|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
33-561 |
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: 1048.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 33 VPAKFNFASDVLDHWADMEKAGKRPPSPALWWVNGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEW 112
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 113 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLN 192
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 193 EASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAG-WTGLQASDIMWTISDTGWILNILCSLMEPWA 271
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRyWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 272 LGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIR 351
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 352 ESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIR 431
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 432 GDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSH 511
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3C5E_A 512 DPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 561
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
74-558 |
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: 670.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 153
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPKMAEHSySSLGL 233
Cdd:cd05972 78 -------------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHT-HSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 234 KAKMDA-GWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL 312
Cdd:cd05972 108 GHIPTAaYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 313 QQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKG 392
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 393 NVLPPGTEGDIGIRVKpirPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVE 472
Cdd:cd05972 268 RELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 473 NALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQ 552
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*.
3C5E_A 553 RAKLRD 558
Cdd:cd05972 423 RVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
33-561 |
4.16e-178 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 514.66 E-value: 4.16e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 33 VPAKFNFASDVLDHWADmEKAGKrppsPALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEW 112
Cdd:COG0365 4 VGGRLNIAYNCLDRHAE-GRGDK----VALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 113 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVI---------QEVDTVASECPSLRIKLLV----SEK 179
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 180 SCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAG-WTGLQASDIMWTISDTGW 258
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 259 I---LNILCSlmePWALGACTFVH-LLPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTV 330
Cdd:COG0365 238 AtghSYIVYG---PLLNGATVVLYeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 331 GESLLPETLENWRAQTGLDIRESYGQTETGlTCMVSK--TMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvK 408
Cdd:COG0365 315 GEPLNPEVWEWWYEAVGVPIVDGWGQTETG-GIFISNlpGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK-G 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 409 PiRPiGIFSGYVDNPDKTAANIRGDF---WLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETA 485
Cdd:COG0365 393 P-WP-GMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3C5E_A 486 VISSPDPVRGEVVKAFVVLASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 561
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 ... |
33-560 |
1.36e-171 |
|
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: 497.02 E-value: 1.36e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 33 VPAKFNFASDVLDHWADMEkagkrPPSPALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEW 112
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEY-----PDKLALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 113 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA--GDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKL 190
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 191 LNEASTT----HHCVETGSQEASAIYFTSGTSGLPKMAEHSYS-SLG--LKAKMdagWTGLQASDIMWTISDTGWILNIL 263
Cdd:cd05970 166 IKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTyPLGhiVTAKY---WQNVREGGLHLTVADTGWGKAVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 264 CSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWR 343
Cdd:cd05970 243 GKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 344 AQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNP 423
Cdd:cd05970 323 EKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 424 DKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVV 503
Cdd:cd05970 403 EKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
3C5E_A 504 LASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKE 560
Cdd:cd05970 483 LAKGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
42-562 |
9.43e-118 |
|
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: 356.04 E-value: 9.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 42 DVLDHWADmekagKRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIR 121
Cdd:COG0318 3 DLLRRAAA-----RHPDRPALVFGGRR-----LTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 122 AGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgdeviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcv 201
Cdd:COG0318 72 AGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 202 etgsqeaSAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTIS----DTGWILNILCSLMepwaLGACtf 277
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALplfhVFGLTVGLLAPLL----AGAT-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 278 VHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQ 356
Cdd:COG0318 170 LVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGL 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 357 TETGLTCMVSKTMKI--KPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDF 434
Cdd:COG0318 250 TETSPVVTVNPEDPGerRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGW 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 435 WLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPE 514
Cdd:COG0318 325 LRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR------PGA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
3C5E_A 515 QLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 562
Cdd:COG0318 399 ELDaEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAA 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
36-560 |
6.42e-115 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 353.05 E-value: 6.42e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 36 KFNFASDVLDHWADMEKAGKrppsPALWWVNGKGKELmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLV 115
Cdd:PRK04319 41 KVNIAYEAIDRHADGGRKDK----VALRYLDASRKEK-YTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 116 ILGCIRAGLI-------FMPGTIQMkstdilyRLQMSKAKAIVAGDEVIQEVdtVASECPSLRIKLLVSE--KSCDGWLN 186
Cdd:PRK04319 115 LLGALKNGAIvgplfeaFMEEAVRD-------RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEdvEEGPGTLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 187 FKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--------MAEHSYSSlglKAKMDagwtgLQASDIMWTISDTGW 258
Cdd:PRK04319 186 FNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKgvlhvhnaMLQHYQTG---KYVLD-----LHEDDVYWCTADPGW 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 259 ILNILCSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLL 335
Cdd:PRK04319 258 VTGTSYGIFAPWLNGA-TNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddlVKKYDLSSLRHILSVGEPLN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 336 PETLENWRAQTGLDIRESYGQTETGlTCMVSKT--MKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIrvKPIRPi 413
Cdd:PRK04319 337 PEVVRWGMKVFGLPIHDNWWMTETG-GIMIANYpaMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 414 GIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPV 493
Cdd:PRK04319 413 SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPV 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3C5E_A 494 RGEVVKAFVVLASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKE 560
Cdd:PRK04319 493 RGEIIKAFVALRP---GYEPsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
76-560 |
1.62e-111 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 339.54 E-value: 1.62e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAkAIVAGDE 155
Cdd:cd05974 3 FAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA-VYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 ViqevdTVASEcPSLrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGLKA 235
Cdd:cd05974 81 N-----THADD-PML----------------------------------------LYFTSGTTSKPKLVEHTHRSYPVGH 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 236 KMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD 315
Cdd:cd05974 115 LSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 316 LSSYKFPhLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETglTCMVSKT--MKIKPGYMGTAASCYDVQIIDDKGN 393
Cdd:cd05974 195 LASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET--TALVGNSpgQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 394 vlpPGTEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN 473
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 474 ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQR 553
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAG--YEPSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRR 425
|
....*..
3C5E_A 554 AKLRDKE 560
Cdd:cd05974 426 VELRRRE 432
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
74-558 |
9.93e-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: 341275 [Multi-domain] Cd Length: 439 Bit Score: 335.17 E-value: 9.93e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 153
Cdd:cd05971 7 VTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPKMAEHSYSSLGL 233
Cdd:cd05971 85 -------------------------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLLG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 234 KAKMDAGWTGL--QASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRML 311
Cdd:cd05971 116 HLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMM 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 312 LQQDLSSYKFP-HLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGL---TCmvSKTMKIKPGYMGTAASCYDVQI 387
Cdd:cd05971 196 RQQGEQLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLvigNC--SALFPIKPGSMGKPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 388 IDDKGNVLPPGTEGDIGIRvkpiRPIGI-FSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRI 466
Cdd:cd05971 274 VDDNGTPLPPGEVGEIAVE----LPDPVaFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 467 GPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 546
Cdd:cd05971 350 GPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNELPRT 427
|
490
....*....|..
3C5E_A 547 VTGKIQRAKLRD 558
Cdd:cd05971 428 ATGKIRRRELRA 439
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
74-560 |
9.40e-102 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 314.83 E-value: 9.40e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 153
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 DEVIQEVDTvasECPSLrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGL 233
Cdd:cd05969 80 EELYERTDP---EDPTL----------------------------------------LHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 234 KAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGaCTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ 313
Cdd:cd05969 117 YYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNG-VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 314 QD---LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGlTCMVSK--TMKIKPGYMGTAASCYDVQII 388
Cdd:cd05969 196 EGdelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETG-SIMIANypCMPIKPGSMGKPLPGVKAAVV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 389 DDKGNVLPPGTEGDIGIrvKPIRPiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGP 468
Cdd:cd05969 275 DENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 469 SEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTV 547
Cdd:cd05969 352 FEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF---EPsDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|...
3C5E_A 548 TGKIQRAKLRDKE 560
Cdd:cd05969 429 SGKIMRRVLKAKE 441
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
48-557 |
4.19e-100 |
|
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: 311.42 E-value: 4.19e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 48 ADM--EKAGKRPPSPALWWvngKGKelMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI 125
Cdd:cd05936 2 ADLleEAARRFPDKTALIF---MGR--KLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 126 FMPGTIQMKSTDILYRLQMSKAKAIVAGDEviqevdtvasecpslrikllvsekscdgwlnFKKLLNEASTTHHCVETGS 205
Cdd:cd05936 76 VVPLNPLYTPRELEHILNDSGAKALIVAVS-------------------------------FTDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 206 QEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTG--LQASDIMwtisdtgwiLNIL---------CSLMEPWALGA 274
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdlLEGDDVV---------LAALplfhvfgltVALLLPLALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 275 CtfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES 353
Cdd:cd05936 196 T--IVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 354 YGQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANI 430
Cdd:cd05936 274 YGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-------GpqVMKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 431 RgDFWLL-GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqfl 509
Cdd:cd05936 347 V-DGWLRtGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL----- 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
3C5E_A 510 sHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd05936 421 -KEGASLTEeEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
76-557 |
4.71e-95 |
|
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: 297.12 E-value: 4.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagde 155
Cdd:cd05973 3 FGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 viqevdTVASECPSLRIKLLVsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSL-GLK 234
Cdd:cd05973 78 ------TDAANRHKLDSDPFV----------------------------------MMFTSGTTGLPKGVPVPLRALaAFG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 235 AKMDAGwTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPkFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ 314
Cdd:cd05973 118 AYLRDA-VDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 315 DLSSYKFP--HLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGltcMV-----SKTMKIKPGYMGTAASCYDVQI 387
Cdd:cd05973 196 GAEVPARPkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELG---MVlanhhALEHPVHAGSAGRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 388 IDDKGNVLPPGTEGDIGIRVKPiRPIGIFSGYVDNPDKTAAnirGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIG 467
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIAN-SPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 468 PSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKT 546
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG---GHEGtPALADELQLHVKKRLSAHAYPRTIHFVDELPKT 425
|
490
....*....|.
3C5E_A 547 VTGKIQRAKLR 557
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 ... |
211-552 |
3.61e-90 |
|
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: 281.10 E-value: 3.61e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCsLMEPWALGACtfVHLLPKFDPLVIL 290
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFG-LLGALLAGGT--VVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 291 KTLSSYPIKSMMGAPIVYRMLLQQDLSS-YKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG--LTCMVSK 367
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARLLKAPESAgYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtVATGPPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 368 TMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDG 447
Cdd:cd04433 162 DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR-----GPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 448 YFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlSHDPEqltkELQQHVKSV 527
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA-DLDAE----ELRAHVRER 311
|
330 340
....*....|....*....|....*
3C5E_A 528 TAPYKYPRKIEFVLNLPKTVTGKIQ 552
Cdd:cd04433 312 LAPYKVPRRVVFVDALPRTASGKID 336
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
35-557 |
2.68e-86 |
|
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: 276.56 E-value: 2.68e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 35 AKFNFASDVLDHwadmeKAGKRPPSPALWwvnGKGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWL 114
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAFI---DDAGSL--TYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 115 VILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVS--EKSCDGWLNFKKLLN 192
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSggAGPEAGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 193 EASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWA 271
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVlGIREDDVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 272 LGACTFvhLLPKF-DPLVILKTLSSYPIKSMMGAPIVYR-MLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLD 349
Cdd:cd05959 230 VGATTV--LMPERpTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 350 IRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAAN 429
Cdd:cd05959 308 ILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSAT-----MYWNNRDKTRDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 430 IRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFl 509
Cdd:cd05959 383 FQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
3C5E_A 510 sHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd05959 462 -EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
41-562 |
3.09e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 271.67 E-value: 3.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 41 SDVLDHWAdmekaGKRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCI 120
Cdd:PRK06187 9 GRILRHGA-----RKHPDKEAVYFDGRR-----TTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 121 RAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDG----WLNFKKLLNEAST 196
Cdd:PRK06187 78 KIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 197 THHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDI------MWTISDTGWilnilcSLMePW 270
Cdd:PRK06187 158 TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVylvivpMFHVHAWGL------PYL-AL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 271 ALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ------QDLSSYKFphlqncVTVGESLLPETL-ENWR 343
Cdd:PRK06187 231 MAGA-KQV-IPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKaprayfVDFSSLRL------VIYGGAALPPALlREFK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 344 AQTGLDIRESYGQTETG--LTCMV-SKTMKIKPGYM---GTAASCYDVQIIDDKGNVLPPGtEGDIG-IRVKpirpiG-- 414
Cdd:PRK06187 303 EKFGIDLVQGYGMTETSpvVSVLPpEDQLPGQWTKRrsaGRPLPGVEARIVDDDGDELPPD-GGEVGeIIVR-----Gpw 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 415 IFSGYVDNPDKTAANIRGDfWLL-GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPV 493
Cdd:PRK06187 377 LMQGYWNRPEATAETIDGG-WLHtGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEK 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 494 RGEVVKAFVVLasqflsHDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 562
Cdd:PRK06187 456 WGERPVAVVVL------KPGATLDaKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
71-557 |
7.26e-82 |
|
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: 263.18 E-value: 7.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 71 ELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmpgtiqmkstdilyrlqmskakai 150
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAI------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 151 vagdeviqevdTVASEcPSLRIKllvsekscdgwlNFKKLLNEASTTHH-CVE--TGSQEASAIYFTSGTSGLPKMAEHS 227
Cdd:cd05958 63 -----------AVATM-PLLRPK------------ELAYILDKARITVAlCAHalTASDDICILAFTSGTTGAPKATMHF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 228 YSSLGLKAKmdaGWT----GLQASDIMWTISDTGWILNILCSLMEPWALGACTFvhLLPKFDPLVILKTLSSYPIKSMMG 303
Cdd:cd05958 119 HRDPLASAD---RYAvnvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGV--LLEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 304 APIVYRMLL------QQDLSSykfphLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMG 377
Cdd:cd05958 194 APTAYRAMLahpdaaGPDLSS-----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 378 TAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpigifSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRAD 456
Cdd:cd05958 269 KPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP--------TGCRYLADKRQRTYVQGGWNItGDTYSRDPDGYFRHQGRSD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 457 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflsHDP-EQLTKELQQHVKSVTAPYKYPR 535
Cdd:cd05958 341 DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPG---VIPgPVLARELQDHAKAHIAPYKYPR 417
|
490 500
....*....|....*....|..
3C5E_A 536 KIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd05958 418 AIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
76-559 |
3.06e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 255.60 E-value: 3.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 155
Cdd:PRK07656 33 YAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 VIqEVDTVASEC-PSLRIKLLV----SEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 230
Cdd:PRK07656 112 FL-GVDYSATTRlPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 231 LGLKAKMDAGWTGLQASDIMWTISDT----GWILNILCSLMEpwalGACTFVHllPKFDPLVILKTLSSYPIKSMMGAPI 306
Cdd:PRK07656 191 LLSNAADWAEYLGLTEGDRYLAANPFfhvfGYKAGVNAPLMR----GATILPL--PVFDPDEVFRLIETERITVLPGPPT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 307 VYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLD-IRESYGQTE-TGLTCM--VSKTMKIKPGYMGTAAS 381
Cdd:PRK07656 265 MYNSLLQHpDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEaSGVTTFnrLDDDRKTVAGTIGTAIA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 382 CYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDI 458
Cdd:PRK07656 345 GVENKIVNELGEEVPVGEVGELLVR-------GpnVMKGYYDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDM 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 459 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKE-LQQHVKSVTAPYKYPRKI 537
Cdd:PRK07656 418 FIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG------AELTEEeLIAYCREHLAKYKVPRSI 491
|
490 500
....*....|....*....|..
3C5E_A 538 EFVLNLPKTVTGKIQRAKLRDK 559
Cdd:PRK07656 492 EFLDELPKNATGKVLKRALREK 513
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
76-557 |
5.80e-74 |
|
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: 242.37 E-value: 5.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 155
Cdd:cd05919 13 YGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 VIqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeASAIYfTSGTSGLPKMAEHSY-SSLGLK 234
Cdd:cd05919 92 DI--------------------------------------------------AYLLY-SSGTTGPPKGVMHAHrDPLLFA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 235 AKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLPKfDPLVILKTLSSYPIKSMMGAPIVY-RMLLQ 313
Cdd:cd05919 121 DAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNLLDS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 314 QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGN 393
Cdd:cd05919 200 CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 394 VLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN 473
Cdd:cd05919 280 TIPPGEEGDLLVRGP-----SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 474 ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
....
3C5E_A 554 AKLR 557
Cdd:cd05919 433 FKLR 436
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
36-558 |
9.37e-74 |
|
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: 243.98 E-value: 9.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 36 KFNFASDVLDHWADMEKAGKrppspaLWWVNGKGKelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLV 115
Cdd:TIGR02262 2 KYNAAEDLLDRNVVEGRGGK------TAFIDDISS---LSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 116 ILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKScDGWLNFKKLLNEAS 195
Cdd:TIGR02262 72 FLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGRPE-AGEVQLAELLATES 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 196 TTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISDTGWILNILCSLMEPWALGA 274
Cdd:TIGR02262 151 EQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTlGIREDDVCFSAAKLFFAYGLGNALTFPMSVGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 275 cTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYR-MLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES 353
Cdd:TIGR02262 231 -TTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 354 YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiGIFS--GYVDNPDKTAANIR 431
Cdd:TIGR02262 310 IGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-------GPSSatMYWNNRAKSRDTFQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 432 GDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsh 511
Cdd:TIGR02262 383 GEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ--- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
3C5E_A 512 dpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:TIGR02262 460 --TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
74-557 |
1.49e-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: 237.96 E-value: 1.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 153
Cdd:cd05934 4 WTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 deviqeVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLGL 233
Cdd:cd05934 81 ------VDPAS----------------------------------------------ILYTSGTTGPPKGVVITHANLTF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 234 KAKMDAGWTGLQASDIMWTISDTGWIlNILC-SLMEPWALGAcTFVhLLPKFDPLVILKTLSSY--PIKSMMGAPIvyRM 310
Cdd:cd05934 109 AGYYSARRFGLGEDDVYLTVLPLFHI-NAQAvSVLAALSVGA-TLV-LLPRFSASRFWSDVRRYgaTVTNYLGAML--SY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 311 LLQQDLSSYKFPHLQNCVTVGESLlPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDD 390
Cdd:cd05934 184 LLAQPPSPDDRAHRLRAAYGAPNP-PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 391 KGNVLPPGTEGDIGIRvkPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSE 470
Cdd:cd05934 263 DGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 471 VENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 549
Cdd:cd05934 341 VERAILRHPAVREAAVVAVPDEVGEDEVKAVVVL------RPGETLDpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTE 414
|
....*...
3C5E_A 550 KIQRAKLR 557
Cdd:cd05934 415 KVAKAQLR 422
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
53-553 |
2.03e-72 |
|
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: 238.28 E-value: 2.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 53 AGKRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQ 132
Cdd:cd17631 5 ARRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 133 MKSTDILYRLQMSKAKAIVagDEVIQevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIY 212
Cdd:cd17631 79 LTPPEVAYILADSGAKVLF--DDLAL----------------------------------------------------LM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 213 FTSGTSGLPKMAEHSYSSL-------GLKAKMDAGWTGLQASDIMWTISDTGWILNILcslmepwALGACtfVHLLPKFD 285
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNLlwnavnaLAALDLGPDDVLLVVAPLFHIGGLGVFTLPTL-------LRGGT--VVILRKFD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 286 PLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQnCVTVGESLLPE-TLENWRAqTGLDIRESYGQTETG-LT 362
Cdd:cd17631 176 PETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLR-AVIYGGAPMPErLLRALQA-RGVKFVQGYGMTETSpGV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 363 CMVSKTMKI-KPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDfWLL-GDR 440
Cdd:cd17631 254 TFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GP----HVMAGYWNRPEATAAAFRDG-WFHtGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 441 GIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT-KE 519
Cdd:cd17631 328 GRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR------PGAELDeDE 401
|
490 500 510
....*....|....*....|....*....|....
3C5E_A 520 LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:cd17631 402 LIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
56-564 |
2.58e-69 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 234.90 E-value: 2.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 56 RPPSPALWWVNG-KGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI-------Fm 127
Cdd:cd05967 64 RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLR-KLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsvvfggF- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 128 pgtiqmKSTDILYRLQMSKAKAIVA------GDEVIQE---VDTVASECPSLRIKLLV---SEKSCD-----GWLNFKKL 190
Cdd:cd05967 142 ------AAKELASRIDDAKPKLIVTascgiePGKVVPYkplLDKALELSGHKPHHVLVlnrPQVPADltkpgRDLDWSEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 191 LNEAsTTHHCVETGSQEASAIYFTSGTSGLPK-----MAEHSyssLGLKAKMDAGWtGLQASDIMWTISDTGWILNILCS 265
Cdd:cd05967 216 LAKA-EPVDCVPVAATDPLYILYTSGTTGKPKgvvrdNGGHA---VALNWSMRNIY-GIKPGDVWWAASDVGWVVGHSYI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 266 LMEPWALGACTFVH-----LLPkfDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD-----LSSYKFPHLQNCVTVGESLL 335
Cdd:cd05967 291 VYGPLLHGATTVLYegkpvGTP--DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyIKKYDLSSLRTLFLAGERLD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 336 PETLENWRAQTGLDIRESYGQTETG----LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVkPIR 411
Cdd:cd05967 369 PPTLEWAENTLGVPVIDHWWQTETGwpitANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLP 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 412 PiGIFSGYVDNPDKTAANIRGDF---WLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVIS 488
Cdd:cd05967 448 P-GCLLTLWKNDERFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 489 SPDPVRGEVVKAFVVLASQfLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD----KEWKMS 564
Cdd:cd05967 527 VRDELKGQVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKiadgEDYTIP 605
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
74-558 |
4.18e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 226.74 E-value: 4.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 153
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 DEVIQEVDTVASECPSLRIKLLVSEK---SCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 230
Cdd:PRK08316 116 PALAPTAEAALALLPVDTLILSLVLGgreAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 231 L---GLKAKMDAGWTglqASDIMwtisdtgwiLNIL----CSLME----PW-ALGACTfvHLLPKFDPLVILKTLSSYPI 298
Cdd:PRK08316 196 LiaeYVSCIVAGDMS---ADDIP---------LHALplyhCAQLDvflgPYlYVGATN--VILDAPDPELILRTIEAERI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 299 KSMMGAPIVYRMLL------QQDLSSykfphLQNCVtVGESLLP-ETLENWRAQ-TGLDIRESYGQTETGLTCMV--SKT 368
Cdd:PRK08316 262 TSFFAPPTVWISLLrhpdfdTRDLSS-----LRKGY-YGASIMPvEVLKELRERlPGLRFYNCYGQTEIAPLATVlgPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 369 MKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGY 448
Cdd:PRK08316 336 HLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR-SP----QLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 449 FQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLT-KELQQHVKSV 527
Cdd:PRK08316 411 ITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG------ATVTeDELIAHCRAR 484
|
490 500 510
....*....|....*....|....*....|.
3C5E_A 528 TAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK08316 485 LAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
76-558 |
1.06e-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: 223.32 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGde 155
Cdd:cd05941 14 YADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVLDP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 viqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeaSAIYFTSGTSGLPKMAEHSYSSLG--L 233
Cdd:cd05941 92 -----------------------------------------------------ALILYTSGTTGRPKGVVLTHANLAanV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 234 KAKMDAgWTglqasdimWTISDT-----------GWILNILCSLmepWALGACtfvHLLPKFDPLVILKTLSSYPIKSMM 302
Cdd:cd05941 119 RALVDA-WR--------WTEDDVllhvlplhhvhGLVNALLCPL---FAGASV---EFLPKFDPKEVAISRLMPSITVFM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 303 GAPIVYRMLLQQdlSSYKFPHLQNCVTVGES-----------LLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKI 371
Cdd:cd05941 184 GVPTIYTRLLQY--YEAHFTDPQFARAAAAErlrlmvsgsaaLPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 372 KPGYMGTAASCYDVQIIDDKGN-VLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYF 449
Cdd:cd05941 262 RPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GP----SVFKEYWNKPEATKEEFTDDGWFkTGDLGVVDEDGYY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 450 QFMGR-ADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEqltkELQQHVKSVT 528
Cdd:cd05941 337 WILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE----ELKEWAKQRL 412
|
490 500 510
....*....|....*....|....*....|
3C5E_A 529 APYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:cd05941 413 APYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
35-558 |
1.59e-65 |
|
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: 224.36 E-value: 1.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 35 AKFNFASDVLDHWAdmekaGKRPPSPALWWV-NGKGKELMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEww 113
Cdd:cd05966 50 GKLNISYNCLDRHL-----KERGDKVAIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPE-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 114 LVI--LGCIRAGLI-------FMPGTIQMkstdilyRLQMSKAKAIVAGDE------VI---QEVDTVASECPSLRiKLL 175
Cdd:cd05966 122 LVIamLACARIGAVhsvvfagFSAESLAD-------RINDAQCKLVITADGgyrggkVIplkEIVDEALEKCPSVE-KVL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 176 VSEKSC---------DGWLNfkKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQ 245
Cdd:cd05966 194 VVKRTGgevpmtegrDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVfDYH 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 246 ASDIMWTISDTGWILNILCSLMEPWALGACTfvhllpkfdplVILKTLSSYPIKSMM-------------GAPIVYRMLL 312
Cdd:cd05966 272 PDDIYWCTADIGWITGHSYIVYGPLANGATT-----------VMFEGTPTYPDPGRYwdivekhkvtifyTAPTAIRALM 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 313 QQ--------DLSSYKFPHlqncvTVGESLLPETLENWRAQTG---LDIRESYGQTETG---LTCMVSKTmKIKPGYMGT 378
Cdd:cd05966 341 KFgdewvkkhDLSSLRVLG-----SVGEPINPEAWMWYYEVIGkerCPIVDTWWQTETGgimITPLPGAT-PLKPGSATR 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 379 AASCYDVQIIDDKGNVLPPGTEGDIGIRvkpiRPI-GIFSGYVDNPD---KTAANIRGDFWLLGDRGIKDEDGYFQFMGR 454
Cdd:cd05966 415 PFFGIEPAILDEEGNEVEGEVEGYLVIK----RPWpGMARTIYGDHEryeDTYFSKFPGYYFTGDGARRDEDGYYWITGR 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 455 ADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflSHDPEQ-LTKELQQHVKSVTAPYKY 533
Cdd:cd05966 491 VDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKD---GEEPSDeLRKELRKHVRKEIGPIAT 567
|
570 580
....*....|....*....|....*
3C5E_A 534 PRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:cd05966 568 PDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
51-462 |
1.73e-65 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 219.49 E-value: 1.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPAlwWVNGKGKELmwNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGT 130
Cdd:pfam00501 3 RQAARTPDKTA--LEVGEGRRL--TYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 131 IQMKSTDILYRLQMSKAKAIVAGDE-VIQEVDTVASECPSLRIKLLVSEkscDGWLNFKKLLNEASTTHHCVETGSQEAS 209
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDR---DPVLKEEPLPEEAKPADVPPPPPPPPDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 210 ----AIYFTSGTSGLPKMAEHS----YSSLGLKAKMDAGWTGLQASDIMWTIS----DTGWILNILCSLMepwaLGACtf 277
Cdd:pfam00501 155 ddlaYIIYTSGTTGKPKGVMLThrnlVANVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLSLGLLGPLL----AGAT-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 278 VHLLPKF---DPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRES 353
Cdd:pfam00501 229 VVLPPGFpalDPAALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 354 YGQTETGLTCMVSKTMKIK---PGYMGTAASCYDVQIIDDK-GNVLPPGTEGDIGIRvkpiRPiGIFSGYVDNPDKTAAN 429
Cdd:pfam00501 309 YGLTETTGVVTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEA 383
|
410 420 430
....*....|....*....|....*....|....
3C5E_A 430 IRGDFWLL-GDRGIKDEDGYFQFMGRADDIINSS 462
Cdd:pfam00501 384 FDEDGWYRtGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
74-558 |
1.07e-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: 1.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 153
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 DEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASA---IYFTSGTSGLPKMAEHSYSS 230
Cdd:cd05926 94 KGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDlalILHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 231 LGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACtfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRM 310
Cdd:cd05926 174 LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGS--VVLPPRFSASTFWPDVRDYNATWYTAVPTIHQI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 311 LLQQDLSSY--KFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG--LTCMVSKTMKIKPGYMGTAASCyDVQ 386
Cdd:cd05926 252 LLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKPGSVGKPVGV-EVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 387 IIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRADDIINSSGYR 465
Cdd:cd05926 331 ILDEDGEILPPGVVGEICLRGP-----NVTRGYLNNPEANAEAAFKDGWFRtGDLGYLDADGYLFLTGRIKELINRGGEK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 466 IGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPK 545
Cdd:cd05926 406 ISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRE-----GASVTEEELRAFCRKHLAAFKVPKKVYFVDELPK 480
|
490
....*....|...
3C5E_A 546 TVTGKIQRAKLRD 558
Cdd:cd05926 481 TATGKIQRRKVAE 493
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
74-552 |
3.00e-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: 217.85 E-value: 3.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 153
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 DEVIQEVDTVASECPSLRiKLLVSEKSCDGWLNFKKLLNEASTTHH-----CVETGSQEASAIYFTSGTSGLPKMAEHSY 228
Cdd:cd05911 90 PDGLEKVKEAAKELGPKD-KIIVLDDKPDGVLSIEDLLSPTLGEEDedlppPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 229 SSLglkakmdagwtgLQASDIMWTISDTGWILN--ILCSLMEPWALGACTFVHLL---------PKFDPLVILKTLSSYP 297
Cdd:cd05911 169 RNL------------IANLSQVQTFLYGNDGSNdvILGFLPLYHIYGLFTTLASLlngatviimPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 298 IKSMMGAP-IVYRMLLQQDLSSYKFPHLQNcVTVG--------ESLLPETLENWRaqtgldIRESYGQTETGLTCMVSKT 368
Cdd:cd05911 237 ITFLYLVPpIAAALAKSPLLDKYDLSSLRV-ILSGgaplskelQELLAKRFPNAT------IKQGYGMTETGGILTVNPD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 369 MKIKPGYMGTAASCYDVQIIDDKGN-VLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDED 446
Cdd:cd05911 310 GDDKPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVR-----GPQVMKGYYNNPEATKETFDEDGWLhTGDIGYFDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 447 GYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT-KELQQHVK 525
Cdd:cd05911 385 GYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRK------PGEKLTeKEVKDYVA 458
|
490 500
....*....|....*....|....*...
3C5E_A 526 SVTAPYKYPRK-IEFVLNLPKTVTGKIQ 552
Cdd:cd05911 459 KKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
47-566 |
1.27e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 217.91 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 47 WADMEKAGKRPPS-PALWWVngkGKELmwNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI 125
Cdd:PRK08314 13 FHNLEVSARRYPDkTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 126 FMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEV------------------DTVASECP-----SLRIKLLVSEKSCD 182
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 183 GWLnfkkLLNEASTTHHC---VETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWI 259
Cdd:PRK08314 168 GVV----AWKEALAAGLApppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 260 LNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ------DLSSYKfphlqnCVTVGES 333
Cdd:PRK08314 244 TGMVHSMNAPIYAGA-TVV-LMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASpglaerDLSSLR------YIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 334 LLPETL-ENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRvkpir 411
Cdd:PRK08314 316 AMPEAVaERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH----- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 412 piG--IFSGYVDNPDKTAA---NIRGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETA 485
Cdd:PRK08314 391 --GpqVFKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAC 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 486 VISSPDPVRGEVVKAFVVLASQFLSHDPEQltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSG 565
Cdd:PRK08314 469 VIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAA 545
|
.
3C5E_A 566 K 566
Cdd:PRK08314 546 K 546
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
35-551 |
7.15e-63 |
|
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: 217.06 E-value: 7.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 35 AKFNFASDVLD-HWADmekagkRPPSPALWWVNGKGKEL-MWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEW 112
Cdd:cd17634 50 ATLNLAANALDrHLRE------NGDRTAIIYEGDDTSQSrTISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 113 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTV----------ASECPSLRIKLLVSEKSCD 182
Cdd:cd17634 123 AVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVplkknvddalNPNVTSVEHVIVLKRTGSD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 183 ------GWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMWTISD 255
Cdd:cd17634 203 idwqegRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVfDYGPGDIYWCTAD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 256 TGWILNILCSLMEPWALGACTFVHL-LPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTV 330
Cdd:cd17634 283 VGWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 331 GESLLPETLE-NWR--AQTGLDIRESYGQTETGLTCMvsktmKIKPGYMGTAASC-------YDVQIIDDKGNVLPPGTE 400
Cdd:cd17634 363 GEPINPEAYEwYWKkiGKEKCPVVDTWWQTETGGFMI-----TPLPGAIELKAGSatrpvfgVQPAVVDNEGHPQPGGTE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 401 GDIGIRVKpiRPIGIFSGYVDNPDKTAANIR--GDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEH 478
Cdd:cd17634 438 GNLVITDP--WPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAH 515
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3C5E_A 479 PAVVETAVISSPDPVRGEVVKAFVVLASQFLshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 551
Cdd:cd17634 516 PKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
75-556 |
8.50e-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: 212.72 E-value: 8.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 75 NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGd 154
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 155 eviQEVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSGTSGLPKMAEHSYSSLGLK 234
Cdd:cd05935 81 ---SELDDLA---------------------------------------------LIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 235 AKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL-- 312
Cdd:cd05935 113 ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGG-TYV-LMARWDRETALELIEKYKVTFWTNIPTMLVDLLat 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 313 ----QQDLSSYKFphlqncVTVGESLLPETL-ENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQI 387
Cdd:cd05935 191 pefkTRDLSSLKV------LTGGGAPMPPAVaEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 388 ID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAA---NIRG-DFWLLGDRGIKDEDGYFQFMGRADDIINSS 462
Cdd:cd05935 265 IDiETGRELPPNEVGEIVVR-GP----QIFKGYWNRPEETEEsfiEIKGrRFFRTGDLGYMDEEGYFFFVDRVKRMINVS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 463 GYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQltkELQQHVKSVTAPYKYPRKIEFVLN 542
Cdd:cd05935 340 GFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDE 416
|
490
....*....|....
3C5E_A 543 LPKTVTGKIQRAKL 556
Cdd:cd05935 417 LPRSASGKILWRLL 430
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
27-557 |
1.45e-62 |
|
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: 216.59 E-value: 1.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 27 QWGHQEVPAKFNFASDVLDHWAdmekaGKRPPSPALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVL 106
Cdd:cd05968 50 PWAAWFVGGRMNIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 107 PRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD---------EVIQEVDTVASECPSLRiKLLVS 177
Cdd:cd05968 124 PMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTVE-KVVVV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 178 E--KSCDGWLNFKKL---LNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASDIMW 251
Cdd:cd05968 203 RhlGNDFTPAKGRDLsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQfDLKPGDLLT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 252 TISDTGWilnilcsLMEPWA------LGACTFVHL-LPKFD-PLVILKTLSSYPIKSMMGAPIVYRMLL--------QQD 315
Cdd:cd05968 283 WFTDLGW-------MMGPWLifggliLGATMVLYDgAPDHPkADRLWRMVEDHEITHLGLSPTLIRALKprgdapvnAHD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 316 LSSykfphLQNCVTVGESLLPETLeNWRAQTGLD----IRESYGQTETG---LTCMVSKtmKIKPGYMGTAASCYDVQII 388
Cdd:cd05968 356 LSS-----LRVLGSTGEPWNPEPW-NWLFETVGKgrnpIINYSGGTEISggiLGNVLIK--PIKPSSFNGPVPGMKADVL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 389 DDKGNVLPPgTEGDIGIRvKPIrpIGIFSGYVDNPDK---TAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYR 465
Cdd:cd05968 428 DESGKPARP-EVGELVLL-APW--PGMTRGFWRDEDRyleTYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKR 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 466 IGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPK 545
Cdd:cd05968 504 VGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGV--TPTEALAEELMERVADELGKPLSPERILFVKDLPK 581
|
570
....*....|..
3C5E_A 546 TVTGKIQRAKLR 557
Cdd:cd05968 582 TRNAKVMRRVIR 593
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
27-556 |
6.66e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 213.75 E-value: 6.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 27 QWGHQEVPAkfnfaSDVLDHWADmekagKRPPSPALWWVngkGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVL 106
Cdd:PRK06178 27 EYPHGERPL-----TEYLRAWAR-----ERPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 107 PRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASEC-----------------PS 169
Cdd:PRK06178 91 PNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhvivtsladvlpaePT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 170 LRIKLLVSE--KSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTG-LQA 246
Cdd:PRK06178 171 LPLPDSLRAprLAAAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVvGGE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 247 SDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL------QQDLSSYK 320
Cdd:PRK06178 251 DSVFLSFLPEFWIAGENFGLLFPLFSGA-TLV-LLARWDAVAFMAAVERYRVTRTVMLVDNAVELMdhprfaEYDLSSLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 321 FPhlqNCVTVGESLLPETLENWRAQTGLDIRE-SYGQTETGlTC------MVSKTMKIK--PGYMGTAASCYDVQIID-D 390
Cdd:PRK06178 329 QV---RVVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTETH-TCdtftagFQDDDFDLLsqPVFVGLPVPGTEFKICDfE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 391 KGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPS 469
Cdd:PRK06178 405 TGELLPLGAEGEIVVR-TP----SLLKGYWNKPEATAEALR-DGWLhTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 470 EVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPrKIEFVLNLPKTVTG 549
Cdd:PRK06178 479 EVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP-----GADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATG 552
|
....*..
3C5E_A 550 KIQRAKL 556
Cdd:PRK06178 553 KVRKQDL 559
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
50-559 |
2.52e-59 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 205.49 E-value: 2.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 50 MEKAGKRPPSPALWWVNGkgkeLMWNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPG 129
Cdd:PRK07514 9 LRAAFADRDAPFIETPDG----LRYTYGDLDAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 130 TIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSekscDGWLNFKKLLNEASTTHHCVETGSQEAS 209
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDA----DGTGSLLEAAAAAPDDFETVPRGADDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 210 AIYFTSGTSGLPKMAEHSYSSLGLKAKM--DA-GWTG----LQASDIMWTisdTGWILNILCSLMEpwalGACTFvhLLP 282
Cdd:PRK07514 160 AILYTSGTTGRSKGAMLSHGNLLSNALTlvDYwRFTPddvlIHALPIFHT---HGLFVATNVALLA----GASMI--FLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 283 KFDPLVILKTLSSypIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGl 361
Cdd:PRK07514 231 KFDPDAVLALMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETN- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 362 tcmvsktMKI--------KPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANI 430
Cdd:PRK07514 308 -------MNTsnpydgerRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 431 RGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAfVVLASQFL 509
Cdd:PRK07514 374 RADgFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA-VVVPKPGA 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3C5E_A 510 SHDPEQLTKELQQHVksvtAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 559
Cdd:PRK07514 453 ALDEAAILAALKGRL----ARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
74-562 |
2.56e-58 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 203.83 E-value: 2.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 153
Cdd:PRK06087 50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 DEVIQ-----EVDTVASECPSLRIKLLV-SEKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHS 227
Cdd:PRK06087 129 TLFKQtrpvdLILPLQNQLPQLQQIVGVdKLAPATSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 228 YSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFvhLLPKFDPLVILKTLSSYPIKSMMGA-PI 306
Cdd:PRK06087 209 HNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDACLALLEQQRCTCMLGAtPF 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 307 VYRML--LQQ---DLSSYKFphlqncVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMV--SKTMKIKPGYMGTA 379
Cdd:PRK06087 287 IYDLLnlLEKqpaDLSALRF------FLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVnlDDPLSRFMHTDGYA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 380 ASCYDVQIIDDKGNVLPPGTEGDigirvKPIRPIGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRADDI 458
Cdd:PRK06087 361 AAGVEIKVVDEARKTLPPGCEGE-----EASRGPNVFMGYLDEPELTARALDEEGWYYsGDLCRMDEAGYIKITGRKKDI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 459 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKEL-QQHVksvtAPYKYPRKI 537
Cdd:PRK06087 436 IVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFsRKRV----AKYKYPEHI 511
|
490 500
....*....|....*....|....*
3C5E_A 538 EFVLNLPKTVTGKIQRAKLRdKEWK 562
Cdd:PRK06087 512 VVIDKLPRTASGKIQKFLLR-KDIM 535
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
74-567 |
3.51e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 199.36 E-value: 3.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 153
Cdd:PRK08276 12 VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 DEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETgsqEASAIYFTSGTSGLPK----------- 222
Cdd:PRK08276 91 AALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADET---AGADMLYSSGTTGRPKgikrplpgldp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 223 --MAEHSYSSLGLKAKMDAGWTGLQASDIMWTiSDTGWILNILcslmepwALGAcTFVhLLPKFDPLVILKTLSSYPIKS 300
Cdd:PRK08276 168 deAPGMMLALLGFGMYGGPDSVYLSPAPLYHT-APLRFGMSAL-------ALGG-TVV-VMEKFDAEEALALIERYRVTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 301 MMGAPIVY-RML-LQQ------DLSSYKF------PhlqnC-VTVGESLLpetlENWraqtGLDIRESYGQTET-GLTCM 364
Cdd:PRK08276 238 SQLVPTMFvRMLkLPEevraryDVSSLRVaihaaaP----CpVEVKRAMI----DWW----GPIIHEYYASSEGgGVTVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 365 VSKTMKIKPGYMGTAASCyDVQIIDDKGNVLPPGTEGDIGIRvkpiRPIGIFSgYVDNPDKTAANIRGDFWL-LGDRGIK 443
Cdd:PRK08276 306 TSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE----MDGYPFE-YHNDPEKTAAARNPHGWVtVGDVGYL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 444 DEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQ 522
Cdd:PRK08276 380 DEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPAD---GADAgDALAAELIA 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
3C5E_A 523 HVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKA 567
Cdd:PRK08276 457 WLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQRA 501
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
76-558 |
6.02e-57 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 201.91 E-value: 6.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI-------FMPGTIQMkstdilyRLQMSKAK 148
Cdd:PRK00174 101 YRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvfggFSAEALAD-------RIIDAGAK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 149 AIVAGDEVI---------QEVDTVASECPSLRiKLLVSEKSC---------DGWLNfkKLLNEASTTHHCVETGSQEASA 210
Cdd:PRK00174 173 LVITADEGVrggkpiplkANVDEALANCPSVE-KVIVVRRTGgdvdwvegrDLWWH--ELVAGASDECEPEPMDAEDPLF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKMAEHS------YSSLGLKAKMDagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACTfvhllpkf 284
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHTtggylvYAAMTMKYVFD-----YKDGDVYWCTADVGWVTGHSYIVYGPLANGATT-------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 285 dplVILKTLSSYPIKSMMG-------------APIVYRMLLQQ--------DLSSYKFPHlqncvTVGESLLPETLENWR 343
Cdd:PRK00174 317 ---LMFEGVPNYPDPGRFWevidkhkvtifytAPTAIRALMKEgdehpkkyDLSSLRLLG-----SVGEPINPEAWEWYY 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 344 AQTGLD---IRESYGQTETGlTCMVSK---TMKIKPGymgtaaSC------YDVQIIDDKGNVLPPGTEGDIGIRvKP-- 409
Cdd:PRK00174 389 KVVGGErcpIVDTWWQTETG-GIMITPlpgATPLKPG------SAtrplpgIQPAVVDEEGNPLEGGEGGNLVIK-DPwp 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 410 --IRPIgifsgYVDnPD---KTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVET 484
Cdd:PRK00174 461 gmMRTI-----YGD-HErfvKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEA 534
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3C5E_A 485 AVISSPDPVRGEVVKAFVVLASqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK00174 535 AVVGRPDDIKGQGIYAFVTLKG---GEEPsDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
75-558 |
2.23e-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: 197.14 E-value: 2.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 75 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgD 154
Cdd:cd12118 31 TWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV-D 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 155 EVIQEVDTVASECPSLriKLLVSEKSCDgwlnfkkllneastthhcvetgsqeASAIYFTSGTSGLPKMAEHSYSSLGLK 234
Cdd:cd12118 109 REFEYEDLLAEGDPDF--EWIPPADEWD-------------------------PIALNYTSGTTGRPKGVVYHHRGAYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 235 AKMDAGWTGLQASDI-MWTISD---TGWILnilcslmePWALGACTFVHL-LPKFDPLVILKTLSSYPIKSMMGAPIVYR 309
Cdd:cd12118 162 ALANILEWEMKQHPVyLWTLPMfhcNGWCF--------PWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVTHFCGAPTVLN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 310 MLLQ-QDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTET---GLTCMVSKT-----------MKIKPG 374
Cdd:cd12118 234 MLANaPPSDARPLPHRVH-VMTAGAPPPAAVLAKMEELGFDVTHVYGLTETygpATVCAWKPEwdelpteerarLKARQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 375 --YMGTAAscydVQIIDDKGNVLPPG---TEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDG 447
Cdd:cd12118 313 vrYVGLEE----VDVLDPETMKPVPRdgkTIGEIVFR-------GniVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 448 YFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVKS 526
Cdd:cd12118 382 YIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL------KEGAKVTeEEIIAFCRE 455
|
490 500 510
....*....|....*....|....*....|..
3C5E_A 527 VTAPYKYPRKIEFVlNLPKTVTGKIQRAKLRD 558
Cdd:cd12118 456 HLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
51-557 |
3.58e-56 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 197.21 E-value: 3.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGT 130
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTANLFY-SLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 131 IQMKSTDILYRLQMSKAKAIVAGDE---VIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTT-HHCVETGSQ 206
Cdd:PRK08008 94 ARLLREESAWILQNSQASLLVTSAQfypMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPATlCYAPPLSTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 207 EASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVhLLPKFDP 286
Cdd:PRK08008 174 DTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGA-TFV-LLEKYSA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 287 LVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETgLTCMVS 366
Cdd:PRK08008 252 RAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMFYLNLSDQEKDAFEERFGVRLLTSYGMTET-IVGIIG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 367 KTmkikPG------YMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPIgiFSGYVDNPDKTAANIRGDFWL-LGD 439
Cdd:PRK08008 331 DR----PGdkrrwpSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTI--FKEYYLDPKATAKVLEADGWLhTGD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 440 RGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKE 519
Cdd:PRK08008 405 TGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN------EGETLSEE 478
|
490 500 510
....*....|....*....|....*....|....*....
3C5E_A 520 -LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:PRK08008 479 eFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
74-557 |
6.48e-55 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 196.33 E-value: 6.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGlIFMPGTIQMKSTDILYRLQMSKAKAIVA- 152
Cdd:PRK07529 59 WTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 153 ----GDEVIQEVDTVASECPSLR-----------------IKLLVSEKSCDGWLNFKKLLNEASTTHHCVET--GSQEAS 209
Cdd:PRK07529 137 gpfpGTDIWQKVAEVLAALPELRtvvevdlarylpgpkrlAVPLIRRKAHARILDFDAELARQPGDRLFSGRpiGPDDVA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 210 AIYFTSGTSGLPKMAEHSYSSLglkakMDAGWTGLQASDImwTISDTgwilnILCSL------------MEPWALGAcTF 277
Cdd:PRK07529 217 AYFHTGGTTGMPKLAQHTHGNE-----VANAWLGALLLGL--GPGDT-----VFCGLplfhvnallvtgLAPLARGA-HV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 278 VHLLPK--FDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-----DLSSYKFphlqncVTVGESLLP-ETLENWRAQT 346
Cdd:PRK07529 284 VLATPQgyRGPGVIanfWKIVERYRINFLSGVPTVYAALLQVpvdghDISSLRY------ALCGAAPLPvEVFRRFEAAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 347 GLDIRESYGQTETglTCMVS---KTMKIKPGYMGTAASCYDVQII--DDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVd 421
Cdd:PRK07529 358 GVRIVEGYGLTEA--TCVSSvnpPDGERRIGSVGLRLPYQRVRVVilDDAGRYLRDCAVDEVGVLC--IAGPNVFSGYL- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 422 NPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKA 500
Cdd:PRK07529 433 EAAHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVA 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
3C5E_A 501 FVVLA--SQFlshDPEQLTKELQQHVKSVTApykYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:PRK07529 513 YVQLKpgASA---TEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
71-558 |
5.10e-54 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 191.90 E-value: 5.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 71 ELMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 150
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 151 VAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGW-LNFKKL-LNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSY 228
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpAGWSTApLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 229 SSLGLKAKMDAGWTGLQASDIMWT---ISDTGwILNILCSLMepwaLGACTFVhLLPKF------DPLVILKTLSSYPIK 299
Cdd:PRK06155 203 AQFYWWGRNSAEDLEIGADDVLYTtlpLFHTN-ALNAFFQAL----LAGATYV-LEPRFsasgfwPAVRRHGATVTYLLG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 300 SMMgapivyRMLLQQDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKiKPGYMGTA 379
Cdd:PRK06155 277 AMV------SILLSQPARESDRAHRVR-VALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 380 ASCYDVQIIDDKGNVLPPGTEGDIGIRVKPirPIGIFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADDI 458
Cdd:PRK06155 349 APGFEARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWR-NLWFhTGDRVVRDADGWFRFVDRIKDA 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 459 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLaSQFLSHDPEqltkELQQHVKSVTAPYKYPRKIE 538
Cdd:PRK06155 426 IRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVL-RDGTALEPV----ALVRHCEPRLAYFAVPRYVE 500
|
490 500
....*....|....*....|
3C5E_A 539 FVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK06155 501 FVAALPKTENGKVQKFVLRE 520
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
31-562 |
5.87e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 192.17 E-value: 5.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 31 QEVPAKFNFASDVLDHWADmEKAGKRPPSPALWWVngkGKELmwNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVP 110
Cdd:PRK06710 13 EEIPSTISYDIQPLHKYVE-QMASRYPEKKALHFL---GKDI--TFSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNCP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 111 EWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpSLRIKLLVSEKSCDgWLNFKKL 190
Cdd:PRK06710 86 QAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQS---ATKIEHVIVTRIAD-FLPFPKN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 191 L----------------NEASTTH--HCVE----TG-------SQEASAIYFTSGTSGLPKMAEHSYSSLglkakmdagw 241
Cdd:PRK06710 162 LlypfvqkkqsnlvvkvSESETIHlwNSVEkevnTGvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNL---------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 242 tglqasdIMWTISDTGWILNilCSLMEPWALGACTFVH-------------------LLPKFDPLVILKTLSSYPIKSMM 302
Cdd:PRK06710 232 -------VSNTLMGVQWLYN--CKEGEEVVLGVLPFFHvygmtavmnlsimqgykmvLIPKFDMKMVFEAIKKHKVTLFP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 303 GAPIVYRMLLQQDL-SSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG-LTCMVSKTMKIKPGYMGTAA 380
Cdd:PRK06710 303 GAPTIYIALLNSPLlKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 381 SCYDVQIID-DKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADDI 458
Cdd:PRK06710 383 PDTEAMIMSlETGEALPPGEIGEIVVKGPQI-----MKGYWNKPEETAAVLQ-DGWLhTGDVGYMDEDGFFYVKDRKKDM 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 459 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqfLSHDPEQLTKELQQHVKSVTAPYKYPRKIE 538
Cdd:PRK06710 457 IVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVV-----LKEGTECSEEELNQFARKYLAAYKVPKVYE 531
|
570 580
....*....|....*....|....
3C5E_A 539 FVLNLPKTVTGKIQRAKLRDKEWK 562
Cdd:PRK06710 532 FRDELPKTTVGKILRRVLIEEEKR 555
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
76-557 |
2.10e-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: 187.59 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 155
Cdd:cd05903 4 YSELDTRADRLAAGLA-ALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 viqevdtvasecpslrikllvsekscdgwlnFKKllneasttHHCVETGSQEAsAIYFTSGTSGLPKMAEHSYSSLGLKA 235
Cdd:cd05903 83 -------------------------------FRQ--------FDPAAMPDAVA-LLLFTSGTTGEPKGVMHSHNTLSASI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 236 KMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACtfVHLLPKFDPLVILKTLSSYPIKSMMGA-PIVYRMLLQQ 314
Cdd:cd05903 123 RQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAP--VVLQDIWDPDKALALMREHGVTFMMGAtPFLTDLLNAV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 315 DLSSYKFPHLQnCVTVGESLLPETLENwRAQT--GLDIRESYGQTETGltcmvSKTMKIKPGYMGtAASCYD-------- 384
Cdd:cd05903 201 EEAGEPLSRLR-TFVCGGATVPRSLAR-RAAEllGAKVCSAYGSTECP-----GAVTSITPAPED-RRLYTDgrplpgve 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 385 VQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGY 464
Cdd:cd05903 273 IKVVDDTGATLAPGVEGELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 465 RIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT-KELQQHVKSV-TAPYKYPRKIEFVLN 542
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVT------KSGALLTfDELVAYLDRQgVAKQYWPERLVHVDD 421
|
490
....*....|....*
3C5E_A 543 LPKTVTGKIQRAKLR 557
Cdd:cd05903 422 LPRTPSGKVQKFRLR 436
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
55-569 |
2.85e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 186.73 E-value: 2.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 55 KRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVI-----LGCIRAGLIFMpG 129
Cdd:PRK06188 24 RYPDRPALVLGDTR-----LTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMAIgaaqlAGLRRTALHPL-G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 130 TIQmkstDILYRLQMSKAKAIVAGDEVIQE-VDTVASECPSLRIKLLVSEksCDGWLNFKKLLNEASTTHHCVETGSQEA 208
Cdd:PRK06188 97 SLD----DHAYVLEDAGISTLIVDPAPFVErALALLARVPSLKHVLTLGP--VPDGVDLLAAAAKFGPAPLVAAALPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 209 SAIYFTSGTSGLPKMAEHSYSSLglkakmdAGWTGLQASDIMWT----------ISDTGWILnILCSLMEpwalGActFV 278
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSI-------ATMAQIQLAEWEWPadprflmctpLSHAGGAF-FLPTLLR----GG--TV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 279 HLLPKFDPLVILKTLSSYPIKSMMGAP-IVYRMLLQQDLSSYKFPHLQNCVTVGESLLPEtlenwRAQTGLDI-----RE 352
Cdd:PRK06188 237 IVLAKFDPAEVLRAIEEQRITATFLVPtMIYALLDHPDLRTRDLSSLETVYYGASPMSPV-----RLAEAIERfgpifAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 353 SYGQTETGLTCMVSKTMKIKPGYMGTAASC------YDVQIIDDKGNVLPPGTEGDIGIRvKPIrpigIFSGYVDNPDKT 426
Cdd:PRK06188 312 YYGQTEAPMVITYLRKRDHDPDDPKRLTSCgrptpgLRVALLDEDGREVAQGEVGEICVR-GPL----VMDGYWNRPEET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 427 AANIRGDfWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA 505
Cdd:PRK06188 387 AEAFRDG-WLhTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLR 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
3C5E_A 506 SQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWkmSGKARA 569
Cdd:PRK06188 466 PG-AAVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYW--EGRGRA 522
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
75-558 |
1.88e-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: 184.37 E-value: 1.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 75 NFRELSENSQQAANVLSGAcGLQRGDRVAVVL---PRVPEWWLVILGcirAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 151
Cdd:cd12119 27 TYAEVAERARRLANALRRL-GVKPGDRVATLAwntHRHLELYYAVPG---MGAVLHTINPRLFPEQIAYIINHAEDRVVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 152 AGDEVIQEVDTVASECPSLRIKLLVS------EKSCDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 225
Cdd:cd12119 103 VDRDFLPLLEAIAPRLPTVEHVVVMTddaampEPAGVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 226 HSYSSLGLKA--KMDAGWTGLQASDIMWTISD----TGWILNILCSLmepwaLGACtfvHLLP--KFDPLVILKTLSSYP 297
Cdd:cd12119 183 YSHRSLVLHAmaALLTDGLGLSESDVVLPVVPmfhvNAWGLPYAAAM-----VGAK---LVLPgpYLDPASLAELIEREG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 298 IKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSK--------- 367
Cdd:cd12119 255 VTFAAGVPTVWQGLLDhLEANGRDLSSLRR-VVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARppsehsnls 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 368 -----TMKIKPGYmgtaaSCYDVQ--IIDDKGNVLP--PGTEGDIGIRvKPIrpigIFSGYVDNPDKTAANIRGDFWLLG 438
Cdd:cd12119 334 edeqlALRAKQGR-----PVPGVElrIVDDDGRELPwdGKAVGELQVR-GPW----VTKSYYKNDEESEALTEDGWLRTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 439 DRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLT- 517
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLK------EGATVTa 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
3C5E_A 518 KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:cd12119 478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
71-558 |
2.87e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 184.59 E-value: 2.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 71 ELMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 150
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 151 VAGD--------EVIQEV--DTVASEC--------PSLRIKLLVSEKSCDGWLNFKKLLNEAST-THHCVETGSQ----- 206
Cdd:PRK12583 122 ICADafktsdyhAMLQELlpGLAEGQPgalacerlPELRGVVSLAPAPPPGFLAWHELQARGETvSREALAERQAsldrd 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 207 EASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDT----GWIL-NILCSlmepwALGACTfvhLL 281
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhcfGMVLaNLGCM-----TVGACL---VY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 282 PK--FDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGL-DIRESYGQT 357
Cdd:PRK12583 274 PNeaFDPLATLQAVEEERCTALYGVPTMFIAELDHpQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 358 ETG----LTCmVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD 433
Cdd:PRK12583 354 ETSpvslQTT-AADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTR-----GYSVMKGYWNNPEATAESIDED 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 434 FWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHD 512
Cdd:PRK12583 428 GWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRL------HP 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
3C5E_A 513 PEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK12583 502 GHAASeEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
46-559 |
7.15e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 183.44 E-value: 7.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 46 HWADM--EKAGKRPPSPALWWvngKGKELMWnfRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAG 123
Cdd:PRK07786 18 NWVNQlaRHALMQPDAPALRF---LGNTTTW--RELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 124 LIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVET 203
Cdd:PRK07786 92 AIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 204 GSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDA-GWTGLQASDI------MWTISDTGwilNILCSLMepwaLGACT 276
Cdd:PRK07786 172 PNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLrTNGADINSDVgfvgvpLFHIAGIG---SMLPGLL----LGAPT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 277 FVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLL------QQDLSsykfphLQNcVTVGESLLPETLENWRAQT--GL 348
Cdd:PRK07786 245 VIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCaeqqarPRDLA------LRV-LSWGAAPASDTLLRQMAATfpEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 349 DIRESYGQTE-TGLTCMVSKTMKI-KPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKT 426
Cdd:PRK07786 318 QILAAFGQTEmSPVTCMLLGEDAIrKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP-----TLMSGYWNNPEAT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 427 AANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAS 506
Cdd:PRK07786 393 AEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
3C5E_A 507 qflshDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 559
Cdd:PRK07786 473 -----DDAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
57-556 |
7.49e-51 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 180.80 E-value: 7.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 57 PPSPALWWVNGKgkelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkst 136
Cdd:cd05930 1 PDAVAVVDGDQS-----LTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVP-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 137 dilyrlqmskakaivagdeviqeVDTvasECPSLRIKLLVSEkscdgwlnfkkllneasTTHHCVETGSQEASAIYFTSG 216
Cdd:cd05930 67 -----------------------LDP---SYPAERLAYILED-----------------SGAKLVLTDPDDLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 217 TSGLPK--MAEH-SYSSLgLKAKMDAgwTGLQASDIMWTISDTGWILnilcSLME---PWALGACtfVHLLPK---FDPL 287
Cdd:cd05930 104 STGKPKgvMVEHrGLVNL-LLWMQEA--YPLTPGDRVLQFTSFSFDV----SVWEifgALLAGAT--LVVLPEevrKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 288 VILKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPHLQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTET--GLTCM 364
Cdd:cd05930 175 ALADLLAEEGITVLHLTPSLLRLLLQ-ELELAALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtvDATYY 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 365 VSKTMKIKPGYM--GTAASCYDVQIIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVDNPDKTAANIRGDFWLL-- 437
Cdd:cd05930 254 RVPPDDEEDGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELyigGA--------GLARGYLNRPELTAERFVPNPFGPge 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 438 -----GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflsHD 512
Cdd:cd05930 326 rmyrtGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPD-----EG 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....
3C5E_A 513 PEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd05930 401 GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
69-556 |
3.91e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 180.44 E-value: 3.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 69 GKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAK 148
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 149 AIVAGDE---VIQEVDTVASECPSLRIKLL--VSEKSCDGWlnfkkllneastthhcVETGSQEASAIYFTSGTSGLPKM 223
Cdd:PRK06839 103 VLFVEKTfqnMALSMQKVSYVQRVISITSLkeIEDRKIDNF----------------VEKNESASFIICYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 224 AEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHllPKFDPLVILKTLSSYPIKSMMG 303
Cdd:PRK06839 167 AVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVP--RKFEPTKALSMIEKHKVTVVMG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 304 APIVYRMLLQQ-DLSSYKFPHLQNCVTvGESLLPETLENWRAQTGLDIRESYGQTETGLTC-MVSKT-MKIKPGYMGTAA 380
Cdd:PRK06839 245 VPTIHQALINCsKFETTNLQSVRWFYN-GGAPCPEELMREFIDRGFLFGQGFGMTETSPTVfMLSEEdARRKVGSIGKPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 381 SCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIIN 460
Cdd:PRK06839 324 LFCDYELIDENKNKVEVGEVGELLIR-GP----NVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMII 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 461 SSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDpeqltKELQQHVKSVTAPYKYPRKIEFV 540
Cdd:PRK06839 399 SGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKIPKEIVFL 473
|
490
....*....|....*.
3C5E_A 541 LNLPKTVTGKIQRAKL 556
Cdd:PRK06839 474 KELPKNATGKIQKAQL 489
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
69-558 |
6.26e-50 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 180.99 E-value: 6.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 69 GKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMpgtiqmkSTDILY-------R 141
Cdd:PRK07059 46 GKAI--TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV-------NVNPLYtprelehQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 142 LQMSKAKAIV-------AGDEVIQEVDT----VASECPSL------------RIKLLVSEKSCDGWLNFKKLLNE-ASTT 197
Cdd:PRK07059 116 LKDSGAEAIVvlenfatTVQQVLAKTAVkhvvVASMGDLLgfkghivnfvvrRVKKMVPAWSLPGHVRFNDALAEgARQT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 198 HHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS-LGLKAKMDAgWtgLQASDIMWTISDTgwiLNILCSLmeP----WAL 272
Cdd:PRK07059 196 FKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNiVANVLQMEA-W--LQPAFEKKPRPDQ---LNFVCAL--PlyhiFAL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 273 GACTFVH--------LLPkfDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLE 340
Cdd:PRK07059 268 TVCGLLGmrtggrniLIP--NPRDIpgfIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 341 NWRAQTGLDIRESYGQTETG--LTCMVSKTMKIKpGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IF 416
Cdd:PRK07059 346 RWLEMTGCPITEGYGLSETSpvATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-------GpqVM 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 417 SGYVDNPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRG 495
Cdd:PRK07059 418 AGYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSG 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
3C5E_A 496 EVVKAFVVlasqflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK07059 498 EAVKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
95-557 |
8.22e-50 |
|
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: 178.40 E-value: 8.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 95 GLQRGDRVAVVLPRVPEWWLVILGCIRAG----LIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSL 170
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 171 RIKLLVsekscDGWLNfkkllNEASTTHHCVEtgSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIM 250
Cdd:cd05922 94 GTVLDA-----DGIRA-----ARASAPAHEVS--HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 251 WTISDTGWI--LNILCSLMEpwaLGACTFVHLLPKFDPLVIlKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCV 328
Cdd:cd05922 162 LTVLPLSYDygLSVLNTHLL---RGATLVLTNDGVLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 329 TVGESLLPETLENWR-AQTGLDIRESYGQTET--GLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGI 405
Cdd:cd05922 238 QAGGRLPQETIARLReLLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 406 RvkpiRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETA 485
Cdd:cd05922 318 R----GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3C5E_A 486 VISSPDPVrGEVVKAFVVLasqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd05922 394 AVGLPDPL-GEKLALFVTA-------PDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
55-553 |
1.13e-48 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 178.99 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 55 KRPPSPALWWVNGK-GKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLI-------F 126
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsvvfggF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 127 mpgtiqmKSTDILYRLQMSKAKAIV---AG-------------DEVIQE----------VDTVASECP----------SL 170
Cdd:PRK10524 144 -------ASHSLAARIDDAKPVLIVsadAGsrggkvvpykpllDEAIALaqhkprhvllVDRGLAPMArvagrdvdyaTL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 171 RIKLLVSEKSCDgWLNfkkllneastthhcvetgSQEASAIYFTSGTSGLPKMAEHS---YSsLGLKAKMDAGWTGlQAS 247
Cdd:PRK10524 217 RAQHLGARVPVE-WLE------------------SNEPSYILYTSGTTGKPKGVQRDtggYA-VALATSMDTIFGG-KAG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 248 DIMWTISDTGWILNILCSLMEPWALGACTFVH----LLPkfDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYK 320
Cdd:PRK10524 276 ETFFCASDIGWVVGHSYIVYAPLLAGMATIMYeglpTRP--DAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 321 FPHLQNCVTVGESLlPETLENWRAQT-GLDIRESYGQTETGLTCMVS----KTMKIKPGYMGTAASCYDVQIIDDK-GNV 394
Cdd:PRK10524 354 LSSLRALFLAGEPL-DEPTASWISEAlGVPVIDNYWQTETGWPILAIargvEDRPTRLGSPGVPMYGYNVKLLNEVtGEP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 395 LPPGTEGDIGIRvkPIRPIGIFSgyvdnpdktaaNIRGD-------FWLLGDR--------GIKDEDGYFQFMGRADDII 459
Cdd:PRK10524 433 CGPNEKGVLVIE--GPLPPGCMQ-----------TVWGDddrfvktYWSLFGRqvystfdwGIRDADGYYFILGRTDDVI 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 460 NSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQ---LTKELQQHVKSVTAPYKYPRK 536
Cdd:PRK10524 500 NVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPAR 579
|
570
....*....|....*..
3C5E_A 537 IEFVLNLPKTVTGKIQR 553
Cdd:PRK10524 580 VWFVSALPKTRSGKLLR 596
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
69-566 |
1.16e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 177.65 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 69 GKELmwNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAK 148
Cdd:PRK05677 47 GKTL--TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 149 AIVA-------GDEVIQE-------VDTVASECPSLR----------IKLLVSEKSCDGWLNFKKLLNE-ASTTHHCVET 203
Cdd:PRK05677 125 ALVClanmahlAEKVLPKtgvkhviVTEVADMLPPLKrllinavvkhVKKMVPAYHLPQAVKFNDALAKgAGQPVTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 204 GSQEASAIYFTSGTSGLPK--MAEHSysslGLKAKMdagwtgLQASDIMwtisdtGWILNILCS-LMEPWALG------- 273
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKgaMLTHR----NLVANM------LQCRALM------GSNLNEGCEiLIAPLPLYhiyaftf 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 274 ACTFVHLLPKFDPLV--------ILKTLSSYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENWRA 344
Cdd:PRK05677 269 HCMAMMLIGNHNILIsnprdlpaMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 345 QTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPD 424
Cdd:PRK05677 349 VTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GP----QVMKGYWQRPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 425 KTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVV 503
Cdd:PRK05677 424 ATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVV 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
3C5E_A 504 LASQflshdpEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGK 566
Cdd:PRK05677 504 VKPG------ETLTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAGL 561
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
57-557 |
6.02e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 174.43 E-value: 6.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 57 PPSPALWwVNGKGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKST 136
Cdd:PRK13390 11 PDRPAVI-VAETGEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 137 DILYRLQMSKAKAIVAGDEVIQEVDTVASECPsLRIKLlvsEKSCDGWLNFKKLLNEAS---TTHHCvetgsqeASAIYF 213
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLAAKVGADLP-LRLSF---GGEIDGFGSFEAALAGAGprlTEQPC-------GAVMLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 214 TSGTSGLPKMAEHSYSSLGLKAKMD------AGWTGLQASDIMWT------ISDTGWilnilCSLMEpwALGACtfVHLL 281
Cdd:PRK13390 156 SSGTTGFPKGIQPDLPGRDVDAPGDpivaiaRAFYDISESDIYYSsapiyhAAPLRW-----CSMVH--ALGGT--VVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 282 PKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESL---LPETLENWraqTGLDIRESYG 355
Cdd:PRK13390 227 KRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDadvRTRYDVSSLRAVIHAAAPCpvdVKHAMIDW---LGPIVYEYYS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 356 QTET-GLTCMVSKTMKIKPGYMGTAAsCYDVQIIDDKGNVLPPGTEGDIGIRvkpiRPIGIFSgYVDNPDKTAA--NIRG 432
Cdd:PRK13390 304 STEAhGMTFIDSPDWLAHPGSVGRSV-LGDLHICDDDGNELPAGRIGTVYFE----RDRLPFR-YLNDPEKTAAaqHPAH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 433 DFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsh 511
Cdd:PRK13390 378 PFWTtVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI--- 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
3C5E_A 512 DP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:PRK13390 455 RGsDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
46-556 |
1.15e-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: 173.57 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 46 HWADMEKAGKRPPSPALwwVNG-KGKELmwNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGL 124
Cdd:cd05904 8 DSVSFLFASAHPSRPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 125 IFMPGTIQMKSTDILYRLQMSKAKAIVAgdeviqeVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETG 204
Cdd:cd05904 83 VVTTANPLSTPAEIAKQVKDSGAKLAFT-------TAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 205 SQ-EASAIYFTSGTSGLPK--MAEHSysslGLKAkMDAGWTGLQASDI-----------MWTISDTGWILniLCSLmepw 270
Cdd:cd05904 156 KQdDVAALLYSSGTTGRSKgvMLTHR----NLIA-MVAQFVAGEGSNSdsedvflcvlpMFHIYGLSSFA--LGLL---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 271 ALGACTFVhlLPKFDPLVILKTLSSYPIKSMMGAP-IVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQ-TGL 348
Cdd:cd05904 225 RLGATVVV--MPRFDLEELLAAIERYKVTHLPVVPpIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 349 DIRESYGQTETG---LTCMVSKTMKIKPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPD 424
Cdd:cd05904 303 DLGQGYGMTESTgvvAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGYLNNPE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 425 KTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVV 503
Cdd:cd05904 378 ATAATIDKEGWLhTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVV 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
3C5E_A 504 LASQ-FLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd05904 458 RKPGsSLTED------EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
260-553 |
5.51e-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: 167.45 E-value: 5.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 260 LNILCSLMEpwaLGACTFVhlLPKFDPLVILKTLSSYPIkSMMG--APIVYRMLLQQDLSSYKFPHLQNcvtVGESLLPE 337
Cdd:cd17637 56 LNLALATFH---AGGANVV--MEKFDPAEALELIEEEKV-TLMGsfPPILSNLLDAAEKSGVDLSSLRH---VLGLDAPE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 338 TLENWRAQTGLDIRESYGQTET-GLTCMVSKTMKikPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIF 416
Cdd:cd17637 127 TIQRFEETTGATFWSLYGQTETsGLVTLSPYRER--PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR-GP----LVF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 417 SGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGR--ADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 494
Cdd:cd17637 200 QGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKW 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 495 GEVVKAFVVL-ASQFLShdpeqlTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:cd17637 280 GEGIKAVCVLkPGATLT------ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
76-560 |
1.16e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 171.65 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLsGACGLQRGDRVAVvLPRVPEWWLV-ILGCIRAGL-IFMPGT----IQMKstDILYRLqmsKAKA 149
Cdd:PRK07788 77 YAELDEQSNALARGL-LALGVRAGDGVAV-LARNHRGFVLaLYAAGKVGArIILLNTgfsgPQLA--EVAARE---GVKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 150 IVAGDEVIQEVDTVASECPSLRIKLLVSEK---SCDGWLNFKKLLneASTTHHCVETGSQEASAIYFTSGTSGLPKMAEH 226
Cdd:PRK07788 150 LVYDDEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLI--AGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 227 ----SYSSLG-------LKAKMdagwTGLQASDIMWTisdTGW-ILNIlcslmePWALGaCTFVhLLPKFDPLVILKTLS 294
Cdd:PRK07788 228 pepsPLAPLAgllsrvpFRAGE----TTLLPAPMFHA---TGWaHLTL------AMALG-STVV-LRRRFDPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 295 SYPIKSMMGAPIVYRMLLQQ--------DLSSYKFphlqnCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS 366
Cdd:PRK07788 293 KHKATALVVVPVMLSRILDLgpevlakyDTSSLKI-----IFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIAT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 367 -KTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVkpirpiGI-FSGYVDNPDKtaANIRGdfwLL--GDRGI 442
Cdd:PRK07788 368 pEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGN------GFpFEGYTDGRDK--QIIDG---LLssGDVGY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 443 KDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKE-LQ 521
Cdd:PRK07788 437 FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKA------PGAALDEDaIK 510
|
490 500 510
....*....|....*....|....*....|....*....
3C5E_A 522 QHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKE 560
Cdd:PRK07788 511 DYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
50-563 |
4.84e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 165.91 E-value: 4.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 50 MEKAGKRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGC--IRAGLIFM 127
Cdd:PRK03640 9 KQRAFLTPDRTAIEFEEKK-----VTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALqqLGAVAVLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 128 PGTIQMKstDILYRLQMSKAKAIVAGDEVIQEVDTVA----SECPSLRIKLLVSEKSCDgwlnfkklLNEASTthhcvet 203
Cdd:PRK03640 83 NTRLSRE--ELLWQLDDAEVKCLITDDDFEAKLIPGIsvkfAELMNGPKEEAEIQEEFD--------LDEVAT------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 204 gsqeasaIYFTSGTSGLPKMAEHSY---------SSLGLkakmdagwtGLQASDiMWTISDTgwILNI--LCSLMEPWAL 272
Cdd:PRK03640 146 -------IMYTSGTTGKPKGVIQTYgnhwwsavgSALNL---------GLTEDD-CWLAAVP--IFHIsgLSILMRSVIY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 273 GaCTfVHLLPKFDPLVILKTLSSYPIkSMMGApiVYRML--LQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDI 350
Cdd:PRK03640 207 G-MR-VVLVEKFDAEKINKLLQTGGV-TIISV--VSTMLqrLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 351 RESYGQTETGltcmvSKTMKIKPGYM----GTAAS-CYDVQI-IDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVDNPD 424
Cdd:PRK03640 282 YQSYGMTETA-----SQIVTLSPEDAltklGSAGKpLFPCELkIEKDGVVVPPFEEGEIVVKGPNVTK-----GYLNRED 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 425 KTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVV 503
Cdd:PRK03640 352 ATRETFQ-DGWFkTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 504 LASQFlshdPEQltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKM 563
Cdd:PRK03640 431 KSGEV----TEE---ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
93-557 |
5.16e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 165.55 E-value: 5.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 93 ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgdeviqEVDTVASECPSLRI 172
Cdd:PRK07787 39 AERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLG------PAPDDPAGLPHVPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 173 KLlvsekscdgwlnfkkllnEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL--GLKAKMDAgWTglqasdim 250
Cdd:PRK07787 113 RL------------------HARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIaaDLDALAEA-WQ-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 251 WTISDT-----------GWILNILCSLMepwaLGAcTFVHLLpKFDPLVILKTLSSYpiKSMM-GAPIVYRMLLQQDLSS 318
Cdd:PRK07787 166 WTADDVlvhglplfhvhGLVLGVLGPLR----IGN-RFVHTG-RPTPEAYAQALSEG--GTLYfGVPTVWSRIAADPEAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 319 YKFPHLQNCVTvGESLLPET-LENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPP 397
Cdd:PRK07787 238 RALRGARLLVS-GSAALPVPvFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 398 GTE--GDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR-ADDIINSSGYRIGPSEVEN 473
Cdd:PRK07787 317 DGEtvGELQVR-GP----TLFDGYLNRPDATAAAFTADGWFrTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 474 ALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflSHDPEQLTkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:PRK07787 392 ALLGHPGVREAAVVGVPDDDLGQRIVAYVV------GADDVAAD-ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLK 464
|
....
3C5E_A 554 AKLR 557
Cdd:PRK07787 465 KQLL 468
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
41-558 |
6.36e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 167.48 E-value: 6.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 41 SDVLDhwadmEKAGKRPPSPALWWVngkGKELMWnfRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCI 120
Cdd:PRK05605 35 VDLYD-----NAVARFGDRPALDFF---GATTTY--AELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 121 RAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV---IQE------VDTVAS-----------------ECPSLRIKL 174
Cdd:PRK05605 104 RLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVaptVERlrrttpLETIVSvnmiaampllqrlalrlPIPALRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 175 LVSEKSCDGWLNFKKLLNEA----STTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWT-GLQASD- 248
Cdd:PRK05605 184 AALTGPAPGTVPWETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVpGLGDGPe 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 249 IMWTI----SDTGWILNILCSLMepwaLGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ------DLSS 318
Cdd:PRK05605 264 RVLAAlpmfHAYGLTLCLTLAVS----IGG-ELV-LLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvDLSG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 319 ykfphLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCM---VSKTMKikPGYMGTAASCYDVQIID--DKGN 393
Cdd:PRK05605 338 -----VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVgnpMSDDRR--PGYVGVPFPDTEVRIVDpeDPDE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 394 VLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEV 471
Cdd:PRK05605 411 TMPDGEEGELLVR-------GpqVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 472 ENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKI 551
Cdd:PRK05605 484 EEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPE----GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
....*..
3C5E_A 552 QRAKLRD 558
Cdd:PRK05605 559 RRREVRE 565
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
95-558 |
7.78e-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: 7.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 95 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLR-IK 173
Cdd:cd17642 65 GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKtII 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 174 LLVSEKSCDGWL---NFKK-----LLNEASTTHHCVETGSQeASAIYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQ 245
Cdd:cd17642 145 ILDSKEDYKGYQclyTFITqnlppGFNEYDFKPPSFDRDEQ-VALIMNSSGSTGLPKGVQLTHKNI--VARFSHARDPIF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 246 ASDIMWTISdtgwILNILcslmePWALG----------ACTF-VHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ 314
Cdd:cd17642 222 GNQIIPDTA----ILTVI-----PFHHGfgmfttlgylICGFrVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 315 DL-SSYKFPHLQNCVTVGESLLPETLENWRAQTGLD-IRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIID-DK 391
Cdd:cd17642 293 TLvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDT 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 392 GNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSE 470
Cdd:cd17642 373 GKTLGPNERGELCVKGP-----MIMKGYVNNPEATKALIDKDGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 471 VENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLT-KELQQHVKSVTAPYKYPR-KIEFVLNLPKTVT 548
Cdd:cd17642 448 LESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAG------KTMTeKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLT 521
|
490
....*....|
3C5E_A 549 GKIQRAKLRD 558
Cdd:cd17642 522 GKIDRRKIRE 531
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
32-567 |
8.35e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 166.77 E-value: 8.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 32 EVPAKFNfaSDVLDHWADM-EKAGKR-PPSPAlwWVNgKGKELmwNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRV 109
Cdd:PRK08974 12 DVPAEIN--PDRYQSLVDMfEQAVARyADQPA--FIN-MGEVM--TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 110 PEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECP------------------SL- 170
Cdd:PRK08974 85 LQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPvkhviltrmgdqlstakgTLv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 171 -----RIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEASA-IYFTSGTSGLPK--MAEH------------SYSS 230
Cdd:PRK08974 165 nfvvkYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAfLQYTGGTTGVAKgaMLTHrnmlanleqakaAYGP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 231 LgLKAKMDAGWTGLQASDImwtisdtgWILNILCSL-MEpwaLGACTFVHLLPKFDPLVIlKTLSSYPIKSMMGAPIVYR 309
Cdd:PRK08974 245 L-LHPGKELVVTALPLYHI--------FALTVNCLLfIE---LGGQNLLITNPRDIPGFV-KELKKYPFTAITGVNTLFN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 310 MLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQI 387
Cdd:PRK08974 312 ALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 388 IDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGY 464
Cdd:PRK08974 392 VDDDGNEVPPGEPGELWVK-------GpqVMLGYWQRPEATDEVIK-DGWLaTGDIAVMDEEGFLRIVDRKKDMILVSGF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 465 RIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLP 544
Cdd:PRK08974 464 NVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEE------ELITHCRRHLTGYKVPKLVEFRDELP 537
|
570 580
....*....|....*....|...
3C5E_A 545 KTVTGKIQRAKLRDKEWKMSGKA 567
Cdd:PRK08974 538 KSNVGKILRRELRDEARAKVDNK 560
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
74-570 |
1.06e-44 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 166.52 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMpgTIQ--MKSTDILYRLQMSKAKAIV 151
Cdd:PRK08315 44 WTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV--TINpaYRLSELEYALNQSGCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 152 AGDEV-----IQEVDTVASEC-------------PSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHcVETGSQEASA--- 210
Cdd:PRK08315 121 AADGFkdsdyVAMLYELAPELatcepgqlqsarlPELRRVIFLGDEKHPGMLNFDELLALGRAVDD-AELAARQATLdpd 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 ----IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASD---I---------MwtisdtgwILNILCSLmepwALGA 274
Cdd:PRK08315 200 dpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrlcIpvplyhcfgM--------VLGNLACV----THGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 275 CTfVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCVTVGeSLLP-ETLEnwRAQTGLDIRE 352
Cdd:PRK08315 268 TM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLRTGIMAG-SPCPiEVMK--RVIDKMHMSE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 353 ---SYGQTETG-LTCM----------VSKTMKIKPGYmgtaascyDVQIID-DKGNVLPPGTEGDIGIRvkpirpiG--I 415
Cdd:PRK08315 344 vtiAYGMTETSpVSTQtrtddplekrVTTVGRALPHL--------EVKIVDpETGETVPRGEQGELCTR-------GysV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 416 FSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 494
Cdd:PRK08315 409 MKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKY 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3C5E_A 495 GEVVKAFVVLasqflsHDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKARAQ 570
Cdd:PRK08315 489 GEEVCAWIIL------RPGATLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGLQAAK 559
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
74-558 |
2.13e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 164.21 E-value: 2.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGAcGLQRGDRVAVvLPRVPEWWLVI-LGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVa 152
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRRR-GCVDGERLAV-LARNSVWLVALhFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 153 GDEVIQevdtvASECPSLRIKLLVSEKSCDGWLNFKKLLNEAstthhcvetgsqeASAIYFTSGTSGLPKMA-------E 225
Cdd:PRK09088 100 GDDAVA-----AGRTDVEDLAAFIASADALEPADTPSIPPER-------------VSLILFTSGTSGQPKGVmlsernlQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 226 HSYSSLGLKAKMDAGWTGLQASDIMWTIsdtGWILNILCSLMEpwalGACTFVHllPKFDPLVILKTLS--SYPIKSMMG 303
Cdd:PRK09088 162 QTAHNFGVLGRVDAHSSFLCDAPMFHII---GLITSVRPVLAV----GGSILVS--NGFEPKRTLGRLGdpALGITHYFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 304 APIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQtGLDIRESYGQTETGLTCMVSKTMKI---KPGYMGTA 379
Cdd:PRK09088 233 VPQMAQAFRAQpGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDViraKAGAAGIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 380 ASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDI 458
Cdd:PRK09088 312 TPTVQTRVVDDQGNDCPAGVPGELLLRGP-----NLSPGYWRRPQATARAFTGDGWFrTGDIARRDADGFFWVVDRKKDM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 459 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIE 538
Cdd:PRK09088 387 FISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-APLDLE----RIRSHLSTRLAKYKVPKHLR 461
|
490 500
....*....|....*....|
3C5E_A 539 FVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK09088 462 LVDALPRTASGKLQKARLRD 481
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
76-558 |
2.28e-44 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 165.82 E-value: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 155
Cdd:PRK08751 53 YREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 VIQEVDTVASECPSLR------------------------IKLLVSEKSCDGWLNFKKLLneASTTHHCVETGSQEASAI 211
Cdd:PRK08751 133 FGTTVQQVIADTPVKQvittglgdmlgfpkaalvnfvvkyVKKLVPEYRINGAIRFREAL--ALGRKHSMPTLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 212 YF---TSGTSGLPKMAEHSYSSLGLKAKMDAGWTG-----LQASDIMWTISDTGWILNILCSLMEPWALGACTfvHLL-- 281
Cdd:PRK08751 211 AFlqyTGGTTGVAKGAMLTHRNLVANMQQAHQWLAgtgklEEGCEVVITALPLYHIFALTANGLVFMKIGGCN--HLIsn 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 282 PKFDPLVIlKTLSSYPIKSMMGAPIVYRMLL------QQDLSSYKFPhLQNCVTVGESLlpetLENWRAQTGLDIRESYG 355
Cdd:PRK08751 289 PRDMPGFV-KELKKTRFTAFTGVNTLFNGLLntpgfdQIDFSSLKMT-LGGGMAVQRSV----AERWKQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 356 QTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPirpigIFSGYVDNPDKTAANIRGDF 434
Cdd:PRK08751 363 LTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQ-----VMKGYWKRPEETAKVMDADG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 435 WL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflSHDP 513
Cdd:PRK08751 438 WLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------KKDP 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
3C5E_A 514 EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK08751 512 ALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
74-558 |
3.08e-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: 162.13 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKaivag 153
Cdd:cd05912 2 YTFAELFEEVSRLAEHL-AALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 deviqeVDTVASecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasaIYFTSGTSGLPKMAE-----HSY 228
Cdd:cd05912 76 ------LDDIAT---------------------------------------------IMYTSGTTGKPKGVQqtfgnHWW 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 229 SSLGLKAKMdagwtGLQASDI------MWTISDtgwiLNILC-SLMEpwalgACTfVHLLPKFDPLVILKTLSSYPIKSM 301
Cdd:cd05912 105 SAIGSALNL-----GLTEDDNwlcalpLFHISG----LSILMrSVIY-----GMT-VYLVDKFDAEQVLHLINSGKVTII 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 302 MGAPIVYRMLLQQDLSSYKfPHLQnCVTVGESLLPETLENWRAQTGLDIRESYGQTETgltCMVSKTMKI-----KPGYM 376
Cdd:cd05912 170 SVVPTMLQRLLEILGEGYP-NNLR-CILLGGGPAPKPLLEQCKEKGIPVYQSYGMTET---CSQIVTLSPedalnKIGSA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 377 GTAASCYDVQIIDDKGnvlPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRAD 456
Cdd:cd05912 245 GKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTK-----GYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 457 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDPEQLTKELQQHVksvtAPYKYPRK 536
Cdd:cd05912 317 DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKL----AKYKVPKK 389
|
490 500
....*....|....*....|..
3C5E_A 537 IEFVLNLPKTVTGKIQRAKLRD 558
Cdd:cd05912 390 IYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
76-558 |
4.67e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 164.99 E-value: 4.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD- 154
Cdd:PRK12492 52 YAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNm 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 155 --EVIQEVdtvaseCPSLRIKLLVSEKSCD------GWL---------------------NFKKLLNE-ASTTHHCVETG 204
Cdd:PRK12492 132 fgKLVQEV------LPDTGIEYLIEAKMGDllpaakGWLvntvvdkvkkmvpayhlpqavPFKQALRQgRGLSLKPVPVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 205 SQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGA---CTFV--- 278
Cdd:PRK12492 206 LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEGQEVMIAPLPLYHIYAFTAncmCMMVsgn 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 279 HLLPKFDPLVI---LKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESY 354
Cdd:PRK12492 286 HNVLITNPRDIpgfIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 355 GQTETG-LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGD 433
Cdd:PRK12492 366 GLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK-GP----QVMKGYWQQPEATAEALDAE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 434 FWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHD 512
Cdd:PRK12492 441 GWFkTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVE 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
3C5E_A 513 peqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK12492 521 ------ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
41-557 |
1.41e-43 |
|
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: 163.01 E-value: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 41 SDVLDHWADmekagKRPPSPALwwVNGKGKelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCI 120
Cdd:COG1021 28 GDLLRRRAE-----RHPDRIAV--VDGERR---LSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 121 RAGLI---FMPGtiqMKSTDILYRLQMSKAKAIVAGDEV-----IQEVDTVASECPSLRIKLLVSEKscDGWLNFKKLLN 192
Cdd:COG1021 97 RAGAIpvfALPA---HRRAEISHFAEQSEAVAYIIPDRHrgfdyRALARELQAEVPSLRHVLVVGDA--GEFTSLDALLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 193 EASTtHHCVETGSQEASAIYFTSGTSGLPKM-----AEHSYSslglkAKMDAGWTGLQASDIMwtisdtgwilniLCSL- 266
Cdd:COG1021 172 APAD-LSEPRPDPDDVAFFQLSGGTTGLPKLiprthDDYLYS-----VRASAEICGLDADTVY------------LAALp 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 267 ------------MEPWALGACtfVHLLPKFDPLVILK-------TLSSypiksmMGAPIVYRML-----LQQDLSSYKFp 322
Cdd:COG1021 234 aahnfplsspgvLGVLYAGGT--VVLAPDPSPDTAFPlierervTVTA------LVPPLALLWLdaaerSRYDLSSLRV- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 323 hLQncvtVGESLLPETLENwRAQTGLDIR--ESYGQTEtGLTCM---------VSKTMkikpgymGTAASCYD-VQIIDD 390
Cdd:COG1021 305 -LQ----VGGAKLSPELAR-RVRPALGCTlqQVFGMAE-GLVNYtrlddpeevILTTQ-------GRPISPDDeVRIVDE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 391 KGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIG 467
Cdd:COG1021 371 DGNPVPPGEVGELLTR-------GpyTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 468 PSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflshDPEQLT-KELQQHVKSV-TAPYKYPRKIEFVLNLPK 545
Cdd:COG1021 444 AEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-------RGEPLTlAELRRFLRERgLAAFKLPDRLEFVDALPL 516
|
570
....*....|..
3C5E_A 546 TVTGKIQRAKLR 557
Cdd:COG1021 517 TAVGKIDKKALR 528
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
50-559 |
2.09e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 162.52 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 50 MEKAGKRPPS-PALWWvngkgKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMP 128
Cdd:PRK07470 13 LRQAARRFPDrIALVW-----GDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 129 GTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRikLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEA 208
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLT--HVVAIGGARAGLDYEALVARHLGARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 209 SAIYF-TSGTSGLPKMAEHSYSSLGL-----KAKMDAGWTGLQASDIMWTISDtGWILNILCSLmepwALGACTFVHLLP 282
Cdd:PRK07470 165 PCWFFfTSGTTGRPKAAVLTHGQMAFvitnhLADLMPGTTEQDASLVVAPLSH-GAGIHQLCQV----ARGAATVLLPSE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 283 KFDPLVILKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPH--LQNCVTVGESLLPETLENWRAQTGLDIRESYGQTEtg 360
Cdd:PRK07470 240 RFDPAEVWALVERHRVTNLFTVPTILKMLVE-HPAVDRYDHssLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGE-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 361 ltcmVSKTMKIKPGYM-----GTAA---SC------YDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKT 426
Cdd:PRK07470 317 ----VTGNITVLPPALhdaedGPDArigTCgfertgMEVQIQDDEGRELPPGETGEICVIGPAV-----FAGYYNNPEAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 427 AANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLas 506
Cdd:PRK07470 388 AKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA-- 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
3C5E_A 507 qflsHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 559
Cdd:PRK07470 466 ----RDGAPVDEaELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
211-557 |
2.27e-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: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIM------WTISdtGWILNILCSLMEpwalgACTFVHLLPKF 284
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplFHCF--GSVLGVLACLTH-----GATMVFPSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 285 DPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGL-DIRESYGQTETGLT 362
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 363 CMVSKT---MKIKPGYMGTAASCYDVQIIDDKGNVLPP-GTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGDFWL-L 437
Cdd:cd05917 160 STQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTAEAIDGDGWLhT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 438 GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLT 517
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL------KEGAELT 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
3C5E_A 518 KE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd05917 309 EEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
53-562 |
3.56e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 161.40 E-value: 3.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 53 AGKRPPSPALWwVNGKGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVL---PRVPEwwlVILGCIRAGLIFMPG 129
Cdd:PRK13391 7 AQTTPDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 130 TIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLV-SEKSCDGWLNFKKLLNEASTTHHCVETgsqEA 208
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPATPIADES---LG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 209 SAIYFTSGTSGLPKMAEHSYSSLGLKAKMdaGWTGLQASdiMWTI-SDTGWilniLC-----------SLMEPWALGACT 276
Cdd:PRK13391 157 TDMLYSSGTTGRPKGIKRPLPEQPPDTPL--PLTAFLQR--LWGFrSDMVY----LSpaplyhsapqrAVMLVIRLGGTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 277 FVhlLPKFDPLVILKTLSSYPIKSMMGAPIVY-RML-------LQQDLSSykfphLQNCVTVGESLLPETLENWRAQTGL 348
Cdd:PRK13391 229 IV--MEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLklpeevrDKYDLSS-----LEVAIHAAAPCPPQVKEQMIDWWGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 349 DIRESYGQTE-TGLTCMVSKTMKIKPGYMGTAASCyDVQIIDDKGNVLPPGTEGDIGIRVKpiRPigiFSgYVDNPDKTA 427
Cdd:PRK13391 302 IIHEYYAATEgLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGG--RP---FE-YLNDPAKTA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 428 A--NIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA 505
Cdd:PRK13391 375 EarHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPV 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
3C5E_A 506 SQFlshDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK 562
Cdd:PRK13391 455 DGV---DPgPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
46-558 |
3.99e-43 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 161.76 E-value: 3.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 46 HWAD-------MEKAGKRPPSPALWWVN-GKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVIL 117
Cdd:PRK13295 20 HWHDrtinddlDACVASCPDKTAVTAVRlGTGAPRRFTYRELAALVDRVAVGLA-RLGVGRGDVVSCQLPNWWEFTVLYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 118 GCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA-----GDEVIQEVDTVASECPSLRIKLLVSEkscDGWLNFKKLLN 192
Cdd:PRK13295 99 ACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLRPELPALRHVVVVGG---DGADSFEALLI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 193 E--------ASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILC 264
Cdd:PRK13295 176 TpaweqepdAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 265 SLMEPWALGAcTFVhLLPKFDPLVILKTLSSYPIKSMMGA-PIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWR 343
Cdd:PRK13295 256 GLMMPVMLGA-TAV-LQDIWDPARAAELIRTEGVTFTMAStPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERAR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 344 AQTGLDIRESYGQTETGLTCMvsktmkIKPGYMGTAASCYD--------VQIIDDKGNVLPPGTEGdigiRVKpIRPIGI 415
Cdd:PRK13295 334 AALGAKIVSAWGMTENGAVTL------TKLDDPDERASTTDgcplpgveVRVVDADGAPLPAGQIG----RLQ-VRGCSN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 416 FSGYVDNPDKTAANIRGdfWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 494
Cdd:PRK13295 403 FGGYLKRPQLNGTDADG--WFdTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
3C5E_A 495 GEVVKAFVVL-ASQflSHDPEQLTKELQQHvkSVTAPYkYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK13295 481 GERACAFVVPrPGQ--SLDFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
77-567 |
1.23e-42 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 159.86 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 77 RELSENSQQAANVLSG--ACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 154
Cdd:PRK12406 12 RSFDELAQRAARAAGGlaALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 155 EVIQEV-DTVASEC--------PSLRIKLLVSEKSC---------DGWLNfkklLNEASTThhcvETGSQEASAIYfTSG 216
Cdd:PRK12406 92 DLLHGLaSALPAGVtvlsvptpPEIAAAYRISPALLtppagaidwEGWLA----QQEPYDG----PPVPQPQSMIY-TSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 217 TSGLPKmaehsysslglKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEP--------WALGACTFVH---LLPKFD 285
Cdd:PRK12406 163 TTGHPK-----------GVRRAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPlyhsapnaYGLRAGRLGGvlvLQPRFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 286 PLVILKTLSSYPIKSMMGAPIVYRMLLQ--------QDLSSYKFphlqncVTVGESLLP-----ETLENWraqtGLDIRE 352
Cdd:PRK12406 232 PEELLQLIERHRITHMHMVPTMFIRLLKlpeevrakYDVSSLRH------VIHAAAPCPadvkrAMIEWW----GPVIYE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 353 SYGQTETGL--TCMVSKTMKiKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpIRPIGIFSgYVDNPDKTAANI 430
Cdd:PRK12406 302 YYGSTESGAvtFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSR---IAGNPDFT-YHNKPEKRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 431 RGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVvlasqfls 510
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV-------- 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
3C5E_A 511 hDPEQL----TKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWKMSGKA 567
Cdd:PRK12406 449 -EPQPGatldEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
77-486 |
6.25e-42 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 155.89 E-value: 6.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 77 RELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILY---RLQM----SKAKA 149
Cdd:TIGR01733 3 RELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP-------LDPAYpaeRLAFiledAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 150 IVAGDEVIQEVDTVASECPSLRIKLLVSEKSCdgwlnfkkllneASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYS 229
Cdd:TIGR01733 76 LLTDSALASRLAGLVLPVILLDPLELAALDDA------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 230 SLglkAKMdAGWT----GLQASDIMW---TIS-DTgwilnilcSLME---PWALGACTFVHL--LPKFDPLVILKTLSSY 296
Cdd:TIGR01733 144 SL---VNL-LAWLarryGLDPDDRVLqfaSLSfDA--------SVEEifgALLAGATLVVPPedEERDDAALLAALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 297 PIKSMMGAPIVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENWRAQTGlDIR--ESYGQTETGLTCMVSKTMKIKPG 374
Cdd:TIGR01733 212 PVTVLNLTPSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGP-GARliNLYGPTETTVWSTATLVDPDDAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 375 YM-----GTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAAN-IRGDFWLL--------GDR 440
Cdd:TIGR01733 289 REspvpiGRPLANTRLYVLDDDLRPVPVGVVGELYIG-----GPGVARGYLNRPELTAERfVPDPFAGGdgarlyrtGDL 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
3C5E_A 441 GIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAV 486
Cdd:TIGR01733 364 VRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
65-559 |
1.73e-40 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 154.37 E-value: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 65 VNGKGkelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQM 144
Cdd:PLN02330 51 VTGKA----VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 145 SKAKAIVAGDEVIQEVDtvasecpSLRIKLLV-SEKSCDGWLNFKKLLN---EASTTHHCVETGSQEASAIYFTSGTSGL 220
Cdd:PLN02330 126 AGAKLIVTNDTNYGKVK-------GLGLPVIVlGEEKIEGAVNWKELLEaadRAGDTSDNEEILQTDLCALPFSSGTTGI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 221 PK--MAEHSysslGLKAKMDAGWTGLqASDIMWTISDTGWI--------LNILCSLMEPWALgactfVHLLPKFDPLVIL 290
Cdd:PLN02330 199 SKgvMLTHR----NLVANLCSSLFSV-GPEMIGQVVTLGLIpffhiygiTGICCATLRNKGK-----VVVMSRFELRTFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 291 KTLSSYPIKSmmgAPIVYRMLL---------QQDLSSYKfphLQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTETG 360
Cdd:PLN02330 269 NALITQEVSF---APIVPPIILnlvknpiveEFDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 361 LTCMV----SKTMKI-KPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDF 434
Cdd:PLN02330 343 CITLThgdpEKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYNNKEETDRTIDEDG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 435 WL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqfLSHDP 513
Cdd:PLN02330 418 WLhTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVV-----INPKA 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
3C5E_A 514 EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 559
Cdd:PLN02330 493 KESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
53-556 |
2.25e-40 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 152.40 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 53 AGKRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiq 132
Cdd:cd05945 1 AAANPDRPAVVEGGRT-----LTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 133 mksTDILY---RLQMskAKAIVAGDEVIQEVDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeas 209
Cdd:cd05945 71 ---LDASSpaeRIRE--ILDAAKPALLIADGDDNA--------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 210 AIYFTSGTSGLPKMAEHSYSSLglkakmdagwtglqASDIMWTISDTGWI----------LNILCSLME---PWALGACt 276
Cdd:cd05945 101 YIIFTSGSTGRPKGVQISHDNL--------------VSFTNWMLSDFPLGpgdvflnqapFSFDLSVMDlypALASGAT- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 277 fVHLLPK---FDPLVILKTLSSYPIKSMMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENWRAQT-GLDIR 351
Cdd:cd05945 166 -LVPVPRdatADPKQLFRFLAEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIY 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 352 ESYGQTETGLTCMVSK-TMKIKPGY----MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPD 424
Cdd:cd05945 245 NTYGPTEATVAVTYIEvTPEVLDGYdrlpIGYAKPGAKLVILDEDGRPVPPGEKGELVIS-------GpsVSKGYLNNPE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 425 KTA-ANIRGDFWLL---GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVIssPDPVRGEVVK- 499
Cdd:cd05945 318 KTAaAFFPDEGQRAyrtGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVV--PKYKGEKVTEl 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
3C5E_A 500 -AFVVLAsqflSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd05945 396 iAFVVPK----PGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
207-553 |
2.49e-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: 149.19 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 207 EASAIYFTSGTSGLPK--MAEHSYSSLGLKAKMDAGwtGLQASDIMWTIS----DTGWILNILCSLMEpwalGACTFVHL 280
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQTLRAAAAWADCA--DLTEDDRYLIINpffhTFGYKAGIVACLLT----GATVVPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 281 LpkFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLD-IRESYGQTE 358
Cdd:cd17638 75 V--FDVDAILEAIERERITVLPGPPTLFQSLLDHpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 359 TGLTCM---------VSKTMkikpgymGTAASCYDVQIIDDkGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAAN 429
Cdd:cd17638 153 AGVATMcrpgddaetVATTC-------GRACPGFEVRIADD-GEVL--------------VRGYNVMQGYLDDPEATAEA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 430 IRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqf 508
Cdd:cd17638 211 IDADGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR--- 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
3C5E_A 509 lshDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:cd17638 288 ---PGVTLTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
30-558 |
3.77e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 150.66 E-value: 3.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 30 HQEVPAKFNFASdVLDhwadmEKAGKRPPSPALwwvngKGKELMWNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRV 109
Cdd:PRK06164 3 HDAAPRADTLAS-LLD-----AHARARPDAVAL-----IDEDRPLSRAELRALVDRLAAWL-AAQGVRRGDRVAVWLPNC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 110 PEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD--------EVIQEVDTvaSECPSLRIKLLVSEKSC 181
Cdd:PRK06164 71 IEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPgfkgidfaAILAAVPP--DALPPLRAIAVVDDAAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 182 D-------GWLNFKKLLNEASTTHHCVETGSQEASAIYFT-SGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMwti 253
Cdd:PRK06164 149 AtpapapgARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVL--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 254 sdtgwilniLCSLmePW-----------ALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFP 322
Cdd:PRK06164 226 ---------LAAL--PFcgvfgfstllgALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 323 HLQNCvtvG-ESLLP--ETLENWRAQTGLDIRESYGQTEtgLTCMVS-------KTMKIKPGymGTAASC-YDVQIID-D 390
Cdd:PRK06164 295 SARLF---GfASFAPalGELAALARARGVPLTGLYGSSE--VQALVAlqpatdpVSVRIEGG--GRPASPeARVRARDpQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 391 KGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPS 469
Cdd:PRK06164 368 DGALLPDGESGEIEIRAP-----SLMRGYLDNPDATARALTDDGYFrTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 470 EVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 549
Cdd:PRK06164 443 EIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDG-ASPDEA----GLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
570
....*....|..
3C5E_A 550 ---KIQRAKLRD 558
Cdd:PRK06164 517 ngaKIQKHRLRE 528
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
46-556 |
1.12e-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: 148.24 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 46 HWAD-------MEKAGKRPPSPALwwVNGKGKelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILG 118
Cdd:cd05920 11 YWQDeplgdllARSAARHPDRIAV--VDGDRR---LTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 119 CIRAGLI---FMPGtiqMKSTDILYRLQMSKAKAIVAGDEvIQEVD------TVASECPSLRIKLLvsekscdgwlnfkk 189
Cdd:cd05920 85 LLRLGAVpvlALPS---HRRSELSAFCAHAEAVAYIVPDR-HAGFDhralarELAESIPEVALFLL-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 190 llneastthhcvetgsqeasaiyfTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCslmeP 269
Cdd:cd05920 147 ------------------------SGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAC----P 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 270 WALGACTF---VHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ------DLSSYKFphLQncvtVGESLLPETL- 339
Cdd:cd05920 199 GVLGTLLAggrVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAaasrraDLSSLRL--LQ----VGGARLSPALa 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 340 ENWRAQTGLDIRESYGQTEtGLTCM--VSKTMKIKPGYMGTAASCYD-VQIIDDKGNVLPPGTEGDIGIRvkpirpiG-- 414
Cdd:cd05920 273 RRVPPVLGCTLQQVFGMAE-GLLNYtrLDDPDEVIIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTR-------Gpy 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 415 IFSGYVDNPDKTAANIRGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPV 493
Cdd:cd05920 345 TIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEL 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
3C5E_A 494 RGEVVKAFVVLAsqflshDPEQLTKELQQHVKSV-TAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd05920 425 LGERSCAFVVLR------DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
280-558 |
1.66e-38 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 147.52 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 280 LLPKFDPLVILKTLSSYPIKSMMGAP-IVYRM--LLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQ 356
Cdd:cd05929 199 LMEKFDPEEFLRLIERYRVTFAQFVPtMFVRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 357 TE-TGLTCMVSKTMKIKPGYMGTAASCyDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigifSGYVDNPDKTAANIRGDFW 435
Cdd:cd05929 279 TEgQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAARNEGGW 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 436 -LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqfLSHDPE 514
Cdd:cd05929 352 sTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAP--GADAGT 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....
3C5E_A 515 QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:cd05929 430 ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
37-559 |
2.29e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 147.72 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 37 FNFASDVLDHwadmekAGKRPPSPALWWvngKGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVI 116
Cdd:PRK06145 2 FNLSASIAFH------ARRTPDRAALVY---RDQEI--SYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 117 LGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagdeVIQEVDTVasecPSLRIKLLVSEKSCDGWLNFKKLLNEAST 196
Cdd:PRK06145 70 FAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL----VDEEFDAI----VALETPKIVIDAAAQADSRRLAQGGLEIP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 197 THHCVetGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTIsdtGWILNI-LCSLMEPWALGAC 275
Cdd:PRK06145 142 PQAAV--APTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVV---GPLYHVgAFDLPGIAVLWVG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 276 TFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLLQQDLSSYKFPHLQNCVTVGESLlPETL--ENWRAQTGLDIRE 352
Cdd:PRK06145 217 GTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEKT-PESRirDFTRVFTRARYID 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 353 SYGQTET--GLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRpigifSGYVDNPDKTAANI 430
Cdd:PRK06145 296 AYGLTETcsGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVT-----KGYWKDPEKTAEAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 431 RGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAS-QFL 509
Cdd:PRK06145 371 YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgATL 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3C5E_A 510 SHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 559
Cdd:PRK06145 451 TLE------ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
142-559 |
3.38e-38 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 147.98 E-value: 3.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 142 LQMSKAKAIVAGDEVIQEVDTVASECP-SLRIKLLVSEKScdgwlnfkKLLNEASTTHHC---VETGSQEASAIYFTSGT 217
Cdd:PRK13382 136 VTREGVDTVIYDEEFSATVDRALADCPqATRIVAWTDEDH--------DLTVEVLIAAHAgqrPEPTGRKGRVILLTSGT 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 218 SGLPKMAEHSYS--SLGLKAKMD-AGWTGLQASDIMWTISDTGWILNILCSlmepwALGACTFVhLLPKFDPLVILKTLS 294
Cdd:PRK13382 208 TGTPKGARRSGPggIGTLKAILDrTPWRAEEPTVIVAPMFHAWGFSQLVLA-----ASLACTIV-TRRRFDPEATLDLID 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 295 SYPIKSMMGAPIVYRMLLQ---QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS-KTMK 370
Cdd:PRK13382 282 RHRATGLAVVPVMFDRIMDlpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATpADLR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 371 IKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKtaaNIRGDFWLLGDRGIKDEDGYFQ 450
Cdd:PRK13382 362 AAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQ-----FDGYTSGSTK---DFHDGFMASGDVGYLDENGRLF 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 451 FMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAP 530
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG-ASATPE----TLKQHVRDNLAN 508
|
410 420
....*....|....*....|....*....
3C5E_A 531 YKYPRKIEFVLNLPKTVTGKIQRAKLRDK 559
Cdd:PRK13382 509 YKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
75-559 |
4.62e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 147.40 E-value: 4.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 75 NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD 154
Cdd:PRK08162 45 TWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 155 EVIQEVDTVASECPSLRIkLLV-------SEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPK--MA 224
Cdd:PRK08162 124 EFAEVAREALALLPGPKP-LVIdvddpeyPGGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKgvVY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 225 EHSYSSLGLKAKMDAgWTGLQASDIMWTISD---TGWilnilCSlmePWALGACTFVHL-LPKFDPLVILKTLSSYPIKS 300
Cdd:PRK08162 203 HHRGAYLNALSNILA-WGMPKHPVYLWTLPMfhcNGW-----CF---PWTVAARAGTNVcLRKVDPKLIFDLIREHGVTH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 301 MMGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLLPETLENwRAQTGLDIRESYGQTETgltcmvsktmkikpgYmGTA 379
Cdd:PRK08162 274 YCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAK-MEEIGFDLTHVYGLTET---------------Y-GPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 380 ASCYDVQIIDDkgnvLPPGTEGDI------------GIRV------KPI----RPIG--------IFSGYVDNPDKTAAN 429
Cdd:PRK08162 337 TVCAWQPEWDA----LPLDERAQLkarqgvryplqeGVTVldpdtmQPVpadgETIGeimfrgniVMKGYLKNPKATEEA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 430 IRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqfl 509
Cdd:PRK08162 413 FAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELK---- 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
3C5E_A 510 shDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQRAKLRDK 559
Cdd:PRK08162 489 --DGASATEeEIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQ 536
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
210-557 |
4.77e-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: 143.78 E-value: 4.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 210 AIYF-TSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSLMEPWALGAcTFVHLLPK--FDP 286
Cdd:cd05944 5 AAYFhTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGA-HVVLAGPAgyRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 287 LV---ILKTLSSYPIKSMMGAPIVYRMLLQ----QDLSSYKFphlqncVTVGESLLPETLEN-WRAQTGLDIRESYGQTE 358
Cdd:cd05944 84 GLfdnFWKLVERYRITSLSTVPTVYAALLQvpvnADISSLRF------AMSGAAPLPVELRArFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 359 TglTCMVSKTMK---IKPGYMGTAASCYDVQI--IDDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVDNPDKTAANIrGD 433
Cdd:cd05944 158 A--TCLVAVNPPdgpKRPGSVGLRLPYARVRIkvLDGVGRLLRDCAPDEVGEIC--VAGPGVFGGYLYTEGNKNAFV-AD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 434 FWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsQFLSHD 512
Cdd:cd05944 233 GWLnTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLK-PGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
3C5E_A 513 PEQLTKELQQHVKSVTApykYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd05944 312 EEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
51-559 |
8.13e-37 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 143.97 E-value: 8.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPALwwVNGK-GKELmwNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPG 129
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGAtGRVY--TYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 130 TIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPslrIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQEAS 209
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDG---VTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 210 AIYFTSGTSGLPK--MAEHS--YSSLGLKAKMDAGWTGLQASDI------MWTIsdtgWILN--ILCSLMepwaLGACtf 277
Cdd:PLN02246 183 ALPYSSGTTGLPKgvMLTHKglVTSVAQQVDGENPNLYFHSDDVilcvlpMFHI----YSLNsvLLCGLR----VGAA-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 278 VHLLPKFDPLVILKTLSSYPIK-SMMGAPIVYRM-----LLQQDLSSYKFphlqncVTVGESLLPETLEN-WRAQ-TGLD 349
Cdd:PLN02246 253 ILIMPKFEIGALLELIQRHKVTiAPFVPPIVLAIakspvVEKYDLSSIRM------VLSGAAPLGKELEDaFRAKlPNAV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 350 IRESYGQTETG---LTCMV-SKT-MKIKPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNP 423
Cdd:PLN02246 327 LGQGYGMTEAGpvlAMCLAfAKEpFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQI-----MKGYLNDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 424 DKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFV 502
Cdd:PLN02246 402 EATANTIDKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFV 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
3C5E_A 503 VLASQF-LSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 559
Cdd:PLN02246 482 VRSNGSeITED------EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
37-550 |
2.95e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 142.33 E-value: 2.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 37 FNFAsDVLDHWADmekagKRPPSPALwwVNGkgkELMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVI 116
Cdd:PRK07798 3 WNIA-DLFEAVAD-----AVPDRVAL--VCG---DRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 117 LGCIRAGLIfmPGTIQMKSTD--ILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLV----SEKSCDGWLNFKKL 190
Cdd:PRK07798 71 LGAFKARAV--PVNVNYRYVEdeLRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 191 LNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MAEHS---YSSLGLKAKMdagwTGLQASDiMWTISD-----TGWIL 260
Cdd:PRK07798 149 LAAGSPERDFGERSPDDLYLLY-TGGTTGMPKgvMWRQEdifRVLLGGRDFA----TGEPIED-EEELAKraaagPGMRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 261 NILCSLME---PWAL------GACTFVHLLPKFDPLVILKTLSSYPIKSM------MGAPIV--YRMLLQQDLSSykfph 323
Cdd:PRK07798 223 FPAPPLMHgagQWAAfaalfsGQTVVLLPDVRFDADEVWRTIEREKVNVItivgdaMARPLLdaLEARGPYDLSS----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 324 LQNCVTVGESLLPETLENWRAQ-TGLDIRESYGQTETGLtCMVSKTMKIKPGYMG---TAAScyDVQIIDDKGNVLPPGt 399
Cdd:PRK07798 298 LFAIASGGALFSPSVKEALLELlPNVVLTDSIGSSETGF-GGSGTVAKGAVHTGGprfTIGP--RTVVLDEDGNPVEPG- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 400 EGDIGI--RVKPIrPIGifsgYVDNPDKTAAN---IRGDFW-LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN 473
Cdd:PRK07798 374 SGEIGWiaRRGHI-PLG----YYKDPEKTAETfptIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3C5E_A 474 ALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGK 550
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 ... |
74-523 |
6.24e-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: 6.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdiLYrlQMSKAKAIvag 153
Cdd:cd05907 6 ITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP----------IY--PTSSAEQI--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 deviqevdtvasecpslrikllvsekscdGWLnfkklLNEASTTHHCVETGSQEASAIYfTSGTSGLPKMAEHSYSSLgl 233
Cdd:cd05907 70 -----------------------------AYI-----LNDSEAKALFVEDPDDLATIIY-TSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 234 KAKMDAGWTGLQASDIMWTIS--DTGWILNILCSLMEPWALGACTFVHLLPKfdplVILKTLSSYPIKSMMGAPIVYRML 311
Cdd:cd05907 113 LSNALALAERLPATEGDRHLSflPLAHVFERRAGLYVPLLAGARIYFASSAE----TLLDDLSEVRPTVFLAVPRVWEKV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 312 ---LQQDLSS------YKFPHLQNC--VTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAA 380
Cdd:cd05907 189 yaaIKVKAVPglkrklFDLAVGGRLrfAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 381 SCYDVQIIDDkGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADD-I 458
Cdd:cd05907 269 PGVEVRIADD-GEIL--------------VRGPNVMLGYYKNPEATAEALDADGWLhTGDLGEIDEDGFLHITGRKKDlI 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
3C5E_A 459 INSSGYRIGPSEVENALMEHPAVVETAVISSPDPvrgeVVKAFVVLasqflshDPEQLTKELQQH 523
Cdd:cd05907 334 ITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVP-------DPEALEAWAEEH 387
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
42-553 |
6.76e-35 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 138.10 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 42 DVLDHwadmeKAGKRPPSPALWWVNGKgkeLMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIR 121
Cdd:PRK05852 20 DLVEV-----AATRLPEAPALVVTADR---IAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 122 AGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCV 201
Cdd:PRK05852 91 ADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATST 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 202 ETGSQEASA-IYFTSGTSGLPKMAEHSYSSLGlkAKMDAGWTGLQASD------IMWTISDTGWILNILCSLMEPWALga 274
Cdd:PRK05852 171 PEGLRPDDAmIMFTGGTTGLPKMVPWTHANIA--SSVRAIITGYRLSPrdatvaVMPLYHGHGLIAALLATLASGGAV-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 275 ctfvhLLP---KFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQ---DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGL 348
Cdd:PRK05852 247 -----LLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILLERaatEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 349 DIRESYGQTET----------GLTCMVSKTMKIKPGYMGTAAscyDVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSG 418
Cdd:PRK05852 322 PVVCAFGMTEAthqvtttqieGIGQTENPVVSTGLVGRSTGA---QIRIVGSDGLPLPAGAVGEVWLRGTTV-----VRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 419 YVDNPDKTAANIRgDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEV 497
Cdd:PRK05852 394 YLGDPTITAANFT-DGWLrTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
3C5E_A 498 VKAFVV-LASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:PRK05852 473 VAAVIVpRESAPPTAE------ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
51-557 |
8.07e-35 |
|
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: 137.48 E-value: 8.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGT 130
Cdd:cd17651 3 RQAARTPDAPALVAEGRR-----LTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 131 IQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpslrikllvsekscDGWLNFKKLLNEASTTHHCVETGSQEASA 210
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPALAGELAVELV----------------AVTLLDQPGAAAGADAEPDPALDADDLAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKMAEHSYSSLGL-------KAKMDAGWTGLQASDIMWTISdTGWILNILCSlmepwalGACtfVHLLP- 282
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLANlvawqarASSLGPGARTLQFAGLGFDVS-VQEIFSTLCA-------GAT--LVLPPe 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 283 --KFDPLVILKTLSSYPI-KSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESL-LPETLENW-RAQTGLDIRESYGQT 357
Cdd:cd17651 211 evRTDPPALAAWLDEQRIsRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLvLTEDLREFcAGLPGLRLHNHYGPT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 358 ETglTCMVSKTMKIKPGYMGTAASC------YDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIR 431
Cdd:cd17651 291 ET--HVVTALSLPGDPAAWPAPPPIgrpidnTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAERFV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 432 GD-------FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVl 504
Cdd:cd17651 364 PDpfvpgarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV- 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
3C5E_A 505 ASQFLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd17651 443 GDPEAPVDAA----ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
95-563 |
3.40e-34 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 136.51 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 95 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagdeVIQEVDTVASEcpSLRI-- 172
Cdd:PLN02479 66 SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM----VDQEFFTLAEE--ALKIla 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 173 ---------KLLV--SEKSCD----------GWLNFKKLLneastthhcvETGSQE-----------ASAIYFTSGTSGL 220
Cdd:PLN02479 140 ekkkssfkpPLLIviGDPTCDpkslqyalgkGAIEYEKFL----------ETGDPEfawkppadewqSIALGYTSGTTAS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 221 PKMAEHSYSSLGLKAKMDAGWTGLQASDI-MWTISD---TGWILnilcslmePWALGA-CTFVHLLPKFDPLVILKTLSS 295
Cdd:PLN02479 210 PKGVVLHHRGAYLMALSNALIWGMNEGAVyLWTLPMfhcNGWCF--------TWTLAAlCGTNICLRQVTAKAIYSAIAN 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 296 YPIKSMMGAPIVYRMLLQQDLSS--YKFPHLQNCVTVGESLLPETLENWrAQTGLDIRESYGQTET-------------- 359
Cdd:PLN02479 282 YGVTHFCAAPVVLNTIVNAPKSEtiLPLPRVVHVMTAGAAPPPSVLFAM-SEKGFRVTHTYGLSETygpstvcawkpewd 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 360 GLTCMVSKTMKIKPGYMGTAASCYDVqiIDDKGNVLPPGTEGDIGIRVkpIRPIGIFSGYVDNPDKTAANIRGDFWLLGD 439
Cdd:PLN02479 361 SLPPEEQARLNARQGVRYIGLEGLDV--VDTKTMKPVPADGKTMGEIV--MRGNMVMKGYLKNPKANEEAFANGWFHSGD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 440 RGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDPEQLTKE 519
Cdd:PLN02479 437 LGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAED 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....
3C5E_A 520 LQQHVKSVTAPYKYPRKIEFVlNLPKTVTGKIQRAKLRDKEWKM 563
Cdd:PLN02479 517 IMKFCRERLPAYWVPKSVVFG-PLPKTATGKIQKHVLRAKAKEM 559
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
74-557 |
3.88e-34 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 134.80 E-value: 3.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivag 153
Cdd:cd17649 13 LSYAELDARANRLAHRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 deviqevdtVASECPSLRIKLLVsEKSCDGWLnfkkllneasTTHHcvetGSQEASAIYfTSGTSGLPKMAEHSYSSLGL 233
Cdd:cd17649 67 ---------LDPEYPAERLRYML-EDSGAGLL----------LTHH----PRQLAYVIY-TSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 234 KAKMDAGWTGLQASDIMWTISDTGWILNILCsLMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVY-RMLL 312
Cdd:cd17649 122 HCQATAERYGLTPGDRELQFASFNFDGAHEQ-LLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYlQQLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 313 QQ--DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIREsYGQTETGLTCMVSKT---MKIKPGYM--GTAASCYDV 385
Cdd:cd17649 201 EEadRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNA-YGPTEATVTPLVWKCeagAARAGASMpiGRPLGGRSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 386 QIIDDKGNVLPPGTEGD--IGIRvkpirpiGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMGRA 455
Cdd:cd17649 280 YILDADLNPVPVGVTGElyIGGE-------GLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGRV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 456 DDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVL-ASQFLSHDPEQltkeLQQHVKSVTAPYKYP 534
Cdd:cd17649 353 DHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLrAAAAQPELRAQ----LRTALRASLPDYMVP 427
|
490 500
....*....|....*....|...
3C5E_A 535 RKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd17649 428 AHLVFLARLPLTPNGKLDRKALP 450
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
78-556 |
1.44e-33 |
|
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: 133.79 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 78 ELSENSQQAANVLSGacGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD--E 155
Cdd:cd05923 34 LRARIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVdaQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 VIQEVDTVASECpsLRIKLLVSEKSCDgwlNFKKLLNEASTthhcvetGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKA 235
Cdd:cd05923 112 VMDAIFQSGVRV--LALSDLVGLGEPE---SAGPLIEDPPR-------EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 236 KMDAGWTGLQASDimwtisdtgwiLNILCSLMEPW-----------ALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGA 304
Cdd:cd05923 180 LFMSTQAGLRHGR-----------HNVVLGLMPLYhvigffavlvaALALDGTYVVVEEFDPADALKLIEQERVTSLFAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 305 PIVYRMLLQQDL-SSYKFPHLQNCVTVGESL---LPETLENWRAQTGLDIresYGQTETgltcMVSKTMK-IKPGYMGTA 379
Cdd:cd05923 249 PTHLDALAAAAEfAGLKLSSLRHVTFAGATMpdaVLERVNQHLPGEKVNI---YGTTEA----MNSLYMRdARTGTEMRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 380 ASCYDVQIIDDKGNV---LPPGTEGDIgirVKPIRPIGIFSGYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRAD 456
Cdd:cd05923 322 GFFSEVRIVRIGGSPdeaLANGEEGEL---IVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 457 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFLSHDpeqltkELQQHVK-SVTAPYKYPR 535
Cdd:cd05923 399 DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD------ELDQFCRaSELADFKRPR 472
|
490 500
....*....|....*....|.
3C5E_A 536 KIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd05923 473 RYFFLDELPKNAMNKVLRRQL 493
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
53-559 |
1.85e-33 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 134.84 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 53 AGKRPPSPALWW-VNGKGKELMWnfRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtI 131
Cdd:COG1022 21 AARFPDRVALREkEDGIWQSLTW--AEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP--I 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 132 QMKST--DILYRLQMSKAKAIVAGD-EVIQEVDTVASECPSLRiKLLV----SEKSCDGWLNFKKLLNEASTTHH--CVE 202
Cdd:COG1022 96 YPTSSaeEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVldprGLRDDPRLLSLDELLALGREVADpaELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 203 TGSQEASA-----IYFTSGTSGLPKMAEHSYSSLglkakmdagWTGLQASDIMWTISDTGWILNILcslmePWA------ 271
Cdd:COG1022 175 ARRAAVKPddlatIIYTSGTTGRPKGVMLTHRNL---------LSNARALLERLPLGPGDRTLSFL-----PLAhvfert 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 272 -------LGAC--------TFVHLLPKFDPLVIL---------------KTLSSYPIKSM-----MGAPIVYRMLLQQDL 316
Cdd:COG1022 241 vsyyalaAGATvafaespdTLAEDLREVKPTFMLavprvwekvyagiqaKAEEAGGLKRKlfrwaLAVGRRYARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 317 S---SYKFPH------------------LQNCVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKTMKIKPGY 375
Cdd:COG1022 321 SpslLLRLKHaladklvfsklrealggrLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRPGDNRIGT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 376 MGTAAScyDVQI-IDDKGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMG 453
Cdd:COG1022 400 VGPPLP--GVEVkIAEDGEIL--------------VRGPNVMKGYYKNPEATAEAFDADGWLHtGDIGELDEDGFLRITG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 454 RADDII-NSSGYRIGPSEVENALMEHP----AVV--E-----TAVIsSPDPvrgEVVK--------AFVVLASqfLSHDP 513
Cdd:COG1022 464 RKKDLIvTSGGKNVAPQPIENALKASPlieqAVVvgDgrpflAALI-VPDF---EALGewaeenglPYTSYAE--LAQDP 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
3C5E_A 514 EqLTKELQQHVKSVTApyKYPR--KI-EFVLnLPK---------TVTGKIQRAKLRDK 559
Cdd:COG1022 538 E-VRALIQEEVDRANA--GLSRaeQIkRFRL-LPKeftiengelTPTLKLKRKVILEK 591
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
354-549 |
3.29e-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: 129.34 E-value: 3.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 354 YGQTE-TGLTCMvsktmkikPGYMGTAASCY-------DVQIIDDKGNVLPPGTEGDIGIRvKPIrpigIFSGYVDNPDK 425
Cdd:cd17636 143 YGQTEvMGLATF--------AALGGGAIGGAgrpsplvQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 426 TAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL- 504
Cdd:cd17636 210 NARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLk 289
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
3C5E_A 505 ASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 549
Cdd:cd17636 290 PGASVTEA------ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
51-556 |
1.70e-32 |
|
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: 130.53 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGT 130
Cdd:cd17655 5 EQAEKTPDHTAVVFEDQT-----LTYRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 131 IQMKSTDILYRLQMSKAKAIVAGDEVIQevdtvasecpslrikLLVSEKSCDgWLNFKKLLNEASTTHHCVETGSQEASA 210
Cdd:cd17655 79 PDYPEERIQYILEDSGADILLTQSHLQP---------------PIAFIGLID-LLDEDTIYHEESENLEPVSKSDDLAYV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYfTSGTSGLPK--MAEHS-----YSSLGLKAKMDAGWTGLQASDIMWTISDTgwilnilcSLMEPWALGACtfVHLLPK 283
Cdd:cd17655 143 IY-TSGSTGKPKgvMIEHRgvvnlVEWANKVIYQGEHLRVALFASISFDASVT--------EIFASLLSGNT--LYIVRK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 284 ---FDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENW--RAQTGLDIRESYGQTE 358
Cdd:cd17655 212 etvLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 359 TGLTCMV-----SKTMKIKPgYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD 433
Cdd:cd17655 290 TTVDASIyqyepETDQQVSV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE-----GVARGYLNRPELTAEKFVDD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 434 FWLLGDRGIKD-------EDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAS 506
Cdd:cd17655 364 PFVPGERMYRTgdlarwlPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3C5E_A 507 QFlshDPEQLTKELQQHVKSVTAPyKYPRKIEfvlNLPKTVTGKIQRAKL 556
Cdd:cd17655 444 EL---PVAQLREFLARELPDYMIP-SYFIKLD---EIPLTPNGKVDRKAL 486
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
51-556 |
3.02e-32 |
|
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: 129.70 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPALWWVngkGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgt 130
Cdd:cd17646 6 EQAARTPDAPAVVDE---GRTL--TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 131 iqmksTDILY---RLQM--SKAKAIVagdeVIQEVDTVASECPSLRIKLLVSEkscdgwlnfkkLLNEASTTHHCVETGS 205
Cdd:cd17646 78 -----LDPGYpadRLAYmlADAGPAV----VLTTADLAARLPAGGDVALLGDE-----------ALAAPPATPPLVPPRP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 206 QEASAIYFTSGTSGLPK--MAEHSYSS---LGLKAK--MDAGWTGLQASDIMWTISdtGW-ILnilcslmepWAL--GAC 275
Cdd:cd17646 138 DNLAYVIYTSGSTGRPKgvMVTHAGIVnrlLWMQDEypLGPGDRVLQKTPLSFDVS--VWeLF---------WPLvaGAR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 276 TFV-----HLlpkfDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSyKFPHLQNCVTVGESLLPETLENWRAQTGLDI 350
Cdd:cd17646 207 LVVarpggHR----DPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAG-SCASLRRVFCSGEALPPELAARFLALPGAEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 351 RESYGQTE-----TGLTCMVSKTMKIKP-GYMGTAASCYdvqIIDDKGNVLPPGTEGDI---GIRVKpirpigifSGYVD 421
Cdd:cd17646 282 HNLYGPTEaaidvTHWPVRGPAETPSVPiGRPVPNTRLY---VLDDALRPVPVGVPGELylgGVQLA--------RGYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 422 NPDKTAANIRGD-------FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 494
Cdd:cd17646 351 RPALTAERFVPDpfgpgsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAG 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
3C5E_A 495 GEVVKAFVVLASQFLSHDPEqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17646 431 AARLVGYVVPAAGAAGPDTA----ALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
76-557 |
5.63e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 129.13 E-value: 5.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGACGLQRgdRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 155
Cdd:PRK07638 29 YKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 VIQEVDTVasECPSLRIkllvsekscDGWlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSlglka 235
Cdd:PRK07638 107 KLNDLPDE--EGRVIEI---------DEW---KRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 236 kmdagWT-GLQASDIMWTISDTGWILnILCSLMEPWAL-GACT------FVHLLPKFDPLVILKTLSSYPIKSMMGAPIV 307
Cdd:PRK07638 168 -----WLhSFDCNVHDFHMKREDSVL-IAGTLVHSLFLyGAIStlyvgqTVHLMRKFIPNQVLDKLETENISVMYTVPTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 308 YRMLLQQDlssyKFPhlQNCVTV---GESLLPETLEnwRAQTG---LDIRESYGQTETG-LTCMVSKTMKIKPGYMGTAA 380
Cdd:PRK07638 242 LESLYKEN----RVI--ENKMKIissGAKWEAEAKE--KIKNIfpyAKLYEFYGASELSfVTALVDEESERRPNSVGRPF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 381 SCYDVQIIDDKGNVLPPGTEGDIGIRvKPIRpigiFSGYVdNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDII 459
Cdd:PRK07638 314 HNVQVRICNEAGEEVQKGEIGTVYVK-SPQF----FMGYI-IGGVLARELNADGWMtVRDVGYEDEEGFIYIVGREKNMI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 460 NSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVvlasqflshDPEQLTKELQQHVKSVTAPYKYPRKIEF 539
Cdd:PRK07638 388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKEWHF 458
|
490
....*....|....*...
3C5E_A 540 VLNLPKTVTGKIQRAKLR 557
Cdd:PRK07638 459 VDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
51-556 |
8.79e-32 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 128.47 E-value: 8.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPALwwVNGKGKelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGT 130
Cdd:cd12117 5 EQAARTPDAVAV--VYGDRS---LTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 131 IQMKSTDILYRLQMSKAKAIVAgdeviQEVDTVASECPSLRIKLLVSEKSCDGwlnfkklLNEASTthhcvetGSQEASA 210
Cdd:cd12117 79 PELPAERLAFMLADAGAKVLLT-----DRSLAGRAGGLEVAVVIDEALDAGPA-------GNPAVP-------VSPDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 -IYFTSGTSGLPK--MAEHsYSSLGLKakMDAGWTGLQASDIMWTISDTGWIlnilCSLMEPW-AL--GACtfVHLLPK- 283
Cdd:cd12117 140 yVMYTSGSTGRPKgvAVTH-RGVVRLV--KNTNYVTLGPDDRVLQTSPLAFD----ASTFEIWgALlnGAR--LVLAPKg 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 284 --FDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETG 360
Cdd:cd12117 211 tlLDPDALGALIAEEGVTVLWLTAALFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 361 L--TCMVsktmkIKPGYM-------GTAASCYDVQIIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVDNPDKTA- 427
Cdd:cd12117 289 TftTSHV-----VTELDEvagsipiGRPIANTRVYVLDEDGRPVPPGVPGELyvgGD--------GLALGYLNRPALTAe 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 428 ---ANIRGD---FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPD-PVRGEVVkA 500
Cdd:cd12117 356 rfvADPFGPgerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDaGGDKRLV-A 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
3C5E_A 501 FVVlASQFLSHDpeqltkELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd12117 435 YVV-AEGALDAA------ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
213-559 |
1.22e-31 |
|
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: 124.75 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 213 FTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDimwtisdtGWilniLCSLmeP------------WALGACTFVhL 280
Cdd:cd17630 7 LTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD--------SW----LLSL--PlyhvgglailvrSLLAGAELV-L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 281 LPKFDPLviLKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNcVTVGESLLPETLENWRAQTGLDIRESYGQTETG 360
Cdd:cd17630 72 LERNQAL--AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRA-VLLGGAPIPPELLERAADRGIPLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 361 LTcmvsktmkikpgymgTAASCYDVQIIDDKGNVLPpgtegDIGIRVKP-----IRPIGIFSGYVDNPDKTAANIRGdfW 435
Cdd:cd17630 149 SQ---------------VATKRPDGFGRGGVGVLLP-----GRELRIVEdgeiwVGGASLAMGYLRGQLVPEFNEDG--W 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 436 L-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflshDPE 514
Cdd:cd17630 207 FtTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
3C5E_A 515 QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDK 559
Cdd:cd17630 280 ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
66-559 |
9.05e-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: 126.04 E-value: 9.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 66 NGKGKELMWNfrELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMS 145
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 146 KAKAIVAG--DEVIQEVDTVASECPSLRIKLLVSEKSCDGWlnfKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKM 223
Cdd:cd05932 78 ESKALFVGklDDWKAMAPGVPEGLISISLPPPSAANCQYQW---DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 224 AEHSYSSLGLKAKMDAGWTGLQASDIMW-----------TISDTGWILNilcSLMEPWALGACTFVHLLPKFDPLVI--- 289
Cdd:cd05932 155 VMLTFGSFAWAAQAGIEHIGTEENDRMLsylplahvterVFVEGGSLYG---GVLVAFAESLDTFVEDVQRARPTLFfsv 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 290 --LKTLSSYPIKSMMGA---------PIVYRMLLQQDLSSYKFPHLQnCVTVGESLLPETLENWRAQTGLDIRESYGQTE 358
Cdd:cd05932 232 prLWTKFQQGVQDKIPQqklnlllkiPVVNSLVKRKVLKGLGLDQCR-LAGCGSAPVPPALLEWYRSLGLNILEAYGMTE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 359 TGLTCMVSKTMKIKPGYMGTAAScyDVQI-IDDKGNVLppgtegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWL- 436
Cdd:cd05932 311 NFAYSHLNYPGRDKIGTVGNAGP--GVEVrISEDGEIL--------------VRSPALMMGYYKDPEATAEAFTADGFLr 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 437 LGDRGIKDEDGYFQFMGRADDIINSS-GYRIGPSEVENALMEHPAVVETAVISS--PDPVRGEVVKAFVVLASqfLSHDP 513
Cdd:cd05932 375 TGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRA--DAFAR 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
3C5E_A 514 EQLTKELQQHVKSVTAPYKYPRKIEFVL---------NLPKTVTGKIQRAKLRDK 559
Cdd:cd05932 453 AELEASLRAHLARVNSTLDSHEQLAGIVvvkdpwsidNGILTPTLKIKRNVLEKA 507
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
210-553 |
9.17e-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: 122.75 E-value: 9.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 210 AIYFTSGTSGLPKMAEHSYSSLGLKAKMdagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACTF-----VHLLPKF 284
Cdd:cd17635 5 AVIFTSGTTGEPKAVLLANKTFFAVPDI------LQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIhgglcVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 285 DPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVG-ESLLPETLENWRAQTGLDIRESYGQTETG-LT 362
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGgSRAIAADVRFIEATGLTNTAQVYGLSETGtAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 363 CMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGI 442
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSP-----ANMLGYWNNPERTAEVLIDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 443 KDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshDPEQLTKELQQ 522
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE----LDENAIRALKH 309
|
330 340 350
....*....|....*....|....*....|.
3C5E_A 523 HVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:cd17635 310 TIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
62-557 |
1.38e-30 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 126.55 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 62 LWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYR 141
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 142 LQMSKAKAIVA------GDEVIQEVDTV-------ASECPSLRIKLLVSEKSC------------DGWlnFKKLLNEAST 196
Cdd:PLN02654 188 IVDCKPKVVITcnavkrGPKTINLKDIVdaaldesAKNGVSVGICLTYENQLAmkredtkwqegrDVW--WQDVVPNYPT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 197 THHCVETGSQEASAIYFTSGTSGLPKMAEHS------YSSLGLKAKMDagwtgLQASDIMWTISDTGWILNILCSLMEPW 270
Cdd:PLN02654 266 KCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTtggymvYTATTFKYAFD-----YKPTDVYWCTADCGWITGHSYVTYGPM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 271 ALGACTFV-HLLPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQQD---LSSYKFPHLQNCVTVGESLLPETlenWR-- 343
Cdd:PLN02654 341 LNGATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSA---WRwf 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 344 ----AQTGLDIRESYGQTETGlTCMVSKTMKIKPGYMGTAA-SCYDVQ--IIDDKGNVLppgtEGDIG--IRVKPIRPiG 414
Cdd:PLN02654 418 fnvvGDSRCPISDTWWQTETG-GFMITPLPGAWPQKPGSATfPFFGVQpvIVDEKGKEI----EGECSgyLCVKKSWP-G 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 415 IFS---GYVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPD 491
Cdd:PLN02654 492 AFRtlyGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEH 571
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
3C5E_A 492 PVRGEVVKAFVVLASQFLShdPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:PLN02654 572 EVKGQGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
83-557 |
4.10e-30 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 124.53 E-value: 4.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 83 SQQAANVLSGACGL-----QRGDRVAVVLPRvPEW---WLVILGCirAGLIFMPgtiqmkstdILYRLQMSKAKAIVagd 154
Cdd:PLN02860 36 HEFVDGVLSLAAGLlrlglRNGDVVAIAALN-SDLyleWLLAVAC--AGGIVAP---------LNYRWSFEEAKSAM--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 155 EVIQEVDTVASE-------------CPSLRIKLLVSEKSCDGWLNFKKLLN-EASTTHHCVETGSQEASA------IYFT 214
Cdd:PLN02860 101 LLVRPVMLVTDEtcsswyeelqndrLPSLMWQVFLESPSSSVFIFLNSFLTtEMLKQRALGTTELDYAWApddavlICFT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 215 SGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTIS---DTGWILNILCSLMepwaLGACtfvH-LLPKFDPLVIL 290
Cdd:PLN02860 181 SGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAplcHIGGLSSALAMLM----VGAC---HvLLPKFDAKAAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 291 KTLSSYPIKSMMGAPIVYRMLL---QQDLSSYKFPHLQNCVTVGES----LLPETLENW-RAQtgldIRESYGQTET--G 360
Cdd:PLN02860 254 QAIKQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSlssrLLPDAKKLFpNAK----LFSAYGMTEAcsS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 361 LTCMV--SKTMKIKPGYMGTAASCYDvQIIDDKGNVL----PPGTEgdIGIRVKPIRPIG-IFS-------GYVDNPDKT 426
Cdd:PLN02860 330 LTFMTlhDPTLESPKQTLQTVNQTKS-SSVHQPQGVCvgkpAPHVE--LKIGLDESSRVGrILTrgphvmlGYWGQNSET 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 427 AANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL- 504
Cdd:PLN02860 407 ASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLr 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
3C5E_A 505 -------ASQFLSHDPEQLTKE-LQQHV--KSVTApYKYPRKieFVLN---LPKTVTGKIQRAKLR 557
Cdd:PLN02860 487 dgwiwsdNEKENAKKNLTLSSEtLRHHCreKNLSR-FKIPKL--FVQWrkpFPLTTTGKIRRDEVR 549
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
95-564 |
1.58e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 123.60 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 95 GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQmkstdiLYRlqmskakaivaGDEVIQEVDTVASecpslrikL 174
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE------LHR-----------DDHALAARNTEPA--------L 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 175 LVSEKS-CDGW-----LNFKKLLNEAS---TTHHCVETGSQEASAIYfTSGTSGLPKMAEHSYSS-LGLKAKMDAGWTGL 244
Cdd:PRK06060 106 VVTSDAlRDRFqpsrvAEAAELMSEAArvaPGGYEPMGGDALAYATY-TSGTTGPPKAAIHRHADpLTFVDAMCRKALRL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 245 QASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLP-----------KFDPLVilktlssypiksMMGAPIVYRMLLQ 313
Cdd:PRK06060 185 TPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPvtpeaaailsaRFGPSV------------LYGVPNFFARVID 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 314 QdLSSYKFPHLQNCVTVGESL---LPETLENWRAqtGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDD 390
Cdd:PRK06060 253 S-CSPDSFRSLRCVVSAGEALelgLAERLMEFFG--GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 391 KGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANirGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSE 470
Cdd:PRK06060 330 DGTTAGPGVEGDLWVR-GP----AIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 471 VENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAS-QFLShdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 549
Cdd:PRK06060 403 VERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSgATID---GSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNG 479
|
490 500
....*....|....*....|
3C5E_A 550 KIQRAKLRDKE-----WKMS 564
Cdd:PRK06060 480 KLVRGALRKQSptkpiWELS 499
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
76-557 |
6.47e-29 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 121.04 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDE 155
Cdd:PRK05620 41 FAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 VIQEVDTVASECPSLRIKLLVSEKSCDG----------WLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 225
Cdd:PRK05620 121 LAEQLGEILKECPCVRAVVFIGPSDADSaaahmpegikVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 226 HSYSSLGLKAkmdagwTGLQASDIMWTISDTGW-----ILNIL--CSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPI 298
Cdd:PRK05620 201 YSHRSLYLQS------LSLRTTDSLAVTHGESFlccvpIYHVLswGVPLAAFMSGT-PLVFPGPDLSAPTLAKIIATAMP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 299 KSMMGAPIVYRMLLQQDL-SSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSKTmkiKPGYMG 377
Cdd:PRK05620 274 RVAHGVPTLWIQLMVHYLkNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARP---PSGVSG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 378 TAASCYDV-----------QIIDDkGNVLPPG--TEGDIGIRvKPIRPIGIFSGYVDNPDKTAANIRG------------ 432
Cdd:PRK05620 351 EARWAYRVsqgrfpasleyRIVND-GQVMESTdrNEGEIQVR-GNWVTASYYHSPTEEGGGAASTFRGedvedandrfta 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 433 DFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlsh 511
Cdd:PRK05620 429 DGWLrTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGI--- 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
3C5E_A 512 DPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:PRK05620 506 EPTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
53-556 |
6.52e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 122.96 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 53 AGKRPPSPALWWvngkGKELMwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQ 132
Cdd:PRK12467 522 ARQHPERPALVF----GEQVL-SYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 133 MKSTDILYRLQMSKAKAIVAGDEVIQEVDtVASECPSLRIKLLvsekscdgwlnfKKLLNEASTTHHCVETGSQEASAIY 212
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLP-VPAGLRSLCLDEP------------ADLLCGYSGHNPEVALDPDNLAYVI 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 213 FTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILcslMEPWALGACTFVHLLPK---FDPLVI 289
Cdd:PRK12467 663 YTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVT---ELFGALASGATLHLLPPdcaRDAEAF 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 290 LKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPhlQNCVTV-GESLLPETLENWRA-QTGLDIRESYGQTETglTCMVS- 366
Cdd:PRK12467 740 AALMADQGVTVLKIVPSHLQALLQASRVALPRP--QRALVCgGEALQVDLLARVRAlGPGARLINHYGPTET--TVGVSt 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 367 -----KTMKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD-------- 433
Cdd:PRK12467 816 yelsdEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGA-----GLARGYHRRPALTAERFVPDpfgadggr 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 434 FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQFLSHDP 513
Cdd:PRK12467 891 LYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEH 969
|
490 500 510 520
....*....|....*....|....*....|....*....|...
3C5E_A 514 EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:PRK12467 970 QATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
74-556 |
9.02e-29 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 119.32 E-value: 9.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 153
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 DEviqEVDTVASECPSLRIKLLvsekscdgwlnfkkllnEASTTHHCVETGSQEASAIY--FTSGTSGLPKMAEHSYSSL 231
Cdd:cd12116 92 DA---LPDRLPAGLPVLLLALA-----------------AAAAAPAAPRTPVSPDDLAYviYTSGSTGRPKGVVVSHRNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 232 G--LKAKMDAgwTGLQASDIMWTISDTGWILNILCSLMePWALGACtfVHLLPK---FDPLVILKTLSSYPIKSMMGAPI 306
Cdd:cd12116 152 VnfLHSMRER--LGLGPGDRLLAVTTYAFDISLLELLL-PLLAGAR--VVIAPRetqRDPEALARLIEAHSITVMQATPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 307 VYRMLL---QQDLSSYKfphlqncVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTcmvSKTMKIKPGY----MGTA 379
Cdd:cd12116 227 TWRMLLdagWQGRAGLT-------ALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIW---STAARVTAAAgpipIGRP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 380 ASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQF 451
Cdd:cd12116 297 LANTQVYVLDAALRPVPPGVPGELYIG-----GDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 452 MGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQfLSHDPEQLTKELQQHVKSVTAPY 531
Cdd:cd12116 372 LGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAG-AAPDAAALRAHLRATLPAYMVPS 449
|
490 500
....*....|....*....|....*
3C5E_A 532 KYPRKIEFvlnlPKTVTGKIQRAKL 556
Cdd:cd12116 450 AFVRLDAL----PLTANGKLDRKAL 470
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
211-561 |
1.34e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 119.79 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDImwtisdtgwilnILCSL--------MEPWALGACT--FVHL 280
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDV------------CYVSMplfhsnavMAGWAVALAAgaSIAL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 281 LPKFDPLVILKTLSSYPIKSM--MGAPIVYRmllqqdLSSYKFP-HLQNCVTV--GESLLPETLENWRAQTGLDIRESYG 355
Cdd:PRK07867 225 RRKFSASGFLPDVRRYGATYAnyVGKPLSYV------LATPERPdDADNPLRIvyGNEGAPGDIARFARRFGCVVVDGFG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 356 QTETGLTcmVSKTMKIKPGYMGTAAScyDVQIID-DKGNVLPPGtEGDIGIRVKPIRPIG---------IFSGYVDNPDK 425
Cdd:PRK07867 299 STEGGVA--ITRTPDTPPGALGPLPP--GVAIVDpDTGTECPPA-EDADGRLLNADEAIGelvntagpgGFEGYYNDPEA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 426 TAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA 505
Cdd:PRK07867 374 DAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
3C5E_A 506 --SQFlshDPEQLTKELqqHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 561
Cdd:PRK07867 454 pgAKF---DPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
74-558 |
1.84e-28 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 121.12 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLsGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtIqmkstDILY---RLQM----SK 146
Cdd:COG1020 502 LTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP--L-----DPAYpaeRLAYmledAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 147 AKAIVAGDEViqevdtvASECPSLRIKLLVsekscdgwLNFKKLLNEASTTHHCVETGSQEASAIYfTSGTSGLPK--MA 224
Cdd:COG1020 574 ARLVLTQSAL-------AARLPELGVPVLA--------LDALALAAEPATNPPVPVTPDDLAYVIY-TSGSTGRPKgvMV 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 225 EHSysslGLKAKMDA--GWTGLQASDIM---WTIS-DTgwilnilcSLME---PWALGACtfVHLLPK---FDPLVILKT 292
Cdd:COG1020 638 EHR----ALVNLLAWmqRRYGLGPGDRVlqfASLSfDA--------SVWEifgALLSGAT--LVLAPPearRDPAALAEL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 293 LSSYPIKSMMGAPIVYRMLLQQDLSSykFPHLQNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETglTCMVSkTMKI 371
Cdd:COG1020 704 LARHRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTET--TVDST-YYEV 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 372 KPGYMGTAASCY-------DVQIIDDKGNVLPPGTEGDI---GIrvkpirpiGIFSGYVDNPDKTAAN-IRGDFWLL--- 437
Cdd:COG1020 779 TPPDADGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELyigGA--------GLARGYLNRPELTAERfVADPFGFPgar 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 438 ----GDRGIKDEDGYFQFMGRADD---IinsSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqfls 510
Cdd:COG1020 851 lyrtGDLARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA---- 923
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
3C5E_A 511 hDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:COG1020 924 -GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
76-558 |
3.41e-28 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 117.03 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivagde 155
Cdd:cd17653 25 YGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP--------------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 viqeVDTvasECPSLRIKLLVSEKSCdgwlnfkKLlneastthhCVETGSQEASA-IYFTSGTSGLPK--MAEHS----Y 228
Cdd:cd17653 77 ----LDA---KLPSARIQAILRTSGA-------TL---------LLTTDSPDDLAyIIFTSGSTGIPKgvMVPHRgvlnY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 229 SSLGlKAKMDA--GWTGLQASDIMWTISdTGWILNILC--------SLMEPWA--LGACTFVHLLPKFdplvilktLSSY 296
Cdd:cd17653 134 VSQP-PARLDVgpGSRVAQVLSIAFDAC-IGEIFSTLCnggtlvlaDPSDPFAhvARTVDALMSTPSI--------LSTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 297 PIKSmmgapivyrmllqqdlssykFPHLQNCVTVGESLLPETLENWRAqtGLDIRESYGQTETGLTCMVSKTMKIKPGYM 376
Cdd:cd17653 204 SPQD--------------------FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 377 GTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAANIRGD-FW------LLGDRGIKDEDGYF 449
Cdd:cd17653 262 GKPIPNSTCYILDADLQPVPEGVVGEICIS-----GVQVARGYLGNPALTASKFVPDpFWpgsrmyRTGDYGRWTEDGGL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 450 QFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISspdpVRGEVVKAFVVLASQflshDPEQLTKELQQHVKSvta 529
Cdd:cd17653 337 EFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI----VVNGRLVAFVTPETV----DVDGLRSELAKHLPS--- 405
|
490 500
....*....|....*....|....*....
3C5E_A 530 pYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:cd17653 406 -YAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
86-558 |
4.02e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 118.58 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 86 AANVLSgaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA-------GDEVIQ 158
Cdd:PLN03102 53 AASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVdrsfeplAREVLH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 159 EVDTVASEcPSLRIKLL----VSEKSCDGWLNFKKLLNEASTTHHCVET-----GSQEASAIYFTSGTSGLPKMAEHSYS 229
Cdd:PLN03102 131 LLSSEDSN-LNLPVIFIheidFPKRPSSEELDYECLIQRGEPTPSLVARmfriqDEHDPISLNYTSGTTADPKGVVISHR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 230 SLGLKA-KMDAGWTGLQASDIMWTISD---TGWILnilcslmePWALGA------CTFVHLLPKfdplvILKTLSSYPIK 299
Cdd:PLN03102 210 GAYLSTlSAIIGWEMGTCPVYLWTLPMfhcNGWTF--------TWGTAArggtsvCMRHVTAPE-----IYKNIEMHNVT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 300 SMMGAPIVYRMLLQQDLS--SYKFPHLQncVTVGESLLPETLENWRAQTGLDIRESYGQTE-TG--LTCM---------V 365
Cdd:PLN03102 277 HMCCVPTVFNILLKGNSLdlSPRSGPVH--VLTGGSPPPAALVKKVQRLGFQVMHAYGLTEaTGpvLFCEwqdewnrlpE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 366 SKTMKIKPGYMGTAASCYDVQIIDDKGNVLPP---GTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGI 442
Cdd:PLN03102 355 NQQMELKARQGVSILGLADVDVKNKETQESVPrdgKTMGEIVIKGS-----SIMKGYLKNPKATSEAFKHGWLNTGDVGV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 443 KDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL--ASQFLSHDPEQL-TKE 519
Cdd:PLN03102 430 IHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVDKLvTRE 509
|
490 500 510 520
....*....|....*....|....*....|....*....|.
3C5E_A 520 --LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PLN03102 510 rdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
211-553 |
1.11e-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: 113.65 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQASdimwtiSDTgwILNILCSLMEPWALGACTF-------VHLLPK 283
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSW--IESFVCNEDLFNIS------GED--AILAPGPLSHSLFLYGAISalylggtFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 284 FDPLVILKTLSSYPIKSMMGAPivyrMLLQQdLSSYKFPHL--QNCVTVGESLLPETLENWRAQT-GLDIRESYGQTETG 360
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVP----TMLQA-LARTLEPESkiKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 361 LTCMVSKTMKIKPGYMGTAASCYDVQIIDDKGNVlppgtegdIG-IRVK-PIrpigIFSGYVD----NPDKtaanirgdf 434
Cdd:cd17633 150 FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGE--------IGkIFVKsEM----VFSGYVRggfsNPDG--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 435 WL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflshdp 513
Cdd:cd17633 209 WMsVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSG--------- 279
|
330 340 350 360
....*....|....*....|....*....|....*....|.
3C5E_A 514 EQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:cd17633 280 DKLTyKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
84-558 |
3.02e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 115.71 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 84 QQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMpgTIQMKSTDILYRLQMSKAKAIVAgdevIQEVDTV 163
Cdd:PLN02574 77 KSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVT--TMNPSSSLGEIKKRVVDCSVGLA----FTSPENV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 164 aSECPSLRIK-LLVSEKscdgwLNFKKLLNEASTTHHCVET----------GSQEASAIYFTSGTSGLPK--MAEHS--Y 228
Cdd:PLN02574 151 -EKLSPLGVPvIGVPEN-----YDFDSKRIEFPKFYELIKEdfdfvpkpviKQDDVAAIMYSSGTTGASKgvVLTHRnlI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 229 SSLGLKAKMDAGWTGLQASD-IMWTISDTGWILNILCSLMEPWALGACTFVhlLPKFDPLVILKTLSSYPIKSMMGAPIV 307
Cdd:PLN02574 225 AMVELFVRFEASQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVV--MRRFDASDMVKVIDRFKVTHFPVVPPI 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 308 YRMLLQ--QDLSSYKFPHLQNCVTVGESLLPETLENW-RAQTGLDIRESYGQTET---GLTCMVSKTMKiKPGYMGTAAS 381
Cdd:PLN02574 303 LMALTKkaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTEStavGTRGFNTEKLS-KYSSVGLLAP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 382 CYDVQIID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDII 459
Cdd:PLN02574 382 NMQAKVVDwSTGCLLPPGNCGELWIQ-GP----GVMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEII 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 460 NSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKE-LQQHVKSVTAPYKYPRKIE 538
Cdd:PLN02574 457 KYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQEaVINYVAKQVAPYKKVRKVV 530
|
490 500
....*....|....*....|
3C5E_A 539 FVLNLPKTVTGKIQRAKLRD 558
Cdd:PLN02574 531 FVQSIPKSPAGKILRRELKR 550
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
71-557 |
4.00e-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: 115.22 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 71 ELMWNFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAI 150
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 151 VAGDEVIqevdTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQ-EASAIYFTSGTSGLPKMAEHSY- 228
Cdd:cd05915 101 LFDPNLL----PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 229 ------SSLGLKAKMDAGWTGLQASDI-MWTISdtGWilnilCSLMEPWALGAcTFVHLLPKFDPLVILKTLSSYPIKSM 301
Cdd:cd05915 177 alvlhsLAASLVDGTALSEKDVVLPVVpMFHVN--AW-----CLPYAATLVGA-KQVLPGPRLDPASLVELFDGEGVTFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 302 MGAPIVYRMLLQ-QDLSSYKFPHLQNCVTVGESLlPETLENWRAQTGLDIRESYGQTET---GLTCMVSKTMKIKPGYMG 377
Cdd:cd05915 249 AGVPTVWLALADyLESTGHRLKTLRRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETspvVVQNFVKSHLESLSEEEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 378 TAASCYD-VQIIDDKGNVLPPGT-----EGDIgIRVKPIRPIGIFSGYVDNPDKTAAN-IRGDFWLLGDRGIKDEDGYFQ 450
Cdd:cd05915 328 LTLKAKTgLPIPLVRLRVADEEGrpvpkDGKA-LGEVQLKGPWITGGYYGNEEATRSAlTPDGFFRTGDIAVWDEEGYVE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 451 FMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLasqflsHDPEQLTKELQQHVKSVTAP 530
Cdd:cd05915 407 IKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVP------RGEKPTPEELNEHLLKAGFA 480
|
490 500
....*....|....*....|....*...
3C5E_A 531 YKY-PRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd05915 481 KWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
51-556 |
1.03e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.21 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPALWWvngkGKELMwNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGT 130
Cdd:PRK12316 4559 ERARMTPDAVAVVF----DEEKL-TYAELNRRANRLAHALI-ARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLD 4632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 131 IQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecpslrIKLLVSEKSCDgWLNFkkllneaSTTHHCVETGSQEASA 210
Cdd:PRK12316 4633 PEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDG------LASLALDRDED-WEGF-------PAHDPAVRLHPDNLAY 4698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKMAEHSYSSL-------GLKAKMDAGWTGLQASDIMWTISDTGWilnilcslMEPWALGACTFVHLLPK 283
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGSLvnhlhatGERYELTPDDRVLQFMSFSFDGSHEGL--------YHPLINGASVVIRDDSL 4770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 284 FDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETL-ENWRAQTGLDIRESYGQTETGLT 362
Cdd:PRK12316 4771 WDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYdLAWRALKPVYLFNGYGPTETTVT 4850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 363 CMVSKTMKIKP---GYM--GTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD---- 433
Cdd:PRK12316 4851 VLLWKARDGDAcgaAYMpiGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE-----GVARGYLERPALTAERFVPDpfga 4925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 434 ----FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVkAFVVLASQFL 509
Cdd:PRK12316 4926 pggrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQDPAL 5004
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3C5E_A 510 SHDPE---QLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:PRK12316 5005 ADADEaqaELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
470-550 |
2.15e-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: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 470 EVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTG 549
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
3C5E_A 550 K 550
Cdd:pfam13193 76 K 76
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
205-553 |
2.61e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 111.28 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 205 SQEASAIYFTSGTSGLPKMAEHSYSSLglKAKMDAGWTGLQASDIMWTIsdtgwilnILCSLMEPWALGACTFV------ 278
Cdd:PRK08308 100 AEEPSLLQYSSGTTGEPKLIRRSWTEI--DREIEAYNEALNCEQDETPI--------VACPVTHSYGLICGVLAaltrgs 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 279 --HLLPKFDPLVILKTLSSYPIKSMMGAPIVY----RMLLQQDlssykfpHLQNCVTVGeSLLPET-LENWRAQTgLDIR 351
Cdd:PRK08308 170 kpVIITNKNPKFALNILRNTPQHILYAVPLMLhilgRLLPGTF-------QFHAVMTSG-TPLPEAwFYKLRERT-TYMM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 352 ESYGQTETGltCM-VSKTMKiKPGYMGTAASCYDVQIIDDKGNvlpPGtegDIGIRVKpirpigifsgyvdnpDKTAANi 430
Cdd:PRK08308 241 QQYGCSEAG--CVsICPDMK-SHLDLGNPLPHVSVSAGSDENA---PE---EIVVKMG---------------DKEIFT- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 431 rgdfwllGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAfvvlasQFLS 510
Cdd:PRK08308 296 -------KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVIS 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
3C5E_A 511 H---DPEQLTKELQQHVksvtAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:PRK08308 363 HeeiDPVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSR 404
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
51-558 |
3.03e-26 |
|
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: 112.25 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPewWLV--ILGCIRAGLIFMP 128
Cdd:cd05918 7 ERARSQPDAPAVCAWDGS-----LTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSK--WAVvaMLAVLKAGGAFVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 129 gtiqmksTDILY---RLQmskakaivagdEVIQEVDtvasecpslrIKLLVSekscdgwlnfkkllneastthhcvetgS 205
Cdd:cd05918 79 -------LDPSHplqRLQ-----------EILQDTG----------AKVVLT---------------------------S 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 206 QEASAIY--FTSGTSGLPK--MAEHSYSSLGLKA-----KMDAGWTGLQASDIMWTISdtgwILNILCSLMepwaLGACT 276
Cdd:cd05918 104 SPSDAAYviFTSGSTGKPKgvVIEHRALSTSALAhgralGLTSESRVLQFASYTFDVS----ILEIFTTLA----AGGCL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 277 FVhlLPKFDPLVIL-KTLSSYPIKSMMGAPIVYRMLLQQDlssykFPHLQNCVTVGESLLPETLENWraQTGLDIRESYG 355
Cdd:cd05918 176 CI--PSEEDRLNDLaGFINRLRVTWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTW--ADRVRLINAYG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 356 QTETGLTCMVSK-TMKIKPGYMGTAASCydVQIIDDKGN---VLPPGTEGDI---GirvkPIrpigIFSGYVDNPDKTAA 428
Cdd:cd05918 247 PAECTIAATVSPvVPSTDPRNIGRPLGA--TCWVVDPDNhdrLVPIGAVGELlieG----PI----LARGYLNDPEKTAA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 429 N-IRGDFWLL-------------GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAV---VETAVISSPD 491
Cdd:cd05918 317 AfIEDPAWLKqegsgrgrrlyrtGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGakeVVVEVVKPKD 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3C5E_A 492 PVRGEVVKAFVVLASQFLSHDPEQ------------LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:cd05918 397 GSSSPQLVAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
76-556 |
3.67e-26 |
|
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: 111.19 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyrlqmskakaivagde 155
Cdd:cd17652 15 YAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLP--------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 viqeVDtvaSECPSLRIKLLVSEKSCdgwlnfkkllneastthHCVETGSQEASAIYFTSGTSGLPK--MAEHSysslGL 233
Cdd:cd17652 67 ----LD---PAYPAERIAYMLADARP-----------------ALLLTTPDNLAYVIYTSGSTGRPKgvVVTHR----GL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 234 KAKMDAGWT--GLQASDIMWTISDTGWILNILCSLMepwALGACTFVHLLPKfDPLV----ILKTLSSYPIKSMMGAPIV 307
Cdd:cd17652 119 ANLAAAQIAafDVGPGSRVLQFASPSFDASVWELLM---ALLAGATLVLAPA-EELLpgepLADLLREHRITHVTLPPAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 308 YRMLLQQDLssykfPHLQNCVTVGESLLPETLENWraQTGLDIRESYGQTETGLTCMVSK---TMKIKPgyMGTAASCYD 384
Cdd:cd17652 195 LAALPPDDL-----PDLRTLVVAGEACPAELVDRW--APGRRMINAYGPTETTVCATMAGplpGGGVPP--IGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 385 VQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTA----ANIRGD----FWLLGDRGIKDEDGYFQFMGRAD 456
Cdd:cd17652 266 VYVLDARLRPVPPGVPGEL-----YIAGAGLARGYLNRPGLTAerfvADPFGApgsrMYRTGDLARWRADGQLEFLGRAD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 457 DIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASqflshDPEQLTKELQQHVKSVTAPYKYPRK 536
Cdd:cd17652 341 DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVPAA 415
|
490 500
....*....|....*....|
3C5E_A 537 IEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17652 416 FVVLDALPLTPNGKLDRRAL 435
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
211-550 |
1.02e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 108.62 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPK--MAEH--SYSSLGLKAKMDAGwtglQASDIMWTI----SDTGWILNILCSLME---PWA-----LGA 274
Cdd:cd05924 8 ILYTGGTTGMPKgvMWRQedIFRMLMGGADFGTG----EFTPSEDAHkaaaAAAGTVMFPAPPLMHgtgSWTafgglLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 275 CTFVHLLPKFDPLVILKTLSSYPIKSM------MGAPIV--YRMLLQQDLSSykfphLQNCVTVGESLLPETLENW-RAQ 345
Cdd:cd05924 84 QTVVLPDDRFDPEEVWRTIEKHKVTSMtivgdaMARPLIdaLRDAGPYDLSS-----LFAISSGGALLSPEVKQGLlELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 346 TGLDIRESYGQTETGLT-CMVSKTMKIKPGYMGTAAScyDVQIIDDKGNVLPPGTE--GDIGIR-VKPIrpigifsGYVD 421
Cdd:cd05924 159 PNITLVDAFGSSETGFTgSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGgvGWIARRgHIPL-------GYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 422 NPDKTAANIR---GDFW-LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEV 497
Cdd:cd05924 230 DEAKTAETFPevdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
3C5E_A 498 VKAFVVLASqflSHDPEQltKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGK 550
Cdd:cd05924 310 VVAVVQLRE---GAGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
74-557 |
1.18e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 110.85 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELsensQQAANVLSGAC---GLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDIL-YRLQM----- 144
Cdd:PRK10946 49 FSYREL----NQASDNLACSLrrqGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNaYASQIepall 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 145 --SKAKAIVAGDEVIqevDTVASECPSLRIKLLVSEkscDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPK 222
Cdd:PRK10946 125 iaDRQHALFSDDDFL---NTLVAEHSSLRVVLLLND---DGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 223 MA-----EHSYSslglkakmdagwtgLQAS-DIMWTISDTGWilniLCSL--------MEPWALG---ACTFVHLLPKFD 285
Cdd:PRK10946 199 LIprthnDYYYS--------------VRRSvEICGFTPQTRY----LCALpaahnypmSSPGALGvflAGGTVVLAPDPS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 286 PLVILKTLSSYPIKSMMGAPIVYRMLLQ--------QDLSSYKFphLQncvtVGESLLPETLEnwR---AQTGLDIRESY 354
Cdd:PRK10946 261 ATLCFPLIEKHQVNVTALVPPAVSLWLQaiaeggsrAQLASLKL--LQ----VGGARLSETLA--RripAELGCQLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 355 GQTEtGLtcmVSKT-MKIKPGYMGTAASCY-----DVQIIDDKGNVLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKT 426
Cdd:PRK10946 333 GMAE-GL---VNYTrLDDSDERIFTTQGRPmspddEVWVADADGNPLPQGEVGRLMTR-------GpyTFRGYYKSPQHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 427 AANIRGD-FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA 505
Cdd:PRK10946 402 ASAFDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
3C5E_A 506 SQFlshDPEQLTKEL-QQHVksvtAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:PRK10946 482 EPL---KAVQLRRFLrEQGI----AEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
74-559 |
7.86e-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: 7.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 153
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 DEviQEVD---TVASECPSLRIKLLVSEKSC----DGWLNFKKLLNEASTTHHCVETGSQEA----------SAIYFTSG 216
Cdd:cd17641 91 DE--EQVDkllEIADRIPSVRYVIYCDPRGMrkydDPRLISFEDVVALGRALDRRDPGLYERevaagkgedvAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 217 TSGLPKMA--------EHSYSSLGLKAK---------MDAGWTGLQasdiMWTISD---TGWILNILCS---LMEPWALG 273
Cdd:cd17641 169 TTGKPKLAmlshgnflGHCAAYLAADPLgpgdeyvsvLPLPWIGEQ----MYSVGQalvCGFIVNFPEEpetMMEDLREI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 274 ACTFVHLLPK-FDPL---VILKTLSSYPIKSMM-------------------------------GAPIVYRMLLQQdlss 318
Cdd:cd17641 245 GPTFVLLPPRvWEGIaadVRARMMDATPFKRFMfelgmklglraldrgkrgrpvslwlrlaswlADALLFRPLRDR---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 319 YKFPHLQNCVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIiDDKGNVLppg 398
Cdd:cd17641 321 LGFSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVGEIL--- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 399 tegdigirvkpIRPIGIFSGYVDNPDKTAANIRGDFWLL-GDRGIKDEDGYFQFMGRADDIINSS-GYRIGPSEVENALM 476
Cdd:cd17641 396 -----------VRSPGVFVGYYKNPEATAEDFDEDGWLHtGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 477 EHPAVVETAVISSPDP-------VRGEVV------KAFVVLASQFLSHDPEqLTKELQQHVKSVTAPYKYPRKIEFVLNL 543
Cdd:cd17641 465 FSPYIAEAVVLGAGRPyltaficIDYAIVgkwaeqRGIAFTTYTDLASRPE-VYELIRKEVEKVNASLPEAQRIRRFLLL 543
|
570 580
....*....|....*....|....*
3C5E_A 544 PK---------TVTGKIQRAKLRDK 559
Cdd:cd17641 544 YKeldaddgelTRTRKVRRGVIAEK 568
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
76-556 |
2.26e-24 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 106.24 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagde 155
Cdd:cd17643 15 YGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVP-------IDPAY--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 viqevdtvasecPSLRIKLLV--SEKSCdgwlnfkkLLNEASTThhcvetgsqeASAIYfTSGTSGLPK--MAEHSySSL 231
Cdd:cd17643 72 ------------PVERIAFILadSGPSL--------LLTDPDDL----------AYVIY-TSGSTGRPKgvVVSHA-NVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 232 GLKAKMDAgWTGLQASDIMWTISDTGWILnilcSLMEPW-ALGACTFVHLLPKF---DPLVILKTLSSYPIKSMMGAPIV 307
Cdd:cd17643 120 ALFAATQR-WFGFNEDDVWTLFHSYAFDF----SVWEIWgALLHGGRLVVVPYEvarSPEDFARLLRDEGVTVLNQTPSA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 308 YRMLLQQDLSSYKFPH-LQNCVTVGESLLPETLENWRAQTGL---DIRESYGQTETglTCMVSKTmKIKPGYMGTAA--- 380
Cdd:cd17643 195 FYQLVEAADRDGRDPLaLRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITET--TVHVTFR-PLDAADLPAAAasp 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 381 -----SCYDVQIIDDKGNVLPPGTEGDIGIRvkpiRPiGIFSGYVDNPDKTAANIRGD-FWLLGDRGIKDED-------G 447
Cdd:cd17643 272 igrplPGLRVYVLDADGRPVPPGVVGELYVS----GA-GVARGYLGRPELTAERFVANpFGGPGSRMYRTGDlarrlpdG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 448 YFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdPEQLTKELQQHVKSV 527
Cdd:cd17643 347 ELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG-----AAADIAELRALLKEL 421
|
490 500
....*....|....*....|....*....
3C5E_A 528 TAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17643 422 LPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
75-567 |
7.19e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 105.60 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 75 NFRELSENSQQAANVLSGAcGLQRGDRVAVV---LPRVPEWWLVILGcirAGLIFMPGTIQMKSTDILYRLQMSKAKAIV 151
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWYGIMG---IGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 152 AGDEVIQEVDTVASECPSLRIKLLVSEKS------CDGWLNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE 225
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTDAAhmpqttLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 226 HSYSSLGLKAKM--DAGWTGLQASDIMWTI----SDTGWILNILCSLMepwalGAcTFVHLLPKFDPLVILKTLSSYPIK 299
Cdd:PRK06018 197 YSHRSNVLHALManNGDALGTSAADTMLPVvplfHANSWGIAFSAPSM-----GT-KLVMPGAKLDGASVYELLDTEKVT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 300 SMMGAPIVYRMLLQQ-DLSSYKFPHLqNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVSK----------- 367
Cdd:PRK06018 271 FTAGVPTVWLMLLQYmEKEGLKLPHL-KMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAAlkppfsklpgd 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 368 ---TMKIKPGYmgtAASCYDVQIIDDKGNVLPpgTEGDIGIRVKpIRPIGIFSGYVdnpdKTAANIRGD--FWLLGDRGI 442
Cdd:PRK06018 350 arlDVLQKQGY---PPFGVEMKITDDAGKELP--WDGKTFGRLK-VRGPAVAAAYY----RVDGEILDDdgFFDTGDVAT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 443 KDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTK-ELQ 521
Cdd:PRK06018 420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG------ETATReEIL 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
3C5E_A 522 QHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD--KEWKMSGKA 567
Cdd:PRK06018 494 KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREqfKDYKLPTAA 541
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
69-553 |
3.40e-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: 102.91 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 69 GKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAK 148
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 149 AIVAGDEviqevDTVAsecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIYFTSGTSGLPKMAEHSY 228
Cdd:cd05914 82 AIFVSDE-----DDVA---------------------------------------------LINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 229 SSLglKAKMDAG--WTGLQASDIMWTISDTGWILNILCSLMEPWALGActFVHLLPKFDPLVILKtLSSYPIKSMMGAPI 306
Cdd:cd05914 112 RNI--VSNVDGVkeVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGA--HVVFLDKIPSAKIIA-LAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 307 VYRM--------LLQQDLSSYKFP------------------------HLQNCVTVGESLLPETLENWRaQTGLDIRESY 354
Cdd:cd05914 187 PLVIekifkmdiIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLR-TIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 355 GQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIDDKgnvlPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDF 434
Cdd:cd05914 266 GMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP-----NVMKGYYKNPEATAEAFDKDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 435 WL-LGDRGIKDEDGYFQFMGRADD-IINSSGYRIGPSEVENALMEHPAVVETAVIsspdpVRGEVVKAFVVLASQFL--- 509
Cdd:cd05914 337 WFhTGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFLdvk 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
3C5E_A 510 ----SHDPEQLTKELQQHVKSVTAPYKYPRKIEFVL-NLPKTVTGKIQR 553
Cdd:cd05914 412 alkqRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVKeEFEKTPKGKIKR 460
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
211-561 |
4.34e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 103.18 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWtisdtgwilniLC-------SLMEPW--ALGACTFVHLL 281
Cdd:PRK13388 155 LIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCY-----------VSmplfhsnAVMAGWapAVASGAAVALP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 282 PKFDPLVILKTLSSYPIKSM--MGAPIVYRMLlqqdlSSYKFPHLQNCVTV--GESLLPETLENWRAQTGLDIRESYGQT 357
Cdd:PRK13388 224 AKFSASGFLDDVRRYGATYFnyVGKPLAYILA-----TPERPDDADNPLRVafGNEASPRDIAEFSRRFGCQVEDGYGSS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 358 ETGltCMVSKTMKIKPGYMGTAAScyDVQIID-DKGNVLPPGTEGDIGIRVKPIRPIG---------IFSGYVDNPDKTA 427
Cdd:PRK13388 299 EGA--VIVVREPGTPPGSIGRGAP--GVAIYNpETLTECAVARFDAHGALLNADEAIGelvntagagFFEGYYNNPEATA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 428 ANIR-GDFWLlGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAs 506
Cdd:PRK13388 375 ERMRhGMYWS-GDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLR- 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
3C5E_A 507 QFLSHDPEQLTKELqqHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 561
Cdd:PRK13388 453 DGATFDPDAFAAFL--AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGW 505
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
74-558 |
5.51e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 102.86 E-value: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLsGACGLQRGDRVAVVL---PRVPEWWLVILGCIRAGLIFMPgtiqmkstdilyRLQMSKAKAI 150
Cdd:PRK07008 40 YTYRDCERRAKQLAQAL-AALGVEPGDRVGTLAwngYRHLEAYYGVSGSGAVCHTINP------------RLFPEQIAYI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 151 V--AGDEVI-------QEVDTVASECPSLRIKLLVSEKS---CDG--WLNFKKLLNEASTTHHCVETGSQEASAIYFTSG 216
Cdd:PRK07008 107 VnhAEDRYVlfdltflPLVDALAPQCPNVKGWVAMTDAAhlpAGStpLLCYETLVGAQDGDYDWPRFDENQASSLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 217 TSGLPKMAEHSYSSLGLKAKM----DAgwTGLQASDI------MWTISdtGWILNILCslmepwALGACTFVHLLPKFDP 286
Cdd:PRK07008 187 TTGNPKGALYSHRSTVLHAYGaalpDA--MGLSARDAvlpvvpMFHVN--AWGLPYSA------PLTGAKLVLPGPDLDG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 287 LVILKTLSSYPIKSMMGAPIVYRMLLQQ-DLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTET---GLT 362
Cdd:PRK07008 257 KSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMsplGTL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 363 C-MVSKTMKIKPG-------YMGTAASCYDVQIIDDKGNVLP--PGTEGDIGIRvkpirpiG--IFSGYVdnpdKTAANI 430
Cdd:PRK07008 337 CkLKWKHSQLPLDeqrklleKQGRVIYGVDMKIVGDDGRELPwdGKAFGDLQVR-------GpwVIDRYF----RGDASP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 431 RGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFl 509
Cdd:PRK07008 406 LVDGWFpTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA- 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3C5E_A 510 shdpeQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK07008 485 -----EVTReELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
30-556 |
9.42e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.50 E-value: 9.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 30 HQEVPAKFN-----FASDVLDHWADMEKAGKRPPSPALWWvngkGKELMwNFRELSENSQQAANVLSgACGLQRGDRVAV 104
Cdd:PRK12316 1985 RQRILADWDrtpeaYPRGPGVHQRIAEQAARAPEAIAVVF----GDQHL-SYAELDSRANRLAHRLR-ARGVGPEVRVAI 2058
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 105 VLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAkAIVAGDEVIQEVDTVASECPSLRIkllvsekSCDGW 184
Cdd:PRK12316 2059 AAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGA-ALLLTQRHLLERLPLPAGVARLPL-------DRDAE 2130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 185 LNfkkllnEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-------GLKAKMDAGWTGLQASDIMWTISDTG 257
Cdd:PRK12316 2131 WA------DYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALvahcqaaGERYELSPADCELQFMSFSFDGAHEQ 2204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 258 WilnilcslMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPE 337
Cdd:PRK12316 2205 W--------FHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAA 2276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 338 TLEN-WRAQTGLDIRESYGQTETGLTCMVSKTMKIKPG---YM--GTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpir 411
Cdd:PRK12316 2277 SLRLaWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgaaYVpiGRALGNRRAYILDADLNLLAPGMAGELYLGGE--- 2353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 412 piGIFSGYVDNPDKTA--------ANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVE 483
Cdd:PRK12316 2354 --GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVRE 2431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3C5E_A 484 TAVISSpDPVRGEVVKAFVVlasqflSHDP-EQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:PRK12316 2432 AVVVAQ-DGASGKQLVAYVV------PDDAaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
76-556 |
1.05e-22 |
|
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: 101.24 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagde 155
Cdd:cd12115 27 YAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP-------LDPAY--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 viqevdtvasecPSLRIKLLVSEKSCdgwlnfkkllneastthHCVETGSQEASAIYFTSGTSGLPK--MAEHSysslGL 233
Cdd:cd12115 84 ------------PPERLRFILEDAQA-----------------RLVLTDPDDLAYVIYTSGSTGRPKgvAIEHR----NA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 234 KAKMDagWTG-----------LQASDIMWTISdtgwILNILCSLMEpwalGACtfVHLLpkfDPLVILKTLSSYPIKSMM 302
Cdd:cd12115 131 AAFLQ--WAAaafsaeelagvLASTSICFDLS----VFELFGPLAT----GGK--VVLA---DNVLALPDLPAAAEVTLI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 303 GA-PIVYRMLLQQDlssyKFPHLQNCVTV-GESLLPETLENWRAQTGLD-IRESYGQTET---GLTCMVSKTMKIKPGyM 376
Cdd:cd12115 196 NTvPSAAAELLRHD----ALPASVRVVNLaGEPLPRDLVQRLYARLQVErVVNLYGPSEDttySTVAPVPPGASGEVS-I 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 377 GTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTAANIRGD-------FWLLGDRGIKDEDGYF 449
Cdd:cd12115 271 GRPLANTQAYVLDRALQPVPLGVPGEL-----YIGGAGVARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 450 QFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqfLSHDPEQLTKELQQHVKSVTA 529
Cdd:cd12115 346 EFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV-----AEPGAAGLVEDLRRHLGTRLP 420
|
490 500
....*....|....*....|....*..
3C5E_A 530 PYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd12115 421 AYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
211-553 |
1.18e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 102.13 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKMAEHSYSS--LGLKAKmdagWTGLQASD---IMWTISDTGWIL--NILCSLMepwALGaCTFVH---- 279
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNGPhlVGLKYY----WRSIIEKDiptVVFSHSSIGWVSfhGFLYGSL---SLG-NTFVMfegg 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 280 -LLPKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQD------LSSYKFPHLQNCVTVGESL---LPETLENwraqtGLD 349
Cdd:PTZ00237 331 iIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIeesIPEYIEN-----KLK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 350 IRES--YGQTETGLTCMVSKTMKIKPGY-MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVkPIRPiGIFSGYVDNPD-- 424
Cdd:PTZ00237 406 IKSSrgYGQTEIGITYLYCYGHINIPYNaTGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPP-SFATTFYKNDEkf 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 425 KTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVL 504
Cdd:PTZ00237 484 KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVL 563
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
3C5E_A 505 ASQFLSH--DPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQR 553
Cdd:PTZ00237 564 KQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
74-556 |
1.64e-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: 100.81 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAG 153
Cdd:cd12114 13 LTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 DEViqevdtvASECPSLRIKLLVSEKSCDGWLNFKKllneastthhcVETGSQEASAIYFTSGTSGLPK--MAEHSySSL 231
Cdd:cd12114 92 GPD-------AQLDVAVFDVLILDLDALAAPAPPPP-----------VDVAPDDLAYVIFTSGSTGTPKgvMISHR-AAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 232 GLKAKMDAGWtGLQASDIMWTISDTGWILNILcSLMEPWALGAcTFVhlLP----KFDPLVILKTLSSYPIKSMMGAPIV 307
Cdd:cd12114 153 NTILDINRRF-AVGPDDRVLALSSLSFDLSVY-DIFGALSAGA-TLV--LPdearRRDPAHWAELIERHGVTLWNSVPAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 308 YRMLLQQDLSSYKFPHLQNCVTVGESL----LPETLenWRAQTGLDIRESYGQTETGLTCMVSKTMKIKP-------GYM 376
Cdd:cd12114 228 LEMLLDVLEAAQALLPSLRLVLLSGDWipldLPARL--RALAPDARLISLGGATEASIWSIYHPIDEVPPdwrsipyGRP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 377 GTAASCYdvqIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTAA-----NIRGDFWLLGDRGIKDEDGYFQF 451
Cdd:cd12114 306 LANQRYR---VLDPRGRDCPDWVPGELWIG-----GRGVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGTLEF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 452 MGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPvRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSvtapY 531
Cdd:cd12114 378 LGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPA----Y 452
|
490 500
....*....|....*....|....*
3C5E_A 532 KYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd12114 453 MIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
84-558 |
2.90e-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: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 84 QQAANVLSG--ACGLQRGDRVAVVLPR----VPEWWlvilGCIRAGLIFMPGTIQMKSTDI------LYRL-QMSKAKAI 150
Cdd:cd05906 47 EDARRLAAGlrQLGLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPTYDEPnarlrkLRHIwQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 151 VAGDEVIQEVDTVASECPSLRIKLLVSEkscdgwlnfkkLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSS 230
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIE-----------ELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 231 LgLKAKMDAGWT-GLQASDImwtisdtgwILNilcslmepWA----LGACTFVHLLPKF---------------DPLVIL 290
Cdd:cd05906 192 I-LARSAGKIQHnGLTPQDV---------FLN--------WVpldhVGGLVELHLRAVYlgcqqvhvpteeilaDPLRWL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 291 KTLSSYPIkSMMGAP-IVYRMLLQQ---------DLSSYKFphlqnCVTVGESLLPETLENWR---AQTGLD---IRESY 354
Cdd:cd05906 254 DLIDRYRV-TITWAPnFAFALLNDLleeiedgtwDLSSLRY-----LVNAGEAVVAKTIRRLLrllEPYGLPpdaIRPAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 355 GQTETGLTCMVSKTMkikPGYMGTAA-------SCY---DVQIIDDKGNVLPPGTEGDIGIRVKPIrpigiFSGYVDNPD 424
Cdd:cd05906 328 GMTETCSGVIYSRSF---PTYDHSQAlefvslgRPIpgvSMRIVDDEGQLLPEGEVGRLQVRGPVV-----TKGYYNNPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 425 KTAANIRGDFWL-LGDRGIKDeDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVE--TAVISSPDPVRGEVVKAF 501
Cdd:cd05906 400 ANAEAFTEDGWFrTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAI 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
3C5E_A 502 VVLASQFLSHDPEQLTKELQQHVK---SVTAPYKYP-RKIEFvlnlPKTVTGKIQRAKLRD 558
Cdd:cd05906 479 FFVPEYDLQDALSETLRAIRSVVSrevGVSPAYLIPlPKEEI----PKTSLGKIQRSKLKA 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
26-556 |
7.53e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 100.80 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 26 LQWGHQEVPAKFNFASDVLDHWADMEKAGkrPPSPALwwVNGkgkELMWNFRELSENSQQAANVLSgACGLQRGDRVAVV 105
Cdd:PRK12316 496 LVEGWNATAAEYPLQRGVHRLFEEQVERT--PEAPAL--AFG---EETLDYAELNRRANRLAHALI-ERGVGPDVLVGVA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 106 LPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVA----GDE--VIQEVDTVASECPSLrikllvsek 179
Cdd:PRK12316 568 MERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSqshlGRKlpLAAGVQVLDLDRPAA--------- 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 180 scdgWLNFKKllNEASTTHHCVEtgsQEASAIYfTSGTSGLPKMAEHSYSSLglKAKMDAGWT--GLQASDIMWTISDTG 257
Cdd:PRK12316 639 ----WLEGYS--EENPGTELNPE---NLAYVIY-TSGSTGKPKGAGNRHRAL--SNRLCWMQQayGLGVGDTVLQKTPFS 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 258 WILNILcslMEPWALGACTFVHLLPK---FDPLVILKTLSSYPIKSMMGAPIVYRMLLQ----QDLSSykfphLQNCVTV 330
Cdd:PRK12316 707 FDVSVW---EFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQdedvASCTS-----LRRIVCS 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 331 GESL---LPETLENWRAQTGLdiRESYGQTETGL-----TCMVSKTMKIKPGYMGTAASCYdvqIIDDKGNVLPPGTEGD 402
Cdd:PRK12316 779 GEALpadAQEQVFAKLPQAGL--YNLYGPTEAAIdvthwTCVEEGGDSVPIGRPIANLACY---ILDANLEPVPVGVLGE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 403 IGIRVKpirpiGIFSGYVDNPDKTA----ANIRGD---FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENAL 475
Cdd:PRK12316 854 LYLAGR-----GLARGYHGRPGLTAerfvPSPFVAgerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 928
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 476 MEHPAVVETAVISspdpVRGEVVKAFVVLasqflsHDPEQLTKE-LQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRA 554
Cdd:PRK12316 929 LEHPWVREAAVLA----VDGKQLVGYVVL------ESEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRK 998
|
..
3C5E_A 555 KL 556
Cdd:PRK12316 999 AL 1000
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
74-556 |
7.55e-22 |
|
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: 98.40 E-value: 7.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGaCGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVag 153
Cdd:cd17645 24 LTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 deviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcveTGSQEASAIYFTSGTSGLPK--MAEH-SYSS 230
Cdd:cd17645 101 -------------------------------------------------TNPDDLAYVIYTSGSTGLPKgvMIEHhNLVN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 231 LGLKAKMDAGWTGLQASDIMWTISDTGWILNILCSlmepWALGACtfVHLLPKFDPLVILK----------TLSSYPIKs 300
Cdd:cd17645 132 LCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPH----LTAGAA--LHVVPSERRLDLDAlndyfnqegiTISFLPTG- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 301 mmgapiVYRMLLQQDLSSykfphLQNCVTVGESLlpetleNWRAQTGLDIRESYGQTEtgltCMVSKTM-KIKPGY---- 375
Cdd:cd17645 205 ------AAEQFMQLDNQS-----LRVLLTGGDKL------KKIERKGYKLVNNYGPTE----NTVVATSfEIDKPYanip 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 376 MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDFWLLGDRGIKD-------EDGY 448
Cdd:cd17645 264 IGKPIDNTRVYILDEALQLQPIGVAGELCIAGE-----GLARGYLNRPELTAEKFIVHPFVPGERMYRTgdlakflPDGN 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 449 FQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQFlshDPEqltkELQQHVKSVT 528
Cdd:cd17645 339 IEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEI---PHE----ELREWLKNDL 411
|
490 500
....*....|....*....|....*...
3C5E_A 529 APYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17645 412 PDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
53-558 |
1.16e-21 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 98.85 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 53 AGKRPPSPALWWVN-GKGKELMWNFRELSENSQQAANVLSGACGlqRGDRVAVVLPRVPEWWLVILGCIRAGLI----FM 127
Cdd:cd05931 3 AAARPDRPAYTFLDdEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIavplPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 128 PGtiqmkSTDILYRLQ----MSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKScdgwlnfkkLLNEASTTHHCVET 203
Cdd:cd05931 81 PT-----PGRHAERLAailaDAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDL---------LPDTSAADWPPPSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 204 GSQEASAIYFTSGTSGLPKMAEHSYSSLG--LKAkMDAGWtGLQASDIM--W--TISDTGWILNIL--------CSLMEP 269
Cdd:cd05931 147 DPDDIAYLQYTSGSTGTPKGVVVTHRNLLanVRQ-IRRAY-GLDPGDVVvsWlpLYHDMGLIGGLLtplysggpSVLMSP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 270 WAlgactFVHllpkfDPLVILKTLSSYPIkSMMGAP------IVYRMLLQQ----DLSSykfphLQNCVTVGESLLPETL 339
Cdd:cd05931 225 AA-----FLR-----RPLRWLRLISRYRA-TISAAPnfaydlCVRRVRDEDleglDLSS-----WRVALNGAEPVRPATL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 340 ENWR---AQTGLD---IRESYGQTETglTCMVSkTMKIKPGY-----------------------------MGTAASCYD 384
Cdd:cd05931 289 RRFAeafAPFGFRpeaFRPSYGLAEA--TLFVS-GGPPGTGPvvlrvdrdalagravavaaddpaarelvsCGRPLPDQE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 385 VQIIDDKGN-VLPPGTEGDIGIRvkpirpiG--IFSGYVDNPDKTA------ANIRGDFWL-LGDRGIKDeDGYFQFMGR 454
Cdd:cd05931 366 VRIVDPETGrELPDGEVGEIWVR-------GpsVASGYWGRPEATAetfgalAATDEGGWLrTGDLGFLH-DGELYITGR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 455 ADDIINSSGYRIGPSEVENALME-HPAVVET--AVISSPDPVRGEVVkAFVVLASQFLSHDPEQLTKELQQHVKS---VT 528
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATAEEaHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA 516
|
570 580 590
....*....|....*....|....*....|..
3C5E_A 529 apykyPRKIEFVLN--LPKTVTGKIQRAKLRD 558
Cdd:cd05931 517 -----PADVVLVRPgsIPRTSSGKIQRRACRA 543
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
211-556 |
5.09e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 96.60 E-value: 5.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 211 IYFTSGTSGLPKmaehsysSLGLKAKMDAGwTGLQASDIMWTISDTGWILNI---------LCSLMEPWALGACTFVHll 281
Cdd:PRK13383 179 VLLTSGTTGKPK-------GVPRAPQLRSA-VGVWVTILDRTRLRTGSRISVampmfhglgLGMLMLTIALGGTVLTH-- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 282 PKFDPLVILKTLSSYPIKSMMGAPIVYRMLLQ---QDLSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTE 358
Cdd:PRK13383 249 RHFDAEAALAQASLHRADAFTAVPVVLARILElppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 359 TGLTCMVSKT-MKIKPGYMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRpigifSGYVDNPDKtaANIRGdFWLL 437
Cdd:PRK13383 329 VGIGALATPAdLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAG-----TRYTDGGGK--AVVDG-MTST 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 438 GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQfLSHDPEQlt 517
Cdd:PRK13383 401 GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQ-- 477
|
330 340 350
....*....|....*....|....*....|....*....
3C5E_A 518 keLQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:PRK13383 478 --LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
74-556 |
1.71e-20 |
|
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: 94.46 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKaivag 153
Cdd:cd17656 14 LTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVR----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 deviqevdtvasecpslrikLLVSEKSCDGWLNFKK--------LLNEASTTHHCVETGSQEASAIYFTSGTSGLPK--M 223
Cdd:cd17656 88 --------------------VVLTQRHLKSKLSFNKstilledpSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKgvQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 224 AEHSySSLGL------KAKMDAGWTGLQASDIMWTISDTGwILNILCSlmepwalGACtfVHLLPK-----FDPLVILkt 292
Cdd:cd17656 148 LEHK-NMVNLlhfereKTNINFSDKVLQFATCSFDVCYQE-IFSTLLS-------GGT--LYIIREetkrdVEQLFDL-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 293 LSSYPIKSMmgapIVYRMLLQQDLSSYKF-PHLQNCV----TVGESL-LPETLENWRAQTGLDIRESYGQTETGL--TCM 364
Cdd:cd17656 215 VKRHNIEVV----FLPVAFLKFIFSEREFiNRFPTCVkhiiTAGEQLvITNEFKEMLHEHNVHLHNHYGPSETHVvtTYT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 365 VSKTMKIkPGY--MGTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTA---------ANIRgd 433
Cdd:cd17656 291 INPEAEI-PELppIGKPISNTWIYILDQEQQLQPQGIVGEL-----YISGASVARGYLNRQELTAekffpdpfdPNER-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 434 FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflshdP 513
Cdd:cd17656 363 MYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---------M 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
3C5E_A 514 EQL--TKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17656 434 EQElnISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
201-556 |
2.78e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.79 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 201 VETGSQEASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILcSLMEPWALGACTFVHL 280
Cdd:PRK12316 3191 IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVE-ELFWPLMSGARVVLAG 3269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 281 LPKF-DPLVILKTLSSYPIKSMMGAPIVYRMLLQqDLSSYKFPHLQNCVTVGESLLPETLENWRAqtGLDIRESYGQTET 359
Cdd:PRK12316 3270 PEDWrDPALLVELINSEGVDVLHAYPSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEA 3346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 360 GLTCMVSKTMKIKPGY--MGTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTAANIRGDFWLL 437
Cdd:PRK12316 3347 TITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGEL-----YLGGEGLARGYHNRPGLTAERFVPDPFVP 3421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 438 GDRGIKD-------EDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISspdpVRGEVVKAFVVLASQfls 510
Cdd:PRK12316 3422 GERLYRTgdlaryrADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE--- 3494
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
3C5E_A 511 hdPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:PRK12316 3495 --AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
117-556 |
2.79e-20 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 94.19 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 117 LGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAgdevIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEAST 196
Cdd:PRK04813 70 LGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIA----TEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 197 THhcvetgsqeasaIYFTSGTSGLPKMAEHSYSSLglkakmdagwtglqasdimwtISDTGWILN---------IL---- 263
Cdd:PRK04813 146 YY------------IIFTSGTTGKPKGVQISHDNL---------------------VSFTNWMLEdfalpegpqFLnqap 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 264 ----CSLMEpW----ALGAcTFVhLLPK---FDPLVILKTLSSYPIKSMMGAPIVYRM-LLQQDLSSYKFPHLQNCVTVG 331
Cdd:PRK04813 193 ysfdLSVMD-LyptlASGG-TLV-ALPKdmtANFKQLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 332 ESLLPETlenwrAQTGLD------IRESYGQTETglTCMVSK---TMKIKPGY----MGTAASCYDVQIIDDKGNVLPPG 398
Cdd:PRK04813 270 EELPHKT-----AKKLLErfpsatIYNTYGPTEA--TVAVTSieiTDEMLDQYkrlpIGYAKPDSPLLIIDEEGTKLPDG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 399 TEGDIGIrvkpirpIG--IFSGYVDNPDKTAANirgdFWLL--------GDRGIKDeDGYFQFMGRADDIINSSGYRIGP 468
Cdd:PRK04813 343 EQGEIVI-------SGpsVSKGYLNNPEKTAEA----FFTFdgqpayhtGDAGYLE-DGLLFYQGRIDFQIKLNGYRIEL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 469 SEVENALMEHPAVVETAVIsspdPV-RGEVVK---AFVVLASqflsHDPE---QLTKELQQHVKSVTAPYKYPRKIEFVL 541
Cdd:PRK04813 411 EEIEQNLRQSSYVESAVVV----PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRD 482
|
490
....*....|....*
3C5E_A 542 NLPKTVTGKIQRAKL 556
Cdd:PRK04813 483 SLPLTPNGKIDRKAL 497
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
76-556 |
9.30e-20 |
|
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: 92.08 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRvPEWWLV-ILGCIRAGLIFMPgtiqmksTDILYrlqmskakaivagd 154
Cdd:cd17648 15 YRELNERANRLAHYLLSVAEIRPDDLVGLVLDK-SELMIIaILAVWKAGAAYVP-------IDPSY-------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 155 eviqevdtvasecPSLRIKLLVSEkscdgwlnfkkllneasTTHHCVETGSQEASAIYFTSGTSGLPK--MAEHSySSLG 232
Cdd:cd17648 73 -------------PDERIQFILED-----------------TGARVVITNSTDLAYAIYTSGTTGKPKgvLVEHG-SVVN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 233 LKAKMDAGWtGLQASDIMWTISDTGWILNILCSLMEPWALGACTFVHLLP--KFDPLVILKTLSSYPIKSMMGAPIVyrm 310
Cdd:cd17648 122 LRTSLSERY-FGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDemRFDPDRFYAYINREKVTYLSGTPSV--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 311 lLQQ-DLSSykFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYGQTETGLTCMVS-------KTMKIKPGYMGTAasC 382
Cdd:cd17648 198 -LQQyDLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRffpgdqrFDKSLGRPVRNTK--C 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 383 YdvqIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTA----AN--------IRGDFWLL---GDRGIKDEDG 447
Cdd:cd17648 273 Y---VLNDAMKRVPVGAVGEL-----YLGGDGVARGYLNRPELTAerflPNpfqteqerARGRNARLyktGDLVRWLPSG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 448 YFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRG-EVVKAFVVlasQFLSHDPEQLTK-ELQQHVK 525
Cdd:cd17648 345 ELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAqSRIQKYLV---GYYLPEPGHVPEsDLLSFLR 421
|
490 500 510
....*....|....*....|....*....|.
3C5E_A 526 SVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17648 422 AKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
50-556 |
5.46e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 90.45 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 50 MEKAGKRPPSPALWWVNGKGKelmWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPG 129
Cdd:PRK05857 21 FEQARQQPEAIALRRCDGTSA---LRYRELVAEVGGLAADLR-AQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 130 TIQMKSTDILYRLQMSKAKAIVAGDEV---IQEVDTVASECPSLRIKLL--VSEKSCDGWLNFKKLLneastthhcVETG 204
Cdd:PRK05857 97 DGNLPIAAIERFCQITDPAAALVAPGSkmaSSAVPEALHSIPVIAVDIAavTRESEHSLDAASLAGN---------ADQG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 205 SQEASAIYFTSGTSGLPK---MAEHSYSSLG--LKAK---------MDAGWTGLQASDI--MWtisdtgWILNilcSLME 268
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKavlLANRTFFAVPdiLQKEglnwvtwvvGETTYSPLPATHIggLW------WILT---CLMH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 269 PwalGACtfvhLLPKFDPLVILKTLSSYPIKSMMGAP-IVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAqTG 347
Cdd:PRK05857 239 G---GLC----VTGGENTTSLLEILTTNAVATTCLVPtLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEA-TG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 348 LDIRESYGQTETGLTCMVSKT-----MKIKPGYMGTAASCYDVQIID-DKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVD 421
Cdd:PRK05857 311 VRTAQVYGLSETGCTALCLPTddgsiVKIEAGAVGRPYPGVDVYLAAtDGIGPTAPGAGPSASFGTLWIKSPANMLGYWN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 422 NPDKTAaNIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKA 500
Cdd:PRK05857 391 NPERTA-EVLIDGWVnTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGL 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
3C5E_A 501 FVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:PRK05857 470 AVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
41-486 |
6.52e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 90.32 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 41 SDVLDHWADmekagKRPPSPALwwvNGKGKELmwNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCI 120
Cdd:PRK08279 40 GDVFEEAAA-----RHPDRPAL---LFEDQSI--SYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 121 RAGLIF-MPGTIQMKstDIL-YRLQMSKAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCD---GWLNFKKLLNEAS 195
Cdd:PRK08279 109 KLGAVVaLLNTQQRG--AVLaHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDdpeGYEDLAAAAAGAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 196 TTHHCVETGSQ-EASAIY-FTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASDIMWTI----SDTGwiLNI-LCSLMe 268
Cdd:PRK08279 187 TTNPASRSGVTaKDTAFYiYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCClplyHNTG--GTVaWSSVL- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 269 pwaLGACTFVhLLPKFD-----PLVILK--TLssypiksmmgapIVY-----RMLLQQDLSSYKFPHLQNCVtVGESLLP 336
Cdd:PRK08279 264 ---AAGATLA-LRRKFSasrfwDDVRRYraTA------------FQYigelcRYLLNQPPKPTDRDHRLRLM-IGNGLRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 337 ETLENWRAQTGLD-IRESYGQTE--TGLTCM--VSKTMKIKPGYMGTAASC--YDVQ----IIDDKGNVLPPGTeGDIGI 405
Cdd:PRK08279 327 DIWDEFQQRFGIPrILEFYAASEgnVGFINVfnFDGTVGRVPLWLAHPYAIvkYDVDtgepVRDADGRCIKVKP-GEVGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 406 RVKPIRPIGIFSGYVDnPDKTAANI------RGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEH 478
Cdd:PRK08279 406 LIGRITDRGPFDGYTD-PEASEKKIlrdvfkKGDAWFnTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGF 484
|
....*...
3C5E_A 479 PAVVETAV 486
Cdd:PRK08279 485 PGVEEAVV 492
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
200-558 |
8.85e-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: 89.31 E-value: 8.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 200 CVETGSQEASAIYFTSGTSGLPKMAEHSYSSL-----GLKAKMDAgwtglQASDIMwtisdtgwiLNIL---------CS 265
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLlanveQITAIFDP-----NPEDVV---------FGALpffhsfgltGC 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 266 LMEPWALGACTFVHllpkFDPL---VILKTLSSYPIKSMMGAPIVYRMLLQQdLSSYKFPHLQNCVTVGESLLPETLENW 342
Cdd:cd05909 207 LWLPLLSGIKVVFH----PNPLdykKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEF 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 343 RAQTGLDIRESYGQTETGLTCMVSK-TMKIKPGYMGTAASCYDVQIIDDKGNV-LPPGTEGDIGIRvkpirpiG--IFSG 418
Cdd:cd05909 282 QEKFGIRILEGYGTTECSPVISVNTpQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVR-------GpnVMLG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 419 YVDNPDKTAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEH-PAVVETAVISSPDPVRGEV 497
Cdd:cd05909 355 YLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
3C5E_A 498 VKAFVVLasqflsHDPEQLtkELQQHVKSVTAPYKY-PRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:cd05909 435 IVLLTTT------TDTDPS--SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
76-556 |
4.13e-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: 87.73 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEW---W--LVILGCIRAgliFMPGTIQMKStdILYRLQMSKAKAI 150
Cdd:cd05938 8 YRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWlgLAKLGCPVA---FLNTNIRSKS--LLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 151 VAGDEVIQEVDTVaseCPSLR-----IKLLVSEKSCDGWLNFKKLLNEASTT-----HHCVETGSQEASAIYfTSGTSGL 220
Cdd:cd05938 83 VVAPELQEAVEEV---LPALRadgvsVWYLSHTSNTEGVISLLDKVDAASDEpvpasLRAHVTIKSPALYIY-TSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 221 PKMAEHSYsslgLKAKMDAGWT---GLQASDIMWTI----SDTGWILNILCSLmepwALGAcTFVhLLPKFDPLVILKTL 293
Cdd:cd05938 159 PKAARISH----LRVLQCSGFLslcGVTADDVIYITlplyHSSGFLLGIGGCI----ELGA-TCV-LKPKFSASQFWDDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 294 SSYPIKSMMGAPIVYRMLLQQDLSSYKFPHLQNcVTVGESLLPETLENWRAQTG-LDIRESYGQTEtGLTCMVSKTMKIk 372
Cdd:cd05938 229 RKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVR-LAIGNGLRADVWREFLRRFGpIRIREFYGSTE-GNIGFFNYTGKI- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 373 pGYMGTaASC------------YDVQ----IIDDKGNVLPPGTeGDIGIRVKPIRPIGIFSGYVDNP----DKTAANI-- 430
Cdd:cd05938 306 -GAVGR-VSYlykllfpfelikFDVEkeepVRDAQGFCIPVAK-GEPGLLVAKITQQSPFLGYAGDKeqteKKLLRDVfk 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 431 RGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLAsqf 508
Cdd:cd05938 383 KGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPgHEGRIGMAAVKLK--- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
3C5E_A 509 lshDPEQLT-KELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd05938 460 ---PGHEFDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
336-558 |
1.33e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.43 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 336 PETLENWRaQTGLDIRESYGQTETGltcmvSKTMKIKPG-YMGTAASCydvqiiddkGNVLPPGTegdIGIRVKPIRPIG 414
Cdd:PRK07445 244 PSLLEQAR-QLQLRLAPTYGMTETA-----SQIATLKPDdFLAGNNSS---------GQVLPHAQ---ITIPANQTGNIT 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 415 I-----FSGYVdnPDKTAANIrgdFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISS 489
Cdd:PRK07445 306 IqaqslALGYY--PQILDSQG---IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGL 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3C5E_A 490 PDPVRGEVVKAFVVLAsqflshDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRD 558
Cdd:PRK07445 381 PDPHWGEVVTAIYVPK------DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
305-556 |
1.98e-17 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 85.18 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 305 PIVYRMLLQQDLSSYKFP---HLQNCVTVGESLLPETLENWRAQTGLDIR--ESYGQTETGLTCMVS-----KTMKIKPG 374
Cdd:cd17644 204 PPAYWHLLVLELLLSTIDlpsSLRLVIVGGEAVQPELVRQWQKNVGNFIQliNVYGPTEATIAATVCrltqlTERNITSV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 375 YMGTAASCYDVQIIDDKGNVLPPGTEGDIgirvkPIRPIGIFSGYVDNPDKTAANIRGD---------FWLLGDRGIKDE 445
Cdd:cd17644 284 PIGRPIANTQVYILDENLQPVPVGVPGEL-----HIGGVGLARGYLNRPELTAEKFISHpfnsseserLYKTGDLARYLP 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 446 DGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVlasqflSHDPEQ-LTKELQQHV 524
Cdd:cd17644 359 DGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV------PHYEESpSTVELRQFL 432
|
250 260 270
....*....|....*....|....*....|..
3C5E_A 525 KSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17644 433 KAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
50-559 |
2.35e-17 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 85.52 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 50 MEKAGKRPPSPALWWVNGKGKELMWNF---RELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIF 126
Cdd:PLN03052 182 TPKPSKTDDSIAIIWRDEGSDDLPVNRmtlSELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 127 MPGTIQMKSTDILYRLQMSKAKA------IVAGDEVIQEVDTVASECPSLRIKLLVSEKSC-----DGWLNFKKLLNEAS 195
Cdd:PLN03052 261 VSIADSFAPSEIATRLKISKAKAiftqdvIVRGGKSIPLYSRVVEAKAPKAIVLPADGKSVrvklrEGDMSWDDFLARAN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 196 TTHHCVETGSQEASA-----IYFTSGTSGLPKMAEHSYSSlGLKAKMDAgWTGL--QASDIMWTISDTGWilnilcsLME 268
Cdd:PLN03052 341 GLRRPDEYKAVEQPVeaftnILFSSGTTGEPKAIPWTQLT-PLRAAADA-WAHLdiRKGDIVCWPTNLGW-------MMG 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 269 PWALGACtfvhllpkfdpLVILKTLSSY---PIKS------------MMGA--PIVYRMLLQQDLSSYKFPHLQNCVTVG 331
Cdd:PLN03052 412 PWLVYAS-----------LLNGATLALYngsPLGRgfakfvqdakvtMLGTvpSIVKTWKNTNCMAGLDWSSIRCFGSTG 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 332 E-SLLPETLenW---RAQTGlDIRESYGQTETGlTCMVSKTMkIKP---GYMGTAASCYDVQIIDDKGNVLP---PGTeG 401
Cdd:PLN03052 481 EaSSVDDYL--WlmsRAGYK-PIIEYCGGTELG-GGFVTGSL-LQPqafAAFSTPAMGCKLFILDDSGNPYPddaPCT-G 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 402 DIGIRVKpirpigIF--SGYVDNPDKTAANIRG-DFW---LL---GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVE 472
Cdd:PLN03052 555 ELALFPL------MFgaSSTLLNADHYKVYFKGmPVFngkILrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 473 ---NALmeHPAVVETAVISSPDPVRG--EVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTV 547
Cdd:PLN03052 629 rvcNAA--DESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTA 706
|
570
....*....|..
3C5E_A 548 TGKIQRAKLRDK 559
Cdd:PLN03052 707 SNKVMRRVLRQQ 718
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
74-557 |
2.58e-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: 84.78 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAg 153
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 154 dEVIQEVDTVASECPslrikllvseKSCDGwLNFKKLLneastthhcvetgsqeaSAIYfTSGTSGLPKMA--EHS--YS 229
Cdd:cd05939 82 -NLLDPLLTQSSTEP----------PSQDD-VNFRDKL-----------------FYIY-TSGTTGLPKAAviVHSryYR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 230 SLGLKAKMdagwTGLQASDIMWT----ISDTGWILNILCSLmepwaLGACTFVhLLPKFDPLVILKTLSSY--PIKSMMG 303
Cdd:cd05939 132 IAAGAYYA----FGMRPEDVVYDclplYHSAGGIMGVGQAL-----LHGSTVV-IRKKFSASNFWDDCVKYncTIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 304 ApiVYRMLLQQDLSSYKFPHlqnCV--TVGESLLPETLENWRAQTGL-DIRESYGQTEtGLTCMVSKTMKIKP-GYMG-T 378
Cdd:cd05939 202 E--ICRYLLAQPPSEEEQKH---NVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATE-GNSSLVNIDNHVGAcGFNSrI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 379 AASCYDVQII-----------DDKGNVLP--PGTEGDIGIRVKPIRPIGIFSGYVDNPD---KTAANI--RGD-FWLLGD 439
Cdd:cd05939 276 LPSVYPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGAtnkKIARDVfkKGDsAFLSGD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 440 RGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLASQFLshDPEQLTK 518
Cdd:cd05939 356 VLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAGMAAIVDPERKV--DLDRFSA 433
|
490 500 510
....*....|....*....|....*....|....*....
3C5E_A 519 ELQqhvkSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd05939 434 VLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
74-561 |
2.58e-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: 84.79 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmPGTIQ--MKSTDILYRLQMSKAKAIV 151
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--PAFINynLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 152 AGDEViqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqEASAIYfTSGTSGLPKMAEHSYSSL 231
Cdd:cd05937 84 VDPDD--------------------------------------------------PAILIY-TSGTTGLPKAAAISWRRT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 232 GLKAKMDAGWTGLQASDIMWT----ISDTGWILNILCSLMEpwalGACtfVHLLPKFDplviLKTLSSYPIKSmmGAP-I 306
Cdd:cd05937 113 LVTSNLLSHDLNLKNGDRTYTcmplYHGTAAFLGACNCLMS----GGT--LALSRKFS----ASQFWKDVRDS--GATiI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 307 VY-----RMLLQQDLSSYKFPHLQNCVTvGESLLPETLENWRAQTGL-DIRESYGQTETgltcmVSKTMKIKPGYMGTAA 380
Cdd:cd05937 181 QYvgelcRYLLSTPPSPYDRDHKVRVAW-GNGLRPDIWERFRERFNVpEIGEFYAATEG-----VFALTNHNVGDFGAGA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 381 SCYD--------------VQIIDDKGNVL-----------PPGTEGDIGIRVkPIRPIGIFSGYVDNPDKTAANI----- 430
Cdd:cd05937 255 IGHHglirrwkfenqvvlVKMDPETDDPIrdpktgfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKLvrdvf 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 431 -RGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLASQ 507
Cdd:cd05937 334 rKGDIYFrTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEES 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
3C5E_A 508 flSHDPEQLTK-ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEW 561
Cdd:cd05937 414 --SAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
70-556 |
6.99e-17 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 83.29 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 70 KELMWNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKA 149
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 150 IVagdevIQEVDTvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeASAIYfTSGTSGLPK--MAEHS 227
Cdd:cd17650 88 LL-----TQPEDL---------------------------------------------AYVIY-TSGTTGKPKgvMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 228 YSslglkAKMDAGW-----------TGLQASDIMWTISdTGWILNILCslmepwALGACTFVHLLPKFDPLVILKTLSSY 296
Cdd:cd17650 117 NV-----AHAAHAWrreyeldsfpvRLLQMASFSFDVF-AGDFARSLL------NGGTLVICPDEVKLDPAALYDLILKS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 297 PIKSMMGAPIVYRMLL------QQDLSSYKFphlqncVTVGESLLPETLENW---RAQTGLDIRESYGQTETgltCMVSK 367
Cdd:cd17650 185 RITLMESTPALIRPVMayvyrnGLDLSAMRL------LIVGSDGCKAQDFKTlaaRFGQGMRIINSYGVTEA---TIDST 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 368 TMKIKPGYMGTAASC--------YDVQIIDDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD------ 433
Cdd:cd17650 256 YYEEGRDPLGDSANVpigrplpnTAMYVLDERLQPQPVGVAGELYIGGA-----GVARGYLNRPELTAERFVENpfapge 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 434 -FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPvRGEVVKAFVVLASQFLShd 512
Cdd:cd17650 331 rMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARLCAYVVAAATLN-- 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....
3C5E_A 513 peqlTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17650 408 ----TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
75-525 |
1.83e-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: 82.02 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 75 NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVagd 154
Cdd:cd17640 7 TYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 155 eviqevdtvasecpslrikllvsekscdgwlnfkkllneastthhcVETGSQEASAIYFTSGTSGLPK--MAEHSysslG 232
Cdd:cd17640 83 ----------------------------------------------VENDSDDLATIIYTSGTTGNPKgvMLTHA----N 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 233 LKAKMDAGWTGLQAS--DIMWTISDTGWILNILCSLMEPWALGACTF---VHL---LPKFDPLVIL------KTLSSYPI 298
Cdd:cd17640 113 LLHQIRSLSDIVPPQpgDRFLSILPIWHSYERSAEYFIFACGCSQAYtsiRTLkddLKRVKPHYIVsvprlwESLYSGIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 299 KSMMGAPIVYRMLLQQDLS--SYKFPhlqncVTVGESLLPETLENWRAqTGLDIRESYGQTETGLTCMVSKTMKIKPGYM 376
Cdd:cd17640 193 KQVSKSSPIKQFLFLFFLSggIFKFG-----ISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 377 GTAASCYDVQIIDDKGN-VLPPGTEGDIGIRVKPIrpigiFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGR 454
Cdd:cd17640 267 GRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVLDSDGWFnTGDLGWLTCGGELVLTGR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 455 ADD-IINSSGYRIGPSEVENALMEHPaVVETAVISSPD---------PVRGEVVKAFVVLAsQFLSHDPEQL------TK 518
Cdd:cd17640 342 AKDtIVLSNGENVEPQPIEEALMRSP-FIEQIMVVGQDqkrlgalivPNFEELEKWAKESG-VKLANDRSQLlaskkvLK 419
|
....*..
3C5E_A 519 ELQQHVK 525
Cdd:cd17640 420 LYKNEIK 426
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-565 |
5.12e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.13 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 14 LGTENLYFQSMSLQWGHQEVPAKFNFASDVLDHWADMEKAGKRPPSPALwwVNGkGKELmwNFRELsensQQAANVLSGA 93
Cdd:PRK12467 3066 LGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPAL--VFG-DQQL--SYAEL----NRRANRLAHR 3136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 94 CgLQRG---DR-VAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASecps 169
Cdd:PRK12467 3137 L-IAIGvgpDVlVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAG---- 3211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 170 lrIKLLVSEkscdgwlnfkkLLNEASTTHHCVETGSQEASAIY--FTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQAS 247
Cdd:PRK12467 3212 --DTALTLD-----------RLDLNGYSENNPSTRVMGENLAYviYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAN 3278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 248 D---IMWTISDTGWILNILCSLMEpwalGACTFVHLLPKFDPLVILKTLSSYPIkSMMGAPIVYRMLLQQDLSSYKFPHL 324
Cdd:PRK12467 3279 DrvlLFMSFSFDGAQERFLWTLIC----GGCLVVRDNDLWDPEELWQAIHAHRI-SIACFPPAYLQQFAEDAGGADCASL 3353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 325 QNCVTVGESLLPETLENWRA---QTGLdiRESYGQTETGLTCMVSKTmkIKPGYMGTAA----------SCYdvqIIDDK 391
Cdd:PRK12467 3354 DIYVFGGEAVPPAAFEQVKRklkPRGL--TNGYGPTEAVVTVTLWKC--GGDAVCEAPYapigrpvagrSIY---VLDGQ 3426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 392 GNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGD-FWLLGDRGIKD-------EDGYFQFMGRADDIINSSG 463
Cdd:PRK12467 3427 LNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAERFVADpFSGSGGRLYRTgdlaryrADGVIEYLGRIDHQVKIRG 3501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 464 YRIGPSEVENALMEHPAVVETAVISSpDPVRGEVVKAFVVLasqflsHDPEQ-LTKELQQHVKSVTAPYKYPRKIEFVLN 542
Cdd:PRK12467 3502 FRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP------ADPQGdWRETLRDHLAASLPDYMVPAQLLVLAA 3574
|
570 580
....*....|....*....|...
3C5E_A 543 LPKTVTGKIQRAKLRDKEWKMSG 565
Cdd:PRK12467 3575 MPLGPNGKVDRKALPDPDAKGSR 3597
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
53-523 |
7.54e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 80.71 E-value: 7.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 53 AGKRPPSPALWWVNGKGKELMW-----NFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFM 127
Cdd:PRK09274 16 AQERPDQLAVAVPGGRGADGKLaydelSFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 128 ---PGtiqMKSTDILYRLQMSKAKAIVAgdeviQEVDTVAS-----ECPSLRIKLLVSEKSCDGWLNFKKLlnEASTTHH 199
Cdd:PRK09274 95 lvdPG---MGIKNLKQCLAEAQPDAFIG-----IPKAHLARrlfgwGKPSVRRLVTVGGRLLWGGTTLATL--LRDGAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 200 ---CVETGSQEASAIYFTSGTSGLPKMAEHSYSSLglkakmDAGWTGLQASdimWTISDTGWILNI--LCSLMEPwALGA 274
Cdd:PRK09274 165 pfpMADLAPDDMAAILFTSGSTGTPKGVVYTHGMF------EAQIEALRED---YGIEPGEIDLPTfpLFALFGP-ALGM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 275 CTfvhLLPKFD--------PLVILKTLSSYPIKSMMGAPIVYRMLLQQDLSS-YKFPHLQNCVTVGESLLPETLENWRA- 344
Cdd:PRK09274 235 TS---VIPDMDptrpatvdPAKLFAAIERYGVTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGAPVPIAVIERFRAm 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 345 -QTGLDIRESYGQTETGLTCMVS------KTMKIK---PGY-MGTAASCYDVQIID---------DKGNVLPPGTEGDIg 404
Cdd:PRK09274 312 lPPDAEILTPYGATEALPISSIEsreilfATRAATdngAGIcVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEI- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 405 irvkpirpigIFSG------YVDNPDKTAAN----IRGDFW-LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN 473
Cdd:PRK09274 391 ----------VVAGpmvtrsYYNRPEATRLAkipdGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCER 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3C5E_A 474 ALMEHPAVVETAVISSPDPvrGEVVKAFVVLASQFLSHDPEQLTKELQQH 523
Cdd:PRK09274 461 IFNTHPGVKRSALVGVGVP--GAQRPVLCVELEPGVACSKSALYQELRAL 508
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
51-556 |
4.06e-15 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 78.93 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 51 EKAGKRPPSPALwwvNGKGKELmwNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPgt 130
Cdd:PRK10252 466 QQAAKTPDAPAL---ADARYQF--SYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP-- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 131 iqmksTDILY---RLQM----SKAKAIVAGDEVIQE-VDTVASECPSLRIKLLVSEKSCDGwlnfkkllneASTTHHcve 202
Cdd:PRK10252 538 -----LDTGYpddRLKMmledARPSLLITTADQLPRfADVPDLTSLCYNAPLAPQGAAPLQ----------LSQPHH--- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 203 tgsqeASAIYFTSGTSGLPK--MAEHsysslglkakmdagwtglQAsdimwtisdtgwILNILCSLMEPWALGA------ 274
Cdd:PRK10252 600 -----TAYIIFTSGSTGRPKgvMVGQ------------------TA------------IVNRLLWMQNHYPLTAddvvlq 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 275 ---CTF-VHLLPKF------------------DPLVILKTLSSYPIKSMMGAPivyRML------LQQDLSSYKFPHLQN 326
Cdd:PRK10252 645 ktpCSFdVSVWEFFwpfiagaklvmaepeahrDPLAMQQFFAEYGVTTTHFVP---SMLaafvasLTPEGARQSCASLRQ 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 327 CVTVGESLLPETLENWRAQTGLDIRESYGQTETG------------LTCMVSKTMKIKPGYMGTAascydVQIIDDKGNV 394
Cdd:PRK10252 722 VFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAvdvswypafgeeLAAVRGSSVPIGYPVWNTG-----LRILDARMRP 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 395 LPPGTEGDI---GIRVKpirpigifSGYVDNPDKTAANIRGD-------FWLLGDRGIKDEDGYFQFMGRADDIINSSGY 464
Cdd:PRK10252 797 VPPGVAGDLyltGIQLA--------QGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQ 868
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 465 RIGPSEVENALMEHP----AVVETAVISSPDPVRGEVVK--AFVVlASQFLSHDpeqlTKELQQHVKSVTAPYKYPRKIE 538
Cdd:PRK10252 869 RIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQlvGYLV-SQSGLPLD----TSALQAQLRERLPPHMVPVVLL 943
|
570
....*....|....*...
3C5E_A 539 FVLNLPKTVTGKIQRAKL 556
Cdd:PRK10252 944 QLDQLPLSANGKLDRKAL 961
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
439-557 |
1.03e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.85 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 439 DRGIKDeDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflsHDPEQLTK 518
Cdd:PRK07824 240 DLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGD-----GGPAPTLE 313
|
90 100 110
....*....|....*....|....*....|....*....
3C5E_A 519 ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
74-557 |
1.08e-14 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 76.62 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmPGTI--QMKSTDILYRLQMSKAKAIV 151
Cdd:cd05940 4 LTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV--AALInyNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 152 agdeviqeVDTvasecpslrikllvsekscdgwlnfkkllneastthhcvetgsqeasAIY-FTSGTSGLPKMAEHSYSS 230
Cdd:cd05940 81 --------VDA-----------------------------------------------ALYiYTSGTTGLPKAAIISHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 231 LGLKAKMDAGWTGLQASDIMWTI----SDTGWILNILCSLMEpwalGACtfvhllpkfdpLVILKTLSSY----PIKSMM 302
Cdd:cd05940 106 AWRGGAFFAGSGGALPSDVLYTClplyHSTALIVGWSACLAS----GAT-----------LVIRKKFSASnfwdDIRKYQ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 303 GAPIVY-----RMLLQQDLSSYKFPHLQNCVtVGESLLPETLENWRAQTGL-DIRESYGQTE--------TGLTCMVSKT 368
Cdd:cd05940 171 ATIFQYigelcRYLLNQPPKPTERKHKVRMI-FGNGLRPDIWEEFKERFGVpRIAEFYAATEgnsgfinfFGKPGAIGRN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 369 MKIKPGYMGTAASCYDVQ----IIDDKGNVLPPGtEGDIGIRVKPIRPIGIFSGYVDNPDKTAANIR-----GDFWLL-G 438
Cdd:cd05940 250 PSLLRKVAPLALVKYDLEsgepIRDAEGRCIKVP-RGEPGLLISRINPLEPFDGYTDPAATEKKILRdvfkkGDAWFNtG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 439 DRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDP-VRGEVVKAFVVLASQflshDPEQLT 517
Cdd:cd05940 329 DLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPN----EEFDLS 404
|
490 500 510 520
....*....|....*....|....*....|....*....|
3C5E_A 518 KeLQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:cd05940 405 A-LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
22-562 |
1.74e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.13 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 22 QSMSLQWGHQEVPAKFNFASDVLDHwadmeKAGKRPPSPALWWVNGKgkelmWNFRELSENSQQAANVLSGaCGLQRGDR 101
Cdd:PRK05691 1115 RAQLAQWGQAPCAPAQAWLPELLNE-----QARQTPERIALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVC 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 102 VAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVDTVASECPslrikLLVSEKSC 181
Cdd:PRK05691 1184 VAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSA-----IALDSLHL 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 182 DGWLNFKKLLNeastTHhcvetGSQEASAIYfTSGTSGLPKMAEHSYSSLGLKAK-MDAGWtGLQASDIMWTISDTGWIL 260
Cdd:PRK05691 1259 DSWPSQAPGLH----LH-----GDNLAYVIY-TSGSTGQPKGVGNTHAALAERLQwMQATY-ALDDSDVLMQKAPISFDV 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 261 NIL-CSlmepWAL-GACTFVHLLP--KFDPLVILKTLSSYPIKSMMGAPIVYRMLLQQdlssykfPHLQNCVTV------ 330
Cdd:PRK05691 1328 SVWeCF----WPLiTGCRLVLAGPgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE-------PLAAACTSLrrlfsg 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 331 GESLLPETLENWRAQ-TGLDIRESYGQTETGLT-----CMVSKTMKIKPGYMGTAASCydvQIIDDKGNVLPPGTEGDIG 404
Cdd:PRK05691 1397 GEALPAELRNRVLQRlPQVQLHNRYGPTETAINvthwqCQAEDGERSPIGRPLGNVLC---RVLDAELNLLPPGVAGELC 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 405 IRvkpirPIGIFSGYVDNPDKTAANIRGD--------FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALM 476
Cdd:PRK05691 1474 IG-----GAGLARGYLGRPALTAERFVPDplgedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLL 1548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 477 EHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:PRK05691 1549 AQPGVAQAAVLVREGAAGAQLVGYYTGEAGQ------EAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
....*.
3C5E_A 557 RDKEWK 562
Cdd:PRK05691 1623 PEPVWQ 1628
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
327-556 |
4.49e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.98 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 327 CVTVGESLLPETLENWRA--QTGLdIRESYGQTET---GLTCMVSKTMKIKPGY--MGTAASCYDVQIIDDKGNVLPPGT 399
Cdd:PRK05691 2453 CITGGEALTGEHLQRIRQafAPQL-FFNAYGPTETvvmPLACLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGA 2531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 400 EGDIGIRVKpirpiGIFSGYVDNPDKTA--------ANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEV 471
Cdd:PRK05691 2532 TGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEI 2606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 472 ENALMEHPAVVETAVISSPDPVRGEVVKafvVLASQFLSHDPEQ---LTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVT 548
Cdd:PRK05691 2607 ESRLLEHPAVREAVVLALDTPSGKQLAG---YLVSAVAGQDDEAqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTAN 2683
|
....*...
3C5E_A 549 GKIQRAKL 556
Cdd:PRK05691 2684 GKLDRRAL 2691
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
77-555 |
5.28e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 74.65 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 77 RELSENSQQAANVLSGAcGLQRGDRVAV-------VLPRVPEWWLvilgciRAGLIFM-----PGT-IQMKSTDILYRLQ 143
Cdd:PRK07768 33 GEVHERARRIAGGLAAA-GVGPGDAVAVlagapveIAPTAQGLWM------RGASLTMlhqptPRTdLAVWAEDTLRVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 144 MSKAKAIVAGDEVIQEVDTVASEcpSLRIkLLVSEkscdgwlnfkkLLNEASTTHhcVETGsQEASAIY-FTSGTSGLPK 222
Cdd:PRK07768 106 MIGAKAVVVGEPFLAAAPVLEEK--GIRV-LTVAD-----------LLAADPIDP--VETG-EDDLALMqLTSGSTGSPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 223 MAEHSYSSLglKAKMDAGWTGLQA---SDIM--W--TISDTGWIlNILCSlmePWALGaCTFVHLLP-KF--DPLVILKT 292
Cdd:PRK07768 169 AVQITHGNL--YANAEAMFVAAEFdveTDVMvsWlpLFHDMGMV-GFLTV---PMYFG-AELVKVTPmDFlrDPLLWAEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 293 LSSYPiKSMMGAP-----IVYRMLLQQ------DLSSYKFphlqnCVTVGESLLPETLENWRAQT---GLD---IRESYG 355
Cdd:PRK07768 242 ISKYR-GTMTAAPnfayaLLARRLRRQakpgafDLSSLRF-----ALNGAEPIDPADVEDLLDAGarfGLRpeaILPAYG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 356 QTETGLTC-----------------MVSKTMKIKPGYMGTAASC---------YDVQIIDDKGNVLPPGTEGDIGIRVKP 409
Cdd:PRK07768 316 MAEATLAVsfspcgaglvvdevdadLLAALRRAVPATKGNTRRLatlgpplpgLEVRVVDEDGQVLPPRGVGVIELRGES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 410 IRPigifsGYVDnPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVIS 488
Cdd:PRK07768 396 VTP-----GYLT-MDGFIPAQDADGWLdTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3C5E_A 489 SPDPvRGEVVKAFVVLASQFLSHDPEQLTKELQQHVKSVTAPYKY-PRKIeFVL---NLPKTVTGKIQRAK 555
Cdd:PRK07768 470 VRLD-AGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVrPRNV-VVLgpgSIPKTPSGKLRRAN 538
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
35-552 |
2.01e-13 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 73.07 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 35 AKFNFASDVLDHwadmekagKRPPSPALWWVNGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWL 114
Cdd:cd05943 68 ARLNYAENLLRH--------ADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALR-ALGVKPGDRVAGYLPNIPEAVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 115 VILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVI---------QEVDTVASECPSLRIKLLVSEKSCDGWL 185
Cdd:cd05943 139 AMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTyngkrhdvrEKVAELVKGLPSLLAVVVVPYTVAAGQP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 186 NFKKLLNeastTHHCVETGSQEASA--------------IYFTSGTSGLPKMAEHSYSSLGLKAKMDAGW-TGLQASDIM 250
Cdd:cd05943 219 DLSKIAK----ALTLEDFLATGAAGelefeplpfdhplyILYSSGTTGLPKCIVHGAGGTLLQHLKEHILhCDLRPGDRL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 251 WTISDTGWIL-NILCSLMepwALGAcTFV-----HLLPkfDPLVILKTLSSYPIkSMMGAPIVYRMLLQQ---------D 315
Cdd:cd05943 295 FYYTTCGWMMwNWLVSGL---AVGA-TIVlydgsPFYP--DTNALWDLADEEGI-TVFGTSAKYLDALEKaglkpaethD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 316 LSSykfphLQNCVTVGESLLPETLE----NWRAqtGLDIRESYGQTETgLTCMVSkTMKIKPGYMGtAASC----YDVQI 387
Cdd:cd05943 368 LSS-----LRTILSTGSPLKPESFDyvydHIKP--DVLLASISGGTDI-ISCFVG-GNPLLPVYRG-EIQCrglgMAVEA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 388 IDDKGNVLPpGTEGDIGIrVKPI--RPIGiFSGYVDNPDKTAA--NIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSG 463
Cdd:cd05943 438 FDEEGKPVW-GEKGELVC-TKPFpsMPVG-FWNDPDGSRYRAAyfAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGG 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 464 YRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLASQflshdpEQLTKELQQHVKSVTA----PYKYPRKIEF 539
Cdd:cd05943 515 VRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDELRKRIRSTIRsalsPRHVPAKIIA 588
|
570
....*....|...
3C5E_A 540 VLNLPKTVTGKIQ 552
Cdd:cd05943 589 VPDIPRTLSGKKV 601
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
74-556 |
5.02e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.51 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 74 WNFRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMP---GTIQMKSTDILyrlQMSKAKAI 150
Cdd:PRK05691 3746 WSYAELNRAANRLGHALRAA-GVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPldpGLPAQRLQRII---ELSRTPVL 3821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 151 VAGDEVIQEVDTVASECP-SLRIKLLVSEKscdgwlnfkkLLNEASTTHH-CVETGSQEASAIYFTSGTSGLPK------ 222
Cdd:PRK05691 3822 VCSAACREQARALLDELGcANRPRLLVWEE----------VQAGEVASHNpGIYSGPDNLAYVIYTSGSTGLPKgvmveq 3891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 223 --MAEHSYSS---LGLKAKMDAGWTGLQASDI-MWTIsdtgwilnilcslmepwaLGACTF---VHLLPK---FDPLVIL 290
Cdd:PRK05691 3892 rgMLNNQLSKvpyLALSEADVIAQTASQSFDIsVWQF------------------LAAPLFgarVEIVPNaiaHDPQGLL 3953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 291 KTLSSYPIKSMMGAP-IVYRMLLQQDLSsykFPHLQNCVTVGESLLPETLENW---RAQTGLdiRESYGQTEtgltC--- 363
Cdd:PRK05691 3954 AHVQAQGITVLESVPsLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWlqrYPQIGL--VNAYGPAE----Csdd 4024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 364 -------MVSKTMKIKPgyMGTAASCYDVQIIDDKGNVLPPGTEGDIGIRvkpirPIGIFSGYVDNPDKTA----ANIRG 432
Cdd:PRK05691 4025 vaffrvdLASTRGSYLP--IGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTAlafvPHPFG 4097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 433 D----FWLLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSpDPVRGEVVKAFVVLASQF 508
Cdd:PRK05691 4098 ApgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ-EGVNGKHLVGYLVPHQTV 4176
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
3C5E_A 509 lsHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:PRK05691 4177 --LAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
35-552 |
1.32e-11 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 67.13 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 35 AKFNFASDVLDHwadmekagKRPPSPALWWVNGKGKELMWNFRELSEnsqQAANVLSG--ACGLQRGDRVAVVLPRVPEW 112
Cdd:PRK03584 84 ARLNYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRR---QVAALAAAlrALGVGPGDRVAAYLPNIPET 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 113 WLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGD---------EVIQEVDTVASECPSLRIKLLVS------ 177
Cdd:PRK03584 153 VVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLEHVVVVPylgpaa 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 178 -EKSCDGWLNFKKLLNEAstthhcvetgsqEASAIYFT-------------SGTSGLPKMAEHSYSSLGLKA-KMDAGWT 242
Cdd:PRK03584 233 aAAALPGALLWEDFLAPA------------EAAELEFEpvpfdhplwilysSGTTGLPKCIVHGHGGILLEHlKELGLHC 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 243 GLQASDIMWTISDTGWIL-NILCSLMepwALGACTFVH----LLPKFDPL---------VILKTLSSYpIKSMMGAPIVY 308
Cdd:PRK03584 301 DLGPGDRFFWYTTCGWMMwNWLVSGL---LVGATLVLYdgspFYPDPNVLwdlaaeegvTVFGTSAKY-LDACEKAGLVP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 309 RmllqqdlSSYKFPHLQNCVTVGESLLPETL----ENWRAQT-------GLDIresygqtetgLTCMV--SKTMKIKPGY 375
Cdd:PRK03584 377 G-------ETHDLSALRTIGSTGSPLPPEGFdwvyEHVKADVwlasisgGTDI----------CSCFVggNPLLPVYRGE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 376 MGTAASCYDVQIIDDKGNVLppgtEGDIGIRV--KPI--RPIGiFSGYVDNPDKTAA------NIrgdfWLLGDRGIKDE 445
Cdd:PRK03584 440 IQCRGLGMAVEAWDEDGRPV----VGEVGELVctKPFpsMPLG-FWNDPDGSRYRDAyfdtfpGV----WRHGDWIEITE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 446 DGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLAsqflshDPEQLTKELQQHVK 525
Cdd:PRK03584 511 HGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLA------EGVTLDDALRARIR 584
|
570 580 590
....*....|....*....|....*....|.
3C5E_A 526 SV----TAPYKYPRKIEFVLNLPKTVTGKIQ 552
Cdd:PRK03584 585 TTirtnLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
376-557 |
1.81e-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: 66.36 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 376 MGTAASCYDVQIIDDKGNVLPPGTEGDIGIRVKPIRPigifsGYVDNPDKTAANIRGDFWLL-GDRG-IKDEDGYFqfMG 453
Cdd:cd05908 316 VGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP-----GYYNNPEATAKVFTDDGWLKtGDLGfIRNGRLVI--TG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 454 RADDIINSSGYRIGPSEVENalmehpavvetaVISSPDPVR-GEVVKAFVvlasqflsHDPEQLTKEL---QQHVKSVTA 529
Cdd:cd05908 389 REKDIIFVNGQNVYPHDIER------------IAEELEGVElGRVVACGV--------NNSNTRNEEIfcfIEHRKSEDD 448
|
170 180 190 200
....*....|....*....|....*....|....*....|...
3C5E_A 530 PYKYPRKIEFVLN---------------LPKTVTGKIQRAKLR 557
Cdd:cd05908 449 FYPLGKKIKKHLNkrggwqinevlpirrIPKTTSGKVKRYELA 491
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
78-556 |
4.43e-11 |
|
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: 65.19 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 78 ELSENSQQAANVLSGACglQRGDR-VAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEV 156
Cdd:cd17654 21 DLAEKISNLSNFLRKKF--QTEERaIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 157 IQEvdtvasecPSLRIKLLVsekscdgwlNFKKLLNEAStthhcvetgsqeaSAIYFTSGTSGLPK---MAEHSYSS--L 231
Cdd:cd17654 99 DNA--------PLSFTPEHR---------HFNIRTDECL-------------AYVIHTSGTTGTPKivaVPHKCILPniQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 232 GLKAKMDagwtgLQASDIMWTISDTGW---ILNILCSLmepwALGAC-----TFVHLLP-KFDPlvILKTLSSypIKSMM 302
Cdd:cd17654 149 HFRSLFN-----ITSEDILFLTSPLTFdpsVVEIFLSL----SSGATllivpTSVKVLPsKLAD--ILFKRHR--ITVLQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 303 GAPIVYRMLLQQDLSSYKFPHLQN--CVTVGESLLPETLEN--WRAQ-TGLDIRESYGQTETgltCMVSKTMKIK----P 373
Cdd:cd17654 216 ATPTLFRRFGSQSIKSTVLSATSSlrVLALGGEPFPSLVILssWRGKgNRTRIFNIYGITEV---SCWALAYKVPeedsP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 374 GYMGTAASCYDVQIIDDKGNvlppgtEGDIGIRVKPIRPIGIFSGYVDNPdktaaniRGDFWLLGDRgIKDEDGYFQFMG 453
Cdd:cd17654 293 VQLGSPLLGTVIEVRDQNGS------EGTGQVFLGGLNRVCILDDEVTVP-------KGTMRATGDF-VTVKDGELFFLG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 454 RADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDpvrgEVVKAFVVLASqflSHDPEQltKELQQHVKSvtaPYKY 533
Cdd:cd17654 359 RKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGES---SSSRIH--KELQLTLLS---SHAI 426
|
490 500
....*....|....*....|...
3C5E_A 534 PRKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17654 427 PDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
66-481 |
8.38e-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: 64.69 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 66 NGKGKELMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfMPGTIQMKSTD-ILYRLQM 144
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFL-KLGLERFHGVGILGFNSPEWFIAAVGAIFAGGI-AVGIYTTNSPEaCQYVAET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 145 SKAKAIVAGDEV-IQEVDTVASECPSLR----IKLLVSEKSCD--GWLNFKKLLNEASTTHHCVETGSQEAS---AIYFT 214
Cdd:cd05933 79 SEANILVVENQKqLQKILQIQDKLPHLKaiiqYKEPLKEKEPNlySWDEFMELGRSIPDEQLDAIISSQKPNqccTLIYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 215 SGTSGLPK--MAEH---------------------------SYSSLG-LKAKMDAGWTGL---------QASDIMWTISD 255
Cdd:cd05933 159 SGTTGMPKgvMLSHdnitwtakaasqhmdlrpatvgqesvvSYLPLShIAAQILDIWLPIkvggqvyfaQPDALKGTLVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 256 T------------GWILNILCSLMEPWALGACTFVHLLPKFDPLVILKTLSsypiKSMMG---APIVYRMLLQQDLSSYK 320
Cdd:cd05933 239 TlrevrptafmgvPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNL----KLMGGespSPLFYRLAKKLVFKKVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 321 ----FPHLQNCVTVGESLLPETLENWraqTGLDIR--ESYGQTET-GLtcmvsKTMKIKPGYmgTAASCydvqiiddkGN 393
Cdd:cd05933 315 kalgLDRCQKFFTGAAPISRETLEFF---LSLNIPimELYGMSETsGP-----HTISNPQAY--RLLSC---------GK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 394 VLPpgtegdiGIRVKPIRP----IG--------IFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADD-II 459
Cdd:cd05933 376 ALP-------GCKTKIHNPdadgIGeicfwgrhVFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElII 448
|
490 500
....*....|....*....|...
3C5E_A 460 NSSGYRIGPSEVENAL-MEHPAV 481
Cdd:cd05933 449 TAGGENVPPVPIEDAVkKELPII 471
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
106-568 |
1.13e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 64.07 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 106 LPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQE------VDTVASECPSLRIKLLVSEK 179
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralplYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 180 SCD--------GWLNFkklLNEASTTHhcvETGSQEASAIY----------FTSGTSGLPKMAEHSYSSlGLKAKMDaGW 241
Cdd:PLN03051 81 PVAvplreqdlSWCDF---LGVAAAQG---SVGGNEYSPVYapvesvtnilFSSGTTGEPKAIPWTHLS-PLRCASD-GW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 242 TGL--QASDIMWTISDTGWILN-ILcsLMEPWALGACTFVH----LLPKFDPLV------ILKTlssypIKSMMGApivY 308
Cdd:PLN03051 153 AHMdiQPGDVVCWPTNLGWMMGpWL--LYSAFLNGATLALYggapLGRGFGKFVqdagvtVLGL-----VPSIVKA---W 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 309 RMLLQQDLSSYKFPHLQNCVTVGESLLPET---LENWRAQTGlDIRESYGQTETGLTCMVSKTMKIK-PGYMGTAASCYD 384
Cdd:PLN03051 223 RHTGAFAMEGLDWSKLRVFASTGEASAVDDvlwLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQaPGAFSTASLGTR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 385 VQIIDDKGNVLPPGTE--GDIGIRVkpirPIGIFSGYVDNPDKTAANIRG---------DFWLLGDRGIKDEDGYFQFMG 453
Cdd:PLN03051 302 FVLLNDNGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmpmygskgmPLRRHGDIMKRTPGGYFCVQG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 454 RADDIINSSGYRIGPSEVENALME-HPAVVETAVISSPDPVRGE----VVKAFVVLASQFLSHDPEQLTKELQQHVKSVT 528
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNL 457
|
490 500 510 520
....*....|....*....|....*....|....*....|.
3C5E_A 529 APYKYPRKIEFVLNLPKTVTGKIQRAKLRDKEWK-MSGKAR 568
Cdd:PLN03051 458 NPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKKeLSGRSK 498
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
76-557 |
3.40e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 62.72 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSGAcGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMPGTIQMK-------STDILYRLQMSKAK 148
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 149 AIVAGDEVIQEVDTVASecpSLRIKLLVSekscdgWLNFKkLLNEASTThhcVETGSQEASA-IYFTSGTSGLPK----- 222
Cdd:PRK09192 131 AIITPDELLPWVNEATH---GNPLLHVLS------HAWFK-ALPEADVA---LPRPTPDDIAyLQYSSGSTRFPRgviit 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 223 ----MAE-HSYSSLGLKakmdagwtgLQASD--IMW-----TISDTGWILNILCSLMEpwalgactfVHLLPKFD----P 286
Cdd:PRK09192 198 hralMANlRAISHDGLK---------VRPGDrcVSWlpfyhDMGLVGFLLTPVATQLS---------VDYLPTRDfarrP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 287 LVILK-------TLSSYPiksMMGAPIVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWR---AQTGLDIRE---S 353
Cdd:PRK09192 260 LQWLDlisrnrgTISYSP---PFGYELCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAeafAPAGFDDKAfmpS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 354 YGQTETGL------------------TCMVSKTMKIKPGYMGTAAS----C------YDVQIIDDKGNVLPPGTEGDIGI 405
Cdd:PRK09192 337 YGLAEATLavsfsplgsgivveevdrDRLEYQGKAVAPGAETRRVRtfvnCgkalpgHEIEIRNEAGMPLPERVVGHICV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 406 RvKPirpiGIFSGYVDNPDkTAANIRGDFWL-LGDRGIKdEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVV-- 482
Cdd:PRK09192 417 R-GP----SLMSGYFRDEE-SQDVLAADGWLdTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsg 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 483 ETAVISSPDPvRGEVVkafVVLASQFLShDPE---QLTKELQQHVKSVTApykYPRKIEFV--LNLPKTVTGKIQRAKLR 557
Cdd:PRK09192 490 DAAAFSIAQE-NGEKI---VLLVQCRIS-DEErrgQLIHALAALVRSEFG---VEAAVELVppHSLPRTSSGKLSRAKAK 561
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
76-494 |
1.82e-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: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 76 FRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIfmpgtiqmkstDILyrlqmskakaivagde 155
Cdd:cd05910 5 FRELDERSDRIAQGLT-AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV-----------PVL---------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 156 viqeVDtvasecPSLRIKllvsekscdgwlNFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAEHSYSSLglKA 235
Cdd:cd05910 57 ----ID------PGMGRK------------NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTF--AA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 236 KMDAGWT--GLQASDI-MWTISdtgwilniLCSLMEPwALGACTFV----HLLP-KFDPLVILKTLSSYPIKSMMGAPIV 307
Cdd:cd05910 113 QIDALRQlyGIRPGEVdLATFP--------LFALFGP-ALGLTSVIpdmdPTRPaRADPQKLVGAIRQYGVSIVFGSPAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 308 YRML----LQQDLssyKFPHLQNCVTVGESLLPETLENWRA--QTGLDIRESYGQTETGLTCMV-------SKTMKIKPG 374
Cdd:cd05910 184 LERVarycAQHGI---TLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVSSIgsrellaTTTAATSGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 375 Y---MGTAASCYDVQIID---------DKGNVLPPGTEGDI---GIRVKPirpigifsGYVDNPDKTAA----NIRGDFW 435
Cdd:cd05910 261 AgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEItvtGPTVTP--------TYVNRPVATALakidDNSEGFW 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 436 -LLGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPVR 494
Cdd:cd05910 333 hRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGC 392
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
205-557 |
2.93e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 59.72 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 205 SQEASAIYFTSGTSGLPKMAEHSYSSLglkakmdagwtgLQASDIMWTISDTGWILNILCSLMEPWALGACtfVHLlpkF 284
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSL------------LANVEQIKTIADFTPNDRFMSALPLFHSFGLT--VGL---F 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 285 DPLVILKTLSSYPiksmmgAPIVYRML--LQQD------------LSSY-KFPH------LQNCVTVGESLLPETLENWR 343
Cdd:PRK08043 427 TPLLTGAEVFLYP------SPLHYRIVpeLVYDrnctvlfgtstfLGNYaRFANpydfarLRYVVAGAEKLQESTKQLWQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 344 AQTGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIddkgNVlpPGTEGdiGIRVKpIRPIGIFSGY--VD 421
Cdd:PRK08043 501 DKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLL----SV--PGIEQ--GGRLQ-LKGPNIMNGYlrVE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 422 NPDK----TAANIRGDF---WL-LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVEN-ALMEHPAVVETAVISSpDP 492
Cdd:PRK08043 572 KPGVlevpTAENARGEMergWYdTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKS-DA 650
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3C5E_A 493 VRGEvvkAFVVLASqflshDPEqLTKE-LQQHVKSVTAP-YKYPRKIEFVLNLPKTVTGKIQRAKLR 557
Cdd:PRK08043 651 SKGE---ALVLFTT-----DSE-LTREkLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLK 708
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
210-558 |
8.20e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 58.78 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 210 AIYFTSGTSGLPKMAEHSYSSLGLKAKmdagwtglQASDIMWTISDTgwilNILCSLmePW--ALG--ACTFVHLLPKF- 284
Cdd:PRK08633 786 TIIFSSGSEGEPKGVMLSHHNILSNIE--------QISDVFNLRNDD----VILSSL--PFfhSFGltVTLWLPLLEGIk 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 285 -----DPL---VILKTLSSYPIKSMMGAPIVYRMLLQQD-LSSYKFPHLQNCVTVGESLLPETLENWRAQTGLDIRESYG 355
Cdd:PRK08633 852 vvyhpDPTdalGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYG 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 356 QTETGLTCMVSKTMKIKPGYM---------------GTAascydVQIID-DKGNVLPPGTEGDIgirvkPIRPIGIFSGY 419
Cdd:PRK08633 932 ATETSPVASVNLPDVLAADFKrqtgskegsvgmplpGVA-----VRIVDpETFEELPPGEDGLI-----LIGGPQVMKGY 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 420 VDNPDKTA---ANIRGDFWLL-GDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALME--HPAVVETAVISSPDPV 493
Cdd:PRK08633 1002 LGDPEKTAeviKDIDGIGWYVtGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEK 1081
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3C5E_A 494 RGEVVkafVVLASQflshdPEQLTKELQQHVKSVTAP--YKyPRKIEFVLNLPKTVTGKIQRAKLRD 558
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 ... |
110-558 |
1.28e-07 |
|
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: 54.53 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 110 PEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIV--AGDEVIQevdtvasecpslrikllvsekscdgWLNF 187
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFcdAGVKVYS-------------------------LEEF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 188 KKLLNEASTTHhcvETGSQEASA-IYFTSGTSGLPKMAEHSYSSlglkakmdagwtglqasdIMWTISDTGWILNILCSL 266
Cdd:cd05927 98 EKLGKKNKVPP---PPPKPEDLAtICYTSGTTGNPKGVMLTHGN------------------IVSNVAGVFKILEILNKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 267 MEpwalgacTFVHL--LP---KFDPLVILKTLS--------SYPIKSMM------------GAPIVY-RML--LQQDLS- 317
Cdd:cd05927 157 NP-------TDVYIsyLPlahIFERVVEALFLYhgakigfySGDIRLLLddikalkptvfpGVPRVLnRIYdkIFNKVQa 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 318 -------------SYKFPHLQN---------------------------CVTVGESLLPETLENWRAQTGLDIRESYGQT 357
Cdd:cd05927 230 kgplkrklfnfalNYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 358 ETGLTCMVSKTMKIKPGYMGTAASCYDVQIID--DKG-NVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDKTAANIRGDF 434
Cdd:cd05927 310 ECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpEMNyDAKDPNPRGEVCIRGP-----NVFSGYYKDPEKTAEALDEDG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 435 WLL-GDRGIKDEDGYFQFMGRADDIIN-SSGYRIGPSEVENALMEHPAVVETAV-----------ISSPDPvrgEVVKAF 501
Cdd:cd05927 385 WLHtGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIYARSPFVAQIFVygdslksflvaIVVPDP---DVLKEW 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3C5E_A 502 vvLASQFL-SHDPEQLTK--ELQQHV---------KSVTAPYKYPRKIEFVLNLPK------TVTGKIQRAKLRD 558
Cdd:cd05927 462 --AASKGGgTGSFEELCKnpEVKKAIledlvrlgkENGLKGFEQVKAIHLEPEPFSvengllTPTFKLKRPQLKK 534
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
275-556 |
2.43e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 47.13 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 275 CTFVHLLPKFDPLviLKTLSSYPIKSMMGAPIVYRMLLQQDLSSykfphLQ----NCVTVGeslLPETLENWRAQTGLDI 350
Cdd:cd17647 201 ATVTHLTPAMGQL--LTAQATTPFPKLHHAFFVGDILTKRDCLR-----LQtlaeNVRIVN---MYGTTETQRAVSYFEV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 351 ReSYGQTETGLtcmvsKTMK-IKPGYMGTaascYDVQII----DDKGNVLPPGTEGDIGIRVKpirpiGIFSGYVDNPDK 425
Cdd:cd17647 271 P-SRSSDPTFL-----KNLKdVMPAGRGM----LNVQLLvvnrNDRTQICGIGEVGEIYVRAG-----GLAEGYRGLPEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 426 TAANIRGD---------------------FWL--------LGDRGIKDEDGYFQFMGRADDIINSSGYRIGPSEVENALM 476
Cdd:cd17647 336 NKEKFVNNwfvepdhwnyldkdnnepwrqFWLgprdrlyrTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHIS 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 477 EHPAVVET------------AVIS--SPDPVRGEVVKAFVVLASQFLSHDP--------EQLTKELQQHVKSVTAPYKYP 534
Cdd:cd17647 416 QHPLVRENitlvrrdkdeepTLVSyiVPRFDKPDDESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIP 495
|
330 340
....*....|....*....|..
3C5E_A 535 RKIEFVLNLPKTVTGKIQRAKL 556
Cdd:cd17647 496 SLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
46-561 |
3.02e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 46.79 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 46 HWADMekagkRPPSPALwwVNGKGkelMWNFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLVILGCIRAG-- 123
Cdd:PRK09029 11 HWAQV-----RPQAIAL--RLNDE---VLTWQQLCARIDQLAAGFA-QQGVVEGSGVALRGKNSPETLLAYLALLQCGar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 124 -LIFMPGTIQMKSTDILYRLQmskakaivagdeviqeVDTVASECPSLRIKLLVSekscdgwlnfkKLLNEASTTHHCVE 202
Cdd:PRK09029 80 vLPLNPQLPQPLLEELLPSLT----------------LDFALVLEGENTFSALTS-----------LHLQLVEGAHAVAW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 203 TGSQEASAIyFTSGTSGLPKMAEHSY-----SSLGLKAKMDagwtgLQASDimwtisdtGWILnilcSLmepwalgactf 277
Cdd:PRK09029 133 QPQRLATMT-LTSGSTGLPKAAVHTAqahlaSAEGVLSLMP-----FTAQD--------SWLL----SL----------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 278 vhllpkfdPL--VilktlssypikSMMGapIVYRMLLQ---------QDLSSykfpHLQNCVTVgeSLLPeT-----LEN 341
Cdd:PRK09029 184 --------PLfhV-----------SGQG--IVWRWLYAgatlvvrdkQPLEQ----ALAGCTHA--SLVP-TqlwrlLDN 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 342 WRAQTGLD--------IRESYGQ--TETGLTCMVsktmkikpGY-MGTAASCYDVQIIDDKGNV-LP-PGTE-----GDI 403
Cdd:PRK09029 236 RSEPLSLKavllggaaIPVELTEqaEQQGIRCWC--------GYgLTEMASTVCAKRADGLAGVgSPlPGREvklvdGEI 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 404 GIRVKpirpiGIFSGYvdnpdktaanirgdfWLlgDRGIK---DEDGYFQ-------------FMGRADDIINSSGYRIG 467
Cdd:PRK09029 308 WLRGA-----SLALGY---------------WR--QGQLVplvNDEGWFAtrdrgewqngeltILGRLDNLFFSGGEGIQ 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 468 PSEVENALMEHPAVVETAVISSPD------PVrgevvkAFVVLASqflshdpEQLTKELQQHVKSVTAPYKYPrkIEFVL 541
Cdd:PRK09029 366 PEEIERVINQHPLVQQVFVVPVADaefgqrPV------AVVESDS-------EAAVVNLAEWLQDKLARFQQP--VAYYL 430
|
570 580
....*....|....*....|...
3C5E_A 542 nLPKTV-TG--KIQRAKLrdKEW 561
Cdd:PRK09029 431 -LPPELkNGgiKISRQAL--KEW 450
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
334-500 |
3.03e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.02 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 334 LLPETLENWRAQTGLDIRESYGQTETglTCMVSKTMK--IKPGYMGTAASCYDVQIID---------DKgnvlpPGTEGD 402
Cdd:PLN02736 388 LSPDVMEFLRICFGGRVLEGYGMTET--SCVISGMDEgdNLSGHVGSPNPACEVKLVDvpemnytseDQ-----PYPRGE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 403 IGIRvKPIrpigIFSGYVDNPDKTAANIRGDFWL-LGDRGIKDEDGYFQFMGRADDIIN-SSGYRIGPSEVENALMEHPA 480
Cdd:PLN02736 461 ICVR-GPI----IFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYIAPEKIENVYAKCKF 535
|
170 180 190
....*....|....*....|....*....|.
3C5E_A 481 VVETAV-----------ISSPDPvrgEVVKA 500
Cdd:PLN02736 536 VAQCFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
48-557 |
3.79e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.09 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 48 ADMEKAGKRPPSPALWWVNGKGKE-LMWNFRELSENSQQAANVLSGACGLqrGDRVAVVLPRVPEWWLVILGCIRAGLIF 126
Cdd:PRK05691 14 ALQRRAAQTPDRLALRFLADDPGEgVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 127 MPGTIQMKSTdilyRLQMSKAKAIVAgDEVIQEVDTVASECPSLRIKLLVSEKSCDGWLNFKKLLNEASTTHHCVETGSQ 206
Cdd:PRK05691 92 VPAYPPESAR----RHHQERLLSIIA-DAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 207 EASAIYFTSGTSGLPKMAEHSYSSLGLKAKMDAGWTGLQASD----IMWT--ISDTGWILNIL--------CSLMEPwal 272
Cdd:PRK05691 167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddviVSWLplYHDMGLIGGLLqpifsgvpCVLMSP--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 273 gactfVHLLPKfdPLVILKTLSSYPIKSMMGAPIVYRMLLQQdlssykfphlqncvtVGESLLPE-TLENWR-AQTGLD- 349
Cdd:PRK05691 244 -----AYFLER--PLRWLEAISEYGGTISGGPDFAYRLCSER---------------VSESALERlDLSRWRvAYSGSEp 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 350 IRE----------------------SYGQTETglTCMVSKTMK------------------IKPGYMGTAASC------Y 383
Cdd:PRK05691 302 IRQdslerfaekfaacgfdpdsffaSYGLAEA--TLFVSGGRRgqgipaleldaealarnrAEPGTGSVLMSCgrsqpgH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 384 DVQIID-DKGNVLPPGTEGDIGIRvKPirpiGIFSGYVDNPDKTA---ANIRGDFWL-LGDRGIKdEDGYFQFMGRADDI 458
Cdd:PRK05691 380 AVLIVDpQSLEVLGDNRVGEIWAS-GP----SIAHGYWRNPEASAktfVEHDGRTWLrTGDLGFL-RDGELFVTGRLKDM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 459 INSSGYRIGPSEVENalmehpaVVETAVisspDPVRGEVVKAFVV---------LASQF-----LSHDPEQLTKELQQHV 524
Cdd:PRK05691 454 LIVRGHNLYPQDIEK-------TVEREV----EVVRKGRVAAFAVnhqgeegigIAAEIsrsvqKILPPQALIKSIRQAV 522
|
570 580 590
....*....|....*....|....*....|....*.
3C5E_A 525 KSVtapYKYPRKIEFVLN---LPKTVTGKIQRAKLR 557
Cdd:PRK05691 523 AEA---CQEAPSVVLLLNpgaLPKTSSGKLQRSACR 555
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
41-561 |
1.07e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 45.19 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 41 SDVLDHWADMEK-AGKRPPSPALWW---VNGKGKELMW-NFRELSENSQQAANVLSgACGLQRGDRVAVVLPRVPEWWLV 115
Cdd:PLN02430 39 SDITTAWDIFSKsVEKYPDNKMLGWrriVDGKVGPYMWkTYKEVYEEVLQIGSALR-ASGAEPGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 116 ILGCIRAGLIFMPGTIQMKSTDILYRLQMSKAKAIVAGDEVIQEVdtVASECPSL-RIKLLVS-----EKSCD------- 182
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKEL--LEPDCKSAkRLKAIVSftsvtEEESDkasqigv 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 183 ---GWLNFKKLLNEASTthhcvETGSQEAS---AIYFTSGTSGLPKMAEHSYSSL-----GLKAKMDagwtglQASDIMw 251
Cdd:PLN02430 196 ktySWIDFLHMGKENPS-----ETNPPKPLdicTIMYTSGTSGDPKGVVLTHEAVatfvrGVDLFME------QFEDKM- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 252 TISDTGW----ILNILCSLMEPWAL--GACT-FVH------------LLPKF---DPLV-------ILKTLSSY-PIKSM 301
Cdd:PLN02430 264 THDDVYLsflpLAHILDRMIEEYFFrkGASVgYYHgdlnalrddlmeLKPTLlagVPRVferihegIQKALQELnPRRRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 302 MgAPIVYRMLLQQDLSSYK------------FPHLQN--------CVTVGESLLPETLENWRAQTGLDIRESYGQTET-G 360
Cdd:PLN02430 344 I-FNALYKYKLAWMNRGYShkkaspmadflaFRKVKAklggrlrlLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 361 LT--------CMVsktmkikpGYMGTAASCYDVQI-------IDDKGNvlPPgtEGDIGIRVKPirpigIFSGYVDNPDK 425
Cdd:PLN02430 423 PTtlgfpdemCML--------GTVGAPAVYNELRLeevpemgYDPLGE--PP--RGEICVRGKC-----LFSGYYKNPEL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 426 TAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIIN-SSGYRIGPSEVENALMEHPAVVETAVISspDPVRGEVVkAFVVL 504
Cdd:PLN02430 486 TEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEYLENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVP 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
3C5E_A 505 asqflshDPEQLTK--ELQQHVKSVTAPYKYPRKIEFVLNLPKTVTgkiQRAKLRDKEW 561
Cdd:PLN02430 563 -------NEENTNKwaKDNGFTGSFEELCSLPELKEHILSELKSTA---EKNKLRGFEY 611
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
410-557 |
1.11e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.14 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 410 IRPIGIFSGYVDnpdktAANIRGDFWL-LGDRGIKDEDGyFQFMGRADDIINSSGYRIGPSEVENALMEHPAVVETAVIS 488
Cdd:PRK05851 377 IRGASMMSGYLG-----QAPIDPDDWFpTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVA 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3C5E_A 489 SPDPVRGevVKAFVVLASQFLSHDPEQLTKELQQHVKSVTApyKYPRKIEFVL--NLPKTVTGKIQRAKLR 557
Cdd:PRK05851 451 VGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
354-504 |
1.99e-03 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 40.88 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 354 YGQTETGLTCMVSKTMKIKPGYMGTAASCYDVQIIddkgnvlPPGteGDIGIRVK-PirpiGIFSGYVDNPDKTAANIRG 432
Cdd:cd05921 328 LGATETAPTATFTHWPTERSGLIGLPAPGTELKLV-------PSG--GKYEVRVKgP----NVTPGYWRQPELTAQAFDE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 433 D-FWLLGDRGI----KDEDGYFQFMGR-ADDIINSSG--YRIGPSEVENALMEHPaVVETAVISSPDpvrGEVVKAFVVL 504
Cdd:cd05921 395 EgFYCLGDAAKladpDDPAKGLVFDGRvAEDFKLASGtwVSVGPLRARAVAACAP-LVHDAVVAGED---RAEVGALVFP 470
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
65-158 |
3.49e-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: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3C5E_A 65 VNGKGKE---LMWnfRELSENSQQAANVLSGACGLQRGDRVAVVLPRVPEWWLVILGCIRAGLIFMP------------- 128
Cdd:cd05905 5 LDSKGKEattLTW--GKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPieppdisqqlgfl 82
|
90 100 110
....*....|....*....|....*....|....
3C5E_A 129 -GTIQM---KSTDILYRLQMSKAKAIVAGDEVIQ 158
Cdd:cd05905 83 lGTCKVrvaLTVEACLKGLPKKLLKSKTAAEIAK 116
|
|
| |
