|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
40-568 |
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: 1029.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 40 VPAKFNFASDVLDHWADMEKAGKRLPSPALWWVNGKGKELMWNFRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEW 119
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 120 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLN 199
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 200 EASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAG-WTGLQASDIMWTISDTGWILNILGSLLESWT 278
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRyWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 279 LGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIR 358
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 359 EFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVENPDKTAANIR 438
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 439 GDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSH 518
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 157311624 519 DPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEW 568
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
81-565 |
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: 659.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGaCGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 160
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPKMAEHSySSLGL 240
Cdd:cd05972 78 -------------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHT-HSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAKMDA-GWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL 319
Cdd:cd05972 108 GHIPTAaYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 320 QQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKG 399
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 400 NVLPPGTEGDIGIRVKpirPIGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVE 479
Cdd:cd05972 268 RELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 480 NALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQ 559
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*.
gi 157311624 560 RTKLRD 565
Cdd:cd05972 423 RVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
40-568 |
3.21e-174 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 505.03 E-value: 3.21e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 40 VPAKFNFASDVLDHWADmEKAGKrlpsPALWWVNGKGKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEW 119
Cdd:COG0365 4 VGGRLNIAYNCLDRHAE-GRGDK----VALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 120 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVI---------QEVDTVASECPSLRIKLLV----SEK 186
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 187 SCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAG-WTGLQASDIMWTISDTGW 265
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 266 ILNILGSLLESWTLGACTFVH-LLPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCLAGGES 340
Cdd:COG0365 238 ATGHSYIVYGPLLNGATVVLYeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 341 LLPETLENWRAQTGLDIREFYGQTETGlTCMVSK--TMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvKPiR 418
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETG-GIFISNlpGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK-GP-W 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 419 PiGIFSGYVENPDKTAANIRGDF---WLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVIS 495
Cdd:COG0365 395 P-GMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157311624 496 SPDPVRGEVVKAFVILASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEW 568
Cdd:COG0365 474 VPDEIRGQVVKAFVVLKPGV--EPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
40-567 |
1.49e-168 |
|
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: 489.70 E-value: 1.49e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 40 VPAKFNFASDVLDHWADMEKagKRLpspALWWVNGKGKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEW 119
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEYP--DKL---ALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 120 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--GDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKL 197
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 198 LNEASTT----HHCVETGSQEASAIYFTSGTSGLPKMAEHSYS-SLG--LKAKMdagWTGLQASDIMWTISDTGWILNIL 270
Cdd:cd05970 166 IKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTyPLGhiVTAKY---WQNVREGGLHLTVADTGWGKAVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 271 GSLLESWTLGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWR 350
Cdd:cd05970 243 GKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 351 AQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVENP 430
Cdd:cd05970 323 EKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 431 DKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVI 510
Cdd:cd05970 403 EKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 157311624 511 LASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKE 567
Cdd:cd05970 483 LAKGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
81-569 |
8.41e-117 |
|
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: 354.12 E-value: 8.41e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 160
Cdd:COG0318 25 LTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeaSAIYFTSGTSGLPKMAEHSYSSLGL 240
Cdd:COG0318 103 -------------------------------------------------------ALILYTSGTTGRPKGVMLTHRNLLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAKMDAGWTGLQASDIMWTIS----DTGWILNILGSLLeswtLGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYR 316
Cdd:COG0318 128 NAAAIAAALGLTPGDVVLVALplfhVFGLTVGLLAPLL----AGAT--LVLLPRFDPERVLELIERERVTVLFGVPTMLA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 317 MLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVSKTMKI--KPGYMGTAASCYDVQ 393
Cdd:COG0318 202 RLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGerRPGSVGRPLPGVEVR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 394 VIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRI 473
Cdd:COG0318 282 IVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 474 GPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflshDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPK 552
Cdd:COG0318 357 YPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR------PGAELDaEELRAFLRERLARYKVPRRVEFVDELPR 430
|
490
....*....|....*..
gi 157311624 553 TVTGKIQRTKLRDKEWK 569
Cdd:COG0318 431 TASGKIDRRALRERYAA 447
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
81-565 |
9.20e-113 |
|
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: 343.26 E-value: 9.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 160
Cdd:cd05971 7 VTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPKMAEHSYSSLGL 240
Cdd:cd05971 85 -------------------------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLLG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAKMDAGWTGL--QASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRML 318
Cdd:cd05971 116 HLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMM 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 319 LQQDLSSYKFP-HLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGL---TCmvSKTMKIKPGYMGTAASCYDVQV 394
Cdd:cd05971 196 RQQGEQLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLvigNC--SALFPIKPGSMGKPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 395 IDDKGNVLPPGTEGDIGIRvkpiRPIGI-FSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRI 473
Cdd:cd05971 274 VDDNGTPLPPGEVGEIAVE----LPDPVaFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 474 GPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 553
Cdd:cd05971 350 GPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNELPRT 427
|
490
....*....|..
gi 157311624 554 VTGKIQRTKLRD 565
Cdd:cd05971 428 ATGKIRRRELRA 439
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-567 |
1.80e-110 |
|
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: 337.23 E-value: 1.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAkAIVAGDE 162
Cdd:cd05974 3 FAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA-VYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 ViqevdTVASEcPSLrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGLKA 242
Cdd:cd05974 81 N-----THADD-PML----------------------------------------LYFTSGTTSKPKLVEHTHRSYPVGH 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 243 KMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD 322
Cdd:cd05974 115 LSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 323 LSSYKFPhLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETglTCMVSKT--MKIKPGYMGTAASCYDVQVIDDKGN 400
Cdd:cd05974 195 LASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET--TALVGNSpgQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 401 vlpPGTEGDIGIRVKPIRPIGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN 480
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 481 ALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQR 560
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG--YEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
....*..
gi 157311624 561 TKLRDKE 567
Cdd:cd05974 426 VELRRRE 432
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
43-567 |
1.48e-108 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 336.87 E-value: 1.48e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 43 KFNFASDVLDHWADMEKAGKrlpsPALWWVNGKGKELmWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLV 122
Cdd:PRK04319 41 KVNIAYEAIDRHADGGRKDK----VALRYLDASRKEK-YTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 123 ILGCIRAGLI-------FMPGTIQMkstdilyRLQMSKAKAIVAGDEVIQEVdtVASECPSLRIKLLVSE--KSCDGWLN 193
Cdd:PRK04319 115 LLGALKNGAIvgplfeaFMEEAVRD-------RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEdvEEGPGTLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 194 FKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--------MAEHSYSSlglKAKMDagwtgLQASDIMWTISDTGW 265
Cdd:PRK04319 186 FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKgvlhvhnaMLQHYQTG---KYVLD-----LHEDDVYWCTADPGW 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 266 ILNILGSLLESWTLGAcTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCLAGGESLL 342
Cdd:PRK04319 258 VTGTSYGIFAPWLNGA-TNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddlVKKYDLSSLRHILSVGEPLN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 343 PETLENWRAQTGLDIREFYGQTETGlTCMVSKT--MKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIrvKPIRPi 420
Cdd:PRK04319 337 PEVVRWGMKVFGLPIHDNWWMTETG-GIMIANYpaMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 421 GIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPV 500
Cdd:PRK04319 413 SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPV 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157311624 501 RGEVVKAFVILASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKE 567
Cdd:PRK04319 493 RGEIIKAFVALRP---GYEPsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
81-567 |
3.77e-99 |
|
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: 308.28 E-value: 3.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEVIQEVDTvasECPSLrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGL 240
Cdd:cd05969 80 EELYERTDP---EDPTL----------------------------------------LHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWtLGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ 320
Cdd:cd05969 117 YYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPW-LNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 321 QD---LSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGlTCMVSK--TMKIKPGYMGTAASCYDVQVI 395
Cdd:cd05969 196 EGdelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETG-SIMIANypCMPIKPGSMGKPLPGVKAAVV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 396 DDKGNVLPPGTEGDIGIrvKPIRPiGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGP 475
Cdd:cd05969 275 DENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 476 SEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlshDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTV 554
Cdd:cd05969 352 FEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF---EPsDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|...
gi 157311624 555 TGKIQRTKLRDKE 567
Cdd:cd05969 429 SGKIMRRVLKAKE 441
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
55-564 |
5.33e-97 |
|
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: 303.33 E-value: 5.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 55 ADM-EKAGKRLP-SPALWWvngKGKelMWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLI 132
Cdd:cd05936 2 ADLlEEAARRFPdKTALIF---MGR--KLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 133 FMPGTIQMKSTDILYRLQMSKAKAIVAGDEviqevdtvasecpslrikllvsekscdgwlnFKKLLNEASTTHHCVETGS 212
Cdd:cd05936 76 VVPLNPLYTPRELEHILNDSGAKALIVAVS-------------------------------FTDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 213 QEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTG--LQASDIMwtisdtgwiLNIL---------GSLLESWTLGA 281
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVV---------LAALplfhvfgltVALLLPLALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 282 CtfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREF 360
Cdd:cd05936 196 T--IVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 361 YGQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVENPDKTAANI 437
Cdd:cd05936 274 YGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-------GpqVMKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 438 RgDFWLL-GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILasqfl 516
Cdd:cd05936 347 V-DGWLRtGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL----- 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 157311624 517 sHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd05936 421 -KEGASLTEeEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-564 |
5.07e-93 |
|
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: 292.11 E-value: 5.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagde 162
Cdd:cd05973 3 FGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 viqevdTVASECPSLRIKLLVsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSL-GLK 241
Cdd:cd05973 78 ------TDAANRHKLDSDPFV----------------------------------MMFTSGTTGLPKGVPVPLRALaAFG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 242 AKMDAGwTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPkFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ 321
Cdd:cd05973 118 AYLRDA-VDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 322 DLSSYKFP--HLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGltcMV-----SKTMKIKPGYMGTAASCYDVQV 394
Cdd:cd05973 196 GAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELG---MVlanhhALEHPVHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 395 IDDKGNVLPPGTEGDIGIRVKPiRPIGIFSGYVENPDKTAAnirGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIG 474
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIAN-SPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 475 PSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 553
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG---GHEGtPALADELQLHVKKRLSAHAYPRTIHFVDELPKT 425
|
490
....*....|.
gi 157311624 554 VTGKIQRTKLR 564
Cdd:cd05973 426 PSGKIQRFLLR 436
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
218-559 |
5.24e-89 |
|
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: 278.40 E-value: 5.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 218 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWIlNILGSLLESWTLGACtfVHLLPKFDPLVIL 297
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGT--VVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 298 KTLSSYPIKSMMGAPIVYRMLLQQDLSS-YKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETG--LTCMVSK 374
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLLKAPESAgYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtVATGPPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 375 TMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDG 454
Cdd:cd04433 162 DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-----GPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 455 YFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlSHDPEqltkELQQHVKSV 534
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA-DLDAE----ELRAHVRER 311
|
330 340
....*....|....*....|....*
gi 157311624 535 TAPYKYPRKIEFVLNLPKTVTGKIQ 559
Cdd:cd04433 312 LAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
81-569 |
1.31e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 267.82 E-value: 1.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:PRK06187 32 TTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEVIQEVDTVASECPSLRIKLLVSEKSCDG----WLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYS 236
Cdd:PRK06187 111 SEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 237 SLGLKAKMDAGWTGLQASDI------MWTISDTGW-ILNILgslleswtLGAcTFVhLLPKFDPLVILKTLSSYPIKSMM 309
Cdd:PRK06187 191 NLFLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLpYLALM--------AGA-KQV-IPRRFDPENLLDLIETERVTFFF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 310 GAPIVYRMLLQQDLSS-YKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETG--LTCMV-SKTMKIKPGYM-- 383
Cdd:PRK06187 261 AVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpvVSVLPpEDQLPGQWTKRrs 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 384 -GTAASCYDVQVIDDKGNVLPPGtEGDIG-IRVKpirpiG--IFSGYVENPDKTAANIRGDfWLL-GDRGIKDEDGYFQF 458
Cdd:PRK06187 341 aGRPLPGVEARIVDDDGDELPPD-GGEVGeIIVR-----GpwLMQGYWNRPEATAETIDGG-WLHtGDVGYIDEDGYLYI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 459 MGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILasqflsHDPEQLT-KELQQHVKSVTAP 537
Cdd:PRK06187 414 TDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL------KPGATLDaKELRAFLRGRLAK 487
|
490 500 510
....*....|....*....|....*....|..
gi 157311624 538 YKYPRKIEFVLNLPKTVTGKIQRTKLRDKEWK 569
Cdd:PRK06187 488 FKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
42-564 |
2.11e-82 |
|
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: 266.93 E-value: 2.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 42 AKFNFASDVLDHwadmeKAGKRLPSPALWwvnGKGKELmwNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWL 121
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAFI---DDAGSL--TYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 122 VILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVS--EKSCDGWLNFKKLLN 199
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSggAGPEAGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 200 EASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILGSLLESWT 278
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVlGIREDDVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 279 LGACTFvhLLPKF-DPLVILKTLSSYPIKSMMGAPIVYR-MLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLD 356
Cdd:cd05959 230 VGATTV--LMPERpTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 357 IREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVENPDKTAAN 436
Cdd:cd05959 308 ILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSAT-----MYWNNRDKTRDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 437 IRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFl 516
Cdd:cd05959 383 FQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 157311624 517 sHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd05959 462 -EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
78-564 |
2.21e-80 |
|
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: 259.33 E-value: 2.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 78 ELMWNFRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIfmpgtiqmkstdilyrlqmskakai 157
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAI------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 vagdeviqevdTVASEcPSLRIKllvsekscdgwlNFKKLLNEASTTHH-CVE--TGSQEASAIYFTSGTSGLPKMAEHS 234
Cdd:cd05958 63 -----------AVATM-PLLRPK------------ELAYILDKARITVAlCAHalTASDDICILAFTSGTTGAPKATMHF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 235 YSSLGLKAKmdaGWT----GLQASDIMWTISDTGWILNILGSLLESWTLGACTFvhLLPKFDPLVILKTLSSYPIKSMMG 310
Cdd:cd05958 119 HRDPLASAD---RYAvnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGV--LLEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 311 APIVYRMLL------QQDLSSykfphLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMG 384
Cdd:cd05958 194 APTAYRAMLahpdaaGPDLSS-----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 385 TAASCYDVQVIDDKGNVLPPGTEGDIGIRVKpirpigifSGYVENPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRAD 463
Cdd:cd05958 269 KPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP--------TGCRYLADKRQRTYVQGGWNItGDTYSRDPDGYFRHQGRSD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 464 DIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflsHDP-EQLTKELQQHVKSVTAPYKYPR 542
Cdd:cd05958 341 DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPG---VIPgPVLARELQDHAKAHIAPYKYPR 417
|
490 500
....*....|....*....|..
gi 157311624 543 KIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd05958 418 AIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
58-566 |
3.93e-75 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 247.90 E-value: 3.93e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 58 EKAGKRLP-SPALWWvngkgKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPG 136
Cdd:PRK07656 12 ARAARRFGdKEAYVF-----GDQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 137 TIQMKSTDILYRLQMSKAKAIVAGDEVIqEVDTVASEC-PSLRIKLLV----SEKSCDGWLNFKKLLNEASTTHHCVETG 211
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFL-GVDYSATTRlPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 212 SQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDT----GWILNILGSLLEswtlGACTFVHl 287
Cdd:PRK07656 165 PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFfhvfGYKAGVNAPLMR----GATILPL- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 288 lPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLD-IREFYGQTE 365
Cdd:PRK07656 240 -PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 366 -TGLTCM--VSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVENPDKTAANIRGD 440
Cdd:PRK07656 319 aSGVTTFnrLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR-------GpnVMKGYYDDPEATAAAIDAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 441 FWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflshd 519
Cdd:PRK07656 392 GWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG----- 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 157311624 520 pEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDK 566
Cdd:PRK07656 467 -AELTEEeLIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-564 |
1.49e-70 |
|
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: 232.95 E-value: 1.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 160
Cdd:cd05934 4 WTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 deviqeVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGL 240
Cdd:cd05934 81 ------VDPAS----------------------------------------------ILYTSGTTGPPKGVVITHANLTF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGAcTFVhLLPKFDPLVILKTLSSY--PIKSMMGAPIvyRML 318
Cdd:cd05934 109 AGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGA-TLV-LLPRFSASRFWSDVRRYgaTVTNYLGAML--SYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 319 LQQDLSSYKFPHLQNCLAGGESLlPETLENWRAQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDK 398
Cdd:cd05934 185 LAQPPSPDDRAHRLRAAYGAPNP-PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 399 GNVLPPGTEGDIGIRvkPIRPIGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEV 478
Cdd:cd05934 264 GQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 479 ENALMKHPAVVETAVISSPDPVRGEVVKAFVILasqflsHDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGK 557
Cdd:cd05934 342 ERAILRHPAVREAAVVAVPDEVGEDEVKAVVVL------RPGETLDpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEK 415
|
....*..
gi 157311624 558 IQRTKLR 564
Cdd:cd05934 416 VAKAQLR 422
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
43-565 |
1.72e-70 |
|
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: 235.50 E-value: 1.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 43 KFNFASDVLDHWADMEKAGKrlpspaLWWVNGKGKelmWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLV 122
Cdd:TIGR02262 2 KYNAAEDLLDRNVVEGRGGK------TAFIDDISS---LSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 123 ILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKScDGWLNFKKLLNEAS 202
Cdd:TIGR02262 72 FLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGRPE-AGEVQLAELLATES 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 203 TTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILGSLLESWTLGA 281
Cdd:TIGR02262 151 EQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTlGIREDDVCFSAAKLFFAYGLGNALTFPMSVGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 282 cTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYR-MLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREF 360
Cdd:TIGR02262 231 -TTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 361 YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirpiGIFS--GYVENPDKTAANIR 438
Cdd:TIGR02262 310 IGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-------GPSSatMYWNNRAKSRDTFQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 439 GDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlsh 518
Cdd:TIGR02262 383 GEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ--- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 157311624 519 dpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:TIGR02262 460 --TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
40-571 |
1.33e-69 |
|
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: 235.67 E-value: 1.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 40 VPAKFNFASDVLDHWADMEKAGKrlpsPALWWVNG-KGKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPE 118
Cdd:cd05967 45 VGGRLNTCYNALDRHVEAGRGDQ----IALIYDSPvTGTERTYTYAELLDEVSRLAGVLR-KLGVVKGDRVIIYMPMIPE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 119 WWLVILGCIRAGLI-------FmpgtiqmKSTDILYRLQMSKAKAIVA------GDEVIQE---VDTVASECPSLRIKLL 182
Cdd:cd05967 120 AAIAMLACARIGAIhsvvfggF-------AAKELASRIDDAKPKLIVTascgiePGKVVPYkplLDKALELSGHKPHHVL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 183 V---SEKSCD-----GWLNFKKLLNEAsTTHHCVETGSQEASAIYFTSGTSGLPK-----MAEHSyssLGLKAKMDAGWt 249
Cdd:cd05967 193 VlnrPQVPADltkpgRDLDWSELLAKA-EPVDCVPVAATDPLYILYTSGTTGKPKgvvrdNGGHA---VALNWSMRNIY- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 250 GLQASDIMWTISDTGWILN----ILGSLLeswtLGACTFVH-----LLPkfDPLVILKTLSSYPIKSMMGAPIVYRMLLQ 320
Cdd:cd05967 268 GIKPGDVWWAASDVGWVVGhsyiVYGPLL----HGATTVLYegkpvGTP--DPGAFWRVIEKYQVNALFTAPTAIRAIRK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 321 QD-----LSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETG----LTCMVSKTMKIKPGYMGTAASCYD 391
Cdd:cd05967 342 EDpdgkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGwpitANPVGLEPLPIKAGSPGKPVPGYQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 392 VQVIDDKGNVLPPGTEGDIGIRVkPIRPiGIFSGYVENPDKTAANIRGDF---WLLGDRGIKDEDGYFQFMGRADDIINS 468
Cdd:cd05967 422 VQVLDEDGEPVGPNELGNIVIKL-PLPP-GCLLTLWKNDERFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINV 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 469 SGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQfLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVL 548
Cdd:cd05967 500 AGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVK 578
|
570 580
....*....|....*....|....*..
gi 157311624 549 NLPKTVTGKIQRTKLRD----KEWKMS 571
Cdd:cd05967 579 RLPKTRSGKILRRTLRKiadgEDYTIP 605
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
83-564 |
2.30e-69 |
|
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: 230.43 E-value: 2.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:cd05919 13 YGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 VIqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeASAIYfTSGTSGLPKMAEHSY-SSLGLK 241
Cdd:cd05919 92 DI--------------------------------------------------AYLLY-SSGTTGPPKGVMHAHrDPLLFA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 242 AKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHLLPKfDPLVILKTLSSYPIKSMMGAPIVY-RMLLQ 320
Cdd:cd05919 121 DAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLDS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 321 QDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGN 400
Cdd:cd05919 200 CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 401 VLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN 480
Cdd:cd05919 280 TIPPGEEGDLLVRGP-----SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 481 ALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
....
gi 157311624 561 TKLR 564
Cdd:cd05919 433 FKLR 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
81-560 |
5.75e-69 |
|
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: 229.42 E-value: 5.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 160
Cdd:cd17631 21 LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEVIQevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGL 240
Cdd:cd17631 98 DDLAL----------------------------------------------------LMYTSGTTGRPKGAMLTHRNLLW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAkMDAGWT-GLQASDI------MWTISDTGwiLNILGSLLeswtLGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAPI 313
Cdd:cd17631 126 NA-VNALAAlDLGPDDVllvvapLFHIGGLG--VFTLPTLL----RGGT--VVILRKFDPETVLDLIERHRVTSFFLVPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 314 VYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAqTGLDIREFYGQTETG-LTCMVSKTMKI-KPGYMGTAASCY 390
Cdd:cd17631 197 MIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGRPVFFV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 391 DVQVIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANIRGDfWLL-GDRGIKDEDGYFQFMGRADDIINSS 469
Cdd:cd17631 276 EVRIVDPDGREVPPGEVGEIVVR-GP----HVMAGYWNRPEATAAAFRDG-WFHtGDLGRLDEDGYLYIVDRKKDMIISG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 470 GYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflshDPEQLT-KELQQHVKSVTAPYKYPRKIEFVL 548
Cdd:cd17631 350 GENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR------PGAELDeDELIAHCRERLARYKIPKSVEFVD 423
|
490
....*....|..
gi 157311624 549 NLPKTVTGKIQR 560
Cdd:cd17631 424 ALPRNATGKILK 435
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
83-565 |
2.47e-65 |
|
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: 219.85 E-value: 2.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGde 162
Cdd:cd05941 14 YADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVLDP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 viqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeaSAIYFTSGTSGLPKMAEHSYSSLG--L 240
Cdd:cd05941 92 -----------------------------------------------------ALILYTSGTTGRPKGVVLTHANLAanV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAKMDAgWTglqasdimWTISDT-----------GWILNILGSLlesWTLGACtfvHLLPKFDPLVILKTLSSYPIKSMM 309
Cdd:cd05941 119 RALVDA-WR--------WTEDDVllhvlplhhvhGLVNALLCPL---FAGASV---EFLPKFDPKEVAISRLMPSITVFM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 310 GAPIVYRMLLQQdlSSYKFPHLQNCLAGGES-----------LLPETLENWRAQTGLDIREFYGQTETGLTCMVSKTMKI 378
Cdd:cd05941 184 GVPTIYTRLLQY--YEAHFTDPQFARAAAAErlrlmvsgsaaLPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 379 KPGYMGTAASCYDVQVIDDKGN-VLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYF 456
Cdd:cd05941 262 RPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GP----SVFKEYWNKPEATKEEFTDDGWFkTGDLGVVDEDGYY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 457 QFMGR-ADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEqltkELQQHVKSVT 535
Cdd:cd05941 337 WILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE----ELKEWAKQRL 412
|
490 500 510
....*....|....*....|....*....|
gi 157311624 536 APYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:cd05941 413 APYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
34-564 |
1.84e-64 |
|
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: 221.98 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 34 QWGHQEVPAKFNFASDVLDHWAdmekaGKRLPSPALWWVNGKGKELMWNFRELSENSQQAANILSgACGLQRGDRVAVML 113
Cdd:cd05968 50 PWAAWFVGGRMNIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 114 PRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD---------EVIQEVDTVASECPSLRiKLLVS 184
Cdd:cd05968 124 PMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTVE-KVVVV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 185 E--KSCDGWLNFKKL---LNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMW 258
Cdd:cd05968 203 RhlGNDFTPAKGRDLsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQfDLKPGDLLT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 259 TISDTGWILN---ILGSLLeswtLGACTFVHL-LPKFD-PLVILKTLSSYPIKSMMGAPIVYRMLL--------QQDLSS 325
Cdd:cd05968 283 WFTDLGWMMGpwlIFGGLI----LGATMVLYDgAPDHPkADRLWRMVEDHEITHLGLSPTLIRALKprgdapvnAHDLSS 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 326 YKfphlqncLAG--GESLLPETLeNWRAQTGLD----IREFYGQTETG---LTCMVSKtmKIKPGYMGTAASCYDVQVID 396
Cdd:cd05968 359 LR-------VLGstGEPWNPEPW-NWLFETVGKgrnpIINYSGGTEISggiLGNVLIK--PIKPSSFNGPVPGMKADVLD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 397 DKGNVLPPgTEGDIGIRvKPIrpIGIFSGYVENPDK---TAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRI 473
Cdd:cd05968 429 ESGKPARP-EVGELVLL-APW--PGMTRGFWRDEDRyleTYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRV 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 474 GPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 553
Cdd:cd05968 505 GPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGV--TPTEALAEELMERVADELGKPLSPERILFVKDLPKT 582
|
570
....*....|.
gi 157311624 554 VTGKIQRTKLR 564
Cdd:cd05968 583 RNAKVMRRVIR 593
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
81-565 |
2.78e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 219.42 E-value: 2.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEVIQEVDTVASECPSLRIKLLVSEK---SCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 237
Cdd:PRK08316 116 PALAPTAEAALALLPVDTLILSLVLGgreAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 238 L---GLKAKMDAGWTglqASDIMwtisdtgwiLNIL---------GSLLESWTLGACTfvHLLPKFDPLVILKTLSSYPI 305
Cdd:PRK08316 196 LiaeYVSCIVAGDMS---ADDIP---------LHALplyhcaqldVFLGPYLYVGATN--VILDAPDPELILRTIEAERI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 306 KSMMGAPIVYRMLL------QQDLSSykfphLQNCLAGGeSLLP-ETLENWRAQ-TGLDIREFYGQTETGLTCMV--SKT 375
Cdd:PRK08316 262 TSFFAPPTVWISLLrhpdfdTRDLSS-----LRKGYYGA-SIMPvEVLKELRERlPGLRFYNCYGQTEIAPLATVlgPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 376 MKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGY 455
Cdd:PRK08316 336 HLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR-SP----QLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 456 FQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflshdpEQLT-KELQQHVKSV 534
Cdd:PRK08316 411 ITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG------ATVTeDELIAHCRAR 484
|
490 500 510
....*....|....*....|....*....|.
gi 157311624 535 TAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK08316 485 LAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
82-563 |
5.30e-64 |
|
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: 216.19 E-value: 5.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGd 161
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 eviQEVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSGTSGLPKMAEHSYSSLGLK 241
Cdd:cd05935 81 ---SELDDLA---------------------------------------------LIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 242 AKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL-- 319
Cdd:cd05935 113 ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGG-TYV-LMARWDRETALELIEKYKVTFWTNIPTMLVDLLat 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 320 ----QQDLSSYKFphlqncLAGGESLLPETL-ENWRAQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQV 394
Cdd:cd05935 191 pefkTRDLSSLKV------LTGGGAPMPPAVaEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 395 ID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAA---NIRG-DFWLLGDRGIKDEDGYFQFMGRADDIINSS 469
Cdd:cd05935 265 IDiETGRELPPNEVGEIVVR-GP----QIFKGYWNRPEETEEsfiEIKGrRFFRTGDLGYMDEEGYFFFVDRVKRMINVS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 470 GYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQltkELQQHVKSVTAPYKYPRKIEFVLN 549
Cdd:cd05935 340 GFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDE 416
|
490
....*....|....
gi 157311624 550 LPKTVTGKIQRTKL 563
Cdd:cd05935 417 LPRSASGKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
54-573 |
9.39e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 218.29 E-value: 9.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 54 WADMEKAGKRLPS-PALWWVngkGKELmwNFRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLI 132
Cdd:PRK08314 13 FHNLEVSARRYPDkTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 133 FMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEV------------------DTVASECP-----SLRIKLLVSEKSCD 189
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 190 GWLnfkkLLNEASTTHHC---VETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWI 266
Cdd:PRK08314 168 GVV----AWKEALAAGLApppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 267 LNILGSLLESWTLGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAP-IVYRMLLQQDLSSYKFPHLQnCLAGGESLLPET 345
Cdd:PRK08314 244 TGMVHSMNAPIYAGA-TVV-LMPRWDREAAARLIERYRVTHWTNIPtMVVDFLASPGLAERDLSSLR-YIGGGGAAMPEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 346 L-ENWRAQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVID-DKGNVLPPGTEGDIGIRvkpirpiG-- 421
Cdd:PRK08314 321 VaERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH-------Gpq 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 422 IFSGYVENPDKTAA---NIRGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSP 497
Cdd:PRK08314 394 VFKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157311624 498 DPVRGEVVKAFVILASQFLSHDPEQltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEWKMSGK 573
Cdd:PRK08314 474 DPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
81-469 |
4.21e-63 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 213.33 E-value: 4.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:pfam00501 22 LTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DE-VIQEVDTVASECPSLRIKLLVSEkscDGWLNFKKLLNEASTTHHCVETGSQEAS----AIYFTSGTSGLPKMAEHS- 234
Cdd:pfam00501 101 DAlKLEELLEALGKLEVVKLVLVLDR---DPVLKEEPLPEEAKPADVPPPPPPPPDPddlaYIIYTSGTTGKPKGVMLTh 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 235 ---YSSLGLKAKMDAGWTGLQASDIMWTIS----DTGWILNILGSLLeswtLGACtfVHLLPKF---DPLVILKTLSSYP 304
Cdd:pfam00501 178 rnlVANVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLSLGLLGPLL----AGAT--VVLPPGFpalDPAALLELIERYK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 305 IKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVSKTMKIK---P 380
Cdd:pfam00501 252 VTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDlrsL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 381 GYMGTAASCYDVQVIDDK-GNVLPPGTEGDIGIRvkpiRPiGIFSGYVENPDKTAANIRGDFWLL-GDRGIKDEDGYFQF 458
Cdd:pfam00501 332 GSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAFDEDGWYRtGDLGRRDEDGYLEI 406
|
410
....*....|.
gi 157311624 459 MGRADDIINSS 469
Cdd:pfam00501 407 VGRKKDQIKLG 417
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
81-565 |
1.04e-62 |
|
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: 214.48 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASA---IYFTSGTSGLPKMAEHSYSS 237
Cdd:cd05926 94 KGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDlalILHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 238 LGLKAKMDAGWTGLQASDIMWTISDTGWILNILGSLLEswTLGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRM 317
Cdd:cd05926 174 LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLS--TLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 318 LLQQDLSSY--KFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETG--LTCMVSKTMKIKPGYMGTAASCyDVQ 393
Cdd:cd05926 252 LLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVGV-EVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 394 VIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRADDIINSSGYR 472
Cdd:cd05926 331 ILDEDGEILPPGVVGEICLRGP-----NVTRGYLNNPEANAEAAFKDGWFRtGDLGYLDADGYLFLTGRIKELINRGGEK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 473 IGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPK 552
Cdd:cd05926 406 ISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRE-----GASVTEEELRAFCRKHLAAFKVPKKVYFVDELPK 480
|
490
....*....|...
gi 157311624 553 TVTGKIQRTKLRD 565
Cdd:cd05926 481 TATGKIQRRKVAE 493
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
81-559 |
2.51e-62 |
|
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: 213.23 E-value: 2.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEVIQEVDTVASECPSLRiKLLVSEKSCDGWLNFKKLLNEASTTHH-----CVETGSQEASAIYFTSGTSGLPKMAEHSY 235
Cdd:cd05911 90 PDGLEKVKEAAKELGPKD-KIIVLDDKPDGVLSIEDLLSPTLGEEDedlppPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 SSLGLKAKM--DAGWTGLQASDIMWTISDTGWILNILgSLLESWTLGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAP- 312
Cdd:cd05911 169 RNLIANLSQvqTFLYGNDGSNDVILGFLPLYHIYGLF-TTLASLLNGAT--VIIMPKFDSELFLDLIEKYKITFLYLVPp 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 313 IVYRMLLQQDLSSYKFPHLQNCLAGG-------ESLLPETLENWRAQTGldirefYGQTETGLTCMVSKTMKIKPGYMGT 385
Cdd:cd05911 246 IAAALAKSPLLDKYDLSSLRVILSGGaplskelQELLAKRFPNATIKQG------YGMTETGGILTVNPDGDDKPGSVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 386 AASCYDVQVIDDKGN-VLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRAD 463
Cdd:cd05911 320 LLPNVEAKIVDDDGKdSLGPNEPGEICVR-----GPQVMKGYYNNPEATKETFDEDGWLhTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 464 DIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflshDPEQLT-KELQQHVKSVTAPYKYPR 542
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRK------PGEKLTeKEVKDYVAKKVASYKQLR 468
|
490
....*....|....*...
gi 157311624 543 K-IEFVLNLPKTVTGKIQ 559
Cdd:cd05911 469 GgVVFVDEIPKSASGKIL 486
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
3-558 |
2.56e-62 |
|
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: 215.52 E-value: 2.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 3 WLRKVQGLCTLWGTQMSSRTLYinSRQLVSLQWGHQevpAKFNFASDVLDHwaDMEKAGKRLpspALWWVNGKGKEL-MW 81
Cdd:cd17634 16 WGEAGKILDWITPYQKVKNTSF--APGAPSIKWFED---ATLNLAANALDR--HLRENGDRT---AIIYEGDDTSQSrTI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:cd17634 86 SYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 EVIQEVDTV----------ASECPSLRIKLLVSEKSCD------GWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTS 225
Cdd:cd17634 165 GGVRAGRSVplkknvddalNPNVTSVEHVIVLKRTGSDidwqegRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 226 GLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILN----ILGSLLeswtLGACTFVHL-LPKF-DPLVILK 298
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAATTMKYVfDYGPGDIYWCTADVGWVTGhsylLYGPLA----CGATTLLYEgVPNWpTPARMWQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 299 TLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCLAGGESLLPETLE-NWR--AQTGLDIREFYGQTETGLTCMv 372
Cdd:cd17634 321 VVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPINPEAYEwYWKkiGKEKCPVVDTWWQTETGGFMI- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 373 sktmKIKPGYMGTAASC-------YDVQVIDDKGNVLPPGTEGDIGIRVKpiRPIGIFSGYVENPDKTAANIR--GDFWL 443
Cdd:cd17634 400 ----TPLPGAIELKAGSatrpvfgVQPAVVDNEGHPQPGGTEGNLVITDP--WPGQTRTLFGDHERFEQTYFStfKGMYF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 444 LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLshDPEQL 523
Cdd:cd17634 474 SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPEL 551
|
570 580 590
....*....|....*....|....*....|....*
gi 157311624 524 TKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 558
Cdd:cd17634 552 YAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
81-565 |
3.59e-60 |
|
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: 210.11 E-value: 3.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEwwLVI--LGCIRAGLI-------FMPGTIQMkstdilyRLQM 151
Cdd:cd05966 85 ITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPE--LVIamLACARIGAVhsvvfagFSAESLAD-------RIND 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 152 SKAKAIVAGDE------VI---QEVDTVASECPSLRiKLLVSEKSC---------DGWLNfkKLLNEASTTHHCVETGSQ 213
Cdd:cd05966 155 AQCKLVITADGgyrggkVIplkEIVDEALEKCPSVE-KVLVVKRTGgevpmtegrDLWWH--DLMAKQSPECEPEWMDSE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 214 EASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILN----ILGSLLeswtLGACTfvhll 288
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVfDYHPDDIYWCTADIGWITGhsyiVYGPLA----NGATT----- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 289 pkfdplVILKTLSSYPIKSMM-------------GAPIVYRMLLQQ--------DLSSYKfphlqncLAG--GESLLPET 345
Cdd:cd05966 303 ------VMFEGTPTYPDPGRYwdivekhkvtifyTAPTAIRALMKFgdewvkkhDLSSLR-------VLGsvGEPINPEA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 346 LENWRAQTG---LDIREFYGQTETG---LTCMVSKTmKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpiRP 419
Cdd:cd05966 370 WMWYYEVIGkerCPIVDTWWQTETGgimITPLPGAT-PLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK----RP 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 420 I-GIFSGYVENPD---KTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVIS 495
Cdd:cd05966 445 WpGMARTIYGDHEryeDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVG 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157311624 496 SPDPVRGEVVKAFVILASqflSHDPEQ-LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:cd05966 525 RPHDIKGEAIYAFVTLKD---GEEPSDeLRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
79-566 |
9.93e-59 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 203.95 E-value: 9.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 79 LMWNFRELSENSQQAANILsGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 158
Cdd:PRK07514 27 LRYTYGDLDAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 159 AGDEVIQEVDTVASECPSLRIKLLVSekscDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL 238
Cdd:PRK07514 106 CDPANFAWLSKIAAAAGAPHVETLDA----DGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 239 GLKAKM--DA-GWTG----LQASDIMWTisdTGWILNILGSLLEswtlGACTFvhLLPKFDPLVILKTLSSypIKSMMGA 311
Cdd:PRK07514 182 LSNALTlvDYwRFTPddvlIHALPIFHT---HGLFVATNVALLA----GASMI--FLPKFDPDAVLALMPR--ATVMMGV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 312 PIVY-RMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGltcmvsktMKI--------KPGY 382
Cdd:PRK07514 251 PTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETN--------MNTsnpydgerRAGT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 383 MGTAASCYDVQVID-DKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVENPDKTAANIRGD-FWLLGDRGIKDEDGYFQF 458
Cdd:PRK07514 323 VGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 459 MGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAfVILASQFLSHDPEQLTKELQQHVksvtAPY 538
Cdd:PRK07514 396 VGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA-VVVPKPGAALDEAAILAALKGRL----ARF 470
|
490 500
....*....|....*....|....*...
gi 157311624 539 KYPRKIEFVLNLPKTVTGKIQRTKLRDK 566
Cdd:PRK07514 471 KQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
81-569 |
4.73e-58 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 203.06 E-value: 4.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:PRK06087 50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEVIQ-----EVDTVASECPSLRIKLLV-SEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHS 234
Cdd:PRK06087 129 TLFKQtrpvdLILPLQNQLPQLQQIVGVdKLAPATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 235 YSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFvhLLPKFDPLVILKTLSSYPIKSMMGA-PI 313
Cdd:PRK06087 209 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDACLALLEQQRCTCMLGAtPF 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 314 VYRMLLQQDLSSYKFPHLQNCLAGGeSLLPETLENWRAQTGLDIREFYGQTETGLTCMV--SKTMKIKPGYMGTAASCYD 391
Cdd:PRK06087 287 IYDLLNLLEKQPADLSALRFFLCGG-TTIPKKVARECQQRGIKLLSVYGSTESSPHAVVnlDDPLSRFMHTDGYAAAGVE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 392 VQVIDDKGNVLPPGTEGDigirvKPIRPIGIFSGYVENPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRADDIINSSG 470
Cdd:PRK06087 366 IKVVDEARKTLPPGCEGE-----EASRGPNVFMGYLDEPELTARALDEEGWYYsGDLCRMDEAGYIKITGRKKDIIVRGG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 471 YRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQLTKEL-QQHVksvtAPYKYPRKIEFVLN 549
Cdd:PRK06087 441 ENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFsRKRV----AKYKYPEHIVVIDK 516
|
490 500
....*....|....*....|
gi 157311624 550 LPKTVTGKIQRTKLRdKEWK 569
Cdd:PRK06087 517 LPRTASGKIQKFLLR-KDIM 535
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
34-563 |
8.65e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 202.96 E-value: 8.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 34 QWGHQEVPAkfnfaSDVLDHWAdmekagKRLPS-PALWWVngkGKELmwNFRELSENSQQAANILSGAcGLQRGDRVAVM 112
Cdd:PRK06178 27 EYPHGERPL-----TEYLRAWA------RERPQrPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 113 LPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASEC-----------------P 175
Cdd:PRK06178 90 LPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhvivtsladvlpaeP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 176 SLRIKLLVSE--KSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQA 253
Cdd:PRK06178 170 TLPLPDSLRAprLAAAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 254 SD--------IMWtIS--DTGWILNILgslleswtLGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL---- 319
Cdd:PRK06178 250 EDsvflsflpEFW-IAgeNFGLLFPLF--------SGA-TLV-LLARWDAVAFMAAVERYRVTRTVMLVDNAVELMdhpr 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 320 --QQDLSSYKFPhlqNCLAGGESLLPETLENWRAQTGLDIREF-YGQTETGlTC------MVSKTMKIK--PGYMGTAAS 388
Cdd:PRK06178 319 faEYDLSSLRQV---RVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETH-TCdtftagFQDDDFDLLsqPVFVGLPVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 389 CYDVQVID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADDII 466
Cdd:PRK06178 395 GTEFKICDfETGELLPLGAEGEIVVR-TP----SLLKGYWNKPEATAEALR-DGWLhTGDIGKIDEQGFLHYLGRRKEML 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 467 NSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASqflshDPEQLTKELQQHVKSVTAPYKYPrKIEF 546
Cdd:PRK06178 469 KVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP-----GADLTAAALQAWCRENMAVYKVP-EIRI 542
|
570
....*....|....*..
gi 157311624 547 VLNLPKTVTGKIQRTKL 563
Cdd:PRK06178 543 VDALPMTATGKVRKQDL 559
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-565 |
4.28e-56 |
|
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: 196.37 E-value: 4.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgD 161
Cdd:cd12118 31 TWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV-D 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 EVIQEVDTVASECPSLriKLLVSEKSCDgwlnfkkllneastthhcvetgsqeASAIYFTSGTSGLPKMAEHSYSSLGLK 241
Cdd:cd12118 109 REFEYEDLLAEGDPDF--EWIPPADEWD-------------------------PIALNYTSGTTGRPKGVVYHHRGAYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 242 AKMDAGWTGLQASDI-MWTISD---TGWILnilgslleSWTLGACTFVHL-LPKFDPLVILKTLSSYPIKSMMGAPIVYR 316
Cdd:cd12118 162 ALANILEWEMKQHPVyLWTLPMfhcNGWCF--------PWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGAPTVLN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 317 MLLQ-QDLSSYKFPHLQNCLAGGESLLPETLENwRAQTGLDIREFYGQTET---GLTCMVSKT-----------MKIKPG 381
Cdd:cd12118 234 MLANaPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVCAWKPEwdelpteerarLKARQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 382 --YMGTAAscydVQVIDDKGNVLPPG---TEGDIGIRvkpirpiG--IFSGYVENPDKTAANIRGDFWLLGDRGIKDEDG 454
Cdd:cd12118 313 vrYVGLEE----VDVLDPETMKPVPRdgkTIGEIVFR-------GniVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 455 YFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILasqflsHDPEQLT-KELQQHVKS 533
Cdd:cd12118 382 YIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL------KEGAKVTeEEIIAFCRE 455
|
490 500 510
....*....|....*....|....*....|..
gi 157311624 534 VTAPYKYPRKIEFVlNLPKTVTGKIQRTKLRD 565
Cdd:cd12118 456 HLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
81-574 |
1.21e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 195.51 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:PRK08276 12 VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETgsqEASAIYFTSGTSGLPK----------- 229
Cdd:PRK08276 91 AALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADET---AGADMLYSSGTTGRPKgikrplpgldp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 230 --MAEHSYSSLGLKAKMDAGWTGLQASDIMWTiSDTGWILNILgslleswTLGAcTFVhLLPKFDPLVILKTLSSYPIKS 307
Cdd:PRK08276 168 deAPGMMLALLGFGMYGGPDSVYLSPAPLYHT-APLRFGMSAL-------ALGG-TVV-VMEKFDAEEALALIERYRVTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 308 MMGAPIVY-RML-LQQ------DLSSYKFphlqnCLAGGESLLPET----LENWraqtGLDIREFYGQTET-GLTCMVSK 374
Cdd:PRK08276 238 SQLVPTMFvRMLkLPEevraryDVSSLRV-----AIHAAAPCPVEVkramIDWW----GPIIHEYYASSEGgGVTVITSE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 375 TMKIKPGYMGTAASCyDVQVIDDKGNVLPPGTEGDIGIRvkpiRPIGIFSgYVENPDKTAANIRGDFWL-LGDRGIKDED 453
Cdd:PRK08276 309 DWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE----MDGYPFE-YHNDPEKTAAARNPHGWVtVGDVGYLDED 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 454 GYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASqflSHDP-EQLTKELQQHVK 532
Cdd:PRK08276 383 GYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPAD---GADAgDALAAELIAWLR 459
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 157311624 533 SVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEWKMSGKA 574
Cdd:PRK08276 460 GRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQRA 501
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
78-565 |
4.72e-55 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 194.98 E-value: 4.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 78 ELMWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 157
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 VAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGW-LNFKKL-LNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSY 235
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpAGWSTApLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 SSLGLKAKMDAGWTGLQASDIMWT---ISDTgwilNILGSLLESwTLGACTFVhLLPKF------DPLVILKTLSSYPIK 306
Cdd:PRK06155 203 AQFYWWGRNSAEDLEIGADDVLYTtlpLFHT----NALNAFFQA-LLAGATYV-LEPRFsasgfwPAVRRHGATVTYLLG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 307 SMMgapivyRMLLQQDLSSYKFPH-LQNCLAGGESllPETLENWRAQTGLDIREFYGQTETGLTCMVSKTMKiKPGYMGT 385
Cdd:PRK06155 277 AMV------SILLSQPARESDRAHrVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 386 AASCYDVQVIDDKGNVLPPGTEGDIGIRVKPirPIGIFSGYVENPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADD 464
Cdd:PRK06155 348 LAPGFEARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWR-NLWFhTGDRVVRDADGWFRFVDRIKD 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 465 IINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAfVILASQFLSHDPEqltkELQQHVKSVTAPYKYPRKI 544
Cdd:PRK06155 425 AIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMA-AVVLRDGTALEPV----ALVRHCEPRLAYFAVPRYV 499
|
490 500
....*....|....*....|.
gi 157311624 545 EFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK06155 500 EFVAALPKTENGKVQKFVLRE 520
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
68-564 |
1.15e-54 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 193.36 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 68 ALWWVNGKGKELMWNFRELSENSQQAANiLSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILY 147
Cdd:PRK08008 25 ALIFESSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 148 RLQMSKAKAIVAGDE---VIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTT-HHCVETGSQEASAIYFTSG 223
Cdd:PRK08008 104 ILQNSQASLLVTSAQfypMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPATlCYAPPLSTDDTAEILFTSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 224 TSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGAcTFVhLLPKFDPLVILKTLSSY 303
Cdd:PRK08008 184 TTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGA-TFV-LLEKYSARAFWGQVCKY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 304 PIKSMMGAPIVYRMLLQQDLSSYKFPHlqnCLAGGESLLPETLENWRA-QTGLDIREF--YGQTETgLTCMVSKTmkikP 380
Cdd:PRK08008 262 RATITECIPMMIRTLMVQPPSANDRQH---CLREVMFYLNLSDQEKDAfEERFGVRLLtsYGMTET-IVGIIGDR----P 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 381 G------YMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPIgiFSGYVENPDKTAANIRGDFWL-LGDRGIKDED 453
Cdd:PRK08008 334 GdkrrwpSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTI--FKEYYLDPKATAKVLEADGWLhTGDTGYVDEE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 454 GYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflshDPEQLTKE-LQQHVK 532
Cdd:PRK08008 412 GFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN------EGETLSEEeFFAFCE 485
|
490 500 510
....*....|....*....|....*....|..
gi 157311624 533 SVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:PRK08008 486 QNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
83-565 |
8.41e-54 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 193.43 E-value: 8.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLI-------FMPGTIQMkstdilyRLQMSKAK 155
Cdd:PRK00174 101 YRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvfggFSAEALAD-------RIIDAGAK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 156 AIVAGDEVI---------QEVDTVASECPSLRiKLLVSEKSC---------DGWLNfkKLLNEASTTHHCVETGSQEASA 217
Cdd:PRK00174 173 LVITADEGVrggkpiplkANVDEALANCPSVE-KVIVVRRTGgdvdwvegrDLWWH--ELVAGASDECEPEPMDAEDPLF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 218 IYFTSGTSGLPKMAEHS------YSSLGLKAKMDagwtgLQASDIMWTISDTGWILN----ILGSLLEswtlGACTfvhl 287
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHTtggylvYAAMTMKYVFD-----YKDGDVYWCTADVGWVTGhsyiVYGPLAN----GATT---- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 288 lpkfdplVILKTLSSYPIKSMMG-------------APIVYRMLLQQ--------DLSSYKfphlqncLAG--GESLLPE 344
Cdd:PRK00174 317 -------LMFEGVPNYPDPGRFWevidkhkvtifytAPTAIRALMKEgdehpkkyDLSSLR-------LLGsvGEPINPE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 345 TLENWRAQTGLD---IREFYGQTETGlTCMVSK---TMKIKPGymgtaaSC------YDVQVIDDKGNVLPPGTEGDIGI 412
Cdd:PRK00174 383 AWEWYYKVVGGErcpIVDTWWQTETG-GIMITPlpgATPLKPG------SAtrplpgIQPAVVDEEGNPLEGGEGGNLVI 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 413 RvKP----IRPI---------GIFSGYvenPDKtaanirgdfWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVE 479
Cdd:PRK00174 456 K-DPwpgmMRTIygdherfvkTYFSTF---KGM---------YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 480 NALMKHPAVVETAVISSPDPVRGEVVKAFVILASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 558
Cdd:PRK00174 523 SALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKG---GEEPsDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKI 599
|
....*..
gi 157311624 559 QRTKLRD 565
Cdd:PRK00174 600 MRRILRK 606
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
75-566 |
5.10e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 189.22 E-value: 5.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 75 KGKELMWnfRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKA 154
Cdd:PRK07786 39 LGNTTTW--RELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 155 KAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHS 234
Cdd:PRK07786 116 HVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 235 YSSLGLKAkmdagWTGLQASDIMwTISDTGWI------LNILGSLLESWTLGACTFVHLLPKFDPLVILKTLSSYPIKSM 308
Cdd:PRK07786 196 HANLTGQA-----MTCLRTNGAD-INSDVGFVgvplfhIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 309 MGAPIVYRMLL------QQDLSsykfphLQNcLAGGESLLPETLENWRAQT--GLDIREFYGQTE-TGLTCMVSKTMKI- 378
Cdd:PRK07786 270 FLVPAQWQAVCaeqqarPRDLA------LRV-LSWGAAPASDTLLRQMAATfpEAQILAAFGQTEmSPVTCMLLGEDAIr 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 379 KPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQF 458
Cdd:PRK07786 343 KLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP-----TLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 459 MGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASqflshDPEQLT-KELQQHVKSVTAP 537
Cdd:PRK07786 418 VDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN-----DDAALTlEDLAEFLTDRLAR 492
|
490 500
....*....|....*....|....*....
gi 157311624 538 YKYPRKIEFVLNLPKTVTGKIQRTKLRDK 566
Cdd:PRK07786 493 YKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
38-569 |
5.85e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 189.86 E-value: 5.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 38 QEVPAKFNFASDVLDHWadMEKAGKRLPS-PALWWVngkGKELmwNFRELSENSQQAANILSgACGLQRGDRVAVMLPRV 116
Cdd:PRK06710 13 EEIPSTISYDIQPLHKY--VEQMASRYPEkKALHFL---GKDI--TFSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 117 PEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpSLRIKLLVSEKSCDgWLNFKK 196
Cdd:PRK06710 85 PQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQS---ATKIEHVIVTRIAD-FLPFPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 197 LL----------------NEASTTH--HCVE----TG-------SQEASAIYFTSGTSGLPKMAEHSYSSLglkakmdag 247
Cdd:PRK06710 161 NLlypfvqkkqsnlvvkvSESETIHlwNSVEkevnTGvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNL--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 248 wtglqasdIMWTISDTGWILNILGSllESWTLGACTFVH-------------------LLPKFDPLVILKTLSSYPIKSM 308
Cdd:PRK06710 232 --------VSNTLMGVQWLYNCKEG--EEVVLGVLPFFHvygmtavmnlsimqgykmvLIPKFDMKMVFEAIKKHKVTLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 309 MGAPIVYRMLLQQDL-SSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETG-LTCMVSKTMKIKPGYMGTA 386
Cdd:PRK06710 302 PGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 387 ASCYDVQVID-DKGNVLPPGTEGDIGIRVKPIrpigiFSGYVENPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADD 464
Cdd:PRK06710 382 WPDTEAMIMSlETGEALPPGEIGEIVVKGPQI-----MKGYWNKPEETAAVLQ-DGWLhTGDVGYMDEDGFFYVKDRKKD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 465 IINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIlasqfLSHDPEQLTKELQQHVKSVTAPYKYPRKI 544
Cdd:PRK06710 456 MIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVV-----LKEGTECSEEELNQFARKYLAAYKVPKVY 530
|
570 580
....*....|....*....|....*
gi 157311624 545 EFVLNLPKTVTGKIQRTKLRDKEWK 569
Cdd:PRK06710 531 EFRDELPKTTVGKILRRVLIEEEKR 555
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
83-564 |
6.33e-53 |
|
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: 186.43 E-value: 6.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:cd05903 4 YSELDTRADRLAAGLA-ALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 viqevdtvasecpslrikllvsekscdgwlnFKKllneasttHHCVETGSQEAsAIYFTSGTSGLPKMAEHSYSSLGLKA 242
Cdd:cd05903 83 -------------------------------FRQ--------FDPAAMPDAVA-LLLFTSGTTGEPKGVMHSHNTLSASI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 243 KMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACtfVHLLPKFDPLVILKTLSSYPIKSMMGA-PIVYRMLLQQ 321
Cdd:cd05903 123 RQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAP--VVLQDIWDPDKALALMREHGVTFMMGAtPFLTDLLNAV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 322 DLSSYKFPHLQNCLAGGESLLPETLEnwRAQTGLDIREF--YGQTETGltcmvSKTMKIKPGYMGtAASCYD-------- 391
Cdd:cd05903 201 EEAGEPLSRLRTFVCGGATVPRSLAR--RAAELLGAKVCsaYGSTECP-----GAVTSITPAPED-RRLYTDgrplpgve 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 392 VQVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGY 471
Cdd:cd05903 273 IKVVDDTGATLAPGVEGELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 472 RIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILasqflsHDPEQLT-KELQQHVKSV-TAPYKYPRKIEFVLN 549
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVT------KSGALLTfDELVAYLDRQgVAKQYWPERLVHVDD 421
|
490
....*....|....*
gi 157311624 550 LPKTVTGKIQRTKLR 564
Cdd:cd05903 422 LPRTPSGKVQKFRLR 436
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
60-576 |
2.25e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 187.12 E-value: 2.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 60 AGKRLPS-PALWWVNGKgkelmWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVI-----LGCIRAGLIF 133
Cdd:PRK06188 21 ALKRYPDrPALVLGDTR-----LTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMAIgaaqlAGLRRTALHP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 134 MpGTIQmkstDILYRLQMSKAKAIVAGDEVIQE-VDTVASECPSLRIKLLVSEksCDGWLNFKKLLNEASTTHHCVETGS 212
Cdd:PRK06188 95 L-GSLD----DHAYVLEDAGISTLIVDPAPFVErALALLARVPSLKHVLTLGP--VPDGVDLLAAAAKFGPAPLVAAALP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 213 QEASAIYFTSGTSGLPKMAEHSYSSLglkakmdAGWTGLQASDIMW----------TISDTGWILnILGSLLESWTlgac 282
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRSI-------ATMAQIQLAEWEWpadprflmctPLSHAGGAF-FLPTLLRGGT---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 283 tfVHLLPKFDPLVILKTLSSYPIKSMMGAP-IVYRMLLQQDLSSYKFPHLQNCLAGGESLLPEtlenwRAQTGLDI---- 357
Cdd:PRK06188 236 --VIVLAKFDPAEVLRAIEEQRITATFLVPtMIYALLDHPDLRTRDLSSLETVYYGASPMSPV-----RLAEAIERfgpi 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 358 -REFYGQTETGLTCMVSKTMKIKPGYMGTAASC------YDVQVIDDKGNVLPPGTEGDIGIRvKPIrpigIFSGYVENP 430
Cdd:PRK06188 309 fAQYYGQTEAPMVITYLRKRDHDPDDPKRLTSCgrptpgLRVALLDEDGREVAQGEVGEICVR-GPL----VMDGYWNRP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 431 DKTAANIRGDfWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFV 509
Cdd:PRK06188 384 EETAEAFRDG-WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157311624 510 ILASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEWkmSGKARA 576
Cdd:PRK06188 463 VLRPG-AAVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYW--EGRGRA 522
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
81-564 |
2.80e-52 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 189.01 E-value: 2.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGlIFMPGTIQMKSTDILYRLQMSKAKAIVA- 159
Cdd:PRK07529 59 WTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 160 ----GDEVIQEVDTVASECPSLR-----------------IKLLVSEKSCDGWLNFKKLLNEASTTHHCVET--GSQEAS 216
Cdd:PRK07529 137 gpfpGTDIWQKVAEVLAALPELRtvvevdlarylpgpkrlAVPLIRRKAHARILDFDAELARQPGDRLFSGRpiGPDDVA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 217 AIYFTSGTSGLPKMAEHSYSSLglkakmdagwtglqasdimwtISDtGWILNILGSLLESWTL---------GACTFVHL 287
Cdd:PRK07529 217 AYFHTGGTTGMPKLAQHTHGNE---------------------VAN-AWLGALLLGLGPGDTVfcglplfhvNALLVTGL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 288 LPKF--------------DPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-----DLSSYKFphlqncLAGGESLLP-E 344
Cdd:PRK07529 275 APLArgahvvlatpqgyrGPGVIanfWKIVERYRINFLSGVPTVYAALLQVpvdghDISSLRY------ALCGAAPLPvE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 345 TLENWRAQTGLDIREFYGQTETglTCMVS---KTMKIKPGYMGTAASCYDVQVI--DDKGNVLPPGTEGDIGIRVkpIRP 419
Cdd:PRK07529 349 VFRRFEAATGVRIVEGYGLTEA--TCVSSvnpPDGERRIGSVGLRLPYQRVRVVilDDAGRYLRDCAVDEVGVLC--IAG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 420 IGIFSGYVEnPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPD 498
Cdd:PRK07529 425 PNVFSGYLE-AAHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPD 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157311624 499 PVRGEVVKAFVILA--SQFlshDPEQLTKELQQHVKSVTApykYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:PRK07529 504 AHAGELPVAYVQLKpgASA---TEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
78-565 |
1.91e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 185.36 E-value: 1.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 78 ELMWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 157
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 VAGD--------EVIQEV--DTVASEC--------PSLRIKLLVSEKSCDGWLNFKKLLNEAST-THHCVETGSQ----- 213
Cdd:PRK12583 122 ICADafktsdyhAMLQELlpGLAEGQPgalacerlPELRGVVSLAPAPPPGFLAWHELQARGETvSREALAERQAsldrd 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 214 EASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDT----GWILNILGSLleswTLGACTfvhLLP 289
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhcfGMVLANLGCM----TVGACL---VYP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 290 K--FDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQTGL-DIREFYGQTE 365
Cdd:PRK12583 275 NeaFDPLATLQAVEEERCTALYGVPTMFIAELDHpQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 366 TG----LTCmVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTAANIRGDF 441
Cdd:PRK12583 355 TSpvslQTT-AADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTR-----GYSVMKGYWNNPEATAESIDEDG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 442 WL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILasqflsHDP 520
Cdd:PRK12583 429 WMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRL------HPG 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 157311624 521 EQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK12583 503 HAASeEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
76-573 |
3.93e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 184.58 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 76 GKELmwNFRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAK 155
Cdd:PRK05677 47 GKTL--TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 156 AIVA-------GDEVIQE-------VDTVASECPSLR----------IKLLVSEKSCDGWLNFKKLLNE-ASTTHHCVET 210
Cdd:PRK05677 125 ALVClanmahlAEKVLPKtgvkhviVTEVADMLPPLKrllinavvkhVKKMVPAYHLPQAVKFNDALAKgAGQPVTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 211 GSQEASAIYFTSGTSGLPK--MAEHSysslGLKAKMdagwtgLQASDIMWTISDTGwiLNILGSLLESWTLGACTFvHLL 288
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKgaMLTHR----NLVANM------LQCRALMGSNLNEG--CEILIAPLPLYHIYAFTF-HCM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 289 --------------PKFDPLVIlKTLSSYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCLAGGESLLPETLENWRAQT 353
Cdd:PRK05677 272 ammlignhnilisnPRDLPAMV-KELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKEVT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 354 GLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKT 433
Cdd:PRK05677 351 GCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GP----QVMKGYWQRPEAT 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 434 AANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILA 512
Cdd:PRK05677 426 DEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVK 505
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157311624 513 SQflshdpEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEWKMSGK 573
Cdd:PRK05677 506 PG------ETLTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAGL 561
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
76-563 |
7.05e-51 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 182.37 E-value: 7.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 76 GKELMWNFRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAK 155
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 156 AIVAGDE---VIQEVDTVASECPSLRIKLL--VSEKSCDGWlnfkkllneastthhcVETGSQEASAIYFTSGTSGLPKM 230
Cdd:PRK06839 103 VLFVEKTfqnMALSMQKVSYVQRVISITSLkeIEDRKIDNF----------------VEKNESASFIICYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 231 AEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILGSLLESWTLGACTFVHllPKFDPLVILKTLSSYPIKSMMG 310
Cdd:PRK06839 167 AVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVP--RKFEPTKALSMIEKHKVTVVMG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 311 APIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLlPETLENWRAQTGLDIREFYGQTETGLTC-MVSKT-MKIKPGYMGTAA 387
Cdd:PRK06839 245 VPTIHQALINCsKFETTNLQSVRWFYNGGAPC-PEELMREFIDRGFLFGQGFGMTETSPTVfMLSEEdARRKVGSIGKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 388 SCYDVQVIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIIN 467
Cdd:PRK06839 324 LFCDYELIDENKNKVEVGEVGELLIR-GP----NVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMII 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 468 SSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDpeqltKELQQHVKSVTAPYKYPRKIEFV 547
Cdd:PRK06839 399 SGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPKEIVFL 473
|
490
....*....|....*.
gi 157311624 548 LNLPKTVTGKIQRTKL 563
Cdd:PRK06839 474 KELPKNATGKIQKAQL 489
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
66-563 |
1.29e-50 |
|
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: 180.42 E-value: 1.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 66 SPALWWVNGKgkelmWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdi 145
Cdd:cd05930 3 AVAVVDGDQS-----LTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVP---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 146 lyrlqmskakaivagdeviqeVDTvasECPSLRIKLLVSEkscdgwlnfkkllneasTTHHCVETGSQEASAIYFTSGTS 225
Cdd:cd05930 67 ---------------------LDP---SYPAERLAYILED-----------------SGAKLVLTDPDDLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 226 GLPK--MAEHS-----YSSLGLKAKMDAGWTGLQASDIMWTISdtgwILNILGSLLEswtlGACtfVHLLPK---FDPLV 295
Cdd:cd05930 106 GKPKgvMVEHRglvnlLLWMQEAYPLTPGDRVLQFTSFSFDVS----VWEIFGALLA----GAT--LVVLPEevrKDPEA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 296 ILKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPHLQNCLAGGESLLPETLENWRAQ-TGLDIREFYGQTET--GLTCMV 372
Cdd:cd05930 176 LADLLAEEGITVLHLTPSLLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtvDATYYR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 373 SKTMKIKPGYM--GTAASCYDVQVIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVENPDKTAANIRGDFWLL--- 444
Cdd:cd05930 255 VPPDDEEDGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELyigGA--------GLARGYLNRPELTAERFVPNPFGPger 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 445 ----GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflsHDP 520
Cdd:cd05930 327 myrtGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPD-----EGG 401
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 157311624 521 EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd05930 402 ELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
76-565 |
3.39e-49 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 179.06 E-value: 3.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 76 GKELmwNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMpgtiqmkSTDILY-------R 148
Cdd:PRK07059 46 GKAI--TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV-------NVNPLYtprelehQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 149 LQMSKAKAIV-------AGDEVIQEVDT----VASECPSL------------RIKLLVSEKSCDGWLNFKKLLNE-ASTT 204
Cdd:PRK07059 116 LKDSGAEAIVvlenfatTVQQVLAKTAVkhvvVASMGDLLgfkghivnfvvrRVKKMVPAWSLPGHVRFNDALAEgARQT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 205 HHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS-LGLKAKMDAgWtgLQASDIMWTISDTgwiLNILGSL--LESWTLGA 281
Cdd:PRK07059 196 FKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNiVANVLQMEA-W--LQPAFEKKPRPDQ---LNFVCALplYHIFALTV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 282 CTFVH--------LLPkfDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENW 349
Cdd:PRK07059 270 CGLLGmrtggrniLIP--NPRDIpgfIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAERW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 350 RAQTGLDIREFYGQTETG--LTCMVSKTMKIKpGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSG 425
Cdd:PRK07059 348 LEMTGCPITEGYGLSETSpvATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-------GpqVMAG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 426 YVENPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEV 504
Cdd:PRK07059 420 YWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEA 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157311624 505 VKAFVIlasqflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK07059 500 VKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-565 |
9.01e-49 |
|
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: 177.05 E-value: 9.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSGAcGLQRGDRVAVML---PRVPEWWLVILGcirAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 158
Cdd:cd12119 27 TYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYAVPG---MGAVLHTINPRLFPEQIAYIINHAEDRVVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 159 AGDEVIQEVDTVASECPSLRIKLLVS------EKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 232
Cdd:cd12119 103 VDRDFLPLLEAIAPRLPTVEHVVVMTddaampEPAGVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 233 HSYSSLGLKA--KMDAGWTGLQASDIMWTISD----TGWILNILGSLLeswtlGACtfvHLLP--KFDPLVILKTLSSYP 304
Cdd:cd12119 183 YSHRSLVLHAmaALLTDGLGLSESDVVLPVVPmfhvNAWGLPYAAAMV-----GAK---LVLPgpYLDPASLAELIEREG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 305 IKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCLAGGeSLLPETLENWRAQTGLDIREFYGQTETGLTCMVSK--------- 374
Cdd:cd12119 255 VTFAAGVPTVWQGLLDhLEANGRDLSSLRRVVIGG-SAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARppsehsnls 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 375 -----TMKIKPGYmgtaaSCYDVQ--VIDDKGNVLP--PGTEGDIGIRvKPIrpigIFSGYVENPDKTAANIRGDFWLLG 445
Cdd:cd12119 334 edeqlALRAKQGR-----PVPGVElrIVDDDGRELPwdGKAVGELQVR-GPW----VTKSYYKNDEESEALTEDGWLRTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 446 DRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflshDPEQLT- 524
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLK------EGATVTa 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 157311624 525 KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:cd12119 478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
62-560 |
9.11e-48 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 176.29 E-value: 9.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 62 KRLPSPALWWVNGK-GKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLI-------F 133
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfggF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 134 mpgtiqmKSTDILYRLQMSKAKAIV---AG-------------DEVIQE----------VDTVASECP----------SL 177
Cdd:PRK10524 144 -------ASHSLAARIDDAKPVLIVsadAGsrggkvvpykpllDEAIALaqhkprhvllVDRGLAPMArvagrdvdyaTL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 178 RIKLLVSEKSCDgWLNfkkllneastthhcvetgSQEASAIYFTSGTSGLPKMAEHS---YSsLGLKAKMDAGWTGlQAS 254
Cdd:PRK10524 217 RAQHLGARVPVE-WLE------------------SNEPSYILYTSGTTGKPKGVQRDtggYA-VALATSMDTIFGG-KAG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 255 DIMWTISDTGWIL----NILGSLLEswtlGACTFVH----LLPkfDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---L 323
Cdd:PRK10524 276 ETFFCASDIGWVVghsyIVYAPLLA----GMATIMYeglpTRP--DAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 324 SSYKFPHLQNCLAGGESLlPETLENWRAQT-GLDIREFYGQTETGLTCMVS----KTMKIKPGYMGTAASCYDVQVIDDK 398
Cdd:PRK10524 350 RKHDLSSLRALFLAGEPL-DEPTASWISEAlGVPVIDNYWQTETGWPILAIargvEDRPTRLGSPGVPMYGYNVKLLNEV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 399 -GNVLPPGTEGDIGIRvkPIRPIGIFSgyvenpdktaaNIRGD-------FWLLGDR--------GIKDEDGYFQFMGRA 462
Cdd:PRK10524 429 tGEPCGPNEKGVLVIE--GPLPPGCMQ-----------TVWGDddrfvktYWSLFGRqvystfdwGIRDADGYYFILGRT 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 463 DDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQ---LTKELQQHVKSVTAPYK 539
Cdd:PRK10524 496 DDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVA 575
|
570 580
....*....|....*....|.
gi 157311624 540 YPRKIEFVLNLPKTVTGKIQR 560
Cdd:PRK10524 576 RPARVWFVSALPKTRSGKLLR 596
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
82-564 |
1.79e-47 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 173.27 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 EVIQEVDTVASECPsLRIKLlvsEKSCDGWLNFKKLLNEAS---TTHHCvetgsqeASAIYFTSGTSGLPKMAEHSYSSL 238
Cdd:PRK13390 105 ALDGLAAKVGADLP-LRLSF---GGEIDGFGSFEAALAGAGprlTEQPC-------GAVMLYSSGTTGFPKGIQPDLPGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 239 GLKAKMD------AGWTGLQASDIMWTISdtgwilnilgSLLESWTLGACTFVHLL-------PKFDPLVILKTLSSYPI 305
Cdd:PRK13390 174 DVDAPGDpivaiaRAFYDISESDIYYSSA----------PIYHAAPLRWCSMVHALggtvvlaKRFDAQATLGHVERYRI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 306 KSMMGAPIVYRMLLQQD---LSSYKFPHLQNCLAGGESL---LPETLENWraqTGLDIREFYGQTET-GLTCMVSKTMKI 378
Cdd:PRK13390 244 TVTQMVPTMFVRLLKLDadvRTRYDVSSLRAVIHAAAPCpvdVKHAMIDW---LGPIVYEYYSSTEAhGMTFIDSPDWLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 379 KPGYMGTAAsCYDVQVIDDKGNVLPPGTEGDIGIRvkpiRPIGIFSgYVENPDKTAA--NIRGDFWL-LGDRGIKDEDGY 455
Cdd:PRK13390 321 HPGSVGRSV-LGDLHICDDDGNELPAGRIGTVYFE----RDRLPFR-YLNDPEKTAAaqHPAHPFWTtVGDLGSVDEDGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 456 FQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlshDP-EQLTKELQQHVKSV 534
Cdd:PRK13390 395 LYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI---RGsDELARELIDYTRSR 471
|
490 500 510
....*....|....*....|....*....|
gi 157311624 535 TAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:PRK13390 472 IAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
83-565 |
2.11e-47 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 174.29 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:PRK08751 53 YREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 VIQEVDTVASECPSLR------------------------IKLLVSEKSCDGWLNFKKLLneASTTHHCVETGSQEASAI 218
Cdd:PRK08751 133 FGTTVQQVIADTPVKQvittglgdmlgfpkaalvnfvvkyVKKLVPEYRINGAIRFREAL--ALGRKHSMPTLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 219 YF---TSGTSGLPKMAEHSYSSLGLKAKMDAGWTG-----LQASDIMWTISDTGWILNILGSLLESWTLGACTfvHLL-- 288
Cdd:PRK08751 211 AFlqyTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEVVITALPLYHIFALTANGLVFMKIGGCN--HLIsn 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 289 PKFDPLVIlKTLSSYPIKSMMGAPIVYRMLL------QQDLSSYKFphlqnCLAGGESLLPETLENWRAQTGLDIREFYG 362
Cdd:PRK08751 289 PRDMPGFV-KELKKTRFTAFTGVNTLFNGLLntpgfdQIDFSSLKM-----TLGGGMAVQRSVAERWKQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 363 QTETG-LTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANIRGDF 441
Cdd:PRK08751 363 LTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-GP----QVMKGYWKRPEETAKVMDADG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 442 WL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIlasqflSHDP 520
Cdd:PRK08751 438 WLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------KKDP 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 157311624 521 EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK08751 512 ALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
102-564 |
2.77e-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: 171.85 E-value: 2.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 102 GLQRGDRVAVMLPRVPEWWLVILGCIRAG----LIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSL 177
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 178 RIKLLVsekscDGWLNfkkllNEASTTHHCVEtgSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIM 257
Cdd:cd05922 94 GTVLDA-----DGIRA-----ARASAPAHEVS--HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 258 WTISDTGWILNiLGSLLESWTLGACTFVHLLPKFDPLVIlKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAG 337
Cdd:cd05922 162 LTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 338 GESLLPETLENWR-AQTGLDIREFYGQTET--GLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRv 414
Cdd:cd05922 240 GGRLPQETIARLReLLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHR- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 415 kpiRPIGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVI 494
Cdd:cd05922 319 ---GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAV 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 495 SSPDPVrGEVVKAFVILasqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd05922 396 GLPDPL-GEKLALFVTA-------PDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
270-560 |
1.01e-46 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 167.06 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 270 LGSLLESWTLGACTFVhlLPKFDPLVILKTLSSYPIkSMMG--APIVYRMLLQQDLSSYKFPHLQNcLAGGESllPETLE 347
Cdd:cd17637 56 LNLALATFHAGGANVV--MEKFDPAEALELIEEEKV-TLMGsfPPILSNLLDAAEKSGVDLSSLRH-VLGLDA--PETIQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 348 NWRAQTGLDIREFYGQTET-GLTCMVSKTMKikPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGY 426
Cdd:cd17637 130 RFEETTGATFWSLYGQTETsGLVTLSPYRER--PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR-GP----LVFQGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 427 VENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGR--ADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEV 504
Cdd:cd17637 203 WNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEG 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157311624 505 VKAFVIL-ASQFLShdpeqlTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd17637 283 IKAVCVLkPGATLT------ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
100-564 |
3.85e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 169.01 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 100 ACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgdeviqEVDTVASECPSLRI 179
Cdd:PRK07787 39 AERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLG------PAPDDPAGLPHVPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 180 KLlvsekscdgwlnfkkllnEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL--GLKAKMDAgWTglqasdim 257
Cdd:PRK07787 113 RL------------------HARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIaaDLDALAEA-WQ-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 258 WTISDT-----------GWILNILGSLleswTLGAcTFVHLLpKFDPLVILKTLSSYpiKSMM-GAPIVYRMLLQQdlss 325
Cdd:PRK07787 166 WTADDVlvhglplfhvhGLVLGVLGPL----RIGN-RFVHTG-RPTPEAYAQALSEG--GTLYfGVPTVWSRIAAD---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 326 ykfPHLQNCLAG------GESLLPET-LENWRAQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDDK 398
Cdd:PRK07787 234 ---PEAARALRGarllvsGSAALPVPvFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 399 GNVLPPGTE--GDIGIRvKPirpiGIFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR-ADDIINSSGYRIG 474
Cdd:PRK07787 311 GGPVPHDGEtvGELQVR-GP----TLFDGYLNRPDATAAAFTADGWFrTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 475 PSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIlasqflSHDPEQLTkELQQHVKSVTAPYKYPRKIEFVLNLPKTV 554
Cdd:PRK07787 386 AGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV------GADDVAAD-ELIDFVAQQLSVHKRPREVRFVDALPRNA 458
|
490
....*....|
gi 157311624 555 TGKIQRTKLR 564
Cdd:PRK07787 459 MGKVLKKQLL 468
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
81-577 |
6.38e-46 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 169.99 E-value: 6.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAAnilSG--ACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMpgTIQ--MKSTDILYRLQMSKAKA 156
Cdd:PRK08315 44 WTYREFNEEVDALA---KGllALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV--TINpaYRLSELEYALNQSGCKA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 157 IVAGDEV-----IQEVDTVASEC-------------PSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHcVETGSQEASA- 217
Cdd:PRK08315 119 LIAADGFkdsdyVAMLYELAPELatcepgqlqsarlPELRRVIFLGDEKHPGMLNFDELLALGRAVDD-AELAARQATLd 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 218 ------IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASD---I---------MwtisdtgwILNILGSLleswTL 279
Cdd:PRK08315 198 pddpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrlcIpvplyhcfgM--------VLGNLACV----TH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 280 GACTfVHLLPKFDPLVILKTLSS------YPIKSMMGAPIVYRMLLQQDLSSykfphlqncL-----AGgeSLLP-ETLE 347
Cdd:PRK08315 266 GATM-VYPGEGFDPLATLAAVEEerctalYGVPTMFIAELDHPDFARFDLSS---------LrtgimAG--SPCPiEVMK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 348 nwRAQTGLDIREF---YGQTETG-LTCM----------VSKTMKIKPGYmgtaascyDVQVID-DKGNVLPPGTEGDIGI 412
Cdd:PRK08315 334 --RVIDKMHMSEVtiaYGMTETSpVSTQtrtddplekrVTTVGRALPHL--------EVKIVDpETGETVPRGEQGELCT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 413 RvkpirpiG--IFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVV 489
Cdd:PRK08315 404 R-------GysVMKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 490 ETAVISSPDPVRGEVVKAFVILasqflsHDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEW 568
Cdd:PRK08315 477 DVQVVGVPDEKYGEEVCAWIIL------RPGATLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMI 550
|
....*....
gi 157311624 569 KMSGKARAQ 577
Cdd:PRK08315 551 EELGLQAAK 559
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
39-574 |
1.15e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 169.46 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 39 EVPAKFNfaSDVLDHWADM-EKAGKRLPS-PAlwWVNgKGKELmwNFRELSENSQQAANILSGACGLQRGDRVAVMLPRV 116
Cdd:PRK08974 12 DVPAEIN--PDRYQSLVDMfEQAVARYADqPA--FIN-MGEVM--TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 117 PEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECP------------------SL- 177
Cdd:PRK08974 85 LQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPvkhviltrmgdqlstakgTLv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 178 -----RIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASA-IYFTSGTSGLPK--MAEHSYSSLGLkakmdagwt 249
Cdd:PRK08974 165 nfvvkYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAfLQYTGGTTGVAKgaMLTHRNMLANL--------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 250 gLQASDIMWTISDTGWILNILGSLLE---SWTLGACTFVHL------------LPKFdplviLKTLSSYPIKSMMGAPIV 314
Cdd:PRK08974 236 -EQAKAAYGPLLHPGKELVVTALPLYhifALTVNCLLFIELggqnllitnprdIPGF-----VKELKKYPFTAITGVNTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 315 YRMLLQ-QDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETG-LTCMVSKTMKIKPGYMGTAASCYDV 392
Cdd:PRK08974 310 FNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 393 QVIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVENPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADDIINSS 469
Cdd:PRK08974 390 KLVDDDGNEVPPGEPGELWVK-------GpqVMLGYWQRPEATDEVIK-DGWLaTGDIAVMDEEGFLRIVDRKKDMILVS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 470 GYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLN 549
Cdd:PRK08974 462 GFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEE------ELITHCRRHLTGYKVPKLVEFRDE 535
|
570 580
....*....|....*....|....*
gi 157311624 550 LPKTVTGKIQRTKLRDKEWKMSGKA 574
Cdd:PRK08974 536 LPKSNVGKILRRELRDEARAKVDNK 560
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
102-565 |
2.29e-45 |
|
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: 168.09 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 102 GLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLR-IK 180
Cdd:cd17642 65 GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKtII 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 181 LLVSEKSCDGWL---NFKK-----LLNEASTTHHCVETGSQeASAIYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQ 252
Cdd:cd17642 145 ILDSKEDYKGYQclyTFITqnlppGFNEYDFKPPSFDRDEQ-VALIMNSSGSTGLPKGVQLTHKNI--VARFSHARDPIF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 253 ASDIMWTISdtgwILNILG-----SLLESWTLGACTF-VHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDL-SS 325
Cdd:cd17642 222 GNQIIPDTA----ILTVIPfhhgfGMFTTLGYLICGFrVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLvDK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 326 YKFPHLQNCLAGGESLLPETLENWRAQTGLD-IREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVID-DKGNVLP 403
Cdd:cd17642 298 YDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 404 PGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENAL 482
Cdd:cd17642 378 PNERGELCVKGP-----MIMKGYVNNPEATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESIL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 483 MKHPAVVETAVISSPDPVRGEVVKAFVILASQflshdpEQLT-KELQQHVKSVTAPYKYPR-KIEFVLNLPKTVTGKIQR 560
Cdd:cd17642 453 LQHPKIFDAGVAGIPDEDAGELPAAVVVLEAG------KTMTeKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDR 526
|
....*
gi 157311624 561 TKLRD 565
Cdd:cd17642 527 RKIRE 531
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
83-563 |
4.03e-45 |
|
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: 166.64 E-value: 4.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgde 162
Cdd:cd05904 35 YAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 viqeVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPK--MAEHSysslG 239
Cdd:cd05904 111 ----TAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQdDVAALLYSSGTTGRSKgvMLTHR----N 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 240 LKAkMDAGWTGLQASDI-----------MWTISDTGWILniLGSLleswTLGACTFVhlLPKFDPLVILKTLSSYPIKSM 308
Cdd:cd05904 183 LIA-MVAQFVAGEGSNSdsedvflcvlpMFHIYGLSSFA--LGLL----RLGATVVV--MPRFDLEELLAAIERYKVTHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 309 MGAP-IVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQ-TGLDIREFYGQTETG---LTCMVSKTMKIKPGYM 383
Cdd:cd05904 254 PVVPpIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTESTgvvAMCFAPEKDRAKYGSV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 384 GTAASCYDVQVID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR 461
Cdd:cd05904 334 GRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGYLNNPEATAATIDKEGWLhTGDLCYIDEDGYLFIVDR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 462 ADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQ-FLSHDpeqltkELQQHVKSVTAPYKY 540
Cdd:cd05904 409 LKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGsSLTED------EIMDFVAKQVAPYKK 482
|
490 500
....*....|....*....|...
gi 157311624 541 PRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd05904 483 VRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
83-567 |
1.49e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 166.26 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILsGACGLQRGDRVAVMlPRVPEWWLV-ILGCIRAGL-IFMPGT----IQMKstDILYRLqmsKAKA 156
Cdd:PRK07788 77 YAELDEQSNALARGL-LALGVRAGDGVAVL-ARNHRGFVLaLYAAGKVGArIILLNTgfsgPQLA--EVAARE---GVKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 157 IVAGDEVIQEVDTVASECPSLRIKLLVSEK---SCDGWLNFKKLLneASTTHHCVETGSQEASAIYFTSGTSGLPKMAEH 233
Cdd:PRK07788 150 LVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLI--AGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 234 ----SYSSLG-------LKAKMdagwTGLQASDIMWTisdTGW-ILNIlgslleSWTLGaCTFVhLLPKFDPLVILKTLS 301
Cdd:PRK07788 228 pepsPLAPLAgllsrvpFRAGE----TTLLPAPMFHA---TGWaHLTL------AMALG-STVV-LRRRFDPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 302 SYPIKSMMGAPIVYRMLLQQ--------DLSSYKFphlqnCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVS 373
Cdd:PRK07788 293 KHKATALVVVPVMLSRILDLgpevlakyDTSSLKI-----IFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIAT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 374 -KTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVkpirpiGI-FSGYVENPDKtaANIRGdfwLL--GDRGI 449
Cdd:PRK07788 368 pEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGN------GFpFEGYTDGRDK--QIIDG---LLssGDVGY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 450 KDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflshDPEQLTKE-LQ 528
Cdd:PRK07788 437 FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKA------PGAALDEDaIK 510
|
490 500 510
....*....|....*....|....*....|....*....
gi 157311624 529 QHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKE 567
Cdd:PRK07788 511 DYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
83-565 |
1.77e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 166.15 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD- 161
Cdd:PRK12492 52 YAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNm 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 --EVIQEVdtvaseCPSLRIKLLVSEKSCD------GWL---------------------NFKKLLNE-ASTTHHCVETG 211
Cdd:PRK12492 132 fgKLVQEV------LPDTGIEYLIEAKMGDllpaakGWLvntvvdkvkkmvpayhlpqavPFKQALRQgRGLSLKPVPVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 212 SQEASAIYFTSGTSGLPKMAEHSYSSLglKAKMdagwtgLQASDIMWTISDTGWILNILGS--------LLESWTLGA-- 281
Cdd:PRK12492 206 LDDIAVLQYTGGTTGLAKGAMLTHGNL--VANM------LQVRACLSQLGPDGQPLMKEGQevmiaplpLYHIYAFTAnc 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 282 -CTFV---HLLPKFDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQT 353
Cdd:PRK12492 278 mCMMVsgnHNVLITNPRDIpgfIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 354 GLDIREFYGQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDK 432
Cdd:PRK12492 358 GCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK-GP----QVMKGYWQQPEA 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 433 TAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIL 511
Cdd:PRK12492 433 TAEALDAEGWFkTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVA 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 157311624 512 ASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK12492 513 RDPGLSVE------ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
81-570 |
3.10e-44 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 163.98 E-value: 3.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGC--IRAGLIFMPGTIQMKstDILYRLQMSKAKAIV 158
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALqqLGAVAVLLNTRLSRE--ELLWQLDDAEVKCLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 159 AGDEVIQEVDTVA----SECPSLRIKLLVSEKSCDgwlnfkklLNEASTthhcvetgsqeasaIYFTSGTSGLPKMAEHS 234
Cdd:PRK03640 105 TDDDFEAKLIPGIsvkfAELMNGPKEEAEIQEEFD--------LDEVAT--------------IMYTSGTTGKPKGVIQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 235 Y---------SSLGLkakmdagwtGLQASDiMWTISDTgwILNI--LGSLLESWTLGaCTfVHLLPKFDPLVILKTLSSY 303
Cdd:PRK03640 163 YgnhwwsavgSALNL---------GLTEDD-CWLAAVP--IFHIsgLSILMRSVIYG-MR-VVLVEKFDAEKINKLLQTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 304 PIkSMMGApiVYRML--LQQDLSSYKFP-HLQNCLAGGESLLPETLENWRaQTGLDIREFYGQTETGltcmvSKTMKIKP 380
Cdd:PRK03640 229 GV-TIISV--VSTMLqrLLERLGEGTYPsSFRCMLLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETA-----SQIVTLSP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 381 GYM----GTAAS-CYDVQV-IDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVENPDKTAANIRgDFWL-LGDRGIKDED 453
Cdd:PRK03640 300 EDAltklGSAGKpLFPCELkIEKDGVVVPPFEEGEIVVKGPNVTK-----GYLNREDATRETFQ-DGWFkTGDIGYLDEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 454 GYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlshdPEQltkELQQHVKS 533
Cdd:PRK03640 374 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEV----TEE---ELRHFCEE 446
|
490 500 510
....*....|....*....|....*....|....*..
gi 157311624 534 VTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEWKM 570
Cdd:PRK03640 447 KLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-564 |
5.69e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 159.75 E-value: 5.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 218 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIM------WTISdtGWILNILGSLleswTLGaCTFVHLLPKF 291
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplFHCF--GSVLGVLACL----THG-ATMVFPSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 292 DPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGL-DIREFYGQTETGLT 369
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 370 CMVSKT---MKIKPGYMGTAASCYDVQVIDDKGNVLPP-GTEGDIGIRvkpirPIGIFSGYVENPDKTAANIRGDFWL-L 444
Cdd:cd05917 160 STQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTAEAIDGDGWLhT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 445 GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILasqflsHDPEQLT 524
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL------KEGAELT 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 157311624 525 KE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd05917 309 EEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
82-569 |
1.04e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 162.94 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSGAcGLQRGDRVAVML---PRVPEwwlVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 158
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 159 AGDEVIQEVDTVASECPSLRIKLLV-SEKSCDGWLNFKKLLNEASTTHHCVETgsqEASAIYFTSGTSGLPKMAEHSYSS 237
Cdd:PRK13391 102 TSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPATPIADES---LGTDMLYSSGTTGRPKGIKRPLPE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 238 LGLKAKMdaGWTGLQASdiMWTIsDTGWILNILGSLLESWTLGACTFVH-------LLPKFDPLVILKTLSSYPIKSMMG 310
Cdd:PRK13391 179 QPPDTPL--PLTAFLQR--LWGF-RSDMVYLSPAPLYHSAPQRAVMLVIrlggtviVMEHFDAEQYLALIEEYGVTHTQL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 311 APIVY-RML-------LQQDLSSykfphLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTE-TGLTCMVSKTMKIKPG 381
Cdd:PRK13391 254 VPTMFsRMLklpeevrDKYDLSS-----LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEgLGFTACDSEEWLAHPG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 382 YMGTAASCyDVQVIDDKGNVLPPGTEGDIGIRVKpiRPigiFSgYVENPDKTAA--NIRGDFWLLGDRGIKDEDGYFQFM 459
Cdd:PRK13391 329 TVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGG--RP---FE-YLNDPAKTAEarHPDGTWSTVGDIGYVDEDGYLYLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 460 GRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlshDP-EQLTKELQQHVKSVTAPY 538
Cdd:PRK13391 402 DRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGV---DPgPALAAELIAFCRQRLSRQ 478
|
490 500 510
....*....|....*....|....*....|.
gi 157311624 539 KYPRKIEFVLNLPKTVTGKIQRTKLRDKEWK 569
Cdd:PRK13391 479 KCPRSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
48-565 |
1.39e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 163.63 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 48 SDVLDHwaDMEKAGKRlpsPALWWVngkGKELMWnfRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCI 127
Cdd:PRK05605 35 VDLYDN--AVARFGDR---PALDFF---GATTTY--AELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 128 RAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV---IQE------VDTVAS-----------------ECPSLRIKL 181
Cdd:PRK05605 104 RLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVaptVERlrrttpLETIVSvnmiaampllqrlalrlPIPALRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 182 LVSEKSCDGWLNFKKLLNEA----STTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASD- 255
Cdd:PRK05605 184 AALTGPAPGTVPWETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVpGLGDGPe 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 256 IMWTI----SDTGWILNILGSLLeswtLGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ------DLSS 325
Cdd:PRK05605 264 RVLAAlpmfHAYGLTLCLTLAVS----IGG-ELV-LLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvDLSG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 326 ykfphLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCM---VSKTMKikPGYMGTAASCYDVQVID--DKGN 400
Cdd:PRK05605 338 -----VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVgnpMSDDRR--PGYVGVPFPDTEVRIVDpeDPDE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 401 VLPPGTEGDIGIRvkpirpiG--IFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEV 478
Cdd:PRK05605 411 TMPDGEEGELLVR-------GpqVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 479 ENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 558
Cdd:PRK05605 484 EEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPE----GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
....*..
gi 157311624 559 QRTKLRD 565
Cdd:PRK05605 559 RRREVRE 565
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
84-574 |
1.62e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 162.56 E-value: 1.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 84 RELSENSQQAANILSG--ACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK12406 12 RSFDELAQRAARAAGGlaALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 EVIQEV-DTVASEC--------PSLRIKLLVSEKSC---------DGWLNfkklLNEASTThhcvETGSQEASAIYfTSG 223
Cdd:PRK12406 92 DLLHGLaSALPAGVtvlsvptpPEIAAAYRISPALLtppagaidwEGWLA----QQEPYDG----PPVPQPQSMIY-TSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 224 TSGLPK-----------------MAEHSYsslGLKAKMDAGWTGlqasdIMWTISDtgwilNILGslLESWTLGACtfVH 286
Cdd:PRK12406 163 TTGHPKgvrraaptpeqaaaaeqMRALIY---GLKPGIRALLTG-----PLYHSAP-----NAYG--LRAGRLGGV--LV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 287 LLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ--------QDLSSYKFphlqncLAGGESLLP-----ETLENWraqt 353
Cdd:PRK12406 226 LQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpeevrakYDVSSLRH------VIHAAAPCPadvkrAMIEWW---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 354 GLDIREFYGQTETGL--TCMVSKTMKiKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpIRPIGIFSgYVENPD 431
Cdd:PRK12406 296 GPVIYEYYGSTESGAvtFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSR---IAGNPDFT-YHNKPE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 432 KTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVil 511
Cdd:PRK12406 371 KRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV-- 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157311624 512 asqflshDPEQL----TKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEWKMSGKA 574
Cdd:PRK12406 449 -------EPQPGatldEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
81-565 |
2.39e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 161.51 E-value: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVmLPRVPEWWLVI-LGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVa 159
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRRR-GCVDGERLAV-LARNSVWLVALhFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 160 GDEVIQevdtvASECPSLRIKLLVSEKSCDGWLNFKKLLNEAstthhcvetgsqeASAIYFTSGTSGLPKMA-------E 232
Cdd:PRK09088 100 GDDAVA-----AGRTDVEDLAAFIASADALEPADTPSIPPER-------------VSLILFTSGTSGQPKGVmlsernlQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 233 HSYSSLGLKAKMDAGWTGLQASDIMWTIsdtGWILNILGSLLESWTlgactfVHLLPKFDPLVILKTLS--SYPIKSMMG 310
Cdd:PRK09088 162 QTAHNFGVLGRVDAHSSFLCDAPMFHII---GLITSVRPVLAVGGS------ILVSNGFEPKRTLGRLGdpALGITHYFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 311 APIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQtGLDIREFYGQTETGLTCMVSKTMKI---KPGYMGTA 386
Cdd:PRK09088 233 VPQMAQAFRAQpGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDViraKAGAAGIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 387 ASCYDVQVIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDI 465
Cdd:PRK09088 312 TPTVQTRVVDDQGNDCPAGVPGELLLR-GP----NLSPGYWRRPQATARAFTGDGWFrTGDIARRDADGFFWVVDRKKDM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 466 INSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIE 545
Cdd:PRK09088 387 FISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-APLDLE----RIRSHLSTRLAKYKVPKHLR 461
|
490 500
....*....|....*....|
gi 157311624 546 FVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK09088 462 LVDALPRTASGKLQKARLRD 481
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
81-565 |
4.46e-43 |
|
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: 159.05 E-value: 4.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILsGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKaivag 160
Cdd:cd05912 2 YTFAELFEEVSRLAEHL-AALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 deviqeVDTVASecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAE-----HSY 235
Cdd:cd05912 76 ------LDDIAT---------------------------------------------IMYTSGTTGKPKGVQqtfgnHWW 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 SSLGLKAKMdagwtGLQASDiMWTIsdtgwILNI-----LGSLLESWTLGacTFVHLLPKFDPLVILKTLSSYPIKSMMG 310
Cdd:cd05912 105 SAIGSALNL-----GLTEDD-NWLC-----ALPLfhisgLSILMRSVIYG--MTVYLVDKFDAEQVLHLINSGKVTIISV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 311 APIVYRMLLQQDLSSYKfPHLQNCLAGGESLLPETLENWRaQTGLDIREFYGQTETgltCMVSKTMKI-----KPGYMGT 385
Cdd:cd05912 172 VPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCK-EKGIPVYQSYGMTET---CSQIVTLSPedalnKIGSAGK 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 386 AASCYDVQVIDDKGnvlPPGTEGDIGIRVKPIRPigifsGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDI 465
Cdd:cd05912 247 PLFPVELKIEDDGQ---PPYEVGEILLKGPNVTK-----GYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 466 INSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlshDPEQLTKELQQHVksvtAPYKYPRKIE 545
Cdd:cd05912 319 IISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKL----AKYKVPKKIY 391
|
490 500
....*....|....*....|
gi 157311624 546 FVLNLPKTVTGKIQRTKLRD 565
Cdd:cd05912 392 FVDELPRTASGKLLRHELKQ 411
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
57-566 |
8.87e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 160.59 E-value: 8.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 57 MEKAGKRLPS-PALWWvngkgKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMP 135
Cdd:PRK07470 13 LRQAARRFPDrIALVW-----GDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 136 GTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRikLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEA 215
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLT--HVVAIGGARAGLDYEALVARHLGARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 216 SAIYF-TSGTSGLPKMAEHSYSSLGL-----KAKMDAGWTGLQASDIMWTISDTGWIlnilgSLLESWTLGACTFVHLLP 289
Cdd:PRK07470 165 PCWFFfTSGTTGRPKAAVLTHGQMAFvitnhLADLMPGTTEQDASLVVAPLSHGAGI-----HQLCQVARGAATVLLPSE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 290 KFDPLVILKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPH--LQNCLAGGESLLPETLENWRAQTGLDIREFYGQTEtg 367
Cdd:PRK07470 240 RFDPAEVWALVERHRVTNLFTVPTILKMLVE-HPAVDRYDHssLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGE-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 368 ltcmVSKTMKIKPGYM-----GTAA---SC------YDVQVIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVENPDKT 433
Cdd:PRK07470 317 ----VTGNITVLPPALhdaedGPDArigTCgfertgMEVQIQDDEGRELPPGETGEICVIGPAV-----FAGYYNNPEAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 434 AANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAfVILAS 513
Cdd:PRK07470 388 AKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA-VCVAR 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 157311624 514 QFLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDK 566
Cdd:PRK07470 467 DGAPVDEA----ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
84-493 |
2.30e-42 |
|
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: 157.04 E-value: 2.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 84 RELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM----SKAKA 156
Cdd:TIGR01733 3 RELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP-------LDPAYpaeRLAFiledAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 157 IVAGDEVIQEVDTVASECPSLRIKLLVSEKSCdgwlnfkkllneASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYS 236
Cdd:TIGR01733 76 LLTDSALASRLAGLVLPVILLDPLELAALDDA------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 237 SL----GLKAKMDAGWTG---LQASDIMWTISdtgwILNILGSLLeswtLGACTFVHL--LPKFDPLVILKTLSSYPIKS 307
Cdd:TIGR01733 144 SLvnllAWLARRYGLDPDdrvLQFASLSFDAS----VEEIFGALL----AGATLVVPPedEERDDAALLAALIAEHPVTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 308 MMGAPIVYRMLLQQDLSSykFPHLQNCLAGGESLLPETLENWRAQTGlDIREF--YGQTETGLTCMVSKTMKIKPGYM-- 383
Cdd:TIGR01733 216 LNLTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGP-GARLInlYGPTETTVWSTATLVDPDDAPREsp 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 384 ---GTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTAAN-IRGDFWLL--------GDRGIKD 451
Cdd:TIGR01733 293 vpiGRPLANTRLYVLDDDLRPVPVGVVGELYIG-----GPGVARGYLNRPELTAERfVPDPFAGGdgarlyrtGDLVRYL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 157311624 452 EDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAV 493
Cdd:TIGR01733 368 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
48-564 |
4.71e-42 |
|
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: 158.77 E-value: 4.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 48 SDVLDHWADmekagkRLPS-PALwwVNGKGKelmWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGC 126
Cdd:COG1021 28 GDLLRRRAE------RHPDrIAV--VDGERR---LSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 127 IRAGLI---FMPGtiqMKSTDILYRLQMSKAKAIVAGDEV-----IQEVDTVASECPSLRIKLLVSEKscDGWLNFKKLL 198
Cdd:COG1021 96 FRAGAIpvfALPA---HRRAEISHFAEQSEAVAYIIPDRHrgfdyRALARELQAEVPSLRHVLVVGDA--GEFTSLDALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 199 NEASTtHHCVETGSQEASAIYFTSGTSGLPKM-----AEHSYSslglkAKMDAGWTGLQASDIM---------WTISDTG 264
Cdd:COG1021 171 AAPAD-LSEPRPDPDDVAFFQLSGGTTGLPKLiprthDDYLYS-----VRASAEICGLDADTVYlaalpaahnFPLSSPG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 265 wilnILGSLLeswtLGACtfVHLLPKFDPLVILK-------TLSSypiksmMGAPIVYRML-----LQQDLSSYKFphLQ 332
Cdd:COG1021 245 ----VLGVLY----AGGT--VVLAPDPSPDTAFPlierervTVTA------LVPPLALLWLdaaerSRYDLSSLRV--LQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 333 NclaGGESLLPETLENWRAQTGLDIREFYGQTEtGLTCM---------VSKTMkikpgymGTAASCYD-VQVIDDKGNVL 402
Cdd:COG1021 307 V---GGAKLSPELARRVRPALGCTLQQVFGMAE-GLVNYtrlddpeevILTTQ-------GRPISPDDeVRIVDEDGNPV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 403 PPGTEGDIGIRvkpirpiG--IFSGYVENPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVE 479
Cdd:COG1021 376 PPGEVGELLTR-------GpyTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 480 NALMKHPAVVETAVISSPDPVRGEVVKAFVILasqflshDPEQLT-KELQQHVKSV-TAPYKYPRKIEFVLNLPKTVTGK 557
Cdd:COG1021 449 NLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-------RGEPLTlAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGK 521
|
....*..
gi 157311624 558 IQRTKLR 564
Cdd:COG1021 522 IDKKALR 528
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
83-565 |
7.73e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 158.29 E-value: 7.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--- 159
Cdd:PRK13295 58 YRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpkt 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 160 --GDEVIQEVDTVASECPSLRIKLLVSEkscDGWLNFKKLLNE--------ASTTHHCVETGSQEASAIYFTSGTSGLPK 229
Cdd:PRK13295 137 frGFDHAAMARRLRPELPALRHVVVVGG---DGADSFEALLITpaweqepdAPAILARLRPGPDDVTQLIYTSGTTGEPK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 230 MAEHSYSSLGLKAKMDAGWTGLQASDIMWTIS----DTGWILNILGSLLeswtLGAcTFVhLLPKFDPLVILKTLSSYPI 305
Cdd:PRK13295 214 GVMHTANTLMANIVPYAERLGLGADDVILMASpmahQTGFMYGLMMPVM----LGA-TAV-LQDIWDPARAAELIRTEGV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 306 KSMMGA-PIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMvsktmkIKPGYMG 384
Cdd:PRK13295 288 TFTMAStPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTL------TKLDDPD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 385 TAASCYD--------VQVIDDKGNVLPPGTEGdigiRVKpIRPIGIFSGYVENPDKTAANIRGdfWL-LGDRGIKDEDGY 455
Cdd:PRK13295 362 ERASTTDgcplpgveVRVVDADGAPLPAGQIG----RLQ-VRGCSNFGGYLKRPQLNGTDADG--WFdTGDLARIDADGY 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 456 FQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIL-ASQflSHDPEQLTKELQQHvkSV 534
Cdd:PRK13295 435 IRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPrPGQ--SLDFEEMVEFLKAQ--KV 510
|
490 500 510
....*....|....*....|....*....|.
gi 157311624 535 TAPYkYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK13295 511 AKQY-IPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
82-566 |
3.25e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 150.87 E-value: 3.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK08162 45 TWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 EVIQEVDTVASECPSLRIkLLV-------SEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPK--MA 231
Cdd:PRK08162 124 EFAEVAREALALLPGPKP-LVIdvddpeyPGGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKgvVY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 232 EHSYSSLGLKAKMDAgWTGLQASDIMWTISD---TGWILnilgslleSWTLGACTFVHL-LPKFDPLVILKTLSSYPIKS 307
Cdd:PRK08162 203 HHRGAYLNALSNILA-WGMPKHPVYLWTLPMfhcNGWCF--------PWTVAARAGTNVcLRKVDPKLIFDLIREHGVTH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 308 MMGAPIVYRMLLQ-QDLSSYKFPHLQNCLAGGESLLPETLENwRAQTGLDIREFYGQTETgltcmvsktmkikpgYmGTA 386
Cdd:PRK08162 274 YCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAK-MEEIGFDLTHVYGLTET---------------Y-GPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 387 ASCYDVQVIDDkgnvLPPGTEGDI------------GIRV------KPI----RPIG--------IFSGYVENPDKTAAN 436
Cdd:PRK08162 337 TVCAWQPEWDA----LPLDERAQLkarqgvryplqeGVTVldpdtmQPVpadgETIGeimfrgniVMKGYLKNPKATEEA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 437 IRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqfl 516
Cdd:PRK08162 413 FAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELK---- 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 157311624 517 shDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQRTKLRDK 566
Cdd:PRK08162 489 --DGASATEeEIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQ 536
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
287-565 |
4.58e-39 |
|
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: 149.06 E-value: 4.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 287 LLPKFDPLVILKTLSSYPIKSMMGAP-IVYRM--LLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQ 363
Cdd:cd05929 199 LMEKFDPEEFLRLIERYRVTFAQFVPtMFVRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 364 TE-TGLTCMVSKTMKIKPGYMGTAASCyDVQVIDDKGNVLPPGTEGDIGIRVKPIrpigifSGYVENPDKTAANIRGDFW 442
Cdd:cd05929 279 TEgQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAARNEGGW 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 443 -LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASqfLSHDPE 521
Cdd:cd05929 352 sTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAP--GADAGT 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 157311624 522 QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:cd05929 430 ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
48-566 |
9.85e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 148.88 E-value: 9.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 48 SDVLDHWAdmekagKRLPS-PALWWvngKGKELmwNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGC 126
Cdd:PRK06145 5 SASIAFHA------RRTPDrAALVY---RDQEI--SYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 127 IRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagdeVIQEVDTVasecPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHH 206
Cdd:PRK06145 73 SYLGAVFLPINYRLAADEVAYILGDAGAKLLL----VDEEFDAI----VALETPKIVIDAAAQADSRRLAQGGLEIPPQA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 207 CVetGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDImwtisdtgwiLNILGSLlesWTLGACT--- 283
Cdd:PRK06145 145 AV--APTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASER----------LLVVGPL---YHVGAFDlpg 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 284 --------FVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCLAGGESLlPEtlenwraqtg 354
Cdd:PRK06145 210 iavlwvggTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEKT-PE---------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 355 LDIREF------------YGQTET--GLTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRpi 420
Cdd:PRK06145 279 SRIRDFtrvftraryidaYGLTETcsGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVT-- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 421 gifSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPV 500
Cdd:PRK06145 357 ---KGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDR 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157311624 501 RGEVVKAFVILAS-QFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDK 566
Cdd:PRK06145 434 WGERITAVVVLNPgATLTLE------ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
67-563 |
1.06e-38 |
|
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: 147.78 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 67 PALWWVNGKgkelmWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDIL 146
Cdd:cd05945 8 PAVVEGGRT-----LTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP-------LDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 147 Y---RLQMskAKAIVAGDEVIQEVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSG 223
Cdd:cd05945 75 SpaeRIRE--ILDAAKPALLIADGDDNA---------------------------------------------YIIFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 224 TSGLPKMAEHSYSSLglkakmdagwtglqASDIMWTISDTGW-----ILNI--------LGSLLESWTLGACtfVHLLPK 290
Cdd:cd05945 108 STGRPKGVQISHDNL--------------VSFTNWMLSDFPLgpgdvFLNQapfsfdlsVMDLYPALASGAT--LVPVPR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 291 ---FDPLVILKTLSSYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCLAGGESLLPETLENWRAQT-GLDIREFYGQTE 365
Cdd:cd05945 172 datADPKQLFRFLAEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 366 TGLTCMVSK-TMKIKPGY----MGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVENPDKTA-ANI 437
Cdd:cd05945 252 ATVAVTYIEvTPEVLDGYdrlpIGYAKPGAKLVILDEDGRPVPPGEKGELVIS-------GpsVSKGYLNNPEKTAaAFF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 438 RGDFWLL---GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVIssPDPVRGEVVK--AFVILA 512
Cdd:cd05945 325 PDEGQRAyrtGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVV--PKYKGEKVTEliAFVVPK 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 157311624 513 sqflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd05945 403 ----PGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
82-565 |
1.43e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 149.12 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILsGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK06164 37 SRAELRALVDRLAAWL-AAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 --------EVIQEVDTvaSECPSLRIKLLVSEKSCD-------GWLNFKKLLNEASTTHHCVETGSQEASAIYFT-SGTS 225
Cdd:PRK06164 116 gfkgidfaAILAAVPP--DALPPLRAIAVVDDAADAtpapapgARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 226 GLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNiLGSLLESWTLGACtfVHLLPKFDPLVILKTLSSYPI 305
Cdd:PRK06164 194 SGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG-FSTLLGALAGGAP--LVCEPVFDAARTARALRRHRV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 306 KSMMGAPIVYRMLLQQDLSSYKFPHLQNClaGGESLLP--ETLENWRAQTGLDIREFYGQTEtgLTCMVS-------KTM 376
Cdd:PRK06164 271 THTFGNDEMLRRILDTAGERADFPSARLF--GFASFAPalGELAALARARGVPLTGLYGSSE--VQALVAlqpatdpVSV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 377 KIKPGymGTAASC-YDVQVID-DKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWL-LGDRGIKDED 453
Cdd:PRK06164 347 RIEGG--GRPASPeARVRARDpQDGALLPDGESGEIEIRAP-----SLMRGYLDNPDATARALTDDGYFrTGDLGYTRGD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 454 GYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVkAFVILASQfLSHDPEqltkELQQHVKS 533
Cdd:PRK06164 420 GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDG-ASPDEA----GLMAACRE 493
|
490 500 510
....*....|....*....|....*....|....*
gi 157311624 534 VTAPYKYPRKIEFVLNLPKTVTG---KIQRTKLRD 565
Cdd:PRK06164 494 ALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
81-563 |
2.28e-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: 147.47 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLI---FMPGtiqMKSTDILYRLQMSKAKAI 157
Cdd:cd05920 41 LTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvlALPS---HRRSELSAFCAHAEAVAY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 VAGDEvIQEVD------TVASECPSLRIKLLvsekscdgwlnfkkllneastthhcvetgsqeasaiyfTSGTSGLPKMA 231
Cdd:cd05920 117 IVPDR-HAGFDhralarELAESIPEVALFLL--------------------------------------SGGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 232 EHSYSSLGLKAKMDAGWTGLQASDIM---------WTISDTGwilnILGSLLeswtLGACtfVHLLPKFDPLVILKTLSS 302
Cdd:cd05920 158 PRTHNDYAYNVRASAEVCGLDQDTVYlavlpaahnFPLACPG----VLGTLL----AGGR--VVLAPDPSPDAAFPLIER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 303 YPIKSMMGAPIVYRMLLQQ------DLSSYKFphLQnclAGGESLLPETLENWRAQTGLDIREFYGQTEtGLTCM--VSK 374
Cdd:cd05920 228 EGVTVTALVPALVSLWLDAaasrraDLSSLRL--LQ---VGGARLSPALARRVPPVLGCTLQQVFGMAE-GLLNYtrLDD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 375 TMKIKPGYMGTAASCYD-VQVIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVENPDKTAANIRGD-FWLLGDRGIK 450
Cdd:cd05920 302 PDEVIIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTR-------GpyTIRGYYRAPEHNARAFTPDgFYRTGDLVRR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 451 DEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflshDPEQLTKELQQH 530
Cdd:cd05920 375 TPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRF 448
|
490 500 510
....*....|....*....|....*....|....
gi 157311624 531 VKSV-TAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd05920 449 LRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
72-566 |
2.92e-38 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 148.20 E-value: 2.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 72 VNGKGkelmWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQM 151
Cdd:PLN02330 51 VTGKA----VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 152 SKAKAIVAGDEVIQEVDtvasecpSLRIKLLV-SEKSCDGWLNFKKLLN---EASTTHHCVETGSQEASAIYFTSGTSGL 227
Cdd:PLN02330 126 AGAKLIVTNDTNYGKVK-------GLGLPVIVlGEEKIEGAVNWKELLEaadRAGDTSDNEEILQTDLCALPFSSGTTGI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 228 PK--MAEHSysslGLKAKMDAGWTGLqASDIMWTISDTGWI--LNILGslleswTLGACTF-------VHLLPKFDPLVI 296
Cdd:PLN02330 199 SKgvMLTHR----NLVANLCSSLFSV-GPEMIGQVVTLGLIpfFHIYG------ITGICCAtlrnkgkVVVMSRFELRTF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 297 LKTLSSYPIKSmmgAPIVYRMLL---------QQDLSSYKfphLQNCLAGGESLLPETLENWRAQ-TGLDIREFYGQTET 366
Cdd:PLN02330 268 LNALITQEVSF---APIVPPIILnlvknpiveEFDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEH 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 367 GLTCMV----SKTMKI-KPGYMGTAASCYDVQVID-DKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGD 440
Cdd:PLN02330 342 SCITLThgdpEKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYNNKEETDRTIDED 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 441 FWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIlasqfLSHD 519
Cdd:PLN02330 417 GWLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVV-----INPK 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 157311624 520 PEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDK 566
Cdd:PLN02330 492 AKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
214-560 |
3.05e-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: 143.80 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 214 EASAIYFTSGTSGLPK--MAEHSYSSLGLKAKMDAGwtGLQASDIMWTIS----DTGWILNILGSLLESWTLgactfvhl 287
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQTLRAAAAWADCA--DLTEDDRYLIINpffhTFGYKAGIVACLLTGATV-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 288 LPK--FDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLD-IREFYGQ 363
Cdd:cd17638 71 VPVavFDVDAILEAIERERITVLPGPPTLFQSLLDHpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 364 TETGLTCM---------VSKTMkikpgymGTAASCYDVQVIDDkGNVLppgtegdigirvkpIRPIGIFSGYVENPDKTA 434
Cdd:cd17638 151 TEAGVATMcrpgddaetVATTC-------GRACPGFEVRIADD-GEVL--------------VRGYNVMQGYLDDPEATA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 435 ANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAs 513
Cdd:cd17638 209 EAIDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR- 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 157311624 514 qflshDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd17638 288 -----PGVTLTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
83-566 |
1.11e-37 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 146.44 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGACGLQRgDRVAVMLPRVPEWWLVILGCIRAG---LIFMPGTIQMKSTDILYRlqmSKAKAIVA 159
Cdd:PRK13382 71 WRELDERSDALAAALQALPIGEP-RVVGIMCRNHRGFVEALLAANRIGadiLLLNTSFAGPALAEVVTR---EGVDTVIY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 160 GDEVIQEVDTVASECP-SLRIKLLVSEKScdgwlnfkKLLNEASTTHHC---VETGSQEASAIYFTSGTSGLPKMAEHSY 235
Cdd:PRK13382 147 DEEFSATVDRALADCPqATRIVAWTDEDH--------DLTVEVLIAAHAgqrPEPTGRKGRVILLTSGTTGTPKGARRSG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 S--SLGLKAKMD-AGWTGLQASDIM------WTISDtgwiLNILGSLleswtlgACTFVhLLPKFDPLVILKTLSSYPIK 306
Cdd:PRK13382 219 PggIGTLKAILDrTPWRAEEPTVIVapmfhaWGFSQ----LVLAASL-------ACTIV-TRRRFDPEATLDLIDRHRAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 307 SMMGAPIVYRMLLQ---QDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVS-KTMKIKPGY 382
Cdd:PRK13382 287 GLAVVPVMFDRIMDlpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATpADLRAAPDT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 383 MGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVENPDKtaaNIRGDFWLLGDRGIKDEDGYFQFMGRA 462
Cdd:PRK13382 367 AGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQ-----FDGYTSGSTK---DFHDGFMASGDVGYLDENGRLFVVGRD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 463 DDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQfLSHDPEqltkELQQHVKSVTAPYKYPR 542
Cdd:PRK13382 439 DEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG-ASATPE----TLKQHVRDNLANYKVPR 513
|
490 500
....*....|....*....|....
gi 157311624 543 KIEFVLNLPKTVTGKIQRTKLRDK 566
Cdd:PRK13382 514 DIVVLDELPRGATGKILRRELQAR 537
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
217-564 |
5.80e-37 |
|
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: 140.69 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 217 AIYF-TSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWT---ISDTGWILNILGSLLESwtlGAcTFVHLLPK-- 290
Cdd:cd05944 5 AAYFhTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCglpLFHVNGSVVTLLTPLAS---GA-HVVLAGPAgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 291 FDPLV---ILKTLSSYPIKSMMGAPIVYRMLLQ----QDLSSYKFPhlqnclAGGESLLPETLEN-WRAQTGLDIREFYG 362
Cdd:cd05944 81 RNPGLfdnFWKLVERYRITSLSTVPTVYAALLQvpvnADISSLRFA------MSGAAPLPVELRArFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 363 QTETglTCMVSKTMK---IKPGYMGTAASCYDVQ--VIDDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVENPDKTAANI 437
Cdd:cd05944 155 LTEA--TCLVAVNPPdgpKRPGSVGLRLPYARVRikVLDGVGRLLRDCAPDEVGEIC--VAGPGVFGGYLYTEGNKNAFV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 438 rGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsQFL 516
Cdd:cd05944 231 -ADGWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLK-PGA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 157311624 517 SHDPEQLTKELQQHVKSVTApykYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd05944 309 VVEEEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
58-564 |
4.36e-34 |
|
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: 135.55 E-value: 4.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 58 EKAGKRLP-SPALWWVNGKgkelmWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPG 136
Cdd:cd17651 2 ERQAARTPdAPALVAEGRR-----LTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 137 TIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpslrikllvsekscDGWLNFKKLLNEASTTHHCVETGSQEAS 216
Cdd:cd17651 76 DPAYPAERLAFMLADAGPVLVLTHPALAGELAVELV----------------AVTLLDQPGAAAGADAEPDPALDADDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 217 AIYFTSGTSGLPKMAEHSYSSLGL-------KAKMDAGWTGLQASDIMWTISdtgwILNILGSLleswTLGACtfVHLLP 289
Cdd:cd17651 140 YVIYTSGSTGRPKGVVMPHRSLANlvawqarASSLGPGARTLQFAGLGFDVS----VQEIFSTL----CAGAT--LVLPP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 290 ---KFDPLVILKTLSSYPI-KSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESL-LPETLENW-RAQTGLDIREFYGQ 363
Cdd:cd17651 210 eevRTDPPALAAWLDEQRIsRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLvLTEDLREFcAGLPGLRLHNHYGP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 364 TETglTCMVSKTMKIKPGYMGTAASC------YDVQVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANI 437
Cdd:cd17651 290 TET--HVVTALSLPGDPAAWPAPPPIgrpidnTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAERF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 438 RGD-------FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVI 510
Cdd:cd17651 363 VPDpfvpgarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 157311624 511 lASQFLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd17651 443 -GDPEAPVDAA----ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
58-566 |
4.65e-34 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 135.88 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 58 EKAGKRLPSPALwwVNGK-GKELmwNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPG 136
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGAtGRVY--TYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 137 TIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPslrIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEAS 216
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDG---VTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 217 AIYFTSGTSGLPK--MAEHSYSSLGLKAKMDAgwtglQASDIMWTISDTgwILNIL---------GSLLESWTLGACtfV 285
Cdd:PLN02246 183 ALPYSSGTTGLPKgvMLTHKGLVTSVAQQVDG-----ENPNLYFHSDDV--ILCVLpmfhiyslnSVLLCGLRVGAA--I 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 286 HLLPKFDPLVILKTLSSYPIK-SMMGAPIVYRM-----LLQQDLSSYKFphlqnCLAGGESLLPETLENWRAQ-TGLDIR 358
Cdd:PLN02246 254 LIMPKFEIGALLELIQRHKVTiAPFVPPIVLAIakspvVEKYDLSSIRM-----VLSGAAPLGKELEDAFRAKlPNAVLG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 359 EFYGQTETG---LTCMV-SKT-MKIKPGYMGTAASCYDVQVID-DKGNVLPPGTEGDIGIRVKPIrpigiFSGYVENPDK 432
Cdd:PLN02246 329 QGYGMTEAGpvlAMCLAfAKEpFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQI-----MKGYLNDPEA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 433 TAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIL 511
Cdd:PLN02246 404 TANTIDKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVR 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 157311624 512 ASQF-LSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDK 566
Cdd:PLN02246 484 SNGSeITED------EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
83-563 |
7.53e-34 |
|
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: 134.76 E-value: 7.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:cd17655 25 YRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 VIQevdtvasecpslrikLLVSEKSCDgWLNFKKLLNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MAEHS-----Y 235
Cdd:cd17655 104 LQP---------------PIAFIGLID-LLDEDTIYHEESENLEPVSKSDDLAYVIY-TSGSTGKPKgvMIEHRgvvnlV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 SSLGLKAKMDAGWTGLQASDIMWTISDTgwilNILGSLLESWTLgactfvHLLPK---FDPLVILKTLSSYPIKSMMGAP 312
Cdd:cd17655 167 EWANKVIYQGEHLRVALFASISFDASVT----EIFASLLSGNTL------YIVRKetvLDGQALTQYIRQNRITIIDLTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 313 IVYRMLLQQDLSSykFPHLQNCLAGGESLLPETLENWRAQTGLDIREF--YGQTETGLTCMV-----SKTMKIKPgYMGT 385
Cdd:cd17655 237 AHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIIELFGTNPTITnaYGPTETTVDASIyqyepETDQQVSV-PIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 386 AASCYDVQVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWLLGDRGIKD-------EDGYFQF 458
Cdd:cd17655 314 PLGNTRIYILDQYGRPQPVGVAGELYIGGE-----GVARGYLNRPELTAEKFVDDPFVPGERMYRTgdlarwlPDGNIEF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 459 MGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlshDPEQLTKELQQHVKSVTAPy 538
Cdd:cd17655 389 LGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKEL---PVAQLREFLARELPDYMIP- 464
|
490 500
....*....|....*....|....*
gi 157311624 539 KYPRKIEfvlNLPKTVTGKIQRTKL 563
Cdd:cd17655 465 SYFIKLD---EIPLTPNGKVDRKAL 486
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
81-530 |
8.53e-34 |
|
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: 133.87 E-value: 8.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdiLYrlQMSKAKAIvag 160
Cdd:cd05907 6 ITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP----------IY--PTSSAEQI--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 deviqevdtvasecpslrikllvsekscdGWLnfkklLNEASTTHHCVETGSQEASAIYfTSGTSGLPKMAEHSYSSLgl 240
Cdd:cd05907 70 -----------------------------AYI-----LNDSEAKALFVEDPDDLATIIY-TSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 kakmdagWTGLQASDIMWTISDTGWILnilgSLLESWTLGACTFVHLLP-------KFDPLV--ILKTLSSYPIKSMMGA 311
Cdd:cd05907 113 -------LSNALALAERLPATEGDRHL----SFLPLAHVFERRAGLYVPllagariYFASSAetLLDDLSEVRPTVFLAV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 312 PIVYRML----LQQDLSSYK--------FPHLQNCLAGGESLLPETLENWRAqTGLDIREFYGQTETGLTCMVSKTMKIK 379
Cdd:cd05907 182 PRVWEKVyaaiKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 380 PGYMGTAASCYDVQvIDDKGNVLppgtegdigirvkpIRPIGIFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQF 458
Cdd:cd05907 261 IGTVGKPLPGVEVR-IADDGEIL--------------VRGPNVMLGYYKNPEATAEALDADGWLhTGDLGEIDEDGFLHI 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157311624 459 MGRADD-IINSSGYRIGPSEVENALMKHPAVVETAVISSPDPvrgeVVKAFVILasqflshDPEQLTKELQQH 530
Cdd:cd05907 326 TGRKKDlIITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVP-------DPEALEAWAEEH 387
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
83-564 |
9.17e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 134.52 E-value: 9.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGACGLQRgdRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:PRK07638 29 YKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 VIQEVDTVasECPSLRIkllvsekscDGWlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSlglka 242
Cdd:PRK07638 107 KLNDLPDE--EGRVIEI---------DEW---KRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 243 kmdagWT-GLQASDIMWTISDTGWILnILGSLLESWTL-GACT------FVHLLPKFDPLVILKTLSSYPIKSMMGAPIV 314
Cdd:PRK07638 168 -----WLhSFDCNVHDFHMKREDSVL-IAGTLVHSLFLyGAIStlyvgqTVHLMRKFIPNQVLDKLETENISVMYTVPTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 315 YRMLLQQDlssyKFP-HLQNCLAGGESLLPETLEnwRAQTG---LDIREFYGQTETG-LTCMVSKTMKIKPGYMGTAASC 389
Cdd:PRK07638 242 LESLYKEN----RVIeNKMKIISSGAKWEAEAKE--KIKNIfpyAKLYEFYGASELSfVTALVDEESERRPNSVGRPFHN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 390 YDVQVIDDKGNVLPPGTEGDIGIRvKPIRpigiFSGYVeNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINS 468
Cdd:PRK07638 316 VQVRICNEAGEEVQKGEIGTVYVK-SPQF----FMGYI-IGGVLARELNADGWMtVRDVGYEDEEGFIYIVGREKNMILF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 469 SGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVilasqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVL 548
Cdd:PRK07638 390 GGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKEWHFVD 460
|
490
....*....|....*.
gi 157311624 549 NLPKTVTGKIQRTKLR 564
Cdd:PRK07638 461 EIPYTNSGKIARMEAK 476
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
102-570 |
2.62e-33 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 134.20 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 102 GLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagdeVIQEVDTVASEcpSLRI-- 179
Cdd:PLN02479 66 SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM----VDQEFFTLAEE--ALKIla 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 180 ---------KLLV--SEKSCD----------GWLNFKKLLneastthhcvETGSQE-----------ASAIYFTSGTSGL 227
Cdd:PLN02479 140 ekkkssfkpPLLIviGDPTCDpkslqyalgkGAIEYEKFL----------ETGDPEfawkppadewqSIALGYTSGTTAS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 228 PKMAEHSYSSLGLKAKMDAGWTGLQASDI-MWTISD---TGWILnilgslleSWTLGA-CTFVHLLPKFDPLVILKTLSS 302
Cdd:PLN02479 210 PKGVVLHHRGAYLMALSNALIWGMNEGAVyLWTLPMfhcNGWCF--------TWTLAAlCGTNICLRQVTAKAIYSAIAN 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 303 YPIKSMMGAPIVYRMLLQQDLSS--YKFPHLQNCLAGGESLLPETLENWrAQTGLDIREFYGQTET-------------- 366
Cdd:PLN02479 282 YGVTHFCAAPVVLNTIVNAPKSEtiLPLPRVVHVMTAGAAPPPSVLFAM-SEKGFRVTHTYGLSETygpstvcawkpewd 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 367 GLTCMVSKTMKIKPG--YMGTAAscydVQVIDDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVENPDKTAANIRGDFWLL 444
Cdd:PLN02479 361 SLPPEEQARLNARQGvrYIGLEG----LDVVDTKTMKPVPADGKTMGEIV--MRGNMVMKGYLKNPKANEEAFANGWFHS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 445 GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQLT 524
Cdd:PLN02479 435 GDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALA 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 157311624 525 KELQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQRTKLRDKEWKM 570
Cdd:PLN02479 515 EDIMKFCRERLPAYWVPKSVVFG-PLPKTATGKIQKHVLRAKAKEM 559
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
47-560 |
3.33e-33 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 133.47 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 47 ASDVLDHWADM-EKAGKRLPS-PALWWVNGKgkeLMWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVIL 124
Cdd:PRK05852 11 ASDFGPRIADLvEVAATRLPEaPALVVTADR---IAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 125 GCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTT 204
Cdd:PRK05852 87 AASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 205 HHCVETGSQEASA-IYFTSGTSGLPKMAEHSYSSLGlkAKMDAGWTGLQASD------IMWTISDTGWILNILGSLLESW 277
Cdd:PRK05852 167 ATSTPEGLRPDDAmIMFTGGTTGLPKMVPWTHANIA--SSVRAIITGYRLSPrdatvaVMPLYHGHGLIAALLATLASGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 278 TLgactfvhLLP---KFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ---DLSSYKFPHLQNCLAGGESLLPETLENWRA 351
Cdd:PRK05852 245 AV-------LLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILLERaatEPSGRKPAALRFIRSCSAPLTAETAQALQT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 352 QTGLDIREFYGQTET----------GLTCMVSKTMKIKPGYMGTAAscyDVQVIDDKGNVLPPGTEGDIGIRVKPIrpig 421
Cdd:PRK05852 318 EFAAPVVCAFGMTEAthqvtttqieGIGQTENPVVSTGLVGRSTGA---QIRIVGSDGLPLPAGAVGEVWLRGTTV---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 422 iFSGYVENPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPV 500
Cdd:PRK05852 391 -VRGYLGDPTITAANFT-DGWLrTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 501 RGEVVKAfVILASQFLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:PRK05852 469 YGEAVAA-VIVPRESAPPTAE----ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
44-557 |
3.99e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 133.09 E-value: 3.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 44 FNFAsDVLDHWADmeKAGKRlpsPALwwVNGkgkELMWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVI 123
Cdd:PRK07798 3 WNIA-DLFEAVAD--AVPDR---VAL--VCG---DRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 124 LGCIRAGLIfmPGTIQMKSTD--ILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLV----SEKSCDGWLNFKKL 197
Cdd:PRK07798 71 LGAFKARAV--PVNVNYRYVEdeLRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 198 LNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MAEHS---YSSLGLKAKMdagwTGLQASDiMWTISD-----TGWIL 267
Cdd:PRK07798 149 LAAGSPERDFGERSPDDLYLLY-TGGTTGMPKgvMWRQEdifRVLLGGRDFA----TGEPIED-EEELAKraaagPGMRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 268 NILGSLLE---SWTL------GACTFVHLLPKFDPLVILKTLSSYPIKSM------MGAPIV--YRMLLQQDLSSykfph 330
Cdd:PRK07798 223 FPAPPLMHgagQWAAfaalfsGQTVVLLPDVRFDADEVWRTIEREKVNVItivgdaMARPLLdaLEARGPYDLSS----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 331 LQNCLAGGESLLPETLENWRAQ-TGLDIREFYGQTETGLtCMVSKTMKIKPGYMG---TAAScyDVQVIDDKGNVLPPGt 406
Cdd:PRK07798 298 LFAIASGGALFSPSVKEALLELlPNVVLTDSIGSSETGF-GGSGTVAKGAVHTGGprfTIGP--RTVVLDEDGNPVEPG- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 407 EGDIGI--RVKPIrPIGifsgYVENPDKTAAN---IRGDFW-LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN 480
Cdd:PRK07798 374 SGEIGWiaRRGHI-PLG----YYKDPEKTAETfptIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157311624 481 ALMKHPAVVETAVISSPDPVRGEVVKAFVILASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGK 557
Cdd:PRK07798 449 ALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
85-563 |
1.11e-32 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 131.48 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 85 ELSENSQQAANILSGacGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD--E 162
Cdd:cd05923 34 LRARIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVdaQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 VIQEVDTVASECpsLRIKLLVSEKSCDgwlNFKKLLNEASTthhcvetGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKA 242
Cdd:cd05923 112 VMDAIFQSGVRV--LALSDLVGLGEPE---SAGPLIEDPPR-------EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 243 KMDAGWTGLQ--ASDIMWTISDTGWILNILGSLLESWTLGacTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ 320
Cdd:cd05923 180 LFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALD--GTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 321 QDL-SSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETgltcMVSKTMK-IKPGYMGTAASCYDVQVIDDK 398
Cdd:cd05923 258 AAEfAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA----MNSLYMRdARTGTEMRPGFFSEVRIVRIG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 399 GNV---LPPGTEGDIgirVKPIRPIGIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGP 475
Cdd:cd05923 334 GSPdeaLANGEEGEL---IVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 476 SEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDpeqltkELQQHVK-SVTAPYKYPRKIEFVLNLPKTV 554
Cdd:cd05923 411 SEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD------ELDQFCRaSELADFKRPRRYFFLDELPKNA 484
|
....*....
gi 157311624 555 TGKIQRTKL 563
Cdd:cd05923 485 MNKVLRRQL 493
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
73-566 |
1.56e-32 |
|
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: 131.05 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 73 NGKGKELMWNfrELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMS 152
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 153 KAKAIVAG--DEVIQEVDTVASECPSLRIKLLVSEKSCDGWlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKM 230
Cdd:cd05932 78 ESKALFVGklDDWKAMAPGVPEGLISISLPPPSAANCQYQW---DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 231 AEHSYSSLGLKAKMDAGWTGLQASDIMW-----------TISDTGWIlnILGSLL---ESWTlgacTFVHLLPKFDPLVI 296
Cdd:cd05932 155 VMLTFGSFAWAAQAGIEHIGTEENDRMLsylplahvterVFVEGGSL--YGGVLVafaESLD----TFVEDVQRARPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 297 -----LKTLSSYPIKSMMGA---------PIVYRMLLQQDLSSYKFPHLQnCLAGGESLLPETLENWRAQTGLDIREFYG 362
Cdd:cd05932 229 fsvprLWTKFQQGVQDKIPQqklnlllkiPVVNSLVKRKVLKGLGLDQCR-LAGCGSAPVPPALLEWYRSLGLNILEAYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 363 QTETGLTCMVSKTMKIKPGYMGTAAScyDVQV-IDDKGNVLppgtegdigirvkpIRPIGIFSGYVENPDKTAANIRGDF 441
Cdd:cd05932 308 MTENFAYSHLNYPGRDKIGTVGNAGP--GVEVrISEDGEIL--------------VRSPALMMGYYKDPEATAEAFTADG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 442 WL-LGDRGIKDEDGYFQFMGRADDIINSS-GYRIGPSEVENALMKHPAVVETAVISS--PDPVRGEVVKAFVILASqfLS 517
Cdd:cd05932 372 FLrTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRA--DA 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 157311624 518 HDPEQLTKELQQHVKSVTAPYKYPRKIEFVL---------NLPKTVTGKIQRTKLRDK 566
Cdd:cd05932 450 FARAELEASLRAHLARVNSTLDSHEQLAGIVvvkdpwsidNGILTPTLKIKRNVLEKA 507
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-563 |
3.83e-32 |
|
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: 129.63 E-value: 3.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgde 162
Cdd:cd12117 25 YAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 viQEVDTVASECPSLRIKLLVSEKSCDGwlnfkklLNEASTthhcvetGSQEASA-IYFTSGTSGLPK--MAEHsYSSLG 239
Cdd:cd12117 101 --DRSLAGRAGGLEVAVVIDEALDAGPA-------GNPAVP-------VSPDDLAyVMYTSGSTGRPKgvAVTH-RGVVR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 240 LKakMDAGWTGLQASDIMWTISDTGW---ILNILGSLLEswtlGACtfVHLLPK---FDPLVILKTLSSYPIKSMMGAPI 313
Cdd:cd12117 164 LV--KNTNYVTLGPDDRVLQTSPLAFdasTFEIWGALLN----GAR--LVLAPKgtlLDPDALGALIAEEGVTVLWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 314 VYRMLLQQDLSSykFPHLQNCLAGGESLLPETLENWRAQT-GLDIREFYGQTETGL--TCMVsktmkIKPGYM------- 383
Cdd:cd12117 236 LFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTftTSHV-----VTELDEvagsipi 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 384 GTAASCYDVQVIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVENPDKTA----ANIRGD---FWLLGDRGIKDED 453
Cdd:cd12117 309 GRPIANTRVYVLDEDGRPVPPGVPGELyvgGD--------GLALGYLNRPALTAerfvADPFGPgerLYRTGDLARWLPD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 454 GYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPD-PVRGEVVkAFVIlASQFLSHDpeqltkELQQHVK 532
Cdd:cd12117 381 GRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDaGGDKRLV-AYVV-AEGALDAA------ELRAFLR 452
|
490 500 510
....*....|....*....|....*....|.
gi 157311624 533 SVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd12117 453 ERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
49-566 |
1.15e-31 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 129.45 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 49 DVLDHWAdmEKAGKRlpsPALWW-VNGKGKELMWnfRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCI 127
Cdd:COG1022 15 DLLRRRA--ARFPDR---VALREkEDGIWQSLTW--AEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 128 RAGLIFMPgtIQMKST--DILYRLQMSKAKAIVAGD-EVIQEVDTVASECPSLRiKLLV----SEKSCDGWLNFKKLLNE 200
Cdd:COG1022 87 AAGAVTVP--IYPTSSaeEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVldprGLRDDPRLLSLDELLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 201 ASTTHH--CVETGSQEASA-----IYFTSGTSGLPKMAEHSYSSLglkakmdagWTGLQASDIMWTISDTGWILNIL--- 270
Cdd:COG1022 164 GREVADpaELEARRAAVKPddlatIIYTSGTTGRPKGVMLTHRNL---------LSNARALLERLPLGPGDRTLSFLpla 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 271 ---GSLLESWTL--GAC--------TFVHLLPKFDPLVIL---------------KTLSSYPIKSM-----MGAPIVYRM 317
Cdd:COG1022 235 hvfERTVSYYALaaGATvafaespdTLAEDLREVKPTFMLavprvwekvyagiqaKAEEAGGLKRKlfrwaLAVGRRYAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 318 LLQQDLS---SYKFPH------------------LQNCLAGGESLLPETLENWRAqTGLDIREFYGQTETGLTCMVSKTM 376
Cdd:COG1022 315 ARLAGKSpslLLRLKHaladklvfsklrealggrLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 377 KIKPGYMGTAAScyDVQV-IDDKGNVLppgtegdigirvkpIRPIGIFSGYVENPDKTAANIRGDFWLL-GDRGIKDEDG 454
Cdd:COG1022 394 DNRIGTVGPPLP--GVEVkIAEDGEIL--------------VRGPNVMKGYYKNPEATAEAFDADGWLHtGDIGELDEDG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 455 YFQFMGRADDII-NSSGYRIGPSEVENALMKHP----AVV--E-----TAVIsSPDPvrgEVVK--------AFVILASq 514
Cdd:COG1022 458 FLRITGRKKDLIvTSGGKNVAPQPIENALKASPlieqAVVvgDgrpflAALI-VPDF---EALGewaeenglPYTSYAE- 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157311624 515 fLSHDPEqLTKELQQHVKSVTApyKYPR--KI-EFVLnLPK---------TVTGKIQRTKLRDK 566
Cdd:COG1022 533 -LAQDPE-VRALIQEEVDRANA--GLSRaeQIkRFRL-LPKeftiengelTPTLKLKRKVILEK 591
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
81-564 |
1.21e-31 |
|
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: 127.48 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivag 160
Cdd:cd17649 13 LSYAELDARANRLAHRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 deviqevdtVASECPSLRIKLLVsEKSCDGWLnfkkllneasTTHHcvetGSQEASAIYfTSGTSGLPKMAEHSYSSLGL 240
Cdd:cd17649 67 ---------LDPEYPAERLRYML-EDSGAGLL----------LTHH----PRQLAYVIY-TSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAKMDAGWTGLQASDIM---WTISDTGWILNILGSLLEswtlGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-R 316
Cdd:cd17649 122 HCQATAERYGLTPGDRElqfASFNFDGAHEQLLPPLIC----GACVVLRPDELWASADELAEMVRELGVTVLDLPPAYlQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 317 MLLQQ--DLSSYKFPHLQNCLAGGESLLPETLENWRAQtglDIREF--YGQTETGLTCMVSKT---MKIKPGYM--GTAA 387
Cdd:cd17649 198 QLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRWLKA---PVRLFnaYGPTEATVTPLVWKCeagAARAGASMpiGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 388 SCYDVQVIDDKGNVLPPGTEGD--IGIRvkpirpiGIFSGYVENPDKTAANIRGD--------FWLLGDRGIKDEDGYFQ 457
Cdd:cd17649 275 GGRSAYILDADLNPVPVGVTGElyIGGE-------GLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 458 FMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQltkeLQQHVKSVTAP 537
Cdd:cd17649 348 YLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQ----LRTALRASLPD 423
|
490 500
....*....|....*....|....*..
gi 157311624 538 YKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd17649 424 YMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
83-564 |
2.10e-31 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 128.75 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:PRK05620 41 FAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 VIQEVDTVASECPSLRIKLLVSEKSCDG----------WLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 232
Cdd:PRK05620 121 LAEQLGEILKECPCVRAVVFIGPSDADSaaahmpegikVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 233 HSYSSLGLKAkmdagwTGLQASDIMWTISDTGW-----ILNIL--GSLLESWTLGAcTFVHLLPKFDPLVILKTLSSYPI 305
Cdd:PRK05620 201 YSHRSLYLQS------LSLRTTDSLAVTHGESFlccvpIYHVLswGVPLAAFMSGT-PLVFPGPDLSAPTLAKIIATAMP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 306 KSMMGAPIVYRMLLQQDL-SSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVSKTmkiKPGYMG 384
Cdd:PRK05620 274 RVAHGVPTLWIQLMVHYLkNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARP---PSGVSG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 385 TAASCYDV-----------QVIDDkGNVLPPG--TEGDIGIRvKPIRPIGIFSGYVENPDKTAANIRG------------ 439
Cdd:PRK05620 351 EARWAYRVsqgrfpasleyRIVND-GQVMESTdrNEGEIQVR-GNWVTASYYHSPTEEGGGAASTFRGedvedandrfta 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 440 DFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlsh 518
Cdd:PRK05620 429 DGWLrTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGI--- 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 157311624 519 DPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:PRK05620 506 EPTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
81-563 |
2.22e-31 |
|
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: 127.02 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEviqEVDTVASECPSLRIKLLvsekscdgwlnfkkllnEASTTHHCVETGSQEASAIY--FTSGTSGLPKMAEHSYSSL 238
Cdd:cd12116 92 DA---LPDRLPAGLPVLLLALA-----------------AAAAAPAAPRTPVSPDDLAYviYTSGSTGRPKGVVVSHRNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 239 G--LKAKMDAgwTGLQASDIMWTISDTGW---ILNILGSLLEswtlGACtfVHLLPK---FDPLVILKTLSSYPIKSMMG 310
Cdd:cd12116 152 VnfLHSMRER--LGLGPGDRLLAVTTYAFdisLLELLLPLLA----GAR--VVIAPRetqRDPEALARLIEAHSITVMQA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 311 APIVYRMLL---QQDLSSYKFphlqncLAGGESLlPETLENWRAQTGLDIREFYGQTETGLTcmvSKTMKIKPGY----M 383
Cdd:cd12116 224 TPATWRMLLdagWQGRAGLTA------LCGGEAL-PPDLAARLLSRVGSLWNLYGPTETTIW---STAARVTAAAgpipI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 384 GTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTAANIRGD--------FWLLGDRGIKDEDGY 455
Cdd:cd12116 294 GRPLANTQVYVLDAALRPVPPGVPGELYIG-----GDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 456 FQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVkAFVILASQfLSHDPEQLTKELQQHVKSVT 535
Cdd:cd12116 369 LEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAG-AAPDAAALRAHLRATLPAYM 446
|
490 500
....*....|....*....|....*...
gi 157311624 536 APYKYPRKIEFvlnlPKTVTGKIQRTKL 563
Cdd:cd12116 447 VPSAFVRLDAL----PLTANGKLDRKAL 470
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
218-560 |
2.32e-31 |
|
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: 124.05 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 218 IYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQASdimwtiSDTgwILNILGSLLESWTLGACTF-------VHLLPK 290
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSW--IESFVCNEDLFNIS------GED--AILAPGPLSHSLFLYGAISalylggtFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 291 FDPLVILKTLSSYPIKSMMGAPivyrMLLQQdLSSYKFPHL--QNCLAGGESLLPETLENWRAQT-GLDIREFYGQTETG 367
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVP----TMLQA-LARTLEPESkiKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 368 LTCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVlppgtegdIG-IRVK-PIrpigIFSGYVE----NPDKtaanirgdf 441
Cdd:cd17633 150 FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGE--------IGkIFVKsEM----VFSGYVRggfsNPDG--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 442 WL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVkAFVILAsqflshdp 520
Cdd:cd17633 209 WMsVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSG-------- 279
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 157311624 521 EQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd17633 280 DKLTyKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
322-556 |
3.05e-31 |
|
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: 123.95 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 322 DLSSYKFPhlqNCLAGGESLLPETLENWRAQTGLdirefYGQTE-TGLTCMvsktmkikPGYMGTAASCY-------DVQ 393
Cdd:cd17636 112 DLSSLRSS---PAAPEWNDMATVDTSPWGRKPGG-----YGQTEvMGLATF--------AALGGGAIGGAgrpsplvQVR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 394 VIDDKGNVLPPGTEGDIGIRvKPIrpigIFSGYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRI 473
Cdd:cd17636 176 ILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 474 GPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIL-ASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPK 552
Cdd:cd17636 251 YPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLkPGASVTEA------ELIEHCRARIASYKKPKSVEFADALPR 324
|
....
gi 157311624 553 TVTG 556
Cdd:cd17636 325 TAGG 328
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
217-560 |
3.83e-31 |
|
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: 123.91 E-value: 3.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 217 AIYFTSGTSGLPKMAEHSYSSLGLKAKMdagwtgLQASDIMWTISDTGWILNILGSLLESWTLGACTF-----VHLLPKF 291
Cdd:cd17635 5 AVIFTSGTTGEPKAVLLANKTFFAVPDI------LQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIhgglcVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 292 DPLVILKTLSSYPIKSMMGAPIV--YRMLLQQDLSSYKfPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETG-L 368
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLlsKLVSELKSANATV-PSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGtA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 369 TCMVSKTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWLLGDRG 448
Cdd:cd17635 158 LCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSP-----ANMLGYWNNPERTAEVLIDGWVNTGDLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 449 IKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflshDPEQLTKELQ 528
Cdd:cd17635 233 ERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE----LDENAIRALK 308
|
330 340 350
....*....|....*....|....*....|..
gi 157311624 529 QHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
83-563 |
1.84e-30 |
|
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: 124.70 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM--SKAKAI 157
Cdd:cd17646 26 YRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP-------LDPGYpadRLAYmlADAGPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 VagdeVIQEVDTVASECPSLRIKLLVSEkscdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--MAEHSY 235
Cdd:cd17646 98 V----VLTTADLAARLPAGGDVALLGDE-----------ALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKgvMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 SS---LGLKAK--MDAGWTGLQASDIMWTISdtGW-ILnilgsllesWTL--GACTFV-----HLlpkfDPLVILKTLSS 302
Cdd:cd17646 163 IVnrlLWMQDEypLGPGDRVLQKTPLSFDVS--VWeLF---------WPLvaGARLVVarpggHR----DPAYLAALIRE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 303 YPIKSMMGAPIVYRMLLQQDLSSyKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTE-----TGLTCMVSKTMK 377
Cdd:cd17646 228 HGVTTCHFVPSMLRVFLAEPAAG-SCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEaaidvTHWPVRGPAETP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 378 IKP-GYMGTAASCYdvqVIDDKGNVLPPGTEGDI---GIRVKpirpigifSGYVENPDKTAANIRGD-------FWLLGD 446
Cdd:cd17646 307 SVPiGRPVPNTRLY---VLDDALRPVPVGVPGELylgGVQLA--------RGYLGRPALTAERFVPDpfgpgsrMYRTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 447 RGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEqltkE 526
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTA----A 451
|
490 500 510
....*....|....*....|....*....|....*..
gi 157311624 527 LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17646 452 LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
220-566 |
2.22e-30 |
|
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: 121.28 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 220 FTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDimwtisdtGWILN-----------ILGSLLESWTLgactfvHLL 288
Cdd:cd17630 7 LTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD--------SWLLSlplyhvgglaiLVRSLLAGAEL------VLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 289 PKFDPLviLKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQtGLDIREFYGQTETGL 368
Cdd:cd17630 73 ERNQAL--AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 369 TcmvsktmkikpgymgTAASCYDVQVIDDKGNVLPpgtegDIGIRVKP-----IRPIGIFSGYVENPDKTAANIRGdfWL 443
Cdd:cd17630 150 Q---------------VATKRPDGFGRGGVGVLLP-----GRELRIVEdgeiwVGGASLAMGYLRGQLVPEFNEDG--WF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 444 -LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVilasqflSHDPEQ 522
Cdd:cd17630 208 tTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI-------VGRGPA 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 157311624 523 LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDK 566
Cdd:cd17630 281 DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
102-564 |
1.66e-29 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 122.60 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 102 GLQRGDRVAVMLPRVPEW--WLVILGCirAGLIFMPgtiqmkstdILYRLQMSKAKAIVagdEVIQEVDTVASE------ 173
Cdd:PLN02860 53 GLRNGDVVAIAALNSDLYleWLLAVAC--AGGIVAP---------LNYRWSFEEAKSAM---LLVRPVMLVTDEtcsswy 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 174 -------CPSLRIKLLVSEKSCDGWLNFKKLLN-EASTTHHCVETGSQEASA------IYFTSGTSGLPKMAEHSYSSLG 239
Cdd:PLN02860 119 eelqndrLPSLMWQVFLESPSSSVFIFLNSFLTtEMLKQRALGTTELDYAWApddavlICFTSGTTGRPKGVTISHSALI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 240 LKAKMDAGWTGLQASDIMWTISDTGWILNIlGSLLESWTLGACtfvH-LLPKFDPLVILKTLSSYPIKSMMGAPIVYRML 318
Cdd:PLN02860 199 VQSLAKIAIVGYGEDDVYLHTAPLCHIGGL-SSALAMLMVGAC---HvLLPKFDAKAALQAIKQHNVTSMITVPAMMADL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 319 L---QQDLSSYKFPHLQNCLAGGES----LLPETLENW-RAQtgldIREFYGQTET--GLTCMV--SKTMKIKPGYMGTA 386
Cdd:PLN02860 275 IsltRKSMTWKVFPSVRKILNGGGSlssrLLPDAKKLFpNAK----LFSAYGMTEAcsSLTFMTlhDPTLESPKQTLQTV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 387 ASCYDvQVIDDKGNVL----PPGTEgdIGIRVKPIRPIG-IFS-------GYVENPDKTAANIRGDFWL-LGDRGIKDED 453
Cdd:PLN02860 351 NQTKS-SSVHQPQGVCvgkpAPHVE--LKIGLDESSRVGrILTrgphvmlGYWGQNSETASVLSNDGWLdTGDIGWIDKA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 454 GYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIL--------ASQFLSHDPEQLTK 525
Cdd:PLN02860 428 GNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLrdgwiwsdNEKENAKKNLTLSS 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 157311624 526 E-LQQHV--KSVTApYKYPRKieFVLN---LPKTVTGKIQRTKLR 564
Cdd:PLN02860 508 EtLRHHCreKNLSR-FKIPKL--FVQWrkpFPLTTTGKIRRDEVR 549
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
81-565 |
6.09e-29 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 122.66 E-value: 6.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILsGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtIqmkstDILY---RLQM----SK 153
Cdd:COG1020 502 LTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP--L-----DPAYpaeRLAYmledAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 154 AKAIVAGDEViqevdtvASECPSLRIKLLVsekscdgwLNFKKLLNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MA 231
Cdd:COG1020 574 ARLVLTQSAL-------AARLPELGVPVLA--------LDALALAAEPATNPPVPVTPDDLAYVIY-TSGSTGRPKgvMV 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 232 EHSysslGLKAKMDA--GWTGLQASDIM---WTIS-DTGwILNILGSLLeswtLGACtfVHLLPK---FDPLVILKTLSS 302
Cdd:COG1020 638 EHR----ALVNLLAWmqRRYGLGPGDRVlqfASLSfDAS-VWEIFGALL----SGAT--LVLAPPearRDPAALAELLAR 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 303 YPIKSMMGAPIVYRMLLQQDLSSykFPHLQNCLAGGESLLPETLENWRAQT-GLDIREFYGQTETglTCMVSkTMKIKPG 381
Cdd:COG1020 707 HRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTET--TVDST-YYEVTPP 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 382 YMGTAASCY-------DVQVIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVENPDKTAAN-IRGDFWLL------ 444
Cdd:COG1020 782 DADGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELyigGA--------GLARGYLNRPELTAERfVADPFGFPgarlyr 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 445 -GDRGIKDEDGYFQFMGRADD---IinsSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASqflshDP 520
Cdd:COG1020 854 tGDLARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA-----GA 925
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 157311624 521 EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:COG1020 926 AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
69-564 |
1.28e-28 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 120.77 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 69 LWWVNGKGKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYR 148
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 149 LQMSKAKAIVA------GDEVIQEVDTV-------ASECPSLRIKLLVSEKSC------------DGWlnFKKLLNEAST 203
Cdd:PLN02654 188 IVDCKPKVVITcnavkrGPKTINLKDIVdaaldesAKNGVSVGICLTYENQLAmkredtkwqegrDVW--WQDVVPNYPT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 204 THHCVETGSQEASAIYFTSGTSGLPKMAEHS------YSSLGLKAKMDagwtgLQASDIMWTISDTGWILN----ILGSL 273
Cdd:PLN02654 266 KCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTtggymvYTATTFKYAFD-----YKPTDVYWCTADCGWITGhsyvTYGPM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 274 LEswtlGACTFV-HLLPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCLAGGESLLPETlen 348
Cdd:PLN02654 341 LN----GATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSA--- 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 349 WR------AQTGLDIREFYGQTETGlTCMVSKTMKIKPGYMGTAA-SCYDVQ--VIDDKGNVLppgtEGDIG--IRVKPI 417
Cdd:PLN02654 414 WRwffnvvGDSRCPISDTWWQTETG-GFMITPLPGAWPQKPGSATfPFFGVQpvIVDEKGKEI----EGECSgyLCVKKS 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 418 RPiGIFS---GYVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVI 494
Cdd:PLN02654 489 WP-GAFRtlyGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVV 567
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 495 SSPDPVRGEVVKAFVILASQFLShdPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:PLN02654 568 GIEHEVKGQGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
93-565 |
3.50e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 118.97 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 93 AANILSgaCGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA-------GDEVIQ 165
Cdd:PLN03102 53 AASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVdrsfeplAREVLH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 166 EVDTVASEcPSLRIKLL----VSEKSCDGWLNFKKLLNEASTTHHCVET-----GSQEASAIYFTSGTSGLPKMAEHSYS 236
Cdd:PLN03102 131 LLSSEDSN-LNLPVIFIheidFPKRPSSEELDYECLIQRGEPTPSLVARmfriqDEHDPISLNYTSGTTADPKGVVISHR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 237 SLGLKA-KMDAGWTGLQASDIMWTISD---TGWILnilgslleSWTLGA------CTFVHLLPKfdplvILKTLSSYPIK 306
Cdd:PLN03102 210 GAYLSTlSAIIGWEMGTCPVYLWTLPMfhcNGWTF--------TWGTAArggtsvCMRHVTAPE-----IYKNIEMHNVT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 307 SMMGAPIVYRMLLQQDLS--SYKFPHLQnCLAGGESLlPETLENWRAQTGLDIREFYGQTE-TG--LTCM---------V 372
Cdd:PLN03102 277 HMCCVPTVFNILLKGNSLdlSPRSGPVH-VLTGGSPP-PAALVKKVQRLGFQVMHAYGLTEaTGpvLFCEwqdewnrlpE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 373 SKTMKIKPGYMGTAASCYDVQVIDDKGNVLPP---GTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWLLGDRGI 449
Cdd:PLN03102 355 NQQMELKARQGVSILGLADVDVKNKETQESVPrdgKTMGEIVIKGS-----SIMKGYLKNPKATSEAFKHGWLNTGDVGV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 450 KDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIL--ASQFLSHDPEQL-TKE 526
Cdd:PLN03102 430 IHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLvTRE 509
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 157311624 527 --LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PLN03102 510 rdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-564 |
4.48e-28 |
|
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: 117.92 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 78 ELMWNFRELSENSQQAANILSGaCGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 157
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 VAGDEVIqevdTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPKMAEHSY- 235
Cdd:cd05915 101 LFDPNLL----PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 ------SSLGLKAKMDAGWTGLQASDI-MWTISdtGWILnilgslleSWTLGAC--TFVHLLPKFDPLVILKTLSSYPIK 306
Cdd:cd05915 177 alvlhsLAASLVDGTALSEKDVVLPVVpMFHVN--AWCL--------PYAATLVgaKQVLPGPRLDPASLVELFDGEGVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 307 SMMGAPIVYRMLLQ-QDLSSYKFPHLQNCLAGGESLlPETLENWRAQTGLDIREFYGQTET---GLTCMVSKTMKIKPGY 382
Cdd:cd05915 247 FTAGVPTVWLALADyLESTGHRLKTLRRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETspvVVQNFVKSHLESLSEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 383 MGTAASCYD-VQVIDDKGNVLPPGT-----EGDIgIRVKPIRPIGIFSGYVENPDKTAAN-IRGDFWLLGDRGIKDEDGY 455
Cdd:cd05915 326 EKLTLKAKTgLPIPLVRLRVADEEGrpvpkDGKA-LGEVQLKGPWITGGYYGNEEATRSAlTPDGFFRTGDIAVWDEEGY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 456 FQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILasqflsHDPEQLTKELQQHVKSVT 535
Cdd:cd05915 405 VEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVP------RGEKPTPEELNEHLLKAG 478
|
490 500 510
....*....|....*....|....*....|
gi 157311624 536 APYKY-PRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd05915 479 FAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-565 |
6.00e-28 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 116.64 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivagde 162
Cdd:cd17653 25 YGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP--------------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 viqeVDTvasECPSLRIKLLVSEKSCdgwlnfkKLlneastthhCVETGSQEASA-IYFTSGTSGLPK--MAEHS----Y 235
Cdd:cd17653 77 ----LDA---KLPSARIQAILRTSGA-------TL---------LLTTDSPDDLAyIIFTSGSTGIPKgvMVPHRgvlnY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 SSLGlKAKMDA--GWTGLQasdiMWTISDTGWILNILGSLLESWTL----GACTFVHLLPKFDPLvilktlssypiksmM 309
Cdd:cd17653 134 VSQP-PARLDVgpGSRVAQ----VLSIAFDACIGEIFSTLCNGGTLvladPSDPFAHVARTVDAL--------------M 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 310 GAPIVYRMLLQQDlssykFPHLQNCLAGGESLLPETLENWRAqtGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASC 389
Cdd:cd17653 195 STPSILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPN 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 390 YDVQVIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTAANIRGD-FW------LLGDRGIKDEDGYFQFMGRA 462
Cdd:cd17653 268 STCYILDADLQPVPEGVVGEICIS-----GVQVARGYLGNPALTASKFVPDpFWpgsrmyRTGDYGRWTEDGGLEFLGRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 463 DDIINSSGYRIGPSEVENALMKHPAVVETAVISspdpVRGEVVKAFVILASQflshDPEQLTKELQQHVKSvtapYKYPR 542
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI----VVNGRLVAFVTPETV----DVDGLRSELAKHLPS----YAVPD 410
|
490 500
....*....|....*....|...
gi 157311624 543 KIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:cd17653 411 RIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
91-565 |
6.06e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 118.02 E-value: 6.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 91 QQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMpgTIQMKSTDILYRLQMSKAKAIVAgdevIQEVDTV 170
Cdd:PLN02574 77 KSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT--TMNPSSSLGEIKKRVVDCSVGLA----FTSPENV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 171 aSECPSLRIK-LLVSEKscdgwLNFKKLLNEASTTHHCVET----------GSQEASAIYFTSGTSGLPK--MAEHS--Y 235
Cdd:PLN02574 151 -EKLSPLGVPvIGVPEN-----YDFDSKRIEFPKFYELIKEdfdfvpkpviKQDDVAAIMYSSGTTGASKgvVLTHRnlI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 SSLGLKAKMDAGWTGLQASD-------IMWTIsdTGWILNILGSLleswTLGACTFVhlLPKFDPLVILKTLSSYPIKSM 308
Cdd:PLN02574 225 AMVELFVRFEASQYEYPGSDnvylaalPMFHI--YGLSLFVVGLL----SLGSTIVV--MRRFDASDMVKVIDRFKVTHF 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 309 mgaPIVYRMLL-----QQDLSSYKFPHLQNCLAGGESLLPETLENW-RAQTGLDIREFYGQTET---GLTCMVSKTMKiK 379
Cdd:PLN02574 297 ---PVVPPILMaltkkAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTEStavGTRGFNTEKLS-K 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 380 PGYMGTAASCYDVQVID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQ 457
Cdd:PLN02574 373 YSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ-GP----GVMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLY 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 458 FMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflshdpEQLTKE-LQQHVKSVTA 536
Cdd:PLN02574 448 IVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQEaVINYVAKQVA 521
|
490 500
....*....|....*....|....*....
gi 157311624 537 PYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PLN02574 522 PYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-563 |
3.18e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 117.57 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 EVIQEVDtVASECPSLRIKLLvsekscdgwlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLK 241
Cdd:PRK12467 618 HLLAQLP-VPAGLRSLCLDEP------------ADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANY 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 242 AKMDAGWTGLQASDIMW---TISDTGWILNILGSLleswTLGACtfVHLLPK---FDPLVILKTLSSYPIKSMMGAPIVY 315
Cdd:PRK12467 685 VCVIAERLQLAADDSMLmvsTFAFDLGVTELFGAL----ASGAT--LHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHL 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 316 RMLLQQDLSSYKFPHLQnCLAGGESLLPETLENWRA-QTGLDIREFYGQTETglTCMVS------KTMKIKPGYMGTAAS 388
Cdd:PRK12467 759 QALLQASRVALPRPQRA-LVCGGEALQVDLLARVRAlGPGARLINHYGPTET--TVGVStyelsdEERDFGNVPIGQPLA 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 389 CYDVQVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMG 460
Cdd:PRK12467 836 NLGLYILDHYLNPVPVGVVGELYIGGA-----GLARGYHRRPALTAERFVPDpfgadggrLYRTGDLARYRADGVIEYLG 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 461 RADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVkAFVILASQFLSHDPEQLTKELQQHVKSVTAPYKY 540
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMV 989
|
490 500
....*....|....*....|...
gi 157311624 541 PRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:PRK12467 990 PAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
102-571 |
6.56e-27 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 115.51 E-value: 6.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 102 GLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQmkstdiLYRlqmskakaivaGDEVIQEVDTVASecpslrikL 181
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE------LHR-----------DDHALAARNTEPA--------L 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 182 LVSEKS-CDGW-----LNFKKLLNEAS---TTHHCVETGSQEASAIYfTSGTSGLPKMAEHSYSS-LGLKAKMDAGWTGL 251
Cdd:PRK06060 106 VVTSDAlRDRFqpsrvAEAAELMSEAArvaPGGYEPMGGDALAYATY-TSGTTGPPKAAIHRHADpLTFVDAMCRKALRL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 252 QASDI---------MWTISDTGWILNILGS--LLESWTLGACTFVHLLPKFDPLVilktlssypiksMMGAPIVYRMLLQ 320
Cdd:PRK06060 185 TPEDTglcsarmyfAYGLGNSVWFPLATGGsaVINSAPVTPEAAAILSARFGPSV------------LYGVPNFFARVID 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 321 QdLSSYKFPHLQNCLAGGESL---LPETLENWRAqtGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIDD 397
Cdd:PRK06060 253 S-CSPDSFRSLRCVVSAGEALelgLAERLMEFFG--GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 398 KGNVLPPGTEGDIGIRvKPirpiGIFSGYVENPDKTAANirGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSE 477
Cdd:PRK06060 330 DGTTAGPGVEGDLWVR-GP----AIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 478 VENALMKHPAVVETAVISSPDPVRGEVVKAFVILAS-QFLShdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 556
Cdd:PRK06060 403 VERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgATID---GSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNG 479
|
490 500
....*....|....*....|
gi 157311624 557 KIQRTKLRDKE-----WKMS 571
Cdd:PRK06060 480 KLVRGALRKQSptkpiWELS 499
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
218-568 |
3.09e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 112.47 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 218 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDI----M-WTISdtgwilnilGSLLESWTLGACT--FVHLLPK 290
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVcyvsMpLFHS---------NAVMAGWAVALAAgaSIALRRK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 291 FDPLVILKTLSSYPIKSM--MGAPIVYRmllqqdLSSYKFP-HLQNCL--AGGESLLPETLENWRAQTGLDIREFYGQTE 365
Cdd:PRK07867 228 FSASGFLPDVRRYGATYAnyVGKPLSYV------LATPERPdDADNPLriVYGNEGAPGDIARFARRFGCVVVDGFGSTE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 366 TGLTcmVSKTMKIKPGYMGTAAScyDVQVID-DKGNVLPPGtEGDIGIRVKPIRPIG---------IFSGYVENPDKTAA 435
Cdd:PRK07867 302 GGVA--ITRTPDTPPGALGPLPP--GVAIVDpDTGTECPPA-EDADGRLLNADEAIGelvntagpgGFEGYYNDPEADAE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 436 NIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILA--S 513
Cdd:PRK07867 377 RMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLApgA 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 157311624 514 QFlshDPEQLTKELqqHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEW 568
Cdd:PRK07867 457 KF---DPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
477-557 |
1.56e-25 |
|
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: 99.93 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 477 EVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 556
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 157311624 557 K 557
Cdd:pfam13193 76 K 76
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-563 |
1.63e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 112.36 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 108 RVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpslrIKLLVSEKS 187
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDG------LASLALDRD 4676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 188 CDgWLNFkkllneaSTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-------GLKAKMDAGWTGLQASDIMWTI 260
Cdd:PRK12316 4677 ED-WEGF-------PAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLvnhlhatGERYELTPDDRVLQFMSFSFDG 4748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 261 SDTGWILNIlgslleswTLGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGES 340
Cdd:PRK12316 4749 SHEGLYHPL--------INGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEA 4820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 341 LLPETL-ENWRAQTGLDIREFYGQTETGLTCMVSKTMKIKP---GYM--GTAASCYDVQVIDDKGNVLPPGTEGDIGIRV 414
Cdd:PRK12316 4821 VAQASYdLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDAcgaAYMpiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGG 4900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 415 KpirpiGIFSGYVENPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHP 486
Cdd:PRK12316 4901 E-----GVARGYLERPALTAERFVPDpfgapggrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHP 4975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 487 AVVETAVISSPDPVRGEVVkAFVILASQFLSHDPE---QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:PRK12316 4976 AVREAVVIAQEGAVGKQLV-GYVVPQDPALADADEaqaELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
83-563 |
2.49e-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: 108.88 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivagde 162
Cdd:cd17652 15 YAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLP--------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 viqeVDtvaSECPSLRIKLLVSEKSCdgwlnfkkllneastthHCVETGSQEASAIYFTSGTSGLPK--MAEHS-YSSL- 238
Cdd:cd17652 67 ----LD---PAYPAERIAYMLADARP-----------------ALLLTTPDNLAYVIYTSGSTGRPKgvVVTHRgLANLa 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 239 -GLKAKMDAGWTG--LQASdimwTISDTGWILNILGSLLESWTLgactfvhLLPKFDPLV----ILKTLSSYPIKSMMGA 311
Cdd:cd17652 123 aAQIAAFDVGPGSrvLQFA----SPSFDASVWELLMALLAGATL-------VLAPAEELLpgepLADLLREHRITHVTLP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 312 PIVYRMLLQQDLssykfPHLQNCLAGGESLLPETLENWrAQTgldiREF---YGQTETGLTCMVSK---TMKIKPgyMGT 385
Cdd:cd17652 192 PAALAALPPDDL-----PDLRTLVVAGEACPAELVDRW-APG----RRMinaYGPTETTVCATMAGplpGGGVPP--IGR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 386 AASCYDVQVIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVENPDKTA----ANIRGD----FWLLGDRGIKDEDGYFQ 457
Cdd:cd17652 260 PVPGTRVYVLDARLRPVPPGVPGEL-----YIAGAGLARGYLNRPGLTAerfvADPFGApgsrMYRTGDLARWRADGQLE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 458 FMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASqflshDPEQLTKELQQHVKSVTAP 537
Cdd:cd17652 335 FLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPG 409
|
490 500
....*....|....*....|....*.
gi 157311624 538 YKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17652 410 YMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
81-566 |
6.92e-25 |
|
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: 108.66 E-value: 6.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEviQEVD---TVASECPSLRIKLLVSEKSC----DGWLNFKKLLNEASTTHHCVETGSQEA----------SAIYFTSG 223
Cdd:cd17641 91 DE--EQVDkllEIADRIPSVRYVIYCDPRGMrkydDPRLISFEDVVALGRALDRRDPGLYERevaagkgedvAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 224 TSGLPKMA--------EHSYSSLGLKAK---------MDAGWTGLQasdiMWTISD---TGWILNILGS---LLESWTLG 280
Cdd:cd17641 169 TTGKPKLAmlshgnflGHCAAYLAADPLgpgdeyvsvLPLPWIGEQ----MYSVGQalvCGFIVNFPEEpetMMEDLREI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 281 ACTFVHLLPK-FDPL---VILKTLSSYPIKSMM-------------------------------GAPIVYRMLLQQdlss 325
Cdd:cd17641 245 GPTFVLLPPRvWEGIaadVRARMMDATPFKRFMfelgmklglraldrgkrgrpvslwlrlaswlADALLFRPLRDR---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 326 YKFPHLQNCLAGGESLLPETLENWRAqTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAAScyDVQV-IDDKGNVLpp 404
Cdd:cd17641 321 LGFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFP--GTEVrIDEVGEIL-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 405 gtegdigirvkpIRPIGIFSGYVENPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRADDIINSS-GYRIGPSEVENAL 482
Cdd:cd17641 396 ------------VRSPGVFVGYYKNPEATAEDFDEDGWLHtGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 483 MKHPAVVETAVISSPDP-------VRGEVV------KAFVILASQFLSHDPEqLTKELQQHVKSVTAPYKYPRKIEFVLN 549
Cdd:cd17641 464 KFSPYIAEAVVLGAGRPyltaficIDYAIVgkwaeqRGIAFTTYTDLASRPE-VYELIRKEVEKVNASLPEAQRIRRFLL 542
|
570 580
....*....|....*....|....*.
gi 157311624 550 LPK---------TVTGKIQRTKLRDK 566
Cdd:cd17641 543 LYKeldaddgelTRTRKVRRGVIAEK 568
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
212-560 |
1.13e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 106.66 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 212 SQEASAIYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQASDIMWTI------SDTGWILNILGSLleswTLGACtfV 285
Cdd:PRK08308 100 AEEPSLLQYSSGTTGEPKLIRRSWTEI--DREIEAYNEALNCEQDETPIvacpvtHSYGLICGVLAAL----TRGSK--P 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 286 HLLPKFDPLVILKTLSSYPIKSMMGAPIVY----RMLLQQDlssykfpHLQNCLAGGeSLLPET-LENWRAQTGLDIREf 360
Cdd:PRK08308 172 VIITNKNPKFALNILRNTPQHILYAVPLMLhilgRLLPGTF-------QFHAVMTSG-TPLPEAwFYKLRERTTYMMQQ- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 361 YGQTETGltCMvsktmkikpgymgtaASCYDVQVIDDKGNVLPpgtEGDIGIRVKPIRPIGIFsgyVENPDKTAANirgd 440
Cdd:PRK08308 243 YGCSEAG--CV---------------SICPDMKSHLDLGNPLP---HVSVSAGSDENAPEEIV---VKMGDKEIFT---- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 441 fwllGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAfvilasQFLSH-- 518
Cdd:PRK08308 296 ----KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVISHee 365
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 157311624 519 -DPEQLTKELQQHVksvtAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:PRK08308 366 iDPVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSR 404
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
83-563 |
1.32e-24 |
|
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: 107.01 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagde 162
Cdd:cd17643 15 YGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVP-------IDPAY--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 viqevdtvasecPSLRIKLLV--SEKSCdgwlnfkkLLNEASTThhcvetgsqeASAIYfTSGTSGLPK--MAEHSySSL 238
Cdd:cd17643 72 ------------PVERIAFILadSGPSL--------LLTDPDDL----------AYVIY-TSGSTGRPKgvVVSHA-NVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 239 GLKAKMDAgWTGLQASDIMWTISDTG-----WilNILGSLL--------ESWTLGACTFVHLLPKFDPLVIL-KTlssyp 304
Cdd:cd17643 120 ALFAATQR-WFGFNEDDVWTLFHSYAfdfsvW--EIWGALLhggrlvvvPYEVARSPEDFARLLRDEGVTVLnQT----- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 305 iksmmgaPIVYRMLLQQDLSSYKFPH-LQNCLAGGESLLPETLENWRAQTGLDIREF---YGQTETglTCMVSKTmKIKP 380
Cdd:cd17643 192 -------PSAFYQLVEAADRDGRDPLaLRYVIFGGEALEAAMLRPWAGRFGLDRPQLvnmYGITET--TVHVTFR-PLDA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 381 GYMGTAA--------SCYDVQVIDDKGNVLPPGTEGDIGIRvkpiRPiGIFSGYVENPDKTAANIRGD-FWLLGDRGIKD 451
Cdd:cd17643 262 ADLPAAAaspigrplPGLRVYVLDADGRPVPPGVVGELYVS----GA-GVARGYLGRPELTAERFVANpFGGPGSRMYRT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 452 ED-------GYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflshdPEQLT 524
Cdd:cd17643 337 GDlarrlpdGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG-----AAADI 411
|
490 500 510
....*....|....*....|....*....|....*....
gi 157311624 525 KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17643 412 AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-557 |
1.68e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 105.16 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 218 IYFTSGTSGLPK--MAEH--SYSSLGLKAKMDAGwtglQASDIMWTI----SDTGWILNILGSLLE---SWT-----LGA 281
Cdd:cd05924 8 ILYTGGTTGMPKgvMWRQedIFRMLMGGADFGTG----EFTPSEDAHkaaaAAAGTVMFPAPPLMHgtgSWTafgglLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 282 CTFVHLLPKFDPLVILKTLSSYPIKSM------MGAPIV--YRMLLQQDLSSykfphLQNCLAGGESLLPETLENW-RAQ 352
Cdd:cd05924 84 QTVVLPDDRFDPEEVWRTIEKHKVTSMtivgdaMARPLIdaLRDAGPYDLSS-----LFAISSGGALLSPEVKQGLlELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 353 TGLDIREFYGQTETGLT-CMVSKTMKIKPGYMGTAAScyDVQVIDDKGNVLPPGTE--GDIGIR-VKPIrpigifsGYVE 428
Cdd:cd05924 159 PNITLVDAFGSSETGFTgSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGgvGWIARRgHIPL-------GYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 429 NPDKTAANIR---GDFW-LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEV 504
Cdd:cd05924 230 DEAKTAETFPevdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 157311624 505 VKAFVILASqflSHDPEQltKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGK 557
Cdd:cd05924 310 VVAVVQLRE---GAGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
218-560 |
4.88e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 106.36 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 218 IYFTSGTSGLPKMAEHSYSS--LGLKAKmdagWTGLQASD---IMWTISDTGWILnILGSLLESWTLGaCTFVH-----L 287
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPhlVGLKYY----WRSIIEKDiptVVFSHSSIGWVS-FHGFLYGSLSLG-NTFVMfeggiI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 288 LPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD------LSSYKFPHLQNCLAGGESL---LPETLENwraqtGLDIR 358
Cdd:PTZ00237 333 KNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIeesIPEYIEN-----KLKIK 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 359 --EFYGQTETGLTCMVSKTMKIKPGY-MGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVkPIRPiGIFSGYVENPD--KT 433
Cdd:PTZ00237 408 ssRGYGQTEIGITYLYCYGHINIPYNaTGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPP-SFATTFYKNDEkfKQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 434 AANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAS 513
Cdd:PTZ00237 486 LFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQ 565
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 157311624 514 QFLSH--DPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:PTZ00237 566 DQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
81-564 |
9.27e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 105.07 E-value: 9.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELsensQQAANILSGAC---GLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDIL-YRLQM----- 151
Cdd:PRK10946 49 FSYREL----NQASDNLACSLrrqGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNaYASQIepall 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 152 --SKAKAIVAGDEVIqevDTVASECPSLRIKLLVSEkscDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK 229
Cdd:PRK10946 125 iaDRQHALFSDDDFL---NTLVAEHSSLRVVLLLND---DGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 230 M--------------------------------AEHSY--SSLGLKAKMDAGWTGLQASDIMWTISdtgwilnilGSLLE 275
Cdd:PRK10946 199 LiprthndyyysvrrsveicgftpqtrylcalpAAHNYpmSSPGALGVFLAGGTVVLAPDPSATLC---------FPLIE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 276 SWTLgacTFVHLLPkfdPLVIL----KTLSSYpiksmmgapivyrmllQQDLSSYKFphLQnclAGGESLLPETLENWRA 351
Cdd:PRK10946 270 KHQV---NVTALVP---PAVSLwlqaIAEGGS----------------RAQLASLKL--LQ---VGGARLSETLARRIPA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 352 QTGLDIREFYGQTEtGLtcmVSKT-MKIKPGYMGTAASCY-----DVQVIDDKGNVLPPGTEGDIGIRvkpirpiG--IF 423
Cdd:PRK10946 323 ELGCQLQQVFGMAE-GL---VNYTrLDDSDERIFTTQGRPmspddEVWVADADGNPLPQGEVGRLMTR-------GpyTF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 424 SGYVENPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRG 502
Cdd:PRK10946 392 RGYYKSPQHNASAFDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157311624 503 EVVKAFVILASQFlshDPEQLTKEL-QQHVksvtAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:PRK10946 472 EKSCAFLVVKEPL---KAVQLRRFLrEQGI----AEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
81-563 |
1.12e-23 |
|
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: 103.79 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGaCGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 160
Cdd:cd17645 24 LTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPK--MAEH-SYSS 237
Cdd:cd17645 101 -------------------------------------------------TNPDDLAYVIYTSGSTGLPKgvMIEHhNLVN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 238 LGLKAKMDAGWTGLQASDIMWTISDTGWILNILgsllESWTLGACtfVHLLPKFDPLVILK----------TLSSYPIKs 307
Cdd:cd17645 132 LCEWHRPYFGVTPADKSLVYASFSFDASAWEIF----PHLTAGAA--LHVVPSERRLDLDAlndyfnqegiTISFLPTG- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 308 mmgapiVYRMLLQQDLSSykfphLQNCLAGGESLlpetleNWRAQTGLDIREFYGQTEtgltCMVSKTM-KIKPGY---- 382
Cdd:cd17645 205 ------AAEQFMQLDNQS-----LRVLLTGGDKL------KKIERKGYKLVNNYGPTE----NTVVATSfEIDKPYanip 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 383 MGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWLLGDRGIKD-------EDGY 455
Cdd:cd17645 264 IGKPIDNTRVYILDEALQLQPIGVAGELCIAGE-----GLARGYLNRPELTAEKFIVHPFVPGERMYRTgdlakflPDGN 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 456 FQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFlshDPEqltkELQQHVKSVT 535
Cdd:cd17645 339 IEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEI---PHE----ELREWLKNDL 411
|
490 500
....*....|....*....|....*...
gi 157311624 536 APYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17645 412 PDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
81-565 |
1.72e-23 |
|
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: 103.78 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPewWLV--ILGCIRAGLIFMPgtiqmksTDILY---RLQmskak 155
Cdd:cd05918 25 LTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSK--WAVvaMLAVLKAGGAFVP-------LDPSHplqRLQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 156 aivagdEVIQEVDtvasecpslrIKLLVSekscdgwlnfkkllneastthhcvetgSQEASAIY--FTSGTSGLPK--MA 231
Cdd:cd05918 90 ------EILQDTG----------AKVVLT---------------------------SSPSDAAYviFTSGSTGKPKgvVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 232 EHSYSSLGLKA-----KMDAGWTGLQASDIMWTISdtgwILNILGslleSWTLGACTFVhlLPKFDPLVIL-KTLSSYPI 305
Cdd:cd05918 127 EHRALSTSALAhgralGLTSESRVLQFASYTFDVS----ILEIFT----TLAAGGCLCI--PSEEDRLNDLaGFINRLRV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 306 KSMMGAPIVYRMLLQQDlssykFPHLQNCLAGGESLLPETLENWraQTGLDIREFYGQTETGLTCMVSK-TMKIKPGYMG 384
Cdd:cd05918 197 TWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTW--ADRVRLINAYGPAECTIAATVSPvVPSTDPRNIG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 385 TA--ASCYdvqVID--DKGNVLPPGTEGDI---GirvkPIrpigIFSGYVENPDKTAAN-IRGDFWLL------------ 444
Cdd:cd05918 270 RPlgATCW---VVDpdNHDRLVPIGAVGELlieG----PI----LARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyr 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 445 -GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAV---VETAVISSPDPVRGEVVKAFVILASQFLSHDP 520
Cdd:cd05918 339 tGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGakeVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGD 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 157311624 521 EQ------------LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:cd05918 419 GDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
82-574 |
1.91e-23 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 104.06 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSGAcGLQRGDRVAVM---LPRVPEWWLVILGcirAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 158
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWYGIMG---IGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 159 AGDEVIQEVDTVASECPSLRIKLLVSEKS------CDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 232
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTDAAhmpqttLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 233 HSYSSLGLKAKM--DAGWTGLQASDIMWTISDTgWILNILGSLLESWTLGAcTFVHLLPKFDPLVILKTLSSYPIKSMMG 310
Cdd:PRK06018 197 YSHRSNVLHALManNGDALGTSAADTMLPVVPL-FHANSWGIAFSAPSMGT-KLVMPGAKLDGASVYELLDTEKVTFTAG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 311 APIVYRMLLQQ-DLSSYKFPHLQNCLAGGeSLLPETLENWRAQTGLDIREFYGQTETGLTCMVSK--------------T 375
Cdd:PRK06018 275 VPTVWLMLLQYmEKEGLKLPHLKMVVCGG-SAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAAlkppfsklpgdarlD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 376 MKIKPGYmgtAASCYDVQVIDDKGNVLPpgTEGDIGIRVKpIRPIGIFSGYVenpdKTAANIRGD--FWLLGDRGIKDED 453
Cdd:PRK06018 354 VLQKQGY---PPFGVEMKITDDAGKELP--WDGKTFGRLK-VRGPAVAAAYY----RVDGEILDDdgFFDTGDVATIDAY 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 454 GYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflshdpEQLTK-ELQQHVK 532
Cdd:PRK06018 424 GYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG------ETATReEILKYMD 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 157311624 533 SVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD--KEWKMSGKA 574
Cdd:PRK06018 498 GKIAKWWMPDDVAFVDAIPHTATGKILKTALREqfKDYKLPTAA 541
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
76-560 |
2.07e-23 |
|
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: 103.29 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 76 GKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAK 155
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 156 AIVAGDEviqevDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSGTSGLPKMAEHSY 235
Cdd:cd05914 82 AIFVSDE-----DDVA---------------------------------------------LINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 SSLglKAKMDAG--WTGLQASDIMWTISDTGWILNILGSLLESWTLGActFVHLLPKFDPLVILKtLSSYPIKSMMGAPI 313
Cdd:cd05914 112 RNI--VSNVDGVkeVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGA--HVVFLDKIPSAKIIA-LAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 314 VYRM--------LLQQDLSSYKFP------------------------HLQNCLAGGESLLPETLENWRaQTGLDIREFY 361
Cdd:cd05914 187 PLVIekifkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLR-TIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 362 GQTETGLTCMVSKTMKIKPGYMGTAASCYDVQvIDDKGnvlPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDF 441
Cdd:cd05914 266 GMTETAPIISYSPPNRIRLGSAGKVIDGVEVR-IDSPD---PATGEGEIIVRGP-----NVMKGYYKNPEATAEAFDKDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 442 WL-LGDRGIKDEDGYFQFMGRADD-IINSSGYRIGPSEVENALMKHPAVVETAVIsspdpVRGEVVKAFVILASQFL--- 516
Cdd:cd05914 337 WFhTGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFLdvk 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 157311624 517 ----SHDPEQLTKELQQHVKSVTAPYKYPRKIEFVL-NLPKTVTGKIQR 560
Cdd:cd05914 412 alkqRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVKeEFEKTPKGKIKR 460
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
81-563 |
3.48e-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: 102.73 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd12114 13 LTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEViqevdtvASECPSLRIKLLVSEKSCDGWLNFKKllneastthhcVETGSQEASAIYFTSGTSGLPK--MAEHSySSL 238
Cdd:cd12114 92 GPD-------AQLDVAVFDVLILDLDALAAPAPPPP-----------VDVAPDDLAYVIFTSGSTGTPKgvMISHR-AAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 239 GLKAKMDAGWtGLQASDIMWTISDTGW---ILNILGSLleswTLGAcTFVhlLP----KFDPLVILKTLSSYPIKSMMGA 311
Cdd:cd12114 153 NTILDINRRF-AVGPDDRVLALSSLSFdlsVYDIFGAL----SAGA-TLV--LPdearRRDPAHWAELIERHGVTLWNSV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 312 PIVYRMLL------QQDLssykfPHLQNCLAGGESL---LPETLenWRAQTGLDIREFYGQTETGLTCMVSKTMKIKP-- 380
Cdd:cd12114 225 PALLEMLLdvleaaQALL-----PSLRLVLLSGDWIpldLPARL--RALAPDARLISLGGATEASIWSIYHPIDEVPPdw 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 381 -----GYMGTAASCYdvqVIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTAA-----NIRGDFWLLGDRGIK 450
Cdd:cd12114 298 rsipyGRPLANQRYR---VLDPRGRDCPDWVPGELWIG-----GRGVALGYLGDPELTAArfvthPDGERLYRTGDLGRY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 451 DEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPvRGEVVKAFVILASQFLSHDPEQLTKELQQH 530
Cdd:cd12114 370 RPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQT 448
|
490 500 510
....*....|....*....|....*....|...
gi 157311624 531 VKSvtapYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd12114 449 LPA----YMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
81-565 |
5.73e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 102.86 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILsGACGLQRGDRVAVML---PRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyRLQMSKAKAI 157
Cdd:PRK07008 40 YTYRDCERRAKQLAQAL-AALGVEPGDRVGTLAwngYRHLEAYYGVSGSGAVCHTINP------------RLFPEQIAYI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 V--AGDEVI-------QEVDTVASECPSLRIKLLVSEKS---CDG--WLNFKKLLNEASTTHHCVETGSQEASAIYFTSG 223
Cdd:PRK07008 107 VnhAEDRYVlfdltflPLVDALAPQCPNVKGWVAMTDAAhlpAGStpLLCYETLVGAQDGDYDWPRFDENQASSLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 224 TSGLPKMAEHSYSSLGLKAKM----DAgwTGLQASDI------MWTISDTGwilnilgsLLESWTLGACTFVHLLPKFDP 293
Cdd:PRK07008 187 TTGNPKGALYSHRSTVLHAYGaalpDA--MGLSARDAvlpvvpMFHVNAWG--------LPYSAPLTGAKLVLPGPDLDG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 294 LVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTET---GLT 369
Cdd:PRK07008 257 KSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMsplGTL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 370 C-MVSKTMKIKPG-------YMGTAASCYDVQVIDDKGNVLP--PGTEGDIGIRvkpirpiG--IFSGYVenpdKTAANI 437
Cdd:PRK07008 337 CkLKWKHSQLPLDeqrklleKQGRVIYGVDMKIVGDDGRELPwdGKAFGDLQVR-------GpwVIDRYF----RGDASP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 438 RGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGE-----VVKafvil 511
Cdd:PRK07008 406 LVDGWFpTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDErpllvVVK----- 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 157311624 512 asqflsHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK07008 481 ------RPGAEVTReELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
83-563 |
7.10e-22 |
|
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: 99.29 E-value: 7.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEW---W--LVILGCIRAgliFMPGTIQMKStdILYRLQMSKAKAI 157
Cdd:cd05938 8 YRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWlgLAKLGCPVA---FLNTNIRSKS--LLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 VAGDEVIQEVDTVaseCPSLR-----IKLLVSEKSCDGWLNFKKLLNEASTT-----HHCVETGSQEASAIYfTSGTSGL 227
Cdd:cd05938 83 VVAPELQEAVEEV---LPALRadgvsVWYLSHTSNTEGVISLLDKVDAASDEpvpasLRAHVTIKSPALYIY-TSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 228 PKMAEHSYsslgLKAKMDAGWT---GLQASDIMWTI----SDTGWILNILGSLleswTLGAcTFVhLLPKFDPLVILKTL 300
Cdd:cd05938 159 PKAARISH----LRVLQCSGFLslcGVTADDVIYITlplyHSSGFLLGIGGCI----ELGA-TCV-LKPKFSASQFWDDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 301 SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNcLAGGESLLPETLENWRAQTG-LDIREFYGQTEtGLTCMVSKTMKIk 379
Cdd:cd05938 229 RKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVR-LAIGNGLRADVWREFLRRFGpIRIREFYGSTE-GNIGFFNYTGKI- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 380 pGYMGTaASC------------YDVQ----VIDDKGNVLPPGTeGDIGIRVKPIRPIGIFSGYVENP----DKTAANI-- 437
Cdd:cd05938 306 -GAVGR-VSYlykllfpfelikFDVEkeepVRDAQGFCIPVAK-GEPGLLVAKITQQSPFLGYAGDKeqteKKLLRDVfk 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 438 RGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDP-VRGEVVKAFVILAsqf 515
Cdd:cd05938 383 KGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKLK--- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 157311624 516 lshDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd05938 460 ---PGHEFDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
82-563 |
1.61e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 98.14 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK13383 62 SYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 EVIQEV----DTVASECPSlrikllvsekscdgwlnfkkllneastTHHCVETGSQEASA-----IYFTSGTSGLPKmae 232
Cdd:PRK13383 141 EFAERIagadDAVAVIDPA---------------------------TAGAEESGGRPAVAapgriVLLTSGTTGKPK--- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 233 hsysSLGLKAKMDAGwTGLQASDIMWTISDTGWILNI---------LGSLLESWTLGACTFVHllPKFDPLVILKTLSSY 303
Cdd:PRK13383 191 ----GVPRAPQLRSA-VGVWVTILDRTRLRTGSRISVampmfhglgLGMLMLTIALGGTVLTH--RHFDAEAALAQASLH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 304 PIKSMMGAPIVYRMLLQ---QDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVSKT-MKIK 379
Cdd:PRK13383 264 RADAFTAVPVVLARILElppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPAdLRDA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 380 PGYMGTAASCYDVQVIDDKGNVLPPGTEGDIgirvkpirpigiFSGYVENPDKTA-----ANIRGdFWLLGDRGIKDEDG 454
Cdd:PRK13383 344 PETVGKPVAGCPVRILDRNNRPVGPRVTGRI------------FVGGELAGTRYTdgggkAVVDG-MTSTGDMGYLDNAG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 455 YFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQfLSHDPEQltkeLQQHVKSV 534
Cdd:PRK13383 411 RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ----LRDYLKDR 485
|
490 500
....*....|....*....|....*....
gi 157311624 535 TAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:PRK13383 486 VSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-563 |
1.75e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.65 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 2 HWLRKVQGLCTLWGTQMSSRTLyINSRQLVSLQWGHQEVPAKFNFASDVLDHWadmEKAGKRLP-SPALwwVNGkgkELM 80
Cdd:PRK12316 466 HWQNLLRGMVENPQARVDELPM-LDAEERGQLVEGWNATAAEYPLQRGVHRLF---EEQVERTPeAPAL--AFG---EET 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA- 159
Cdd:PRK12316 537 LDYAELNRRANRLAHALI-ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSq 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 160 ---GDE--VIQEVDTVASECPSLrikllvsekscdgWLNFKKllNEASTTHHCVEtgsQEASAIYfTSGTSGLPKMAEHS 234
Cdd:PRK12316 616 shlGRKlpLAAGVQVLDLDRPAA-------------WLEGYS--EENPGTELNPE---NLAYVIY-TSGSTGKPKGAGNR 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 235 YSSLGLKA-------KMDAGWTGLQASDIMWTISDtgWILnilgslleSWTLGACTFVHLLPK---FDPLVILKTLSSYP 304
Cdd:PRK12316 677 HRALSNRLcwmqqayGLGVGDTVLQKTPFSFDVSV--WEF--------FWPLMSGARLVVAAPgdhRDPAKLVELINREG 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 305 IKSMMGAPIVYRMLLQ----QDLSSykfphLQNCLAGGESL---LPETLENWRAQTGLdiREFYGQTETGL-----TCMV 372
Cdd:PRK12316 747 VDTLHFVPSMLQAFLQdedvASCTS-----LRRIVCSGEALpadAQEQVFAKLPQAGL--YNLYGPTEAAIdvthwTCVE 819
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 373 SKTMKIKPGYMGTAASCYdvqVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTA----ANIRGD---FWLLG 445
Cdd:PRK12316 820 EGGDSVPIGRPIANLACY---ILDANLEPVPVGVLGELYLAGR-----GLARGYHGRPGLTAerfvPSPFVAgerMYRTG 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 446 DRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISspdpVRGEVVKAFVILasqflsHDPEQLTK 525
Cdd:PRK12316 892 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL------ESEGGDWR 961
|
570 580 590
....*....|....*....|....*....|....*....
gi 157311624 526 E-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:PRK12316 962 EaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
81-563 |
1.95e-21 |
|
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: 97.54 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKaivag 160
Cdd:cd17656 14 LTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVR----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 deviqevdtvasecpslrikLLVSEKSCDGWLNFKK--------LLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--M 230
Cdd:cd17656 88 --------------------VVLTQRHLKSKLSFNKstilledpSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKgvQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 231 AEHSySSLGL------KAKMDAGWTGLQASDIMWTISdtgwILNILGSLLESWTLgactfvHLLPK-----FDPLVILkt 299
Cdd:cd17656 148 LEHK-NMVNLlhfereKTNINFSDKVLQFATCSFDVC----YQEIFSTLLSGGTL------YIIREetkrdVEQLFDL-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 300 LSSYPIKSMMGAPIVYRMLLQQDLSSYKFPH-LQNCLAGGESL-LPETLENWRAQTGLDIREFYGQTETGL--TCMVSKT 375
Cdd:cd17656 215 VKRHNIEVVFLPVAFLKFIFSEREFINRFPTcVKHIITAGEQLvITNEFKEMLHEHNVHLHNHYGPSETHVvtTYTINPE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 376 MKIkPGY--MGTAASCYDVQVIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVENPDKTA---------ANIRgdFWLL 444
Cdd:cd17656 295 AEI-PELppIGKPISNTWIYILDQEQQLQPQGIVGEL-----YISGASVARGYLNRQELTAekffpdpfdPNER--MYRT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 445 GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIlasqflshdPEQL- 523
Cdd:cd17656 367 GDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---------MEQEl 437
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 157311624 524 -TKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17656 438 nISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
83-563 |
3.48e-21 |
|
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: 96.62 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagde 162
Cdd:cd12115 27 YAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP-------LDPAY--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 163 viqevdtvasecPSLRIKLLVSEKSCdgwlnfkkllneastthHCVETGSQEASAIYFTSGTSGLPK--MAEHSysslGL 240
Cdd:cd12115 84 ------------PPERLRFILEDAQA-----------------RLVLTDPDDLAYVIYTSGSTGRPKgvAIEHR----NA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAKMDagWTG-----------LQASDIMWTISdtgwILNILGSLleswTLGACtfVHLLpkfDPLVILKTLSSYPIKSMM 309
Cdd:cd12115 131 AAFLQ--WAAaafsaeelagvLASTSICFDLS----VFELFGPL----ATGGK--VVLA---DNVLALPDLPAAAEVTLI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 310 GA-PIVYRMLLQQDlssyKFPhlQN----CLAGgESLLPETLENWRAQTGLD-IREFYGQTET---GLTCMVSKTMKIKP 380
Cdd:cd12115 196 NTvPSAAAELLRHD----ALP--ASvrvvNLAG-EPLPRDLVQRLYARLQVErVVNLYGPSEDttySTVAPVPPGASGEV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 381 GyMGTAASCYDVQVIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVENPDKTAANIRGD-------FWLLGDRGIKDED 453
Cdd:cd12115 269 S-IGRPLANTQAYVLDRALQPVPLGVPGEL-----YIGGAGVARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 454 GYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVIlasqfLSHDPEQLTKELQQHVKS 533
Cdd:cd12115 343 GLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV-----AEPGAAGLVEDLRRHLGT 417
|
490 500 510
....*....|....*....|....*....|
gi 157311624 534 VTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd12115 418 RLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
91-565 |
1.41e-20 |
|
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: 95.43 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 91 QQAANILSG--ACGLQRGDRVAVMLPR----VPEWWlvilGCIRAGLIFMPGTIQMKSTDI------LYRL-QMSKAKAI 157
Cdd:cd05906 47 EDARRLAAGlrQLGLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPTYDEPnarlrkLRHIwQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 VAGDEVIQEVDTVASECPSLRIKLLVSEkscdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 237
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIE-----------ELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 238 LgLKAKMDAGWT-GLQASDImwTISdtgWI-LNILGSLLESWTLG---ACTFVHLLPKF---DPLVILKTLSSYPIkSMM 309
Cdd:cd05906 192 I-LARSAGKIQHnGLTPQDV--FLN---WVpLDHVGGLVELHLRAvylGCQQVHVPTEEilaDPLRWLDLIDRYRV-TIT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 310 GAP-IVYRMLLQQ---------DLSSYKFphlqnCLAGGESLLPETLENWR---AQTGLD---IREFYGQTETGLTCMVS 373
Cdd:cd05906 265 WAPnFAFALLNDLleeiedgtwDLSSLRY-----LVNAGEAVVAKTIRRLLrllEPYGLPpdaIRPAFGMTETCSGVIYS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 374 KTMkikPGYMGTAA-------SCY---DVQVIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVENPDKTAANIRGDFWL 443
Cdd:cd05906 340 RSF---PTYDHSQAlefvslgRPIpgvSMRIVDDEGQLLPEGEVGRLQVRGPVV-----TKGYYNNPEANAEAFTEDGWF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 444 -LGDRGIKDeDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVE--TAVISSPDPVRGEVVKAFVILASQFLSHDP 520
Cdd:cd05906 412 rTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIFFVPEYDLQDAL 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 157311624 521 EQLTKELQQHVK---SVTAPYKYP-RKIEFvlnlPKTVTGKIQRTKLRD 565
Cdd:cd05906 491 SETLRAIRSVVSrevGVSPAYLIPlPKEEI----PKTSLGKIQRSKLKA 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-563 |
2.20e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.18 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 2 HWLRKVQGLC-TLWGTQMSSRTLYINSRQLVSLQWGHQEVPakfnFASDVLDHWADMEKAGKRLPSPALWWvngkGKELM 80
Cdd:PRK12316 1958 HLLHLLEQMAeDAQAALGELALLDAGERQRILADWDRTPEA----YPRGPGVHQRIAEQAARAPEAIAVVF----GDQHL 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 wNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAkAIVAG 160
Cdd:PRK12316 2030 -SYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGA-ALLLT 2106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 DEVIQEVDTVASECPSLRIkllvsekSCDGWLNfkkllnEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-- 238
Cdd:PRK12316 2107 QRHLLERLPLPAGVARLPL-------DRDAEWA------DYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALva 2173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 239 -----GLKAKMDAGWTGLQASDIMWTISDTGWilnilgslLESWTLGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPI 313
Cdd:PRK12316 2174 hcqaaGERYELSPADCELQFMSFSFDGAHEQW--------FHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPV 2245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 314 VYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLEN-WRAQTGLDIREFYGQTETGLTCMVSKTMKIKPG---YM--GTAA 387
Cdd:PRK12316 2246 YLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgaaYVpiGRAL 2325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 388 SCYDVQVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTA--------ANIRGDFWLLGDRGIKDEDGYFQFM 459
Cdd:PRK12316 2326 GNRRAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYL 2400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 460 GRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSpDPVRGEVVKAFVIlasqflSHDP-EQLTKELQQHVKSVTAPY 538
Cdd:PRK12316 2401 GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV------PDDAaEDLLAELRAWLAARLPAY 2473
|
570 580
....*....|....*....|....*
gi 157311624 539 KYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:PRK12316 2474 MVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
218-568 |
7.08e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 93.17 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 218 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASD-------------IMwtisdTGWILnILGSlleswtlGACtf 284
Cdd:PRK13388 155 LIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDvcyvsmplfhsnaVM-----AGWAP-AVAS-------GAA-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 285 VHLLPKFDPLVILKTLSSYPIKSM--MGAPIVYRMLlqqdlSSYKFPHLQNCL--AGGESLLPETLENWRAQTGLDIREF 360
Cdd:PRK13388 220 VALPAKFSASGFLDDVRRYGATYFnyVGKPLAYILA-----TPERPDDADNPLrvAFGNEASPRDIAEFSRRFGCQVEDG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 361 YGQTETGltCMVSKTMKIKPGYMGTAA---SCYD--------VQVIDDKGNVLPPgtEGDIGIRVKpIRPIGIFSGYVEN 429
Cdd:PRK13388 295 YGSSEGA--VIVVREPGTPPGSIGRGApgvAIYNpetltecaVARFDAHGALLNA--DEAIGELVN-TAGAGFFEGYYNN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 430 PDKTAANIR-GDFWLlGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAF 508
Cdd:PRK13388 370 PEATAERMRhGMYWS-GDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAA 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 509 VILAsQFLSHDPEQLTKELqqHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEW 568
Cdd:PRK13388 449 LVLR-DGATFDPDAFAAFL--AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGW 505
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
124-563 |
8.20e-20 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 92.65 E-value: 8.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 124 LGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgdevIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEAST 203
Cdd:PRK04813 70 LGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIA----TEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 204 THhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLglkakmdagwtglqasdimwtISDTGWILNILG------------ 271
Cdd:PRK04813 146 YY------------IIFTSGTTGKPKGVQISHDNL---------------------VSFTNWMLEDFAlpegpqflnqap 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 272 --------SLLESWTLGAcTFVhLLPK---FDPLVILKTLSSYPIKSMMGAPIVYRM-LLQQDLSSYKFPHLQNCLAGGE 339
Cdd:PRK04813 193 ysfdlsvmDLYPTLASGG-TLV-ALPKdmtANFKQLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 340 SLLPETlenwrAQTGLD------IREFYGQTETglTCMVSK---TMKIKPGY----MGTAASCYDVQVIDDKGNVLPPGT 406
Cdd:PRK04813 271 ELPHKT-----AKKLLErfpsatIYNTYGPTEA--TVAVTSieiTDEMLDQYkrlpIGYAKPDSPLLIIDEEGTKLPDGE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 407 EGDIGIrvkpirpIG--IFSGYVENPDKTAANirgdFWLL--------GDRGIKDeDGYFQFMGRADDIINSSGYRIGPS 476
Cdd:PRK04813 344 QGEIVI-------SGpsVSKGYLNNPEKTAEA----FFTFdgqpayhtGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 477 EVENALMKHPAVVETAVIsspdPV-RGEVVK---AFVILASqflsHDPE---QLTKELQQHVKSVTAPYKYPRKIEFVLN 549
Cdd:PRK04813 412 EIEQNLRQSSYVESAVVV----PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRDS 483
|
490
....*....|....
gi 157311624 550 LPKTVTGKIQRTKL 563
Cdd:PRK04813 484 LPLTPNGKIDRKAL 497
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
208-563 |
1.20e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 208 VETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILgSLLESWTLGACTFVHL 287
Cdd:PRK12316 3191 IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVE-ELFWPLMSGARVVLAG 3269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 288 LPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPHLQNCLAGGESLLPETLENWRAqtGLDIREFYGQTET 366
Cdd:PRK12316 3270 PEDWrDPALLVELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEA 3346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 367 GLTCMVSKTMKIKPGY--MGTAASCYDVQVIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVENPDKTAANIRGDFWLL 444
Cdd:PRK12316 3347 TITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGEL-----YLGGEGLARGYHNRPGLTAERFVPDPFVP 3421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 445 GDRGIKD-------EDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISspdpVRGEVVKAFVILASQfls 517
Cdd:PRK12316 3422 GERLYRTgdlaryrADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE--- 3494
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 157311624 518 hdPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:PRK12316 3495 --AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
81-564 |
2.03e-19 |
|
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: 91.33 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 160
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 161 dEVIQEVDTVASECPslrikllvseKSCDGwLNFKKLLneastthhcvetgsqeaSAIYfTSGTSGLPKMAEHSYSSLgL 240
Cdd:cd05939 82 -NLLDPLLTQSSTEP----------PSQDD-VNFRDKL-----------------FYIY-TSGTTGLPKAAVIVHSRY-Y 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 241 KAKMDAGWT-GLQASDIMWT----ISDTGWILNIlGSLLeswtLGACTFVhLLPKFDPLVILKTLSSY--PIKSMMGApi 313
Cdd:cd05939 131 RIAAGAYYAfGMRPEDVVYDclplYHSAGGIMGV-GQAL----LHGSTVV-IRKKFSASNFWDDCVKYncTIVQYIGE-- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 314 VYRMLLQQDLSSYKFPHlQNCLAGGESLLPETLENWRAQTGL-DIREFYGQTEtGLTCMVSKTMKIKP-GYMG-TAASCY 390
Cdd:cd05939 203 ICRYLLAQPPSEEEQKH-NVRLAVGNGLRPQIWEQFVRRFGIpQIGEFYGATE-GNSSLVNIDNHVGAcGFNSrILPSVY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 391 DVQVI-----------DDKGNVLP--PGTEGDIGIRVKPIRPIGIFSGYV---ENPDKTAANI--RGD-FWLLGDRGIKD 451
Cdd:cd05939 281 PIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVnegATNKKIARDVfkKGDsAFLSGDVLVMD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 452 EDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDP-VRGEVVKAFVilASQFLSHDPEQLTKELQqh 530
Cdd:cd05939 361 ELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAGMAAI--VDPERKVDLDRFSAVLA-- 436
|
490 500 510
....*....|....*....|....*....|....
gi 157311624 531 vkSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd05939 437 --KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
81-568 |
5.95e-19 |
|
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: 89.80 E-value: 5.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIfmPGTIQ--MKSTDILYRLQMSKAKAIV 158
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--PAFINynLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 159 AGDEViqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqEASAIYfTSGTSGLPKMAEHSYSSL 238
Cdd:cd05937 84 VDPDD--------------------------------------------------PAILIY-TSGTTGLPKAAAISWRRT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 239 GLKAKMDAGWTGLQASDIMWT----ISDTGWILNILGSLLESWTLGactfvhLLPKFDplviLKTLSSYPIKSmmGAP-I 313
Cdd:cd05937 113 LVTSNLLSHDLNLKNGDRTYTcmplYHGTAAFLGACNCLMSGGTLA------LSRKFS----ASQFWKDVRDS--GATiI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 314 VY-----RMLLQQDLSSYKFPHlqNC-LAGGESLLPETLENWRAQTGL-DIREFYGQTETgltcmVSKTMKIKPGYMGTA 386
Cdd:cd05937 181 QYvgelcRYLLSTPPSPYDRDH--KVrVAWGNGLRPDIWERFRERFNVpEIGEFYAATEG-----VFALTNHNVGDFGAG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 387 ASCY----------DVQVI------------DDKGN---VLPPGTEGDIGIRVkPIRPIGIFSGYVENPDKTAANI---- 437
Cdd:cd05937 254 AIGHhglirrwkfeNQVVLvkmdpetddpirDPKTGfcvRAPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKLvrdv 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 438 --RGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDP-VRGEVVKAFVILAS 513
Cdd:cd05937 333 frKGDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEE 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 157311624 514 QflSHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEW 568
Cdd:cd05937 413 S--SAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
100-563 |
6.21e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 90.07 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 100 ACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV---IQEVDTVASECPS 176
Cdd:PRK05857 60 AQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSkmaSSAVPEALHSIPV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 177 LRIKLL--VSEKSCDGWLNFKKLLneastthhcVETGSQEASAIYFTSGTSGLPK---MAEHSYSSLG--LKAK------ 243
Cdd:PRK05857 140 IAVDIAavTRESEHSLDAASLAGN---------ADQGSEDPLAMIFTSGTTGEPKavlLANRTFFAVPdiLQKEglnwvt 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 244 ---MDAGWTGLQASDI--MWtisdtgWILNILGSLLESWTLGACTfvhllpkfdpLVILKTLSSYPIKSMMGAP-IVYRM 317
Cdd:PRK05857 211 wvvGETTYSPLPATHIggLW------WILTCLMHGGLCVTGGENT----------TSLLEILTTNAVATTCLVPtLLSKL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 318 LLQQDLSSYKFPHLQNCLAGGESLLPETLENWRAqTGLDIREFYGQTETGLTCMVSKT-----MKIKPGYMGTAASCYDV 392
Cdd:PRK05857 275 VSELKSANATVPSLRLVGYGGSRAIAADVRFIEA-TGVRTAQVYGLSETGCTALCLPTddgsiVKIEAGAVGRPYPGVDV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 393 QVID-DKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVENPDKTAaNIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSG 470
Cdd:PRK05857 354 YLAAtDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTA-EVLIDGWVnTGDLLERREDGFFYIKGRSSEMIICGG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 471 YRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNL 550
Cdd:PRK05857 433 VNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDI 512
|
490
....*....|...
gi 157311624 551 PKTVTGKIQRTKL 563
Cdd:PRK05857 513 PRTQSGKVMRASL 525
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
48-493 |
8.40e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 89.93 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 48 SDVLDHWADmeKAGKRlpsPALwwvNGKGKELmwNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCI 127
Cdd:PRK08279 40 GDVFEEAAA--RHPDR---PAL---LFEDQSI--SYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 128 RAGLIF-MPGTIQMKstDIL-YRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCD---GWLNFKKLLNEAS 202
Cdd:PRK08279 109 KLGAVVaLLNTQQRG--AVLaHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDdpeGYEDLAAAAAGAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 203 TTHHCVETGSQ-EASAIY-FTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTI----SDTGwiLNI-LGSLLe 275
Cdd:PRK08279 187 TTNPASRSGVTaKDTAFYiYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCClplyHNTG--GTVaWSSVL- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 276 swtLGACTFVhLLPKFD-----PLVILK--TLssypiksmmgapIVY-----RMLLQQDLSSYKFPHLQNCLAG-GesLL 342
Cdd:PRK08279 264 ---AAGATLA-LRRKFSasrfwDDVRRYraTA------------FQYigelcRYLLNQPPKPTDRDHRLRLMIGnG--LR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 343 PETLENWRAQTGLD-IREFYGQTE--TGLTCM--VSKTMKIKPGYMGTAASC--YDVQ----VIDDKGNVLPPGTeGDIG 411
Cdd:PRK08279 326 PDIWDEFQQRFGIPrILEFYAASEgnVGFINVfnFDGTVGRVPLWLAHPYAIvkYDVDtgepVRDADGRCIKVKP-GEVG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 412 IRVKPIRPIGIFSGYVeNPDKTAANI------RGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMK 484
Cdd:PRK08279 405 LLIGRITDRGPFDGYT-DPEASEKKIlrdvfkKGDAWFnTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSG 483
|
....*....
gi 157311624 485 HPAVVETAV 493
Cdd:PRK08279 484 FPGVEEAVV 492
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
83-563 |
1.98e-18 |
|
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: 88.23 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGACGLQRGDRVAVMLPRvPEWWLV-ILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagd 161
Cdd:cd17648 15 YRELNERANRLAHYLLSVAEIRPDDLVGLVLDK-SELMIIaILAVWKAGAAYVP-------IDPSY-------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 eviqevdtvasecPSLRIKLLVSEkscdgwlnfkkllneasTTHHCVETGSQEASAIYFTSGTSGLPK--MAEHSySSLG 239
Cdd:cd17648 73 -------------PDERIQFILED-----------------TGARVVITNSTDLAYAIYTSGTTGKPKgvLVEHG-SVVN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 240 LKAKMDAGWtGLQASDIMWTISDTGWILN-----ILGSLLESWTLgactfvhLLP----KFDPLVILKTLSSYPIKSMMG 310
Cdd:cd17648 122 LRTSLSERY-FGRDNGDEAVLFFSNYVFDffveqMTLALLNGQKL-------VVPpdemRFDPDRFYAYINREKVTYLSG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 311 APIVyrmlLQQ-DLSSykFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVS-------KTMKIKPGY 382
Cdd:cd17648 194 TPSV----LQQyDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRffpgdqrFDKSLGRPV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 383 MGTAasCYdvqVIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVENPDKTA----AN--------IRGDFWLL---GDR 447
Cdd:cd17648 268 RNTK--CY---VLNDAMKRVPVGAVGEL-----YLGGDGVARGYLNRPELTAerflPNpfqteqerARGRNARLyktGDL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 448 GIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqFLSHDPEQLTK-E 526
Cdd:cd17648 338 VRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQKYLVG--YYLPEPGHVPEsD 415
|
490 500 510
....*....|....*....|....*....|....*..
gi 157311624 527 LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17648 416 LLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
207-565 |
8.41e-18 |
|
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: 86.23 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 207 CVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-----GLKAKMDAgwtglQASDIMwtisdtgwiLNIL---------GS 272
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLlanveQITAIFDP-----NPEDVV---------FGALpffhsfgltGC 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 273 LLESWTLGACTFVHllpkFDPL---VILKTLSSYPIKSMMGAPIVYRMLLQQdLSSYKFPHLQNCLAGGESLLPETLENW 349
Cdd:cd05909 207 LWLPLLSGIKVVFH----PNPLdykKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEF 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 350 RAQTGLDIREFYGQTETGLTCMVSK-TMKIKPGYMGTAASCYDVQVIDDKGNV-LPPGTEGDIGIRvkpirpiG--IFSG 425
Cdd:cd05909 282 QEKFGIRILEGYGTTECSPVISVNTpQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVR-------GpnVMLG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 426 YVENPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKH-PAVVETAVISSPDPVRGEV 504
Cdd:cd05909 355 YLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157311624 505 VKAFvilasqflsHDPEQLTK-ELQQHVKSVTAPYKY-PRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:cd05909 435 IVLL---------TTTTDTDPsSLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
77-563 |
1.63e-17 |
|
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: 85.21 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 77 KELMWNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKA 156
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 157 IVagdevIQEVDTvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeASAIYfTSGTSGLPK--MAEHS 234
Cdd:cd17650 88 LL-----TQPEDL---------------------------------------------AYVIY-TSGTTGKPKgvMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 235 YSslglkAKMDAGW-----------TGLQASDIMWTISdTGwilNILGSLLESWTLGACTFVhllPKFDPLVILKTLSSY 303
Cdd:cd17650 117 NV-----AHAAHAWrreyeldsfpvRLLQMASFSFDVF-AG---DFARSLLNGGTLVICPDE---VKLDPAALYDLILKS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 304 PIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIR--EFYGQTETgltCMVSKTMKIKP 380
Cdd:cd17650 185 RITLMESTPALIRPVMAYvYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRiiNSYGVTEA---TIDSTYYEEGR 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 381 GYMGTAASC--------YDVQVIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGD-------FWLLG 445
Cdd:cd17650 262 DPLGDSANVpigrplpnTAMYVLDERLQPQPVGVAGELYIGGA-----GVARGYLNRPELTAERFVENpfapgerMYRTG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 446 DRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPvRGEVVKAFVILASQFLShdpeqlTK 525
Cdd:cd17650 337 DLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARLCAYVVAAATLN------TA 409
|
490 500 510
....*....|....*....|....*....|....*...
gi 157311624 526 ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17650 410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
215-563 |
2.52e-17 |
|
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: 84.79 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 215 ASAIYfTSGTSGLPK--MAEHSY---SSLGLKAKMDAGWTG--LQASDIMWTISdtgwILNILGSLLESWTLgactfvHL 287
Cdd:cd17644 109 AYVIY-TSGSTGKPKgvMIEHQSlvnLSHGLIKEYGITSSDrvLQFASIAFDVA----AEEIYVTLLSGATL------VL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 288 LPK---FDPLVILKTLSSYPIkSMMGAPIVYRMLLQQDLSSYKFP---HLQNCLAGGESLLPETLENWRAQTGLDIR--E 359
Cdd:cd17644 178 RPEemrSSLEDFVQYIQQWQL-TVLSLPPAYWHLLVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKNVGNFIQliN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 360 FYGQTETGLTCMVS-----KTMKIKPGYMGTAASCYDVQVIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVENPDKTA 434
Cdd:cd17644 257 VYGPTEATIAATVCrltqlTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGEL-----HIGGVGLARGYLNRPELTA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 435 ANIRGD---------FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVV 505
Cdd:cd17644 332 EKFISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRL 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 157311624 506 KAFVIlasqflSHDPEQ-LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17644 412 VAYIV------PHYEESpSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
335-565 |
3.14e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 84.28 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 335 LAGGESLLPETLENWRaQTGLDIREFYGQTETGltcmvSKTMKIKPG-YMGTAASCydvqviddkGNVLPPGTegdIGIR 413
Cdd:PRK07445 236 LLGGAPAWPSLLEQAR-QLQLRLAPTYGMTETA-----SQIATLKPDdFLAGNNSS---------GQVLPHAQ---ITIP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 414 VKPIRPIGI-----FSGYVenPDKTAANIrgdFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAV 488
Cdd:PRK07445 298 ANQTGNITIqaqslALGYY--PQILDSQG---IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLV 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157311624 489 VETAVISSPDPVRGEVVKAFVILAsqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK07445 373 QDVCVLGLPDPHWGEVVTAIYVPK------DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
82-532 |
5.35e-17 |
|
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: 83.95 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagd 161
Cdd:cd17640 7 TYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 162 eviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcVETGSQEASAIYFTSGTSGLPK--MAEHSysslG 239
Cdd:cd17640 83 ----------------------------------------------VENDSDDLATIIYTSGTTGNPKgvMLTHA----N 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 240 LKAKMDAGWTGLQAS--DIMWtisdtgwilnilgSLLESW---------TLGAC-------TFVHL---LPKFDPLVIL- 297
Cdd:cd17640 113 LLHQIRSLSDIVPPQpgDRFL-------------SILPIWhsyersaeyFIFACgcsqaytSIRTLkddLKRVKPHYIVs 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 298 -----KTLSSYPIKSMMGAPIVYRMLLQQDLS--SYKFPhlqncLAGGESLLPETLENWRAqTGLDIREFYGQTETGLTC 370
Cdd:cd17640 180 vprlwESLYSGIQKQVSKSSPIKQFLFLFFLSggIFKFG-----ISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 371 MVSKTMKIKPGYMGTAASCYDVQVIDDKGN-VLPPGTEGDIGIRVKPIrpigiFSGYVENPDKTAANIRGDFWL-LGDRG 448
Cdd:cd17640 254 SARRLKCNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVLDSDGWFnTGDLG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 449 IKDEDGYFQFMGRADD-IINSSGYRIGPSEVENALMKHPaVVETAVISSPD---------PVRGEVVKAFVILAsQFLSH 518
Cdd:cd17640 329 WLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSP-FIEQIMVVGQDqkrlgalivPNFEELEKWAKESG-VKLAN 406
|
490 500
....*....|....*....|
gi 157311624 519 DPEQL------TKELQQHVK 532
Cdd:cd17640 407 DRSQLlaskkvLKLYKNEIK 426
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
81-565 |
9.60e-17 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 83.44 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGACGlqRGDRVAVMLPRVPEWWLVILGCIRAGLI----FMPGtiqmkSTDILYRLQ----MS 152
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIavplPPPT-----PGRHAERLAailaDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 153 KAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKScdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 232
Cdd:cd05931 98 GPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDL---------LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 233 HSYSSLG--LKAkMDAGWtGLQASDIM--W--TISDTGWILNILGSLLeswtLGACtfVHLLPKFD----PLVILKTLSS 302
Cdd:cd05931 169 VTHRNLLanVRQ-IRRAY-GLDPGDVVvsWlpLYHDMGLIGGLLTPLY----SGGP--SVLMSPAAflrrPLRWLRLISR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 303 YPIkSMMGAP------IVYRMLLQQ----DLSSykfphLQNCLAGGESLLPETLENWR---AQTGLD---IREFYGQTET 366
Cdd:cd05931 241 YRA-TISAAPnfaydlCVRRVRDEDleglDLSS-----WRVALNGAEPVRPATLRRFAeafAPFGFRpeaFRPSYGLAEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 367 glTCMVSkTMKIKPGY-----------------------------MGTAASCYDVQVIDDKGN-VLPPGTEGDIGIRvkp 416
Cdd:cd05931 315 --TLFVS-GGPPGTGPvvlrvdrdalagravavaaddpaarelvsCGRPLPDQEVRIVDPETGrELPDGEVGEIWVR--- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 417 irpiG--IFSGYVENPDKTA------ANIRGDFWL-LGDRGIKDeDGYFQFMGRADDIINSSGYRIGPSEVENALMK-HP 486
Cdd:cd05931 389 ----GpsVASGYWGRPEATAetfgalAATDEGGWLrTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 487 AVVET--AVISSPDPVRGEVVkAFVILASQFLSHDPEQLTKELQQHVKS---VTapykyPRKIEFVLN--LPKTVTGKIQ 559
Cdd:cd05931 464 ALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA-----PADVVLVRPgsIPRTSSGKIQ 537
|
....*.
gi 157311624 560 RTKLRD 565
Cdd:cd05931 538 RRACRA 543
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
57-566 |
1.64e-16 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 83.20 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 57 MEKAGKRLPSPALWWVNGKGKELMWNF---RELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIF 133
Cdd:PLN03052 182 TPKPSKTDDSIAIIWRDEGSDDLPVNRmtlSELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 134 MPGTIQMKSTDILYRLQMSKAKA------IVAGDEVIQEVDTVASECPSLRIKLLVSEKSC-----DGWLNFKKLLNEAS 202
Cdd:PLN03052 261 VSIADSFAPSEIATRLKISKAKAiftqdvIVRGGKSIPLYSRVVEAKAPKAIVLPADGKSVrvklrEGDMSWDDFLARAN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 203 TTHHCVETGSQEASA-----IYFTSGTSGLPKMAEHSYSSlGLKAKMDAgWTGL--QASDIMWTISDTGWILN---ILGS 272
Cdd:PLN03052 341 GLRRPDEYKAVEQPVeaftnILFSSGTTGEPKAIPWTQLT-PLRAAADA-WAHLdiRKGDIVCWPTNLGWMMGpwlVYAS 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 273 LLESWTL----------GACTFVHllpkfDPLV-ILKTLSSypiksmmgapIVYRMLLQQDLSSYKFPHLQnCLA--GGE 339
Cdd:PLN03052 419 LLNGATLalyngsplgrGFAKFVQ-----DAKVtMLGTVPS----------IVKTWKNTNCMAGLDWSSIR-CFGstGEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 340 SLLPETLenW---RAQTGlDIREFYGQTETGlTCMVSKTMkIKP---GYMGTAASCYDVQVIDDKGNVLP---PGTeGDI 410
Cdd:PLN03052 483 SSVDDYL--WlmsRAGYK-PIIEYCGGTELG-GGFVTGSL-LQPqafAAFSTPAMGCKLFILDDSGNPYPddaPCT-GEL 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 411 GIRVKpirpigIF--SGYVENPDKTAANIRG-DFW---LL---GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENA 481
Cdd:PLN03052 557 ALFPL------MFgaSSTLLNADHYKVYFKGmPVFngkILrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERV 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 482 LMK-HPAVVETAVISSPDPVRG--EVVKAFVILASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 558
Cdd:PLN03052 631 CNAaDESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKV 710
|
....*...
gi 157311624 559 QRTKLRDK 566
Cdd:PLN03052 711 MRRVLRQQ 718
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
81-564 |
7.52e-16 |
|
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: 80.09 E-value: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIfmPGTI--QMKSTDILYRLQMSKAKAIV 158
Cdd:cd05940 4 LTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--AALInyNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 159 agdeviqeVDTvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIY-FTSGTSGLPKMAEHSYSS 237
Cdd:cd05940 81 --------VDA-----------------------------------------------ALYiYTSGTTGLPKAAIISHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 238 LGLKAKMDAGWTGLQASDIMWTI----SDTGWILNILGSLLESWTLgactfvhllpkfdplVILKTLSSY----PIKSMM 309
Cdd:cd05940 106 AWRGGAFFAGSGGALPSDVLYTClplyHSTALIVGWSACLASGATL---------------VIRKKFSASnfwdDIRKYQ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 310 GAPIVY-----RMLLQQDLSSYKFPHLQNClAGGESLLPETLENWRAQTGL-DIREFYGQTE--------TGLTCMVSKT 375
Cdd:cd05940 171 ATIFQYigelcRYLLNQPPKPTERKHKVRM-IFGNGLRPDIWEEFKERFGVpRIAEFYAATEgnsgfinfFGKPGAIGRN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 376 MKIKPGYMGTAASCYDV---QVIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVeNPDKTAANI------RGDFWLL-G 445
Cdd:cd05940 250 PSLLRKVAPLALVKYDLesgEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYT-DPAATEKKIlrdvfkKGDAWFNtG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 446 DRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDP-VRGEVVKAFVILASQflshDPEQLT 524
Cdd:cd05940 329 DLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPN----EEFDLS 404
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 157311624 525 KeLQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:cd05940 405 A-LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
68-569 |
3.06e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 76.36 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 68 ALWWVNGKgkelmWNFRELSENSQQAANILSGaCGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILY 147
Cdd:PRK05691 1149 ALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAY 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 148 RLQMSKAKAIVAGDEVIQEVDTVASECPslrikLLVSEKSCDGWLNFKKLLNeastTHhcvetGSQEASAIYfTSGTSGL 227
Cdd:PRK05691 1223 MLADSGVELLLTQSHLLERLPQAEGVSA-----IALDSLHLDSWPSQAPGLH----LH-----GDNLAYVIY-TSGSTGQ 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 228 PKMAEHSYSSLGLKAK-MDAGWtGLQASDIMWTISDTGWILnilgSLLES-WTL-GACTFVHLLP--KFDPLVILKTLSS 302
Cdd:PRK05691 1288 PKGVGNTHAALAERLQwMQATY-ALDDSDVLMQKAPISFDV----SVWECfWPLiTGCRLVLAGPgeHRDPQRIAELVQQ 1362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 303 YPIKSMMGAPIVYRMLLQQdlssykfPHLQNC------LAGGESLLPETLENWRAQ-TGLDIREFYGQTETGLT-----C 370
Cdd:PRK05691 1363 YGVTTLHFVPPLLQLFIDE-------PLAAACtslrrlFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAINvthwqC 1435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 371 MVSKTMKIKPGYMGTAASCydvQVIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTAANIRGD--------FW 442
Cdd:PRK05691 1436 QAEDGERSPIGRPLGNVLC---RVLDAELNLLPPGVAGELCIG-----GAGLARGYLGRPALTAERFVPDplgedgarLY 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 443 LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflshdpEQ 522
Cdd:PRK05691 1508 RTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQ------EA 1581
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 157311624 523 LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEWK 569
Cdd:PRK05691 1582 EAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ 1628
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
84-562 |
3.28e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 75.42 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 84 RELSENSQQAANILSGAcGLQRGDRVAV-------MLPRVPEWWLvilgciRAGLIFM-----PGT-IQMKSTDILYRLQ 150
Cdd:PRK07768 33 GEVHERARRIAGGLAAA-GVGPGDAVAVlagapveIAPTAQGLWM------RGASLTMlhqptPRTdLAVWAEDTLRVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 151 MSKAKAIVAGDEVIQEVDTVASEcpSLRIkLLVSEkscdgwlnfkkLLNEASTTHhcVETGsQEASAIY-FTSGTSGLPK 229
Cdd:PRK07768 106 MIGAKAVVVGEPFLAAAPVLEEK--GIRV-LTVAD-----------LLAADPIDP--VETG-EDDLALMqLTSGSTGSPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 230 MAEHSYSSLglKAKMDAGWTGLQA---SDIM--W--TISDTGWIlnilGSLLESWTLGaCTFVHLLP-KF--DPLVILKT 299
Cdd:PRK07768 169 AVQITHGNL--YANAEAMFVAAEFdveTDVMvsWlpLFHDMGMV----GFLTVPMYFG-AELVKVTPmDFlrDPLLWAEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 300 LSSYPiKSMMGAP-----IVYRMLLQQ------DLSSYKFphlqnCLAGGESLLPETLENWRAQT---GLD---IREFYG 362
Cdd:PRK07768 242 ISKYR-GTMTAAPnfayaLLARRLRRQakpgafDLSSLRF-----ALNGAEPIDPADVEDLLDAGarfGLRpeaILPAYG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 363 QTETGLTC-----------------MVSKTMKIKPGYMGTAASC---------YDVQVIDDKGNVLPPGTEGDIGIRVKP 416
Cdd:PRK07768 316 MAEATLAVsfspcgaglvvdevdadLLAALRRAVPATKGNTRRLatlgpplpgLEVRVVDEDGQVLPPRGVGVIELRGES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 417 IRPigifsGYVEnPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVIS 495
Cdd:PRK07768 396 VTP-----GYLT-MDGFIPAQDADGWLdTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157311624 496 SPDPvRGEVVKAFVILASQFLSHDPEQLTKELQQHVKSVTAPYKY-PRKIeFVL---NLPKTVTGKIQRTK 562
Cdd:PRK07768 470 VRLD-AGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVrPRNV-VVLgpgSIPKTPSGKLRRAN 538
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
446-564 |
4.87e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 73.93 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 446 DRGIKDeDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflsHDPEQLTK 525
Cdd:PRK07824 240 DLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGD-----GGPAPTLE 313
|
90 100 110
....*....|....*....|....*....|....*....
gi 157311624 526 ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
42-559 |
1.61e-13 |
|
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: 73.46 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 42 AKFNFASDVLDHwadmekagKRLPSPALWWVNGKGKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWL 121
Cdd:cd05943 68 ARLNYAENLLRH--------ADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALR-ALGVKPGDRVAGYLPNIPEAVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 122 VILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVI---------QEVDTVASECPSLRIKLLVSEKSCDGWL 192
Cdd:cd05943 139 AMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTyngkrhdvrEKVAELVKGLPSLLAVVVVPYTVAAGQP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 193 NFKKLLNeastTHHCVETGSQEASA--------------IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGW-TGLQASDIM 257
Cdd:cd05943 219 DLSKIAK----ALTLEDFLATGAAGelefeplpfdhplyILYSSGTTGLPKCIVHGAGGTLLQHLKEHILhCDLRPGDRL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 258 WTISDTGWIL-NILGSLLeswtLGACTFV-----HLLPkfDPLVILKTLSSYPIkSMMGAPIVYRMLLQQ---------D 322
Cdd:cd05943 295 FYYTTCGWMMwNWLVSGL----AVGATIVlydgsPFYP--DTNALWDLADEEGI-TVFGTSAKYLDALEKaglkpaethD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 323 LSSykfphLQNCLAGGESLLPETLE----NWRAqtGLDIREFYGQTETgLTCMVSkTMKIKPGYMGtAASC----YDVQV 394
Cdd:cd05943 368 LSS-----LRTILSTGSPLKPESFDyvydHIKP--DVLLASISGGTDI-ISCFVG-GNPLLPVYRG-EIQCrglgMAVEA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 395 IDDKGNVLPpGTEGDIGIrVKPI--RPIGiFSGyvenpDKTAANIR-------GDFWLLGDRGIKDEDGYFQFMGRADDI 465
Cdd:cd05943 438 FDEEGKPVW-GEKGELVC-TKPFpsMPVG-FWN-----DPDGSRYRaayfakyPGVWAHGDWIEITPRGGVVILGRSDGT 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 466 INSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILASQflshdpEQLTKELQQHVKSVTA----PYKYP 541
Cdd:cd05943 510 LNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDELRKRIRSTIRsalsPRHVP 583
|
570
....*....|....*...
gi 157311624 542 RKIEFVLNLPKTVTGKIQ 559
Cdd:cd05943 584 AKIIAVPDIPRTLSGKKV 601
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-563 |
2.54e-13 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 73.15 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM----SKA 154
Cdd:PRK10252 485 SYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP-------LDTGYpddRLKMmledARP 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 155 KAIVAGDEVIQE-VDTVASECPSLRIKLLVSEKSCDGwlnfkkllneASTTHHcvetgsqeASAIYFTSGTSGLPK--MA 231
Cdd:PRK10252 557 SLLITTADQLPRfADVPDLTSLCYNAPLAPQGAAPLQ----------LSQPHH--------TAYIIFTSGSTGRPKgvMV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 232 EHsysslglkakmdagwtglQAsdimwtisdtgwILNILGSLLESWTLGA---------CTF-VHLLPKF---------- 291
Cdd:PRK10252 619 GQ------------------TA------------IVNRLLWMQNHYPLTAddvvlqktpCSFdVSVWEFFwpfiagaklv 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 292 --------DPLVILKTLSSYPIKSMMGAPivyRML------LQQDLSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDI 357
Cdd:PRK10252 669 maepeahrDPLAMQQFFAEYGVTTTHFVP---SMLaafvasLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPL 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 358 REFYGQTETG------------LTCMVSKTMKIKPGYMGTAascydVQVIDDKGNVLPPGTEGDI---GIRVKpirpigi 422
Cdd:PRK10252 746 HNLYGPTEAAvdvswypafgeeLAAVRGSSVPIGYPVWNTG-----LRILDARMRPVPPGVAGDLyltGIQLA------- 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 423 fSGYVENPDKTAANIRGD-------FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHP----AVVET 491
Cdd:PRK10252 814 -QGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHA 892
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157311624 492 AVISSPDPVRGEVVKafviLASQFLSHDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:PRK10252 893 CVINQAAATGGDARQ----LVGYLVSQSGLPLDTSaLQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
82-530 |
6.93e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 71.08 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 82 NFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFM---PGtiqMKSTDILYRLQMSKAKAIV 158
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 159 AgdeviQEVDTVAS-----ECPSLRIKLLVSEKSCDGWLNFKKLlnEASTTHH---CVETGSQEASAIYFTSGTSGLPKM 230
Cdd:PRK09274 119 G-----IPKAHLARrlfgwGKPSVRRLVTVGGRLLWGGTTLATL--LRDGAAApfpMADLAPDDMAAILFTSGSTGTPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 231 AEHSYSSLglkakmDAGWTGLQASdimWTISDTGWILNI--LGSLLeSWTLGACTfvhLLPKFD--------PLVILKTL 300
Cdd:PRK09274 192 VVYTHGMF------EAQIEALRED---YGIEPGEIDLPTfpLFALF-GPALGMTS---VIPDMDptrpatvdPAKLFAAI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 301 SSYPIKSMMGAPIVYRMLLQQDLSS-YKFPHLQNCLAGGESLLPETLENWRAQTGLDIREF--YGQTETGLTCMVS---- 373
Cdd:PRK09274 259 ERYGVTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGAPVPIAVIERFRAMLPPDAEILtpYGATEALPISSIEsrei 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 374 --KTMKIK---PGY-MGTAASCYDVQVID---------DKGNVLPPGTEGDIgirvkpirpigIFSG------YVENPDK 432
Cdd:PRK09274 339 lfATRAATdngAGIcVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEI-----------VVAGpmvtrsYYNRPEA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 433 TAAN----IRGDFW-LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPvrGEVVKA 507
Cdd:PRK09274 408 TRLAkipdGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPV 485
|
490 500
....*....|....*....|...
gi 157311624 508 FVILASQFLSHDPEQLTKELQQH 530
Cdd:PRK09274 486 LCVELEPGVACSKSALYQELRAL 508
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
334-563 |
7.21e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.12 E-value: 7.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 334 CLAGGESLLPETLENWRAqtGLDIREF---YGQTET---GLTCMVSKTMKIKPGY--MGTAASCYDVQVIDDKGNVLPPG 405
Cdd:PRK05691 2453 CITGGEALTGEHLQRIRQ--AFAPQLFfnaYGPTETvvmPLACLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQG 2530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 406 TEGDIGIRVKpirpiGIFSGYVENPDKTA--------ANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSE 477
Cdd:PRK05691 2531 ATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGE 2605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 478 VENALMKHPAVVETAVISSPDPVRGEVVKafvILASQFLSHDPEQ---LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTV 554
Cdd:PRK05691 2606 IESRLLEHPAVREAVVLALDTPSGKQLAG---YLVSAVAGQDDEAqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTA 2682
|
....*....
gi 157311624 555 TGKIQRTKL 563
Cdd:PRK05691 2683 NGKLDRRAL 2691
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
85-563 |
3.18e-12 |
|
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: 68.65 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 85 ELSENSQQAANILSGACglQRGDR-VAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV 163
Cdd:cd17654 21 DLAEKISNLSNFLRKKF--QTEERaIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 164 IQEvdtvasecPSLRIKLLVsekscdgwlNFKKLLNEAStthhcvetgsqeaSAIYFTSGTSGLPK---MAEHSYSS--L 238
Cdd:cd17654 99 DNA--------PLSFTPEHR---------HFNIRTDECL-------------AYVIHTSGTTGTPKivaVPHKCILPniQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 239 GLKAKMDagwtgLQASDIMWTISDTGW---ILNILGSLLEswtlGAC-----TFVHLLP-KFDPlvILKTLSSypIKSMM 309
Cdd:cd17654 149 HFRSLFN-----ITSEDILFLTSPLTFdpsVVEIFLSLSS----GATllivpTSVKVLPsKLAD--ILFKRHR--ITVLQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 310 GAPIVYRMLLQQDLSSY---KFPHLQNCLAGGESLLPETLENWRAQTGLDIREF--YGQTETgltCMVSKTMKIK----P 380
Cdd:cd17654 216 ATPTLFRRFGSQSIKSTvlsATSSLRVLALGGEPFPSLVILSSWRGKGNRTRIFniYGITEV---SCWALAYKVPeedsP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 381 GYMGTAASCYDVQVIDDKGNvlppgtEGDIGIRVKPIRPIGIFSGYVENPdktaaniRGDFWLLGDRgIKDEDGYFQFMG 460
Cdd:cd17654 293 VQLGSPLLGTVIEVRDQNGS------EGTGQVFLGGLNRVCILDDEVTVP-------KGTMRATGDF-VTVKDGELFFLG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 461 RADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDpvrgEVVKAFVILASqflSHDPEQltKELQQHVKSvtaPYKY 540
Cdd:cd17654 359 RKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGES---SSSRIH--KELQLTLLS---SHAI 426
|
490 500
....*....|....*....|...
gi 157311624 541 PRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17654 427 PDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
81-563 |
5.94e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.04 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMP---GTIQMKSTDILyrlQMSKAKAI 157
Cdd:PRK05691 3746 WSYAELNRAANRLGHALRAA-GVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPldpGLPAQRLQRII---ELSRTPVL 3821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 VAGDEVIQEVDTVASECP-SLRIKLLVSEKscdgwlnfkkLLNEASTTHH-CVETGSQEASAIYFTSGTSGLPK------ 229
Cdd:PRK05691 3822 VCSAACREQARALLDELGcANRPRLLVWEE----------VQAGEVASHNpGIYSGPDNLAYVIYTSGSTGLPKgvmveq 3891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 230 --MAEHSYSS---LGLKAKMDAGWTGLQASDI-MWTIsdtgwilnilgslleswtLGACTF---VHLLPK---FDPLVIL 297
Cdd:PRK05691 3892 rgMLNNQLSKvpyLALSEADVIAQTASQSFDIsVWQF------------------LAAPLFgarVEIVPNaiaHDPQGLL 3953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 298 KTLSSYPIKSMMGAP-IVYRMLLQQDLSsykFPHLQNCLAGGESLLPETLENW---RAQTGLdiREFYGQTEtgltC--- 370
Cdd:PRK05691 3954 AHVQAQGITVLESVPsLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWlqrYPQIGL--VNAYGPAE----Csdd 4024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 371 -------MVSKTMKIKPgyMGTAASCYDVQVIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVENPDKTA----ANIRG 439
Cdd:PRK05691 4025 vaffrvdLASTRGSYLP--IGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTAlafvPHPFG 4097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 440 D----FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSpDPVRGEVVKAFVILASQF 515
Cdd:PRK05691 4098 ApgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ-EGVNGKHLVGYLVPHQTV 4176
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 157311624 516 lsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:PRK05691 4177 --LAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
73-484 |
2.10e-11 |
|
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: 66.61 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 73 NGKGKELMWNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIfMPGTIQMKSTD-ILYRLQM 151
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFL-KLGLERFHGVGILGFNSPEWFIAAVGAIFAGGI-AVGIYTTNSPEaCQYVAET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 152 SKAKAIVAGDEV-IQEVDTVASECPSLR----IKLLVSEKSCD--GWLNFKKLLNEASTTHHCVETGSQEAS---AIYFT 221
Cdd:cd05933 79 SEANILVVENQKqLQKILQIQDKLPHLKaiiqYKEPLKEKEPNlySWDEFMELGRSIPDEQLDAIISSQKPNqccTLIYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 222 SGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILN-ILGSLLESWT---LGACTFvhlLPKFDPL--V 295
Cdd:cd05933 159 SGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLShIAAQILDIWLpikVGGQVY---FAQPDALkgT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 296 ILKTLSSYPIKSMMGAPIVY--------------------------RMLLQQDLSSYK---------------------- 327
Cdd:cd05933 236 LVKTLREVRPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakGVGLETNLKLMGgespsplfyrlakklvfkkvrk 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 328 ---FPHLQNCLAGGESLLPETLENWraqTGLDIR--EFYGQTET-GLtcmvsKTMKIKPGYmgTAASCydvqviddkGNV 401
Cdd:cd05933 316 algLDRCQKFFTGAAPISRETLEFF---LSLNIPimELYGMSETsGP-----HTISNPQAY--RLLSC---------GKA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 402 LPpgtegdiGIRVKPIRP----IG--------IFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADD-IIN 467
Cdd:cd05933 377 LP-------GCKTKIHNPdadgIGeicfwgrhVFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIIT 449
|
490
....*....|....*..
gi 157311624 468 SSGYRIGPSEVENALMK 484
Cdd:cd05933 450 AGGENVPPVPIEDAVKK 466
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
42-559 |
6.95e-11 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 65.20 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 42 AKFNFASDVLDHwadmekagKRLPSPALWWVNGKGKELMWNFRELSEnsqQAANILSG--ACGLQRGDRVAVMLPRVPEW 119
Cdd:PRK03584 84 ARLNYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRR---QVAALAAAlrALGVGPGDRVAAYLPNIPET 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 120 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD---------EVIQEVDTVASECPSLRIKLLVS------ 184
Cdd:PRK03584 153 VVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLEHVVVVPylgpaa 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 185 -EKSCDGWLNFKKLLNEAstthhcvetgsqEASAIYFT-------------SGTSGLPKMAEHSYSSLGLKA-KMDAGWT 249
Cdd:PRK03584 233 aAAALPGALLWEDFLAPA------------EAAELEFEpvpfdhplwilysSGTTGLPKCIVHGHGGILLEHlKELGLHC 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 250 GLQASDIMWTISDTGWIL-NIL-GSLLeswtLGACTFVH----LLPKFDPL---------VILKTLSSYpIKSMMGAPIV 314
Cdd:PRK03584 301 DLGPGDRFFWYTTCGWMMwNWLvSGLL----VGATLVLYdgspFYPDPNVLwdlaaeegvTVFGTSAKY-LDACEKAGLV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 315 YRmllqqdlSSYKFPHLQNCLAGGESLLPETL----ENWRAQT-------GLDIrefygqtetgLTCMV--SKTMKIKPG 381
Cdd:PRK03584 376 PG-------ETHDLSALRTIGSTGSPLPPEGFdwvyEHVKADVwlasisgGTDI----------CSCFVggNPLLPVYRG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 382 YMGTAASCYDVQVIDDKGNVLppgtEGDIGIRV--KPI--RPIGI-------------FSGYvenpdktaANIrgdfWLL 444
Cdd:PRK03584 439 EIQCRGLGMAVEAWDEDGRPV----VGEVGELVctKPFpsMPLGFwndpdgsryrdayFDTF--------PGV----WRH 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 445 GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVILAsqflshDPEQLT 524
Cdd:PRK03584 503 GDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLA------EGVTLD 576
|
570 580 590
....*....|....*....|....*....|....*....
gi 157311624 525 KELQQHVKSV----TAPYKYPRKIEFVLNLPKTVTGKIQ 559
Cdd:PRK03584 577 DALRARIRTTirtnLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
212-564 |
7.34e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 65.12 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 212 SQEASAIYFTSGTSGLPKMAEHSYSSLglkakmdagwtgLQASDIMWTISDTGWILNILGSL--LESWTLGactfVHLlp 289
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSL------------LANVEQIKTIADFTPNDRFMSALplFHSFGLT----VGL-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 290 kFDPLVILKTLSSYPiksmmgAPIVYRML--LQQD------------LSSY-KFPH------LQNCLAGGESLLPETLEN 348
Cdd:PRK08043 426 -FTPLLTGAEVFLYP------SPLHYRIVpeLVYDrnctvlfgtstfLGNYaRFANpydfarLRYVVAGAEKLQESTKQL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 349 WRAQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVIddkgNVlpPGTEGdiGIRVKpIRPIGIFSGY-- 426
Cdd:PRK08043 499 WQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLL----SV--PGIEQ--GGRLQ-LKGPNIMNGYlr 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 427 VENPDK----TAANIRGDF---WL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN-ALMKHPAVVETAVISSp 497
Cdd:PRK08043 570 VEKPGVlevpTAENARGEMergWYdTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKS- 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157311624 498 DPVRGEvvkAFVILASqflshDPEqLTKE-LQQHVKSVTAP-YKYPRKIEFVLNLPKTVTGKIQRTKLR 564
Cdd:PRK08043 649 DASKGE---ALVLFTT-----DSE-LTREkLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLK 708
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
83-564 |
8.87e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 64.64 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 83 FRELSENSQQAANILSGAcGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMK-------STDILYRLQMSKAK 155
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 156 AIVAGDEVIQEVDTVASecpSLRIKLLVSekscdgWLNFKkLLNEASTThhcVETGSQEASA-IYFTSGTSGLPK----- 229
Cdd:PRK09192 131 AIITPDELLPWVNEATH---GNPLLHVLS------HAWFK-ALPEADVA---LPRPTPDDIAyLQYSSGSTRFPRgviit 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 230 ----MAE-HSYSSLGLKakmdagwtgLQASD--IMWT--ISDTGWIlnilGSLLeswTLGACTF-VHLLPKFD----PLV 295
Cdd:PRK09192 198 hralMANlRAISHDGLK---------VRPGDrcVSWLpfYHDMGLV----GFLL---TPVATQLsVDYLPTRDfarrPLQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 296 ILK-------TLSSYPiksMMGAPIVYRMLLQQDLSSYKFPHLQNCLAGGESLLPETLENWR---AQTGLDIREF---YG 362
Cdd:PRK09192 262 WLDlisrnrgTISYSP---PFGYELCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAeafAPAGFDDKAFmpsYG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 363 QTETGL------------------TCMVSKTMKIKPGYMGTAAS----C------YDVQVIDDKGNVLPPGTEGDIGIRv 414
Cdd:PRK09192 339 LAEATLavsfsplgsgivveevdrDRLEYQGKAVAPGAETRRVRtfvnCgkalpgHEIEIRNEAGMPLPERVVGHICVR- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 415 KPirpiGIFSGYVENPDkTAANIRGDFWL-LGDRGIKdEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVV--ET 491
Cdd:PRK09192 418 GP----SLMSGYFRDEE-SQDVLAADGWLdTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDA 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157311624 492 AVISSPDPvRGEVVKAFVilasQFLSHDPE---QLTKELQQHVKSVTApykYPRKIEFV--LNLPKTVTGKIQRTKLR 564
Cdd:PRK09192 492 AAFSIAQE-NGEKIVLLV----QCRISDEErrgQLIHALAALVRSEFG---VEAAVELVppHSLPRTSSGKLSRAKAK 561
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
383-564 |
8.94e-11 |
|
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: 64.43 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 383 MGTAASCYDVQVIDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVENPDKTAANIRGDFWLL-GDRG-IKDEDGYFqfMG 460
Cdd:cd05908 316 VGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP-----GYYNNPEATAKVFTDDGWLKtGDLGfIRNGRLVI--TG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 461 RADDIINSSGYRIGPSEVENalmkhpavvetaVISSPDPVR-GEVVKAFVilasqflsHDPEQLTKEL---QQHVKSVTA 536
Cdd:cd05908 389 REKDIIFVNGQNVYPHDIER------------IAEELEGVElGRVVACGV--------NNSNTRNEEIfcfIEHRKSEDD 448
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157311624 537 PYKYPRKIEFVLN---------------LPKTVTGKIQRTKLR 564
Cdd:cd05908 449 FYPLGKKIKKHLNkrggwqinevlpirrIPKTTSGKVKRYELA 491
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
217-565 |
1.82e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 60.71 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 217 AIYFTSGTSGLPKMAEHSYSSLGLKAKmdagwtglQASDIMWTISDTgwilNILGSL--LESWTLGACTFVHLLPKF--- 291
Cdd:PRK08633 786 TIIFSSGSEGEPKGVMLSHHNILSNIE--------QISDVFNLRNDD----VILSSLpfFHSFGLTVTLWLPLLEGIkvv 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 292 ---DPL---VILKTLSSYPIKSMMGAPIVYRMLLQQD-LSSYKFPHLQNCLAGGESLLPETLENWRAQTGLDIREFYGQT 364
Cdd:PRK08633 854 yhpDPTdalGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGAT 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 365 ETGLTCMVSKTMKIKPGYM---------------GTAascydVQVID-DKGNVLPPGTEGDIgirvkPIRPIGIFSGYVE 428
Cdd:PRK08633 934 ETSPVASVNLPDVLAADFKrqtgskegsvgmplpGVA-----VRIVDpETFEELPPGEDGLI-----LIGGPQVMKGYLG 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 429 NPDKTA---ANIRGDFWLL-GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMK--HPAVVETAVISSPDPVRG 502
Cdd:PRK08633 1004 DPEKTAeviKDIDGIGWYVtGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKG 1083
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157311624 503 EVVkafVILASQflshdPEQLTKELQQHVKSVTAP--YKyPRKIEFVLNLPKTVTGKIQRTKLRD 565
Cdd:PRK08633 1084 EKL---VVLHTC-----GAEDVEELKRAIKESGLPnlWK-PSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
113-575 |
2.61e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 59.83 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 113 LPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQE------VDTVASECPSLRIKLLVSEK 186
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralplYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 187 SCD--------GWLNFkklLNEASTTHhcvETGSQEASAIY----------FTSGTSGLPKMAEHSYSSlGLKAKMDaGW 248
Cdd:PLN03051 81 PVAvplreqdlSWCDF---LGVAAAQG---SVGGNEYSPVYapvesvtnilFSSGTTGEPKAIPWTHLS-PLRCASD-GW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 249 TGL--QASDIMWTISDTGWILnilGSLL--ESWTLGACTFVH----LLPKFDPLV------ILKTlssypIKSMMGApiv 314
Cdd:PLN03051 153 AHMdiQPGDVVCWPTNLGWMM---GPWLlySAFLNGATLALYggapLGRGFGKFVqdagvtVLGL-----VPSIVKA--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 315 YRMLLQQDLSSYKFPHLQNCLAGGESLLPET---LENWRAQTGlDIREFYGQTETGLTCMVSKTMKIK-PGYMGTAASCY 390
Cdd:PLN03051 222 WRHTGAFAMEGLDWSKLRVFASTGEASAVDDvlwLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQaPGAFSTASLGT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 391 DVQVIDDKGNVLPPGTE--GDIGIRVkpirPIGIFSGYVENPDKTAANIRG---------DFWLLGDRGIKDEDGYFQFM 459
Cdd:PLN03051 301 RFVLLNDNGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmpmygskgmPLRRHGDIMKRTPGGYFCVQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 460 GRADDIINSSGYRIGPSEVENALMK-HPAVVETAVISSPDPVRGE----VVKAFVILASQFLSHDPEQLTKELQQHVKSV 534
Cdd:PLN03051 377 GRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTN 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 157311624 535 TAPYKYPRKIEFVLNLPKTVTGKIQRTKLRDKEWK-MSGKAR 575
Cdd:PLN03051 457 LNPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKKeLSGRSK 498
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
80-565 |
1.34e-08 |
|
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: 57.61 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 80 MW-NFRELSENSQQAAN-ILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 157
Cdd:cd05927 4 EWiSYKEVAERADNIGSaLRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 V--AGDEVIQevdtvasecpslrikllvsekscdgWLNFKKLLNEASTTHhcvETGSQEASA-IYFTSGTSGLPKMAEHS 234
Cdd:cd05927 84 FcdAGVKVYS-------------------------LEEFEKLGKKNKVPP---PPPKPEDLAtICYTSGTTGNPKGVMLT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 235 YSSlglkakmdagwtglqasdIMWTISDTGWILNILGSLLEswtlgacTFVHL--LP---KFDPLVILKTLS-------- 301
Cdd:cd05927 136 HGN------------------IVSNVAGVFKILEILNKINP-------TDVYIsyLPlahIFERVVEALFLYhgakigfy 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 302 SYPIKSMM------------GAPIVY-RML--LQQDLS--------------SYKFPHLQN------------------- 333
Cdd:cd05927 191 SGDIRLLLddikalkptvfpGVPRVLnRIYdkIFNKVQakgplkrklfnfalNYKLAELRSgvvraspfwdklvfnkikq 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 334 --------CLAGGESLLPETLENWRAQTGLDIREFYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQVID--DKG-NVL 402
Cdd:cd05927 271 alggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpEMNyDAK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 403 PPGTEGDIGIRVKpirpiGIFSGYVENPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRADDIIN-SSGYRIGPSEVEN 480
Cdd:cd05927 351 DPNPRGEVCIRGP-----NVFSGYYKDPEKTAEALDEDGWLHtGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIEN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 481 ALMKHPAVVETAV-----------ISSPDPvrgEVVKAfvILASQFL-SHDPEQLTK--ELQQHV---------KSVTAP 537
Cdd:cd05927 426 IYARSPFVAQIFVygdslksflvaIVVPDP---DVLKE--WAASKGGgTGSFEELCKnpEVKKAIledlvrlgkENGLKG 500
|
570 580 590
....*....|....*....|....*....|....
gi 157311624 538 YKYPRKIEFVLNLPK------TVTGKIQRTKLRD 565
Cdd:cd05927 501 FEQVKAIHLEPEPFSvengllTPTFKLKRPQLKK 534
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
335-507 |
3.20e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 50.10 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 335 LAGGESLLPETLENWRAQTGLDIREFYGQTETglTCMVSKTMK--IKPGYMGTAASCYDVQVID---------DKgnvlp 403
Cdd:PLN02736 382 SSGASPLSPDVMEFLRICFGGRVLEGYGMTET--SCVISGMDEgdNLSGHVGSPNPACEVKLVDvpemnytseDQ----- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 404 PGTEGDIGIRvKPIrpigIFSGYVENPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIIN-SSGYRIGPSEVENA 481
Cdd:PLN02736 455 PYPRGEICVR-GPI----IFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENV 529
|
170 180 190
....*....|....*....|....*....|....*..
gi 157311624 482 LMKHPAVVETAV-----------ISSPDPvrgEVVKA 507
Cdd:PLN02736 530 YAKCKFVAQCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
48-568 |
1.98e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 47.50 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 48 SDVLDHWADMEKAGKRLP-SPALWW---VNGKGKELMW-NFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLV 122
Cdd:PLN02430 39 SDITTAWDIFSKSVEKYPdNKMLGWrriVDGKVGPYMWkTYKEVYEEVLQIGSALR-ASGAEPGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 123 ILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVdtVASECPSL-RIKLLVS-----EKSCD------- 189
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKEL--LEPDCKSAkRLKAIVSftsvtEEESDkasqigv 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 190 ---GWLNFKKLLNEASTthhcvETGSQEAS---AIYFTSGTSGLPKMAEHSYSSL-----GLKAKMDagwtglQASDIMw 258
Cdd:PLN02430 196 ktySWIDFLHMGKENPS-----ETNPPKPLdicTIMYTSGTSGDPKGVVLTHEAVatfvrGVDLFME------QFEDKM- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 259 TISDTGW----ILNILGSLLESWTL--GACT-FVH------------LLPKF---DPLV-------ILKTLSSY-PIKSM 308
Cdd:PLN02430 264 THDDVYLsflpLAHILDRMIEEYFFrkGASVgYYHgdlnalrddlmeLKPTLlagVPRVferihegIQKALQELnPRRRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 309 MgAPIVYRMLLQQDLSSYK------------FPHLQNCL--------AGGESLLPETLENWRAQTGLDIREFYGQTET-G 367
Cdd:PLN02430 344 I-FNALYKYKLAWMNRGYShkkaspmadflaFRKVKAKLggrlrlliSGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 368 LT--------CMVsktmkikpGYMGTAASCYDVQV-------IDDKGNvlPPgtEGDIGIRVKPIrpigiFSGYVENPDK 432
Cdd:PLN02430 423 PTtlgfpdemCML--------GTVGAPAVYNELRLeevpemgYDPLGE--PP--RGEICVRGKCL-----FSGYYKNPEL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 433 TAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIIN-SSGYRIGPSEVENALMKHPAVVETAVISspDPVRGEVVkAFVIL 511
Cdd:PLN02430 486 TEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEYLENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVP 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 157311624 512 asqflshDPEQLTK--ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTgkiQRTKLRDKEW 568
Cdd:PLN02430 563 -------NEENTNKwaKDNGFTGSFEELCSLPELKEHILSELKSTA---EKNKLRGFEY 611
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
81-568 |
5.94e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 45.63 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 81 WNFRELSENSQQAANILSgACGLQRGDRVAVMLPRVPEWWLVILGCIRAG---LIFMPGTIQMKSTDILYRLQmskakai 157
Cdd:PRK09029 29 LTWQQLCARIDQLAAGFA-QQGVVEGSGVALRGKNSPETLLAYLALLQCGarvLPLNPQLPQPLLEELLPSLT------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 158 vagdeviqeVDTVASECPSLRIKLLVSekscdgwlnfkKLLNEASTTHHCVETGSQEASAIyFTSGTSGLPKMAEHSY-- 235
Cdd:PRK09029 101 ---------LDFALVLEGENTFSALTS-----------LHLQLVEGAHAVAWQPQRLATMT-LTSGSTGLPKAAVHTAqa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 236 ---SSLGLKAKMDagwtgLQASD---------------IMWTISDTGWILNI--LGSLLESwtLGACTFVHLLPkfdplV 295
Cdd:PRK09029 160 hlaSAEGVLSLMP-----FTAQDswllslplfhvsgqgIVWRWLYAGATLVVrdKQPLEQA--LAGCTHASLVP-----T 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 296 ILKTLSSYPiksmmgapivyrmllQQDLSsykfphLQNCLAGGeSLLPETLENWRAQTGldIREF--YGQTEtgltcmvs 373
Cdd:PRK09029 228 QLWRLLDNR---------------SEPLS------LKAVLLGG-AAIPVELTEQAEQQG--IRCWcgYGLTE-------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 374 ktmkikpgymgtAASCYDVQVIDDKGNV-LP-PGTE-----GDIGIRVKpirpiGIFSGYvenpdktaanirgdfWLlgD 446
Cdd:PRK09029 276 ------------MASTVCAKRADGLAGVgSPlPGREvklvdGEIWLRGA-----SLALGY---------------WR--Q 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 447 RGIK---DEDGYFQ-------------FMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVISSPDPVRGEVVKAFVi 510
Cdd:PRK09029 322 GQLVplvNDEGWFAtrdrgewqngeltILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV- 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157311624 511 lasQFLShdpEQLTKELQQHVKSVTAPYKYPrkIEFVLnLPKTV-TG--KIQRTKLrdKEW 568
Cdd:PRK09029 401 ---ESDS---EAAVVNLAEWLQDKLARFQQP--VAYYL-LPPELkNGgiKISRQAL--KEW 450
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
437-563 |
9.06e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 45.20 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 437 IRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVET------------AVIS--SPDPVRG 502
Cdd:cd17647 369 PRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKP 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157311624 503 EVVKAFVILASQFLSHDP--------EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRTKL 563
Cdd:cd17647 449 DDESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
417-564 |
2.72e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 43.60 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 417 IRPIGIFSGYVenpdkTAANIRGDFWL-LGDRGIKDEDGyFQFMGRADDIINSSGYRIGPSEVENALMKHPAVVETAVIS 495
Cdd:PRK05851 377 IRGASMMSGYL-----GQAPIDPDDWFpTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVA 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157311624 496 SPDPVRGevVKAFVILASQFLSHDPEQLTKELQQHVKSVTApyKYPRKIEFVL--NLPKTVTGKIQRTKLR 564
Cdd:PRK05851 451 VGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
72-165 |
4.11e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 40.02 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157311624 72 VNGKGKE---LMWnfRELSENSQQAANILSGACGLQRGDRVAVMLPRVPEWWLVILGCIRAGLIFMP------------- 135
Cdd:cd05905 5 LDSKGKEattLTW--GKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPieppdisqqlgfl 82
|
90 100 110
....*....|....*....|....*....|....
gi 157311624 136 -GTIQM---KSTDILYRLQMSKAKAIVAGDEVIQ 165
Cdd:cd05905 83 lGTCKVrvaLTVEACLKGLPKKLLKSKTAAEIAK 116
|
|
| |
