|
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: 1041.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 40 VPAKFNFASDVLDHWADMEKAGKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEW 119
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 120 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLN 199
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 200 EASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAG-WTGLQASDIMWTISDTGWILNILCSLMEPWA 278
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRyWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 279 LGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIR 358
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 359 ESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIR 438
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 439 GDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSH 518
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1034593582 519 DPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 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: 669.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 160
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPKMAEHSySSLGL 240
Cdd:cd05972 78 -------------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHT-HSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDA-GWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL 319
Cdd:cd05972 108 GHIPTAaYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 320 QQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKG 399
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 400 NVLPPGTEGDIGIRVKpirPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVE 479
Cdd:cd05972 268 RELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 480 NALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQ 559
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*.
gi 1034593582 560 RAKLRD 565
Cdd:cd05972 423 RVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
40-568 |
2.41e-176 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 510.42 E-value: 2.41e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 40 VPAKFNFASDVLDHWADmEKAGKrlpsPALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEW 119
Cdd:COG0365 4 VGGRLNIAYNCLDRHAE-GRGDK----VALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 120 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVI---------QEVDTVASECPSLRIKLLV----SEK 186
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 187 SCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAG-WTGLQASDIMWTISDTGW 265
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 266 I---LNILCSlmePWALGACTFVH-LLPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTV 337
Cdd:COG0365 238 AtghSYIVYG---PLLNGATVVLYeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 338 GESLLPETLENWRAQTGLDIRESYGQTETGlTCMVSK--TMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvK 415
Cdd:COG0365 315 GEPLNPEVWEWWYEAVGVPIVDGWGQTETG-GIFISNlpGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK-G 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 416 PiRPiGIFSGYVDNPDKTAANIRGDF---WLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETA 492
Cdd:COG0365 393 P-WP-GMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034593582 493 VISSPDPVRGEVVKAFVVLASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 568
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPGV--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 |
3.59e-169 |
|
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: 491.24 E-value: 3.59e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 40 VPAKFNFASDVLDHWADMEKagKRLpspALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEW 119
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEYP--DKL---ALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 120 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--GDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKL 197
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 198 LNEASTT----HHCVETGSQEASAIYFTSGTSGLPKMAEHSYS-SLG--LKAKMdagWTGLQASDIMWTISDTGWILNIL 270
Cdd:cd05970 166 IKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTyPLGhiVTAKY---WQNVREGGLHLTVADTGWGKAVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 271 CSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWR 350
Cdd:cd05970 243 GKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 351 AQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNP 430
Cdd:cd05970 323 EKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 431 DKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVV 510
Cdd:cd05970 403 EKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034593582 511 LASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKE 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 |
1.09e-115 |
|
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: 351.03 E-value: 1.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 160
Cdd:COG0318 25 LTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeaSAIYFTSGTSGLPKMAEHSYSSLGL 240
Cdd:COG0318 103 -------------------------------------------------------ALILYTSGTTGRPKGVMLTHRNLLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDAGWTGLQASDIMWTIS----DTGWILNILCSLMepwaLGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYR 316
Cdd:COG0318 128 NAAAIAAALGLTPGDVVLVALplfhVFGLTVGLLAPLL----AGAT--LVLLPRFDPERVLELIERERVTVLFGVPTMLA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 317 MLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKI--KPGYMGTAASCYDVQ 393
Cdd:COG0318 202 RLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGerRPGSVGRPLPGVEVR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 394 IIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRI 473
Cdd:COG0318 282 IVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 474 GPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPK 552
Cdd:COG0318 357 YPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR------PGAELDaEELRAFLRERLARYKVPRRVEFVDELPR 430
|
490
....*....|....*..
gi 1034593582 553 TVTGKIQRAKLRDKEWK 569
Cdd:COG0318 431 TASGKIDRRALRERYAA 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
43-567 |
9.08e-114 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 350.35 E-value: 9.08e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 43 KFNFASDVLDHWADMEKAGKrlpsPALWWVNGKGKELmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLV 122
Cdd:PRK04319 41 KVNIAYEAIDRHADGGRKDK----VALRYLDASRKEK-YTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 123 ILGCIRAGLI-------FMPGTIQMkstdilyRLQMSKAKAIVAGDEVIQEVdtVASECPSLRIKLLVSE--KSCDGWLN 193
Cdd:PRK04319 115 LLGALKNGAIvgplfeaFMEEAVRD-------RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEdvEEGPGTLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 194 FKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--------MAEHSYSSlglKAKMDagwtgLQASDIMWTISDTGW 265
Cdd:PRK04319 186 FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKgvlhvhnaMLQHYQTG---KYVLD-----LHEDDVYWCTADPGW 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 266 ILNILCSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLL 342
Cdd:PRK04319 258 VTGTSYGIFAPWLNGA-TNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddlVKKYDLSSLRHILSVGEPLN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 343 PETLENWRAQTGLDIRESYGQTETGlTCMVSKT--MKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIrvKPIRPi 420
Cdd:PRK04319 337 PEVVRWGMKVFGLPIHDNWWMTETG-GIMIANYpaMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 421 GIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPV 500
Cdd:PRK04319 413 SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPV 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034593582 501 RGEVVKAFVVLASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKE 567
Cdd:PRK04319 493 RGEIIKAFVALRP---GYEPsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-567 |
1.47e-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: 1.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAkAIVAGDE 162
Cdd:cd05974 3 FAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA-VYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 ViqevdTVASEcPSLrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGLKA 242
Cdd:cd05974 81 N-----THADD-PML----------------------------------------LYFTSGTTSKPKLVEHTHRSYPVGH 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 243 KMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD 322
Cdd:cd05974 115 LSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 323 LSSYKFPhLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETglTCMVSKT--MKIKPGYMGTAASCYDVQIIDDKGN 400
Cdd:cd05974 195 LASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET--TALVGNSpgQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 401 vlpPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN 480
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 481 ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQR 560
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG--YEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
....*..
gi 1034593582 561 AKLRDKE 567
Cdd:cd05974 426 VELRRRE 432
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
81-565 |
1.41e-108 |
|
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: 332.47 E-value: 1.41e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 160
Cdd:cd05971 7 VTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPKMAEHSYSSLGL 240
Cdd:cd05971 85 -------------------------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLLG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDAGWTGL--QASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRML 318
Cdd:cd05971 116 HLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMM 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 319 LQQDLSSYKFP-HLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGL---TCmvSKTMKIKPGYMGTAASCYDVQI 394
Cdd:cd05971 196 RQQGEQLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLvigNC--SALFPIKPGSMGKPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 395 IDDKGNVLPPGTEGDIGIRvkpiRPIGI-FSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRI 473
Cdd:cd05971 274 VDDNGTPLPPGEVGEIAVE----LPDPVaFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 474 GPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 553
Cdd:cd05971 350 GPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNELPRT 427
|
490
....*....|..
gi 1034593582 554 VTGKIQRAKLRD 565
Cdd:cd05971 428 ATGKIRRRELRA 439
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
81-567 |
6.27e-101 |
|
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: 312.90 E-value: 6.27e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEVIQEVDTvasECPSLrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGL 240
Cdd:cd05969 80 EELYERTDP---EDPTL----------------------------------------LHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGaCTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ 320
Cdd:cd05969 117 YYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNG-VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 321 QD---LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGlTCMVSK--TMKIKPGYMGTAASCYDVQII 395
Cdd:cd05969 196 EGdelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETG-SIMIANypCMPIKPGSMGKPLPGVKAAVV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 396 DDKGNVLPPGTEGDIGIrvKPIRPiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGP 475
Cdd:cd05969 275 DENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 476 SEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTV 554
Cdd:cd05969 352 FEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF---EPsDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|...
gi 1034593582 555 TGKIQRAKLRDKE 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 |
3.00e-99 |
|
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: 309.11 E-value: 3.00e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 55 ADM-EKAGKRLP-SPALWWvngKGKelMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI 132
Cdd:cd05936 2 ADLlEEAARRFPdKTALIF---MGR--KLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 133 FMPGTIQMKSTDILYRLQMSKAKAIVAGDEviqevdtvasecpslrikllvsekscdgwlnFKKLLNEASTTHHCVETGS 212
Cdd:cd05936 76 VVPLNPLYTPRELEHILNDSGAKALIVAVS-------------------------------FTDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 213 QEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTG--LQASDIMwtisdtgwiLNIL---------CSLMEPWALGA 281
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVV---------LAALplfhvfgltVALLLPLALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 282 CtfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES 360
Cdd:cd05936 196 T--IVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 361 YGQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANI 437
Cdd:cd05936 274 YGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-------GpqVMKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 438 RgDFWLL-GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqfl 516
Cdd:cd05936 347 V-DGWLRtGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL----- 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034593582 517 sHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd05936 421 -KEGASLTEeEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-564 |
5.42e-94 |
|
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: 294.81 E-value: 5.42e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagde 162
Cdd:cd05973 3 FGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viqevdTVASECPSLRIKLLVsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSL-GLK 241
Cdd:cd05973 78 ------TDAANRHKLDSDPFV----------------------------------MMFTSGTTGLPKGVPVPLRALaAFG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 242 AKMDAGwTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPkFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ 321
Cdd:cd05973 118 AYLRDA-VDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 322 DLSSYKFP--HLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGltcMV-----SKTMKIKPGYMGTAASCYDVQI 394
Cdd:cd05973 196 GAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELG---MVlanhhALEHPVHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 395 IDDKGNVLPPGTEGDIGIRVKPiRPIGIFSGYVDNPDKTAAnirGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIG 474
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIAN-SPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 475 PSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 553
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG---GHEGtPALADELQLHVKKRLSAHAYPRTIHFVDELPKT 425
|
490
....*....|.
gi 1034593582 554 VTGKIQRAKLR 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 |
1.92e-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: 279.56 E-value: 1.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCsLMEPWALGACtfVHLLPKFDPLVIL 297
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFG-LLGALLAGGT--VVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 298 KTLSSYPIKSMMGAPIVYRMLLQQDLSS-YKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG--LTCMVSK 374
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLLKAPESAgYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtVATGPPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 375 TMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDG 454
Cdd:cd04433 162 DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-----GPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 455 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlSHDPEqltkELQQHVKSV 534
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA-DLDAE----ELRAHVRER 311
|
330 340
....*....|....*....|....*
gi 1034593582 535 TAPYKYPRKIEFVLNLPKTVTGKIQ 559
Cdd:cd04433 312 LAPYKVPRRVVFVDALPRTASGKID 336
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
42-564 |
7.07e-85 |
|
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: 273.09 E-value: 7.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 42 AKFNFASDVLDHwadmeKAGKRLPSPALWwvnGKGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWL 121
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAFI---DDAGSL--TYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 122 VILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVS--EKSCDGWLNFKKLLN 199
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSggAGPEAGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 200 EASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWA 278
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVlGIREDDVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 279 LGACTFvhLLPKF-DPLVILKTLSSYPIKSMMGAPIVYR-MLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLD 356
Cdd:cd05959 230 VGATTV--LMPERpTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 357 IRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAAN 436
Cdd:cd05959 308 ILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSAT-----MYWNNRDKTRDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 437 IRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFl 516
Cdd:cd05959 383 FQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1034593582 517 sHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd05959 462 -EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
81-569 |
1.73e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 267.44 E-value: 1.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:PRK06187 32 TTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEVIQEVDTVASECPSLRIKLLVSEKSCDG----WLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYS 236
Cdd:PRK06187 111 SEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 237 SLGLKAKMDAGWTGLQASDI------MWTISDTGWilnilcSLMePWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMG 310
Cdd:PRK06187 191 NLFLHSLAVCAWLKLSRDDVylvivpMFHVHAWGL------PYL-ALMAGA-KQV-IPRRFDPENLLDLIETERVTFFFA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 311 APIVYRMLLQ------QDLSSYKFphlqncVTVGESLLPETL-ENWRAQTGLDIRESYGQTETG--LTCMV-SKTMKIKP 380
Cdd:PRK06187 262 VPTIWQMLLKaprayfVDFSSLRL------VIYGGAALPPALlREFKEKFGIDLVQGYGMTETSpvVSVLPpEDQLPGQW 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 381 GYM---GTAASCYDVQIIDDKGNVLPPGtEGDIG-IRVKpirpiG--IFSGYVDNPDKTAANIRGDfWLL-GDRGIKDED 453
Cdd:PRK06187 336 TKRrsaGRPLPGVEARIVDDDGDELPPD-GGEVGeIIVR-----GpwLMQGYWNRPEATAETIDGG-WLHtGDVGYIDED 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 454 GYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVK 532
Cdd:PRK06187 409 GYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL------KPGATLDaKELRAFLR 482
|
490 500 510
....*....|....*....|....*....|....*..
gi 1034593582 533 SVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 569
Cdd:PRK06187 483 GRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
78-564 |
8.71e-81 |
|
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: 260.49 E-value: 8.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 78 ELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmpgtiqmkstdilyrlqmskakai 157
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAI------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 vagdeviqevdTVASEcPSLRIKllvsekscdgwlNFKKLLNEASTTHH-CVE--TGSQEASAIYFTSGTSGLPKMAEHS 234
Cdd:cd05958 63 -----------AVATM-PLLRPK------------ELAYILDKARITVAlCAHalTASDDICILAFTSGTTGAPKATMHF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 235 YSSLGLKAKmdaGWT----GLQASDIMWTISDTGWILNILCSLMEPWALGACTFvhLLPKFDPLVILKTLSSYPIKSMMG 310
Cdd:cd05958 119 HRDPLASAD---RYAvnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGV--LLEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 311 APIVYRMLL------QQDLSSykfphLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMG 384
Cdd:cd05958 194 APTAYRAMLahpdaaGPDLSS-----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 385 TAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpigifSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRAN 463
Cdd:cd05958 269 KPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP--------TGCRYLADKRQRTYVQGGWNItGDTYSRDPDGYFRHQGRSD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 464 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflsHDP-EQLTKELQQHVKSVTAPYKYPR 542
Cdd:cd05958 341 DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPG---VIPgPVLARELQDHAKAHIAPYKYPR 417
|
490 500
....*....|....*....|..
gi 1034593582 543 KIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd05958 418 AIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
58-566 |
2.60e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 255.98 E-value: 2.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 58 EKAGKRLP-SPALWWvngkgKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPG 136
Cdd:PRK07656 12 ARAARRFGdKEAYVF-----GDQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 137 TIQMKSTDILYRLQMSKAKAIVAGDEVIqEVDTVASEC-PSLRIKLLV----SEKSCDGWLNFKKLLNEASTTHHCVETG 211
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFL-GVDYSATTRlPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 212 SQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDT----GWILNILCSLMEpwalGACTFVHl 287
Cdd:PRK07656 165 PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFfhvfGYKAGVNAPLMR----GATILPL- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 288 lPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLD-IRESYGQTE 365
Cdd:PRK07656 240 -PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 366 -TGLTCM--VSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGD 440
Cdd:PRK07656 319 aSGVTTFnrLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR-------GpnVMKGYYDDPEATAAAIDAD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 441 FWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshd 519
Cdd:PRK07656 392 GWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG----- 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1034593582 520 pEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 566
Cdd:PRK07656 467 -AELTEEeLIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
83-564 |
7.23e-73 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 239.67 E-value: 7.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:cd05919 13 YGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 VIqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeASAIYfTSGTSGLPKMAEHSY-SSLGLK 241
Cdd:cd05919 92 DI--------------------------------------------------AYLLY-SSGTTGPPKGVMHAHrDPLLFA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 242 AKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKfDPLVILKTLSSYPIKSMMGAPIVY-RMLLQ 320
Cdd:cd05919 121 DAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLDS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 321 QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGN 400
Cdd:cd05919 200 CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 401 VLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN 480
Cdd:cd05919 280 TIPPGEEGDLLVRGP-----SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 481 ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
....
gi 1034593582 561 AKLR 564
Cdd:cd05919 433 FKLR 436
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
43-565 |
9.27e-73 |
|
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: 241.28 E-value: 9.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 43 KFNFASDVLDHWADMEKAGKrlpspaLWWVNGKGKelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLV 122
Cdd:TIGR02262 2 KYNAAEDLLDRNVVEGRGGK------TAFIDDISS---LSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 123 ILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKScDGWLNFKKLLNEAS 202
Cdd:TIGR02262 72 FLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGRPE-AGEVQLAELLATES 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 203 TTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWALGA 281
Cdd:TIGR02262 151 EQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTlGIREDDVCFSAAKLFFAYGLGNALTFPMSVGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 282 cTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYR-MLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES 360
Cdd:TIGR02262 231 -TTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 361 YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiGIFS--GYVDNPDKTAANIR 438
Cdd:TIGR02262 310 IGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-------GPSSatMYWNNRAKSRDTFQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 439 GDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsh 518
Cdd:TIGR02262 383 GEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ--- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1034593582 519 dpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:TIGR02262 460 --TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-564 |
1.42e-72 |
|
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: 238.35 E-value: 1.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 160
Cdd:cd05934 4 WTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 deviqeVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGL 240
Cdd:cd05934 81 ------VDPAS----------------------------------------------ILYTSGTTGPPKGVVITHANLTF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDAGWTGLQASDIMWTISDTGWIlNILC-SLMEPWALGAcTFVhLLPKFDPLVILKTLSSY--PIKSMMGAPIvyRM 317
Cdd:cd05934 109 AGYYSARRFGLGEDDVYLTVLPLFHI-NAQAvSVLAALSVGA-TLV-LLPRFSASRFWSDVRRYgaTVTNYLGAML--SY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 318 LLQQDLSSYKFPHLQNCVTVGESLlPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDD 397
Cdd:cd05934 184 LLAQPPSPDDRAHRLRAAYGAPNP-PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 398 KGNVLPPGTEGDIGIRvkPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSE 477
Cdd:cd05934 263 DGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 478 VENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 556
Cdd:cd05934 341 VERAILRHPAVREAAVVAVPDEVGEDEVKAVVVL------RPGETLDpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTE 414
|
....*...
gi 1034593582 557 KIQRAKLR 564
Cdd:cd05934 415 KVAKAQLR 422
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
81-560 |
6.86e-71 |
|
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: 234.43 E-value: 6.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 160
Cdd:cd17631 21 LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEVIQevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSL-- 238
Cdd:cd17631 98 DDLAL----------------------------------------------------LMYTSGTTGRPKGAMLTHRNLlw 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 239 -----GLKAKMDAGWTGLQASDIMWTISDTGWILNILcslmepwALGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAPI 313
Cdd:cd17631 126 navnaLAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL-------LRGGT--VVILRKFDPETVLDLIERHRVTSFFLVPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 314 VYRMLLQQ-DLSSYKFPHLQnCVTVGESLLPE-TLENWRAqTGLDIRESYGQTETG-LTCMVSKTMKI-KPGYMGTAASC 389
Cdd:cd17631 197 MIQALLQHpRFATTDLSSLR-AVIYGGAPMPErLLRALQA-RGVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGRPVFF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 390 YDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDfWLL-GDRGIKDEDGYFQFMGRANDIINS 468
Cdd:cd17631 275 VEVRIVDPDGREVPPGEVGEIVVR-GP----HVMAGYWNRPEATAAAFRDG-WFHtGDLGRLDEDGYLYIVDRKKDMIIS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 469 SGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT-KELQQHVKSVTAPYKYPRKIEFV 547
Cdd:cd17631 349 GGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR------PGAELDeDELIAHCRERLARYKIPKSVEFV 422
|
490
....*....|...
gi 1034593582 548 LNLPKTVTGKIQR 560
Cdd:cd17631 423 DALPRNATGKILK 435
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
40-571 |
6.92e-68 |
|
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: 231.44 E-value: 6.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 40 VPAKFNFASDVLDHWADMEKAGKrlpsPALWWVNG-KGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPE 118
Cdd:cd05967 45 VGGRLNTCYNALDRHVEAGRGDQ----IALIYDSPvTGTERTYTYAELLDEVSRLAGVLR-KLGVVKGDRVIIYMPMIPE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 119 WWLVILGCIRAGLI-------FmpgtiqmKSTDILYRLQMSKAKAIVA------GDEVIQE---VDTVASECPSLRIKLL 182
Cdd:cd05967 120 AAIAMLACARIGAIhsvvfggF-------AAKELASRIDDAKPKLIVTascgiePGKVVPYkplLDKALELSGHKPHHVL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 183 V---SEKSCD-----GWLNFKKLLNEAsTTHHCVETGSQEASAIYFTSGTSGLPK-----MAEHSyssLGLKAKMDAGWt 249
Cdd:cd05967 193 VlnrPQVPADltkpgRDLDWSELLAKA-EPVDCVPVAATDPLYILYTSGTTGKPKgvvrdNGGHA---VALNWSMRNIY- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 250 GLQASDIMWTISDTGWILNILCSLMEPWALGACTFVH-----LLPkfDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD-- 322
Cdd:cd05967 268 GIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYegkpvGTP--DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpd 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 323 ---LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG----LTCMVSKTMKIKPGYMGTAASCYDVQII 395
Cdd:cd05967 346 gkyIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGwpitANPVGLEPLPIKAGSPGKPVPGYQVQVL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 396 DDKGNVLPPGTEGDIGIRVkPIRPiGIFSGYVDNPDKTAANIRGDF---WLLGDRGIKDEDGYFQFMGRANDIINSSGYR 472
Cdd:cd05967 426 DEDGEPVGPNELGNIVIKL-PLPP-GCLLTLWKNDERFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHR 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 473 IGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPK 552
Cdd:cd05967 504 LSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPK 582
|
570 580
....*....|....*....|...
gi 1034593582 553 TVTGKIQRAKLRD----KEWKMS 571
Cdd:cd05967 583 TRSGKILRRTLRKiadgEDYTIP 605
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
81-565 |
4.02e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 226.74 E-value: 4.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEVIQEVDTVASECPSLRIKLLVSEK---SCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 237
Cdd:PRK08316 116 PALAPTAEAALALLPVDTLILSLVLGgreAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 238 L---GLKAKMDAGWTglqASDIMwtisdtgwiLNIL----CSLME----PW-ALGACTfvHLLPKFDPLVILKTLSSYPI 305
Cdd:PRK08316 196 LiaeYVSCIVAGDMS---ADDIP---------LHALplyhCAQLDvflgPYlYVGATN--VILDAPDPELILRTIEAERI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 306 KSMMGAPIVYRMLL------QQDLSSykfphLQNCVtVGESLLP-ETLENWRAQ-TGLDIRESYGQTETGLTCMV--SKT 375
Cdd:PRK08316 262 TSFFAPPTVWISLLrhpdfdTRDLSS-----LRKGY-YGASIMPvEVLKELRERlPGLRFYNCYGQTEIAPLATVlgPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 376 MKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGY 455
Cdd:PRK08316 336 HLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR-SP----QLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 456 FQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLT-KELQQHVKSV 534
Cdd:PRK08316 411 ITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG------ATVTeDELIAHCRAR 484
|
490 500 510
....*....|....*....|....*....|.
gi 1034593582 535 TAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK08316 485 LAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
83-565 |
4.93e-66 |
|
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: 221.78 E-value: 4.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGde 162
Cdd:cd05941 14 YADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVLDP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeaSAIYFTSGTSGLPKMAEHSYSSLG--L 240
Cdd:cd05941 92 -----------------------------------------------------ALILYTSGTTGRPKGVVLTHANLAanV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDAgWTglqasdimWTISDT-----------GWILNILCSLmepWALGACtfvHLLPKFDPLVILKTLSSYPIKSMM 309
Cdd:cd05941 119 RALVDA-WR--------WTEDDVllhvlplhhvhGLVNALLCPL---FAGASV---EFLPKFDPKEVAISRLMPSITVFM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 310 GAPIVYRMLLQQdlSSYKFPHLQNCVTVGES-----------LLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKI 378
Cdd:cd05941 184 GVPTIYTRLLQY--YEAHFTDPQFARAAAAErlrlmvsgsaaLPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 379 KPGYMGTAASCYDVQIIDDKGN-VLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYF 456
Cdd:cd05941 262 RPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GP----SVFKEYWNKPEATKEEFTDDGWFkTGDLGVVDEDGYY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 457 QFMGRAN-DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEqltkELQQHVKSVT 535
Cdd:cd05941 337 WILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE----ELKEWAKQRL 412
|
490 500 510
....*....|....*....|....*....|
gi 1034593582 536 APYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:cd05941 413 APYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
81-565 |
1.03e-64 |
|
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: 219.49 E-value: 1.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASA---IYFTSGTSGLPKMAEHSYSS 237
Cdd:cd05926 94 KGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDlalILHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 238 LGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRM 317
Cdd:cd05926 174 LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGS--VVLPPRFSASTFWPDVRDYNATWYTAVPTIHQI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 318 LLQQDLSSY--KFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG--LTCMVSKTMKIKPGYMGTAASCyDVQ 393
Cdd:cd05926 252 LLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVGV-EVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 394 IIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRANDIINSSGYR 472
Cdd:cd05926 331 ILDEDGEILPPGVVGEICLRGP-----NVTRGYLNNPEANAEAAFKDGWFRtGDLGYLDADGYLFLTGRIKELINRGGEK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 473 IGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPK 552
Cdd:cd05926 406 ISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRE-----GASVTEEELRAFCRKHLAAFKVPKKVYFVDELPK 480
|
490
....*....|...
gi 1034593582 553 TVTGKIQRAKLRD 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 |
2.90e-64 |
|
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: 218.24 E-value: 2.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEVIQEVDTVASECPSLRiKLLVSEKSCDGWLNFKKLLNEASTTHH-----CVETGSQEASAIYFTSGTSGLPKMAEHSY 235
Cdd:cd05911 90 PDGLEKVKEAAKELGPKD-KIIVLDDKPDGVLSIEDLLSPTLGEEDedlppPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 236 SSLglkakmdagwtgLQASDIMWTISDTGWILN--ILCSLMEPWALGACTFVHLL---------PKFDPLVILKTLSSYP 304
Cdd:cd05911 169 RNL------------IANLSQVQTFLYGNDGSNdvILGFLPLYHIYGLFTTLASLlngatviimPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 305 IKSMMGAP-IVYRMLLQQDLSSYKFPHLQNcVTVG--------ESLLPETLENWRaqtgldIRESYGQTETGLTCMVSKT 375
Cdd:cd05911 237 ITFLYLVPpIAAALAKSPLLDKYDLSSLRV-ILSGgaplskelQELLAKRFPNAT------IKQGYGMTETGGILTVNPD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 376 MKIKPGYMGTAASCYDVQIIDDKGN-VLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDED 453
Cdd:cd05911 310 GDDKPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVR-----GPQVMKGYYNNPEATKETFDEDGWLhTGDIGYFDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 454 GYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT-KELQQHVK 532
Cdd:cd05911 385 GYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRK------PGEKLTeKEVKDYVA 458
|
490 500
....*....|....*....|....*...
gi 1034593582 533 SVTAPYKYPRK-IEFVLNLPKTVTGKIQ 559
Cdd:cd05911 459 KKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
54-573 |
4.75e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 219.06 E-value: 4.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 54 WADMEKAGKRLPS-PALWWVngkGKELmwNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI 132
Cdd:PRK08314 13 FHNLEVSARRYPDkTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 133 FMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEV------------------DTVASECP-----SLRIKLLVSEKSCD 189
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 190 GWLnfkkLLNEASTTHHC---VETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWI 266
Cdd:PRK08314 168 GVV----AWKEALAAGLApppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 267 LNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ------DLSSYKfphlqnCVTVGES 340
Cdd:PRK08314 244 TGMVHSMNAPIYAGA-TVV-LMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASpglaerDLSSLR------YIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 341 LLPETL-ENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRvkpir 418
Cdd:PRK08314 316 AMPEAVaERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH----- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 419 piG--IFSGYVDNPDKTAA---NIRGD-FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETA 492
Cdd:PRK08314 391 --GpqVFKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAC 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 493 VISSPDPVRGEVVKAFVVLASQFLSHDPEQltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSG 572
Cdd:PRK08314 469 VIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAA 545
|
.
gi 1034593582 573 K 573
Cdd:PRK08314 546 K 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
81-469 |
1.08e-63 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 214.87 E-value: 1.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:pfam00501 22 LTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DE-VIQEVDTVASECPSLRIKLLVSEkscDGWLNFKKLLNEASTTHHCVETGSQEAS----AIYFTSGTSGLPKMAEHS- 234
Cdd:pfam00501 101 DAlKLEELLEALGKLEVVKLVLVLDR---DPVLKEEPLPEEAKPADVPPPPPPPPDPddlaYIIYTSGTTGKPKGVMLTh 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 235 ---YSSLGLKAKMDAGWTGLQASDIMWTIS----DTGWILNILCSLMepwaLGACtfVHLLPKF---DPLVILKTLSSYP 304
Cdd:pfam00501 178 rnlVANVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLSLGLLGPLL----AGAT--VVLPPGFpalDPAALLELIERYK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 305 IKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIK---P 380
Cdd:pfam00501 252 VTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDlrsL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 381 GYMGTAASCYDVQIIDDK-GNVLPPGTEGDIGIRvkpiRPiGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQF 458
Cdd:pfam00501 332 GSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAFDEDGWYRtGDLGRRDEDGYLEI 406
|
410
....*....|.
gi 1034593582 459 MGRANDIINSS 469
Cdd:pfam00501 407 VGRKKDQIKLG 417
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
81-565 |
1.95e-63 |
|
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: 218.97 E-value: 1.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEwwLVI--LGCIRAGLI-------FMPGTIQMkstdilyRLQM 151
Cdd:cd05966 85 ITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPE--LVIamLACARIGAVhsvvfagFSAESLAD-------RIND 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 152 SKAKAIVAGDE------VI---QEVDTVASECPSLRiKLLVSEKSC---------DGWLNfkKLLNEASTTHHCVETGSQ 213
Cdd:cd05966 155 AQCKLVITADGgyrggkVIplkEIVDEALEKCPSVE-KVLVVKRTGgevpmtegrDLWWH--DLMAKQSPECEPEWMDSE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 214 EASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWALGACTfvhllpkfd 292
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVfDYHPDDIYWCTADIGWITGHSYIVYGPLANGATT--------- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 293 plVILKTLSSYPIKSMM-------------GAPIVYRMLLQQ--------DLSSYKFPHlqncvTVGESLLPETLENWRA 351
Cdd:cd05966 303 --VMFEGTPTYPDPGRYwdivekhkvtifyTAPTAIRALMKFgdewvkkhDLSSLRVLG-----SVGEPINPEAWMWYYE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 352 QTG---LDIRESYGQTETG---LTCMVSKTmKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpiRPI-GIFS 424
Cdd:cd05966 376 VIGkerCPIVDTWWQTETGgimITPLPGAT-PLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK----RPWpGMAR 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 425 GYVDNPD---KTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 501
Cdd:cd05966 451 TIYGDHEryeDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIK 530
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034593582 502 GEVVKAFVVLASqflSHDPEQ-LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:cd05966 531 GEAIYAFVTLKD---GEEPSDeLRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
82-563 |
6.64e-63 |
|
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: 213.11 E-value: 6.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGd 161
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 eviQEVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSGTSGLPKMAEHSYSSLGLK 241
Cdd:cd05935 81 ---SELDDLA---------------------------------------------LIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 242 AKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL-- 319
Cdd:cd05935 113 ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGG-TYV-LMARWDRETALELIEKYKVTFWTNIPTMLVDLLat 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 320 ----QQDLSSYKFphlqncVTVGESLLPETL-ENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQI 394
Cdd:cd05935 191 pefkTRDLSSLKV------LTGGGAPMPPAVaEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 395 ID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAA---NIRG-DFWLLGDRGIKDEDGYFQFMGRANDIINSS 469
Cdd:cd05935 265 IDiETGRELPPNEVGEIVVR-GP----QIFKGYWNRPEETEEsfiEIKGrRFFRTGDLGYMDEEGYFFFVDRVKRMINVS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 470 GYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQltkELQQHVKSVTAPYKYPRKIEFVLN 549
Cdd:cd05935 340 GFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDE 416
|
490
....*....|....
gi 1034593582 550 LPKTVTGKIQRAKL 563
Cdd:cd05935 417 LPRSASGKILWRLL 430
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
3-558 |
2.83e-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: 2.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 3 WLRKVQGLCTLWGTQMSSRTLYinSRQLVSLQWGHQevpAKFNFASDVLDHwaDMEKAGKRLpspALWWVNGKGKEL-MW 81
Cdd:cd17634 16 WGEAGKILDWITPYQKVKNTSF--APGAPSIKWFED---ATLNLAANALDR--HLRENGDRT---AIIYEGDDTSQSrTI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:cd17634 86 SYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 EVIQEVDTV----------ASECPSLRIKLLVSEKSCD------GWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTS 225
Cdd:cd17634 165 GGVRAGRSVplkknvddalNPNVTSVEHVIVLKRTGSDidwqegRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 226 GLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHL-LPKF-DPLVILKTLSS 302
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAATTMKYVfDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 303 YPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLLPETLE-NWR--AQTGLDIRESYGQTETGLTCMvsktm 376
Cdd:cd17634 325 HGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPINPEAYEwYWKkiGKEKCPVVDTWWQTETGGFMI----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 377 KIKPGYMGTAASC-------YDVQIIDDKGNVLPPGTEGDIGIRVKpiRPIGIFSGYVDNPDKTAANIR--GDFWLLGDR 447
Cdd:cd17634 400 TPLPGAIELKAGSatrpvfgVQPAVVDNEGHPQPGGTEGNLVITDP--WPGQTRTLFGDHERFEQTYFStfKGMYFSGDG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 448 GIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLshDPEQLTKEL 527
Cdd:cd17634 478 ARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAEL 555
|
570 580 590
....*....|....*....|....*....|.
gi 1034593582 528 QQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 558
Cdd:cd17634 556 RNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
34-564 |
4.71e-61 |
|
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: 212.74 E-value: 4.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 34 QWGHQEVPAKFNFASDVLDHWAdmekaGKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVL 113
Cdd:cd05968 50 PWAAWFVGGRMNIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 114 PRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD---------EVIQEVDTVASECPSLRiKLLVS 184
Cdd:cd05968 124 PMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTVE-KVVVV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 185 E--KSCDGWLNFKKL---LNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMW 258
Cdd:cd05968 203 RhlGNDFTPAKGRDLsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQfDLKPGDLLT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 259 TISDTGWilnilcsLMEPWA------LGACTFVHL-LPKFD-PLVILKTLSSYPIKSMMGAPIVYRMLL--------QQD 322
Cdd:cd05968 283 WFTDLGW-------MMGPWLifggliLGATMVLYDgAPDHPkADRLWRMVEDHEITHLGLSPTLIRALKprgdapvnAHD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 323 LSSykfphLQNCVTVGESLLPETLeNWRAQTGLD----IRESYGQTETG---LTCMVSKtmKIKPGYMGTAASCYDVQII 395
Cdd:cd05968 356 LSS-----LRVLGSTGEPWNPEPW-NWLFETVGKgrnpIINYSGGTEISggiLGNVLIK--PIKPSSFNGPVPGMKADVL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 396 DDKGNVLPPgTEGDIGIRvKPIrpIGIFSGYVDNPDK---TAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYR 472
Cdd:cd05968 428 DESGKPARP-EVGELVLL-APW--PGMTRGFWRDEDRyleTYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKR 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 473 IGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPK 552
Cdd:cd05968 504 VGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGV--TPTEALAEELMERVADELGKPLSPERILFVKDLPK 581
|
570
....*....|..
gi 1034593582 553 TVTGKIQRAKLR 564
Cdd:cd05968 582 TRNAKVMRRVIR 593
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
34-563 |
1.47e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 210.28 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 34 QWGHQEVPAkfnfaSDVLDHWAdmekagKRLPS-PALWWVngkGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVV 112
Cdd:PRK06178 27 EYPHGERPL-----TEYLRAWA------RERPQrPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 113 LPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASEC-----------------P 175
Cdd:PRK06178 90 LPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhvivtsladvlpaeP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 176 SLRIKLLVSE--KSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTG-LQ 252
Cdd:PRK06178 170 TLPLPDSLRAprLAAAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVvGG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 253 ASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL------QQDLSSY 326
Cdd:PRK06178 250 EDSVFLSFLPEFWIAGENFGLLFPLFSGA-TLV-LLARWDAVAFMAAVERYRVTRTVMLVDNAVELMdhprfaEYDLSSL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 327 KFPhlqNCVTVGESLLPETLENWRAQTGLDIRE-SYGQTETGlTC------MVSKTMKIK--PGYMGTAASCYDVQIID- 396
Cdd:PRK06178 328 RQV---RVVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTETH-TCdtftagFQDDDFDLLsqPVFVGLPVPGTEFKICDf 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 397 DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGP 475
Cdd:PRK06178 404 ETGELLPLGAEGEIVVR-TP----SLLKGYWNKPEATAEALR-DGWLhTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 476 SEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPrKIEFVLNLPKTVT 555
Cdd:PRK06178 478 SEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP-----GADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTAT 551
|
....*...
gi 1034593582 556 GKIQRAKL 563
Cdd:PRK06178 552 GKVRKQDL 559
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
79-566 |
2.88e-59 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 205.49 E-value: 2.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 79 LMWNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 158
Cdd:PRK07514 27 LRYTYGDLDAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 159 AGDEVIQEVDTVASECPSLRIKLLVSekscDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL 238
Cdd:PRK07514 106 CDPANFAWLSKIAAAAGAPHVETLDA----DGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 239 GLKAKM--DA-GWTG----LQASDIMWTisdTGWILNILCSLMEpwalGACTFvhLLPKFDPLVILKTLSSypIKSMMGA 311
Cdd:PRK07514 182 LSNALTlvDYwRFTPddvlIHALPIFHT---HGLFVATNVALLA----GASMI--FLPKFDPDAVLALMPR--ATVMMGV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 312 PIVY-RMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGltcmvsktMKI--------KPGY 382
Cdd:PRK07514 251 PTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETN--------MNTsnpydgerRAGT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 383 MGTAASCYDVQIID-DKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGD-FWLLGDRGIKDEDGYFQF 458
Cdd:PRK07514 323 VGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 459 MGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAfVVLASQFLSHDPEQLTKELQQHVksvtAPY 538
Cdd:PRK07514 396 VGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA-VVVPKPGAALDEAAILAALKGRL----ARF 470
|
490 500
....*....|....*....|....*...
gi 1034593582 539 KYPRKIEFVLNLPKTVTGKIQRAKLRDK 566
Cdd:PRK07514 471 KQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
81-569 |
2.43e-58 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 203.83 E-value: 2.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:PRK06087 50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEVIQ-----EVDTVASECPSLRIKLLV-SEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHS 234
Cdd:PRK06087 129 TLFKQtrpvdLILPLQNQLPQLQQIVGVdKLAPATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 235 YSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFvhLLPKFDPLVILKTLSSYPIKSMMGA-PI 313
Cdd:PRK06087 209 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDACLALLEQQRCTCMLGAtPF 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 314 VYRML--LQQ---DLSSYKFphlqncVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMV--SKTMKIKPGYMGTA 386
Cdd:PRK06087 287 IYDLLnlLEKqpaDLSALRF------FLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVnlDDPLSRFMHTDGYA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 387 ASCYDVQIIDDKGNVLPPGTEGDigirvKPIRPIGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRANDI 465
Cdd:PRK06087 361 AAGVEIKVVDEARKTLPPGCEGE-----EASRGPNVFMGYLDEPELTARALDEEGWYYsGDLCRMDEAGYIKITGRKKDI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 466 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKEL-QQHVksvtAPYKYPRKI 544
Cdd:PRK06087 436 IVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFsRKRV----AKYKYPEHI 511
|
490 500
....*....|....*....|....*
gi 1034593582 545 EFVLNLPKTVTGKIQRAKLRdKEWK 569
Cdd:PRK06087 512 VVIDKLPRTASGKIQKFLLR-KDIM 535
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
81-574 |
1.13e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 200.90 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:PRK08276 12 VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETgsqEASAIYFTSGTSGLPK----------- 229
Cdd:PRK08276 91 AALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADET---AGADMLYSSGTTGRPKgikrplpgldp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 230 --MAEHSYSSLGLKAKMDAGWTGLQASDIMWTiSDTGWILNILcslmepwALGAcTFVhLLPKFDPLVILKTLSSYPIKS 307
Cdd:PRK08276 168 deAPGMMLALLGFGMYGGPDSVYLSPAPLYHT-APLRFGMSAL-------ALGG-TVV-VMEKFDAEEALALIERYRVTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 308 MMGAPIVY-RML-LQQ------DLSSYKF------PhlqnC-VTVGESLLpetlENWraqtGLDIRESYGQTET-GLTCM 371
Cdd:PRK08276 238 SQLVPTMFvRMLkLPEevraryDVSSLRVaihaaaP----CpVEVKRAMI----DWW----GPIIHEYYASSEGgGVTVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 372 VSKTMKIKPGYMGTAASCyDVQIIDDKGNVLPPGTEGDIGIRvkpiRPIGIFSgYVDNPDKTAANIRGDFWL-LGDRGIK 450
Cdd:PRK08276 306 TSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE----MDGYPFE-YHNDPEKTAAARNPHGWVtVGDVGYL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 451 DEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQ 529
Cdd:PRK08276 380 DEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPAD---GADAgDALAAELIA 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1034593582 530 HVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKA 574
Cdd:PRK08276 457 WLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQRA 501
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-565 |
1.81e-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: 197.52 E-value: 1.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgD 161
Cdd:cd12118 31 TWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV-D 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 EVIQEVDTVASECPSLriKLLVSEKSCDgwlnfkkllneastthhcvetgsqeASAIYFTSGTSGLPKMAEHSYSSLGLK 241
Cdd:cd12118 109 REFEYEDLLAEGDPDF--EWIPPADEWD-------------------------PIALNYTSGTTGRPKGVVYHHRGAYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 242 AKMDAGWTGLQASDI-MWTISD---TGWILnilcslmePWALGACTFVHL-LPKFDPLVILKTLSSYPIKSMMGAPIVYR 316
Cdd:cd12118 162 ALANILEWEMKQHPVyLWTLPMfhcNGWCF--------PWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGAPTVLN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 317 MLLQ-QDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTET---GLTCMVSKT-----------MKIKPG 381
Cdd:cd12118 234 MLANaPPSDARPLPHRVH-VMTAGAPPPAAVLAKMEELGFDVTHVYGLTETygpATVCAWKPEwdelpteerarLKARQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 382 --YMGTAAscydVQIIDDKGNVLPPG---TEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDG 454
Cdd:cd12118 313 vrYVGLEE----VDVLDPETMKPVPRdgkTIGEIVFR-------GniVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 455 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVKS 533
Cdd:cd12118 382 YIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL------KEGAKVTeEEIIAFCRE 455
|
490 500 510
....*....|....*....|....*....|..
gi 1034593582 534 VTAPYKYPRKIEFVlNLPKTVTGKIQRAKLRD 565
Cdd:cd12118 456 HLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
68-564 |
3.52e-56 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 197.21 E-value: 3.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 68 ALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILY 147
Cdd:PRK08008 25 ALIFESSGGVVRRYSYLELNEEINRTANLFY-SLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAW 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 148 RLQMSKAKAIVAGDE---VIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTT-HHCVETGSQEASAIYFTSG 223
Cdd:PRK08008 104 ILQNSQASLLVTSAQfypMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPATlCYAPPLSTDDTAEILFTSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 224 TSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSY 303
Cdd:PRK08008 184 TTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGA-TFV-LLEKYSARAFWGQVCKY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 304 PIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETgLTCMVSKTmkikPG-- 381
Cdd:PRK08008 262 RATITECIPMMIRTLMVQPPSANDRQHCLREVMFYLNLSDQEKDAFEERFGVRLLTSYGMTET-IVGIIGDR----PGdk 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 382 ----YMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPIgiFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYF 456
Cdd:PRK08008 337 rrwpSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTI--FKEYYLDPKATAKVLEADGWLhTGDTGYVDEEGFF 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 457 QFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKE-LQQHVKSVT 535
Cdd:PRK08008 415 YFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN------EGETLSEEeFFAFCEQNM 488
|
490 500
....*....|....*....|....*....
gi 1034593582 536 APYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:PRK08008 489 AKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
83-565 |
1.60e-55 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 198.06 E-value: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI-------FMPGTIQMkstdilyRLQMSKAK 155
Cdd:PRK00174 101 YRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvfggFSAEALAD-------RIIDAGAK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 156 AIVAGDEVI---------QEVDTVASECPSLRiKLLVSEKSC---------DGWLNfkKLLNEASTTHHCVETGSQEASA 217
Cdd:PRK00174 173 LVITADEGVrggkpiplkANVDEALANCPSVE-KVIVVRRTGgdvdwvegrDLWWH--ELVAGASDECEPEPMDAEDPLF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPKMAEHS------YSSLGLKAKMDagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACTfvhllpkf 291
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHTtggylvYAAMTMKYVFD-----YKDGDVYWCTADVGWVTGHSYIVYGPLANGATT-------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 292 dplVILKTLSSYPIKSMMG-------------APIVYRMLLQQ--------DLSSYKFPHlqncvTVGESLLPETLENWR 350
Cdd:PRK00174 317 ---LMFEGVPNYPDPGRFWevidkhkvtifytAPTAIRALMKEgdehpkkyDLSSLRLLG-----SVGEPINPEAWEWYY 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 351 AQTGLD---IRESYGQTETGlTCMVSK---TMKIKPGymgtaaSC------YDVQIIDDKGNVLPPGTEGDIGIRvKP-- 416
Cdd:PRK00174 389 KVVGGErcpIVDTWWQTETG-GIMITPlpgATPLKPG------SAtrplpgIQPAVVDEEGNPLEGGEGGNLVIK-DPwp 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 417 --IRPIgifsgYVDnPD---KTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVET 491
Cdd:PRK00174 461 gmMRTI-----YGD-HErfvKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEA 534
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034593582 492 AVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK00174 535 AVVGRPDDIKGQGIYAFVTLKG---GEEPsDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
81-564 |
6.14e-55 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 196.33 E-value: 6.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGlIFMPGTIQMKSTDILYRLQMSKAKAIVA- 159
Cdd:PRK07529 59 WTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 160 ----GDEVIQEVDTVASECPSLR-----------------IKLLVSEKSCDGWLNFKKLLNEASTTHHCVET--GSQEAS 216
Cdd:PRK07529 137 gpfpGTDIWQKVAEVLAALPELRtvvevdlarylpgpkrlAVPLIRRKAHARILDFDAELARQPGDRLFSGRpiGPDDVA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 217 AIYFTSGTSGLPKMAEHSYSSLglkakMDAGWTGLQASDImwTISDTgwilnILCSL------------MEPWALGAcTF 284
Cdd:PRK07529 217 AYFHTGGTTGMPKLAQHTHGNE-----VANAWLGALLLGL--GPGDT-----VFCGLplfhvnallvtgLAPLARGA-HV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 285 VHLLPK--FDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-----DLSSYKFphlqncVTVGESLLP-ETLENWRAQT 353
Cdd:PRK07529 284 VLATPQgyRGPGVIanfWKIVERYRINFLSGVPTVYAALLQVpvdghDISSLRY------ALCGAAPLPvEVFRRFEAAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 354 GLDIRESYGQTETglTCMVS---KTMKIKPGYMGTAASCYDVQII--DDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVd 428
Cdd:PRK07529 358 GVRIVEGYGLTEA--TCVSSvnpPDGERRIGSVGLRLPYQRVRVVilDDAGRYLRDCAVDEVGVLC--IAGPNVFSGYL- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 429 NPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKA 507
Cdd:PRK07529 433 EAAHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVA 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034593582 508 FVVLA--SQFlshDPEQLTKELQQHVKSVTApykYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:PRK07529 513 YVQLKpgASA---TEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
78-565 |
4.80e-54 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 192.28 E-value: 4.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 78 ELMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 157
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 VAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGW-LNFKKL-LNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSY 235
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpAGWSTApLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 236 SSLGLKAKMDAGWTGLQASDIMWT---ISDTGwILNILCSLMepwaLGACTFVhLLPKF------DPLVILKTLSSYPIK 306
Cdd:PRK06155 203 AQFYWWGRNSAEDLEIGADDVLYTtlpLFHTN-ALNAFFQAL----LAGATYV-LEPRFsasgfwPAVRRHGATVTYLLG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 307 SMMgapivyRMLLQQDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKiKPGYMGTA 386
Cdd:PRK06155 277 AMV------SILLSQPARESDRAHRVR-VALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 387 ASCYDVQIIDDKGNVLPPGTEGDIGIRVKPirPIGIFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRANDI 465
Cdd:PRK06155 349 APGFEARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWR-NLWFhTGDRVVRDADGWFRFVDRIKDA 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 466 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLaSQFLSHDPEqltkELQQHVKSVTAPYKYPRKIE 545
Cdd:PRK06155 426 IRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVL-RDGTALEPV----ALVRHCEPRLAYFAVPRYVE 500
|
490 500
....*....|....*....|
gi 1034593582 546 FVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK06155 501 FVAALPKTENGKVQKFVLRE 520
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
38-569 |
1.17e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 191.79 E-value: 1.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 38 QEVPAKFNFASDVLDHWadMEKAGKRLPS-PALWWVngkGKELmwNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRV 116
Cdd:PRK06710 13 EEIPSTISYDIQPLHKY--VEQMASRYPEkKALHFL---GKDI--TFSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 117 PEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpSLRIKLLVSEKSCDgWLNFKK 196
Cdd:PRK06710 85 PQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQS---ATKIEHVIVTRIAD-FLPFPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 197 LL----------------NEASTTH--HCVE----TG-------SQEASAIYFTSGTSGLPKMAEHSYSSLglkakmdag 247
Cdd:PRK06710 161 NLlypfvqkkqsnlvvkvSESETIHlwNSVEkevnTGvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNL--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 248 wtglqasdIMWTISDTGWILNilCSLMEPWALGACTFVH-------------------LLPKFDPLVILKTLSSYPIKSM 308
Cdd:PRK06710 232 --------VSNTLMGVQWLYN--CKEGEEVVLGVLPFFHvygmtavmnlsimqgykmvLIPKFDMKMVFEAIKKHKVTLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 309 MGAPIVYRMLLQQDL-SSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG-LTCMVSKTMKIKPGYMGTA 386
Cdd:PRK06710 302 PGAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 387 ASCYDVQIID-DKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRAND 464
Cdd:PRK06710 382 WPDTEAMIMSlETGEALPPGEIGEIVVKGPQI-----MKGYWNKPEETAAVLQ-DGWLhTGDVGYMDEDGFFYVKDRKKD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 465 IINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqfLSHDPEQLTKELQQHVKSVTAPYKYPRKI 544
Cdd:PRK06710 456 MIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVV-----LKEGTECSEEELNQFARKYLAAYKVPKVY 530
|
570 580
....*....|....*....|....*
gi 1034593582 545 EFVLNLPKTVTGKIQRAKLRDKEWK 569
Cdd:PRK06710 531 EFRDELPKTTVGKILRRVLIEEEKR 555
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
83-564 |
1.29e-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: 188.36 E-value: 1.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:cd05903 4 YSELDTRADRLAAGLA-ALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viqevdtvasecpslrikllvsekscdgwlnFKKllneasttHHCVETGSQEAsAIYFTSGTSGLPKMAEHSYSSLGLKA 242
Cdd:cd05903 83 -------------------------------FRQ--------FDPAAMPDAVA-LLLFTSGTTGEPKGVMHSHNTLSASI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 243 KMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACtfVHLLPKFDPLVILKTLSSYPIKSMMGA-PIVYRMLLQQ 321
Cdd:cd05903 123 RQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAP--VVLQDIWDPDKALALMREHGVTFMMGAtPFLTDLLNAV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 322 DLSSYKFPHLQnCVTVGESLLPETLENwRAQT--GLDIRESYGQTETGltcmvSKTMKIKPGYMGtAASCYD-------- 391
Cdd:cd05903 201 EEAGEPLSRLR-TFVCGGATVPRSLAR-RAAEllGAKVCSAYGSTECP-----GAVTSITPAPED-RRLYTDgrplpgve 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 392 VQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGY 471
Cdd:cd05903 273 IKVVDDTGATLAPGVEGELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 472 RIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVKSV-TAPYKYPRKIEFVLN 549
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVT------KSGALLTfDELVAYLDRQgVAKQYWPERLVHVDD 421
|
490
....*....|....*
gi 1034593582 550 LPKTVTGKIQRAKLR 564
Cdd:cd05903 422 LPRTPSGKVQKFRLR 436
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
60-576 |
2.07e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 187.12 E-value: 2.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 60 AGKRLPS-PALWWVNGKgkelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVI-----LGCIRAGLIF 133
Cdd:PRK06188 21 ALKRYPDrPALVLGDTR-----LTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMAIgaaqlAGLRRTALHP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 134 MpGTIQmkstDILYRLQMSKAKAIVAGDEVIQE-VDTVASECPSLRIKLLVSEksCDGWLNFKKLLNEASTTHHCVETGS 212
Cdd:PRK06188 95 L-GSLD----DHAYVLEDAGISTLIVDPAPFVErALALLARVPSLKHVLTLGP--VPDGVDLLAAAAKFGPAPLVAAALP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 213 QEASAIYFTSGTSGLPKMAEHSYSSLglkakmdAGWTGLQASDIMWT----------ISDTGWILnILCSLMEpwalGAc 282
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRSI-------ATMAQIQLAEWEWPadprflmctpLSHAGGAF-FLPTLLR----GG- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 283 tFVHLLPKFDPLVILKTLSSYPIKSMMGAP-IVYRMLLQQDLSSYKFPHLQNCVTVGESLLPEtlenwRAQTGLDI---- 357
Cdd:PRK06188 235 -TVIVLAKFDPAEVLRAIEEQRITATFLVPtMIYALLDHPDLRTRDLSSLETVYYGASPMSPV-----RLAEAIERfgpi 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 358 -RESYGQTETGLTCMVSKTMKIKPGYMGTAASC------YDVQIIDDKGNVLPPGTEGDIGIRvKPIrpigIFSGYVDNP 430
Cdd:PRK06188 309 fAQYYGQTEAPMVITYLRKRDHDPDDPKRLTSCgrptpgLRVALLDEDGREVAQGEVGEICVR-GPL----VMDGYWNRP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 431 DKTAANIRGDfWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFV 509
Cdd:PRK06188 384 EETAEAFRDG-WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034593582 510 VLASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWkmSGKARA 576
Cdd:PRK06188 463 VLRPG-AAVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYW--EGRGRA 522
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-565 |
1.59e-51 |
|
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: 184.76 E-value: 1.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSGAcGLQRGDRVAVVL---PRVPEWWLVILGcirAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 158
Cdd:cd12119 27 TYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYAVPG---MGAVLHTINPRLFPEQIAYIINHAEDRVVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 159 AGDEVIQEVDTVASECPSLRIKLLVS------EKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 232
Cdd:cd12119 103 VDRDFLPLLEAIAPRLPTVEHVVVMTddaampEPAGVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 233 HSYSSLGLKA--KMDAGWTGLQASDIMWTISD----TGWILNILCSLmepwaLGACtfvHLLP--KFDPLVILKTLSSYP 304
Cdd:cd12119 183 YSHRSLVLHAmaALLTDGLGLSESDVVLPVVPmfhvNAWGLPYAAAM-----VGAK---LVLPgpYLDPASLAELIEREG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 305 IKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSK--------- 374
Cdd:cd12119 255 VTFAAGVPTVWQGLLDhLEANGRDLSSLRR-VVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARppsehsnls 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 375 -----TMKIKPGYmgtaaSCYDVQ--IIDDKGNVLP--PGTEGDIGIRvKPIrpigIFSGYVDNPDKTAANIRGDFWLLG 445
Cdd:cd12119 334 edeqlALRAKQGR-----PVPGVElrIVDDDGRELPwdGKAVGELQVR-GPW----VTKSYYKNDEESEALTEDGWLRTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 446 DRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT- 524
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLK------EGATVTa 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1034593582 525 KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:cd12119 478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
78-565 |
2.01e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 185.36 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 78 ELMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 157
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 VAGD--------EVIQEV--DTVASEC--------PSLRIKLLVSEKSCDGWLNFKKLLNEAST-THHCVETGSQ----- 213
Cdd:PRK12583 122 ICADafktsdyhAMLQELlpGLAEGQPgalacerlPELRGVVSLAPAPPPGFLAWHELQARGETvSREALAERQAsldrd 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 214 EASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDT----GWIL-NILCSlmepwALGACTfvhLL 288
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhcfGMVLaNLGCM-----TVGACL---VY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 289 PK--FDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGL-DIRESYGQT 364
Cdd:PRK12583 274 PNeaFDPLATLQAVEEERCTALYGVPTMFIAELDHpQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 365 ETG----LTCmVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD 440
Cdd:PRK12583 354 ETSpvslQTT-AADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTR-----GYSVMKGYWNNPEATAESIDED 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 441 FWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHD 519
Cdd:PRK12583 428 GWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRL------HP 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1034593582 520 PEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK12583 502 GHAASeEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
76-563 |
2.15e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 181.21 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 76 GKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAK 155
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 156 AIVAGDE---VIQEVDTVASECPSLRIKLL--VSEKSCDGWlnfkkllneastthhcVETGSQEASAIYFTSGTSGLPKM 230
Cdd:PRK06839 103 VLFVEKTfqnMALSMQKVSYVQRVISITSLkeIEDRKIDNF----------------VEKNESASFIICYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 231 AEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHllPKFDPLVILKTLSSYPIKSMMG 310
Cdd:PRK06839 167 AVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVP--RKFEPTKALSMIEKHKVTVVMG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 311 APIVYRMLLQQdlSSYKFPHLQNC--VTVGESLLPETLENWRAQTGLDIRESYGQTETGLTC-MVSKT-MKIKPGYMGTA 386
Cdd:PRK06839 245 VPTIHQALINC--SKFETTNLQSVrwFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVfMLSEEdARRKVGSIGKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 387 ASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDII 466
Cdd:PRK06839 323 VLFCDYELIDENKNKVEVGEVGELLIR-GP----NVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 467 NSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDpeqltKELQQHVKSVTAPYKYPRKIEF 546
Cdd:PRK06839 398 ISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPKEIVF 472
|
490
....*....|....*..
gi 1034593582 547 VLNLPKTVTGKIQRAKL 563
Cdd:PRK06839 473 LKELPKNATGKIQKAQL 489
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
76-565 |
5.91e-50 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 181.37 E-value: 5.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 76 GKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMpgtiqmkSTDILY-------R 148
Cdd:PRK07059 46 GKAI--TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV-------NVNPLYtprelehQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 149 LQMSKAKAIV-------AGDEVIQEVDT----VASECPSL------------RIKLLVSEKSCDGWLNFKKLLNE-ASTT 204
Cdd:PRK07059 116 LKDSGAEAIVvlenfatTVQQVLAKTAVkhvvVASMGDLLgfkghivnfvvrRVKKMVPAWSLPGHVRFNDALAEgARQT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 205 HHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS-LGLKAKMDAgWtgLQASDIMWTISDTgwiLNILCSLmeP----WAL 279
Cdd:PRK07059 196 FKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNiVANVLQMEA-W--LQPAFEKKPRPDQ---LNFVCAL--PlyhiFAL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 280 GACTFVH--------LLPkfDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLE 347
Cdd:PRK07059 268 TVCGLLGmrtggrniLIP--NPRDIpgfIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 348 NWRAQTGLDIRESYGQTETG--LTCMVSKTMKIKpGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IF 423
Cdd:PRK07059 346 RWLEMTGCPITEGYGLSETSpvATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-------GpqVM 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 424 SGYVDNPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRG 502
Cdd:PRK07059 418 AGYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSG 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034593582 503 EVVKAFVVlasqflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK07059 498 EAVKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
75-566 |
6.53e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 180.74 E-value: 6.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 75 KGKELMWnfRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKA 154
Cdd:PRK07786 39 LGNTTTW--RELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 155 KAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHS 234
Cdd:PRK07786 116 HVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 235 YSSLGLKAKMDA-GWTGLQASDI------MWTISDTGwilNILCSLMepwaLGACTFVHLLPKFDPLVILKTLSSYPIKS 307
Cdd:PRK07786 196 HANLTGQAMTCLrTNGADINSDVgfvgvpLFHIAGIG---SMLPGLL----LGAPTVIYPLGAFDPGQLLDVLEAEKVTG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 308 MMGAPIVYRMLL------QQDLSsykfphLQNcVTVGESLLPETLENWRAQT--GLDIRESYGQTE-TGLTCMVSKTMKI 378
Cdd:PRK07786 269 IFLVPAQWQAVCaeqqarPRDLA------LRV-LSWGAAPASDTLLRQMAATfpEAQILAAFGQTEmSPVTCMLLGEDAI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 379 -KPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQ 457
Cdd:PRK07786 342 rKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP-----TLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 458 FMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLT-KELQQHVKSVTA 536
Cdd:PRK07786 417 VVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN-----DDAALTlEDLAEFLTDRLA 491
|
490 500 510
....*....|....*....|....*....|
gi 1034593582 537 PYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 566
Cdd:PRK07786 492 RYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
102-564 |
4.72e-49 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 176.48 E-value: 4.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 102 GLQRGDRVAVVLPRVPEWWLVILGCIRAG----LIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSL 177
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 178 RIKLLVsekscDGWLNfkkllNEASTTHHCVEtgSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIM 257
Cdd:cd05922 94 GTVLDA-----DGIRA-----ARASAPAHEVS--HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 258 WTISDTGWI--LNILCSLMEpwaLGACTFVHLLPKFDPLVIlKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCV 335
Cdd:cd05922 162 LTVLPLSYDygLSVLNTHLL---RGATLVLTNDGVLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 336 TVGESLLPETLENWR-AQTGLDIRESYGQTET--GLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGI 412
Cdd:cd05922 238 QAGGRLPQETIARLReLLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 413 RvkpiRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETA 492
Cdd:cd05922 318 R----GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034593582 493 VISSPDPVrGEVVKAFVVLasqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd05922 394 AVGLPDPL-GEKLALFVTA-------PDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
76-573 |
5.89e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 178.42 E-value: 5.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 76 GKELmwNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAK 155
Cdd:PRK05677 47 GKTL--TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 156 AIVA-------GDEVIQE-------VDTVASECPSLR----------IKLLVSEKSCDGWLNFKKLLNE-ASTTHHCVET 210
Cdd:PRK05677 125 ALVClanmahlAEKVLPKtgvkhviVTEVADMLPPLKrllinavvkhVKKMVPAYHLPQAVKFNDALAKgAGQPVTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 211 GSQEASAIYFTSGTSGLPK--MAEHSysslGLKAKMdagwtgLQASDIMwtisdtGWILNILCS-LMEPWALG------- 280
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKgaMLTHR----NLVANM------LQCRALM------GSNLNEGCEiLIAPLPLYhiyaftf 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 281 ACTFVHLLPKFDPLV--------ILKTLSSYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENWRA 351
Cdd:PRK05677 269 HCMAMMLIGNHNILIsnprdlpaMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 352 QTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPD 431
Cdd:PRK05677 349 VTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GP----QVMKGYWQRPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 432 KTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVV 510
Cdd:PRK05677 424 ATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVV 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034593582 511 LASQflshdpEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGK 573
Cdd:PRK05677 504 VKPG------ETLTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAGL 561
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
66-563 |
9.29e-49 |
|
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: 175.41 E-value: 9.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 66 SPALWWVNGKgkelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdi 145
Cdd:cd05930 3 AVAVVDGDQS-----LTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVP---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 146 lyrlqmskakaivagdeviqeVDTvasECPSLRIKLLVSEkscdgwlnfkkllneasTTHHCVETGSQEASAIYFTSGTS 225
Cdd:cd05930 67 ---------------------LDP---SYPAERLAYILED-----------------SGAKLVLTDPDDLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 226 GLPK--MAEH-SYSSLgLKAKMDAgwTGLQASDIMWTISDTGWILnilcSLME---PWALGACtfVHLLPK---FDPLVI 296
Cdd:cd05930 106 GKPKgvMVEHrGLVNL-LLWMQEA--YPLTPGDRVLQFTSFSFDV----SVWEifgALLAGAT--LVVLPEevrKDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 297 LKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPHLQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTET--GLTCMVS 373
Cdd:cd05930 177 ADLLAEEGITVLHLTPSLLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtvDATYYRV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 374 KTMKIKPGYM--GTAASCYDVQIIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVDNPDKTAANIRGDFWLL---- 444
Cdd:cd05930 256 PPDDEEDGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELyigGA--------GLARGYLNRPELTAERFVPNPFGPgerm 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 445 ---GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflsHDPE 521
Cdd:cd05930 328 yrtGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPD-----EGGE 402
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1034593582 522 QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd05930 403 LDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
82-564 |
6.05e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 174.43 E-value: 6.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 EVIQEVDTVASECPsLRIKLlvsEKSCDGWLNFKKLLNEAS---TTHHCvetgsqeASAIYFTSGTSGLPKMAEHSYSSL 238
Cdd:PRK13390 105 ALDGLAAKVGADLP-LRLSF---GGEIDGFGSFEAALAGAGprlTEQPC-------GAVMLYSSGTTGFPKGIQPDLPGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 239 GLKAKMD------AGWTGLQASDIMWT------ISDTGWilnilCSLMEpwALGACtfVHLLPKFDPLVILKTLSSYPIK 306
Cdd:PRK13390 174 DVDAPGDpivaiaRAFYDISESDIYYSsapiyhAAPLRW-----CSMVH--ALGGT--VVLAKRFDAQATLGHVERYRIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 307 SMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESL---LPETLENWraqTGLDIRESYGQTET-GLTCMVSKTMKIK 379
Cdd:PRK13390 245 VTQMVPTMFVRLLKLDadvRTRYDVSSLRAVIHAAAPCpvdVKHAMIDW---LGPIVYEYYSSTEAhGMTFIDSPDWLAH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 380 PGYMGTAAsCYDVQIIDDKGNVLPPGTEGDIGIRvkpiRPIGIFSgYVDNPDKTAA--NIRGDFWL-LGDRGIKDEDGYF 456
Cdd:PRK13390 322 PGSVGRSV-LGDLHICDDDGNELPAGRIGTVYFE----RDRLPFR-YLNDPEKTAAaqHPAHPFWTtVGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 457 QFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDP-EQLTKELQQHVKSVT 535
Cdd:PRK13390 396 YLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI---RGsDELARELIDYTRSRI 472
|
490 500
....*....|....*....|....*....
gi 1034593582 536 APYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:PRK13390 473 AHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
83-563 |
1.89e-47 |
|
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: 173.19 E-value: 1.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgde 162
Cdd:cd05904 35 YAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viqeVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPK--MAEHSysslG 239
Cdd:cd05904 111 ----TAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQdDVAALLYSSGTTGRSKgvMLTHR----N 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 240 LKAkMDAGWTGLQASDI-----------MWTISDTGWILniLCSLmepwALGACTFVhlLPKFDPLVILKTLSSYPIKSM 308
Cdd:cd05904 183 LIA-MVAQFVAGEGSNSdsedvflcvlpMFHIYGLSSFA--LGLL----RLGATVVV--MPRFDLEELLAAIERYKVTHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 309 MGAP-IVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTETG---LTCMVSKTMKIKPGYM 383
Cdd:cd05904 254 PVVPpIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTESTgvvAMCFAPEKDRAKYGSV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 384 GTAASCYDVQIID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR 461
Cdd:cd05904 334 GRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGYLNNPEATAATIDKEGWLhTGDLCYIDEDGYLFIVDR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 462 ANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQ-FLSHDpeqltkELQQHVKSVTAPYKY 540
Cdd:cd05904 409 LKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGsSLTED------EIMDFVAKQVAPYKK 482
|
490 500
....*....|....*....|...
gi 1034593582 541 PRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd05904 483 VRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
267-560 |
5.11e-47 |
|
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: 167.83 E-value: 5.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 267 LNILCSLMEpwaLGACTFVhlLPKFDPLVILKTLSSYPIkSMMG--APIVYRMLLQQDLSSYKFPHLQNcvtVGESLLPE 344
Cdd:cd17637 56 LNLALATFH---AGGANVV--MEKFDPAEALELIEEEKV-TLMGsfPPILSNLLDAAEKSGVDLSSLRH---VLGLDAPE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 345 TLENWRAQTGLDIRESYGQTET-GLTCMVSKTMKikPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIF 423
Cdd:cd17637 127 TIQRFEETTGATFWSLYGQTETsGLVTLSPYRER--PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR-GP----LVF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 424 SGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGR--ANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 501
Cdd:cd17637 200 QGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKW 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 502 GEVVKAFVVL-ASQFLShdpeqlTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd17637 280 GEGIKAVCVLkPGATLT------ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
62-560 |
2.47e-46 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 172.44 E-value: 2.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 62 KRLPSPALWWVNGK-GKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI-------F 133
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfggF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 134 mpgtiqmKSTDILYRLQMSKAKAIV---AG-------------DEVIQE----------VDTVASECP----------SL 177
Cdd:PRK10524 144 -------ASHSLAARIDDAKPVLIVsadAGsrggkvvpykpllDEAIALaqhkprhvllVDRGLAPMArvagrdvdyaTL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 178 RIKLLVSEKSCDgWLNfkkllneastthhcvetgSQEASAIYFTSGTSGLPKMAEHS---YSsLGLKAKMDAGWTGlQAS 254
Cdd:PRK10524 217 RAQHLGARVPVE-WLE------------------SNEPSYILYTSGTTGKPKGVQRDtggYA-VALATSMDTIFGG-KAG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 255 DIMWTISDTGWILNILCSLMEPWALGACTFVH----LLPkfDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYK 327
Cdd:PRK10524 276 ETFFCASDIGWVVGHSYIVYAPLLAGMATIMYeglpTRP--DAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 328 FPHLQNCVTVGESLlPETLENWRAQT-GLDIRESYGQTETGLTCMVS----KTMKIKPGYMGTAASCYDVQIIDDK-GNV 401
Cdd:PRK10524 354 LSSLRALFLAGEPL-DEPTASWISEAlGVPVIDNYWQTETGWPILAIargvEDRPTRLGSPGVPMYGYNVKLLNEVtGEP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 402 LPPGTEGDIGIRvkPIRPIGIFSgyvdnpdktaaNIRGD-------FWLLGDR--------GIKDEDGYFQFMGRANDII 466
Cdd:PRK10524 433 CGPNEKGVLVIE--GPLPPGCMQ-----------TVWGDddrfvktYWSLFGRqvystfdwGIRDADGYYFILGRTDDVI 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 467 NSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQ---LTKELQQHVKSVTAPYKYPRK 543
Cdd:PRK10524 500 NVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPAR 579
|
570
....*....|....*..
gi 1034593582 544 IEFVLNLPKTVTGKIQR 560
Cdd:PRK10524 580 VWFVSALPKTRSGKLLR 596
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
83-567 |
2.07e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 168.57 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLsGACGLQRGDRVAVvLPRVPEWWLV-ILGCIRAGL-IFMPGT----IQMKstDILYRLqmsKAKA 156
Cdd:PRK07788 77 YAELDEQSNALARGL-LALGVRAGDGVAV-LARNHRGFVLaLYAAGKVGArIILLNTgfsgPQLA--EVAARE---GVKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 157 IVAGDEVIQEVDTVASECPSLRIKLLVSEK---SCDGWLNFKKLLneASTTHHCVETGSQEASAIYFTSGTSGLPKMAEH 233
Cdd:PRK07788 150 LVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLI--AGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 234 ----SYSSLG-------LKAKMdagwTGLQASDIMWTisdTGW-ILNIlcslmePWALGaCTFVhLLPKFDPLVILKTLS 301
Cdd:PRK07788 228 pepsPLAPLAgllsrvpFRAGE----TTLLPAPMFHA---TGWaHLTL------AMALG-STVV-LRRRFDPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 302 SYPIKSMMGAPIVYRMLLQQ--------DLSSYKFphlqnCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS 373
Cdd:PRK07788 293 KHKATALVVVPVMLSRILDLgpevlakyDTSSLKI-----IFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIAT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 374 -KTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVkpirpiGI-FSGYVDNPDKtaANIRGdfwLL--GDRGI 449
Cdd:PRK07788 368 pEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGN------GFpFEGYTDGRDK--QIIDG---LLssGDVGY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 450 KDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKE-LQ 528
Cdd:PRK07788 437 FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKA------PGAALDEDaIK 510
|
490 500 510
....*....|....*....|....*....|....*....
gi 1034593582 529 QHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKE 567
Cdd:PRK07788 511 DYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
81-570 |
2.57e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 167.06 E-value: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGC--IRAGLIFMPGTIQMKstDILYRLQMSKAKAIV 158
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALqqLGAVAVLLNTRLSRE--ELLWQLDDAEVKCLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 159 AGDEVIQEVDTVA----SECPSLRIKLLVSEKSCDgwlnfkklLNEASTthhcvetgsqeasaIYFTSGTSGLPKMAEHS 234
Cdd:PRK03640 105 TDDDFEAKLIPGIsvkfAELMNGPKEEAEIQEEFD--------LDEVAT--------------IMYTSGTTGKPKGVIQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 235 Y---------SSLGLkakmdagwtGLQASDiMWTISDTgwILNI--LCSLMEPWALGaCTfVHLLPKFDPLVILKTLSSY 303
Cdd:PRK03640 163 YgnhwwsavgSALNL---------GLTEDD-CWLAAVP--IFHIsgLSILMRSVIYG-MR-VVLVEKFDAEKINKLLQTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 304 PIkSMMGApiVYRML--LQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGltcmvSKTMKIKPG 381
Cdd:PRK03640 229 GV-TIISV--VSTMLqrLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETA-----SQIVTLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 382 YM----GTAAS-CYDVQI-IDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAANIRgDFWL-LGDRGIKDEDG 454
Cdd:PRK03640 301 DAltklGSAGKpLFPCELkIEKDGVVVPPFEEGEIVVKGPNVTK-----GYLNREDATRETFQ-DGWFkTGDIGYLDEEG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 455 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshdPEQltkELQQHVKSV 534
Cdd:PRK03640 375 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEV----TEE---ELRHFCEEK 447
|
490 500 510
....*....|....*....|....*....|....*.
gi 1034593582 535 TAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKM 570
Cdd:PRK03640 448 LAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
100-564 |
4.25e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 165.93 E-value: 4.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 100 ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgdeviqEVDTVASECPSLRI 179
Cdd:PRK07787 39 AERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLG------PAPDDPAGLPHVPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 180 KLlvsekscdgwlnfkkllnEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL--GLKAKMDAgWTglqasdim 257
Cdd:PRK07787 113 RL------------------HARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIaaDLDALAEA-WQ-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 258 WTISDT-----------GWILNILCSLMepwaLGAcTFVHLLpKFDPLVILKTLSSYpiKSMM-GAPIVYRMLLQQDLSS 325
Cdd:PRK07787 166 WTADDVlvhglplfhvhGLVLGVLGPLR----IGN-RFVHTG-RPTPEAYAQALSEG--GTLYfGVPTVWSRIAADPEAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 326 YKFPHLQNCVTvGESLLPET-LENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPP 404
Cdd:PRK07787 238 RALRGARLLVS-GSAALPVPvFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 405 GTE--GDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR-ANDIINSSGYRIGPSEVEN 480
Cdd:PRK07787 317 DGEtvGELQVR-GP----TLFDGYLNRPDATAAAFTADGWFrTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 481 ALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflSHDPEQLTkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:PRK07787 392 ALLGHPGVREAAVVGVPDDDLGQRIVAYVV------GADDVAAD-ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLK 464
|
....
gi 1034593582 561 AKLR 564
Cdd:PRK07787 465 KQLL 468
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
48-565 |
6.62e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 167.48 E-value: 6.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 48 SDVLDHwaDMEKAGKRlpsPALWWVngkGKELMWnfRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCI 127
Cdd:PRK05605 35 VDLYDN--AVARFGDR---PALDFF---GATTTY--AELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 128 RAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV---IQE------VDTVAS-----------------ECPSLRIKL 181
Cdd:PRK05605 104 RLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVaptVERlrrttpLETIVSvnmiaampllqrlalrlPIPALRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 182 LVSEKSCDGWLNFKKLLNEA----STTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASD- 255
Cdd:PRK05605 184 AALTGPAPGTVPWETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVpGLGDGPe 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 256 IMWTI----SDTGWILNILCSLMepwaLGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ------DLSS 325
Cdd:PRK05605 264 RVLAAlpmfHAYGLTLCLTLAVS----IGG-ELV-LLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvDLSG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 326 ykfphLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCM---VSKTMKikPGYMGTAASCYDVQIID--DKGN 400
Cdd:PRK05605 338 -----VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVgnpMSDDRR--PGYVGVPFPDTEVRIVDpeDPDE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 401 VLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEV 478
Cdd:PRK05605 411 TMPDGEEGELLVR-------GpqVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 479 ENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 558
Cdd:PRK05605 484 EEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPE----GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
....*..
gi 1034593582 559 QRAKLRD 565
Cdd:PRK05605 559 RRREVRE 565
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
39-574 |
6.85e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 167.15 E-value: 6.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 39 EVPAKFNfaSDVLDHWADM-EKAGKRLPS-PAlwWVNgKGKELmwNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRV 116
Cdd:PRK08974 12 DVPAEIN--PDRYQSLVDMfEQAVARYADqPA--FIN-MGEVM--TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 117 PEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECP------------------SL- 177
Cdd:PRK08974 85 LQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPvkhviltrmgdqlstakgTLv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 178 -----RIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASA-IYFTSGTSGLPK--MAEH------------SYSS 237
Cdd:PRK08974 165 nfvvkYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAfLQYTGGTTGVAKgaMLTHrnmlanleqakaAYGP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 238 LgLKAKMDAGWTGLQASDImwtisdtgWILNILCSL-MEpwaLGACTFVHLLPKFDPLVIlKTLSSYPIKSMMGAPIVYR 316
Cdd:PRK08974 245 L-LHPGKELVVTALPLYHI--------FALTVNCLLfIE---LGGQNLLITNPRDIPGFV-KELKKYPFTAITGVNTLFN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 317 MLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQI 394
Cdd:PRK08974 312 ALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 395 IDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGY 471
Cdd:PRK08974 392 VDDDGNEVPPGEPGELWVK-------GpqVMLGYWQRPEATDEVIK-DGWLaTGDIAVMDEEGFLRIVDRKKDMILVSGF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 472 RIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLP 551
Cdd:PRK08974 464 NVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEE------ELITHCRRHLTGYKVPKLVEFRDELP 537
|
570 580
....*....|....*....|...
gi 1034593582 552 KTVTGKIQRAKLRDKEWKMSGKA 574
Cdd:PRK08974 538 KSNVGKILRRELRDEARAKVDNK 560
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
102-565 |
7.18e-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: 166.55 E-value: 7.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 102 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLR-IK 180
Cdd:cd17642 65 GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKtII 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 181 LLVSEKSCDGWL---NFKK-----LLNEASTTHHCVETGSQeASAIYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQ 252
Cdd:cd17642 145 ILDSKEDYKGYQclyTFITqnlppGFNEYDFKPPSFDRDEQ-VALIMNSSGSTGLPKGVQLTHKNI--VARFSHARDPIF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 253 ASDIMWTISdtgwILNILcslmePWALG----------ACTF-VHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ 321
Cdd:cd17642 222 GNQIIPDTA----ILTVI-----PFHHGfgmfttlgylICGFrVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 322 DL-SSYKFPHLQNCVTVGESLLPETLENWRAQTGLD-IRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIID-DK 398
Cdd:cd17642 293 TLvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDT 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 399 GNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSE 477
Cdd:cd17642 373 GKTLGPNERGELCVKGP-----MIMKGYVNNPEATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 478 VENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLT-KELQQHVKSVTAPYKYPR-KIEFVLNLPKTVT 555
Cdd:cd17642 448 LESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAG------KTMTeKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLT 521
|
490
....*....|
gi 1034593582 556 GKIQRAKLRD 565
Cdd:cd17642 522 GKIDRRKIRE 531
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
81-565 |
9.82e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 165.37 E-value: 9.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVvLPRVPEWWLVI-LGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVa 159
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRRR-GCVDGERLAV-LARNSVWLVALhFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 160 GDEVIQevdtvASECPSLRIKLLVSEKSCDGWLNFKKLLNEAstthhcvetgsqeASAIYFTSGTSGLPKMA-------E 232
Cdd:PRK09088 100 GDDAVA-----AGRTDVEDLAAFIASADALEPADTPSIPPER-------------VSLILFTSGTSGQPKGVmlsernlQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 233 HSYSSLGLKAKMDAGWTGLQASDIMWTIsdtGWILNILCSLMEpwalGACTFVHllPKFDPLVILKTLS--SYPIKSMMG 310
Cdd:PRK09088 162 QTAHNFGVLGRVDAHSSFLCDAPMFHII---GLITSVRPVLAV----GGSILVS--NGFEPKRTLGRLGdpALGITHYFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 311 APIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQtGLDIRESYGQTETGLTCMVSKTMKI---KPGYMGTA 386
Cdd:PRK09088 233 VPQMAQAFRAQpGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDViraKAGAAGIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 387 ASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDI 465
Cdd:PRK09088 312 TPTVQTRVVDDQGNDCPAGVPGELLLRGP-----NLSPGYWRRPQATARAFTGDGWFrTGDIARRDADGFFWVVDRKKDM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 466 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIE 545
Cdd:PRK09088 387 FISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-APLDLE----RIRSHLSTRLAKYKVPKHLR 461
|
490 500
....*....|....*....|
gi 1034593582 546 FVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK09088 462 LVDALPRTASGKLQKARLRD 481
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
81-577 |
9.84e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 166.91 E-value: 9.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMpgTIQ--MKSTDILYRLQMSKAKAIV 158
Cdd:PRK08315 44 WTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV--TINpaYRLSELEYALNQSGCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 159 AGDEV-----IQEVDTVASEC-------------PSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHcVETGSQEASA--- 217
Cdd:PRK08315 121 AADGFkdsdyVAMLYELAPELatcepgqlqsarlPELRRVIFLGDEKHPGMLNFDELLALGRAVDD-AELAARQATLdpd 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 ----IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASD---I---------MwtisdtgwILNILCSLmepwALGA 281
Cdd:PRK08315 200 dpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrlcIpvplyhcfgM--------VLGNLACV----THGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 282 CTfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCVTVGeSLLP-ETLEnwRAQTGLDIRE 359
Cdd:PRK08315 268 TM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLRTGIMAG-SPCPiEVMK--RVIDKMHMSE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 360 ---SYGQTETG-LTCM----------VSKTMKIKPGYmgtaascyDVQIID-DKGNVLPPGTEGDIGIRvkpirpiG--I 422
Cdd:PRK08315 344 vtiAYGMTETSpVSTQtrtddplekrVTTVGRALPHL--------EVKIVDpETGETVPRGEQGELCTR-------GysV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 423 FSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 501
Cdd:PRK08315 409 MKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKY 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034593582 502 GEVVKAFVVLasqflsHDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKARAQ 577
Cdd:PRK08315 489 GEEVCAWIIL------RPGATLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGLQAAK 559
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
81-565 |
1.09e-44 |
|
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: 163.67 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKaivag 160
Cdd:cd05912 2 YTFAELFEEVSRLAEHL-AALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 deviqeVDTVASecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAE-----HSY 235
Cdd:cd05912 76 ------LDDIAT---------------------------------------------IMYTSGTTGKPKGVQqtfgnHWW 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 236 SSLGLKAKMdagwtGLQASDI------MWTISDtgwiLNILC-SLMEpwalgACTfVHLLPKFDPLVILKTLSSYPIKSM 308
Cdd:cd05912 105 SAIGSALNL-----GLTEDDNwlcalpLFHISG----LSILMrSVIY-----GMT-VYLVDKFDAEQVLHLINSGKVTII 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 309 MGAPIVYRMLLQQDLSSYKfPHLQnCVTVGESLLPETLENWRAQTGLDIRESYGQTETgltCMVSKTMKI-----KPGYM 383
Cdd:cd05912 170 SVVPTMLQRLLEILGEGYP-NNLR-CILLGGGPAPKPLLEQCKEKGIPVYQSYGMTET---CSQIVTLSPedalnKIGSA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 384 GTAASCYDVQIIDDKGnvlPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRAN 463
Cdd:cd05912 245 GKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTK-----GYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 464 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDPEQLTKELQQHVksvtAPYKYPRK 543
Cdd:cd05912 317 DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKL----AKYKVPKK 389
|
490 500
....*....|....*....|..
gi 1034593582 544 IEFVLNLPKTVTGKIQRAKLRD 565
Cdd:cd05912 390 IYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
83-565 |
1.39e-44 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 166.59 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:PRK08751 53 YREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 VIQEVDTVASECPSLR------------------------IKLLVSEKSCDGWLNFKKLLneASTTHHCVETGSQEASAI 218
Cdd:PRK08751 133 FGTTVQQVIADTPVKQvittglgdmlgfpkaalvnfvvkyVKKLVPEYRINGAIRFREAL--ALGRKHSMPTLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 219 YF---TSGTSGLPKMAEHSYSSLGLKAKMDAGWTG-----LQASDIMWTISDTGWILNILCSLMEPWALGACTfvHLL-- 288
Cdd:PRK08751 211 AFlqyTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEVVITALPLYHIFALTANGLVFMKIGGCN--HLIsn 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 289 PKFDPLVIlKTLSSYPIKSMMGAPIVYRMLL------QQDLSSYKFPhLQNCVTVGESLlpetLENWRAQTGLDIRESYG 362
Cdd:PRK08751 289 PRDMPGFV-KELKKTRFTAFTGVNTLFNGLLntpgfdQIDFSSLKMT-LGGGMAVQRSV----AERWKQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 363 QTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDF 441
Cdd:PRK08751 363 LTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-GP----QVMKGYWKRPEETAKVMDADG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 442 WL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflSHDP 520
Cdd:PRK08751 438 WLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------KKDP 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1034593582 521 EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK08751 512 ALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
57-566 |
3.52e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 164.83 E-value: 3.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 57 MEKAGKRLPS-PALWWvngkgKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMP 135
Cdd:PRK07470 13 LRQAARRFPDrIALVW-----GDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 136 GTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRikLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEA 215
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLT--HVVAIGGARAGLDYEALVARHLGARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 216 SAIYF-TSGTSGLPKMAEHSYSSLGL-----KAKMDAGWTGLQASDIMWTISDtGWILNILCSLmepwALGACTFVHLLP 289
Cdd:PRK07470 165 PCWFFfTSGTTGRPKAAVLTHGQMAFvitnhLADLMPGTTEQDASLVVAPLSH-GAGIHQLCQV----ARGAATVLLPSE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 290 KFDPLVILKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPH--LQNCVTVGESLLPETLENWRAQTGLDIRESYGQTEtg 367
Cdd:PRK07470 240 RFDPAEVWALVERHRVTNLFTVPTILKMLVE-HPAVDRYDHssLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGE-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 368 ltcmVSKTMKIKPGYM-----GTAA---SC------YDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKT 433
Cdd:PRK07470 317 ----VTGNITVLPPALhdaedGPDArigTCgfertgMEVQIQDDEGRELPPGETGEICVIGPAV-----FAGYYNNPEAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 434 AANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLas 513
Cdd:PRK07470 388 AKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA-- 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1034593582 514 qflsHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 566
Cdd:PRK07470 466 ----RDGAPVDEaELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
83-565 |
4.35e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 164.99 E-value: 4.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD- 161
Cdd:PRK12492 52 YAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNm 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 --EVIQEVdtvaseCPSLRIKLLVSEKSCD------GWL---------------------NFKKLLNE-ASTTHHCVETG 211
Cdd:PRK12492 132 fgKLVQEV------LPDTGIEYLIEAKMGDllpaakGWLvntvvdkvkkmvpayhlpqavPFKQALRQgRGLSLKPVPVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 212 SQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGA---CTFV--- 285
Cdd:PRK12492 206 LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEGQEVMIAPLPLYHIYAFTAncmCMMVsgn 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 286 HLLPKFDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESY 361
Cdd:PRK12492 286 HNVLITNPRDIpgfIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 362 GQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGD 440
Cdd:PRK12492 366 GLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK-GP----QVMKGYWQQPEATAEALDAE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 441 FWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHD 519
Cdd:PRK12492 441 GWFkTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVE 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1034593582 520 peqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK12492 521 ------ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-564 |
2.04e-43 |
|
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: 158.21 E-value: 2.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIM------WTISdtGWILNILCSLMEpwalgACTFVHLLPKF 291
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplFHCF--GSVLGVLACLTH-----GATMVFPSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 292 DPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGL-DIRESYGQTETGLT 369
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 370 CMVSKT---MKIKPGYMGTAASCYDVQIIDDKGNVLPP-GTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWL-L 444
Cdd:cd05917 160 STQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTAEAIDGDGWLhT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 445 GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT 524
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL------KEGAELT 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034593582 525 KE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd05917 309 EEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
82-569 |
3.20e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 161.78 E-value: 3.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSGAcGLQRGDRVAVVL---PRVPEwwlVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 158
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 159 AGDEVIQEVDTVASECPSLRIKLLV-SEKSCDGWLNFKKLLNEASTTHHCVETgsqEASAIYFTSGTSGLPKMAEHSYSS 237
Cdd:PRK13391 102 TSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPATPIADES---LGTDMLYSSGTTGRPKGIKRPLPE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 238 LGLKAKMdaGWTGLQASdiMWTI-SDTGWilniLC-----------SLMEPWALGACTFVhlLPKFDPLVILKTLSSYPI 305
Cdd:PRK13391 179 QPPDTPL--PLTAFLQR--LWGFrSDMVY----LSpaplyhsapqrAVMLVIRLGGTVIV--MEHFDAEQYLALIEEYGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 306 KSMMGAPIVY-RML-------LQQDLSSykfphLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTE-TGLTCMVSKTM 376
Cdd:PRK13391 249 THTQLVPTMFsRMLklpeevrDKYDLSS-----LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEgLGFTACDSEEW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 377 KIKPGYMGTAASCyDVQIIDDKGNVLPPGTEGDIGIRVKpiRPigiFSgYVDNPDKTAA--NIRGDFWLLGDRGIKDEDG 454
Cdd:PRK13391 324 LAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGG--RP---FE-YLNDPAKTAEarHPDGTWSTVGDIGYVDEDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 455 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDP-EQLTKELQQHVKS 533
Cdd:PRK13391 397 YLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGV---DPgPALAAELIAFCRQ 473
|
490 500 510
....*....|....*....|....*....|....*.
gi 1034593582 534 VTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 569
Cdd:PRK13391 474 RLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
84-574 |
1.01e-42 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 160.25 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 84 RELSENSQQAANVLSG--ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK12406 12 RSFDELAQRAARAAGGlaALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 EVIQEV-DTVASEC--------PSLRIKLLVSEKSC---------DGWLNfkklLNEASTThhcvETGSQEASAIYfTSG 223
Cdd:PRK12406 92 DLLHGLaSALPAGVtvlsvptpPEIAAAYRISPALLtppagaidwEGWLA----QQEPYDG----PPVPQPQSMIY-TSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 224 TSGLPKmaehsysslglKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEP--------WALGACTFVH---LLPKFD 292
Cdd:PRK12406 163 TTGHPK-----------GVRRAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPlyhsapnaYGLRAGRLGGvlvLQPRFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 293 PLVILKTLSSYPIKSMMGAPIVYRMLLQ--------QDLSSYKFphlqncVTVGESLLP-----ETLENWraqtGLDIRE 359
Cdd:PRK12406 232 PEELLQLIERHRITHMHMVPTMFIRLLKlpeevrakYDVSSLRH------VIHAAAPCPadvkrAMIEWW----GPVIYE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 360 SYGQTETGL--TCMVSKTMKiKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpIRPIGIFSgYVDNPDKTAANI 437
Cdd:PRK12406 302 YYGSTESGAvtFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSR---IAGNPDFT-YHNKPEKRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 438 RGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVvlasqfls 517
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV-------- 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034593582 518 hDPEQL----TKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKA 574
Cdd:PRK12406 449 -EPQPGatldEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
83-565 |
2.09e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 159.83 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--- 159
Cdd:PRK13295 58 YRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpkt 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 160 --GDEVIQEVDTVASECPSLRIKLLVSEkscDGWLNFKKLLNE--------ASTTHHCVETGSQEASAIYFTSGTSGLPK 229
Cdd:PRK13295 137 frGFDHAAMARRLRPELPALRHVVVVGG---DGADSFEALLITpaweqepdAPAILARLRPGPDDVTQLIYTSGTTGEPK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 230 MAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMM 309
Cdd:PRK13295 214 GVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGA-TAV-LQDIWDPARAAELIRTEGVTFTM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 310 GA-PIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMvsktmkIKPGYMGTAAS 388
Cdd:PRK13295 292 AStPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTL------TKLDDPDERAS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 389 CYD--------VQIIDDKGNVLPPGTEGdigiRVKpIRPIGIFSGYVDNPDKTAANIRGdfWL-LGDRGIKDEDGYFQFM 459
Cdd:PRK13295 366 TTDgcplpgveVRVVDADGAPLPAGQIG----RLQ-VRGCSNFGGYLKRPQLNGTDADG--WFdTGDLARIDADGYIRIS 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 460 GRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL-ASQflSHDPEQLTKELQQHvkSVTAPY 538
Cdd:PRK13295 439 GRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPrPGQ--SLDFEEMVEFLKAQ--KVAKQY 514
|
490 500
....*....|....*....|....*..
gi 1034593582 539 kYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK13295 515 -IPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
48-564 |
5.84e-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: 158.39 E-value: 5.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 48 SDVLDHWADmekagkRLPS-PALwwVNGKGKelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGC 126
Cdd:COG1021 28 GDLLRRRAE------RHPDrIAV--VDGERR---LSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 127 IRAGLI---FMPGtiqMKSTDILYRLQMSKAKAIVAGDEV-----IQEVDTVASECPSLRIKLLVSEKscDGWLNFKKLL 198
Cdd:COG1021 96 FRAGAIpvfALPA---HRRAEISHFAEQSEAVAYIIPDRHrgfdyRALARELQAEVPSLRHVLVVGDA--GEFTSLDALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 199 NEASTtHHCVETGSQEASAIYFTSGTSGLPKM-----AEHSYSslglkAKMDAGWTGLQASDIMwtisdtgwilniLCSL 273
Cdd:COG1021 171 AAPAD-LSEPRPDPDDVAFFQLSGGTTGLPKLiprthDDYLYS-----VRASAEICGLDADTVY------------LAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 274 -------------MEPWALGACtfVHLLPKFDPLVILK-------TLSSypiksmMGAPIVYRML-----LQQDLSSYKF 328
Cdd:COG1021 233 paahnfplsspgvLGVLYAGGT--VVLAPDPSPDTAFPlierervTVTA------LVPPLALLWLdaaerSRYDLSSLRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 329 phLQncvtVGESLLPETLENwRAQTGLDIR--ESYGQTEtGLTCM---------VSKTMkikpgymGTAASCYD-VQIID 396
Cdd:COG1021 305 --LQ----VGGAKLSPELAR-RVRPALGCTlqQVFGMAE-GLVNYtrlddpeevILTTQ-------GRPISPDDeVRIVD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 397 DKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRI 473
Cdd:COG1021 370 EDGNPVPPGEVGELLTR-------GpyTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 474 GPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflshDPEQLT-KELQQHVKSV-TAPYKYPRKIEFVLNLP 551
Cdd:COG1021 443 AAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-------RGEPLTlAELRRFLRERgLAAFKLPDRLEFVDALP 515
|
570
....*....|...
gi 1034593582 552 KTVTGKIQRAKLR 564
Cdd:COG1021 516 LTAVGKIDKKALR 528
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
84-493 |
1.11e-40 |
|
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: 152.42 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 84 RELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM----SKAKA 156
Cdd:TIGR01733 3 RELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP-------LDPAYpaeRLAFiledAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 157 IVAGDEVIQEVDTVASECPSLRIKLLVSEKSCdgwlnfkkllneASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYS 236
Cdd:TIGR01733 76 LLTDSALASRLAGLVLPVILLDPLELAALDDA------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 237 SLglkAKMdAGWT----GLQASDIMW---TIS-DTgwilnilcSLME---PWALGACTFVHL--LPKFDPLVILKTLSSY 303
Cdd:TIGR01733 144 SL---VNL-LAWLarryGLDPDDRVLqfaSLSfDA--------SVEEifgALLAGATLVVPPedEERDDAALLAALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 304 PIKSMMGAPIVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENWRAQTGlDIR--ESYGQTETGLTCMVSKTMKIKPG 381
Cdd:TIGR01733 212 PVTVLNLTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGP-GARliNLYGPTETTVWSTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 382 YM-----GTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAAN-IRGDFWLL--------GDR 447
Cdd:TIGR01733 289 REspvpiGRPLANTRLYVLDDDLRPVPVGVVGELYIG-----GPGVARGYLNRPELTAERfVPDPFAGGdgarlyrtGDL 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1034593582 448 GIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAV 493
Cdd:TIGR01733 364 VRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
72-566 |
1.60e-40 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 154.75 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 72 VNGKGkelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQM 151
Cdd:PLN02330 51 VTGKA----VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 152 SKAKAIVAGDEVIQEVDtvasecpSLRIKLLV-SEKSCDGWLNFKKLLN---EASTTHHCVETGSQEASAIYFTSGTSGL 227
Cdd:PLN02330 126 AGAKLIVTNDTNYGKVK-------GLGLPVIVlGEEKIEGAVNWKELLEaadRAGDTSDNEEILQTDLCALPFSSGTTGI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 228 PK--MAEHSysslGLKAKMDAGWTGLqASDIMWTISDTGWI--------LNILCSLMEPWALgactfVHLLPKFDPLVIL 297
Cdd:PLN02330 199 SKgvMLTHR----NLVANLCSSLFSV-GPEMIGQVVTLGLIpffhiygiTGICCATLRNKGK-----VVVMSRFELRTFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 298 KTLSSYPIKSmmgAPIVYRMLL---------QQDLSSYKfphLQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTETG 367
Cdd:PLN02330 269 NALITQEVSF---APIVPPIILnlvknpiveEFDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 368 LTCMV----SKTMKI-KPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDF 441
Cdd:PLN02330 343 CITLThgdpEKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYNNKEETDRTIDEDG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 442 WL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqfLSHDP 520
Cdd:PLN02330 418 WLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVV-----INPKA 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1034593582 521 EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 566
Cdd:PLN02330 493 KESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
214-560 |
2.25e-40 |
|
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: 149.57 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 214 EASAIYFTSGTSGLPK--MAEHSYSSLGLKAKMDAGwtGLQASDIMWTIS----DTGWILNILCSLMEpwalGACTFVHL 287
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQTLRAAAAWADCA--DLTEDDRYLIINpffhTFGYKAGIVACLLT----GATVVPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 288 LpkFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLD-IRESYGQTE 365
Cdd:cd17638 75 V--FDVDAILEAIERERITVLPGPPTLFQSLLDHpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 366 TGLTCM---------VSKTMkikpgymGTAASCYDVQIIDDkGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAAN 436
Cdd:cd17638 153 AGVATMcrpgddaetVATTC-------GRACPGFEVRIADD-GEVL--------------VRGYNVMQGYLDDPEATAEA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 437 IRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqf 515
Cdd:cd17638 211 IDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR--- 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034593582 516 lshDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd17638 288 ---PGVTLTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
287-565 |
1.13e-38 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 148.29 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 287 LLPKFDPLVILKTLSSYPIKSMMGAP-IVYRM--LLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQ 363
Cdd:cd05929 199 LMEKFDPEEFLRLIERYRVTFAQFVPtMFVRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 364 TE-TGLTCMVSKTMKIKPGYMGTAASCyDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigifSGYVDNPDKTAANIRGDFW 442
Cdd:cd05929 279 TEgQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAARNEGGW 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 443 -LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqfLSHDPE 521
Cdd:cd05929 352 sTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAP--GADAGT 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034593582 522 QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:cd05929 430 ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
82-565 |
1.95e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 148.74 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK06164 37 SRAELRALVDRLAAWL-AAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 --------EVIQEVDTvaSECPSLRIKLLVSEKSCD-------GWLNFKKLLNEASTTHHCVETGSQEASAIYFT-SGTS 225
Cdd:PRK06164 116 gfkgidfaAILAAVPP--DALPPLRAIAVVDDAADAtpapapgARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 226 GLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMwtisdtgwilniLCSLmePW-----------ALGACTFVHLLPKFDPL 294
Cdd:PRK06164 194 SGPKLVLHRQATLLRHARAIARAYGYDPGAVL------------LAAL--PFcgvfgfstllgALAGGAPLVCEPVFDAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 295 VILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCvtvG-ESLLP--ETLENWRAQTGLDIRESYGQTEtgLTCM 371
Cdd:PRK06164 260 RTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF---GfASFAPalGELAALARARGVPLTGLYGSSE--VQAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 372 VS-------KTMKIKPGymGTAASC-YDVQIID-DKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFW 442
Cdd:PRK06164 335 VAlqpatdpVSVRIEGG--GRPASPeARVRARDpQDGALLPDGESGEIEIRAP-----SLMRGYLDNPDATARALTDDGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 443 L-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQfLSHDPE 521
Cdd:PRK06164 408 FrTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDG-ASPDEA 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1034593582 522 qltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG---KIQRAKLRD 565
Cdd:PRK06164 486 ----GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
217-564 |
1.97e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 144.93 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 217 AIYF-TSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVHLLPK--FDP 293
Cdd:cd05944 5 AAYFhTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPAgyRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 294 LV---ILKTLSSYPIKSMMGAPIVYRMLLQ----QDLSSYKFphlqncVTVGESLLPETLEN-WRAQTGLDIRESYGQTE 365
Cdd:cd05944 84 GLfdnFWKLVERYRITSLSTVPTVYAALLQvpvnADISSLRF------AMSGAAPLPVELRArFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 366 TglTCMVSKTMK---IKPGYMGTAASCYDVQI--IDDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVDNPDKTAANIrGD 440
Cdd:cd05944 158 A--TCLVAVNPPdgpKRPGSVGLRLPYARVRIkvLDGVGRLLRDCAPDEVGEIC--VAGPGVFGGYLYTEGNKNAFV-AD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 441 FWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsQFLSHD 519
Cdd:cd05944 233 GWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLK-PGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034593582 520 PEQLTKELQQHVKSVTApykYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd05944 312 EEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
82-566 |
4.24e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 147.79 E-value: 4.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK08162 45 TWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 EVIQEVDTVASECPSLRIkLLV-------SEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPK--MA 231
Cdd:PRK08162 124 EFAEVAREALALLPGPKP-LVIdvddpeyPGGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKgvVY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 232 EHSYSSLGLKAKMDAgWTGLQASDIMWTISD---TGWilnilCSlmePWALGACTFVHL-LPKFDPLVILKTLSSYPIKS 307
Cdd:PRK08162 203 HHRGAYLNALSNILA-WGMPKHPVYLWTLPMfhcNGW-----CF---PWTVAARAGTNVcLRKVDPKLIFDLIREHGVTH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 308 MMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENwRAQTGLDIRESYGQTETgltcmvsktmkikpgYmGTA 386
Cdd:PRK08162 274 YCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAK-MEEIGFDLTHVYGLTET---------------Y-GPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 387 ASCYDVQIIDDkgnvLPPGTEGDI------------GIRV------KPI----RPIG--------IFSGYVDNPDKTAAN 436
Cdd:PRK08162 337 TVCAWQPEWDA----LPLDERAQLkarqgvryplqeGVTVldpdtmQPVpadgETIGeimfrgniVMKGYLKNPKATEEA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 437 IRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqfl 516
Cdd:PRK08162 413 FAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELK---- 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1034593582 517 shDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQRAKLRDK 566
Cdd:PRK08162 489 --DGASATEeEIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQ 536
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
48-566 |
4.52e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 146.95 E-value: 4.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 48 SDVLDHWAdmekagKRLPS-PALWWvngKGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGC 126
Cdd:PRK06145 5 SASIAFHA------RRTPDrAALVY---RDQEI--SYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 127 IRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagdeVIQEVDTVasecPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHH 206
Cdd:PRK06145 73 SYLGAVFLPINYRLAADEVAYILGDAGAKLLL----VDEEFDAI----VALETPKIVIDAAAQADSRRLAQGGLEIPPQA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 207 CVetGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTIsdtGWILNI-LCSLMEPWALGACTFV 285
Cdd:PRK06145 145 AV--APTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVV---GPLYHVgAFDLPGIAVLWVGGTL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 286 HLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCVTVGESLlPETL--ENWRAQTGLDIRESYG 362
Cdd:PRK06145 220 RIHREFDPEAVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEKT-PESRirDFTRVFTRARYIDAYG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 363 QTET--GLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRpigifSGYVDNPDKTAANIRGD 440
Cdd:PRK06145 299 LTETcsGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVT-----KGYWKDPEKTAEAFYGD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 441 FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAS-QFLSHD 519
Cdd:PRK06145 374 WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgATLTLE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1034593582 520 peqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 566
Cdd:PRK06145 454 ------ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
67-563 |
4.59e-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: 145.85 E-value: 4.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 67 PALWWVNGKgkelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDIL 146
Cdd:cd05945 8 PAVVEGGRT-----LTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP-------LDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 147 Y---RLQMskAKAIVAGDEVIQEVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSG 223
Cdd:cd05945 75 SpaeRIRE--ILDAAKPALLIADGDDNA---------------------------------------------YIIFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 224 TSGLPKMAEHSYSSLglkakmdagwtglqASDIMWTISDTGWI----------LNILCSLME---PWALGACtfVHLLPK 290
Cdd:cd05945 108 STGRPKGVQISHDNL--------------VSFTNWMLSDFPLGpgdvflnqapFSFDLSVMDlypALASGAT--LVPVPR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 291 ---FDPLVILKTLSSYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENWRAQT-GLDIRESYGQTE 365
Cdd:cd05945 172 datADPKQLFRFLAEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 366 TGLTCMVSK-TMKIKPGY----MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTA-ANI 437
Cdd:cd05945 252 ATVAVTYIEvTPEVLDGYdrlpIGYAKPGAKLVILDEDGRPVPPGEKGELVIS-------GpsVSKGYLNNPEKTAaAFF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 438 RGDFWLL---GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVIssPDPVRGEVVK--AFVVLA 512
Cdd:cd05945 325 PDEGQRAyrtGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVV--PKYKGEKVTEliAFVVPK 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1034593582 513 sqflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd05945 403 ----PGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
81-563 |
7.10e-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: 145.93 E-value: 7.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI---FMPGtiqMKSTDILYRLQMSKAKAI 157
Cdd:cd05920 41 LTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvlALPS---HRRSELSAFCAHAEAVAY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 VAGDEvIQEVD------TVASECPSLRIKLLvsekscdgwlnfkkllneastthhcvetgsqeasaiyfTSGTSGLPKMA 231
Cdd:cd05920 117 IVPDR-HAGFDhralarELAESIPEVALFLL--------------------------------------SGGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 232 EHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCslmePWALGACTF---VHLLPKFDPLVILKTLSSYPIKSM 308
Cdd:cd05920 158 PRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAC----PGVLGTLLAggrVVLAPDPSPDAAFPLIEREGVTVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 309 MGAPIVYRMLLQQ------DLSSYKFphLQncvtVGESLLPETL-ENWRAQTGLDIRESYGQTEtGLTCM--VSKTMKIK 379
Cdd:cd05920 234 ALVPALVSLWLDAaasrraDLSSLRL--LQ----VGGARLSPALaRRVPPVLGCTLQQVFGMAE-GLLNYtrLDDPDEVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 380 PGYMGTAASCYD-VQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGD-FWLLGDRGIKDEDGY 455
Cdd:cd05920 307 IHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTR-------GpyTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 456 FQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKELQQHVKSV- 534
Cdd:cd05920 380 LVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLRERg 453
|
490 500
....*....|....*....|....*....
gi 1034593582 535 TAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd05920 454 LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
149-566 |
3.16e-37 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 145.29 E-value: 3.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 149 LQMSKAKAIVAGDEVIQEVDTVASECP-SLRIKLLVSEKScdgwlnfkKLLNEASTTHHC---VETGSQEASAIYFTSGT 224
Cdd:PRK13382 136 VTREGVDTVIYDEEFSATVDRALADCPqATRIVAWTDEDH--------DLTVEVLIAAHAgqrPEPTGRKGRVILLTSGT 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 225 SGLPKMAEHSYS--SLGLKAKMD-AGWTGLQASDIMWTISDTGWILNILCSlmepwALGACTFVhLLPKFDPLVILKTLS 301
Cdd:PRK13382 208 TGTPKGARRSGPggIGTLKAILDrTPWRAEEPTVIVAPMFHAWGFSQLVLA-----ASLACTIV-TRRRFDPEATLDLID 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 302 SYPIKSMMGAPIVYRMLLQ---QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS-KTMK 377
Cdd:PRK13382 282 RHRATGLAVVPVMFDRIMDlpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATpADLR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 378 IKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKtaaNIRGDFWLLGDRGIKDEDGYFQ 457
Cdd:PRK13382 362 AAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQ-----FDGYTSGSTK---DFHDGFMASGDVGYLDENGRLF 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 458 FMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAP 537
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG-ASATPE----TLKQHVRDNLAN 508
|
410 420
....*....|....*....|....*....
gi 1034593582 538 YKYPRKIEFVLNLPKTVTGKIQRAKLRDK 566
Cdd:PRK13382 509 YKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
44-557 |
9.08e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 143.87 E-value: 9.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 44 FNFAsDVLDHWADmeKAGKRlpsPALwwVNGkgkELMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVI 123
Cdd:PRK07798 3 WNIA-DLFEAVAD--AVPDR---VAL--VCG---DRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 124 LGCIRAGLIfmPGTIQMKSTD--ILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLV----SEKSCDGWLNFKKL 197
Cdd:PRK07798 71 LGAFKARAV--PVNVNYRYVEdeLRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 198 LNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MAEHS---YSSLGLKAKMdagwTGLQASDiMWTISD-----TGWIL 267
Cdd:PRK07798 149 LAAGSPERDFGERSPDDLYLLY-TGGTTGMPKgvMWRQEdifRVLLGGRDFA----TGEPIED-EEELAKraaagPGMRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 268 NILCSLME---PWAL------GACTFVHLLPKFDPLVILKTLSSYPIKSM------MGAPIV--YRMLLQQDLSSykfph 330
Cdd:PRK07798 223 FPAPPLMHgagQWAAfaalfsGQTVVLLPDVRFDADEVWRTIEREKVNVItivgdaMARPLLdaLEARGPYDLSS----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 331 LQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTETGLtCMVSKTMKIKPGYMG---TAAScyDVQIIDDKGNVLPPGt 406
Cdd:PRK07798 298 LFAIASGGALFSPSVKEALLELlPNVVLTDSIGSSETGF-GGSGTVAKGAVHTGGprfTIGP--RTVVLDEDGNPVEPG- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 407 EGDIGI--RVKPIrPIGifsgYVDNPDKTAAN---IRGDFW-LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN 480
Cdd:PRK07798 374 SGEIGWiaRRGHI-PLG----YYKDPEKTAETfptIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034593582 481 ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGK 557
Cdd:PRK07798 449 ALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
81-530 |
5.54e-36 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 140.04 E-value: 5.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdiLYrlQMSKAKAIvag 160
Cdd:cd05907 6 ITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP----------IY--PTSSAEQI--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 deviqevdtvasecpslrikllvsekscdGWLnfkklLNEASTTHHCVETGSQEASAIYfTSGTSGLPKMAEHSYSSLgl 240
Cdd:cd05907 70 -----------------------------AYI-----LNDSEAKALFVEDPDDLATIIY-TSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDAGWTGLQASDIMWTIS--DTGWILNILCSLMEPWALGACTFVHLLPKfdplVILKTLSSYPIKSMMGAPIVYRML 318
Cdd:cd05907 113 LSNALALAERLPATEGDRHLSflPLAHVFERRAGLYVPLLAGARIYFASSAE----TLLDDLSEVRPTVFLAVPRVWEKV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 319 ---LQQDLSS------YKFPHLQNC--VTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAA 387
Cdd:cd05907 189 yaaIKVKAVPglkrklFDLAVGGRLrfAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 388 SCYDVQIIDDkGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRAND-I 465
Cdd:cd05907 269 PGVEVRIADD-GEIL--------------VRGPNVMLGYYKNPEATAEALDADGWLhTGDLGEIDEDGFLHITGRKKDlI 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034593582 466 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPvrgeVVKAFVVLasqflshDPEQLTKELQQH 530
Cdd:cd05907 334 ITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVP-------DPEALEAWAEEH 387
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
58-566 |
7.24e-36 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 141.27 E-value: 7.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 58 EKAGKRLPSPALwwVNGK-GKELmwNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPG 136
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGAtGRVY--TYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 137 TIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPslrIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEAS 216
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDG---VTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 217 AIYFTSGTSGLPK--MAEHS--YSSLGLKAKMDAGWTGLQASDI------MWTIsdtgWILN--ILCSLMepwaLGACtf 284
Cdd:PLN02246 183 ALPYSSGTTGLPKgvMLTHKglVTSVAQQVDGENPNLYFHSDDVilcvlpMFHI----YSLNsvLLCGLR----VGAA-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 285 VHLLPKFDPLVILKTLSSYPIK-SMMGAPIVYRM-----LLQQDLSSYKFphlqncVTVGESLLPETLEN-WRAQ-TGLD 356
Cdd:PLN02246 253 ILIMPKFEIGALLELIQRHKVTiAPFVPPIVLAIakspvVEKYDLSSIRM------VLSGAAPLGKELEDaFRAKlPNAV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 357 IRESYGQTETG---LTCMV-SKT-MKIKPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNP 430
Cdd:PLN02246 327 LGQGYGMTEAGpvlAMCLAfAKEpFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQI-----MKGYLNDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 431 DKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFV 509
Cdd:PLN02246 402 EATANTIDKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFV 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034593582 510 VLASQF-LSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 566
Cdd:PLN02246 482 VRSNGSeITED------EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
47-560 |
7.08e-35 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 138.48 E-value: 7.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 47 ASDVLDHWADM-EKAGKRLPS-PALWWVNGKgkeLMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVIL 124
Cdd:PRK05852 11 ASDFGPRIADLvEVAATRLPEaPALVVTADR---IAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 125 GCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTT 204
Cdd:PRK05852 87 AASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 205 HHCVETGSQEASA-IYFTSGTSGLPKMAEHSYSSLGlkAKMDAGWTGLQASD------IMWTISDTGWILNILCSLMEPW 277
Cdd:PRK05852 167 ATSTPEGLRPDDAmIMFTGGTTGLPKMVPWTHANIA--SSVRAIITGYRLSPrdatvaVMPLYHGHGLIAALLATLASGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 278 ALgactfvhLLP---KFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ---DLSSYKFPHLQNCVTVGESLLPETLENWRA 351
Cdd:PRK05852 245 AV-------LLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILLERaatEPSGRKPAALRFIRSCSAPLTAETAQALQT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 352 QTGLDIRESYGQTET----------GLTCMVSKTMKIKPGYMGTAAscyDVQIIDDKGNVLPPGTEGDIGIRVKPIrpig 421
Cdd:PRK05852 318 EFAAPVVCAFGMTEAthqvtttqieGIGQTENPVVSTGLVGRSTGA---QIRIVGSDGLPLPAGAVGEVWLRGTTV---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 422 iFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPV 500
Cdd:PRK05852 391 -VRGYLGDPTITAANFT-DGWLrTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034593582 501 RGEVVKAFVV-LASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:PRK05852 469 YGEAVAAVIVpRESAPPTAE------ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
102-570 |
2.63e-34 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 136.90 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 102 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagdeVIQEVDTVASEcpSLRI-- 179
Cdd:PLN02479 66 SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM----VDQEFFTLAEE--ALKIla 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 180 ---------KLLV--SEKSCD----------GWLNFKKLLneastthhcvETGSQE-----------ASAIYFTSGTSGL 227
Cdd:PLN02479 140 ekkkssfkpPLLIviGDPTCDpkslqyalgkGAIEYEKFL----------ETGDPEfawkppadewqSIALGYTSGTTAS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 228 PKMAEHSYSSLGLKAKMDAGWTGLQASDI-MWTISD---TGWILnilcslmePWALGA-CTFVHLLPKFDPLVILKTLSS 302
Cdd:PLN02479 210 PKGVVLHHRGAYLMALSNALIWGMNEGAVyLWTLPMfhcNGWCF--------TWTLAAlCGTNICLRQVTAKAIYSAIAN 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 303 YPIKSMMGAPIVYRMLLQQDLSS--YKFPHLQNCVTVGESLLPETLENWrAQTGLDIRESYGQTET-------------- 366
Cdd:PLN02479 282 YGVTHFCAAPVVLNTIVNAPKSEtiLPLPRVVHVMTAGAAPPPSVLFAM-SEKGFRVTHTYGLSETygpstvcawkpewd 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 367 GLTCMVSKTMKIKPGYMGTAASCYDVqiIDDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVDNPDKTAANIRGDFWLLGD 446
Cdd:PLN02479 361 SLPPEEQARLNARQGVRYIGLEGLDV--VDTKTMKPVPADGKTMGEIV--MRGNMVMKGYLKNPKANEEAFANGWFHSGD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 447 RGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKE 526
Cdd:PLN02479 437 LGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAED 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1034593582 527 LQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQRAKLRDKEWKM 570
Cdd:PLN02479 517 IMKFCRERLPAYWVPKSVVFG-PLPKTATGKIQKHVLRAKAKEM 559
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
58-564 |
1.55e-33 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 133.62 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 58 EKAGKRLP-SPALWWVNGKgkelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPG 136
Cdd:cd17651 2 ERQAARTPdAPALVAEGRR-----LTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 137 TIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpslrikllvsekscDGWLNFKKLLNEASTTHHCVETGSQEAS 216
Cdd:cd17651 76 DPAYPAERLAFMLADAGPVLVLTHPALAGELAVELV----------------AVTLLDQPGAAAGADAEPDPALDADDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 217 AIYFTSGTSGLPKMAEHSYSSLGL-------KAKMDAGWTGLQASDIMWTISdTGWILNILCSlmepwalGACtfVHLLP 289
Cdd:cd17651 140 YVIYTSGSTGRPKGVVMPHRSLANlvawqarASSLGPGARTLQFAGLGFDVS-VQEIFSTLCA-------GAT--LVLPP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 290 ---KFDPLVILKTLSSYPI-KSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESL-LPETLENW-RAQTGLDIRESYGQ 363
Cdd:cd17651 210 eevRTDPPALAAWLDEQRIsRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLvLTEDLREFcAGLPGLRLHNHYGP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 364 TETglTCMVSKTMKIKPGYMGTAASC------YDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANI 437
Cdd:cd17651 290 TET--HVVTALSLPGDPAAWPAPPPIgrpidnTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAERF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 438 RGD-------FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVV 510
Cdd:cd17651 363 VPDpfvpgarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1034593582 511 lASQFLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd17651 443 -GDPEAPVDAA----ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
361-556 |
2.58e-33 |
|
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: 129.73 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 361 YGQTE-TGLTCMvsktmkikPGYMGTAASCY-------DVQIIDDKGNVLPPGTEGDIGIRvKPIrpigIFSGYVDNPDK 432
Cdd:cd17636 143 YGQTEvMGLATF--------AALGGGAIGGAgrpsplvQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 433 TAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL- 511
Cdd:cd17636 210 NARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLk 289
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034593582 512 ASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 556
Cdd:cd17636 290 PGASVTEA------ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
81-564 |
4.55e-33 |
|
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: 131.72 E-value: 4.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivag 160
Cdd:cd17649 13 LSYAELDARANRLAHRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 deviqevdtVASECPSLRIKLLVsEKSCDGWLnfkkllneasTTHHcvetGSQEASAIYfTSGTSGLPKMAEHSYSSLGL 240
Cdd:cd17649 67 ---------LDPEYPAERLRYML-EDSGAGLL----------LTHH----PRQLAYVIY-TSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDAGWTGLQASDIMWTISDTGWILNILCsLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLL 319
Cdd:cd17649 122 HCQATAERYGLTPGDRELQFASFNFDGAHEQ-LLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYlQQLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 320 QQ--DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIREsYGQTETGLTCMVSKT---MKIKPGYM--GTAASCYDV 392
Cdd:cd17649 201 EEadRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNA-YGPTEATVTPLVWKCeagAARAGASMpiGRPLGGRSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 393 QIIDDKGNVLPPGTEGD--IGIRvkpirpiGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMGRA 462
Cdd:cd17649 280 YILDADLNPVPVGVTGElyIGGE-------GLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGRV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 463 NDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVL-ASQFLSHDPEQltkeLQQHVKSVTAPYKYP 541
Cdd:cd17649 353 DHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLrAAAAQPELRAQ----LRTALRASLPDYMVP 427
|
490 500
....*....|....*....|...
gi 1034593582 542 RKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd17649 428 AHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
83-564 |
9.28e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 131.44 E-value: 9.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGACGLQRgdRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:PRK07638 29 YKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 VIQEVDTVasECPSLRIkllvsekscDGWlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSlglka 242
Cdd:PRK07638 107 KLNDLPDE--EGRVIEI---------DEW---KRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 243 kmdagWT-GLQASDIMWTISDTGWILnILCSLMEPWAL-GACT------FVHLLPKFDPLVILKTLSSYPIKSMMGAPIV 314
Cdd:PRK07638 168 -----WLhSFDCNVHDFHMKREDSVL-IAGTLVHSLFLyGAIStlyvgqTVHLMRKFIPNQVLDKLETENISVMYTVPTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 315 YRMLLQQDlssyKFPhlQNCVTV---GESLLPETLEnwRAQTG---LDIRESYGQTETG-LTCMVSKTMKIKPGYMGTAA 387
Cdd:PRK07638 242 LESLYKEN----RVI--ENKMKIissGAKWEAEAKE--KIKNIfpyAKLYEFYGASELSfVTALVDEESERRPNSVGRPF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 388 SCYDVQIIDDKGNVLPPGTEGDIGIRvKPIRpigiFSGYVdNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDII 466
Cdd:PRK07638 314 HNVQVRICNEAGEEVQKGEIGTVYVK-SPQF----FMGYI-IGGVLARELNADGWMtVRDVGYEDEEGFIYIVGREKNMI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 467 NSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVvlasqflshDPEQLTKELQQHVKSVTAPYKYPRKIEF 546
Cdd:PRK07638 388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKEWHF 458
|
490
....*....|....*...
gi 1034593582 547 VLNLPKTVTGKIQRAKLR 564
Cdd:PRK07638 459 VDEIPYTNSGKIARMEAK 476
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
85-563 |
1.22e-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: 131.09 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 85 ELSENSQQAANVLSGacGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD--E 162
Cdd:cd05923 34 LRARIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVdaQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 VIQEVDTVASECpsLRIKLLVSEKSCDgwlNFKKLLNEASTthhcvetGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKA 242
Cdd:cd05923 112 VMDAIFQSGVRV--LALSDLVGLGEPE---SAGPLIEDPPR-------EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 243 KMDAGWTGLQASDimwtisdtgwiLNILCSLMEPW-----------ALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGA 311
Cdd:cd05923 180 LFMSTQAGLRHGR-----------HNVVLGLMPLYhvigffavlvaALALDGTYVVVEEFDPADALKLIEQERVTSLFAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 312 PIVYRMLLQQDL-SSYKFPHLQNCVTVGESL---LPETLENWRAQTGLDIresYGQTETgltcMVSKTMK-IKPGYMGTA 386
Cdd:cd05923 249 PTHLDALAAAAEfAGLKLSSLRHVTFAGATMpdaVLERVNQHLPGEKVNI---YGTTEA----MNSLYMRdARTGTEMRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 387 ASCYDVQIIDDKGNV---LPPGTEGDIgirVKPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRAN 463
Cdd:cd05923 322 GFFSEVRIVRIGGSPdeaLANGEEGEL---IVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 464 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDpeqltkELQQHVK-SVTAPYKYPR 542
Cdd:cd05923 399 DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD------ELDQFCRaSELADFKRPR 472
|
490 500
....*....|....*....|.
gi 1034593582 543 KIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd05923 473 RYFFLDELPKNAMNKVLRRQL 493
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
49-566 |
6.81e-32 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 130.22 E-value: 6.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 49 DVLDHWAdmEKAGKRlpsPALWW-VNGKGKELMWnfRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCI 127
Cdd:COG1022 15 DLLRRRA--ARFPDR---VALREkEDGIWQSLTW--AEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 128 RAGLIFMPgtIQMKST--DILYRLQMSKAKAIVAGD-EVIQEVDTVASECPSLRiKLLV----SEKSCDGWLNFKKLLNE 200
Cdd:COG1022 87 AAGAVTVP--IYPTSSaeEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVldprGLRDDPRLLSLDELLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 201 ASTTHH--CVETGSQEASA-----IYFTSGTSGLPKMAEHSYSSLglkakmdagWTGLQASDIMWTISDTGWILNILcsl 273
Cdd:COG1022 164 GREVADpaELEARRAAVKPddlatIIYTSGTTGRPKGVMLTHRNL---------LSNARALLERLPLGPGDRTLSFL--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 274 mePWA-------------LGAC--------TFVHLLPKFDPLVIL---------------KTLSSYPIKSM-----MGAP 312
Cdd:COG1022 232 --PLAhvfertvsyyalaAGATvafaespdTLAEDLREVKPTFMLavprvwekvyagiqaKAEEAGGLKRKlfrwaLAVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 313 IVYRMLLQQDLS---SYKFPH------------------LQNCVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCM 371
Cdd:COG1022 310 RRYARARLAGKSpslLLRLKHaladklvfsklrealggrLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 372 VSKTMKIKPGYMGTAAScyDVQI-IDDKGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWLL-GDRGI 449
Cdd:COG1022 389 VNRPGDNRIGTVGPPLP--GVEVkIAEDGEIL--------------VRGPNVMKGYYKNPEATAEAFDADGWLHtGDIGE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 450 KDEDGYFQFMGRANDII-NSSGYRIGPSEVENALMEHP----AVV--E-----TAVIsSPDPvrgEVVK--------AFV 509
Cdd:COG1022 453 LDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPlieqAVVvgDgrpflAALI-VPDF---EALGewaeenglPYT 528
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034593582 510 VLASqfLSHDPEqLTKELQQHVKSVTApyKYPR--KI-EFVLnLPK---------TVTGKIQRAKLRDK 566
Cdd:COG1022 529 SYAE--LAQDPE-VRALIQEEVDRANA--GLSRaeQIkRFRL-LPKeftiengelTPTLKLKRKVILEK 591
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
217-560 |
5.71e-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: 123.52 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 217 AIYFTSGTSGLPKMAEHSYSSLGLKAKMdagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACTF-----VHLLPKF 291
Cdd:cd17635 5 AVIFTSGTTGEPKAVLLANKTFFAVPDI------LQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIhgglcVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 292 DPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVG-ESLLPETLENWRAQTGLDIRESYGQTETG-LT 369
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGgSRAIAADVRFIEATGLTNTAQVYGLSETGtAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 370 CMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGI 449
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSP-----ANMLGYWNNPERTAEVLIDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 450 KDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshDPEQLTKELQQ 529
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE----LDENAIRALKH 309
|
330 340 350
....*....|....*....|....*....|.
gi 1034593582 530 HVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd17635 310 TIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
73-566 |
7.04e-31 |
|
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: 126.43 E-value: 7.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 73 NGKGKELMWNfrELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMS 152
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 153 KAKAIVAG--DEVIQEVDTVASECPSLRIKLLVSEKSCDGWlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKM 230
Cdd:cd05932 78 ESKALFVGklDDWKAMAPGVPEGLISISLPPPSAANCQYQW---DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 231 AEHSYSSLGLKAKMDAGWTGLQASDIMW-----------TISDTGWILNilcSLMEPWALGACTFVHLLPKFDPLVI--- 296
Cdd:cd05932 155 VMLTFGSFAWAAQAGIEHIGTEENDRMLsylplahvterVFVEGGSLYG---GVLVAFAESLDTFVEDVQRARPTLFfsv 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 297 --LKTLSSYPIKSMMGA---------PIVYRMLLQQDLSSYKFPHLQnCVTVGESLLPETLENWRAQTGLDIRESYGQTE 365
Cdd:cd05932 232 prLWTKFQQGVQDKIPQqklnlllkiPVVNSLVKRKVLKGLGLDQCR-LAGCGSAPVPPALLEWYRSLGLNILEAYGMTE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 366 TGLTCMVSKTMKIKPGYMGTAAScyDVQI-IDDKGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWL- 443
Cdd:cd05932 311 NFAYSHLNYPGRDKIGTVGNAGP--GVEVrISEDGEIL--------------VRSPALMMGYYKDPEATAEAFTADGFLr 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 444 LGDRGIKDEDGYFQFMGRANDIINSS-GYRIGPSEVENALMEHPAVVETAVISS--PDPVRGEVVKAFVVLASqfLSHDP 520
Cdd:cd05932 375 TGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRA--DAFAR 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1034593582 521 EQLTKELQQHVKSVTAPYKYPRKIEFVL---------NLPKTVTGKIQRAKLRDK 566
Cdd:cd05932 453 AELEASLRAHLARVNSTLDSHEQLAGIVvvkdpwsidNGILTPTLKIKRNVLEKA 507
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
83-563 |
7.54e-31 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 125.90 E-value: 7.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:cd17655 25 YRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 VIQevdtvasecpslrikLLVSEKSCDgWLNFKKLLNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MAEHS-----Y 235
Cdd:cd17655 104 LQP---------------PIAFIGLID-LLDEDTIYHEESENLEPVSKSDDLAYVIY-TSGSTGKPKgvMIEHRgvvnlV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 236 SSLGLKAKMDAGWTGLQASDIMWTISDTgwilnilcSLMEPWALGACtfVHLLPK---FDPLVILKTLSSYPIKSMMGAP 312
Cdd:cd17655 167 EWANKVIYQGEHLRVALFASISFDASVT--------EIFASLLSGNT--LYIVRKetvLDGQALTQYIRQNRITIIDLTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 313 IVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENW--RAQTGLDIRESYGQTETGLTCMV-----SKTMKIKPgYMGT 385
Cdd:cd17655 237 AHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqyepETDQQVSV-PIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 386 AASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKD-------EDGYFQF 458
Cdd:cd17655 314 PLGNTRIYILDQYGRPQPVGVAGELYIGGE-----GVARGYLNRPELTAEKFVDDPFVPGERMYRTgdlarwlPDGNIEF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 459 MGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDPEQLTKELQQHVKSVTAPy 538
Cdd:cd17655 389 LGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKEL---PVAQLREFLARELPDYMIP- 464
|
490 500
....*....|....*....|....*
gi 1034593582 539 KYPRKIEfvlNLPKTVTGKIQRAKL 563
Cdd:cd17655 465 SYFIKLD---EIPLTPNGKVDRKAL 486
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
90-564 |
1.47e-30 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 126.07 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 90 SQQAANVLSGACGL-----QRGDRVAVVLPRVPEW--WLVILGCirAGLIFMPgtiqmkstdILYRLQMSKAKAIVagdE 162
Cdd:PLN02860 36 HEFVDGVLSLAAGLlrlglRNGDVVAIAALNSDLYleWLLAVAC--AGGIVAP---------LNYRWSFEEAKSAM---L 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 VIQEVDTVASE-------------CPSLRIKLLVSEKSCDGWLNFKKLLN-EASTTHHCVETGSQEASA------IYFTS 222
Cdd:PLN02860 102 LVRPVMLVTDEtcsswyeelqndrLPSLMWQVFLESPSSSVFIFLNSFLTtEMLKQRALGTTELDYAWApddavlICFTS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 223 GTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTIS---DTGWILNILCSLMepwaLGACtfvH-LLPKFDPLVILK 298
Cdd:PLN02860 182 GTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAplcHIGGLSSALAMLM----VGAC---HvLLPKFDAKAALQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 299 TLSSYPIKSMMGAPIVYRMLL---QQDLSSYKFPHLQNCVTVGES----LLPETLENW-RAQtgldIRESYGQTET--GL 368
Cdd:PLN02860 255 AIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSlssrLLPDAKKLFpNAK----LFSAYGMTEAcsSL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 369 TCMV--SKTMKIKPGYMGTAASCYDvQIIDDKGNVL----PPGTEgdIGIRVKPIRPIG-IFS-------GYVDNPDKTA 434
Cdd:PLN02860 331 TFMTlhDPTLESPKQTLQTVNQTKS-SSVHQPQGVCvgkpAPHVE--LKIGLDESSRVGrILTrgphvmlGYWGQNSETA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 435 ANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL-- 511
Cdd:PLN02860 408 SVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLrd 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034593582 512 ------ASQFLSHDPEQLTKE-LQQHV--KSVTApYKYPRKieFVLN---LPKTVTGKIQRAKLR 564
Cdd:PLN02860 488 gwiwsdNEKENAKKNLTLSSEtLRHHCreKNLSR-FKIPKL--FVQWrkpFPLTTTGKIRRDEVR 549
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
220-566 |
2.38e-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: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 220 FTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDimwtisdtGWilniLCSLmeP------------WALGACTFVhL 287
Cdd:cd17630 7 LTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD--------SW----LLSL--PlyhvgglailvrSLLAGAELV-L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 288 LPKFDPLviLKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTETG 367
Cdd:cd17630 72 LERNQAL--AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRA-VLLGGAPIPPELLERAADRGIPLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 368 LTcmvsktmkikpgymgTAASCYDVQIIDDKGNVLPpgtegDIGIRVKP-----IRPIGIFSGYVDNPDKTAANIRGdfW 442
Cdd:cd17630 149 SQ---------------VATKRPDGFGRGGVGVLLP-----GRELRIVEdgeiwVGGASLAMGYLRGQLVPEFNEDG--W 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 443 L-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflshDPE 521
Cdd:cd17630 207 FtTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034593582 522 QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 566
Cdd:cd17630 280 ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
69-564 |
6.17e-30 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 124.62 E-value: 6.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 69 LWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYR 148
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 149 LQMSKAKAIVA------GDEVIQEVDTV-------ASECPSLRIKLLVSEKSC------------DGWlnFKKLLNEAST 203
Cdd:PLN02654 188 IVDCKPKVVITcnavkrGPKTINLKDIVdaaldesAKNGVSVGICLTYENQLAmkredtkwqegrDVW--WQDVVPNYPT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 204 THHCVETGSQEASAIYFTSGTSGLPKMAEHS------YSSLGLKAKMDagwtgLQASDIMWTISDTGWILNILCSLMEPW 277
Cdd:PLN02654 266 KCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTtggymvYTATTFKYAFD-----YKPTDVYWCTADCGWITGHSYVTYGPM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 278 ALGACTFV-HLLPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLLPETlenWR-- 350
Cdd:PLN02654 341 LNGATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSA---WRwf 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 351 ----AQTGLDIRESYGQTETGlTCMVSKTMKIKPGYMGTAA-SCYDVQ--IIDDKGNVLppgtEGDIG--IRVKPIRPiG 421
Cdd:PLN02654 418 fnvvGDSRCPISDTWWQTETG-GFMITPLPGAWPQKPGSATfPFFGVQpvIVDEKGKEI----EGECSgyLCVKKSWP-G 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 422 IFS---GYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPD 498
Cdd:PLN02654 492 AFRtlyGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEH 571
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034593582 499 PVRGEVVKAFVVLASQFLShdPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:PLN02654 572 EVKGQGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
83-563 |
6.38e-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: 123.15 E-value: 6.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM--SKAKAI 157
Cdd:cd17646 26 YRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP-------LDPGYpadRLAYmlADAGPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 VagdeVIQEVDTVASECPSLRIKLLVSEkscdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--MAEHSY 235
Cdd:cd17646 98 V----VLTTADLAARLPAGGDVALLGDE-----------ALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKgvMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 236 SS---LGLKAK--MDAGWTGLQASDIMWTISdtGW-ILnilcslmepWAL--GACTFV-----HLlpkfDPLVILKTLSS 302
Cdd:cd17646 163 IVnrlLWMQDEypLGPGDRVLQKTPLSFDVS--VWeLF---------WPLvaGARLVVarpggHR----DPAYLAALIRE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 303 YPIKSMMGAPIVYRMLLQQDLSSyKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTE-----TGLTCMVSKTMK 377
Cdd:cd17646 228 HGVTTCHFVPSMLRVFLAEPAAG-SCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEaaidvTHWPVRGPAETP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 378 IKP-GYMGTAASCYdvqIIDDKGNVLPPGTEGDI---GIRVKpirpigifSGYVDNPDKTAANIRGD-------FWLLGD 446
Cdd:cd17646 307 SVPiGRPVPNTRLY---VLDDALRPVPVGVPGELylgGVQLA--------RGYLGRPALTAERFVPDpfgpgsrMYRTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 447 RGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEqltkE 526
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTA----A 451
|
490 500 510
....*....|....*....|....*....|....*..
gi 1034593582 527 LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17646 452 LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-563 |
7.47e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 122.69 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgde 162
Cdd:cd12117 25 YAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viQEVDTVASECPSLRIKLLVSEKSCDGwlnfkklLNEASTthhcvetGSQEASA-IYFTSGTSGLPK--MAEHsYSSLG 239
Cdd:cd12117 101 --DRSLAGRAGGLEVAVVIDEALDAGPA-------GNPAVP-------VSPDDLAyVMYTSGSTGRPKgvAVTH-RGVVR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 240 LKakMDAGWTGLQASDIMWTISDTGWIlnilCSLMEPW-AL--GACtfVHLLPK---FDPLVILKTLSSYPIKSMMGAPI 313
Cdd:cd12117 164 LV--KNTNYVTLGPDDRVLQTSPLAFD----ASTFEIWgALlnGAR--LVLAPKgtlLDPDALGALIAEEGVTVLWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 314 VYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETGL--TCMVsktmkIKPGYM------- 383
Cdd:cd12117 236 LFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTftTSHV-----VTELDEvagsipi 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 384 GTAASCYDVQIIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVDNPDKTA----ANIRGD---FWLLGDRGIKDED 453
Cdd:cd12117 309 GRPIANTRVYVLDEDGRPVPPGVPGELyvgGD--------GLALGYLNRPALTAerfvADPFGPgerLYRTGDLARWLPD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 454 GYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPD-PVRGEVVkAFVVlASQFLSHDpeqltkELQQHVK 532
Cdd:cd12117 381 GRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDaGGDKRLV-AYVV-AEGALDAA------ELRAFLR 452
|
490 500 510
....*....|....*....|....*....|.
gi 1034593582 533 SVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd12117 453 ERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
83-564 |
1.53e-29 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 122.97 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 162
Cdd:PRK05620 41 FAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 VIQEVDTVASECPSLRIKLLVSEKSCDG----------WLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 232
Cdd:PRK05620 121 LAEQLGEILKECPCVRAVVFIGPSDADSaaahmpegikVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 233 HSYSSLGLKAkmdagwTGLQASDIMWTISDTGW-----ILNIL--CSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPI 305
Cdd:PRK05620 201 YSHRSLYLQS------LSLRTTDSLAVTHGESFlccvpIYHVLswGVPLAAFMSGT-PLVFPGPDLSAPTLAKIIATAMP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 306 KSMMGAPIVYRMLLQQDL-SSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTmkiKPGYMG 384
Cdd:PRK05620 274 RVAHGVPTLWIQLMVHYLkNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARP---PSGVSG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 385 TAASCYDV-----------QIIDDkGNVLPPG--TEGDIGIRvKPIRPIGIFSGYVDNPDKTAANIRG------------ 439
Cdd:PRK05620 351 EARWAYRVsqgrfpasleyRIVND-GQVMESTdrNEGEIQVR-GNWVTASYYHSPTEEGGGAASTFRGedvedandrfta 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 440 DFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsh 518
Cdd:PRK05620 429 DGWLrTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGI--- 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1034593582 519 DPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:PRK05620 506 EPTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
102-571 |
8.53e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 121.29 E-value: 8.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 102 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQmkstdiLYRlqmskakaivaGDEVIQEVDTVASecpslrikL 181
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE------LHR-----------DDHALAARNTEPA--------L 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 182 LVSEKS-CDGW-----LNFKKLLNEAS---TTHHCVETGSQEASAIYfTSGTSGLPKMAEHSYSS-LGLKAKMDAGWTGL 251
Cdd:PRK06060 106 VVTSDAlRDRFqpsrvAEAAELMSEAArvaPGGYEPMGGDALAYATY-TSGTTGPPKAAIHRHADpLTFVDAMCRKALRL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 252 QASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLP-----------KFDPLVilktlssypiksMMGAPIVYRMLLQ 320
Cdd:PRK06060 185 TPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPvtpeaaailsaRFGPSV------------LYGVPNFFARVID 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 321 QdLSSYKFPHLQNCVTVGESL---LPETLENWRAqtGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDD 397
Cdd:PRK06060 253 S-CSPDSFRSLRCVVSAGEALelgLAERLMEFFG--GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 398 KGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANirGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSE 477
Cdd:PRK06060 330 DGTTAGPGVEGDLWVR-GP----AIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 478 VENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAS-QFLShdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 556
Cdd:PRK06060 403 VERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgATID---GSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNG 479
|
490 500
....*....|....*....|
gi 1034593582 557 KIQRAKLRDKE-----WKMS 571
Cdd:PRK06060 480 KLVRGALRKQSptkpiWELS 499
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
93-565 |
3.56e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 118.97 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 93 AANVLSgaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA-------GDEVIQ 165
Cdd:PLN03102 53 AASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVdrsfeplAREVLH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 166 EVDTVASEcPSLRIKLL----VSEKSCDGWLNFKKLLNEASTTHHCVET-----GSQEASAIYFTSGTSGLPKMAEHSYS 236
Cdd:PLN03102 131 LLSSEDSN-LNLPVIFIheidFPKRPSSEELDYECLIQRGEPTPSLVARmfriqDEHDPISLNYTSGTTADPKGVVISHR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 237 SLGLKA-KMDAGWTGLQASDIMWTISD---TGWILnilcslmePWALGA------CTFVHLLPKfdplvILKTLSSYPIK 306
Cdd:PLN03102 210 GAYLSTlSAIIGWEMGTCPVYLWTLPMfhcNGWTF--------TWGTAArggtsvCMRHVTAPE-----IYKNIEMHNVT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 307 SMMGAPIVYRMLLQQDLS--SYKFPHLQncVTVGESLLPETLENWRAQTGLDIRESYGQTE-TG--LTCM---------V 372
Cdd:PLN03102 277 HMCCVPTVFNILLKGNSLdlSPRSGPVH--VLTGGSPPPAALVKKVQRLGFQVMHAYGLTEaTGpvLFCEwqdewnrlpE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 373 SKTMKIKPGYMGTAASCYDVQIIDDKGNVLPP---GTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGI 449
Cdd:PLN03102 355 NQQMELKARQGVSILGLADVDVKNKETQESVPrdgKTMGEIVIKGS-----SIMKGYLKNPKATSEAFKHGWLNTGDVGV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 450 KDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL--ASQFLSHDPEQL-TKE 526
Cdd:PLN03102 430 IHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLvTRE 509
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1034593582 527 --LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PLN03102 510 rdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
218-568 |
5.94e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 117.86 E-value: 5.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDImwtisdtgwilnILCSL--------MEPWALGACT--FVHL 287
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDV------------CYVSMplfhsnavMAGWAVALAAgaSIAL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 288 LPKFDPLVILKTLSSYPIKSM--MGAPIVYRmllqqdLSSYKFP-HLQNCVTV--GESLLPETLENWRAQTGLDIRESYG 362
Cdd:PRK07867 225 RRKFSASGFLPDVRRYGATYAnyVGKPLSYV------LATPERPdDADNPLRIvyGNEGAPGDIARFARRFGCVVVDGFG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 363 QTETGLTcmVSKTMKIKPGYMGTAAScyDVQIID-DKGNVLPPGtEGDIGIRVKPIRPIG---------IFSGYVDNPDK 432
Cdd:PRK07867 299 STEGGVA--ITRTPDTPPGALGPLPP--GVAIVDpDTGTECPPA-EDADGRLLNADEAIGelvntagpgGFEGYYNDPEA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 433 TAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA 512
Cdd:PRK07867 374 DAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034593582 513 --SQFlshDPEQLTKELqqHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 568
Cdd:PRK07867 454 pgAKF---DPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
91-565 |
1.08e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 117.25 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 91 QQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMpgTIQMKSTDILYRLQMSKAKAIVAgdevIQEVDTV 170
Cdd:PLN02574 77 KSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT--TMNPSSSLGEIKKRVVDCSVGLA----FTSPENV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 171 aSECPSLRIK-LLVSEKscdgwLNFKKLLNEASTTHHCVET----------GSQEASAIYFTSGTSGLPK--MAEHS--Y 235
Cdd:PLN02574 151 -EKLSPLGVPvIGVPEN-----YDFDSKRIEFPKFYELIKEdfdfvpkpviKQDDVAAIMYSSGTTGASKgvVLTHRnlI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 236 SSLGLKAKMDAGWTGLQASD-IMWTISDTGWILNILCSLMEPWALGACTFVhlLPKFDPLVILKTLSSYPIKSMmgaPIV 314
Cdd:PLN02574 225 AMVELFVRFEASQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVV--MRRFDASDMVKVIDRFKVTHF---PVV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 315 YRMLL-----QQDLSSYKFPHLQNCVTVGESLLPETLENW-RAQTGLDIRESYGQTET---GLTCMVSKTMKiKPGYMGT 385
Cdd:PLN02574 300 PPILMaltkkAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTEStavGTRGFNTEKLS-KYSSVGL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 386 AASCYDVQIID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRAN 463
Cdd:PLN02574 379 LAPNMQAKVVDwSTGCLLPPGNCGELWIQ-GP----GVMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLK 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 464 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKE-LQQHVKSVTAPYKYPR 542
Cdd:PLN02574 454 EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQEaVINYVAKQVAPYKKVR 527
|
490 500
....*....|....*....|...
gi 1034593582 543 KIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PLN02574 528 KVVFVQSIPKSPAGKILRRELKR 550
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
81-563 |
1.26e-27 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 116.24 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEviqEVDTVASECPSLRIKLLvsekscdgwlnfkkllnEASTTHHCVETGSQEASAIY--FTSGTSGLPKMAEHSYSSL 238
Cdd:cd12116 92 DA---LPDRLPAGLPVLLLALA-----------------AAAAAPAAPRTPVSPDDLAYviYTSGSTGRPKGVVVSHRNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 239 G--LKAKMDAgwTGLQASDIMWTISDTGWILNILCSLMePWALGACtfVHLLPK---FDPLVILKTLSSYPIKSMMGAPI 313
Cdd:cd12116 152 VnfLHSMRER--LGLGPGDRLLAVTTYAFDISLLELLL-PLLAGAR--VVIAPRetqRDPEALARLIEAHSITVMQATPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 314 VYRMLL---QQDLSSYKfphlqncVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTcmvSKTMKIKPGY----MGTA 386
Cdd:cd12116 227 TWRMLLdagWQGRAGLT-------ALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIW---STAARVTAAAgpipIGRP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 387 ASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQF 458
Cdd:cd12116 297 LANTQVYVLDAALRPVPPGVPGELYIG-----GDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 459 MGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQfLSHDPEQLTKELQQHVKSVTAPY 538
Cdd:cd12116 372 LGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAG-AAPDAAALRAHLRATLPAYMVPS 449
|
490 500
....*....|....*....|....*
gi 1034593582 539 KYPRKIEFvlnlPKTVTGKIQRAKL 563
Cdd:cd12116 450 AFVRLDAL----PLTANGKLDRKAL 470
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
218-560 |
1.31e-27 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 113.27 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQASdimwtiSDTgwILNILCSLMEPWALGACTF-------VHLLPK 290
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSW--IESFVCNEDLFNIS------GED--AILAPGPLSHSLFLYGAISalylggtFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 291 FDPLVILKTLSSYPIKSMMGAPivyrMLLQQdLSSYKFPHL--QNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETG 367
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVP----TMLQA-LARTLEPESkiKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 368 LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVlppgtegdIG-IRVK-PIrpigIFSGYVD----NPDKtaanirgdf 441
Cdd:cd17633 150 FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGE--------IGkIFVKsEM----VFSGYVRggfsNPDG--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 442 WL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflshdp 520
Cdd:cd17633 209 WMsVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSG--------- 279
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034593582 521 EQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:cd17633 280 DKLTyKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-564 |
2.00e-27 |
|
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: 115.99 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 78 ELMWNFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 157
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 VAGDEVIqevdTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPKMAEHSY- 235
Cdd:cd05915 101 LFDPNLL----PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 236 ------SSLGLKAKMDAGWTGLQASDI-MWTISdtGWilnilCSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPIKSM 308
Cdd:cd05915 177 alvlhsLAASLVDGTALSEKDVVLPVVpMFHVN--AW-----CLPYAATLVGA-KQVLPGPRLDPASLVELFDGEGVTFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 309 MGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLlPETLENWRAQTGLDIRESYGQTET---GLTCMVSKTMKIKPGYMG 384
Cdd:cd05915 249 AGVPTVWLALADyLESTGHRLKTLRRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETspvVVQNFVKSHLESLSEEEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 385 TAASCYD-VQIIDDKGNVLPPGT-----EGDIgIRVKPIRPIGIFSGYVDNPDKTAAN-IRGDFWLLGDRGIKDEDGYFQ 457
Cdd:cd05915 328 LTLKAKTgLPIPLVRLRVADEEGrpvpkDGKA-LGEVQLKGPWITGGYYGNEEATRSAlTPDGFFRTGDIAVWDEEGYVE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 458 FMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLTKELQQHVKSVTAP 537
Cdd:cd05915 407 IKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVP------RGEKPTPEELNEHLLKAGFA 480
|
490 500
....*....|....*....|....*...
gi 1034593582 538 YKY-PRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd05915 481 KWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-563 |
2.08e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 118.34 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 161
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 EVIQEVDtVASECPSLRIKLLvsekscdgwlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLK 241
Cdd:PRK12467 618 HLLAQLP-VPAGLRSLCLDEP------------ADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANY 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 242 AKMDAGWTGLQASDIMWTISDTGWILNILcslMEPWALGACTFVHLLPK---FDPLVILKTLSSYPIKSMMGAPIVYRML 318
Cdd:PRK12467 685 VCVIAERLQLAADDSMLMVSTFAFDLGVT---ELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQAL 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 319 LQQDLSSYKFPhlQNCVTV-GESLLPETLENWRA-QTGLDIRESYGQTETglTCMVS------KTMKIKPGYMGTAASCY 390
Cdd:PRK12467 762 LQASRVALPRP--QRALVCgGEALQVDLLARVRAlGPGARLINHYGPTET--TVGVStyelsdEERDFGNVPIGQPLANL 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 391 DVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMGRA 462
Cdd:PRK12467 838 GLYILDHYLNPVPVGVVGELYIGGA-----GLARGYHRRPALTAERFVPDpfgadggrLYRTGDLARYRADGVIEYLGRM 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 463 NDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPR 542
Cdd:PRK12467 913 DHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPA 991
|
490 500
....*....|....*....|.
gi 1034593582 543 KIEFVLNLPKTVTGKIQRAKL 563
Cdd:PRK12467 992 HLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
83-565 |
4.09e-27 |
|
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: 113.94 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivagde 162
Cdd:cd17653 25 YGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP--------------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viqeVDTvasECPSLRIKLLVSEKSCdgwlnfkKLlneastthhCVETGSQEASA-IYFTSGTSGLPK--MAEHS----Y 235
Cdd:cd17653 77 ----LDA---KLPSARIQAILRTSGA-------TL---------LLTTDSPDDLAyIIFTSGSTGIPKgvMVPHRgvlnY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 236 SSLGlKAKMDA--GWTGLQASDIMWTISdTGWILNILC--------SLMEPWA--LGACTFVHLLPKFdplvilktLSSY 303
Cdd:cd17653 134 VSQP-PARLDVgpGSRVAQVLSIAFDAC-IGEIFSTLCnggtlvlaDPSDPFAhvARTVDALMSTPSI--------LSTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 304 PIKSmmgapivyrmllqqdlssykFPHLQNCVTVGESLLPETLENWRAqtGLDIRESYGQTETGLTCMVSKTMKIKPGYM 383
Cdd:cd17653 204 SPQD--------------------FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 384 GTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD-FW------LLGDRGIKDEDGYF 456
Cdd:cd17653 262 GKPIPNSTCYILDADLQPVPEGVVGEICIS-----GVQVARGYLGNPALTASKFVPDpFWpgsrmyRTGDYGRWTEDGGL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 457 QFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISspdpVRGEVVKAFVVLASQflshDPEQLTKELQQHVKSvta 536
Cdd:cd17653 337 EFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI----VVNGRLVAFVTPETV----DVDGLRSELAKHLPS--- 405
|
490 500
....*....|....*....|....*....
gi 1034593582 537 pYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:cd17653 406 -YAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
81-565 |
1.11e-26 |
|
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: 115.72 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtIqmkstDILY---RLQM----SK 153
Cdd:COG1020 502 LTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP--L-----DPAYpaeRLAYmledAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 154 AKAIVAGDEViqevdtvASECPSLRIKLLVsekscdgwLNFKKLLNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MA 231
Cdd:COG1020 574 ARLVLTQSAL-------AARLPELGVPVLA--------LDALALAAEPATNPPVPVTPDDLAYVIY-TSGSTGRPKgvMV 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 232 EHSysslGLKAKMDA--GWTGLQASDIM---WTIS-DTgwilnilcSLME---PWALGACtfVHLLPK---FDPLVILKT 299
Cdd:COG1020 638 EHR----ALVNLLAWmqRRYGLGPGDRVlqfASLSfDA--------SVWEifgALLSGAT--LVLAPPearRDPAALAEL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 300 LSSYPIKSMMGAPIVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETglTCMVSkTMKI 378
Cdd:COG1020 704 LARHRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTET--TVDST-YYEV 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 379 KPGYMGTAASCY-------DVQIIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVDNPDKTAAN-IRGDFWLL--- 444
Cdd:COG1020 779 TPPDADGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELyigGA--------GLARGYLNRPELTAERfVADPFGFPgar 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 445 ----GDRGIKDEDGYFQFMGRAND---IinsSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqfls 517
Cdd:COG1020 851 lyrtGDLARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA---- 923
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1034593582 518 hDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:COG1020 924 -GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
477-557 |
2.20e-26 |
|
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: 102.24 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 477 EVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 556
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 1034593582 557 K 557
Cdd:pfam13193 76 K 76
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-557 |
3.09e-26 |
|
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: 110.16 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPK--MAEH--SYSSLGLKAKMDAGwtglQASDIMWTI----SDTGWILNILCSLME---PWA-----LGA 281
Cdd:cd05924 8 ILYTGGTTGMPKgvMWRQedIFRMLMGGADFGTG----EFTPSEDAHkaaaAAAGTVMFPAPPLMHgtgSWTafgglLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 282 CTFVHLLPKFDPLVILKTLSSYPIKSM------MGAPIV--YRMLLQQDLSSykfphLQNCVTVGESLLPETLENW-RAQ 352
Cdd:cd05924 84 QTVVLPDDRFDPEEVWRTIEKHKVTSMtivgdaMARPLIdaLRDAGPYDLSS-----LFAISSGGALLSPEVKQGLlELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 353 TGLDIRESYGQTETGLT-CMVSKTMKIKPGYMGTAAScyDVQIIDDKGNVLPPGTE--GDIGIR-VKPIrpigifsGYVD 428
Cdd:cd05924 159 PNITLVDAFGSSETGFTgSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGgvGWIARRgHIPL-------GYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 429 NPDKTAANIR---GDFW-LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEV 504
Cdd:cd05924 230 DEAKTAETFPevdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034593582 505 VKAFVVLASqflSHDPEQltKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGK 557
Cdd:cd05924 310 VVAVVQLRE---GAGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
81-564 |
1.04e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 111.24 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELsensQQAANVLSGAC---GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDIL-YRLQM----- 151
Cdd:PRK10946 49 FSYREL----NQASDNLACSLrrqGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNaYASQIepall 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 152 --SKAKAIVAGDEVIqevDTVASECPSLRIKLLVSEkscDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK 229
Cdd:PRK10946 125 iaDRQHALFSDDDFL---NTLVAEHSSLRVVLLLND---DGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 230 MA-----EHSYSslglkakmdagwtgLQAS-DIMWTISDTGWilniLCSL--------MEPWALG---ACTFVHLLPKFD 292
Cdd:PRK10946 199 LIprthnDYYYS--------------VRRSvEICGFTPQTRY----LCALpaahnypmSSPGALGvflAGGTVVLAPDPS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 293 PLVILKTLSSYPIKSMMGAPIVYRMLLQ--------QDLSSYKFphLQncvtVGESLLPETLEnwR---AQTGLDIRESY 361
Cdd:PRK10946 261 ATLCFPLIEKHQVNVTALVPPAVSLWLQaiaeggsrAQLASLKL--LQ----VGGARLSETLA--RripAELGCQLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 362 GQTEtGLtcmVSKT-MKIKPGYMGTAASCY-----DVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKT 433
Cdd:PRK10946 333 GMAE-GL---VNYTrLDDSDERIFTTQGRPmspddEVWVADADGNPLPQGEVGRLMTR-------GpyTFRGYYKSPQHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 434 AANIRGD-FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA 512
Cdd:PRK10946 402 ASAFDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034593582 513 SQFlshDPEQLTKEL-QQHVksvtAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:PRK10946 482 EPL---KAVQLRRFLrEQGI----AEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
212-560 |
2.69e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 108.59 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 212 SQEASAIYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQASDIMWTIsdtgwilnILCSLMEPWALGACTFV------ 285
Cdd:PRK08308 100 AEEPSLLQYSSGTTGEPKLIRRSWTEI--DREIEAYNEALNCEQDETPI--------VACPVTHSYGLICGVLAaltrgs 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 286 --HLLPKFDPLVILKTLSSYPIKSMMGAPIVY----RMLLQQDlssykfpHLQNCVTVGeSLLPET-LENWRAQTgLDIR 358
Cdd:PRK08308 170 kpVIITNKNPKFALNILRNTPQHILYAVPLMLhilgRLLPGTF-------QFHAVMTSG-TPLPEAwFYKLRERT-TYMM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 359 ESYGQTETGltCM-VSKTMKiKPGYMGTAASCYDVQIIDDKGNvlpPGtegDIGIRVKpirpigifsgyvdnpDKTAANi 437
Cdd:PRK08308 241 QQYGCSEAG--CVsICPDMK-SHLDLGNPLPHVSVSAGSDENA---PE---EIVVKMG---------------DKEIFT- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 438 rgdfwllGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAfvvlasQFLS 517
Cdd:PRK08308 296 -------KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVIS 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034593582 518 H---DPEQLTKELQQHVksvtAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:PRK08308 363 HeeiDPVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSR 404
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
83-563 |
4.72e-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: 108.11 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivagde 162
Cdd:cd17652 15 YAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLP--------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viqeVDtvaSECPSLRIKLLVSEKSCdgwlnfkkllneastthHCVETGSQEASAIYFTSGTSGLPK--MAEHSysslGL 240
Cdd:cd17652 67 ----LD---PAYPAERIAYMLADARP-----------------ALLLTTPDNLAYVIYTSGSTGRPKgvVVTHR----GL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDAGWT--GLQASDIMWTISDTGWILNILCSLMepwALGACTFVHLLPKfDPLV----ILKTLSSYPIKSMMGAPIV 314
Cdd:cd17652 119 ANLAAAQIAafDVGPGSRVLQFASPSFDASVWELLM---ALLAGATLVLAPA-EELLpgepLADLLREHRITHVTLPPAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 315 YRMLLQQDLssykfPHLQNCVTVGESLLPETLENWraQTGLDIRESYGQTETGLTCMVSK---TMKIKPgyMGTAASCYD 391
Cdd:cd17652 195 LAALPPDDL-----PDLRTLVVAGEACPAELVDRW--APGRRMINAYGPTETTVCATMAGplpGGGVPP--IGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 392 VQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTA----ANIRGD----FWLLGDRGIKDEDGYFQFMGRAN 463
Cdd:cd17652 266 VYVLDARLRPVPPGVPGEL-----YIAGAGLARGYLNRPGLTAerfvADPFGApgsrMYRTGDLARWRADGQLEFLGRAD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 464 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPRK 543
Cdd:cd17652 341 DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVPAA 415
|
490 500
....*....|....*....|
gi 1034593582 544 IEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17652 416 FVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-563 |
5.56e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.82 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 108 RVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpslrIKLLVSEKS 187
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDG------LASLALDRD 4676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 188 CDgWLNFkkllneaSTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-------GLKAKMDAGWTGLQASDIMWTI 260
Cdd:PRK12316 4677 ED-WEGF-------PAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLvnhlhatGERYELTPDDRVLQFMSFSFDG 4748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 261 SDTGWilnilcslMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGES 340
Cdd:PRK12316 4749 SHEGL--------YHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEA 4820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 341 LLPETL-ENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKP---GYM--GTAASCYDVQIIDDKGNVLPPGTEGDIGIRV 414
Cdd:PRK12316 4821 VAQASYdLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDAcgaAYMpiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGG 4900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 415 KpirpiGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHP 486
Cdd:PRK12316 4901 E-----GVARGYLERPALTAERFVPDpfgapggrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHP 4975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 487 AVVETAVISSPDPVRGEVVkAFVVLASQFLSHDPE---QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:PRK12316 4976 AVREAVVIAQEGAVGKQLV-GYVVPQDPALADADEaqaELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
81-566 |
6.86e-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: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEviQEVD---TVASECPSLRIKLLVSEKSC----DGWLNFKKLLNEASTTHHCVETGSQEA----------SAIYFTSG 223
Cdd:cd17641 91 DE--EQVDkllEIADRIPSVRYVIYCDPRGMrkydDPRLISFEDVVALGRALDRRDPGLYERevaagkgedvAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 224 TSGLPKMA--------EHSYSSLGLKAK---------MDAGWTGLQasdiMWTISD---TGWILNILCS---LMEPWALG 280
Cdd:cd17641 169 TTGKPKLAmlshgnflGHCAAYLAADPLgpgdeyvsvLPLPWIGEQ----MYSVGQalvCGFIVNFPEEpetMMEDLREI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 281 ACTFVHLLPK-FDPL---VILKTLSSYPIKSMM-------------------------------GAPIVYRMLLQQdlss 325
Cdd:cd17641 245 GPTFVLLPPRvWEGIaadVRARMMDATPFKRFMfelgmklglraldrgkrgrpvslwlrlaswlADALLFRPLRDR---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 326 YKFPHLQNCVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIiDDKGNVLppg 405
Cdd:cd17641 321 LGFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVGEIL--- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 406 tegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRANDIINSS-GYRIGPSEVENALM 483
Cdd:cd17641 396 -----------VRSPGVFVGYYKNPEATAEDFDEDGWLHtGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 484 EHPAVVETAVISSPDP-------VRGEVV------KAFVVLASQFLSHDPEqLTKELQQHVKSVTAPYKYPRKIEFVLNL 550
Cdd:cd17641 465 FSPYIAEAVVLGAGRPyltaficIDYAIVgkwaeqRGIAFTTYTDLASRPE-VYELIRKEVEKVNASLPEAQRIRRFLLL 543
|
570 580
....*....|....*....|....*
gi 1034593582 551 PK---------TVTGKIQRAKLRDK 566
Cdd:cd17641 544 YKeldaddgelTRTRKVRRGVIAEK 568
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
82-574 |
6.02e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 105.60 E-value: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSGAcGLQRGDRVAVV---LPRVPEWWLVILGcirAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 158
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWYGIMG---IGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 159 AGDEVIQEVDTVASECPSLRIKLLVSEKS------CDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 232
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTDAAhmpqttLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 233 HSYSSLGLKAKM--DAGWTGLQASDIMWTI----SDTGWILNILCSLMepwalGAcTFVHLLPKFDPLVILKTLSSYPIK 306
Cdd:PRK06018 197 YSHRSNVLHALManNGDALGTSAADTMLPVvplfHANSWGIAFSAPSM-----GT-KLVMPGAKLDGASVYELLDTEKVT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 307 SMMGAPIVYRMLLQQ-DLSSYKFPHLqNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSK----------- 374
Cdd:PRK06018 271 FTAGVPTVWLMLLQYmEKEGLKLPHL-KMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAAlkppfsklpgd 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 375 ---TMKIKPGYmgtAASCYDVQIIDDKGNVLPpgTEGDIGIRVKpIRPIGIFSGYVdnpdKTAANIRGD--FWLLGDRGI 449
Cdd:PRK06018 350 arlDVLQKQGY---PPFGVEMKITDDAGKELP--WDGKTFGRLK-VRGPAVAAAYY----RVDGEILDDdgFFDTGDVAT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 450 KDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTK-ELQ 528
Cdd:PRK06018 420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG------ETATReEIL 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1034593582 529 QHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD--KEWKMSGKA 574
Cdd:PRK06018 494 KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREqfKDYKLPTAA 541
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
212-565 |
7.79e-24 |
|
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: 104.93 E-value: 7.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 212 SQEASAIY--FTSGTSGLPK--MAEHSYSSLGLKA-----KMDAGWTGLQASDIMWTISdtgwILNILCSLMepwaLGAC 282
Cdd:cd05918 103 SSPSDAAYviFTSGSTGKPKgvVIEHRALSTSALAhgralGLTSESRVLQFASYTFDVS----ILEIFTTLA----AGGC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 283 TFVhlLPKFDPLVIL-KTLSSYPIKSMMGAPIVYRMLLQQDlssykFPHLQNCVTVGESLLPETLENWraQTGLDIRESY 361
Cdd:cd05918 175 LCI--PSEEDRLNDLaGFINRLRVTWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTW--ADRVRLINAY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 362 GQTETGLTCMVSK-TMKIKPGYMGTAASCydVQIIDDKGN---VLPPGTEGDI---GirvkPIrpigIFSGYVDNPDKTA 434
Cdd:cd05918 246 GPAECTIAATVSPvVPSTDPRNIGRPLGA--TCWVVDPDNhdrLVPIGAVGELlieG----PI----LARGYLNDPEKTA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 435 AN-IRGDFWLL-------------GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAV---VETAVISSP 497
Cdd:cd05918 316 AAfIEDPAWLKqegsgrgrrlyrtGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGakeVVVEVVKPK 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 498 DPVRGEVVKAFVVLASQFLSHDPEQ------------LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:cd05918 396 DGSSSPQLVAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
76-560 |
2.11e-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: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 76 GKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAK 155
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 156 AIVAGDEviqevDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSGTSGLPKMAEHSY 235
Cdd:cd05914 82 AIFVSDE-----DDVA---------------------------------------------LINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 236 SSLglKAKMDAG--WTGLQASDIMWTISDTGWILNILCSLMEPWALGActFVHLLPKFDPLVILKtLSSYPIKSMMGAPI 313
Cdd:cd05914 112 RNI--VSNVDGVkeVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGA--HVVFLDKIPSAKIIA-LAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 314 VYRM--------LLQQDLSSYKFP------------------------HLQNCVTVGESLLPETLENWRaQTGLDIRESY 361
Cdd:cd05914 187 PLVIekifkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLR-TIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 362 GQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKgnvlPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDF 441
Cdd:cd05914 266 GMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP-----NVMKGYYKNPEATAEAFDKDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 442 WL-LGDRGIKDEDGYFQFMGRA-NDIINSSGYRIGPSEVENALMEHPAVVETAVIsspdpVRGEVVKAFVVLASQFL--- 516
Cdd:cd05914 337 WFhTGDLGKIDAEGYLYIRGRKkEMIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFLdvk 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034593582 517 ----SHDPEQLTKELQQHVKSVTAPYKYPRKIEFVL-NLPKTVTGKIQR 560
Cdd:cd05914 412 alkqRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVKeEFEKTPKGKIKR 460
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
83-563 |
2.70e-23 |
|
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: 102.77 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagde 162
Cdd:cd17643 15 YGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVP-------IDPAY--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viqevdtvasecPSLRIKLLV--SEKSCdgwlnfkkLLNEASTThhcvetgsqeASAIYfTSGTSGLPK--MAEHSySSL 238
Cdd:cd17643 72 ------------PVERIAFILadSGPSL--------LLTDPDDL----------AYVIY-TSGSTGRPKgvVVSHA-NVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 239 GLKAKMDAgWTGLQASDIMWTISDTGWILnilcSLMEPW-ALGACTFVHLLPKF---DPLVILKTLSSYPIKSMMGAPIV 314
Cdd:cd17643 120 ALFAATQR-WFGFNEDDVWTLFHSYAFDF----SVWEIWgALLHGGRLVVVPYEvarSPEDFARLLRDEGVTVLNQTPSA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 315 YRMLLQQDLSSYKFPH-LQNCVTVGESLLPETLENWRAQTGL---DIRESYGQTETglTCMVSKTmKIKPGYMGTAA--- 387
Cdd:cd17643 195 FYQLVEAADRDGRDPLaLRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITET--TVHVTFR-PLDAADLPAAAasp 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 388 -----SCYDVQIIDDKGNVLPPGTEGDIGIRvkpiRPiGIFSGYVDNPDKTAANIRGD-FWLLGDRGIKDED-------G 454
Cdd:cd17643 272 igrplPGLRVYVLDADGRPVPPGVVGELYVS----GA-GVARGYLGRPELTAERFVANpFGGPGSRMYRTGDlarrlpdG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 455 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdPEQLTKELQQHVKSV 534
Cdd:cd17643 347 ELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG-----AAADIAELRALLKEL 421
|
490 500
....*....|....*....|....*....
gi 1034593582 535 TAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17643 422 LPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
218-568 |
3.74e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 103.18 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWtisdtgwilniLC-------SLMEPW--ALGACTFVHLL 288
Cdd:PRK13388 155 LIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCY-----------VSmplfhsnAVMAGWapAVASGAAVALP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 289 PKFDPLVILKTLSSYPIKSM--MGAPIVYRMLlqqdlSSYKFPHLQNCVTV--GESLLPETLENWRAQTGLDIRESYGQT 364
Cdd:PRK13388 224 AKFSASGFLDDVRRYGATYFnyVGKPLAYILA-----TPERPDDADNPLRVafGNEASPRDIAEFSRRFGCQVEDGYGSS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 365 ETGltCMVSKTMKIKPGYMGTAAScyDVQIID-DKGNVLPPGTEGDIGIRVKPIRPIG---------IFSGYVDNPDKTA 434
Cdd:PRK13388 299 EGA--VIVVREPGTPPGSIGRGAP--GVAIYNpETLTECAVARFDAHGALLNADEAIGelvntagagFFEGYYNNPEATA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 435 ANIR-GDFWLlGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAs 513
Cdd:PRK13388 375 ERMRhGMYWS-GDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLR- 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034593582 514 QFLSHDPEQLTKELqqHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 568
Cdd:PRK13388 453 DGATFDPDAFAAFL--AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGW 505
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
81-565 |
4.83e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 102.86 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLsGACGLQRGDRVAVVL---PRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyRLQMSKAKAI 157
Cdd:PRK07008 40 YTYRDCERRAKQLAQAL-AALGVEPGDRVGTLAwngYRHLEAYYGVSGSGAVCHTINP------------RLFPEQIAYI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 V--AGDEVI-------QEVDTVASECPSLRIKLLVSEKS---CDG--WLNFKKLLNEASTTHHCVETGSQEASAIYFTSG 223
Cdd:PRK07008 107 VnhAEDRYVlfdltflPLVDALAPQCPNVKGWVAMTDAAhlpAGStpLLCYETLVGAQDGDYDWPRFDENQASSLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 224 TSGLPKMAEHSYSSLGLKAKM----DAgwTGLQASDI------MWTISdtGWILNILCslmepwALGACTFVHLLPKFDP 293
Cdd:PRK07008 187 TTGNPKGALYSHRSTVLHAYGaalpDA--MGLSARDAvlpvvpMFHVN--AWGLPYSA------PLTGAKLVLPGPDLDG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 294 LVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTET---GLT 369
Cdd:PRK07008 257 KSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMsplGTL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 370 C-MVSKTMKIKPG-------YMGTAASCYDVQIIDDKGNVLP--PGTEGDIGIRvkpirpiG--IFSGYVdnpdKTAANI 437
Cdd:PRK07008 337 CkLKWKHSQLPLDeqrklleKQGRVIYGVDMKIVGDDGRELPwdGKAFGDLQVR-------GpwVIDRYF----RGDASP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 438 RGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFl 516
Cdd:PRK07008 406 LVDGWFpTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA- 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1034593582 517 shdpeQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK07008 485 -----EVTReELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
91-565 |
3.04e-22 |
|
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: 100.43 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 91 QQAANVLSG--ACGLQRGDRVAVVLPR----VPEWWlvilGCIRAGLIFMPGTIQMKSTDI------LYRL-QMSKAKAI 157
Cdd:cd05906 47 EDARRLAAGlrQLGLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPTYDEPnarlrkLRHIwQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 VAGDEVIQEVDTVASECPSLRIKLLVSEkscdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 237
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIE-----------ELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 238 LgLKAKMDAGWT-GLQASDImwtisdtgwILNilcslmepWA----LGACTFVHLLPKF---------------DPLVIL 297
Cdd:cd05906 192 I-LARSAGKIQHnGLTPQDV---------FLN--------WVpldhVGGLVELHLRAVYlgcqqvhvpteeilaDPLRWL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 298 KTLSSYPIkSMMGAP-IVYRMLLQQ---------DLSSYKFphlqnCVTVGESLLPETLENWR---AQTGLD---IRESY 361
Cdd:cd05906 254 DLIDRYRV-TITWAPnFAFALLNDLleeiedgtwDLSSLRY-----LVNAGEAVVAKTIRRLLrllEPYGLPpdaIRPAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 362 GQTETGLTCMVSKTMkikPGYMGTAA-------SCY---DVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPD 431
Cdd:cd05906 328 GMTETCSGVIYSRSF---PTYDHSQAlefvslgRPIpgvSMRIVDDEGQLLPEGEVGRLQVRGPVV-----TKGYYNNPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 432 KTAANIRGDFWL-LGDRGIKDeDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVE--TAVISSPDPVRGEVVKAF 508
Cdd:cd05906 400 ANAEAFTEDGWFrTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAI 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034593582 509 VVLASQFLSHDPEQLTKELQQHVK---SVTAPYKYP-RKIEFvlnlPKTVTGKIQRAKLRD 565
Cdd:cd05906 479 FFVPEYDLQDALSETLRAIRSVVSrevGVSPAYLIPlPKEEI----PKTSLGKIQRSKLKA 535
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
218-560 |
7.67e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 99.82 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPKMAEHSYSS--LGLKAKmdagWTGLQASD---IMWTISDTGWIL--NILCSLMepwALGaCTFVH---- 286
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPhlVGLKYY----WRSIIEKDiptVVFSHSSIGWVSfhGFLYGSL---SLG-NTFVMfegg 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 287 -LLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD------LSSYKFPHLQNCVTVGESL---LPETLENwraqtGLD 356
Cdd:PTZ00237 331 iIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIeesIPEYIEN-----KLK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 357 IRES--YGQTETGLTCMVSKTMKIKPGY-MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVkPIRPiGIFSGYVDNPD-- 431
Cdd:PTZ00237 406 IKSSrgYGQTEIGITYLYCYGHINIPYNaTGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPP-SFATTFYKNDEkf 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 432 KTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL 511
Cdd:PTZ00237 484 KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVL 563
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034593582 512 ASQFLSH--DPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 560
Cdd:PTZ00237 564 KQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
81-563 |
8.86e-22 |
|
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: 98.50 E-value: 8.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 160
Cdd:cd12114 13 LTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEViqevdtvASECPSLRIKLLVSEKSCDGWLNFKKllneastthhcVETGSQEASAIYFTSGTSGLPK--MAEHSySSL 238
Cdd:cd12114 92 GPD-------AQLDVAVFDVLILDLDALAAPAPPPP-----------VDVAPDDLAYVIFTSGSTGTPKgvMISHR-AAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 239 GLKAKMDAGWtGLQASDIMWTISDTGWILNILcSLMEPWALGAcTFVhlLP----KFDPLVILKTLSSYPIKSMMGAPIV 314
Cdd:cd12114 153 NTILDINRRF-AVGPDDRVLALSSLSFDLSVY-DIFGALSAGA-TLV--LPdearRRDPAHWAELIERHGVTLWNSVPAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 315 YRMLLQQDLSSYKFPHLQNCVTVGESL----LPETLenWRAQTGLDIRESYGQTETGLTCMVSKTMKIKP-------GYM 383
Cdd:cd12114 228 LEMLLDVLEAAQALLPSLRLVLLSGDWipldLPARL--RALAPDARLISLGGATEASIWSIYHPIDEVPPdwrsipyGRP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 384 GTAASCYdvqIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAA-----NIRGDFWLLGDRGIKDEDGYFQF 458
Cdd:cd12114 306 LANQRYR---VLDPRGRDCPDWVPGELWIG-----GRGVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGTLEF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 459 MGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPvRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSvtapY 538
Cdd:cd12114 378 LGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPA----Y 452
|
490 500
....*....|....*....|....*
gi 1034593582 539 KYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd12114 453 MIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
83-563 |
1.11e-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: 98.16 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagde 162
Cdd:cd12115 27 YAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP-------LDPAY--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viqevdtvasecPSLRIKLLVSEKSCdgwlnfkkllneastthHCVETGSQEASAIYFTSGTSGLPK--MAEHSysslGL 240
Cdd:cd12115 84 ------------PPERLRFILEDAQA-----------------RLVLTDPDDLAYVIYTSGSTGRPKgvAIEHR----NA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 241 KAKMDagWTG-----------LQASDIMWTISdtgwILNILCSLMEpwalGACtfVHLLpkfDPLVILKTLSSYPIKSMM 309
Cdd:cd12115 131 AAFLQ--WAAaafsaeelagvLASTSICFDLS----VFELFGPLAT----GGK--VVLA---DNVLALPDLPAAAEVTLI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 310 GA-PIVYRMLLQQDlssyKFPHLQNCVTV-GESLLPETLENWRAQTGLD-IRESYGQTET---GLTCMVSKTMKIKPGyM 383
Cdd:cd12115 196 NTvPSAAAELLRHD----ALPASVRVVNLaGEPLPRDLVQRLYARLQVErVVNLYGPSEDttySTVAPVPPGASGEVS-I 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 384 GTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTAANIRGD-------FWLLGDRGIKDEDGYF 456
Cdd:cd12115 271 GRPLANTQAYVLDRALQPVPLGVPGEL-----YIGGAGVARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 457 QFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqfLSHDPEQLTKELQQHVKSVTA 536
Cdd:cd12115 346 EFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV-----AEPGAAGLVEDLRRHLGTRLP 420
|
490 500
....*....|....*....|....*..
gi 1034593582 537 PYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd12115 421 AYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-563 |
2.53e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.26 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 2 HWLRKVQGLCTLWGTQMSSRTLyINSRQLVSLQWGHQEVPAKFNFASDVLDHWadmEKAGKRLP-SPALwwVNGkgkELM 80
Cdd:PRK12316 466 HWQNLLRGMVENPQARVDELPM-LDAEERGQLVEGWNATAAEYPLQRGVHRLF---EEQVERTPeAPAL--AFG---EET 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA- 159
Cdd:PRK12316 537 LDYAELNRRANRLAHALI-ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSq 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 160 ---GDE--VIQEVDTVASECPSLrikllvsekscdgWLNFKKllNEASTTHHCVEtgsQEASAIYfTSGTSGLPKMAEHS 234
Cdd:PRK12316 616 shlGRKlpLAAGVQVLDLDRPAA-------------WLEGYS--EENPGTELNPE---NLAYVIY-TSGSTGKPKGAGNR 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 235 YSSLglKAKMDAGWT--GLQASDIMWTISDTGWILNILcslMEPWALGACTFVHLLPK---FDPLVILKTLSSYPIKSMM 309
Cdd:PRK12316 677 HRAL--SNRLCWMQQayGLGVGDTVLQKTPFSFDVSVW---EFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLH 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 310 GAPIVYRMLLQ----QDLSSykfphLQNCVTVGESL---LPETLENWRAQTGLdiRESYGQTETGL-----TCMVSKTMK 377
Cdd:PRK12316 752 FVPSMLQAFLQdedvASCTS-----LRRIVCSGEALpadAQEQVFAKLPQAGL--YNLYGPTEAAIdvthwTCVEEGGDS 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 378 IKPGYMGTAASCYdvqIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTA----ANIRGD---FWLLGDRGIK 450
Cdd:PRK12316 825 VPIGRPIANLACY---ILDANLEPVPVGVLGELYLAGR-----GLARGYHGRPGLTAerfvPSPFVAgerMYRTGDLARY 896
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 451 DEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISspdpVRGEVVKAFVVLasqflsHDPEQLTKE-LQQ 529
Cdd:PRK12316 897 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVL------ESEGGDWREaLKA 966
|
570 580 590
....*....|....*....|....*....|....
gi 1034593582 530 HVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:PRK12316 967 HLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-563 |
3.01e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.88 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 2 HWLRKVQGLC-TLWGTQMSSRTLYINSRQLVSLQWGHQEVPakfnFASDVLDHWADMEKAGKRLPSPALWWvngkGKELM 80
Cdd:PRK12316 1958 HLLHLLEQMAeDAQAALGELALLDAGERQRILADWDRTPEA----YPRGPGVHQRIAEQAARAPEAIAVVF----GDQHL 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 wNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAkAIVAG 160
Cdd:PRK12316 2030 -SYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGA-ALLLT 2106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 DEVIQEVDTVASECPSLRIkllvsekSCDGWLNfkkllnEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-- 238
Cdd:PRK12316 2107 QRHLLERLPLPAGVARLPL-------DRDAEWA------DYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALva 2173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 239 -----GLKAKMDAGWTGLQASDIMWTISDTGWilnilcslMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPI 313
Cdd:PRK12316 2174 hcqaaGERYELSPADCELQFMSFSFDGAHEQW--------FHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPV 2245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 314 VYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLEN-WRAQTGLDIRESYGQTETGLTCMVSKTMKIKPG---YM--GTAA 387
Cdd:PRK12316 2246 YLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgaaYVpiGRAL 2325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 388 SCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTA--------ANIRGDFWLLGDRGIKDEDGYFQFM 459
Cdd:PRK12316 2326 GNRRAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYL 2400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 460 GRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSpDPVRGEVVKAFVVlasqflSHDP-EQLTKELQQHVKSVTAPY 538
Cdd:PRK12316 2401 GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV------PDDAaEDLLAELRAWLAARLPAY 2473
|
570 580
....*....|....*....|....*
gi 1034593582 539 KYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:PRK12316 2474 MVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
81-563 |
4.49e-21 |
|
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: 96.08 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 160
Cdd:cd17645 24 LTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPK--MAEH-SYSS 237
Cdd:cd17645 101 -------------------------------------------------TNPDDLAYVIYTSGSTGLPKgvMIEHhNLVN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 238 LGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSlmepWALGACtfVHLLPKFDPLVILK----------TLSSYPIKs 307
Cdd:cd17645 132 LCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPH----LTAGAA--LHVVPSERRLDLDAlndyfnqegiTISFLPTG- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 308 mmgapiVYRMLLQQDLSSykfphLQNCVTVGESLlpetleNWRAQTGLDIRESYGQTEtgltCMVSKTM-KIKPGY---- 382
Cdd:cd17645 205 ------AAEQFMQLDNQS-----LRVLLTGGDKL------KKIERKGYKLVNNYGPTE----NTVVATSfEIDKPYanip 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 383 MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKD-------EDGY 455
Cdd:cd17645 264 IGKPIDNTRVYILDEALQLQPIGVAGELCIAGE-----GLARGYLNRPELTAEKFIVHPFVPGERMYRTgdlakflPDGN 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 456 FQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDPEqltkELQQHVKSVT 535
Cdd:cd17645 339 IEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEI---PHE----ELREWLKNDL 411
|
490 500
....*....|....*....|....*...
gi 1034593582 536 APYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17645 412 PDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
218-563 |
2.59e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 94.29 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPKmaehsysSLGLKAKMDAGwTGLQASDIMWTISDTGWILNI---------LCSLMEPWALGACTFVHll 288
Cdd:PRK13383 179 VLLTSGTTGKPK-------GVPRAPQLRSA-VGVWVTILDRTRLRTGSRISVampmfhglgLGMLMLTIALGGTVLTH-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 289 PKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ---QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTE 365
Cdd:PRK13383 249 RHFDAEAALAQASLHRADAFTAVPVVLARILElppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 366 TGLTCMVSKT-MKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRpigifSGYVDNPDKtaANIRGdFWLL 444
Cdd:PRK13383 329 VGIGALATPAdLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAG-----TRYTDGGGK--AVVDG-MTST 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 445 GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEQlt 524
Cdd:PRK13383 401 GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ-- 477
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034593582 525 keLQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:PRK13383 478 --LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
81-563 |
1.13e-19 |
|
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: 92.15 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKaivag 160
Cdd:cd17656 14 LTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVR----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 deviqevdtvasecpslrikLLVSEKSCDGWLNFKK--------LLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--M 230
Cdd:cd17656 88 --------------------VVLTQRHLKSKLSFNKstilledpSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKgvQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 231 AEHSySSLGL------KAKMDAGWTGLQASDIMWTISDTGwILNILCSlmepwalGACtfVHLLPK-----FDPLVILkt 299
Cdd:cd17656 148 LEHK-NMVNLlhfereKTNINFSDKVLQFATCSFDVCYQE-IFSTLLS-------GGT--LYIIREetkrdVEQLFDL-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 300 LSSYPIKSMmgapIVYRMLLQQDLSSYKF-PHLQNCV----TVGESL-LPETLENWRAQTGLDIRESYGQTETGL--TCM 371
Cdd:cd17656 215 VKRHNIEVV----FLPVAFLKFIFSEREFiNRFPTCVkhiiTAGEQLvITNEFKEMLHEHNVHLHNHYGPSETHVvtTYT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 372 VSKTMKIkPGY--MGTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTA---------ANIRgd 440
Cdd:cd17656 291 INPEAEI-PELppIGKPISNTWIYILDQEQQLQPQGIVGEL-----YISGASVARGYLNRQELTAekffpdpfdPNER-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 441 FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflshdP 520
Cdd:cd17656 363 MYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---------M 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1034593582 521 EQL--TKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17656 434 EQElnISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
81-565 |
1.18e-19 |
|
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: 92.30 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGACGlqRGDRVAVVLPRVPEWWLVILGCIRAGLI----FMPGtiqmkSTDILYRLQ----MS 152
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIavplPPPT-----PGRHAERLAailaDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 153 KAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKScdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 232
Cdd:cd05931 98 GPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDL---------LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 233 HSYSSLG--LKAkMDAGWtGLQASDIM--W--TISDTGWILNIL--------CSLMEPWAlgactFVHllpkfDPLVILK 298
Cdd:cd05931 169 VTHRNLLanVRQ-IRRAY-GLDPGDVVvsWlpLYHDMGLIGGLLtplysggpSVLMSPAA-----FLR-----RPLRWLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 299 TLSSYPIkSMMGAP------IVYRMLLQQ----DLSSykfphLQNCVTVGESLLPETLENWR---AQTGLD---IRESYG 362
Cdd:cd05931 237 LISRYRA-TISAAPnfaydlCVRRVRDEDleglDLSS-----WRVALNGAEPVRPATLRRFAeafAPFGFRpeaFRPSYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 363 QTETglTCMVSkTMKIKPGY-----------------------------MGTAASCYDVQIIDDKGN-VLPPGTEGDIGI 412
Cdd:cd05931 311 LAEA--TLFVS-GGPPGTGPvvlrvdrdalagravavaaddpaarelvsCGRPLPDQEVRIVDPETGrELPDGEVGEIWV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 413 RvkpirpiG--IFSGYVDNPDKTA------ANIRGDFWL-LGDRGIKDeDGYFQFMGRANDIINSSGYRIGPSEVENALM 483
Cdd:cd05931 388 R-------GpsVASGYWGRPEATAetfgalAATDEGGWLrTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 484 E-HPAVVET--AVISSPDPVRGEVVkAFVVLASQFLSHDPEQLTKELQQHVKS---VTapykyPRKIEFVLN--LPKTVT 555
Cdd:cd05931 460 EaHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA-----PADVVLVRPgsIPRTSS 533
|
570
....*....|
gi 1034593582 556 GKIQRAKLRD 565
Cdd:cd05931 534 GKIQRRACRA 543
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
208-563 |
1.45e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 208 VETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILcSLMEPWALGACTFVHL 287
Cdd:PRK12316 3191 IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVE-ELFWPLMSGARVVLAG 3269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 288 LPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPHLQNCVTVGESLLPETLENWRAqtGLDIRESYGQTET 366
Cdd:PRK12316 3270 PEDWrDPALLVELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEA 3346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 367 GLTCMVSKTMKIKPGY--MGTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTAANIRGDFWLL 444
Cdd:PRK12316 3347 TITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGEL-----YLGGEGLARGYHNRPGLTAERFVPDPFVP 3421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 445 GDRGIKD-------EDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISspdpVRGEVVKAFVVLASQfls 517
Cdd:PRK12316 3422 GERLYRTgdlaryrADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE--- 3494
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034593582 518 hdPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:PRK12316 3495 --AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
124-563 |
3.75e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 90.72 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 124 LGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgdevIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEAST 203
Cdd:PRK04813 70 LGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIA----TEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 204 THhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLglkakmdagwtglqasdimwtISDTGWILN---------IL---- 270
Cdd:PRK04813 146 YY------------IIFTSGTTGKPKGVQISHDNL---------------------VSFTNWMLEdfalpegpqFLnqap 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 271 ----CSLMEpW----ALGAcTFVhLLPK---FDPLVILKTLSSYPIKSMMGAPIVYRM-LLQQDLSSYKFPHLQNCVTVG 338
Cdd:PRK04813 193 ysfdLSVMD-LyptlASGG-TLV-ALPKdmtANFKQLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 339 ESLLPETlenwrAQTGLD------IRESYGQTETglTCMVSK---TMKIKPGY----MGTAASCYDVQIIDDKGNVLPPG 405
Cdd:PRK04813 270 EELPHKT-----AKKLLErfpsatIYNTYGPTEA--TVAVTSieiTDEMLDQYkrlpIGYAKPDSPLLIIDEEGTKLPDG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 406 TEGDIGIrvkpirpIG--IFSGYVDNPDKTAANirgdFWLL--------GDRGIKDeDGYFQFMGRANDIINSSGYRIGP 475
Cdd:PRK04813 343 EQGEIVI-------SGpsVSKGYLNNPEKTAEA----FFTFdgqpayhtGDAGYLE-DGLLFYQGRIDFQIKLNGYRIEL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 476 SEVENALMEHPAVVETAVIsspdPV-RGEVVK---AFVVLASqflsHDPE---QLTKELQQHVKSVTAPYKYPRKIEFVL 548
Cdd:PRK04813 411 EEIEQNLRQSSYVESAVVV----PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRD 482
|
490
....*....|....*
gi 1034593582 549 NLPKTVTGKIQRAKL 563
Cdd:PRK04813 483 SLPLTPNGKIDRKAL 497
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
207-565 |
7.28e-19 |
|
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: 89.70 E-value: 7.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 207 CVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-----GLKAKMDAgwtglQASDIMwtisdtgwiLNIL---------CS 272
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLlanveQITAIFDP-----NPEDVV---------FGALpffhsfgltGC 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 273 LMEPWALGACTFVHllpkFDPL---VILKTLSSYPIKSMMGAPIVYRMLLQQdLSSYKFPHLQNCVTVGESLLPETLENW 349
Cdd:cd05909 207 LWLPLLSGIKVVFH----PNPLdykKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEF 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 350 RAQTGLDIRESYGQTETGLTCMVSK-TMKIKPGYMGTAASCYDVQIIDDKGNV-LPPGTEGDIGIRvkpirpiG--IFSG 425
Cdd:cd05909 282 QEKFGIRILEGYGTTECSPVISVNTpQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVR-------GpnVMLG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 426 YVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEH-PAVVETAVISSPDPVRGEV 504
Cdd:cd05909 355 YLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034593582 505 VKAFVVLasqflsHDPEQLtkELQQHVKSVTAPYKY-PRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:cd05909 435 IVLLTTT------TDTDPS--SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
83-563 |
7.76e-19 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 89.38 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRvPEWWLV-ILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagd 161
Cdd:cd17648 15 YRELNERANRLAHYLLSVAEIRPDDLVGLVLDK-SELMIIaILAVWKAGAAYVP-------IDPSY-------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 eviqevdtvasecPSLRIKLLVSEkscdgwlnfkkllneasTTHHCVETGSQEASAIYFTSGTSGLPK--MAEHSySSLG 239
Cdd:cd17648 73 -------------PDERIQFILED-----------------TGARVVITNSTDLAYAIYTSGTTGKPKgvLVEHG-SVVN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 240 LKAKMDAGWtGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLP--KFDPLVILKTLSSYPIKSMMGAPIVyrm 317
Cdd:cd17648 122 LRTSLSERY-FGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDemRFDPDRFYAYINREKVTYLSGTPSV--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 318 lLQQ-DLSSykFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS-------KTMKIKPGYMGTAasC 389
Cdd:cd17648 198 -LQQyDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRffpgdqrFDKSLGRPVRNTK--C 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 390 YdvqIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTA----AN--------IRGDFWLL---GDRGIKDEDG 454
Cdd:cd17648 273 Y---VLNDAMKRVPVGAVGEL-----YLGGDGVARGYLNRPELTAerflPNpfqteqerARGRNARLyktGDLVRWLPSG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 455 YFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRG-EVVKAFVVlasQFLSHDPEQLTK-ELQQHVK 532
Cdd:cd17648 345 ELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAqSRIQKYLV---GYYLPEPGHVPEsDLLSFLR 421
|
490 500 510
....*....|....*....|....*....|.
gi 1034593582 533 SVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17648 422 AKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
83-563 |
3.23e-18 |
|
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: 88.12 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEW---W--LVILGCIRAgliFMPGTIQMKStdILYRLQMSKAKAI 157
Cdd:cd05938 8 YRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWlgLAKLGCPVA---FLNTNIRSKS--LLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 VAGDEVIQEVDTVaseCPSLR-----IKLLVSEKSCDGWLNFKKLLNEASTT-----HHCVETGSQEASAIYfTSGTSGL 227
Cdd:cd05938 83 VVAPELQEAVEEV---LPALRadgvsVWYLSHTSNTEGVISLLDKVDAASDEpvpasLRAHVTIKSPALYIY-TSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 228 PKMAEHSYsslgLKAKMDAGWT---GLQASDIMWTI----SDTGWILNILCSLmepwALGAcTFVhLLPKFDPLVILKTL 300
Cdd:cd05938 159 PKAARISH----LRVLQCSGFLslcGVTADDVIYITlplyHSSGFLLGIGGCI----ELGA-TCV-LKPKFSASQFWDDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 301 SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNcVTVGESLLPETLENWRAQTG-LDIRESYGQTEtGLTCMVSKTMKIk 379
Cdd:cd05938 229 RKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVR-LAIGNGLRADVWREFLRRFGpIRIREFYGSTE-GNIGFFNYTGKI- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 380 pGYMGTaASC------------YDVQ----IIDDKGNVLPPGTeGDIGIRVKPIRPIGIFSGYVDNP----DKTAANI-- 437
Cdd:cd05938 306 -GAVGR-VSYlykllfpfelikFDVEkeepVRDAQGFCIPVAK-GEPGLLVAKITQQSPFLGYAGDKeqteKKLLRDVfk 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 438 RGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLAsqf 515
Cdd:cd05938 383 KGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKLK--- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034593582 516 lshDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd05938 460 ---PGHEFDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
48-493 |
3.35e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 88.01 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 48 SDVLDHWADmeKAGKRlpsPALwwvNGKGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCI 127
Cdd:PRK08279 40 GDVFEEAAA--RHPDR---PAL---LFEDQSI--SYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 128 RAGLIF-MPGTIQMKstDIL-YRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCD---GWLNFKKLLNEAS 202
Cdd:PRK08279 109 KLGAVVaLLNTQQRG--AVLaHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDdpeGYEDLAAAAAGAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 203 TTHHCVETGSQ-EASAIY-FTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTI----SDTGwiLNI-LCSLMe 275
Cdd:PRK08279 187 TTNPASRSGVTaKDTAFYiYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCClplyHNTG--GTVaWSSVL- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 276 pwaLGACTFVhLLPKFD-----PLVILK--TLssypiksmmgapIVY-----RMLLQQDLSSYKFPHLQNCVtVGESLLP 343
Cdd:PRK08279 264 ---AAGATLA-LRRKFSasrfwDDVRRYraTA------------FQYigelcRYLLNQPPKPTDRDHRLRLM-IGNGLRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 344 ETLENWRAQTGLD-IRESYGQTE--TGLTCM--VSKTMKIKPGYMGTAASC--YDVQ----IIDDKGNVLPPGTeGDIGI 412
Cdd:PRK08279 327 DIWDEFQQRFGIPrILEFYAASEgnVGFINVfnFDGTVGRVPLWLAHPYAIvkYDVDtgepVRDADGRCIKVKP-GEVGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 413 RVKPIRPIGIFSGYVDnPDKTAANI------RGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEH 485
Cdd:PRK08279 406 LIGRITDRGPFDGYTD-PEASEKKIlrdvfkKGDAWFnTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGF 484
|
....*...
gi 1034593582 486 PAVVETAV 493
Cdd:PRK08279 485 PGVEEAVV 492
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
100-563 |
1.10e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 86.22 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 100 ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV---IQEVDTVASECPS 176
Cdd:PRK05857 60 AQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSkmaSSAVPEALHSIPV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 177 LRIKLL--VSEKSCDGWLNFKKLLneastthhcVETGSQEASAIYFTSGTSGLPK---MAEHSYSSLG--LKAK------ 243
Cdd:PRK05857 140 IAVDIAavTRESEHSLDAASLAGN---------ADQGSEDPLAMIFTSGTTGEPKavlLANRTFFAVPdiLQKEglnwvt 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 244 ---MDAGWTGLQASDI--MWtisdtgWILNilcSLMEPwalGACtfvhLLPKFDPLVILKTLSSYPIKSMMGAP-IVYRM 317
Cdd:PRK05857 211 wvvGETTYSPLPATHIggLW------WILT---CLMHG---GLC----VTGGENTTSLLEILTTNAVATTCLVPtLLSKL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 318 LLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKT-----MKIKPGYMGTAASCYDV 392
Cdd:PRK05857 275 VSELKSANATVPSLRLVGYGGSRAIAADVRFIEA-TGVRTAQVYGLSETGCTALCLPTddgsiVKIEAGAVGRPYPGVDV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 393 QIID-DKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAaNIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSG 470
Cdd:PRK05857 354 YLAAtDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTA-EVLIDGWVnTGDLLERREDGFFYIKGRSSEMIICGG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 471 YRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNL 550
Cdd:PRK05857 433 VNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDI 512
|
490
....*....|...
gi 1034593582 551 PKTVTGKIQRAKL 563
Cdd:PRK05857 513 PRTQSGKVMRASL 525
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
81-564 |
1.99e-17 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 85.17 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 160
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 161 dEVIQEVDTVASECPslrikllvseKSCDGwLNFKKLLneastthhcvetgsqeaSAIYfTSGTSGLPKMA--EHS--YS 236
Cdd:cd05939 82 -NLLDPLLTQSSTEP----------PSQDD-VNFRDKL-----------------FYIY-TSGTTGLPKAAviVHSryYR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 237 SLGLKAKMdagwTGLQASDIMWT----ISDTGWILNILCSLmepwaLGACTFVhLLPKFDPLVILKTLSSY--PIKSMMG 310
Cdd:cd05939 132 IAAGAYYA----FGMRPEDVVYDclplYHSAGGIMGVGQAL-----LHGSTVV-IRKKFSASNFWDDCVKYncTIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 311 ApiVYRMLLQQDLSSYKFPHlqnCV--TVGESLLPETLENWRAQTGL-DIRESYGQTEtGLTCMVSKTMKIKP-GYMG-T 385
Cdd:cd05939 202 E--ICRYLLAQPPSEEEQKH---NVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATE-GNSSLVNIDNHVGAcGFNSrI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 386 AASCYDVQII-----------DDKGNVLP--PGTEGDIGIRVKPIRPIGIFSGYVDNPD---KTAANI--RGD-FWLLGD 446
Cdd:cd05939 276 LPSVYPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGAtnkKIARDVfkKGDsAFLSGD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 447 RGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLASQFLshDPEQLTK 525
Cdd:cd05939 356 VLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAGMAAIVDPERKV--DLDRFSA 433
|
490 500 510
....*....|....*....|....*....|....*....
gi 1034593582 526 ELQqhvkSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd05939 434 VLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
81-568 |
1.99e-17 |
|
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: 85.18 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmPGTIQ--MKSTDILYRLQMSKAKAIV 158
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--PAFINynLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 159 AGDEViqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqEASAIYfTSGTSGLPKMAEHSYSSL 238
Cdd:cd05937 84 VDPDD--------------------------------------------------PAILIY-TSGTTGLPKAAAISWRRT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 239 GLKAKMDAGWTGLQASDIMWT----ISDTGWILNILCSLMEpwalGACtfVHLLPKFDplviLKTLSSYPIKSmmGAP-I 313
Cdd:cd05937 113 LVTSNLLSHDLNLKNGDRTYTcmplYHGTAAFLGACNCLMS----GGT--LALSRKFS----ASQFWKDVRDS--GATiI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 314 VY-----RMLLQQDLSSYKFPHLQNCVTvGESLLPETLENWRAQTGL-DIRESYGQTETgltcmVSKTMKIKPGYMGTAA 387
Cdd:cd05937 181 QYvgelcRYLLSTPPSPYDRDHKVRVAW-GNGLRPDIWERFRERFNVpEIGEFYAATEG-----VFALTNHNVGDFGAGA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 388 SCYD--------------VQIIDDKGNVL-----------PPGTEGDIGIRVkPIRPIGIFSGYVDNPDKTAANI----- 437
Cdd:cd05937 255 IGHHglirrwkfenqvvlVKMDPETDDPIrdpktgfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKLvrdvf 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 438 -RGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLASQ 514
Cdd:cd05937 334 rKGDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEES 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1034593582 515 flSHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 568
Cdd:cd05937 414 --SAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
57-566 |
5.42e-17 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 84.75 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 57 MEKAGKRLPSPALWWVNGKGKELMWNF---RELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIF 133
Cdd:PLN03052 182 TPKPSKTDDSIAIIWRDEGSDDLPVNRmtlSELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 134 MPGTIQMKSTDILYRLQMSKAKA------IVAGDEVIQEVDTVASECPSLRIKLLVSEKSC-----DGWLNFKKLLNEAS 202
Cdd:PLN03052 261 VSIADSFAPSEIATRLKISKAKAiftqdvIVRGGKSIPLYSRVVEAKAPKAIVLPADGKSVrvklrEGDMSWDDFLARAN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 203 TTHHCVETGSQEASA-----IYFTSGTSGLPKMAEHSYSSlGLKAKMDAgWTGL--QASDIMWTISDTGWilnilcsLME 275
Cdd:PLN03052 341 GLRRPDEYKAVEQPVeaftnILFSSGTTGEPKAIPWTQLT-PLRAAADA-WAHLdiRKGDIVCWPTNLGW-------MMG 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 276 PWALGACtfvhllpkfdpLVILKTLSSY---PIKS------------MMGA--PIVYRMLLQQDLSSYKFPHLQNCVTVG 338
Cdd:PLN03052 412 PWLVYAS-----------LLNGATLALYngsPLGRgfakfvqdakvtMLGTvpSIVKTWKNTNCMAGLDWSSIRCFGSTG 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 339 E-SLLPETLenW---RAQTGlDIRESYGQTETGlTCMVSKTMkIKP---GYMGTAASCYDVQIIDDKGNVLP---PGTeG 408
Cdd:PLN03052 481 EaSSVDDYL--WlmsRAGYK-PIIEYCGGTELG-GGFVTGSL-LQPqafAAFSTPAMGCKLFILDDSGNPYPddaPCT-G 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 409 DIGIRVKpirpigIF--SGYVDNPDKTAANIRG-DFW---LL---GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVE 479
Cdd:PLN03052 555 ELALFPL------MFgaSSTLLNADHYKVYFKGmPVFngkILrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 480 ---NALmeHPAVVETAVISSPDPVRG--EVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTV 554
Cdd:PLN03052 629 rvcNAA--DESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTA 706
|
570
....*....|..
gi 1034593582 555 TGKIQRAKLRDK 566
Cdd:PLN03052 707 SNKVMRRVLRQQ 718
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
343-565 |
9.03e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 83.12 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 343 PETLENWRaQTGLDIRESYGQTETGltcmvSKTMKIKPG-YMGTAASCydvqiiddkGNVLPPGTegdIGIRVKPIRPIG 421
Cdd:PRK07445 244 PSLLEQAR-QLQLRLAPTYGMTETA-----SQIATLKPDdFLAGNNSS---------GQVLPHAQ---ITIPANQTGNIT 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 422 I-----FSGYVdnPDKTAANIrgdFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISS 496
Cdd:PRK07445 306 IqaqslALGYY--PQILDSQG---IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGL 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034593582 497 PDPVRGEVVKAFVVLAsqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK07445 381 PDPHWGEVVTAIYVPK------DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
312-563 |
1.43e-16 |
|
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: 82.48 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 312 PIVYRMLLQQDLSSYKFP---HLQNCVTVGESLLPETLENWRAQTGLDIR--ESYGQTETGLTCMVS-----KTMKIKPG 381
Cdd:cd17644 204 PPAYWHLLVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKNVGNFIQliNVYGPTEATIAATVCrltqlTERNITSV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 382 YMGTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTAANIRGD---------FWLLGDRGIKDE 452
Cdd:cd17644 284 PIGRPIANTQVYILDENLQPVPVGVPGEL-----HIGGVGLARGYLNRPELTAEKFISHpfnsseserLYKTGDLARYLP 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 453 DGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflSHDPEQ-LTKELQQHV 531
Cdd:cd17644 359 DGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV------PHYEESpSTVELRQFL 432
|
250 260 270
....*....|....*....|....*....|..
gi 1034593582 532 KSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17644 433 KAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
82-532 |
1.59e-16 |
|
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: 82.41 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagd 161
Cdd:cd17640 7 TYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 162 eviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcVETGSQEASAIYFTSGTSGLPK--MAEHSysslG 239
Cdd:cd17640 83 ----------------------------------------------VENDSDDLATIIYTSGTTGNPKgvMLTHA----N 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 240 LKAKMDAGWTGLQAS--DIMWTISDTGWILNILCSLMEPWALGACTF---VHL---LPKFDPLVIL------KTLSSYPI 305
Cdd:cd17640 113 LLHQIRSLSDIVPPQpgDRFLSILPIWHSYERSAEYFIFACGCSQAYtsiRTLkddLKRVKPHYIVsvprlwESLYSGIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 306 KSMMGAPIVYRMLLQQDLS--SYKFPhlqncVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKTMKIKPGYM 383
Cdd:cd17640 193 KQVSKSSPIKQFLFLFFLSggIFKFG-----ISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 384 GTAASCYDVQIIDDKGN-VLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR 461
Cdd:cd17640 267 GRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVLDSDGWFnTGDLGWLTCGGELVLTGR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 462 AND-IINSSGYRIGPSEVENALMEHPaVVETAVISSPD---------PVRGEVVKAFVVLAsQFLSHDPEQL------TK 525
Cdd:cd17640 342 AKDtIVLSNGENVEPQPIEEALMRSP-FIEQIMVVGQDqkrlgalivPNFEELEKWAKESG-VKLANDRSQLlaskkvLK 419
|
....*..
gi 1034593582 526 ELQQHVK 532
Cdd:cd17640 420 LYKNEIK 426
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
77-563 |
4.99e-16 |
|
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: 80.59 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 77 KELMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKA 156
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 157 IVagdevIQEVDTvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeASAIYfTSGTSGLPK--MAEHS 234
Cdd:cd17650 88 LL-----TQPEDL---------------------------------------------AYVIY-TSGTTGKPKgvMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 235 YSslglkAKMDAGW-----------TGLQASDIMWTISdTGWILNILCslmepwALGACTFVHLLPKFDPLVILKTLSSY 303
Cdd:cd17650 117 NV-----AHAAHAWrreyeldsfpvRLLQMASFSFDVF-AGDFARSLL------NGGTLVICPDEVKLDPAALYDLILKS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 304 PIKSMMGAPIVYRMLL------QQDLSSYKFphlqncVTVGESLLPETLENW---RAQTGLDIRESYGQTETgltCMVSK 374
Cdd:cd17650 185 RITLMESTPALIRPVMayvyrnGLDLSAMRL------LIVGSDGCKAQDFKTlaaRFGQGMRIINSYGVTEA---TIDST 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 375 TMKIKPGYMGTAASC--------YDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD------ 440
Cdd:cd17650 256 YYEEGRDPLGDSANVpigrplpnTAMYVLDERLQPQPVGVAGELYIGGA-----GVARGYLNRPELTAERFVENpfapge 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 441 -FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPvRGEVVKAFVVLASQFLShd 519
Cdd:cd17650 331 rMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARLCAYVVAAATLN-- 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1034593582 520 peqlTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17650 408 ----TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
82-530 |
1.26e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 79.94 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFM---PGtiqMKSTDILYRLQMSKAKAIV 158
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 159 AgdeviQEVDTVAS-----ECPSLRIKLLVSEKSCDGWLNFKKLlnEASTTHH---CVETGSQEASAIYFTSGTSGLPKM 230
Cdd:PRK09274 119 G-----IPKAHLARrlfgwGKPSVRRLVTVGGRLLWGGTTLATL--LRDGAAApfpMADLAPDDMAAILFTSGSTGTPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 231 AEHSYSSLglkakmDAGWTGLQASdimWTISDTGWILNI--LCSLMEPwALGACTfvhLLPKFD--------PLVILKTL 300
Cdd:PRK09274 192 VVYTHGMF------EAQIEALRED---YGIEPGEIDLPTfpLFALFGP-ALGMTS---VIPDMDptrpatvdPAKLFAAI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 301 SSYPIKSMMGAPIVYRMLLQQDLSS-YKFPHLQNCVTVGESLLPETLENWRA--QTGLDIRESYGQTETGLTCMVS---- 373
Cdd:PRK09274 259 ERYGVTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEALPISSIEsrei 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 374 --KTMKIK---PGY-MGTAASCYDVQIID---------DKGNVLPPGTEGDIgirvkpirpigIFSG------YVDNPDK 432
Cdd:PRK09274 339 lfATRAATdngAGIcVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEI-----------VVAGpmvtrsYYNRPEA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 433 TAAN----IRGDFW-LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPvrGEVVKA 507
Cdd:PRK09274 408 TRLAkipdGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPV 485
|
490 500
....*....|....*....|...
gi 1034593582 508 FVVLASQFLSHDPEQLTKELQQH 530
Cdd:PRK09274 486 LCVELEPGVACSKSALYQELRAL 508
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
81-564 |
8.34e-15 |
|
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: 77.01 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmPGTI--QMKSTDILYRLQMSKAKAIV 158
Cdd:cd05940 4 LTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--AALInyNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 159 agdeviqeVDTvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIY-FTSGTSGLPKMAEHSYSS 237
Cdd:cd05940 81 --------VDA-----------------------------------------------ALYiYTSGTTGLPKAAIISHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 238 LGLKAKMDAGWTGLQASDIMWTI----SDTGWILNILCSLMEpwalGACtfvhllpkfdpLVILKTLSSY----PIKSMM 309
Cdd:cd05940 106 AWRGGAFFAGSGGALPSDVLYTClplyHSTALIVGWSACLAS----GAT-----------LVIRKKFSASnfwdDIRKYQ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 310 GAPIVY-----RMLLQQDLSSYKFPHLQNCVtVGESLLPETLENWRAQTGL-DIRESYGQTE--------TGLTCMVSKT 375
Cdd:cd05940 171 ATIFQYigelcRYLLNQPPKPTERKHKVRMI-FGNGLRPDIWEEFKERFGVpRIAEFYAATEgnsgfinfFGKPGAIGRN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 376 MKIKPGYMGTAASCYDVQ----IIDDKGNVLPPGtEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIR-----GDFWLL-G 445
Cdd:cd05940 250 PSLLRKVAPLALVKYDLEsgepIRDAEGRCIKVP-RGEPGLLISRINPLEPFDGYTDPAATEKKILRdvfkkGDAWFNtG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 446 DRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLASQflshDPEQLT 524
Cdd:cd05940 329 DLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPN----EEFDLS 404
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1034593582 525 KeLQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:cd05940 405 A-LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
218-572 |
4.09e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.97 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 218 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASD---IMWTISDTGWILNILCSLMEpwalGACTFVHLLPKFDPL 294
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDrvlLFMSFSFDGAQERFLWTLIC----GGCLVVRDNDLWDPE 3317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 295 VILKTLSSYPIkSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRA---QTGLdiRESYGQTETGLTCM 371
Cdd:PRK12467 3318 ELWQAIHAHRI-SIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRklkPRGL--TNGYGPTEAVVTVT 3394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 372 VSKTmkIKPGYMGTAA----------SCYdvqIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD- 440
Cdd:PRK12467 3395 LWKC--GGDAVCEAPYapigrpvagrSIY---VLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAERFVADp 3464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 441 FWLLGDRGIKD-------EDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSpDPVRGEVVKAFVVLas 513
Cdd:PRK12467 3465 FSGSGGRLYRTgdlaryrADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP-- 3541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 514 qflsHDPEQ-LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSG 572
Cdd:PRK12467 3542 ----ADPQGdWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSR 3597
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
84-562 |
4.62e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 75.03 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 84 RELSENSQQAANVLSGAcGLQRGDRVAV-------VLPRVPEWWLvilgciRAGLIFM-----PGT-IQMKSTDILYRLQ 150
Cdd:PRK07768 33 GEVHERARRIAGGLAAA-GVGPGDAVAVlagapveIAPTAQGLWM------RGASLTMlhqptPRTdLAVWAEDTLRVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 151 MSKAKAIVAGDEVIQEVDTVASEcpSLRIkLLVSEkscdgwlnfkkLLNEASTTHhcVETGsQEASAIY-FTSGTSGLPK 229
Cdd:PRK07768 106 MIGAKAVVVGEPFLAAAPVLEEK--GIRV-LTVAD-----------LLAADPIDP--VETG-EDDLALMqLTSGSTGSPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 230 MAEHSYSSLglKAKMDAGWTGLQA---SDIM--W--TISDTGWIlNILCSlmePWALGaCTFVHLLP-KF--DPLVILKT 299
Cdd:PRK07768 169 AVQITHGNL--YANAEAMFVAAEFdveTDVMvsWlpLFHDMGMV-GFLTV---PMYFG-AELVKVTPmDFlrDPLLWAEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 300 LSSYPiKSMMGAP-----IVYRMLLQQ------DLSSYKFphlqnCVTVGESLLPETLENWRAQT---GLD---IRESYG 362
Cdd:PRK07768 242 ISKYR-GTMTAAPnfayaLLARRLRRQakpgafDLSSLRF-----ALNGAEPIDPADVEDLLDAGarfGLRpeaILPAYG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 363 QTETGLTC-----------------MVSKTMKIKPGYMGTAASC---------YDVQIIDDKGNVLPPGTEGDIGIRVKP 416
Cdd:PRK07768 316 MAEATLAVsfspcgaglvvdevdadLLAALRRAVPATKGNTRRLatlgpplpgLEVRVVDEDGQVLPPRGVGVIELRGES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 417 IRPigifsGYVDnPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVIS 495
Cdd:PRK07768 396 VTP-----GYLT-MDGFIPAQDADGWLdTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034593582 496 SPDPvRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKY-PRKIeFVL---NLPKTVTGKIQRAK 562
Cdd:PRK07768 470 VRLD-AGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVrPRNV-VVLgpgSIPKTPSGKLRRAN 538
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-563 |
9.20e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 74.70 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 82 NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM----SKA 154
Cdd:PRK10252 485 SYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP-------LDTGYpddRLKMmledARP 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 155 KAIVAGDEVIQE-VDTVASECPSLRIKLLVSEKSCDGwlnfkkllneASTTHHcvetgsqeASAIYFTSGTSGLPK--MA 231
Cdd:PRK10252 557 SLLITTADQLPRfADVPDLTSLCYNAPLAPQGAAPLQ----------LSQPHH--------TAYIIFTSGSTGRPKgvMV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 232 EHsysslglkakmdagwtglQAsdimwtisdtgwILNILCSLMEPWALGA---------CTF-VHLLPKF---------- 291
Cdd:PRK10252 619 GQ------------------TA------------IVNRLLWMQNHYPLTAddvvlqktpCSFdVSVWEFFwpfiagaklv 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 292 --------DPLVILKTLSSYPIKSMMGAPivyRML------LQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDI 357
Cdd:PRK10252 669 maepeahrDPLAMQQFFAEYGVTTTHFVP---SMLaafvasLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPL 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 358 RESYGQTETG------------LTCMVSKTMKIKPGYMGTAascydVQIIDDKGNVLPPGTEGDI---GIRVKpirpigi 422
Cdd:PRK10252 746 HNLYGPTEAAvdvswypafgeeLAAVRGSSVPIGYPVWNTG-----LRILDARMRPVPPGVAGDLyltGIQLA------- 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 423 fSGYVDNPDKTAANIRGD-------FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHP----AVVET 491
Cdd:PRK10252 814 -QGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHA 892
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034593582 492 AVISSPDPVRGEVVK--AFVVlASQFLSHDpeqlTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:PRK10252 893 CVINQAAATGGDARQlvGYLV-SQSGLPLD----TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
446-564 |
9.70e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 72.77 E-value: 9.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 446 DRGIKDeDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflsHDPEQLTK 525
Cdd:PRK07824 240 DLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGD-----GGPAPTLE 313
|
90 100 110
....*....|....*....|....*....|....*....
gi 1034593582 526 ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
334-563 |
2.98e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.28 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 334 CVTVGESLLPETLENWRA--QTGLdIRESYGQTET---GLTCMVSKTMKIKPGY--MGTAASCYDVQIIDDKGNVLPPGT 406
Cdd:PRK05691 2453 CITGGEALTGEHLQRIRQafAPQL-FFNAYGPTETvvmPLACLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGA 2531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 407 EGDIGIRVKpirpiGIFSGYVDNPDKTA--------ANIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEV 478
Cdd:PRK05691 2532 TGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEI 2606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 479 ENALMEHPAVVETAVISSPDPVRGEVVKafvVLASQFLSHDPEQ---LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVT 555
Cdd:PRK05691 2607 ESRLLEHPAVREAVVLALDTPSGKQLAG---YLVSAVAGQDDEAqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTAN 2683
|
....*...
gi 1034593582 556 GKIQRAKL 563
Cdd:PRK05691 2684 GKLDRRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
68-569 |
1.26e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.35 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 68 ALWWVNGKgkelmWNFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILY 147
Cdd:PRK05691 1149 ALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAY 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 148 RLQMSKAKAIVAGDEVIQEVDTVASECPslrikLLVSEKSCDGWLNFKKLLNeastTHhcvetGSQEASAIYfTSGTSGL 227
Cdd:PRK05691 1223 MLADSGVELLLTQSHLLERLPQAEGVSA-----IALDSLHLDSWPSQAPGLH----LH-----GDNLAYVIY-TSGSTGQ 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 228 PKMAEHSYSSLGLKAK-MDAGWtGLQASDIMWTISDTGWILNIL-CSlmepWAL-GACTFVHLLP--KFDPLVILKTLSS 302
Cdd:PRK05691 1288 PKGVGNTHAALAERLQwMQATY-ALDDSDVLMQKAPISFDVSVWeCF----WPLiTGCRLVLAGPgeHRDPQRIAELVQQ 1362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 303 YPIKSMMGAPIVYRMLLQQdlssykfPHLQNCVTV------GESLLPETLENWRAQ-TGLDIRESYGQTETGLT-----C 370
Cdd:PRK05691 1363 YGVTTLHFVPPLLQLFIDE-------PLAAACTSLrrlfsgGEALPAELRNRVLQRlPQVQLHNRYGPTETAINvthwqC 1435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 371 MVSKTMKIKPGYMGTAASCydvQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD--------FW 442
Cdd:PRK05691 1436 QAEDGERSPIGRPLGNVLC---RVLDAELNLLPPGVAGELCIG-----GAGLARGYLGRPALTAERFVPDplgedgarLY 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 443 LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQ 522
Cdd:PRK05691 1508 RTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQ------EA 1581
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1034593582 523 LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 569
Cdd:PRK05691 1582 EAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ 1628
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
81-563 |
3.32e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.81 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMP---GTIQMKSTDILyrlQMSKAKAI 157
Cdd:PRK05691 3746 WSYAELNRAANRLGHALRAA-GVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPldpGLPAQRLQRII---ELSRTPVL 3821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 VAGDEVIQEVDTVASECP-SLRIKLLVSEKscdgwlnfkkLLNEASTTHH-CVETGSQEASAIYFTSGTSGLPK------ 229
Cdd:PRK05691 3822 VCSAACREQARALLDELGcANRPRLLVWEE----------VQAGEVASHNpGIYSGPDNLAYVIYTSGSTGLPKgvmveq 3891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 230 --MAEHSYSS---LGLKAKMDAGWTGLQASDI-MWTIsdtgwilnilcslmepwaLGACTF---VHLLPK---FDPLVIL 297
Cdd:PRK05691 3892 rgMLNNQLSKvpyLALSEADVIAQTASQSFDIsVWQF------------------LAAPLFgarVEIVPNaiaHDPQGLL 3953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 298 KTLSSYPIKSMMGAP-IVYRMLLQQDLSsykFPHLQNCVTVGESLLPETLENW---RAQTGLdiRESYGQTEtgltC--- 370
Cdd:PRK05691 3954 AHVQAQGITVLESVPsLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWlqrYPQIGL--VNAYGPAE----Csdd 4024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 371 -------MVSKTMKIKPgyMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTA----ANIRG 439
Cdd:PRK05691 4025 vaffrvdLASTRGSYLP--IGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTAlafvPHPFG 4097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 440 D----FWLLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSpDPVRGEVVKAFVVLASQF 515
Cdd:PRK05691 4098 ApgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ-EGVNGKHLVGYLVPHQTV 4176
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1034593582 516 lsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:PRK05691 4177 --LAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
42-559 |
1.40e-11 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 67.30 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 42 AKFNFASDVLDHwadmekagKRLPSPALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWL 121
Cdd:cd05943 68 ARLNYAENLLRH--------ADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALR-ALGVKPGDRVAGYLPNIPEAVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 122 VILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVI---------QEVDTVASECPSLRIKLLVSEKSCDGWL 192
Cdd:cd05943 139 AMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTyngkrhdvrEKVAELVKGLPSLLAVVVVPYTVAAGQP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 193 NFKKLLNeastTHHCVETGSQEASA--------------IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGW-TGLQASDIM 257
Cdd:cd05943 219 DLSKIAK----ALTLEDFLATGAAGelefeplpfdhplyILYSSGTTGLPKCIVHGAGGTLLQHLKEHILhCDLRPGDRL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 258 WTISDTGWIL-NILCSLMepwALGAcTFV-----HLLPkfDPLVILKTLSSYPIkSMMGAPIVYRMLLQQ---------D 322
Cdd:cd05943 295 FYYTTCGWMMwNWLVSGL---AVGA-TIVlydgsPFYP--DTNALWDLADEEGI-TVFGTSAKYLDALEKaglkpaethD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 323 LSSykfphLQNCVTVGESLLPETLE----NWRAqtGLDIRESYGQTETgLTCMVSkTMKIKPGYMGtAASC----YDVQI 394
Cdd:cd05943 368 LSS-----LRTILSTGSPLKPESFDyvydHIKP--DVLLASISGGTDI-ISCFVG-GNPLLPVYRG-EIQCrglgMAVEA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 395 IDDKGNVLPpGTEGDIGIrVKPI--RPIGiFSGYVDNPDKTAA--NIRGDFWLLGDRGIKDEDGYFQFMGRANDIINSSG 470
Cdd:cd05943 438 FDEEGKPVW-GEKGELVC-TKPFpsMPVG-FWNDPDGSRYRAAyfAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGG 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 471 YRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKELQQHVKSVTA----PYKYPRKIEF 546
Cdd:cd05943 515 VRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDELRKRIRSTIRsalsPRHVPAKIIA 588
|
570
....*....|...
gi 1034593582 547 VLNLPKTVTGKIQ 559
Cdd:cd05943 589 VPDIPRTLSGKKV 601
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
383-564 |
1.58e-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: 66.74 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 383 MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAANIRGDFWLL-GDRG-IKDEDGYFqfMG 460
Cdd:cd05908 316 VGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP-----GYYNNPEATAKVFTDDGWLKtGDLGfIRNGRLVI--TG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 461 RANDIINSSGYRIGPSEVENalmehpavvetaVISSPDPVR-GEVVKAFVvlasqflsHDPEQLTKEL---QQHVKSVTA 536
Cdd:cd05908 389 REKDIIFVNGQNVYPHDIER------------IAEELEGVElGRVVACGV--------NNSNTRNEEIfcfIEHRKSEDD 448
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034593582 537 PYKYPRKIEFVLN---------------LPKTVTGKIQRAKLR 564
Cdd:cd05908 449 FYPLGKKIKKHLNkrggwqinevlpirrIPKTTSGKVKRYELA 491
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
73-488 |
2.97e-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: 66.23 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 73 NGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfMPGTIQMKSTD-ILYRLQM 151
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFL-KLGLERFHGVGILGFNSPEWFIAAVGAIFAGGI-AVGIYTTNSPEaCQYVAET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 152 SKAKAIVAGDEV-IQEVDTVASECPSLR----IKLLVSEKSCD--GWLNFKKLLNEASTTHHCVETGSQEAS---AIYFT 221
Cdd:cd05933 79 SEANILVVENQKqLQKILQIQDKLPHLKaiiqYKEPLKEKEPNlySWDEFMELGRSIPDEQLDAIISSQKPNqccTLIYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 222 SGTSGLPK--MAEH---------------------------SYSSLG-LKAKMDAGWTGL---------QASDIMWTISD 262
Cdd:cd05933 159 SGTTGMPKgvMLSHdnitwtakaasqhmdlrpatvgqesvvSYLPLShIAAQILDIWLPIkvggqvyfaQPDALKGTLVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 263 T------------GWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSsypiKSMMG---APIVYRMLLQQDLSSYK 327
Cdd:cd05933 239 TlrevrptafmgvPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNL----KLMGGespSPLFYRLAKKLVFKKVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 328 ----FPHLQNCVTVGESLLPETLENWraqTGLDIR--ESYGQTET-GLtcmvsKTMKIKPGYmgTAASCydvqiiddkGN 400
Cdd:cd05933 315 kalgLDRCQKFFTGAAPISRETLEFF---LSLNIPimELYGMSETsGP-----HTISNPQAY--RLLSC---------GK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 401 VLPpgtegdiGIRVKPIRP----IG--------IFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRAND-II 466
Cdd:cd05933 376 ALP-------GCKTKIHNPdadgIGeicfwgrhVFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElII 448
|
490 500
....*....|....*....|...
gi 1034593582 467 NSSGYRIGPSEVENAL-MEHPAV 488
Cdd:cd05933 449 TAGGENVPPVPIEDAVkKELPII 471
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
85-563 |
1.41e-10 |
|
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: 63.65 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 85 ELSENSQQAANVLSGACglQRGDR-VAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV 163
Cdd:cd17654 21 DLAEKISNLSNFLRKKF--QTEERaIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 164 IQEvdtvasecPSLRIKLLVsekscdgwlNFKKLLNEAStthhcvetgsqeaSAIYFTSGTSGLPK---MAEHSYSS--L 238
Cdd:cd17654 99 DNA--------PLSFTPEHR---------HFNIRTDECL-------------AYVIHTSGTTGTPKivaVPHKCILPniQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 239 GLKAKMDagwtgLQASDIMWTISDTGW---ILNILCSLmepwALGAC-----TFVHLLP-KFDPlvILKTLSSypIKSMM 309
Cdd:cd17654 149 HFRSLFN-----ITSEDILFLTSPLTFdpsVVEIFLSL----SSGATllivpTSVKVLPsKLAD--ILFKRHR--ITVLQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 310 GAPIVYRMLLQQDLSSYKFPHLQN--CVTVGESLLPETLEN--WRAQ-TGLDIRESYGQTETgltCMVSKTMKIK----P 380
Cdd:cd17654 216 ATPTLFRRFGSQSIKSTVLSATSSlrVLALGGEPFPSLVILssWRGKgNRTRIFNIYGITEV---SCWALAYKVPeedsP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 381 GYMGTAASCYDVQIIDDKGNvlppgtEGDIGIRVKPIRPIGIFSGYVDNPdktaaniRGDFWLLGDRgIKDEDGYFQFMG 460
Cdd:cd17654 293 VQLGSPLLGTVIEVRDQNGS------EGTGQVFLGGLNRVCILDDEVTVP-------KGTMRATGDF-VTVKDGELFFLG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 461 RANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDpvrgEVVKAFVVLASqflSHDPEQltKELQQHVKSvtaPYKY 540
Cdd:cd17654 359 RKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGES---SSSRIH--KELQLTLLS---SHAI 426
|
490 500
....*....|....*....|...
gi 1034593582 541 PRKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17654 427 PDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
83-564 |
2.89e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.10 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMK-------STDILYRLQMSKAK 155
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 156 AIVAGDEVIQEVDTVASecpSLRIKLLVSekscdgWLNFKkLLNEASTThhcVETGSQEASA-IYFTSGTSGLPK----- 229
Cdd:PRK09192 131 AIITPDELLPWVNEATH---GNPLLHVLS------HAWFK-ALPEADVA---LPRPTPDDIAyLQYSSGSTRFPRgviit 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 230 ----MAE-HSYSSLGLKakmdagwtgLQASD--IMW-----TISDTGWILNILCSLMEpwalgactfVHLLPKFD----P 293
Cdd:PRK09192 198 hralMANlRAISHDGLK---------VRPGDrcVSWlpfyhDMGLVGFLLTPVATQLS---------VDYLPTRDfarrP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 294 LVILK-------TLSSYPiksMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWR---AQTGLDIRE---S 360
Cdd:PRK09192 260 LQWLDlisrnrgTISYSP---PFGYELCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAeafAPAGFDDKAfmpS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 361 YGQTETGL------------------TCMVSKTMKIKPGYMGTAAS----C------YDVQIIDDKGNVLPPGTEGDIGI 412
Cdd:PRK09192 337 YGLAEATLavsfsplgsgivveevdrDRLEYQGKAVAPGAETRRVRtfvnCgkalpgHEIEIRNEAGMPLPERVVGHICV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 413 RvKPirpiGIFSGYVDNPDkTAANIRGDFWL-LGDRGIKdEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVV-- 489
Cdd:PRK09192 417 R-GP----SLMSGYFRDEE-SQDVLAADGWLdTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsg 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 490 ETAVISSPDPvRGEVVkafVVLASQFLShDPE---QLTKELQQHVKSVTApykYPRKIEFV--LNLPKTVTGKIQRAKLR 564
Cdd:PRK09192 490 DAAAFSIAQE-NGEKI---VLLVQCRIS-DEErrgQLIHALAALVRSEFG---VEAAVELVppHSLPRTSSGKLSRAKAK 561
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
113-575 |
5.10e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 62.14 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 113 LPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQE------VDTVASECPSLRIKLLVSEK 186
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralplYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 187 SCD--------GWLNFkklLNEASTTHhcvETGSQEASAIY----------FTSGTSGLPKMAEHSYSSlGLKAKMDaGW 248
Cdd:PLN03051 81 PVAvplreqdlSWCDF---LGVAAAQG---SVGGNEYSPVYapvesvtnilFSSGTTGEPKAIPWTHLS-PLRCASD-GW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 249 TGL--QASDIMWTISDTGWILN-ILcsLMEPWALGACTFVH----LLPKFDPLV------ILKTlssypIKSMMGApivY 315
Cdd:PLN03051 153 AHMdiQPGDVVCWPTNLGWMMGpWL--LYSAFLNGATLALYggapLGRGFGKFVqdagvtVLGL-----VPSIVKA---W 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 316 RMLLQQDLSSYKFPHLQNCVTVGESLLPET---LENWRAQTGlDIRESYGQTETGLTCMVSKTMKIK-PGYMGTAASCYD 391
Cdd:PLN03051 223 RHTGAFAMEGLDWSKLRVFASTGEASAVDDvlwLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQaPGAFSTASLGTR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 392 VQIIDDKGNVLPPGTE--GDIGIRVkpirPIGIFSGYVDNPDKTAANIRG---------DFWLLGDRGIKDEDGYFQFMG 460
Cdd:PLN03051 302 FVLLNDNGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmpmygskgmPLRRHGDIMKRTPGGYFCVQG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 461 RANDIINSSGYRIGPSEVENALME-HPAVVETAVISSPDPVRGE----VVKAFVVLASQFLSHDPEQLTKELQQHVKSVT 535
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNL 457
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1034593582 536 APYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK-MSGKAR 575
Cdd:PLN03051 458 NPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKKeLSGRSK 498
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
83-501 |
1.59e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 60.17 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 83 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmpgtiqmkstDILyrlqmskakaivagde 162
Cdd:cd05910 5 FRELDERSDRIAQGLT-AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV-----------PVL---------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 163 viqeVDtvasecPSLRIKllvsekscdgwlNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLglKA 242
Cdd:cd05910 57 ----ID------PGMGRK------------NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTF--AA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 243 KMDAGWT--GLQASDI-MWTISdtgwilniLCSLMEPwALGACTFV----HLLP-KFDPLVILKTLSSYPIKSMMGAPIV 314
Cdd:cd05910 113 QIDALRQlyGIRPGEVdLATFP--------LFALFGP-ALGLTSVIpdmdPTRPaRADPQKLVGAIRQYGVSIVFGSPAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 315 YRML----LQQDLssyKFPHLQNCVTVGESLLPETLENWRA--QTGLDIRESYGQTETGLTCMV-------SKTMKIKPG 381
Cdd:cd05910 184 LERVarycAQHGI---TLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVSSIgsrellaTTTAATSGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 382 Y---MGTAASCYDVQIID---------DKGNVLPPGTEGDI---GIRVKPirpigifsGYVDNPDKTAA----NIRGDFW 442
Cdd:cd05910 261 AgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEItvtGPTVTP--------TYVNRPVATALakidDNSEGFW 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 443 -LLGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 501
Cdd:cd05910 333 hRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGC 392
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
42-559 |
1.93e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 60.58 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 42 AKFNFASDVLDHwadmekagKRLPSPALWWVNGKGKELMWNFRELSEnsqQAANVLSG--ACGLQRGDRVAVVLPRVPEW 119
Cdd:PRK03584 84 ARLNYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRR---QVAALAAAlrALGVGPGDRVAAYLPNIPET 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 120 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD---------EVIQEVDTVASECPSLRIKLLVS------ 184
Cdd:PRK03584 153 VVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLEHVVVVPylgpaa 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 185 -EKSCDGWLNFKKLLNEAstthhcvetgsqEASAIYFT-------------SGTSGLPKMAEHSYSSLGLKA-KMDAGWT 249
Cdd:PRK03584 233 aAAALPGALLWEDFLAPA------------EAAELEFEpvpfdhplwilysSGTTGLPKCIVHGHGGILLEHlKELGLHC 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 250 GLQASDIMWTISDTGWIL-NILCSLMepwALGACTFVH----LLPKFDPL---------VILKTLSSYpIKSMMGAPIVY 315
Cdd:PRK03584 301 DLGPGDRFFWYTTCGWMMwNWLVSGL---LVGATLVLYdgspFYPDPNVLwdlaaeegvTVFGTSAKY-LDACEKAGLVP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 316 RmllqqdlSSYKFPHLQNCVTVGESLLPETL----ENWRAQT-------GLDIresygqtetgLTCMV--SKTMKIKPGY 382
Cdd:PRK03584 377 G-------ETHDLSALRTIGSTGSPLPPEGFdwvyEHVKADVwlasisgGTDI----------CSCFVggNPLLPVYRGE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 383 MGTAASCYDVQIIDDKGNVLppgtEGDIGIRV--KPI--RPIGiFSGYVDNPDKTAA------NIrgdfWLLGDRGIKDE 452
Cdd:PRK03584 440 IQCRGLGMAVEAWDEDGRPV----VGEVGELVctKPFpsMPLG-FWNDPDGSRYRDAyfdtfpGV----WRHGDWIEITE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 453 DGYFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKELQQHVK 532
Cdd:PRK03584 511 HGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLA------EGVTLDDALRARIR 584
|
570 580 590
....*....|....*....|....*....|.
gi 1034593582 533 SV----TAPYKYPRKIEFVLNLPKTVTGKIQ 559
Cdd:PRK03584 585 TTirtnLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
212-564 |
2.54e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 60.11 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 212 SQEASAIYFTSGTSGLPKMAEHSYSSLglkakmdagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACtfVHLlpkF 291
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSL------------LANVEQIKTIADFTPNDRFMSALPLFHSFGLT--VGL---F 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 292 DPLVILKTLSSYPiksmmgAPIVYRML--LQQD------------LSSY-KFPH------LQNCVTVGESLLPETLENWR 350
Cdd:PRK08043 427 TPLLTGAEVFLYP------SPLHYRIVpeLVYDrnctvlfgtstfLGNYaRFANpydfarLRYVVAGAEKLQESTKQLWQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 351 AQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIddkgNVlpPGTEGdiGIRVKpIRPIGIFSGY--VD 428
Cdd:PRK08043 501 DKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLL----SV--PGIEQ--GGRLQ-LKGPNIMNGYlrVE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 429 NPDK----TAANIRGDF---WL-LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVEN-ALMEHPAVVETAVISSpDP 499
Cdd:PRK08043 572 KPGVlevpTAENARGEMergWYdTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKS-DA 650
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034593582 500 VRGEvvkAFVVLASqflshDPEqLTKE-LQQHVKSVTAP-YKYPRKIEFVLNLPKTVTGKIQRAKLR 564
Cdd:PRK08043 651 SKGE---ALVLFTT-----DSE-LTREkLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLK 708
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
217-565 |
6.20e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 59.17 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 217 AIYFTSGTSGLPKMAEHSYSSLGLKAKmdagwtglQASDIMWTISDTgwilNILCSLmePW--ALG--ACTFVHLLPKF- 291
Cdd:PRK08633 786 TIIFSSGSEGEPKGVMLSHHNILSNIE--------QISDVFNLRNDD----VILSSL--PFfhSFGltVTLWLPLLEGIk 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 292 -----DPL---VILKTLSSYPIKSMMGAPIVYRMLLQQD-LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYG 362
Cdd:PRK08633 852 vvyhpDPTdalGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYG 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 363 QTETGLTCMVSKTMKIKPGYM---------------GTAascydVQIID-DKGNVLPPGTEGDIgirvkPIRPIGIFSGY 426
Cdd:PRK08633 932 ATETSPVASVNLPDVLAADFKrqtgskegsvgmplpGVA-----VRIVDpETFEELPPGEDGLI-----LIGGPQVMKGY 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 427 VDNPDKTA---ANIRGDFWLL-GDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALME--HPAVVETAVISSPDPV 500
Cdd:PRK08633 1002 LGDPEKTAeviKDIDGIGWYVtGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEK 1081
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034593582 501 RGEVVkafVVLASQflshdPEQLTKELQQHVKSVTAP--YKyPRKIEFVLNLPKTVTGKIQRAKLRD 565
Cdd:PRK08633 1082 KGEKL---VVLHTC-----GAEDVEELKRAIKESGLPnlWK-PSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
117-565 |
4.73e-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: 55.68 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 117 PEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIV--AGDEVIQevdtvasecpslrikllvsekscdgWLNF 194
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFcdAGVKVYS-------------------------LEEF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 195 KKLLNEASTTHhcvETGSQEASA-IYFTSGTSGLPKMAEHSYSSlglkakmdagwtglqasdIMWTISDTGWILNILCSL 273
Cdd:cd05927 98 EKLGKKNKVPP---PPPKPEDLAtICYTSGTTGNPKGVMLTHGN------------------IVSNVAGVFKILEILNKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 274 MEpwalgacTFVHL--LP---KFDPLVILKTLS--------SYPIKSMM------------GAPIVY-RML--LQQDLS- 324
Cdd:cd05927 157 NP-------TDVYIsyLPlahIFERVVEALFLYhgakigfySGDIRLLLddikalkptvfpGVPRVLnRIYdkIFNKVQa 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 325 -------------SYKFPHLQN---------------------------CVTVGESLLPETLENWRAQTGLDIRESYGQT 364
Cdd:cd05927 230 kgplkrklfnfalNYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 365 ETGLTCMVSKTMKIKPGYMGTAASCYDVQIID--DKG-NVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDF 441
Cdd:cd05927 310 ECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpEMNyDAKDPNPRGEVCIRGP-----NVFSGYYKDPEKTAEALDEDG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 442 WLL-GDRGIKDEDGYFQFMGRANDIIN-SSGYRIGPSEVENALMEHPAVVETAV-----------ISSPDPvrgEVVKAF 508
Cdd:cd05927 385 WLHtGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIYARSPFVAQIFVygdslksflvaIVVPDP---DVLKEW 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034593582 509 vvLASQFL-SHDPEQLTK--ELQQHV---------KSVTAPYKYPRKIEFVLNLPK------TVTGKIQRAKLRD 565
Cdd:cd05927 462 --AASKGGgTGSFEELCKnpEVKKAIledlvrlgkENGLKGFEQVKAIHLEPEPFSvengllTPTFKLKRPQLKK 534
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
341-507 |
2.64e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.02 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 341 LLPETLENWRAQTGLDIRESYGQTETglTCMVSKTMK--IKPGYMGTAASCYDVQIID---------DKgnvlpPGTEGD 409
Cdd:PLN02736 388 LSPDVMEFLRICFGGRVLEGYGMTET--SCVISGMDEgdNLSGHVGSPNPACEVKLVDvpemnytseDQ-----PYPRGE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 410 IGIRvKPIrpigIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRANDIIN-SSGYRIGPSEVENALMEHPA 487
Cdd:PLN02736 461 ICVR-GPI----IFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENVYAKCKF 535
|
170 180 190
....*....|....*....|....*....|.
gi 1034593582 488 VVETAV-----------ISSPDPvrgEVVKA 507
Cdd:PLN02736 536 VAQCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
417-564 |
9.57e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.14 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 417 IRPIGIFSGYVDnpdktAANIRGDFWL-LGDRGIKDEDGyFQFMGRANDIINSSGYRIGPSEVENALMEHPAVVETAVIS 495
Cdd:PRK05851 377 IRGASMMSGYLG-----QAPIDPDDWFpTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVA 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034593582 496 SPDPVRGevVKAFVVLASQFLSHDPEQLTKELQQHVKSVTApyKYPRKIEFVL--NLPKTVTGKIQRAKLR 564
Cdd:PRK05851 451 VGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
282-563 |
1.45e-04 |
|
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: 44.43 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 282 CTFVHLLPKFDPLviLKTLSSYPIKSMMGAPIVYRMLLQQDLSSykfphLQ----NCVTVGeslLPETLENWRAQTGLDI 357
Cdd:cd17647 201 ATVTHLTPAMGQL--LTAQATTPFPKLHHAFFVGDILTKRDCLR-----LQtlaeNVRIVN---MYGTTETQRAVSYFEV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 358 ReSYGQTETGLtcmvsKTMK-IKPGYMGTaascYDVQII----DDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDK 432
Cdd:cd17647 271 P-SRSSDPTFL-----KNLKdVMPAGRGM----LNVQLLvvnrNDRTQICGIGEVGEIYVRAG-----GLAEGYRGLPEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 433 TAANIRGD---------------------FWL--------LGDRGIKDEDGYFQFMGRANDIINSSGYRIGPSEVENALM 483
Cdd:cd17647 336 NKEKFVNNwfvepdhwnyldkdnnepwrqFWLgprdrlyrTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHIS 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 484 EHPAVVET------------AVIS--SPDPVRGEVVKAFVVLASQFLSHDP--------EQLTKELQQHVKSVTAPYKYP 541
Cdd:cd17647 416 QHPLVRENitlvrrdkdeepTLVSyiVPRFDKPDDESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIP 495
|
330 340
....*....|....*....|..
gi 1034593582 542 RKIEFVLNLPKTVTGKIQRAKL 563
Cdd:cd17647 496 SLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
48-568 |
1.47e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 44.81 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 48 SDVLDHWADMEKAGKRLP-SPALWW---VNGKGKELMW-NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLV 122
Cdd:PLN02430 39 SDITTAWDIFSKSVEKYPdNKMLGWrriVDGKVGPYMWkTYKEVYEEVLQIGSALR-ASGAEPGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 123 ILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVdtVASECPSL-RIKLLVS-----EKSCD------- 189
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKEL--LEPDCKSAkRLKAIVSftsvtEEESDkasqigv 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 190 ---GWLNFKKLLNEASTthhcvETGSQEAS---AIYFTSGTSGLPKMAEHSYSSL-----GLKAKMDagwtglQASDIMw 258
Cdd:PLN02430 196 ktySWIDFLHMGKENPS-----ETNPPKPLdicTIMYTSGTSGDPKGVVLTHEAVatfvrGVDLFME------QFEDKM- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 259 TISDTGW----ILNILCSLMEPWAL--GACT-FVH------------LLPKF---DPLV-------ILKTLSSY-PIKSM 308
Cdd:PLN02430 264 THDDVYLsflpLAHILDRMIEEYFFrkGASVgYYHgdlnalrddlmeLKPTLlagVPRVferihegIQKALQELnPRRRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 309 MgAPIVYRMLLQQDLSSYK------------FPHLQN--------CVTVGESLLPETLENWRAQTGLDIRESYGQTET-G 367
Cdd:PLN02430 344 I-FNALYKYKLAWMNRGYShkkaspmadflaFRKVKAklggrlrlLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 368 LT--------CMVsktmkikpGYMGTAASCYDVQI-------IDDKGNvlPPgtEGDIGIRVKPIrpigiFSGYVDNPDK 432
Cdd:PLN02430 423 PTtlgfpdemCML--------GTVGAPAVYNELRLeevpemgYDPLGE--PP--RGEICVRGKCL-----FSGYYKNPEL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 433 TAANIRGDFWLLGDRGIKDEDGYFQFMGRANDIIN-SSGYRIGPSEVENALMEHPAVVETAVISspDPVRGEVVkAFVVL 511
Cdd:PLN02430 486 TEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEYLENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVP 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034593582 512 asqflshDPEQLTK--ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTgkiQRAKLRDKEW 568
Cdd:PLN02430 563 -------NEENTNKwaKDNGFTGSFEELCSLPELKEHILSELKSTA---EKNKLRGFEY 611
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
68-564 |
7.50e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 68 ALWWVNGKGKE-LMWNFRELSENSQQAANVLSGACGLqrGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTdil 146
Cdd:PRK05691 27 ALRFLADDPGEgVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESAR--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 147 yRLQMSKAKAIVAgDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSG 226
Cdd:PRK05691 102 -RHHQERLLSIIA-DAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQPDDIAFLQYTSGSTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 227 LPKMAEHSYSSLGLKAKMDAGWTGLQASD----IMWT--ISDTGWILNIL--------CSLMEPwalgactfVHLLPKfd 292
Cdd:PRK05691 180 LPKGVQVSHGNLVANEQLIRHGFGIDLNPddviVSWLplYHDMGLIGGLLqpifsgvpCVLMSP--------AYFLER-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 293 PLVILKTLSSYPIKSMMGAPIVYRMLLQQdlssykfphlqncvtVGESLLPE-TLENWR-AQTGLD-IRE---------- 359
Cdd:PRK05691 250 PLRWLEAISEYGGTISGGPDFAYRLCSER---------------VSESALERlDLSRWRvAYSGSEpIRQdslerfaekf 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 360 ------------SYGQTETglTCMVSKTMK------------------IKPGYMGTAASC------YDVQIID-DKGNVL 402
Cdd:PRK05691 315 aacgfdpdsffaSYGLAEA--TLFVSGGRRgqgipaleldaealarnrAEPGTGSVLMSCgrsqpgHAVLIVDpQSLEVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 403 PPGTEGDIGIRvKPirpiGIFSGYVDNPDKTA---ANIRGDFWL-LGDRGIKdEDGYFQFMGRANDIINSSGYRIGPSEV 478
Cdd:PRK05691 393 GDNRVGEIWAS-GP----SIAHGYWRNPEASAktfVEHDGRTWLrTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 479 ENalmehpaVVETAVisspDPVRGEVVKAFVV---------LASQF-----LSHDPEQLTKELQQHVKSVtapYKYPRKI 544
Cdd:PRK05691 467 EK-------TVEREV----EVVRKGRVAAFAVnhqgeegigIAAEIsrsvqKILPPQALIKSIRQAVAEA---CQEAPSV 532
|
570 580
....*....|....*....|...
gi 1034593582 545 EFVLN---LPKTVTGKIQRAKLR 564
Cdd:PRK05691 533 VLLLNpgaLPKTSSGKLQRSACR 555
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
81-245 |
3.05e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 40.24 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 81 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAG---LIFMPGTIQMKSTDILYRLQmskakai 157
Cdd:PRK09029 29 LTWQQLCARIDQLAAGFA-QQGVVEGSGVALRGKNSPETLLAYLALLQCGarvLPLNPQLPQPLLEELLPSLT------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 158 vagdeviqeVDTVASECPSLRIKLLVSekscdgwlnfkKLLNEASTTHHCVETGSQEASAIyFTSGTSGLPKMAEHSY-- 235
Cdd:PRK09029 101 ---------LDFALVLEGENTFSALTS-----------LHLQLVEGAHAVAWQPQRLATMT-LTSGSTGLPKAAVHTAqa 159
|
170
....*....|...
gi 1034593582 236 ---SSLGLKAKMD 245
Cdd:PRK09029 160 hlaSAEGVLSLMP 172
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
72-149 |
3.64e-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: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593582 72 VNGKGKE---LMWnfRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMP------------- 135
Cdd:cd05905 5 LDSKGKEattLTW--GKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPieppdisqqlgfl 82
|
90
....*....|....*...
gi 1034593582 136 -GTIQM---KSTDILYRL 149
Cdd:cd05905 83 lGTCKVrvaLTVEACLKG 100
|
|
| |
