIVLNPDYKLHDqeqlkkeIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd05922 388 LIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
66-576 |
6.21e-47 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 172.47 E-value: 6.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 66 EKTGKRLSNPAFwwVDGNGKEVrWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGT 145
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGL-HKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 146 TQLTQKDILYRLQSSKSKCIITddtLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMA 225
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHTHSsfGLGLSV---------NgrfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhy 296
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN----LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 297 LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIY-EGYGQTE 375
Cdd:PLN02246 256 MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 376 --TVL-ICGNF--KGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL-R 448
Cdd:PLN02246 336 agPVLaMCLAFakEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTIdK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 449 GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLH 528
Cdd:PLN02246 411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 564330613 529 DQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 576
Cdd:PLN02246 491 ED-----EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
298-578 |
1.04e-46 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 171.42 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 298 PRFDSTSILQTLSKFPITVFCSAPTAY-RML-IQNDITRSYKFNSLKHCVSAGEPINPEV----MEQWkkktGLDIYEGY 371
Cdd:PRK12406 228 PRFDPEELLQLIERHRITHMHMVPTMFiRLLkLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEWW----GPVIYEYY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTET--VLICGNFKGMKiKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQV--LPDrpfglFThYVDNPSKTASTL 447
Cdd:PRK12406 304 GSTESgaVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIagNPD-----FT-YHNKPEKRAEID 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 448 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 527
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATL 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 564330613 528 hDQEqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 578
Cdd:PRK12406 457 -DEA----DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYW 502
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
75-573 |
1.20e-46 |
|
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: 169.74 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 75 PAFWWvdgngKEVRWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKdil 154
Cdd:cd05945 8 PAVVE-----GGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 155 yRLQSskskcIItdDTLAPAVDIVAAkcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTG 234
Cdd:cd05945 79 -RIRE-----IL--DAAKPALLIADG----------------------------------------DDNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 235 PPKMIGHTHS---SFGLGLsvNGRFwlDLIASDVMWNTSDtgwaksaWS---SVFS---PWTQGACVFAhyLPR---FDS 302
Cdd:cd05945 111 RPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGATLVP--VPRdatADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 303 TSILQTLSKFPITVFCSAPTAYRMLIqnditRSYKFN-----SLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTET 376
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCL-----LSPTFTpeslpSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 377 VLICgnfKGMKIKPGSM--------GKPSPAFNVEILDENGTILPPGQEGDIAV---QVlpdrpfglFTHYVDNPSKTAS 445
Cdd:cd05945 253 TVAV---TYIEVTPEVLdgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELVIsgpSV--------SKGYLNNPEKTAA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 446 TLRGNF----YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 521
Cdd:cd05945 322 AFFPDEgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVP 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 564330613 522 NPdyklHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd05945 402 KP----GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-575 |
1.32e-46 |
|
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: 167.27 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 220 HNELMAIYFTSGTTGPPKMIGHTHSSF---GLGLSVNGRFWLDliasDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAH 295
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEvynAWMLALNSLFDPD----DVLLCGLPLFHVNGSVVTLLTPLASGAhVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 296 YLPRFDST---SILQTLSKFPITVFCSAPTAYRMLIQNDITRSykFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG 372
Cdd:cd05944 77 PAGYRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNAD--ISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 373 QTE-TVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGT---ILP--PGQEGDIAVQvlpdRPfGLFTHYVDNPSKTAST 446
Cdd:cd05944 155 LTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrlLRDcaPDEVGEICVA----GP-GVFGGYLYTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 447 LRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYK 526
Cdd:cd05944 230 VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 564330613 527 LhDQEQLKKEIQEHVKKTTApykYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:cd05944 310 V-EEEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
76-575 |
3.42e-46 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 172.77 E-value: 3.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 76 AFWWvDGN--GKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDI 153
Cdd:PLN02654 107 AIYW-EGNepGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 154 LYRLQSSKSKCIITDDTLAPAV------DIV-AAKCENLHSKLIV---------SQHSREG--WGNLKEMM------KYA 209
Cdd:PLN02654 185 AQRIVDCKPKVVITCNAVKRGPktinlkDIVdAALDESAKNGVSVgicltyenqLAMKREDtkWQEGRDVWwqdvvpNYP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 210 SDSHTCVDTKHNELMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG 289
Cdd:PLN02654 265 TKCEVEWVDAEDPLFLLY-TSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 290 ACVFA-HYLPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQND---ITRsYKFNSLKHCVSAGEPINPEVMEQWKKKTG 364
Cdd:PLN02654 344 ATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTR-HSRKSLRVLGSVGEPINPSAWRWFFNVVG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 365 ---LDIYEGYGQTETvlicGNFKGMKI------KPGSmgKPSPAFNVE--ILDENGTILPPGQEGDIAVQvlPDRPFGLF 433
Cdd:PLN02654 423 dsrCPISDTWWQTET----GGFMITPLpgawpqKPGS--ATFPFFGVQpvIVDEKGKEIEGECSGYLCVK--KSWPGAFR 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 434 THYVDNPSKTASTLR--GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 511
Cdd:PLN02654 495 TLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVK 574
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564330613 512 GEVVKAFIVLNPDYKLhdQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:PLN02654 575 GQGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
86-574 |
6.35e-46 |
|
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: 169.63 E-value: 6.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAKceNLHSKLIVSQHSREGWGNLKEMMKYASdSHTCVD-----------TKHNELMAIYFTSGTTG 234
Cdd:cd17642 121 FCSKKGLQKVLNVQKK--LKIIKTIIILDSKEDYKGYQCLYTFIT-QNLPPGfneydfkppsfDRDEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 235 PPKMIGHTHSSFGLGLSVngrfwldliASDVMWntsdtGWAKSAWSSVFS--PWTQG---------ACVFAH--YLPRFD 301
Cdd:cd17642 198 LPKGVQLTHKNIVARFSH---------ARDPIF-----GNQIIPDTAILTviPFHHGfgmfttlgyLICGFRvvLMYKFE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 302 STSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGYGQTET---V 377
Cdd:cd17642 264 EELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETtsaI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 378 LICGNfkgMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI-TG 455
Cdd:cd17642 344 LITPE---GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCV-----KGPMIMKGYVNNPEATKALIDKDGWLhSG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 456 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyklHDQEQLKK 535
Cdd:cd17642 416 DIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE-----AGKTMTEK 490
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 564330613 536 EIQEHVKKTTAPYKYPR-KIEFIEELPKTVSGKVKRNELR 574
Cdd:cd17642 491 EVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
90-577 |
6.38e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 170.11 E-value: 6.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMViLPKIPEWW-LANVACLRTGTVLI-----PGTTQLtqKDILYRLqssKSK 163
Cdd:PRK07788 76 TYAELDEQSNALARGLLAL-GVRAGDGVAV-LARNHRGFvLALYAAGKVGARIIllntgFSGPQL--AEVAARE---GVK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 164 CIITDDTLAPAVDIVAAKCENLHSkLIVS----QHSREGWGNLKEMMKYASDSHTCVDTKHNELmaIYFTSGTTGPPKMI 239
Cdd:PRK07788 149 ALVYDDEFTDLLSALPPDLGRLRA-WGGNpdddEPSGSTDETLDDLIAGSSTAPLPKPPKPGGI--VILTSGTTGTPKGA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 240 GHTHSSfglGLSVNGRFwLDLI---ASDVMWNTS----DTGWAKSAWSsvfspWTQGACVFAHYlpRFDSTSILQTLSKF 312
Cdd:PRK07788 226 PRPEPS---PLAPLAGL-LSRVpfrAGETTLLPApmfhATGWAHLTLA-----MALGSTVVLRR--RFDPEATLEDIAKH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 313 PITVFCSAPTAY-RMLIQNDITRS-YKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE----TVlicGNFKGM 386
Cdd:PRK07788 295 KATALVVVPVMLsRILDLGPEVLAkYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvafaTI---ATPEDL 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 387 KIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKtaSTLRGnFYITGDRGYMDEDGYf 466
Cdd:PRK07788 372 AEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV-----GNGFPFEGYTDGRDK--QIIDG-LLSSGDVGYFDEDGL- 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 467 WFVA-RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqeqlKKEIQEHVKKTT 545
Cdd:PRK07788 443 LFVDgRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALD-----EDAIKDYVRDNL 517
|
490 500 510
....*....|....*....|....*....|..
gi 564330613 546 APYKYPRKIEFIEELPKTVSGKVKRNELRRKE 577
Cdd:PRK07788 518 ARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
225-574 |
5.10e-45 |
|
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: 166.01 E-value: 5.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 225 AIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIasdvmwntsdtGWakSAWSSVFSPWT------QGACVFAHYL- 297
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLP-GGPPDNDTLMAAALGF-----------GP--GADSVYLSPAPlyhaapFRWSMTALFMg 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 298 ------PRFDSTSILQTLSKFPITVFCSAPTAY-RMLIQNDITR-SYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYE 369
Cdd:cd05929 195 gtlvlmEKFDPEEFLRLIERYRVTFAQFVPTMFvRLLKLPEAVRnAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 370 GYGQTETV-LICGNFKGMKIKPGSMGKPSPAfNVEILDENGTILPPGQEGDiaVQVLPDRPFglftHYVDNPSKTA-STL 447
Cdd:cd05929 275 YYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGE--VYFANGPGF----EYTNDPEKTAaARN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 448 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAfiVLNPDYKL 527
Cdd:cd05929 348 EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGA 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 564330613 528 HDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd05929 426 DAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
81-575 |
5.95e-45 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 167.15 E-value: 5.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 81 DGNGKEVRWSFEELGSLSRKFANILTEaCSLQRGDrvmVILPKIPEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRL 157
Cdd:PRK13295 48 LGTGAPRRFTYRELAALVDRVAVGLAR-LGVGRGD---VVSCQLPNWWEFTVlylACSRIGAVLNPLMPIFRERELSFML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 158 QSSKSKCIItddtlAPAV----DIvAAKCENLHSKLIVSQH----SREGWGNLKEMM-----KYASDSHTCVDTKH---N 221
Cdd:PRK13295 124 KHAESKVLV-----VPKTfrgfDH-AAMARRLRPELPALRHvvvvGGDGADSFEALLitpawEQEPDAPAILARLRpgpD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 222 ELMAIYFTSGTTGPPKMIGHTHSS-FGLGLSVNGRfwLDLIASDVMWNTS----DTGWAKSAwssvFSPWTQGACVFahY 296
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTlMANIVPYAER--LGLGADDVILMASpmahQTGFMYGL----MMPVMLGATAV--L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 297 LPRFDSTSILQTLSKFPITvFCSAPTAYRMliqnDITRSYK-----FNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGY 371
Cdd:PRK13295 270 QDIWDPARAAELIRTEGVT-FTMASTPFLT----DLTRAVKesgrpVSSLRTFLCAGAPIPGALVERARAALGAKIVSAW 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTETVLICGnfkgmkIKPG--------SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKT 443
Cdd:PRK13295 345 GMTENGAVTL------TKLDdpderastTDGCPLPGVEVRVVDADGAPLPAGQIGRLQV-----RGCSNFGGYLKRPQLN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 444 ASTLRGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 523
Cdd:PRK13295 414 GTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRP 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 564330613 524 DYKLhDQEQLKKEIQEHvkKTTAPYkYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:PRK13295 493 GQSL-DFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
90-574 |
7.01e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 163.13 E-value: 7.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK06145 29 SYAEFHQRILQAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPAVDIVaakcenlHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTkhnELMAIYFTSGTTGPPKMIGHTHSSF--- 246
Cdd:PRK06145 108 EFDAIVALE-------TPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPT---DLVRLMYTSGTTDRPKGVMHSYGNLhwk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 247 ------GLGLSVNGRFW----------LDLIASDVMWntsdtgwaksawssvfspwtQGACVFAHYlpRFDSTSILQTLS 310
Cdd:PRK06145 178 sidhviALGLTASERLLvvgplyhvgaFDLPGIAVLW--------------------VGGTLRIHR--EFDPEAVLAAIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 311 KFPITVFCSAPTAY-RMLIQNDITRsYKFNSLKHCVSAGEPiNPE--VMEQWKKKTGLDIYEGYGQTETvliCGNFKGMK 387
Cdd:PRK06145 236 RHRLTCAWMAPVMLsRVLTVPDRDR-FDLDSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTET---CSGDTLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 388 I-----KPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDE 462
Cdd:PRK06145 311 AgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICM-----RGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 463 DGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqeqlKKEIQEHVK 542
Cdd:PRK06145 386 EGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT-----LEALDRHCR 460
|
490 500 510
....*....|....*....|....*....|..
gi 564330613 543 KTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK06145 461 QRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
89-581 |
7.39e-44 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 164.38 E-value: 7.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 89 WSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 169 DTlapavdiVAAKCENLHSKLIV-SQHSREGWGNLKEMMKyASDShtCVDTKHNE------LMAIYFTSGTTGPPKMIGH 241
Cdd:PLN02330 135 DT-------NYGKVKGLGLPVIVlGEEKIEGAVNWKELLE-AADR--AGDTSDNEeilqtdLCALPFSSGTTGISKGVML 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 242 TH---------SSFGLGLSVNGRF-WLDLIASDVMWNTSDTGWAKSAwssvfspwTQGACVFahyLPRFDSTSILQTLSK 311
Cdd:PLN02330 205 THrnlvanlcsSLFSVGPEMIGQVvTLGLIPFFHIYGITGICCATLR--------NKGKVVV---MSRFELRTFLNALIT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 312 FPITVFCSAPTAYRMLIQNDITRSYKFNSLK--HCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTETVLICGNF----K 384
Cdd:PLN02330 274 QEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlqAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTHgdpeK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 385 GMKI-KPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMD 461
Cdd:PLN02330 354 GHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCV-----RSQCVMQGYYNNKEETDRTIDEDGWLhTGDIGYID 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 462 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhdqeQLKKEIQEHV 541
Cdd:PLN02330 429 DDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAK-----ESEEDILNFV 503
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 564330613 542 KKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTTT 581
Cdd:PLN02330 504 AANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-503 |
1.88e-43 |
|
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: 160.12 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKS 162
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 163 KCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSRegwgnlkemmkyASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHT 242
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDA------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 243 HSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHY--LPRFDSTSILQTLSKFPITVFCSA 320
Cdd:TIGR01733 142 HRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPedEERDDAALLAALIAEHPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 321 PTAYRMLIQNDITRsykFNSLKHCVSAGEPINPEVMEQWKKKTG-LDIYEGYGQTETVLICGnfkgMKIKPGSM------ 393
Cdd:TIGR01733 220 PSLLALLAAALPPA---LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWST----ATLVDPDDapresp 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 394 ---GKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTA---------STLRGNFYITGDRGYMD 461
Cdd:TIGR01733 293 vpiGRPLANTRLYVLDDDLRPVPVGVVGELYI-----GGPGVARGYLNRPELTAerfvpdpfaGGDGARLYRTGDLVRYL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 564330613 462 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV 503
Cdd:TIGR01733 368 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
226-575 |
7.91e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 154.38 E-value: 7.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKmighthssfGLGLSVNGrfwldlIASDVmwntsdTGWAKsAWSsvfspWTqGACVFAHYLP------- 298
Cdd:PRK07787 133 IVYTSGTTGPPK---------GVVLSRRA------IAADL------DALAE-AWQ-----WT-ADDVLVHGLPlfhvhgl 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 299 ------------------RFDSTSILQTLSkFPITVFCSAPTAY-RmlIQNDITRSYKFNSLKHCVSAGEPINPEVMEQW 359
Cdd:PRK07787 185 vlgvlgplrignrfvhtgRPTPEAYAQALS-EGGTLYFGVPTVWsR--IAADPEAARALRGARLLVSGSAALPVPVFDRL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 360 KKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVlpdRPFGLFTHYVDN 439
Cdd:PRK07787 262 AALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV---RGPTLFDGYLNR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 440 PSKTASTLRGN-FYITGDRGYMDEDGYFWFVAR-SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKA 517
Cdd:PRK07787 339 PDATAAAFTADgWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 564330613 518 FIVLNPDYKLhdqeqlkKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:PRK07787 419 YVVGADDVAA-------DELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
64-576 |
1.01e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 156.03 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 64 NTEKTGKRlsnPAFWWVDgNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP 143
Cdd:COG1022 20 RAARFPDR---VALREKE-DGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 144 GTTQLTQKDILYRLQSSKSKCIIT-DDTLAPAVDIVAAKCENLhsKLIVSQHSREGWG-----NLKEMMKYASDSHT--- 214
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDdprllSLDELLALGREVADpae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 215 ----CVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWaksawsSVFS 284
Cdd:COG1022 173 learRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsflpLAHVFERTV------SYYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 285 pWTQGACVfaHYLPRFDStsILQTLSKFPITVFCSAP------------------------------TAYRMLIQNDITR 334
Cdd:COG1022 246 -LAAGATV--AFAESPDT--LAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrklfrwalaVGRRYARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 335 S--------YKF--------------NSLKHCVSAGEPINPEV------MeqwkkktGLDIYEGYGQTET-VLICGNFKG 385
Cdd:COG1022 321 SpslllrlkHALadklvfsklrealgGRLRFAVSGGAALGPELarffraL-------GIPVLEGYGLTETsPVITVNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 386 mKIKPGSMGKPSPafNVEI-LDENGTIL---PpgqegdiavqvlpdrpfGLFTHYVDNPSKTASTLR--GNFYiTGDRGY 459
Cdd:COG1022 394 -DNRIGTVGPPLP--GVEVkIAEDGEILvrgP-----------------NVMKGYYKNPEATAEAFDadGWLH-TGDIGE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 460 MDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVVsspdpirGE----VVkAFIVLNPDY--------- 525
Cdd:COG1022 453 LDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEAlgewaeeng 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564330613 526 -------KLHDQEQLKKEIQEHVKKTT---APYKYPRKIEFI--------EELpkTVSGKVKRNELRRK 576
Cdd:COG1022 525 lpytsyaELAQDPEVRALIQEEVDRANaglSRAEQIKRFRLLpkeftienGEL--TPTLKLKRKVILEK 591
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
86-576 |
3.76e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 153.56 E-value: 3.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYAS-----DSHTCVDTKHNELMAIY--FTSGTTGPPKM 238
Cdd:PRK08162 120 IVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAflasgDPDFAWTLPADEWDAIAlnYTSGTTGNPKG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 239 IGHTHSSFGLGLSVNGRFWlDLIASDV-MW-------NtsdtGWAksawssvFsPWT----QGACVFahyLPRFDSTSIL 306
Cdd:PRK08162 200 VVYHHRGAYLNALSNILAW-GMPKHPVyLWtlpmfhcN----GWC-------F-PWTvaarAGTNVC---LRKVDPKLIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 307 QTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQwKKKTGLDIYEGYGQTET---VLICGNF 383
Cdd:PRK08162 264 DLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAK-MEEIGFDLTHVYGLTETygpATVCAWQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 384 KGMKIKP--------GSMGKPSPAFN-VEILD-ENGTILPPGQE--GDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNF 451
Cdd:PRK08162 343 PEWDALPlderaqlkARQGVRYPLQEgVTVLDpDTMQPVPADGEtiGEIMF-----RGNIVMKGYLKNPKATEEAFAGGW 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 452 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQE 531
Cdd:PRK08162 418 FHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKD-----GAS 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 564330613 532 QLKKEIQEHVKKTTAPYKYPRKIEFiEELPKTVSGKVKRNELRRK 576
Cdd:PRK08162 493 ATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
66-574 |
3.95e-39 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 151.13 E-value: 3.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 66 EKTGKRLSN-PAFwwvdgNGKEVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PRK12492 31 ERSCKKFADrPAF-----SNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 145 TTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLH---SKLIVSQHSREGW------GNLKEMMKY------- 208
Cdd:PRK12492 106 NPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvntvvDKVKKMVPAyhlpqav 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 209 ---------ASDSHTCVDTKHNELMAIYFTSGTTGPPK--MIGH---------THSSFGLGLSVNGRFWLDliASDVMWn 268
Cdd:PRK12492 186 pfkqalrqgRGLSLKPVPVGLDDIAVLQYTGGTTGLAKgaMLTHgnlvanmlqVRACLSQLGPDGQPLMKE--GQEVMI- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 269 tsdtgwAKSAWSSVFSPWTQGACVFA---HYL----PRfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSL 341
Cdd:PRK12492 263 ------APLPLYHIYAFTANCMCMMVsgnHNVlitnPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSAL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 342 KHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDI 420
Cdd:PRK12492 336 KLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGEL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 421 AV---QVLPDrpfglfthYVDNPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHP 496
Cdd:PRK12492 416 CIkgpQVMKG--------YWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHP 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564330613 497 SIAESAVVSSPDPIRGEVVKAFIVlnPDYKLHDQEQLKKeiqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK12492 488 KVANCAAIGVPDERSGEAVKLFVV--ARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
215-575 |
6.66e-39 |
|
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: 149.02 E-value: 6.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 215 CVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF 293
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 294 AHYLPrFDSTSILQTLSKFPITVFCSAPTAYRMLIQNdiTRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQ 373
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 374 TETV-LICGNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNF 451
Cdd:cd05909 296 TECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLV-----RGPNVMLGYLNEPELTSFAFGDGW 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 452 YITGDRGYMDEDGYFWFVARsddviLSSGYRIG----PFE-VESALIEH-PSIAESAVVSSPDPIRGEVVKAFivlnpdY 525
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL------T 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 564330613 526 KLHDQEQLkkEIQEHVKKTTAPYKY-PRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:cd05909 440 TTTDTDPS--SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
225-570 |
7.51e-39 |
|
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: 145.48 E-value: 7.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 225 AIYFTSGTTGPPKMIGHTHSSFGLGLSVngrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYL-----PR 299
Cdd:cd17635 5 AVIFTSGTTGEPKAVLLANKTFFAVPDI-------LQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLcvtggEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 300 FDSTSILQTLSKFPITVFCSAPTAYrmliqNDITRSYKfNSLKHC-------VSAGEPINPEV-MEQWKKKTglDIYEGY 371
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLL-----SKLVSELK-SANATVpslrligYGGSRAIAADVrFIEATGLT--NTAQVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTET-VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVlPDRPFGlfthYVDNPSKTASTLRGN 450
Cdd:cd17635 150 GLSETgTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS-PANMLG----YWNNPERTAEVLIDG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 451 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyklhDQ 530
Cdd:cd17635 225 WVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE----LD 300
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 564330613 531 EQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 570
Cdd:cd17635 301 ENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
226-570 |
1.68e-38 |
|
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: 144.57 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPK--MIGHTHSsfgLGLSVNgrfWldliaSDVMWNTSDTGWA-----------KSAWSSVFspwTQGACV 292
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LTGATV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 293 FAHYLprFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGY 371
Cdd:cd17638 71 VPVAV--FDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTE--TVLICGNFKGMKIKPGSMGKPSPAFNVEILDEngtilppgqeGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRG 449
Cdd:cd17638 149 GLTEagVATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLV-----RGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 450 NFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLh 528
Cdd:cd17638 214 DGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTL- 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 564330613 529 DQEQLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKR 570
Cdd:cd17638 293 TEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
87-574 |
2.52e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 148.81 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 87 VRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCII 166
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 167 TDD------------TLAP------AVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHtcvDTKHNELMA--- 225
Cdd:PRK08315 121 AADgfkdsdyvamlyELAPelatcePGQLQSARLPELRRVIFLGDEKHPGMLNFDELLALGRAVD---DAELAARQAtld 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 ------IYFTSGTTGPPKmiGHTHSSFGLGLsvNGRF---WLDLIASD--------------VMWNTSDTgwaksawssv 282
Cdd:PRK08315 198 pddpinIQYTSGTTGFPK--GATLTHRNILN--NGYFigeAMKLTEEDrlcipvplyhcfgmVLGNLACV---------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 283 fspwTQGAC-VFAhyLPRFDSTSILQTLSKFPITVFCSAPTayrMLI--QNDITR-SYKFNSLKHCVSAGEPINPEVMEQ 358
Cdd:PRK08315 264 ----THGATmVYP--GEGFDPLATLAAVEEERCTALYGVPT---MFIaeLDHPDFaRFDLSSLRTGIMAGSPCPIEVMKR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 359 WKKKTGL-DIYEGYGQTETvlicgnfkgmkiKPGSM---------------GKPSPAFNVEILD-ENGTILPPGQEGDIA 421
Cdd:PRK08315 335 VIDKMHMsEVTIAYGMTET------------SPVSTqtrtddplekrvttvGRALPHLEVKIVDpETGETVPRGEQGELC 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 422 VqvlpdRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:PRK08315 403 T-----RGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564330613 501 SAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK08315 478 VQVVGVPDEKYGEEVCAWIILRPGATLTEE-----DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
80-573 |
4.44e-38 |
|
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: 146.70 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 80 VDGNGkevRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd05920 35 VDGDR---RLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 160 SKSKCIITDDTLAPaVDIVAAKCENLHSklivsqhsregwgnlkemmkyasdshtcvdtkHNELMAIYFTSGTTGPPKMI 239
Cdd:cd05920 111 AEAVAYIVPDRHAG-FDHRALARELAES--------------------------------IPEVALFLLSGGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 240 GHTHSSFGLGLSVngrfwldliASDVMWNTSDT----------GWAKSAWSSVFSPWTQGACVFAhylPRFDSTSILQTL 309
Cdd:cd05920 158 PRTHNDYAYNVRA---------SAEVCGLDQDTvylavlpaahNFPLACPGVLGTLLAGGRVVLA---PDPSPDAAFPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 310 SKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLicgNFKGM--- 386
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL---NYTRLddp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 387 -KIKPGSMGKP-SPAFNVEILDENGTILPPGQEGDIAVQvlpdrpfGLFT--HYVDNPSKTASTLRGN-FYITGDRGYMD 461
Cdd:cd05920 303 dEVIIHTQGRPmSPDDEIRVVDEEGNPVPPGEEGELLTR-------GPYTirGYYRAPEHNARAFTPDgFYRTGDLVRRT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 462 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEhv 541
Cdd:cd05920 376 PDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPP--SAAQLRRFLRE-- 451
|
490 500 510
....*....|....*....|....*....|..
gi 564330613 542 kKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd05920 452 -RGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
289-568 |
9.20e-38 |
|
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: 142.44 E-value: 9.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 289 GACVFahyLPRFDSTSILQTLSKFPIT-VFCSAPTAYRMLIQNDiTRSYKFNSLKHCVSAGE--PINPEVMEQWKKKTGl 365
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNA-DGLYDLSSLRSSPAAPEwnDMATVDTSPWGRKPG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 366 diyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTA 444
Cdd:cd17636 142 ----GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 445 STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 524
Cdd:cd17636 212 RRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 564330613 525 YKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 568
Cdd:cd17636 292 ASVTEA-----ELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
111-574 |
1.93e-37 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 147.49 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD----DTLAPAVDIVAAKcenlh 186
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSdalrDRFQPSRVAEAAE----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 187 sklIVSQHSREGWGNLKEMMKYASDSHTcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVM 266
Cdd:PRK06060 127 ---LMSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 267 WNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRfdSTSILQTLS-KFPITVFCSAPTAYRMLIqnDITRSYKFNSLKHCV 345
Cdd:PRK06060 191 LCSARMYFAYGLGNSVWFPLATGGSAVINSAPV--TPEAAAILSaRFGPSVLYGVPNFFARVI--DSCSPDSFRSLRCVV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 346 SAGEPINPEVMEQWKKK-TGLDIYEGYGQTEtvlICGNFKGMKI---KPGSMGKPSPAFNVEILDENGTILPPGQEGDIA 421
Cdd:PRK06060 267 SAGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLW 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 422 VqvlpdRPFGLFTHYVDNPSKTASTlrGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES 501
Cdd:PRK06060 344 V-----RGPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564330613 502 AVVSSPDPIRGEVVKAFIVlnPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK06060 417 AVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
216-570 |
5.15e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 146.04 E-value: 5.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 216 VDTKHNelMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAksAWSSVFSPWTQGACVFAH 295
Cdd:PTZ00237 251 VESSHP--LYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWV--SFHGFLYGSLSLGNTFVM 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 296 Y-----LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQND-----ITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL 365
Cdd:PTZ00237 327 FeggiiKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 366 DIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQvLPDRPFGLFTHYV-DNPSKT 443
Cdd:PTZ00237 407 KSSRGYGQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK-LPMPPSFATTFYKnDEKFKQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 444 ASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 523
Cdd:PTZ00237 486 LFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQ 565
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 564330613 524 DYKLH--DQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 570
Cdd:PTZ00237 566 DQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
80-575 |
6.16e-37 |
|
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: 144.13 E-value: 6.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 80 VDGngkEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGtvLIPGTT--QLTQKDILYRL 157
Cdd:COG1021 45 VDG---ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFAlpAHRRAEISHFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 158 QSSKSKCIITDDT-----LAPAVDIVAAKCENLHSKLIVsqHSREGWGNLKEMmkYASDSHTCVDTKHNELMAIYFTS-G 231
Cdd:COG1021 119 EQSEAVAYIIPDRhrgfdYRALARELQAEVPSLRHVLVV--GDAGEFTSLDAL--LAAPADLSEPRPDPDDVAFFQLSgG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 232 TTGPPKMIGHTH---------SSFGLGLSVNGRFwldLIASDVMWNtsdtgwakSAWSS--VFSPWTQGAC-VFAhylPR 299
Cdd:COG1021 195 TTGLPKLIPRTHddylysvraSAEICGLDADTVY---LAALPAAHN--------FPLSSpgVLGVLYAGGTvVLA---PD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 300 FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG------- 372
Cdd:COG1021 261 PSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGmaeglvn 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 373 QT------ETVLicgnfkgmkikpGSMGKP-SPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 445
Cdd:COG1021 341 YTrlddpeEVIL------------TTQGRPiSPDDEVRIVDEDGNPVPPGEVGELLT-----RGPYTIRGYYRAPEHNAR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 446 --TLRGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnp 523
Cdd:COG1021 404 afTPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-- 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 564330613 524 dyklhDQEQLK-KEIQEHVK-KTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:COG1021 481 -----RGEPLTlAELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
90-574 |
6.61e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 143.38 E-value: 6.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEACSLQRgdRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPavDIVAAKCEnlhsklIVSqhsregWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:PRK07638 106 YKLN--DLPDEEGR------VIE------IDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 250 LSVNGR-FWLD-----LIASDVMwntsdtgwaksawSSVF-----SPWTQGACVfaHYLPRFDSTSILQTLSKFPITVFC 318
Cdd:PRK07638 172 FDCNVHdFHMKredsvLIAGTLV-------------HSLFlygaiSTLYVGQTV--HLMRKFIPNQVLDKLETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 319 SAPTAYRMLIQNDITRSykfNSLKhCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTE----TVLICGNFKgmkIKPGSM 393
Cdd:PRK07638 237 TVPTMLESLYKENRVIE---NKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASElsfvTALVDEESE---RRPNSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 394 GKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdRPFgLFTHYVdNPSKTASTLRGNFYIT-GDRGYMDEDGYFWFVARS 472
Cdd:PRK07638 310 GRPFHNVQVRICNEAGEEVQKGEIGTVYVK----SPQ-FFMGYI-IGGVLARELNADGWMTvRDVGYEDEEGFIYIVGRE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 473 DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIvlnpdyklhDQEQLKKEIQEHVKKTTAPYKYPR 552
Cdd:PRK07638 384 KNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPK 454
|
490 500
....*....|....*....|..
gi 564330613 553 KIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK07638 455 EWHFVDEIPYTNSGKIARMEAK 476
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
111-573 |
1.58e-36 |
|
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: 142.65 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdILYRLQSSKSKCIITDDTLAPAVDIVAAKcenlhskli 190
Cdd:cd05923 50 LRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL---------INPRLKAAELAELIERGEMTAAVIAVDAQ--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 191 VSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMA--------IYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIA 262
Cdd:cd05923 112 VMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPrepeqpafVFYTSGTTGLPKGAVIPQRA---------------AE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 263 SDVMWNTSDTGWAKSAWSSVFS--PWTQGACVFA-----------HYLPR-FDSTSILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:cd05923 177 SRVLFMSTQAGLRHGRHNVVLGlmPLYHVIGFFAvlvaalaldgtYVVVEeFDPADALKLIEQERVTSLFATPTHLDALA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 329 QNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVlicgNFKGMK-IKPGSMGKPspAFN-----V 402
Cdd:cd05923 257 AAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM----NSLYMRdARTGTEMRP--GFFsevriV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 403 EILDENGTILPPGQEGDIAVQVLPDRPFglfTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYR 482
Cdd:cd05923 331 RIGGSPDEALANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGEN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 483 IGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhdqEQLKKEIQEHVKKTT--APYKYPRKIEFIEEL 560
Cdd:cd05923 408 IHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-------GTLSADELDQFCRASelADFKRPRRYFFLDEL 480
|
490
....*....|...
gi 564330613 561 PKTVSGKVKRNEL 573
Cdd:cd05923 481 PKNAMNKVLRRQL 493
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
88-574 |
1.59e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 142.25 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANIL-TEACSlqRGDRVMViLPKIPEWWLA-NVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLrRRGCV--DGERLAV-LARNSVWLVAlHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLApavdivAAKCENLHSKLIVSQhsregwgnlkemmkyaSDSHTCVDTKH---NELMAIYFTSGTTGPPK--MIG 240
Cdd:PRK09088 99 LGDDAVA------AGRTDVEDLAAFIAS----------------ADALEPADTPSippERVSLILFTSGTSGQPKgvMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 241 -----HTHSSFGLGLSVNGR--FWLDLiasdVMWNTsdTGWAksawSSVFSPWTQGACVFAHylPRFDSTSILQTLS--K 311
Cdd:PRK09088 157 ernlqQTAHNFGVLGRVDAHssFLCDA----PMFHI--IGLI----TSVRPVLAVGGSILVS--NGFEPKRTLGRLGdpA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 312 FPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPiNPEVMEQWKKKTGLDIYEGYGQTE--TVLicgnfkGMKI- 388
Cdd:PRK09088 225 LGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSEagTVF------GMSVd 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 389 ------KPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN-FYITGDRGYMD 461
Cdd:PRK09088 298 cdviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLL-----RGPNLSPGYWRRPQATARAFTGDgWFRTGDIARRD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 462 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEqlkkEIQEHV 541
Cdd:PRK09088 373 ADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPL-DLE----RIRSHL 447
|
490 500 510
....*....|....*....|....*....|...
gi 564330613 542 KKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK09088 448 STRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
89-573 |
2.45e-36 |
|
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: 141.19 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 89 WSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd05907 6 ITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 169 DTlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSSFgl 248
Cdd:cd05907 85 DP--------------------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 249 glsvngrfwldliasdvMWN--TSDTGWAKSA--WSSVFSP-WTQGACVFAHYLP-------RF--DSTSILQTLSKFPI 314
Cdd:cd05907 113 -----------------LSNalALAERLPATEgdRHLSFLPlAHVFERRAGLYVPllagariYFasSAETLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 315 TVFCSAPTAYRMLIQND-----------ITRSYKFNSLKHCVSAGEPINPEVMEQWKKkTGLDIYEGYGQTETV-LICGN 382
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIkvkavpglkrkLFDLAVGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSaVVTLN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 383 FKGmKIKPGSMGKPSPAFNVEIldengtilppGQEGDIAVqvlpdRPFGLFTHYVDNPSKTA-STLRGNFYITGDRGYMD 461
Cdd:cd05907 255 PPG-DNRIGTVGKPLPGVEVRI----------ADDGEILV-----RGPNVMLGYYKNPEATAeALDADGWLHTGDLGEID 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 462 EDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPirgeVVKAFIVLNPDY--------------- 525
Cdd:cd05907 319 EDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEAleawaeehgiaytdv 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 564330613 526 -KLHDQEQLKKEIQEHVK---KTTAPYKYPRKIEFIEElPKTV-------SGKVKRNEL 573
Cdd:cd05907 395 aELAANPAVRAEIEAAVEaanARLSRYEQIKKFLLLPE-PFTIengeltpTLKLKRPVI 452
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
226-570 |
6.81e-36 |
|
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: 136.77 E-value: 6.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHTHSSfglglsvngrfWldlIASDVMwntSDTGWAKSAWSSVFSPWTQG------ACVFAHYLPR 299
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERS-----------W---IESFVC---NEDLFNISGEDAILAPGPLShslflyGAISALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 300 -------FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSykfnSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGY 371
Cdd:cd17633 68 tfigqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPES----KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGtilppGQEGDIAVQvlpdRPFgLFTHYVDNPSKTAstlrGNF 451
Cdd:cd17633 144 GTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVK----SEM-VFSGYVRGGFSNP----DGW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 452 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyklhdqE 531
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--------K 281
|
330 340 350
....*....|....*....|....*....|....*....
gi 564330613 532 QLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 570
Cdd:cd17633 282 LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
86-574 |
7.30e-36 |
|
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: 140.56 E-value: 7.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAkcenlhsklIVSQHSREGWGNLkemmkyASDSHTCVDTKHNELMAIYfTSGTTGPPKmighthss 245
Cdd:cd17651 97 LTHPALAGELAVELV---------AVTLLDQPGAAAG------ADAEPDPALDADDLAYVIY-TSGSTGRPK-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 fglGLSVNGRFWLDLIAsdvmWNT----SDTGWAKSAWSS---------VFSPWTQGACVfaHYLP---RFDSTSILQTL 309
Cdd:cd17651 153 ---GVVMPHRSLANLVA----WQArassLGPGARTLQFAGlgfdvsvqeIFSTLCAGATL--VLPPeevRTDPPALAAWL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 310 SKFPITVfCSAPTAYRMLIQNDITRSYKFN-SLKHCVSAGEP--INPEVMEQWKKKTGLDIYEGYGQTE----TVLICGN 382
Cdd:cd17651 224 DEQRISR-VFLPTVALRALAEHGRPLGVRLaALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTEthvvTALSLPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 383 FKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTL-------RGNFYITG 455
Cdd:cd17651 303 DPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIG-----GAGLARGYLNRPELTAERFvpdpfvpGARMYRTG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 456 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKK 535
Cdd:cd17651 378 DLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPV-DAAELRA 456
|
490 500 510
....*....|....*....|....*....|....*....
gi 564330613 536 EIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd17651 457 ALATHL----PEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
219-575 |
1.16e-35 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 141.13 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 219 KHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWldliASDVMWNTSDTGWAksAWSSVFSPWtqGACVFAHYL- 297
Cdd:PLN02574 196 KQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFE----ASQYEYPGSDNVYL--AALPMFHIY--GLSLFVVGLl 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 298 ---------PRFDSTSILQTLSKFPITVFCSAPTayrmlIQNDITRSYK------FNSLKHCVSAGEPINPEVMEQWKKK 362
Cdd:PLN02574 268 slgstivvmRRFDASDMVKVIDRFKVTHFPVVPP-----ILMALTKKAKgvcgevLKSLKQVSCGAAPLSGKFIQDFVQT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 363 -TGLDIYEGYGQTETVLICG---NFKGMKiKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVQvlpdRPfGLFTHYV 437
Cdd:PLN02574 343 lPHVDFIQGYGMTESTAVGTrgfNTEKLS-KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ----GP-GVMKGYL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 438 DNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 516
Cdd:PLN02574 417 NNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPV 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 564330613 517 AFIVLNPDYKLhDQEQlkkeIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:PLN02574 497 AFVVRRQGSTL-SQEA----VINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
211-574 |
2.65e-35 |
|
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: 138.27 E-value: 2.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 211 DS-HTCVDTKHNELMA-IYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFwLDLIASDVMWNTSDTGWaKSAWSSVFSPWTQ 288
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 289 GACVFAHYLPRFDSTSILQTL-SKFPITVFcSAPTAY-RMLIQN-DITRSYKFNSLKHCVSAGEPINPEVMEQWKKkTGL 365
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVL-DLPPAYlQQLAEEaDRTGDGRPPSLRLYIFGGEALSPELLRRWLK-APV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 366 DIYEGYGQTETVLICGNFK---GMKIKPGSM--GKPSPAFNVEILDENGTILPPGQEGD--IAVQvlpdrpfGLFTHYVD 438
Cdd:cd17649 238 RLFNAYGPTEATVTPLVWKceaGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGE-------GLARGYLG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 439 NPSKTASTL--------RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPI 510
Cdd:cd17649 311 RPELTAERFvpdpfgapGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564330613 511 RGEVVkAFIVLNPDYKlhdQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:cd17649 391 GKQLV-AYVVLRAAAA---QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
84-570 |
5.17e-35 |
|
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: 137.57 E-value: 5.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 84 GKEVRWSFEELGSLSRKFANiLTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFAL-LLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 164 CIITddtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:cd05914 82 AIFV--------------------------------------------------SDEDDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 244 SSfgLGLSVNGRFWLDLI-ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFdSTSILQTLSKFPITVFCSAPT 322
Cdd:cd05914 112 RN--IVSNVDGVKEVVLLgKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKI-PSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 323 A------YRMLIQNDITRS---YKFNS----------------------LKHCVSAGEPINPEVmEQWKKKTGLDIYEGY 371
Cdd:cd05914 187 PlviekiFKMDIIPKLTLKkfkFKLAKkinnrkirklafkkvheafggnIKEFVIGGAKINPDV-EEFLRTIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 372 GQTETV-LICGNFKGmKIKPGSMGKPSPAFNVEILDENgtilPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS--TLR 448
Cdd:cd05914 266 GMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIV-----RGPNVMKGYYKNPEATAEafDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 449 GNFYiTGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVVsspdpIRGEVVKAFIVLNPDY-- 525
Cdd:cd05914 336 GWFH-TGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFld 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 564330613 526 -----KLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFI-EELPKTVSGKVKR 570
Cdd:cd05914 410 vkalkQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
90-573 |
8.52e-35 |
|
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: 137.46 E-value: 8.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:cd17655 24 TYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPAVDIvAAKCENLHSKLIVSQHSRegwgNLKemmkyasdshtcVDTKHNELMAIYFTSGTTGPPK--MIGHtHSSFG 247
Cdd:cd17655 103 HLQPPIAF-IGLIDLLDEDTIYHEESE----NLE------------PVSKSDDLAYVIYTSGSTGKPKgvMIEH-RGVVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 248 LGLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FDSTSILQTLSKFPITVFCSAPTAY 324
Cdd:cd17655 165 LVEWANKVIYQG--EHLRVALFASISFDASVTE-IFASLLSGNTL--YIVRKetvLDGQALTQYIRQNRITIIDLTPAHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 325 RMLIQNDITrsyKFNSLKHCVSAGEPINPEVMEQWKKKTGL--DIYEGYGQTETVLIC--GNFKGMKIKPGS--MGKPSP 398
Cdd:cd17655 240 KLLDAADDS---EGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVDAsiYQYEPETDQQVSvpIGKPLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 399 AFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVAR 471
Cdd:cd17655 317 NTRIYILDQYGRPQPVGVAGELYIG-----GEGVARGYLNRPELTAEKFVDDpfvpgerMYRTGDLARWLPDGNIEFLGR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 472 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqlkKEIQEHVKKTTAPYKYP 551
Cdd:cd17655 392 IDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPV-------AQLREFLARELPDYMIP 464
|
490 500
....*....|....*....|..
gi 564330613 552 RKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17655 465 SYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
87-576 |
2.38e-34 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 137.28 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 87 VRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCII 166
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 167 TDD---TLAP-AVDIVAAKCENLHSK--LIVSQHSREGWGNLKEMM-KYASDSHTCVDTKHNEL-----------MAIYF 228
Cdd:PLN02479 123 VDQeffTLAEeALKILAEKKKSSFKPplLIVIGDPTCDPKSLQYALgKGAIEYEKFLETGDPEFawkppadewqsIALGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 229 TSGTTGPPK-MIGHTHSSFGLGLSvNGRFWLDLIASDVMWNTSD---TGWAksawssvfSPWTQGA-CVFAHYLPRFDST 303
Cdd:PLN02479 203 TSGTTASPKgVVLHHRGAYLMALS-NALIWGMNEGAVYLWTLPMfhcNGWC--------FTWTLAAlCGTNICLRQVTAK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 304 SILQTLSKFPITVFCSAPTAYRMLIqnDITRSYKFNSLKHCV---SAGEPINPEVMEQWKKKtGLDIYEGYGQTETV--- 377
Cdd:PLN02479 274 AIYSAIANYGVTHFCAAPVVLNTIV--NAPKSETILPLPRVVhvmTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETYgps 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 378 LICG----------------------NFKGMK----IKPGSMgKPSPAfnveildeNGTILppgqeGDIAVqvlpdRPFG 431
Cdd:PLN02479 351 TVCAwkpewdslppeeqarlnarqgvRYIGLEgldvVDTKTM-KPVPA--------DGKTM-----GEIVM-----RGNM 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 432 LFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 511
Cdd:PLN02479 412 VMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERW 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564330613 512 GEVVKAFIVLNPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFiEELPKTVSGKVKRNELRRK 576
Cdd:PLN02479 492 GESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
228-576 |
4.41e-34 |
|
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: 132.07 E-value: 4.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 228 FTSGTTGPPKMIGHT-----HSSFG----LGLSVNGRFWLDLIASDV-----MWNtsdtgWAKSAWSSVFSPWTQGAcvf 293
Cdd:cd17630 7 LTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDSWLLSLPLYHVgglaiLVR-----SLLAGAELVLLERNQAL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 294 ahylprfdstsiLQTLSKFPITVFCSAPTAYRMLIQNDITRSyKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQ 373
Cdd:cd17630 79 ------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 374 TETV-LICGNFKGMKiKPGSMGKPSPAFNVEIlDENGTILPPGQegdiavqvlpdrpfGLFTHYVDNPSKTASTLRGNFY 452
Cdd:cd17630 145 TETAsQVATKRPDGF-GRGGVGVLLPGRELRI-VEDGEIWVGGA--------------SLAMGYLRGQLVPEFNEDGWFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 453 iTGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhdqEQ 532
Cdd:cd17630 209 -TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG-------PA 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 564330613 533 LKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 576
Cdd:cd17630 281 DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
226-573 |
9.21e-34 |
|
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: 133.59 E-value: 9.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYfTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFDSTS 304
Cdd:cd17643 99 IY-TSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWE-IWGALLHGGrLVVVPYEVARSPED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 305 ILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL---DIYEGYGQTET-VLIc 380
Cdd:cd17643 176 FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 381 gNFKGMK---IKPGSM---GKPSPAFNVEILDENGTILPPGQEGDIAV---QVLP---DRPFGLFTHYVDNPsKTASTLR 448
Cdd:cd17643 255 -TFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELYVsgaGVARgylGRPELTAERFVANP-FGGPGSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 449 GnfYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyklH 528
Cdd:cd17643 333 M--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD-----D 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 564330613 529 DQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17643 406 GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
90-573 |
4.26e-33 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 132.40 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:cd17646 25 TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLA---PAVDIVAAKCENLHSKLIVSQHSREgwgnlkemmkYASDSHTCVdtkhnelmaIYfTSGTTGPPK--MIGHThs 244
Cdd:cd17646 104 DLAarlPAGGDVALLGDEALAAPPATPPLVP----------PRPDNLAYV---------IY-TSGSTGRPKgvMVTHA-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 245 sfglGLsVNGRFWL----DLIASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHYLPRFDSTSILQTLSKFPITVFCS 319
Cdd:cd17646 162 ----GI-VNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVARPGGHRDPAYLAALIREHGVTTCHF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 320 APTAYRMLIQNDITRSYKfnSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET---VLICGNFKGMKIKPGSMGKP 396
Cdd:cd17646 236 VPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidVTHWPVRGPAETPSVPIGRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 397 SPAFNVEILDENGTILPPGQEGDI---AVQVlpdrPFGlfthYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYF 466
Cdd:cd17646 314 VPNTRLYVLDDALRPVPVGVPGELylgGVQL----ARG----YLGRPALTAERFVPDpfgpgsrMYRTGDLARWRPDGAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 467 WFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLkkeiQEHVKKTTA 546
Cdd:cd17646 386 EFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAAL----RAHLAERLP 461
|
490 500
....*....|....*....|....*..
gi 564330613 547 PYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17646 462 EYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
86-573 |
5.40e-33 |
|
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: 131.94 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDivaakceNLHSKLIVSQHSREGwgnlkemmkYASDSHTCVDTKHneLMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd12117 99 LTDRSLAGRAG-------GLEVAVVIDEALDAG---------PAGNPAVPVSPDD--LAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 FgLGLsVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FDSTSILQTLSKFPITV-FCSAP 321
Cdd:cd12117 161 V-VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTFE-IWGALLNGARL--VLAPKgtlLDPDALGALIAEEGVTVlWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 322 TaYRMLIQNDITRsykFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTE--TVLICGNFKGMKIKPGS--MGKP 396
Cdd:cd12117 236 L-FNQLADEDPEC---FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEntTFTTSHVVTELDEVAGSipIGRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 397 SPAFNVEILDENGTILPPGQEGDIAVqvLPDrpfGLFTHYVDNPSKTAS-------TLRGNFYITGDRGYMDEDGYFWFV 469
Cdd:cd12117 312 IANTRVYVLDEDGRPVPPGVPGELYV--GGD---GLALGYLNRPALTAErfvadpfGPGERLYRTGDLARWLPDGRLEFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 470 ARSDDVILSSGYRIGPFEVESALIEHPSIAESAV-VSSPDPIRGEVVkAFIVlnPDYKLHDQeqlkkEIQEHVKKTTAPY 548
Cdd:cd12117 387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVV--AEGALDAA-----ELRAFLRERLPAY 458
|
490 500
....*....|....*....|....*
gi 564330613 549 KYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd12117 459 MVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
74-581 |
2.58e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 130.96 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 74 NPAFWWVDGngkevRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIpGTTQLTQKDI 153
Cdd:PRK07867 19 DRGLYFEDS-----FTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPV-GLNPTRRGAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 154 LYR-LQSSKSKCIITDDTLAPAVDIVAAKCEnlhsklIVSQHSREgWGNlkEMMKYASDSHTCVDTKHNELMAIYFTSGT 232
Cdd:PRK07867 93 LARdIAHADCQLVLTESAHAELLDGLDPGVR------VINVDSPA-WAD--ELAAHRDAEPPFRVADPDDLFMLIFTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 233 TGPPKMIGHTHSSF-GLGLSVNGRFwlDLIASDVMWntsdtgwaksawssVFSPWTQGACVFAHYLP------------R 299
Cdd:PRK07867 164 SGDPKAVRCTHRKVaSAGVMLAQRF--GLGPDDVCY--------------VSMPLFHSNAVMAGWAValaagasialrrK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 300 FDSTSILQTLSKFPITVF--CSAPTAYRMLI-QNDITRSykfNSLKhcVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET 376
Cdd:PRK07867 228 FSASGFLPDVRRYGATYAnyVGKPLSYVLATpERPDDAD---NPLR--IVYGNEGAPGDIARFARRFGCVVVDGFGSTEG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 377 vlicgnfkGMKIK------PGSMGKPSPafNVEILD-ENGTILPPGQ-------EGDIAVQVL--PDRPfGLFTHYVDNP 440
Cdd:PRK07867 303 --------GVAITrtpdtpPGALGPLPP--GVAIVDpDTGTECPPAEdadgrllNADEAIGELvnTAGP-GGFEGYYNDP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 441 SKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIV 520
Cdd:PRK07867 372 EADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALV 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564330613 521 LNPDYKLhDQEQLKKEIqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTTT 581
Cdd:PRK07867 452 LAPGAKF-DPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA 509
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
213-580 |
4.18e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 130.15 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 213 HTCVDTKHNELMaiYFTSGTTGPPKMIGHTHSSFG-LGLSVNGRFwlDLIASDVMW--------NTSDTGWAKSAwssvf 283
Cdd:PRK13388 144 HREVDAMDPFML--IFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplfhsNAVMAGWAPAV----- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 284 spwTQGACVFAHylPRFDSTSILQTLSKFPITVF--CSAPTAYRML-------IQNDITRSYkfnslkhcvsaGEPINPE 354
Cdd:PRK13388 215 ---ASGAAVALP--AKFSASGFLDDVRRYGATYFnyVGKPLAYILAtperpddADNPLRVAF-----------GNEASPR 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 355 VMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKikPGSMGKPSPafNVEI-------------LDENGTILPPgqegDIA 421
Cdd:PRK13388 279 DIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAP--GVAIynpetltecavarFDAHGALLNA----DEA 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 422 VQVLPDRP-FGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:PRK13388 351 IGELVNTAgAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINR 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 501 SAVVSSPDPIRGEVVKAFIVLNPDYK---------LHDQEQLkkeiqehvkkttAPYKYPRKIEFIEELPKTVSGKVKRN 571
Cdd:PRK13388 431 VAVYAVPDERVGDQVMAALVLRDGATfdpdafaafLAAQPDL------------GTKAWPRYVRIAADLPSTATNKVLKR 498
|
....*....
gi 564330613 572 ELRRKEWTT 580
Cdd:PRK13388 499 ELIAQGWAT 507
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
84-575 |
1.35e-31 |
|
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: 127.04 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 84 GKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdilyrlqssksk 163
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP-------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 164 ciitDDTLAPAVDIVAAkCENLHSKLIVSqhsregwgnlkemmkyasdshtcvDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:cd17653 77 ----LDAKLPSARIQAI-LRTSGATLLLT------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 244 SSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHylPRFDSTSILQTLSKFPITvfcsaPT 322
Cdd:cd17653 128 RGV-LNYVSQPPARLDVGPGSRVAQVLSIAFDACIGE-IFSTLCNGGTlVLAD--PSDPFAHVARTVDALMST-----PS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 323 AYRMLIQNDitrsykFNSLKHCVSAGEPINPEVMEQWKKktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNV 402
Cdd:cd17653 199 ILSTLSPQD------FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTC 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 403 EILDENGTILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARS 472
Cdd:cd17653 271 YILDADLQPVPEGVVGEICIsgvQVARG--------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 473 DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpdpIRGEVVkAFIVlnPDYKlhDQEQLKKEIQEHVkkttAPYKYPR 552
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PETV--DVDGLRSELAKHL----PSYAVPD 410
|
490 500
....*....|....*....|...
gi 564330613 553 KIEFIEELPKTVSGKVKRNELRR 575
Cdd:cd17653 411 RIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
226-575 |
1.54e-31 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 128.76 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHTHSSfglgLSVNGrfwLDLIA------SDVMWNTS---DTGWAKSAWSSVFSpwtqGAC-VFah 295
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSA----LIVQS---LAKIAivgygeDDVYLHTAplcHIGGLSSALAMLMV----GAChVL-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 296 yLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQndITRSYK----FNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEG 370
Cdd:PLN02860 244 -LPKFDAKAALQAIKQHNVTSMITVPAMMADLIS--LTRKSMtwkvFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 371 YGQTET----------VLICGNFK-----GMKIKPGS--------MGKPSPAFNVEI-LDEngtilpPGQEGDIAVqvlp 426
Cdd:PLN02860 321 YGMTEAcssltfmtlhDPTLESPKqtlqtVNQTKSSSvhqpqgvcVGKPAPHVELKIgLDE------SSRVGRILT---- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 427 dRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVS 505
Cdd:PLN02860 391 -RGPHVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 506 SPDPIRGEVVKAFIVLNPDYKLHDQE--------QLKKEIQEH--VKKTTAPYKYPRKIEFIEE-LPKTVSGKVKRNELR 574
Cdd:PLN02860 470 VPDSRLTEMVVACVRLRDGWIWSDNEkenakknlTLSSETLRHhcREKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
|
.
gi 564330613 575 R 575
Cdd:PLN02860 550 R 550
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
86-567 |
2.45e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 128.08 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYfTSGTTGPPK--MI 239
Cdd:PRK07798 105 VYEREFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDALAAGSPERDFGERSPDDLYLLY-TGGTTGMPKgvMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 240 GHT---HSSFGLGLSVNGRFWLD----------------LIASDVMWNTSDtgWAksAWSSVFSpwtqGACVFAHYLPRF 300
Cdd:PRK07798 184 RQEdifRVLLGGRDFATGEPIEDeeelakraaagpgmrrFPAPPLMHGAGQ--WA--AFAALFS----GQTVVLLPDVRF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 301 DSTSILQTLSKFPITVFCSAPTAY-RMLIQN-DITRSYKFNSLKHCVSAGEPINPEVMEQW-KKKTGLDIYEGYGQTETv 377
Cdd:PRK07798 256 DADEVWRTIEREKVNVITIVGDAMaRPLLDAlEARGPYDLSSLFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSET- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 378 licgNFKGMKI-KPGSMGKPSPAFN----VEILDENGTILPPGQE--GDIAvqvlpdR----PFGlfthYVDNPSKTAST 446
Cdd:PRK07798 335 ----GFGGSGTvAKGAVHTGGPRFTigprTVVLDEDGNPVEPGSGeiGWIA------RrghiPLG----YYKDPEKTAET 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 447 LR---GNFY-ITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 522
Cdd:PRK07798 401 FPtidGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 564330613 523 PDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGK 567
Cdd:PRK07798 481 EGARPDLA-----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
110-574 |
4.00e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 127.83 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 110 SLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAP----AVDIVAAKCENL 185
Cdd:PLN03102 60 NITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPlareVLHLLSSEDSNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 186 HSKLIV------------SQHSREGWGNLKEMMKYASDSHTCVDTKHNELmAIYFTSGTTGPPK--MIGHTHSSFGLGLS 251
Cdd:PLN03102 140 NLPVIFiheidfpkrpssEELDYECLIQRGEPTPSLVARMFRIQDEHDPI-SLNYTSGTTADPKgvVISHRGAYLSTLSA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 252 VNGrfWLDLIASDVMWNTSD---TGWAKSaWSSVFSPWTQgACVFAHYLPRfdstsILQTLSKFPITVFCSAPTAYRMLI 328
Cdd:PLN03102 219 IIG--WEMGTCPVYLWTLPMfhcNGWTFT-WGTAARGGTS-VCMRHVTAPE-----IYKNIEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 329 QNDITRSYKFNSLKHCVSAGEPiNPEVMEQWKKKTGLDIYEGYGQTET---VLICG---------NFKGMKIKPGSMGKP 396
Cdd:PLN03102 290 KGNSLDLSPRSGPVHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCEwqdewnrlpENQQMELKARQGVSI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 397 SPAFNVEILDENGTILPPgQEGDIAVQVLPdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVI 476
Cdd:PLN03102 369 LGLADVDVKNKETQESVP-RDGKTMGEIVI-KGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 477 LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLK-----KEIQEHVKKTTAPYKYP 551
Cdd:PLN03102 447 ISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtreRDLIEYCRENLPHFMCP 526
|
490 500
....*....|....*....|...
gi 564330613 552 RKIEFIEELPKTVSGKVKRNELR 574
Cdd:PLN03102 527 RKVVFLQELPKNGNGKILKPKLR 549
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
217-568 |
1.03e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 128.12 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 217 DTKHNELMAIYFTSGTTGPPK--MIGHT----------------------------HSsfgLGLSVNgrFWLDLIasdvm 266
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKgvMLSHHnilsnieqisdvfnlrnddvilsslpffHS---FGLTVT--LWLPLL----- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 267 wntsdtgwaksawssvfspwtQGACVFAHYLPrFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVS 346
Cdd:PRK08633 848 ---------------------EGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 347 AGEPINPEVMEQWKKKTGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPG 415
Cdd:PRK08633 906 GAEKLKPEVADAFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPG 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 416 QEGDIAV---QVLpdrpfglfTHYVDNPSKTASTLR----GNFYITGDRGYMDEDGYFWFVARsddviLSSGYRIG---- 484
Cdd:PRK08633 986 EDGLILIggpQVM--------KGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemv 1052
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 485 PF-EVESALIE--HPSIAESAVVSSPDPIRGEVvkafIVLnpdykLHDQEQLKKE-IQEHVKKTTAP--YKyPRKIEFIE 558
Cdd:PRK08633 1053 PLgAVEEELAKalGGEEVVFAVTAVPDEKKGEK----LVV-----LHTCGAEDVEeLKRAIKESGLPnlWK-PSRYFKVE 1122
|
410
....*....|
gi 564330613 559 ELPKTVSGKV 568
Cdd:PRK08633 1123 ALPLLGSGKL 1132
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
90-574 |
8.01e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 123.70 E-value: 8.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIItdd 169
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 tLAPA---VDIVAAKCENLHSKLIVSQ--------------HSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFT-SG 231
Cdd:PRK06164 113 -VWPGfkgIDFAAILAAVPPDALPPLRaiavvddaadatpaPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTtSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 232 TTGPPKMIGHTHSSF---------GLGLSVNGRFWLDLIASDVMwntsdtgwaksAWSSVFSPWTQGACVfaHYLPRFDS 302
Cdd:PRK06164 192 TTSGPKLVLHRQATLlrharaiarAYGYDPGAVLLAALPFCGVF-----------GFSTLLGALAGGAPL--VCEPVFDA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 303 TSILQTLSKFPIT-VFCSAPTAYRMLIQNDitRSYKFNSLKHC-VSAGEPINPEVMeQWKKKTGLDIYEGYGQTE--TVL 378
Cdd:PRK06164 259 ARTARALRRHRVThTFGNDEMLRRILDTAG--ERADFPSARLFgFASFAPALGELA-ALARARGVPLTGLYGSSEvqALV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 379 ICGNFK---GMKIKPGsmGKP-SPAFNVEILD-ENGTILPPGQEGDIAVQVlpdrPfGLFTHYVDNPSKTASTLRGN-FY 452
Cdd:PRK06164 336 ALQPATdpvSVRIEGG--GRPaSPEARVRARDpQDGALLPDGESGEIEIRA----P-SLMRGYLDNPDATARALTDDgYF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 453 ITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpdPIRGE-VVKAFIVLNPDYKLhDQE 531
Cdd:PRK06164 409 RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDGASP-DEA 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 564330613 532 QLKKeiqeHVKKTTAPYKYPRKIEFIEELPKTVSG---KVKRNELR 574
Cdd:PRK06164 486 GLMA----ACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
86-573 |
1.02e-29 |
|
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: 122.40 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd12116 10 DRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLA-------PAVDIVAAKCENLHSKLIVSQHSregwGNLKEMMkyasdshtcvdtkhnelmaiyFTSGTTGPPKM 238
Cdd:cd12116 89 LTDDALPdrlpaglPVLLLALAAAAAAPAAPRTPVSP----DDLAYVI---------------------YTSGSTGRPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 239 IGHTHSSF-GLGLSVNGRfwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFDSTSILQTLSKFPITV 316
Cdd:cd12116 144 VVVSHRNLvNFLHSMRER--LGLGPGDRLLAVTTYAFDISLLE-LLLPLLAGArVVIAPRETQRDPEALARLIEAHSITV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 317 FCSAPTAYRMLIQNDITRSYKFNSLkhCvsAGEPINPEVMEQWKKKTGlDIYEGYGQTETVL------ICGNFKGMKIkp 390
Cdd:cd12116 221 MQATPATWRMLLDAGWQGRAGLTAL--C--GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 391 gsmGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLPD---RPFGLFTHYVDNPSKTAstlRGNFYITGDRGYMDEDG 464
Cdd:cd12116 294 ---GRPLANTQVYVLDAALRPVPPGVPGELYIggdGVAQGylgRPALTAERFVPDPFAGP---GSRLYRTGDLVRRRADG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 465 YFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLnPDYKLHDQEQLKkeiqEHVKKT 544
Cdd:cd12116 368 RLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALR----AHLRAT 441
|
490 500
....*....|....*....|....*....
gi 564330613 545 TAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd12116 442 LPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
218-573 |
3.76e-29 |
|
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: 120.62 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 218 TKHNELMAIYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFwlDLIASDVMWNTSDTGWAKSAwSSVFSPWTQGAC-VFA 294
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKgvMIEH-QSLVNLSHGLIKEY--GITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 295 HYLPRFDSTSILQTLSKFPITVFcSAPTAYRMLIQNDITRSYK--FNSLKHCVSAGEPINPEVMEQWKKKTGLDI--YEG 370
Cdd:cd17644 179 PEEMRSSLEDFVQYIQQWQLTVL-SLPPAYWHLLVLELLLSTIdlPSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 371 YGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTAS 445
Cdd:cd17644 258 YGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV-----GLARGYLNRPELTAE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 446 TLRGN---------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 516
Cdd:cd17644 333 KFISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLV 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 564330613 517 AFIVlnPDYklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17644 413 AYIV--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
487-567 |
1.44e-28 |
|
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: 108.40 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 487 EVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYklhdqEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSG 566
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 564330613 567 K 567
Cdd:pfam13193 76 K 76
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
86-581 |
2.94e-28 |
|
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: 120.73 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAKCENLhSKLIVSQHSregwgnlkemmkyASDSHTCVDTKHneLMAIYFTSGTTGPPK--MIghTH 243
Cdd:COG1020 578 LTQSALAARLPELGVPVLAL-DALALAAEP-------------ATNPPVPVTPDD--LAYVIYTSGSTGRPKgvMV--EH 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 244 SSFG-LGLSVNGRFWLDliASDVM-WNTS---DTgwakSAWSsVFSPWTQGAC-VFAHYLPRFDSTSILQTLSKFPITVF 317
Cdd:COG1020 640 RALVnLLAWMQRRYGLG--PGDRVlQFASlsfDA----SVWE-IFGALLSGATlVLAPPEARRDPAALAELLARHRVTVL 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 318 CSAPTAYRMLIQNDITRsykFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVL--ICGNFKGMKIKPGSM- 393
Cdd:COG1020 713 NLTPSLLRALLDAAPEA---LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVdsTYYEVTPPDADGGSVp 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 394 -GKPSPAFNVEILDENGTILPPGQEGDIAV---QV----LpDRPfGL----FthyVDNPSKTASTlRgnFYITGDRGYMD 461
Cdd:COG1020 790 iGRPIANTRVYVLDAHLQPVPVGVPGELYIggaGLargyL-NRP-ELtaerF---VADPFGFPGA-R--LYRTGDLARWL 861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 462 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQEQLKKEIQEHV 541
Cdd:COG1020 862 PDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA-----GAAAAAALLRLAL 936
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 564330613 542 KKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTTT 581
Cdd:COG1020 937 ALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA 976
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
90-570 |
3.22e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 118.84 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPAVDIVAAKCENLhsKLIVSQHSREGWGNLKEMMKYASDSHTCVDT----KHNELMaIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK05852 124 DGPHDRAEPTTRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglRPDDAM-IMFTGGTTGLPKMVPWTHAN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 fgLGLSVNGrfwldLIAS----------DVMWNTSDTGWAKSAWSSVFSpwtqGACVFAHYLPRFDSTSILQTLSKFPIT 315
Cdd:PRK05852 201 --IASSVRA-----IITGyrlsprdatvAVMPLYHGHGLIAALLATLAS----GGAVLLPARGRFSAHTFWDDIKAVGAT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 316 VFCSAPTAYRMLIQNDITRSY--KFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--------VLICGNFKG 385
Cdd:PRK05852 270 WYTAVPTIHQILLERAATEPSgrKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqIEGIGQTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 386 MKIKPGSMGKpSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGY 465
Cdd:PRK05852 350 PVVSTGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWL-----RGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 466 FWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKLHDQEQlkkEIQEHVKKTT 545
Cdd:PRK05852 424 LSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTAE---ELVQFCRERL 498
|
490 500
....*....|....*....|....*
gi 564330613 546 APYKYPRKIEFIEELPKTVSGKVKR 570
Cdd:PRK05852 499 AAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
226-573 |
3.68e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 118.18 E-value: 3.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHT-HSSFGLGLsvngrfWLDLIASDVMWNTSDTGWAKSAWSSV-----FSPWTQGACVFAHYlpR 299
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRApQLRSAVGV------WVTILDRTRLRTGSRISVAMPMFHGLglgmlMLTIALGGTVLTHR--H 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 300 FDSTSILQTLSKFPITVFCSAPTAY-RMLIQNDITRSYK-FNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET- 376
Cdd:PRK13383 251 FDAEAALAQASLHRADAFTAVPVVLaRILELPPRVRARNpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVg 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 377 VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV--QVLPDRpfglfthYVDNPSKtaSTLRGnFYIT 454
Cdd:PRK13383 331 IGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVggELAGTR-------YTDGGGK--AVVDG-MTST 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 455 GDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLK 534
Cdd:PRK13383 401 GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGV-DAAQLR 479
|
330 340 350
....*....|....*....|....*....|....*....
gi 564330613 535 KEIQEHVKKttapYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:PRK13383 480 DYLKDRVSR----FEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
107-573 |
7.09e-28 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 117.80 E-value: 7.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 107 EACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDIlyrlqssKSKCIITDdtlaPAVDIVAAKC---- 182
Cdd:PRK05857 59 RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAI-------ERFCQITD----PAAALVAPGSkmas 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 183 ----ENLHSKLIVSQHSREGWGNLKEMMKYASDShTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLG---LSVNGR 255
Cdd:PRK05857 128 savpEALHSIPVIAVDIAAVTRESEHSLDAASLA-GNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 256 FWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYlprfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRS 335
Cdd:PRK05857 207 NWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSAN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 336 YKFNSLKHCVSAG-EPINPEVmeQWKKKTGLDIYEGYGQTET-----VLICGNFKGMKIKPGSMGKPSPAFNVEILDENG 409
Cdd:PRK05857 283 ATVPSLRLVGYGGsRAIAADV--RFIEATGVRTAQVYGLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 410 TilppgqeGDIAVQVLPDRPFGLF--------THYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGY 481
Cdd:PRK05857 361 I-------GPTAPGAGPSASFGTLwikspanmLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGV 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 482 RIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELP 561
Cdd:PRK05857 434 NIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIP 513
|
490
....*....|..
gi 564330613 562 KTVSGKVKRNEL 573
Cdd:PRK05857 514 RTQSGKVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-573 |
1.01e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.29 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEacslqRG----DRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 161
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIA-----RGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSG 4648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 162 SKCIITDDTLAPAVDIVAAkcenLHSKLIVSQHSREGWGNLKEMMKYASDShtcvdtkhneLMAIYFTSGTTGPPKMIGH 241
Cdd:PRK12316 4649 AALLLTQSHLLQRLPIPDG----LASLALDRDEDWEGFPAHDPAVRLHPDN----------LAYVIYTSGSTGRPKGVAV 4714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 242 THSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAP 321
Cdd:PRK12316 4715 SHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPP 4792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 322 TAYRMLIQNDiTRSYKFNSLKHCVSAGEPINPEVMEQ-WKKKTGLDIYEGYGQTETVLICGNFKGMK-IKPGS----MGK 395
Cdd:PRK12316 4793 VYLQQLAEHA-ERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDgDACGAaympIGT 4871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 396 PSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTL--------RGNFYITGDRGYMDEDGYFW 467
Cdd:PRK12316 4872 PLGNRSGYVLDGQLNPLPVGVAGELYLG-----GEGVARGYLERPALTAERFvpdpfgapGGRLYRTGDLARYRADGVID 4946
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 468 FVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLNpDYKLHD----QEQLKKEIQEHVKK 543
Cdd:PRK12316 4947 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQ-DPALADadeaQAELRDELKAALRE 5024
|
490 500 510
....*....|....*....|....*....|
gi 564330613 544 TTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:PRK12316 5025 RLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
90-524 |
3.50e-27 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 115.77 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKSKCII 166
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 167 TddtlapavdIVAA---------KCENLHSKLIVSQhsREGWGN--LKEMM-KYASDSHTCVDTKHNELMAIYFTSGTTG 234
Cdd:PRK09274 119 G---------IPKAhlarrlfgwGKPSVRRLVTVGG--RLLWGGttLATLLrDGAAAPFPMADLAPDDMAAILFTSGSTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 235 PPKMIGHTHSSF---------GLGLSVNGRfwlDLIASDVMwntsdtgwaksawsSVFSPwtqgACVFAHYLPRFDST-- 303
Cdd:PRK09274 188 TPKGVVYTHGMFeaqiealreDYGIEPGEI---DLPTFPLF--------------ALFGP----ALGMTSVIPDMDPTrp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 304 ------SILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKK--KTGLDIYEGYGQTE 375
Cdd:PRK09274 247 atvdpaKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 376 TVLICgnfkgmKIkpGS------------------MGKPSPAFNVEILD---------ENGTILPPGQEGDIAVQ---VL 425
Cdd:PRK09274 327 ALPIS------SI--ESreilfatraatdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAgpmVT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 426 PDrpfglfthYVDNPSKTA-----STLRGNFYITGDRGYMDEDGYFWFVAR-SDDVILSSGyRIGPFEVESALIEHPSIA 499
Cdd:PRK09274 399 RS--------YYNRPEATRlakipDGQGDVWHRMGDLGYLDAQGRLWFCGRkAHRVETAGG-TLYTIPCERIFNTHPGVK 469
|
490 500
....*....|....*....|....*.
gi 564330613 500 ESAVVSSPDPirGEVVKAFIV-LNPD 524
Cdd:PRK09274 470 RSALVGVGVP--GAQRPVLCVeLEPG 493
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-567 |
5.61e-27 |
|
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: 112.48 E-value: 5.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHTHSSFGLGLS-----VNGRFWLDLIASDVMWNTSDTGW--------AKSAWSSVFSPWTQGACV 292
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMggadfGTGEFTPSEDAHKAAAAAAGTVMfpapplmhGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 293 FAHylPRFDSTSILQTLSKFPITVFCSAPTAY-RMLIQN-DITRSYKFNSLKHCVSAGEPINPEVMEQW-KKKTGLDIYE 369
Cdd:cd05924 88 LPD--DRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 370 GYGQTET-VLICGNFKGMKIKPGSMGKPSPafNVEILDENGTILPPGQEGdiaVQVLPDR---PFGlfthYVDNPSKTAS 445
Cdd:cd05924 166 AFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGG---VGWIARRghiPLG----YYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 446 TLR---GNFY-ITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 521
Cdd:cd05924 237 TFPevdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 564330613 522 NPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGK 567
Cdd:cd05924 317 REGAGVDLE-----ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-577 |
1.25e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.03 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILteacsLQRG---DR-VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 161
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRL-----IAIGvgpDVlVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSG 3192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 162 SKCIITDDTLAPAVDIVAAkcenLHSkLIVSQHSREGWgnlkemmkyaSDSHTCVDTKHNELMAIYFTSGTTGPPKMIGH 241
Cdd:PRK12467 3193 VKLLLTQAHLLEQLPAPAG----DTA-LTLDRLDLNGY----------SENNPSTRVMGENLAYVIYTSGSTGKPKGVGV 3257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 242 THSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAP 321
Cdd:PRK12467 3258 RHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPP 3335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 322 TAYRMLIQNDITRSYkfNSLKHCVSAGEPINPEVMEQWKKKTG-LDIYEGYGQTETVLI-----CGNFKGMKIKPGSMGK 395
Cdd:PRK12467 3336 AYLQQFAEDAGGADC--ASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGR 3413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 396 PSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDEDGYFW 467
Cdd:PRK12467 3414 PVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLARYRADGVIE 3488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 468 FVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRGEVVKAFIVLNPdyklhDQEQLKKEIQEHVKKTTAP 547
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD-----PQGDWRETLRDHLAASLPD 3562
|
490 500 510
....*....|....*....|....*....|
gi 564330613 548 YKYPRKIEFIEELPKTVSGKVKRNELRRKE 577
Cdd:PRK12467 3563 YMVPAQLLVLAAMPLGPNGKVDRKALPDPD 3592
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
88-573 |
3.71e-26 |
|
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: 111.49 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 167
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 168 DDtlapavdivaakcenlhsklivsqhsregwGNLKEMMkyasdshtcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFg 247
Cdd:cd17645 102 NP------------------------------DDLAYVI---------------------YTSGSTGLPKGVMIEHHNL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 248 lglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLP---RFDSTSILQTLSKFPITV-FCS 319
Cdd:cd17645 130 ----VNLCEWhrpyFGVTPADKSLVYASFSFDASAWE-IFPHLTAGAAL--HVVPserRLDLDALNDYFNQEGITIsFLP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 320 APTAYR-MLIQNditrsykfNSLKHCVSAGEPINPevmeqwKKKTGLDIYEGYGQTETVLICGNFKGMKIKPG-SMGKPS 397
Cdd:cd17645 203 TGAAEQfMQLDN--------QSLRVLLTGGDKLKK------IERKGYKLVNNYGPTENTVVATSFEIDKPYANiPIGKPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 398 PAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVA 470
Cdd:cd17645 269 DNTRVYILDEALQLQPIGVAGELCIA-----GEGLARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 471 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpdyklhDQEQLKKEIQEHVKKTTAPYKY 550
Cdd:cd17645 344 RLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------PEEIPHEELREWLKNDLPDYMI 416
|
490 500
....*....|....*....|...
gi 564330613 551 PRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17645 417 PTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
218-573 |
4.34e-26 |
|
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: 111.26 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 218 TKHNELMAIYFTSGTTGPPKMIGHTHSSfglglSVNGRFWldliasdvmwntSDTGWAKSAWSSV--------------- 282
Cdd:cd12115 102 TDPDDLAYVIYTSGSTGRPKGVAIEHRN-----AAAFLQW------------AAAAFSAEELAGVlastsicfdlsvfel 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 283 FSPWTQGACVF----AHYL---PRFDSTSILQTLskfpitvfcsaPTAYRMLI-QNDITRSYKFNSLkhcvsAGEPINPE 354
Cdd:cd12115 165 FGPLATGGKVVladnVLALpdlPAAAEVTLINTV-----------PSAAAELLrHDALPASVRVVNL-----AGEPLPRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 355 -VMEQWKKKTGLDIYEGYGQTE-----TVLICGnfKGMKIKPgSMGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdr 428
Cdd:cd12115 229 lVQRLYARLQVERVVNLYGPSEdttysTVAPVP--PGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELYIG----- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 429 PFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES 501
Cdd:cd12115 301 GAGVARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564330613 502 AVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd12115 381 VVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
86-575 |
7.36e-26 |
|
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: 111.37 E-value: 7.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPavdiVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCV-DTKHNELMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05915 101 LFDPNLLP----LVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPvRVPERAACGMAYTTGTTGLPKGVVYSHR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 245 SFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTsILQTLSKFPITVFCSAPTAY 324
Cdd:cd05915 177 ALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPAS-LVELFDGEGVTFTAGVPTVW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 325 RMLI--QNDITRSYKFNSLkhcVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET------VLICGNFKGMKIKPGSMGKP 396
Cdd:cd05915 256 LALAdyLESTGHRLKTLRR---LVVGGSAAPRSLIARFERMGVEVRQGYGLTETspvvvqNFVKSHLESLSEEEKLTLKA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 397 SPAFN-----VEILDENGTILPpgQEGDiAVQVLPDRPFGLFTHYV-DNPSKTASTLRGNFYITGDRGYMDEDGYFWFVA 470
Cdd:cd05915 333 KTGLPiplvrLRVADEEGRPVP--KDGK-ALGEVQLKGPWITGGYYgNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 471 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIvlnpdyKLHDQEQLKKEIQEHVKKTTAPYKY 550
Cdd:cd05915 410 RLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV------VPRGEKPTPEELNEHLLKAGFAKWQ 483
|
490 500
....*....|....*....|....*.
gi 564330613 551 -PRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:cd05915 484 lPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-573 |
9.41e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.13 E-value: 9.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDiVAAKCENL---HSKLIVSQHSREgwgNLKemmkyasdshTCVDTKHneLMAIYFTSGTTGPPKMIGHT 242
Cdd:PRK12316 613 LSQSHLGRKLP-LAAGVQVLdldRPAAWLEGYSEE---NPG----------TELNPEN--LAYVIYTSGSTGKPKGAGNR 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 243 HSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFDSTSILQTLSKFPITVF 317
Cdd:PRK12316 677 HRAL-----SNRLCWmqqaYGLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 318 CSAPTAYRMLIQNDITRSykFNSLKHCVSAGEPINPEVMEQ-WKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MG 394
Cdd:PRK12316 751 HFVPSMLQAFLQDEDVAS--CTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSvpIG 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 395 KPSPAFNVEILDENGTILPPGQEGDIavqVLPDRpfGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFW 467
Cdd:PRK12316 829 RPIANLACYILDANLEPVPVGVLGEL---YLAGR--GLARGYHGRPGLTAERFVPSpfvagerMYRTGDLARYRADGVIE 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 468 FVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLNpdyklHDQEQLKKEIQEHVKKTTAP 547
Cdd:PRK12316 904 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE-----SEGGDWREALKAHLAASLPE 974
|
490 500
....*....|....*....|....*.
gi 564330613 548 YKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:PRK12316 975 YMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-573 |
1.11e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 112.95 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12467 535 EQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAKcenlhSKLIVSQHSREGWGnlkemmkyASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK12467 614 LTQSHLLAQLPVPAGL-----RSLCLDEPADLLCG--------YSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGA 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 FGLGLSVNGRfWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FDSTSILQTLSKFPITVFCSAPT 322
Cdd:PRK12467 681 LANYVCVIAE-RLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLKIVPS 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 323 AYRMLIQNdiTRSYKFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVLICGNFK----GMKIKPGSMGKPS 397
Cdd:PRK12467 757 HLQALLQA--SRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPL 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 398 PAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDEDGYFWFV 469
Cdd:PRK12467 835 ANLGLYILDHYLNPVPVGVVGELYIG-----GAGLARGYHRRPALTAerfvpdpfGADGGRLYRTGDLARYRADGVIEYL 909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 470 ARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVlnPDYKLHDQEQ--LKKEIQEHVKKTTAP 547
Cdd:PRK12467 910 GRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLV--PAAVADGAEHqaTRDELKAQLRQVLPD 986
|
490 500
....*....|....*....|....*.
gi 564330613 548 YKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:PRK12467 987 YMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
88-575 |
1.17e-25 |
|
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: 110.32 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP-GTTQLTQkdilyRLQSskskciI 166
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPlDPSHPLQ-----RLQE------I 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 167 TDDTLAPAVdivaakcenlhsklIVSQHSregwgnlkemmkyasdshtcvdtkhnELMAIYFTSGTTGPPKMIGHTHSSF 246
Cdd:cd05918 92 LQDTGAKVV--------------LTSSPS--------------------------DAAYVIFTSGSTGKPKGVVIEHRAL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 247 ---------GLGLSVNGRfWLDL--IASDVMWNtsdtgwaksawsSVFSPWTQGACV-----------FAHYLPRFDSTS 304
Cdd:cd05918 132 stsalahgrALGLTSESR-VLQFasYTFDVSIL------------EIFTTLAAGGCLcipseedrlndLAGFINRLRVTW 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 305 ILQTlskfpitvfcsaPTAYRMLIQNDITrsykfnSLKHCVSAGEPINPEVMEQWKKKTGLdiYEGYGQTE-TVLICGNF 383
Cdd:cd05918 199 AFLT------------PSVARLLDPEDVP------SLRTLVLGGEALTQSDVDTWADRVRL--INAYGPAEcTIAATVSP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 384 KGMKIKPGSMGKPSPAfNVEILDENGT--ILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTA-------------- 444
Cdd:cd05918 259 VVPSTDPRNIGRPLGA-TCWVVDPDNHdrLVPIGAVGELLIegpILARG--------YLNDPEKTAaafiedpawlkqeg 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 445 STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK---AFIVL 521
Cdd:cd05918 330 SGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlvAFVVL 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330613 522 NPDYKLHDQEQ------------LKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:cd05918 410 DGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
214-573 |
1.22e-25 |
|
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: 109.65 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 214 TCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGlGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVf 293
Cdd:cd17652 86 ALLLTTPDNLAYVIYTSGSTGRPKGVVVTHRGLA-NLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATL- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 294 aHYLPRFDSTS---ILQTLSKFPITVFCSAPTAYRMLIQNDITrsykfnSLKHCVSAGEPINPEVMEQWKKktGLDIYEG 370
Cdd:cd17652 163 -VLAPAEELLPgepLADLLREHRITHVTLPPAALAALPPDDLP------DLRTLVVAGEACPAELVDRWAP--GRRMINA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 371 YGQTETVL---ICGNFKGMKIKPgsMGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTA--- 444
Cdd:cd17652 234 YGPTETTVcatMAGPLPGGGVPP--IGRPVPGTRVYVLDARLRPVPPGVPGELYIA-----GAGLARGYLNRPGLTAerf 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 445 -----STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 519
Cdd:cd17652 307 vadpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 564330613 520 VLNPDYKLhDQEQLKkeiqEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17652 387 VPAPGAAP-TAAELR----AHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
83-576 |
2.81e-25 |
|
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: 109.48 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 83 NGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 162
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 163 KCIIT---DD--TLAPAVDivaakcENLHSkLIVSQHS----REGWGNLKEMMKYASDSHTcvdTKHNELMAIYFTSGTT 233
Cdd:cd05932 80 KALFVgklDDwkAMAPGVP------EGLIS-ISLPPPSaancQYQWDDLIAQHPPLEERPT---RFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 234 GPPKMIGHTHSSFG---------LGLSVNGRF--WLDL--IASDVMwntsdtgwaksawssVFSPWTQGACV--FAHYLP 298
Cdd:cd05932 150 GQPKGVMLTFGSFAwaaqagiehIGTEENDRMlsYLPLahVTERVF---------------VEGGSLYGGVLvaFAESLD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 299 RFdstsiLQTLSKFPITVFCSAP---TAYRMLIQNDITRSyKFNSL----------KHCVSAG-------------EPIN 352
Cdd:cd05932 215 TF-----VEDVQRARPTLFFSVPrlwTKFQQGVQDKIPQQ-KLNLLlkipvvnslvKRKVLKGlgldqcrlagcgsAPVP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 353 PEVMEqWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEIldengtilppGQEGDIAVqvlpdRPFGL 432
Cdd:cd05932 289 PALLE-WYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILV-----RSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 433 FTHYVDNPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSS-GYRIGPFEVESALIEHPSIAESAVVSS--PD 508
Cdd:cd05932 353 MMGYYKDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPA 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564330613 509 PIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEH---VKKTTAPYKYPRKIEFIEElPKTVSG-------KVKRNELRRK 576
Cdd:cd05932 433 PLALVVLSEEARLRADAF--ARAELEASLRAHlarVNSTLDSHEQLAGIVVVKD-PWSIDNgiltptlKIKRNVLEKA 507
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
88-574 |
7.95e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 108.26 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTeACSLQRGDRVMVIlpkipEW-----WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 162
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALA-ALGVEPGDRVGTL-----AWngyrhLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 163 KCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNL-----KEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPK 237
Cdd:PRK07008 113 RYVLFDLTFLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTpllcyETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 238 MIGHTHSS-----FGLGLSVNgrfwLDLIASDV------MWNTSdtgwaksAWSSVFS-PWTQGACVFAHylPRFDSTSI 305
Cdd:PRK07008 193 GALYSHRStvlhaYGAALPDA----MGLSARDAvlpvvpMFHVN-------AWGLPYSaPLTGAKLVLPG--PDLDGKSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 306 LQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLIcGNFKG 385
Cdd:PRK07008 260 YELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPL-GTLCK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 386 MKIKPGSMGKPS----------PAFNVE--ILDENGTILP-PGQE-GDIAVQ---VLpDRPFGlfthyvdnpsKTASTLR 448
Cdd:PRK07008 339 LKWKHSQLPLDEqrkllekqgrVIYGVDmkIVGDDGRELPwDGKAfGDLQVRgpwVI-DRYFR----------GDASPLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 449 GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLH 528
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 564330613 529 DQEQLKkeiqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK07008 488 REELLA-----FYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-575 |
8.40e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.05 E-value: 8.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLA-PAVDIVAAKCenlhsklivsqhsregwgnLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHS 244
Cdd:PRK12316 3159 LSQSHLRlPLAQGVQVLD-------------------LDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 245 SFGLGLSVNGRFwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDS-TSILQTLSKFPITVFCSAPTA 323
Cdd:PRK12316 3220 ALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEE-LFWPLMSGARVVLAGPEDWRDpALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 324 YRMLIQNDITRSYKfnSLKHCVSAGEPINPEVMEQWKkkTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MGKPSPAFN 401
Cdd:PRK12316 3298 LQAFLEEEDAHRCT--SLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRA 3373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 402 VEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSDD 474
Cdd:PRK12316 3374 CYILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAERFVPDpfvpgerLYRTGDLARYRADGVIEYIGRVDH 3448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 475 VILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLNPdyklhDQEQLKKEIQEHVKKTTAPYKYPRKI 554
Cdd:PRK12316 3449 QVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPED-----EAGDLREALKAHLKASLPEYMVPAHL 3519
|
490 500
....*....|....*....|.
gi 564330613 555 EFIEELPKTVSGKVKRNELRR 575
Cdd:PRK12316 3520 LFLERMPLTPNGKLDRKALPR 3540
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
86-574 |
1.33e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 107.77 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTV------------LIPGTTQLTQKdi 153
Cdd:PRK10946 46 ERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVApvnalfshqrseLNAYASQIEPA-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 154 lyRLQSSKSKCIITDDTLapaVDIVAAKCENLhskLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTT 233
Cdd:PRK10946 123 --LLIADRQHALFSDDDF---LNTLVAEHSSL---RVVLLLNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGST 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 234 GPPKMIGHTHSSFGL---------GLSVNGRFWLDLIASDvmwntsdtgwaKSAWSS-----VFspWTQGACVFAhylPR 299
Cdd:PRK10946 195 GTPKLIPRTHNDYYYsvrrsveicGFTPQTRYLCALPAAH-----------NYPMSSpgalgVF--LAGGTVVLA---PD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 300 FDSTSILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV 377
Cdd:PRK10946 259 PSATLCFPLIEKHQVNVTALVPPAVSLWLQaiAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 378 LicgNFKGMKIKP----GSMGKP-SPAFNVEILDENGTILPPGQEGDIAVQvlpdRPFgLFTHYVDNPSKTASTLRGN-F 451
Cdd:PRK10946 339 V---NYTRLDDSDerifTTQGRPmSPDDEVWVADADGNPLPQGEVGRLMTR----GPY-TFRGYYKSPQHNASAFDANgF 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 452 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhdQE 531
Cdd:PRK10946 411 YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLK---AV 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 564330613 532 QLKKEIQEHvkkTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK10946 488 QLRRFLREQ---GIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
89-573 |
2.24e-24 |
|
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: 106.40 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 89 WSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd17656 14 LTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 169 DTLApavdiVAAKCENLHSKLIVSQHSREGWGNLKemMKYASDshtcvdtkhnELMAIYFTSGTTGPPKMIGHTHSSFGL 248
Cdd:cd17656 93 RHLK-----SKLSFNKSTILLEDPSISQEDTSNID--YINNSD----------DLLYIIYTSGTTGKPKGVQLEHKNMVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 249 GLSVNGRFWLDLIASDVMWNTSDTgwAKSAWSSVFSPWTQGACVF-AHYLPRFDSTSILQTLSKFPITVFcSAPTAYRML 327
Cdd:cd17656 156 LLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLLSGGTLYiIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 328 IQNDitRSYK---FNSLKHCVSAGEP--INPEVMEQWKKKtGLDIYEGYGQTETVLIcgnfKGMKIKPGS-------MGK 395
Cdd:cd17656 233 IFSE--REFInrfPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSETHVV----TTYTINPEAeipelppIGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 396 PSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWF 468
Cdd:cd17656 306 PISNTWIYILDQEQQLQPQGIVGELYISGA-----SVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 469 VARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKLHDqEQLKKEIQEHVKKttapY 548
Cdd:cd17656 381 LGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNI-SQLREYLAKQLPE----Y 453
|
490 500
....*....|....*....|....*
gi 564330613 549 KYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17656 454 MIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
84-574 |
2.32e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 107.14 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 84 GKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 163
Cdd:PRK06018 35 GPIVRTTYAQIHDRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 164 CIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKY------ASDSHTCVDTKHNELMAIYFTSGTTGPPK 237
Cdd:PRK06018 114 VVITDLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKNAVAYeewiaeADGDFAWKTFDENTAAGMCYTSGTTGDPK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 238 MIGHTHSSFGL-GLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFahyLP--RFDSTSILQTLSKFPI 314
Cdd:PRK06018 194 GVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLDGASVYELLDTEKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 315 TVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPInPEVMEQWKKKTGLDIYEGYGQTETVLIcgnfkgmkikpGSMG 394
Cdd:PRK06018 270 TFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPL-----------GTLA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 395 KPSPAFNVEILDENGTIL-----PP-GQEGDI---AVQVLP--DRPFGLFThyVDNPSKTASTLRGN--------FYITG 455
Cdd:PRK06018 338 ALKPPFSKLPGDARLDVLqkqgyPPfGVEMKItddAGKELPwdGKTFGRLK--VRGPAVAAAYYRVDgeildddgFFDTG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 456 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQEQLKK 535
Cdd:PRK06018 416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP-----GETATRE 490
|
490 500 510
....*....|....*....|....*....|....*....
gi 564330613 536 EIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK06018 491 EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
81-575 |
8.44e-24 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 105.63 E-value: 8.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 81 DGNGKEVRwSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWW--LANVACLrtGTVLIPGTTQLTQKDILYRLQ 158
Cdd:PRK05620 32 GGAEQEQT-TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 159 SSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHS-REGWGNLKEMMKYAS-----DSHTCV----DTKHNELMAIYF 228
Cdd:PRK05620 109 HAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGPSDaDSAAAHMPEGIKVYSyeallDGRSTVydwpELDETTAAAICY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 229 TSGTTGPPKMIGHTHSSFGLGLsvngrfwLDLIASDVMWNTSDTG-------WAKSAWSSVFSPWTQGACVFahyLPRFD 301
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSLYLQS-------LSLRTTDSLAVTHGESflccvpiYHVLSWGVPLAAFMSGTPLV---FPGPD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 302 STSilQTLSKFPIT----VFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV 377
Cdd:PRK05620 259 LSA--PTLAKIIATamprVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 378 LIcgnfkGMKIKPG-------------SMGKPSPAFNVEILDEnGTILPPG--QEGDIAVqvlpdRPFGLFTHYVDNPSK 442
Cdd:PRK05620 337 PV-----GTVARPPsgvsgearwayrvSQGRFPASLEYRIVND-GQVMESTdrNEGEIQV-----RGNWVTASYYHSPTE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 443 T----ASTLRGN-------------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVS 505
Cdd:PRK05620 406 EgggaASTFRGEdvedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564330613 506 SPDPIRGEVVKAFIVLNPDYKLHDQ--EQLKKEIQEHVKKTTAPYKYprkiEFIEELPKTVSGKVKRNELRR 575
Cdd:PRK05620 486 YPDDKWGERPLAVTVLAPGIEPTREtaERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
80-575 |
9.70e-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: 105.06 E-value: 9.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 80 VDGNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPK----IPEWWlanvACLRTGTVLIPGTTQLTQKDILY 155
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPTYDEPNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 156 RLQSSK-------SKCIITDDTLAPAVDIVAAKCENLHSKLIVSQhsregwgnlkEMMKYASDSHTcVDTKHNELMAIYF 228
Cdd:cd05906 106 RLRKLRhiwqllgSPVVLTDAELVAEFAGLETLSGLPGIRVLSIE----------ELLDTAADHDL-PQSRPDDLALLML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 229 TSGTTGPPKMIGHTHSSF---GLGLSVNGRF--------W--LDLIASDVMWNTSDtgwaksawssVFSPWTQGACVFAH 295
Cdd:cd05906 175 TSGSTGFPKAVPLTHRNIlarSAGKIQHNGLtpqdvflnWvpLDHVGGLVELHLRA----------VYLGCQQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 296 YLPrfDSTSILQTLSKFPITV-FcsAPT-AYRMLIQ---NDITRSYKFNSLKHCVSAGEPINPEVMEQWK---KKTGLD- 366
Cdd:cd05906 245 ILA--DPLRWLDLIDRYRVTItW--APNfAFALLNDlleEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLrllEPYGLPp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 367 --IYEGYGQTET---VLICGNFKGMKIKPG----SMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPdrpfgLFTHYV 437
Cdd:cd05906 321 daIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPV-----VTKGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 438 DNPSKTASTLR-GNFYITGDRGYMDeDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES--AVVSSPDPIRGEV 514
Cdd:cd05906 396 NNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAETE 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564330613 515 VKAfIVLNPDYKLHDQ-EQLKKEIQEHV-KKTTAPYKY----PRkiefiEELPKTVSGKVKRNELRR 575
Cdd:cd05906 475 ELA-IFFVPEYDLQDAlSETLRAIRSVVsREVGVSPAYliplPK-----EEIPKTSLGKIQRSKLKA 535
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
86-573 |
6.85e-23 |
|
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: 101.96 E-value: 6.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd12114 10 DGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAkcenLHSKLIVSQHsregwgnlkemmkyASDSHTCVDTKHNELMAIYFTSGTTGPPK--MIGHTH 243
Cdd:cd12114 89 LTDGPDAQLDVAVFD----VLILDLDALA--------------APAPPPPVDVAPDDLAYVIFTSGSTGTPKgvMISHRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 244 SSFGLgLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHYLPRFDSTSILQTLSKFPITVFCSAPT 322
Cdd:cd12114 151 ALNTI-LDINRRFAVG--PDDRVLALSSLSFDLSVYD-IFGALSAGATlVLPDEARRRDPAHWAELIERHGVTLWNSVPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 323 AYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVlICGNFkgMKIKPGSM-------G 394
Cdd:cd12114 227 LLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIY--HPIDEVPPdwrsipyG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 395 KPSPAFNVEILDENGTILPPGQEGDIavqvlpdrpF----GLFTHYVDNPSKTAS-----TLRGNFYITGDRGYMDEDGY 465
Cdd:cd12114 304 RPLANQRYRVLDPRGRDCPDWVPGEL---------WiggrGVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 466 FWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiRGEVVKAFIVLNPDYklhdQEQLKKEIQEHVKKTT 545
Cdd:cd12114 375 LEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDG----TPIAPDALRAFLAQTL 449
|
490 500
....*....|....*....|....*...
gi 564330613 546 APYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd12114 450 PAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
86-539 |
1.86e-22 |
|
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: 100.51 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ItddtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcVDTKHNELMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd17640 82 V-------------------------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 FGLGLSvngRFW--LDLIASDVMWntsdtgwaksawsSVFSPW--TQGAC---VFA-----HYlprfdsTSI---LQTLS 310
Cdd:cd17640 113 LLHQIR---SLSdiVPPQPGDRFL-------------SILPIWhsYERSAeyfIFAcgcsqAY------TSIrtlKDDLK 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 311 KFPITVFCSAPTAYRML---IQNDITRSYKF-----------NSLKHCVSAGEPINPEVmEQWKKKTGLDIYEGYGQTET 376
Cdd:cd17640 171 RVKPHYIVSVPRLWESLysgIQKQVSKSSPIkqflflfflsgGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTET 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 377 --VLICGNFKGMKIkpGSMGKPSPAFNVEILDENG-TILPPGQEGDIAV---QVLpdrpfglfTHYVDNPSKTASTLRGN 450
Cdd:cd17640 250 spVVSARRLKCNVR--GSVGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVrgpQVM--------KGYYKNPEATSKVLDSD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 451 -FYITGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIaESAVVSSPDPIRgevVKAFIVlnPDYklh 528
Cdd:cd17640 320 gWFNTGDLGWLTCGGELVLTGRAKDTIvLSNGENVEPQPIEEALMRSPFI-EQIMVVGQDQKR---LGALIV--PNF--- 390
|
490
....*....|.
gi 564330613 529 dqEQLKKEIQE 539
Cdd:cd17640 391 --EELEKWAKE 399
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-575 |
1.90e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.73 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 86 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAkcenlhskLIVSQHSREGWgnlkemMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK12316 2105 LTQRHLLERLPLPAG--------VARLPLDRDAE------WADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGA 2170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 246 FGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFcSAPTAYR 325
Cdd:PRK12316 2171 LVAHCQAAGERY-ELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTIL-DFPPVYL 2247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 326 MLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGYGQTETVLICGNFKGMKIKPGS-----MGKPSPA 399
Cdd:PRK12316 2248 QQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGN 2327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 400 FNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDEDGYFWFVAR 471
Cdd:PRK12316 2328 RRAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGR 2402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 472 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRGEVVKAFIVlnPDyklHDQEQLKKEIQEHVKKTTAPYKYP 551
Cdd:PRK12316 2403 IDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PD---DAAEDLLAELRAWLAARLPAYMVP 2476
|
490 500
....*....|....*....|....
gi 564330613 552 RKIEFIEELPKTVSGKVKRNELRR 575
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
210-577 |
5.95e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 210 SDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQG 289
Cdd:PRK12467 1707 SDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADVVLQFTSFAFDVSVWE-LFWPLING 1784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 290 A-CVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDiTRSYKFNSLKHCVSAGEPINPEVMEQWKKKTG-LDI 367
Cdd:PRK12467 1785 ArLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD-EQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGL 1863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 368 YEGYGQTETVL-----IC--GNFKGMKIKPgsMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNP 440
Cdd:PRK12467 1864 FNLYGPTETAVdvthwTCrrKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGELYLGGV-----GLARGYLNRP 1936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 441 SKTA--------STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRG 512
Cdd:PRK12467 1937 ALTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANG 2015
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564330613 513 EVVKAFIVLNPDYKLHD---QEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 577
Cdd:PRK12467 2016 KQLVAYVVPTDPGLVDDdeaQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPD 2083
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
226-580 |
1.09e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 97.80 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFWLD-----LIASDVmwnTSDTGWAksawSSVFSPWTQGA--CVFAHYL 297
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDREIeAYNEALNCEqdetpIVACPV---THSYGLI----CGVLAALTRGSkpVIITNKN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 298 PRFdstsILQTLSKFPITVFCSAPTAYRMLI---QNDITrsykFNSLkhcVSAGEPINPEVMEQWKKKTgLDIYEGYGQT 374
Cdd:PRK08308 179 PKF----ALNILRNTPQHILYAVPLMLHILGrllPGTFQ----FHAV---MTSGTPLPEAWFYKLRERT-TYMMQQYGCS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 375 ET--VLICGNFKgmkiKPGSMGKPSPAFNVEI-LDENgtilppgqegdiavqvlpdrpfglfthyvdNPSKTASTLRGNF 451
Cdd:PRK08308 247 EAgcVSICPDMK----SHLDLGNPLPHVSVSAgSDEN------------------------------APEEIVVKMGDKE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 452 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYklhDQE 531
Cdd:PRK08308 293 IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI---DPV 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 564330613 532 QLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTT 580
Cdd:PRK08308 370 QLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
226-570 |
3.07e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 97.27 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHTHSS-----------FGLGlsvNGRFWL-------DLiasDVMwntsdtgwaksawsSVFSPWT 287
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNlvsftnwmledFALP---EGPQFLnqapysfDL---SVM--------------DLYPTLA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 288 QGACVFAhyLPRfDSTS----ILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKK- 362
Cdd:PRK04813 208 SGGTLVA--LPK-DMTAnfkqLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERf 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 363 TGLDIYEGYGQTE-TVLIcgnfKGMKI--------KPGSMGKPSPAFNVEILDENGTILPPGQEGDI-----AVQVlpdr 428
Cdd:PRK04813 285 PSATIYNTYGPTEaTVAV----TSIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIvisgpSVSK---- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 429 pfGlfthYVDNPSKTAS---TLRGN-FYITGDRGYMDeDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVV 504
Cdd:PRK04813 357 --G----YLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564330613 505 sspdPI-RGEVVK---AFIVLNPdyklHDQE---QLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 570
Cdd:PRK04813 430 ----PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
75-575 |
4.53e-21 |
|
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: 96.92 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 75 PAFWWVD-GNGKEVRWSFEELGSLSRKFANILTEACslQRGDRVMVILPKIPEWWLANVACLRTGTV---LIPGTTQLTQ 150
Cdd:cd05931 10 PAYTFLDdEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPPPTPGRHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 151 KDILYRLQSSKSKCIITDDTLAPAV-DIVAAKCENLHSKLIVSQHSREGwgnlkemmkyASDSHTCVDTKHNELMAIYFT 229
Cdd:cd05931 88 ERLAAILADAGPRVVLTTAAALAAVrAFAASRPAAGTPRLLVVDLLPDT----------SAADWPPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 230 SGTTGPPK--MIGHthssfgLGLSVNgrfwLDLIASDVMWNTSDTGwakSAW----------SSVFSPWTQGA-CVF--- 293
Cdd:cd05931 158 SGSTGTPKgvVVTH------RNLLAN----VRQIRRAYGLDPGDVV---VSWlplyhdmgliGGLLTPLYSGGpSVLmsp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 294 AHYL--P-RFdstsiLQTLSKFPITvFCSAPT-AYRML---IQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKK---T 363
Cdd:cd05931 225 AAFLrrPlRW-----LRLISRYRAT-ISAAPNfAYDLCvrrVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAfapF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 364 GLD---IYEGYGQTE-TVLICGNFKG------------------MKIKPG-------SMGKPSPAFNVEILDENG-TILP 413
Cdd:cd05931 299 GFRpeaFRPSYGLAEaTLFVSGGPPGtgpvvlrvdrdalagravAVAADDpaarelvSCGRPLPDQEVRIVDPETgRELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 414 PGQEGDIAVQ---VLPdrpfGlfthYVDNPSKTASTLR-------GNFYITGDRGYMDeDGYFWFVARSDDVILSSGYRI 483
Cdd:cd05931 379 DGEVGEIWVRgpsVAS----G----YWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 484 GPFEVESALIE-HPSIAES--AVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQ-----EH-VKkttapykyPRKI 554
Cdd:cd05931 450 YPQDIEATAEEaHPALRPGcvAAFSVPDDGEERLVVVAEVERGADPA-DLAAIAAAIRaavarEHgVA--------PADV 520
|
570 580
....*....|....*....|...
gi 564330613 555 EFIE--ELPKTVSGKVKRNELRR 575
Cdd:cd05931 521 VLVRpgSIPRTSSGKIQRRACRA 543
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
284-574 |
5.16e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 96.22 E-value: 5.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 284 SPWTQGACVFAHYlPRFDSTsilQTLSKFPITVFCS-APTAYRMLIQNDITRSYKFNSLkhcVSAGEPINPEVMEQwKKK 362
Cdd:PRK07445 181 SFLTGGKLVILPY-KRLKSG---QELPPNPSDFFLSlVPTQLQRLLQLRPQWLAQFRTI---LLGGAPAWPSLLEQ-ARQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 363 TGLDIYEGYGQTETV-LICgnfkgmKIKPG-------SMGKPSPAFNVEIldengtilPPGQEGDIAVQVlPDRPFGLFT 434
Cdd:PRK07445 253 LQLRLAPTYGMTETAsQIA------TLKPDdflagnnSSGQVLPHAQITI--------PANQTGNITIQA-QSLALGYYP 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 435 HYVDNPsktastlrgNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEV 514
Cdd:PRK07445 318 QILDSQ---------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEV 388
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 515 VKAFIVLNpdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PRK07445 389 VTAIYVPK------DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
90-573 |
1.30e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 93.57 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 90 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 169
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 170 TLAPAVDIVaakcenlhSKLIVSQHSREGWGNLKEMMKYASDSHTCVdtkhnelmaIYFTSGTTGPPK--MIGHThssfg 247
Cdd:PRK10252 564 DQLPRFADV--------PDLTSLCYNAPLAPQGAAPLQLSQPHHTAY---------IIFTSGSTGRPKgvMVGQT----- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 248 lgLSVNGRFWLD----LIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVF-----AHYlprfDSTSILQTLSKFPITV-- 316
Cdd:PRK10252 622 --AIVNRLLWMQnhypLTADDVVLQKTPCSFDVSVWE-FFWPFIAGAKLVmaepeAHR----DPLAMQQFFAEYGVTTth 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 317 --------FCSAPTayrmliQNDITRSYKfnSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVL------ICG- 381
Cdd:PRK10252 695 fvpsmlaaFVASLT------PEGARQSCA--SLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdvswypAFGe 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 382 ---NFKGMKIKPGSmgkpsPAFN--VEILDENGTILPPGQEGDI---AVQvlpdrpfgLFTHYVDNPSKTASTLRGN--- 450
Cdd:PRK10252 767 elaAVRGSSVPIGY-----PVWNtgLRILDARMRPVPPGVAGDLyltGIQ--------LAQGYLGRPDLTASRFIADpfa 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 451 ----FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA----VVSSPDPIRGEVVK--AFIV 520
Cdd:PRK10252 834 pgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGDARQlvGYLV 913
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 564330613 521 LNPDYKLhDQEQLkkeiQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:PRK10252 914 SQSGLPL-DTSAL----QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
216-573 |
1.66e-19 |
|
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: 91.31 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 216 VDTKHNELMAIYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFWLDLIASDVMwntsdtgwaksawsSVFSPWtqgacVF 293
Cdd:cd17648 89 VITNSTDLAYAIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAV--------------LFFSNY-----VF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 294 AHYLPRFdSTSIL--QTLSKFPITVFCSAPTAYRMLIQNDIT---------RSYKF---NSLKHCVSAGEPINPEVMEQW 359
Cdd:cd17648 149 DFFVEQM-TLALLngQKLVVPPDEMRFDPDRFYAYINREKVTylsgtpsvlQQYDLarlPHLKRVDAAGEEFTAPVFEKL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 360 KKKTGLDIYEGYGQTETVL--ICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGD-------IAVQVLpDRPF 430
Cdd:cd17648 228 RSRFAGLIINAYGPTETTVtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGElylggdgVARGYL-NRPE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 431 GLFTHYVDNPSKTAS-TLRGNF---YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSS 506
Cdd:cd17648 307 LTAERFLPNPFQTEQeRARGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564330613 507 PDP-IRGEVVKAFIVlnpDYKLHDQEQL-KKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17648 387 EDAsQAQSRIQKYLV---GYYLPEPGHVpESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
51-574 |
1.54e-18 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 89.37 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 51 YFNFAKDVLdqwtnTEKTGKRLSNPAFWWVD--GNGKEV-RWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEW 127
Cdd:PLN03052 173 VLNVAECCL-----TPKPSKTDDSIAIIWRDegSDDLPVnRMTLSELRSQVSRVANAL-DALGFEKGDAIAIDMPMNVHA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 128 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTL-----------------APAVDIVAAKCENLHSKLi 190
Cdd:PLN03052 247 VIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplysrvveakAPKAIVLPADGKSVRVKL- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 191 vsqhsREGWGNLKEMMKYAS-----DSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGRFWLDLIASDV 265
Cdd:PLN03052 326 -----REGDMSWDDFLARANglrrpDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 266 M-WNTsDTGWAKSAWsSVFSPWTQGACvfahyLPRFDSTSILQTLSKF----PITVFCSAPTAYRMLIQNDITRSYKFNS 340
Cdd:PLN03052 400 VcWPT-NLGWMMGPW-LVYASLLNGAT-----LALYNGSPLGRGFAKFvqdaKVTMLGTVPSIVKTWKNTNCMAGLDWSS 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 341 LKHCVSAGEPINPE----VMEQWKKKTgldIYEGYGQTEtvlICGNF-KGMKIKPGSMGK---PSPAFNVEILDENGTIL 412
Cdd:PLN03052 473 IRCFGSTGEASSVDdylwLMSRAGYKP---IIEYCGGTE---LGGGFvTGSLLQPQAFAAfstPAMGCKLFILDDSGNPY 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 413 PPGQEGDIAVqvlpdrpfGLFTHYVDNPSKTASTLRGNFYITGD--------RGYMDE-----DGYFWFVARSDDVIlss 479
Cdd:PLN03052 547 PDDAPCTGEL--------ALFPLMFGASSTLLNADHYKVYFKGMpvfngkilRRHGDIfertsGGYYRAHGRADDTM--- 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 480 gyRIGPFEVESALIE------HPSIAESAVVSSPDPIRG--EVVKAFIVLNPDYKLHDQEQLKKEIQEHVKKTTAPYKYP 551
Cdd:PLN03052 616 --NLGGIKVSSVEIErvcnaaDESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKV 693
|
570 580
....*....|....*....|...
gi 564330613 552 RKIEFIEELPKTVSGKVKRNELR 574
Cdd:PLN03052 694 SAVVIVPSFPRTASNKVMRRVLR 716
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
218-573 |
4.84e-18 |
|
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: 86.75 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 218 TKHNELMAIYFTSGTTGPPK--MIGH---THSSFGL-------GLSVN----GRFWLDLIASDvmwntsdtgWAKSAWS- 280
Cdd:cd17650 90 TQPEDLAYVIYTSGTTGKPKgvMVEHrnvAHAAHAWrreyeldSFPVRllqmASFSFDVFAGD---------FARSLLNg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 281 SVFSPWTQGAcvfahylpRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEpinpEVMEQWK 360
Cdd:cd17650 161 GTLVICPDEV--------KLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSD----GCKAQDF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 361 K------KTGLDIYEGYGQTETVLICGNFK-GMKIKPGS----MGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrP 429
Cdd:cd17650 229 KtlaarfGQGMRIINSYGVTEATIDSTYYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIG-----G 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 430 FGLFTHYVDNPSKTASTLR-------GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA 502
Cdd:cd17650 304 AGVARGYLNRPELTAERFVenpfapgERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAV 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564330613 503 VVSSPDPiRGEV-VKAFIVlnPDYKLHdqeqlKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17650 384 VAVREDK-GGEArLCAYVV--AAATLN-----TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
89-570 |
5.22e-18 |
|
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: 87.48 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 89 WSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 168
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 169 DTlaPAVDIVAAKCENLHS--KLIVS--------QHSREGW-GNLKEMMKYASDSHTCV------DTKHNELMAIYFTSG 231
Cdd:cd17641 91 DE--EQVDKLLEIADRIPSvrYVIYCdprgmrkyDDPRLISfEDVVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 232 TTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACV-FAHylprfDSTSILQTLS 310
Cdd:cd17641 169 TTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVnFPE-----EPETMMEDLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 311 KFPITVFCSAP------------------------------TAYRMLIQND-------------------ITRSYK---- 337
Cdd:cd17641 243 EIGPTFVLLPPrvwegiaadvrarmmdatpfkrfmfelgmkLGLRALDRGKrgrpvslwlrlaswladalLFRPLRdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 338 FNSLKHCVSAGEPINPEVMeQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEIlDENGTILPPGQe 417
Cdd:cd17641 323 FSRLRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVGEILVRSP- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 418 gdiavqvlpdrpfGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDV-ILSSGYRIGPFEVESALIEH 495
Cdd:cd17641 400 -------------GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 496 PSIAESAVVSSPDPIrgevVKAFIVLNP---------------DYK-LHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEE 559
Cdd:cd17641 467 PYIAEAVVLGAGRPY----LTAFICIDYaivgkwaeqrgiaftTYTdLASRPEVYELIRKEVEKVNASLPEAQRIRRFLL 542
|
570 580
....*....|....*....|
gi 564330613 560 LPK---------TVSGKVKR 570
Cdd:cd17641 543 LYKeldaddgelTRTRKVRR 562
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
45-567 |
1.79e-17 |
|
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: 85.79 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 45 KIEIPEYF-----NFAKDVLdqwtntekTGKRLSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMV 119
Cdd:cd05943 58 IMPGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 120 ILPKIPEwwlANVACLRT---GTVLIPGTTQLTQKDILYRLQSSKSKCIITDDT---------LAPAVDIVAAKCENLHS 187
Cdd:cd05943 129 YLPNIPE---AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPSLLA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 188 KLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNEL----------MAIYFTSGTTGPPKMIghTHSSFGLGLSVNGRFW 257
Cdd:cd05943 206 VVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGELefeplpfdhpLYILYSSGTTGLPKCI--VHGAGGTLLQHLKEHI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 258 L--DLIASDVM-WNTSdTGWAksAWSSVFSPWTQGA-CVFAHYLPRFDSTSILQTL-SKFPITVFCSAPTAYRMLIQNDI 332
Cdd:cd05943 284 LhcDLRPGDRLfYYTT-CGWM--MWNWLVSGLAVGAtIVLYDGSPFYPDTNALWDLaDEEGITVFGTSAKYLDALEKAGL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 333 T--RSYKFNSLKHCVSAGEPINPE----VMEQWKKktGLDIYEGYGQTEtvlICGNFKGMK----IKPGSMGKPSPAFNV 402
Cdd:cd05943 361 KpaETHDLSSLRTILSTGSPLKPEsfdyVYDHIKP--DVLLASISGGTD---IISCFVGGNpllpVYRGEIQCRGLGMAV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 403 EILDENGTILPpGQEGD-IAVQVLPDRPfglfTHYVDNPSktASTLRGNFYIT-------GDRGYMDEDGYFWFVARSDD 474
Cdd:cd05943 436 EAFDEEGKPVW-GEKGElVCTKPFPSMP----VGFWNDPD--GSRYRAAYFAKypgvwahGDWIEITPRGGVVILGRSDG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 475 VILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdQEQLKKEIQEHVKKTTAPYKYPRKI 554
Cdd:cd05943 509 TLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVEL--DDELRKRIRSTIRSALSPRHVPAKI 586
|
570
....*....|...
gi 564330613 555 EFIEELPKTVSGK 567
Cdd:cd05943 587 IAVPDIPRTLSGK 599
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
88-508 |
2.79e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 85.31 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTV--LIpgTTQLTQKDILYRLQSSKSKCI 165
Cdd:PRK08279 62 SISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVvaLL--NTQQRGAVLAHSLNLVDAKHL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 166 ITDDTLAPAVDIVAAKCENLHSKLIVSQ---HSREGWGNLKEMMKyASDSHTCVDTKH--NELMAIY-FTSGTTGPPKMI 239
Cdd:PRK08279 139 IVGEELVEAFEEARADLARPPRLWVAGGdtlDDPEGYEDLAAAAA-GAPTTNPASRSGvtAKDTAFYiYTSGTTGLPKAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 240 GHTH-----SSFGLGLSvngrfwLDLIASDVMWNT----SDTGwAKSAWSSVFSPwtqGACVFAHylPRFDSTSILQTLS 310
Cdd:PRK08279 218 VMSHmrwlkAMGGFGGL------LRLTPDDVLYCClplyHNTG-GTVAWSSVLAA---GATLALR--RKFSASRFWDDVR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 311 KFPITVFCsaptaY-----RMLIQNDITRSYKFNSLKHCVSAGepINPEVMEQWKKKTGLD-IYEGYGQTE--TVLIcgN 382
Cdd:PRK08279 286 RYRATAFQ-----YigelcRYLLNQPPKPTDRDHRLRLMIGNG--LRPDIWDEFQQRFGIPrILEFYAASEgnVGFI--N 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 383 FKGmkiKPGSMGKpSPAFN------VEILDENGTIL----------PPGQEGDIAVQVLPDRPfglFTHYVDnPSKT-AS 445
Cdd:PRK08279 357 VFN---FDGTVGR-VPLWLahpyaiVKYDVDTGEPVrdadgrcikvKPGEVGLLIGRITDRGP---FDGYTD-PEASeKK 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330613 446 TLRGNF------YITGDRGYMDEDGYFWFVARSDDVilssgYR-----IGPFEVESALIEHPSIAESAV--VSSPD 508
Cdd:PRK08279 429 ILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDT-----FRwkgenVATTEVENALSGFPGVEEAVVygVEVPG 499
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
88-575 |
5.94e-17 |
|
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: 83.63 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIpgTTQLTQKDILYRLQSSKSKC 164
Cdd:cd05939 3 HWTFRELNEYSNKVANFF-QAQGYRSGDVVALFMENRLEFvalWLG-LAKIGVETALI--NSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 165 IITDdtlapavdivaakcenlHSKLIVSQHSREgwgnlkemmkyasdSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05939 79 LIFN-----------------LLDPLLTQSSTE--------------PPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 245 SFgLGLSVNGRFWLDLIASDVMWNTsdtgwaKSAWSSVFSPWTQGACVFahylprFDSTSILQtlSKFPITVFCSAPTAY 324
Cdd:cd05939 128 RY-YRIAAGAYYAFGMRPEDVVYDC------LPLYHSAGGIMGVGQALL------HGSTVVIR--KKFSASNFWDDCVKY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 325 RMLIQNDI--------TRSYKFNSLKHCV--SAGEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNFKG-------- 385
Cdd:cd05939 193 NCTIVQYIgeicryllAQPPSEEEQKHNVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLVNIDNhvgacgfn 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 386 ----MKIKPGSMGKPSPAFNVEILDENGTILP--PGQEGDIAVQVLPDRPFGLFTHYVDNPSKTASTLRGNF------YI 453
Cdd:cd05939 273 srilPSVYPIRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFkkgdsaFL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 454 TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKAFIVlNPDYKLhDQE 531
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIV-DPERKV-DLD 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 564330613 532 QLKKEIQehvkKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:cd05939 430 RFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
221-573 |
3.96e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.52 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 221 NELMAIYFTSGTTGPPKmighthssfglGLSVNGRF----------WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTqGA 290
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPK-----------GVMVEQRGmlnnqlskvpYLALSEADVIAQTASQSFDISVWQFLAAPLF-GA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 291 CV------FAHylprfDSTSILQTLSKFPITVFCSAPT-AYRMLIQNDITrsykFNSLKHCVSAGEPINPEVMEQW-KKK 362
Cdd:PRK05691 3937 RVeivpnaIAH-----DPQGLLAHVQAQGITVLESVPSlIQGMLAEDRQA----LDGLRWMLPTGEAMPPELARQWlQRY 4007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 363 TGLDIYEGYGQTETVLICGNFK-GMKIKPGS---MGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVD 438
Cdd:PRK05691 4008 PQIGLVNAYGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVG 4082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 439 NPSKTASTLRGN--------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPi 510
Cdd:PRK05691 4083 DPLRTALAFVPHpfgapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV- 4161
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564330613 511 RGEVVKAFIVlnPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:PRK05691 4162 NGKHLVGYLV--PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-504 |
4.35e-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: 80.97 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 218 TKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLsvngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSPwtqgACVFAHYL 297
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQI--------DALRQLYGIRPGEVDLATFPLFALFGP----ALGLTSVI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 298 PRFDSTS--------ILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKK--KTGLDI 367
Cdd:cd05910 150 PDMDPTRparadpqkLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKmlSDEAEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 368 YEGYGQTETVLICG-------NFKGMKIKPGS---MGKPSPAFNVEILD---------ENGTILPPGQEGDIAV---QVL 425
Cdd:cd05910 230 LTPYGATEALPVSSigsrellATTTAATSGGAgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVtgpTVT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 426 PDrpfglfthYVDNPSKTA----STLRGNF-YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:cd05910 310 PT--------YVNRPVATAlakiDDNSEGFwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRR 381
|
....
gi 564330613 501 SAVV 504
Cdd:cd05910 382 SALV 385
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
121-574 |
1.37e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 79.47 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 121 LPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTL----------------APAVDIV-AAKCE 183
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVlrggralplyskvveaAPAKAIVlPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 184 NLHSKLivsqhsREGWGNLKEMMKYASDSHtCVDTKHNE--------LMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGR 255
Cdd:PLN03051 81 PVAVPL------REQDLSWCDFLGVAAAQG-SVGGNEYSpvyapvesVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 256 FWLDLIASDVM-WNTSdTGWAKSAWsSVFSPWTQGACVfAHYLPRFDSTSILQTLSKFPITVFCSAPTayrmliqndITR 334
Cdd:PLN03051 153 AHMDIQPGDVVcWPTN-LGWMMGPW-LLYSAFLNGATL-ALYGGAPLGRGFGKFVQDAGVTVLGLVPS---------IVK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 335 SYK-----------FNSLKHCVSAGEPINPE------VMEQWKKKT-----GLDIYEGYGQTETVLICGnfkgmkikPGS 392
Cdd:PLN03051 221 AWRhtgafamegldWSKLRVFASTGEASAVDdvlwlsSVRGYYKPVieycgGTELASGYISSTLLQPQA--------PGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 393 MGKPSPAFNVEILDENGTILPPGQE--GDIAVQVL----PDRpfgLF------THYVDNP--SKTASTLRGNfyitGDRG 458
Cdd:PLN03051 293 FSTASLGTRFVLLNDNGVPYPDDQPcvGEVALAPPmlgaSDR---LLnadhdkVYYKGMPmyGSKGMPLRRH----GDIM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 459 YMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIE-HPSIAESAVVSSPDPIRGE----VVKAFIVLNPDYKLHDQEQL 533
Cdd:PLN03051 366 KRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEAL 445
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 564330613 534 KKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 574
Cdd:PLN03051 446 QKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
220-580 |
2.31e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.21 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 220 HNELMAIYfTSGTTGPPKMIGHTHSSFGLGLSvngrfWLD----LIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFA 294
Cdd:PRK05691 1273 DNLAYVIY-TSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVLMQKAPISFDVSVWE-CFWPLITGCrLVLA 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 295 HYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNdiTRSYKFNSLKHCVSAGEPINPE----VMEQWKkktGLDIYEG 370
Cdd:PRK05691 1346 GPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE--PLAAACTSLRRLFSGGEALPAElrnrVLQRLP---QVQLHNR 1420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 371 YGQTETVL-----ICGNFKGMKikpGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA- 444
Cdd:PRK05691 1421 YGPTETAInvthwQCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGA-----GLARGYLGRPALTAe 1492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 445 -------STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVsspdpIRGEVVKA 517
Cdd:PRK05691 1493 rfvpdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGA 1567
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564330613 518 FIV--LNPDYKLHDQ-EQLKKEIQEHVKKttapYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTT 580
Cdd:PRK05691 1568 QLVgyYTGEAGQEAEaERLKAALAAELPE----YMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ 1629
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
81-573 |
3.86e-15 |
|
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: 77.90 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 81 DGNGKEVRWSFEELGSLSRKFANILTEacSLQRGDRVMVI-LPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd17654 9 DQTTSDTTVSYADLAEKISNLSNFLRK--KFQTEERAIGLrCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 160 SKSKCIITDdtlapavdivaakCENLHSKLivsqhsregwgnlkemmkYASDSHTCVDTKHNELMA-IYFTSGTTGPPKM 238
Cdd:cd17654 87 CHVSYLLQN-------------KELDNAPL------------------SFTPEHRHFNIRTDECLAyVIHTSGTTGTPKI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 239 IGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAwSSVFSPWTQGACVFAHYLPRFDSTSILQTL--SKFPITV 316
Cdd:cd17654 136 VAVPHKCI-LPNIQHFRSLFNITSEDILFLTSPLTFDPSV-VEIFLSLSSGATLLIVPTSVKVLPSKLADIlfKRHRITV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 317 FCSAPTAYRMLIQNDITRSY--KFNSLKHCVSAGEPInPE--VMEQWKKK-TGLDIYEGYGQTETVlICGNFKGMKIK-- 389
Cdd:cd17654 214 LQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPF-PSlvILSSWRGKgNRTRIFNIYGITEVS-CWALAYKVPEEds 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 390 PGSMGKPSPAFNVEILDENGTiLPPGQ---EGDIAVQVLPDrpfglfthYVDNPsktastlRGNFYITGDRGYMdEDGYF 466
Cdd:cd17654 292 PVQLGSPLLGTVIEVRDQNGS-EGTGQvflGGLNRVCILDD--------EVTVP-------KGTMRATGDFVTV-KDGEL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 467 WFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDpirgEVVKAFIVLnpdyklhdqEQLKKEIQEHVKKTT- 545
Cdd:cd17654 355 FFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVG---------ESSSSRIHKELQLTLl 421
|
490 500
....*....|....*....|....*...
gi 564330613 546 APYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17654 422 SSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-573 |
1.86e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.13 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYfTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWaKSAWSSVFSPWTQGACVFAHYLPRFDSTS 304
Cdd:PRK05691 2339 IY-TSGSTGKPKGVVVSHGEIAMHCqAVIERF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQGQWGAEE 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 305 ILQTLSKFPITVFCSAPTAYRMLIQNDITRsYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGYGQTETV---LIC 380
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQWLAGQ-GEQLPVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTETVvmpLAC 2493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 381 GNFKGMKIKPGS--MGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA--------STLRGN 450
Cdd:PRK05691 2494 LAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGR 2568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 451 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP----IRGEVVKAFIVLNPDyk 526
Cdd:PRK05691 2569 LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPsgkqLAGYLVSAVAGQDDE-- 2646
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 564330613 527 lhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:PRK05691 2647 --AQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
225-568 |
1.90e-14 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 76.93 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 225 AIYFTSGTTGPPKMIGHTHSSFglgLS----VNGRfwLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRF 300
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLSHRNL---LAnraqVAAR--IDFSPEDKVFNA---------------------------LPVF 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 301 DS---TS--ILQTLSKFPITVFCSaPTAYR------------MLIQND--------ITRSYKFNSLKHCVSAGEPINPEV 355
Cdd:PRK06814 845 HSfglTGglVLPLLSGVKVFLYPS-PLHYRiipeliydtnatILFGTDtflngyarYAHPYDFRSLRYVFAGAEKVKEET 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 356 MEQWKKKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFN-----VEILDENGTILPPGqegdiavqvlPDR 428
Cdd:PRK06814 924 RQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEyrlepVPGIDEGGRLFVRG----------PNV 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 429 PFGlfthYV--DNPSkTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSS 506
Cdd:PRK06814 992 MLG----YLraENPG-VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSI 1066
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564330613 507 PDPIRGEVvkafIVLnpdykLHDQEQLKKE-IQEHVKKTTAPYKY-PRKIEFIEELPKTVSGKV 568
Cdd:PRK06814 1067 PDARKGER----IIL-----LTTASDATRAaFLAHAKAAGASELMvPAEIITIDEIPLLGTGKI 1121
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
221-576 |
2.40e-14 |
|
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: 75.60 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 221 NELMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRfwldLIASDVMWNTSDT--GWAksawssvfsPWTQG--------A 290
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHEN----LVHNMF----AILNSTEWKTKDRilSWM---------PLTHDmgliafhlA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 291 CVFAHYLPRFDSTSI--------LQTLSKFPITVFCSAPTAYRMLI---QNDITRSYKFNSLKHCVSAGEPINPEVMEQW 359
Cdd:cd05908 169 PLIAGMNQYLMPTRLfirrpilwLKKASEHKATIVSSPNFGYKYFLktlKPEKANDWDLSSIRMILNGAEPIDYELCHEF 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 360 KK---KTGLD---IYEGYGQTE-TVLICGNFKGMKIKPG---------------------------SMGKPSPAFNVEIL 405
Cdd:cd05908 249 LDhmsKYGLKrnaILPVYGLAEaSVGASLPKAQSPFKTItlgrrhvthgepepevdkkdsecltfvEVGKPIDETDIRIC 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 406 DENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN-FYITGDRGYMdEDGYFWFVARSDDVILSSGYRIG 484
Cdd:cd05908 329 DEDNKILPDGYIGHIQI-----RGKNVTPGYYNNPEATAKVFTDDgWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVY 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 485 PFEVESALIEHPSIAESAVVS---SPDPIRGEVVKAFIVLNPdyKLHDQEQLKKEIQEHVKKTTApyKYPRKIEFIEELP 561
Cdd:cd05908 403 PHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRK--SEDDFYPLGKKIKKHLNKRGG--WQINEVLPIRRIP 478
|
410
....*....|....*
gi 564330613 562 KTVSGKVKRNELRRK 576
Cdd:cd05908 479 KTTSGKVKRYELAQR 493
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
88-563 |
3.60e-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: 75.41 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSKSKC 164
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 165 IITDDTLAPAVDIV--AAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELM---AIY-FTSGTTGPPK- 237
Cdd:cd05938 82 LVVAPELQEAVEEVlpALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIkspALYiYTSGTTGLPKa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 238 -MIGHTHSSFGLG-LSVNGrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAhylPRFDSTSILQTLSKFPI 314
Cdd:cd05938 162 aRISHLRVLQCSGfLSLCG-----VTADDVIYITLPLYHSSGFLLGIGGCIELGAtCVLK---PKFSASQFWDDCRKHNV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 315 TVF----------CSAPtayrmliQNDITRSYKFNslkhcVSAGEPINPEVMEQWKKKTG-LDIYEGYGQTETVLICGNF 383
Cdd:cd05938 234 TVIqyigellrylCNQP-------QSPNDRDHKVR-----LAIGNGLRADVWREFLRRFGpIRIREFYGSTEGNIGFFNY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 384 KGmkiKPGSMGKPS-------P----AFNVE----ILDENGTILP--PGQEGDIAVQVLPDRPfglFTHYVDNPSKTAST 446
Cdd:cd05938 302 TG---KIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQSP---FLGYAGDKEQTEKK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 447 L------RGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKA 517
Cdd:cd05938 376 LlrdvfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-HEGRIGMA 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 564330613 518 FIVLNPDYKLhDQEQLkkeiQEHVKKTTAPYKYPRKIEFIEELPKT 563
Cdd:cd05938 455 AVKLKPGHEF-DGKKL----YQHVREYLPAYARPRFLRIQDSLEIT 495
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
452-575 |
7.15e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 73.16 E-value: 7.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 452 YITGDRGYMDeDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklHDQE 531
Cdd:PRK07824 236 FRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDG----GPAP 310
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564330613 532 QLkKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:PRK07824 311 TL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
88-575 |
9.38e-14 |
|
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: 73.54 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 88 RWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLtqkdilyRLQSskskciit 167
Cdd:cd05940 3 ALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNL-------RGES-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 168 ddtLAPAVDIVAAKcenlhsklivsqhsregwgnlkemmkyasdsHTCVDTkhneLMAIYfTSGTTGPPKMIGHTHSSFG 247
Cdd:cd05940 67 ---LAHCLNVSSAK-------------------------------HLVVDA----ALYIY-TSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 248 LGLSVNGrFWLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRFDSTSILQTLS-------------KFPI 314
Cdd:cd05940 108 RGGAFFA-GSGGALPSDVLYTC---------------------------LPLYHSTALIVGWSaclasgatlvirkKFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 315 TVFCSAPTAYR-MLIQ--NDITRsYKFNS------LKHCVSA--GEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGN 382
Cdd:cd05940 160 SNFWDDIRKYQaTIFQyiGELCR-YLLNQppkpteRKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFIN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 383 FKGmkiKPGSMG-------KPSPAFNVEILDENGTIL----------PPGQEGDIAVQVLPDRPFglfTHYVDNPSKTAS 445
Cdd:cd05940 239 FFG---KPGAIGrnpsllrKVAPLALVKYDLESGEPIrdaegrcikvPRGEPGLLISRINPLEPF---DGYTDPAATEKK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 446 TLRGNF------YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKA 517
Cdd:cd05940 313 ILRDVFkkgdawFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMA 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 564330613 518 FIVLNPDYKLhDQEQLKKeiqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 575
Cdd:cd05940 392 AIVLQPNEEF-DLSALAA----HLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
53-570 |
3.15e-13 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 72.52 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 53 NFAKDVLdqwtntekTGKRLSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEwwlANV 132
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 133 ACLRT---GTVLIPGTTQLTQKDILYRLQSSKSKCIITDD------TLAPAVDIVAAKCENLHS--KLIVSQHSREG--- 198
Cdd:PRK03584 155 AMLATaslGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggKAFDRRAKVAELRAALPSleHVVVVPYLGPAaaa 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 199 --------WGNLkeMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHssfG---------LGLSvngrfwLDLI 261
Cdd:PRK03584 235 aalpgallWEDF--LAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGH---GgillehlkeLGLH------CDLG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 262 ASD-VMWNTSdTGWAksAWSSVFSPWTQGACVfahYL----PRFDSTSIL-QTLSKFPITVFCSAPTAYRMLIQNDIT-- 333
Cdd:PRK03584 304 PGDrFFWYTT-CGWM--MWNWLVSGLLVGATL---VLydgsPFYPDPNVLwDLAAEEGVTVFGTSAKYLDACEKAGLVpg 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 334 RSYKFNSLKHCVSAGEPINPE----VMEQWKKktglDIY--EGYGQTEtvlICGNFKG----MKIKPGSMGKPSPAFNVE 403
Cdd:PRK03584 378 ETHDLSALRTIGSTGSPLPPEgfdwVYEHVKA----DVWlaSISGGTD---ICSCFVGgnplLPVYRGEIQCRGLGMAVE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 404 ILDENGTilpP--GQEGDIAV-QVLPDRPFGlFTHYVDNpsktaSTLRGNFYIT-------GDRGYMDEDGYFWFVARSD 473
Cdd:PRK03584 451 AWDEDGR---PvvGEVGELVCtKPFPSMPLG-FWNDPDG-----SRYRDAYFDTfpgvwrhGDWIEITEHGGVVIYGRSD 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 474 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqLKKEIQEHVKKTTAPYKYPRK 553
Cdd:PRK03584 522 ATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDA--LRARIRTTIRTNLSPRHVPDK 599
|
570 580
....*....|....*....|..
gi 564330613 554 IEFIEELPKTVSGK-----VKR 570
Cdd:PRK03584 600 IIAVPDIPRTLSGKkvelpVKK 621
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
125-575 |
9.43e-13 |
|
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: 70.71 E-value: 9.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTlapaVDIVAakcenlhsklivsqhsregwgnLKE 204
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAG----VKVYS----------------------LEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 205 MMK-YASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVmwntsdtgwaksawSSVF 283
Cdd:cd05927 97 FEKlGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGN---------------IVSNV--------------AGVF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 284 SPWTQGACVFAH-----YLP-----------------------RFDSTSILQTLSKFPITVFCSAPTAY-RML--IQNDI 332
Cdd:cd05927 148 KILEILNKINPTdvyisYLPlahifervvealflyhgakigfySGDIRLLLDDIKALKPTVFPGVPRVLnRIYdkIFNKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 333 TRS-------------YKFNSLKH---------------------------CVSAGEPINPEVMEQWKKKTGLDIYEGYG 372
Cdd:cd05927 228 QAKgplkrklfnfalnYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 373 QTETV-LICGNFKGMKIkPGSMGKPSPAFNVEILD--E-NGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLR 448
Cdd:cd05927 308 QTECTaGATLTLPGDTS-VGHVGGPLPCAEVKLVDvpEmNYDAKDPNPRGEVCI-----RGPNVFSGYYKDPEKTAEALD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 449 GN-FYITGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVvsspdpiRGEVVKAF----IVLN 522
Cdd:cd05927 382 EDgWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV-------YGDSLKSFlvaiVVPD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 523 PDY-------KLHDQ---------EQLKKEIQEHVKKTTA-----PYKYPRKI-----EFIEE---LpkTVSGKVKRNEL 573
Cdd:cd05927 455 PDVlkewaasKGGGTgsfeelcknPEVKKAILEDLVRLGKenglkGFEQVKAIhlepePFSVEnglL--TPTFKLKRPQL 532
|
..
gi 564330613 574 RR 575
Cdd:cd05927 533 KK 534
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
209-570 |
1.15e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 67.33 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 209 ASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHssfglglsvnGRFWLDL----------IASDVMwntsdtgwakSA 278
Cdd:PRK07768 140 AADPIDPVETGEDDLALMQLTSGSTGSPKAVQITH----------GNLYANAeamfvaaefdVETDVM----------VS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 279 WSSVF----------SPWTQGACVF----AHYLPrfDSTSILQTLSKFPITVFCSAPTAY----RMLIQNDITRSYKFNS 340
Cdd:PRK07768 200 WLPLFhdmgmvgfltVPMYFGAELVkvtpMDFLR--DPLLWAELISKYRGTMTAAPNFAYallaRRLRRQAKPGAFDLSS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 341 LKHCVSAGEPINPEVMEQW---KKKTGLD---IYEGYGQTETVLI-----CGNfkGMKI------------------KPG 391
Cdd:PRK07768 278 LRFALNGAEPIDPADVEDLldaGARFGLRpeaILPAYGMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKGN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 392 -----SMGKPSPAFNVEILDENGTILPPGQEGDIAVQ---VLPdrpfglftHYVDNPSKTASTLRGNFYITGDRGYMDED 463
Cdd:PRK07768 356 trrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRgesVTP--------GYLTMDGFIPAQDADGWLDTGDLGYLTEE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 464 GYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiRGEVVKAFIVLNPDYKLHDQE---QLKKEIQEH 540
Cdd:PRK07768 428 GEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAevrRIRHQVAHE 506
|
410 420 430
....*....|....*....|....*....|..
gi 564330613 541 VKKTTApyKYPRKIEFIE--ELPKTVSGKVKR 570
Cdd:PRK07768 507 VVAEVG--VRPRNVVVLGpgSIPKTPSGKLRR 536
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
226-567 |
5.81e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 62.03 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFA-----HY--LP 298
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypsplHYriVP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 299 R----------FDSTSILQTLSKFpitvfcsaptayrmliqndiTRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIY 368
Cdd:PRK08043 449 ElvydrnctvlFGTSTFLGNYARF--------------------ANPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRIL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 369 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILD----ENGTIL----PPGQEGDIAVQvlpdRPFGLFTHYVDNP 440
Cdd:PRK08043 509 EGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvpgiEQGGRLqlkgPNIMNGYLRVE----KPGVLEVPTAENA 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 441 sktASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVES-ALIEHPSiAESAVVSSPDPIRGEvvkAFI 519
Cdd:PRK08043 585 ---RGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD-KQHATAIKSDASKGE---ALV 657
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 564330613 520 VLNPDYKLHdQEQLKKEIQEHVKKTTApykYPRKIEFIEELPKTVSGK 567
Cdd:PRK08043 658 LFTTDSELT-REKLQQYAREHGVPELA---VPRDIRYLKQLPLLGSGK 701
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
125-504 |
2.63e-09 |
|
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: 60.06 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDtlAPAVDIVAAKCENL-HSKLIVsQHSRE------ 197
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN--QKQLQKILQIQDKLpHLKAII-QYKEPlkekep 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 198 ---GWGNLKEMMKYASDS--HTCVDT-KHNELMAIYFTSGTTGPPK--MIGHTHSSF-GLGLSVNGRF------------ 256
Cdd:cd05933 121 nlySWDEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKgvMLSHDNITWtAKAASQHMDLrpatvgqesvvs 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 257 WLDL--IASDVMwntsdtgwaksawsSVFSPWTQGACVfahYLPRFDST--SILQTLSKFPITVFCSAP----------- 321
Cdd:cd05933 201 YLPLshIAAQIL--------------DIWLPIKVGGQV---YFAQPDALkgTLVKTLREVRPTAFMGVPrvwekiqekmk 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 322 ------TAYRMLI---------------QNDITRSYKFN---------------SLKHCV---SAGEPINPEVMEQWkkk 362
Cdd:cd05933 264 avgaksGTLKRKIaswakgvgletnlklMGGESPSPLFYrlakklvfkkvrkalGLDRCQkffTGAAPISRETLEFF--- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 363 TGLDI--YEGYGQTE-----TVLICGNFKgmkikPGSMGKPSPAFNVEILDEN----GTILPPGQEgdiavqvlpdrpfg 431
Cdd:cd05933 341 LSLNIpiMELYGMSEtsgphTISNPQAYR-----LLSCGKALPGCKTKIHNPDadgiGEICFWGRH-------------- 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564330613 432 LFTHYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDD-VILSSGYRIGPFEVESALIEHPSIAESAVV 504
Cdd:cd05933 402 VFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVKKELPIISNAML 476
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
394-574 |
2.95e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.63 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 394 GKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMdEDGYFWFVARSD 473
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICV-----RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 474 DVILSSGYRIGPFEVESALIEHPSI--AESAVVSSPDPiRGEVVKAFI---VLNPDyklhDQEQLKKEIQEHVKKTTApy 548
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDEE----RRGQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*...
gi 564330613 549 kYPRKIEFI--EELPKTVSGKVKRNELR 574
Cdd:PRK09192 535 -VEAAVELVppHSLPRTSSGKLSRAKAK 561
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
342-578 |
1.19e-08 |
|
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: 57.44 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 342 KHCVSA--GEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP---------AFNVEILDENG 409
Cdd:cd05937 201 DHKVRVawGNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLirrwkfenqVVLVKMDPETD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 410 TIL-----------PPGQEGDIAVQVLPDrPFGLFTHYVDNPSKTASTL------RGN-FYITGDRGYMDEDGYFWFVAR 471
Cdd:cd05937 281 DPIrdpktgfcvraPVGEPGEMLGRVPFK-NREAFQGYLHNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDR 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 472 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP-IRGEVVKAFIVLNPDYKLHDQEQlKKEIQEHVKKTTAPYKY 550
Cdd:cd05937 360 LGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAVPTEFT-KSLLASLARKNLPSYAV 438
|
250 260
....*....|....*....|....*...
gi 564330613 551 PRKIEFIEELPKTVSGKVKRNELRRKEW 578
Cdd:cd05937 439 PLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
226-495 |
3.43e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 56.36 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 226 IYFTSGTTGPPKMIGHTHSSfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPrFDS 302
Cdd:PRK06334 188 ILFTSGTEKLPKGVPLTHAN----LLANQRACLKFFSpkeDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNP-LYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 303 TSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTE-TVLIC 380
Cdd:PRK06334 263 KKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfPHIQLRQGYGTTEcSPVIT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 381 GNFKGMKIKPGSMGKPSPAFNVEILDENGTI-LPPGQEGDIAVqvlpdRPFGLFTHYVDN-PSKTASTLRG-NFYITGDR 457
Cdd:PRK06334 343 INTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLT-----RGTSLFSGYLGEdFGQGFVELGGeTWYVTGDL 417
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564330613 458 GYMDEDGYFWFVARsddviLSSGYRIGPFEV-----ESALIEH 495
Cdd:PRK06334 418 GYVDRHGELFLKGR-----LSRFVKIGAEMVslealESILMEG 455
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
229-576 |
4.77e-08 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 55.71 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 229 TSGTTGPPKMIGHTHSSFglglsvngRFWLDLIA----------SDVMWNTsdTGwaksawssvFSPWTQGACvfAHY-L 297
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDL--------DVWAELVArcldaagvtpGDRVQNA--YG---------YGLFTGGLG--FHYgA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 298 PRFDSTSI----------LQTLSKFPITVFCSAPT--------AYRMLIqnDITRSykfnSLKHCVSAGEPINPEVMEQW 359
Cdd:cd05913 145 ERLGALVIpagggnterqLQLIKDFGPTVLCCTPSyalylaeeAEEEGI--DPREL----SLKVGIFGAEPWTEEMRKRI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 360 KKKTGLDIYEGYGQTE-----TVLICGNFKGMKIKpgsmgkpSPAFNVEILD-ENGTILPPGQEGDIavqvlpdrpfgLF 433
Cdd:cd05913 219 ERRLGIKAYDIYGLTEiigpgVAFECEEKDGLHIW-------EDHFIPEIIDpETGEPVPPGEVGEL-----------VF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 434 THYvdnpSKTASTLRgnFYITGD------------RGYMDEDGyfwFVARSDDVILSSGYRIGPFEVESALIEHPSIAES 501
Cdd:cd05913 281 TTL----TKEAMPLI--RYRTRDitrllpgpcpcgRTHRRIDR---ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPH 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 502 A--VVSSPDP-----IRGEVVKAFIVLNPDyklhdqEQLKKEIQEHVKKTTA--PykyprKIEFIE--ELPKTvSGKVKR 570
Cdd:cd05913 352 YqlILTRQEHldeltIKVEVRPEADDDEKL------EALKQRLERHIKSVLGvtV-----EVELVEpgSLPRS-EGKAKR 419
|
....*.
gi 564330613 571 NELRRK 576
Cdd:cd05913 420 VIDKRK 425
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
229-570 |
7.30e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 51.69 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 229 TSGTTGPPKMIGHTHSSFGLglsvngrfWLDLIA----------SDVMWNTsdTGwaksawssvFSPWTQGacVFAHY-L 297
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDR--------WAELFArslraagvrpGDRVQNA--FG---------YGLFTGG--LGLHYgA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 298 PRF----------DSTSILQTLSKFPITVFCSAPT--------AYRMLIqnDITRSykfnSLKHCVSAGEPInPEVMEQW 359
Cdd:COG1541 150 ERLgatvipagggNTERQLRLMQDFGPTVLVGTPSyllylaevAEEEGI--DPRDL----SLKKGIFGGEPW-SEEMRKE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 360 -KKKTGLDIYEGYGQTET-VLI---CGNFKGMKIKPGSmgkpspaFNVEILD-ENGTILPPGQEGDIavqvlpdrpfgLF 433
Cdd:COG1541 223 iEERWGIKAYDIYGLTEVgPGVayeCEAQDGLHIWEDH-------FLVEIIDpETGEPVPEGEEGEL-----------VV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 434 THYvdnpSKTASTL-RgnfYITGDRGYMDED---------------GyfwfvaRSDDVILSSGYRIGPFEVESALIEHPS 497
Cdd:COG1541 285 TTL----TKEAMPLiR---YRTGDLTRLLPEpcpcgrthprigrilG------RADDMLIIRGVNVFPSQIEEVLLRIPE 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564330613 498 IAESAVVSSPDPIRGEVVKAFIVLNPDYklhDQEQLKKEIQEHVKKTTapyKYPRKIEFIE--ELPKTVsGKVKR 570
Cdd:COG1541 352 VGPEYQIVVDREGGLDELTVRVELAPGA---SLEALAEAIAAALKAVL---GLRAEVELVEpgSLPRSE-GKAKR 419
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
111-517 |
8.49e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 52.02 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdiLY-RLQSSKSKCIITDDTLApAVDIVAAKCENLHS-- 187
Cdd:PLN02736 100 IPKGACVGLYFINRPEWLIVDHACSAYSYVSVP----------LYdTLGPDAVKFIVNHAEVA-AIFCVPQTLNTLLScl 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 188 ------KLIV----------SQHSREGwgnlKEMMKYA-------SDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHs 244
Cdd:PLN02736 169 seipsvRLIVvvggadeplpSLPSGTG----VEIVTYSkllaqgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTH- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 245 sfglglsvngrfwLDLIAS------DVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRF---DSTSILQTLSKFPIT 315
Cdd:PLN02736 244 -------------GNLIANvagsslSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFyqgDNLKLMDDLAALRPT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 316 VFCSAPTAYRMlIQNDITRSYK-------------FNSLKHC------------------------------VSAGEPIN 352
Cdd:PLN02736 311 IFCSVPRLYNR-IYDGITNAVKesgglkerlfnaaYNAKKQAlengknpspmwdrlvfnkikaklggrvrfmSSGASPLS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 353 PEVMEQWKKKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFNVEILDengtiLP---------PGQEGDIAV 422
Cdd:PLN02736 390 PDVMEFLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVD-----VPemnytsedqPYPRGEICV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 423 qvlpdRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAE 500
Cdd:PLN02736 464 -----RGPIIFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQ 538
|
490 500
....*....|....*....|....*...
gi 564330613 501 SAV-----------VSSPDPirgEVVKA 517
Cdd:PLN02736 539 CFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
217-573 |
5.97e-06 |
|
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: 49.14 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 217 DTKHNELMAIYFTSGTTGPPKMIGHTHSSF-----GLGLSVNGRFW--------------LDLIASDV--MWNT------ 269
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLvagiaGLGDRVPELLGpddrylaylplahiFELAAENVclYRGGtigygs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 270 ----SDTGWAKSAWS-SVFSPwTQGACVfahylPR-FDST-----SILQTLSKFPITVFCSAPTAYRMLIQNDITRSY-- 336
Cdd:cd17639 164 prtlTDKSKRGCKGDlTEFKP-TLMVGV-----PAiWDTIrkgvlAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLld 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 337 --KFNS--------LKHCVSAGEPINPEVMEqWKKKTGLDIYEGYGQTETvliCGNfkGMKIKPGSM-----GKPSPAFN 401
Cdd:cd17639 238 elVFKKvraalggrLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTET---CAG--GTVQDPGDLetgrvGPPLPCCE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 402 VEILD--ENG--TILPPGQeGDIAVQvlpdRPFgLFTHYVDNPSKTASTLRGN--FYiTGDRGYMDEDGYFWFVARSDD- 474
Cdd:cd17639 312 IKLVDweEGGysTDKPPPR-GEILIR----GPN-VFKGYYKNPEKTKEAFDGDgwFH-TGDIGEFHPDGTLKIIDRKKDl 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 475 VILSSGYRIGPFEVESALIEHPSIAESAVVSspDPIRGEVVkAFIVLN------------------PDYkLHDQEQLK-- 534
Cdd:cd17639 385 VKLQNGEYIALEKLESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPNekhltklaekhgvinsewEEL-CEDKKLQKav 460
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 564330613 535 -KEIQEHVKKTT-APYKYPRKIEFIEEL--PK----TVSGKVKRNEL 573
Cdd:cd17639 461 lKSLAETARAAGlEKFEIPQGVVLLDEEwtPEnglvTAAQKLKRKEI 507
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
448-573 |
7.57e-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: 48.67 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 448 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES------------AVVS--SPDPIRGE 513
Cdd:cd17647 370 RDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPD 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564330613 514 VVKAFIVLNPDYKLHDQ--------EQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 573
Cdd:cd17647 450 DESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
448-575 |
3.48e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 46.68 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 448 RGNFYITGDRGYMDEDGYFwFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGevVKAFIVLNPDYKL 527
Cdd:PRK05851 394 PDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRG 470
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 564330613 528 HDQEQLKKEIQEHVKKTTApyKYPRKIEFIE--ELPKTVSGKVKRNELRR 575
Cdd:PRK05851 471 PDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
345-558 |
3.80e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 46.73 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 345 VSAGEPINPEVMEQWKKKTGLDIYEGYGQTETvliCGnfkgmkikPGSMGKPspafnveilDEN---GTILPPGQEGDIA 421
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG--------PTTLGFP---------DEMcmlGTVGAPAVYNELR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 422 VQVLPD---RPFG-------------LFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVI-LSSGYRIG 484
Cdd:PLN02430 449 LEEVPEmgyDPLGepprgeicvrgkcLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVA 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 485 PFEVESALIEHPSIAESAVVSspDPIRGEVVkAFIVLNPD---------------YKLHDQEQLKKEIQEHVKKTTAPYK 549
Cdd:PLN02430 529 LEYLENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVPNEEntnkwakdngftgsfEELCSLPELKEHILSELKSTAEKNK 605
|
....*....
gi 564330613 550 YpRKIEFIE 558
Cdd:PLN02430 606 L-RGFEYIK 613
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
369-478 |
3.40e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 40.47 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 369 EGYGQTETVLICGNFKGMKIkpGSMGKPSP--------AFNVE----ILDENGTIlppgQEGDIA-VQVLPDRPFGLFTh 435
Cdd:PRK07868 749 EFFATTDGQAVLANVSGAKI--GSKGRPLPgagrvelaAYDPEhdliLEDDRGFV----RRAEVNeVGVLLARARGPID- 821
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 564330613 436 yvdnpsKTASTLRGNFyITGDR----GYM---DEDGYFWFVARSDDVILS 478
Cdd:PRK07868 822 ------PTASVKRGVF-APADTwistEYLfrrDDDGDYWLVDRRGSVIRT 864
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
165-261 |
3.44e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 40.34 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564330613 165 IITDDTLAPAVDIvaakcenlHSKLIVSqhsregWGNLKEMMKYASDSHTC-VDTKHNELMAIYFTSGTTGPPKMIGHTH 243
Cdd:PTZ00216 221 IIYLDSLPASVDT--------EGCRLVA------WTDVVAKGHSAGSHHPLnIPENNDDLALIMYTSGTTGDPKGVMHTH 286
|
90
....*....|....*....
gi 564330613 244 SSFGLG-LSVNGRFwLDLI 261
Cdd:PTZ00216 287 GSLTAGiLALEDRL-NDLI 304
|
|
| |
