|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1-544 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 1021.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 1 MSRFTEKMFHNARTATTGMVTGEPHMPVRHTWGEVHERARCIAGGLAAAGVGLGDVVGVLAGFPVEIAPTAQALWMRGAS 80
Cdd:PRK07768 1 MSRFTEKMYANARTSPRGMVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 81 LTMLHQPTPRTDLAVWAEDTMTVIGMIEAKAVIVSEPFLVAIPILEQKGMQVLTVADLLASDPIGPIEVGEDDLALMQLT 160
Cdd:PRK07768 81 LTMLHQPTPRTDLAVWAEDTLRVIGMIGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAADPIDPVETGEDDLALMQLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 161 SGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMDFLRDTLLWAK 240
Cdd:PRK07768 161 SGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMDFLRDPLLWAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 241 LIDKYQGTMTAAPNFAYALLAKRLRRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPFGLRPSAILPAYGMAETT 320
Cdd:PRK07768 241 LISKYRGTMTAAPNFAYALLARRLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 321 LAVSFSECNAGLVVDEVDADLLAALRRAVPATKGNTRRLATLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGY 400
Cdd:PRK07768 321 LAVSFSPCGAGLVVDEVDADLLAALRRAVPATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 401 LTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHSRES 480
Cdd:PRK07768 401 LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREG 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889038433 481 FAVAVESNAFEDPAEVRRIEHQVAHEVVAEVDVRPRNVVVLGPGTIPKTPSGKLRRANSVTLVT 544
Cdd:PRK07768 481 FAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRANAAELVT 544
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
18-537 |
5.57e-176 |
|
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: 507.55 E-value: 5.57e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 18 GMVTGEPHMPVRHTWGEVHERARCIAGGLAAAGVGLGDVVGVlAGFPVEIAPTAQALWMRGASLTMLHQPTPRtdlaVWA 97
Cdd:cd05931 13 TFLDDEGGREETLTYAELDRRARAIAARLQAVGKPGDRVLLL-APPGLDFVAAFLGCLYAGAIAVPLPPPTPG----RHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 98 EDTMTVIGMIEAKAVIVSEPFLVAIP----ILEQKGMQVLTVADLLASDPIG---PIEVGEDDLALMQLTSGSTGSPKAV 170
Cdd:cd05931 88 ERLAAILADAGPRVVLTTAAALAAVRafaaSRPAAGTPRLLVVDLLPDTSAAdwpPPSPDPDDIAYLQYTSGSTGTPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 171 QITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMDFLRDTLLWAKLIDKYQGTMT 250
Cdd:cd05931 168 VVTHRNLLANVRQIRRAYGLD-PGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRWLRLISRYRATIS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 251 AAPNFAYALLAKRLRRQAKPGdFDLSTLRFALSGAEPVEPADVEDLLDAGKPFGLRPSAILPAYGMAETTLAVSFSECNA 330
Cdd:cd05931 247 AAPNFAYDLCVRRVRDEDLEG-LDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEATLFVSGGPPGT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 331 GLVVDEVDADLLAALRRAVPATKGNTRRLATLGPLLQDLEARIIDEQGD-VMPARGVGVIELRGESLTPGYLTMG----- 404
Cdd:cd05931 326 GPVVLRVDRDALAGRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASGYWGRPeatae 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 405 --GFIPAQDEHGWYDTGDLGYLTeEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGV-RPGCAVAVRLDAGHSRESF 481
Cdd:cd05931 406 tfGALAATDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlRPGCVAAFSVPDDGEERLV 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 889038433 482 AVAVESNAfEDPAEVRRIEHQVAHEVVAEVDVRPRNVVVLGPGTIPKTPSGKLRRA 537
Cdd:cd05931 485 VVAEVERG-ADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRR 539
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1-536 |
6.58e-101 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 314.40 E-value: 6.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 1 MSRFTEKMFHNARTATTGMVTGEPHMP--VRHTWGEVHERARCIAGGLAAAGVGLGDVVgvlAGFP-VEIAPTAQALWMR 77
Cdd:PRK05851 1 MNELAAALSDAMTASGRDLVVLDRESGlwRRHPWPEVHGRAENVAARLLDRDRPGAVGL---VGEPtVELVAAIQGAWLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 78 GASLTMLHQPTPRTDLAVWAEDTMTVIGMIEAKAVIVSEPFLVAIPILeQKGMQVLTVADLLA---SDPIGPIEVGEddL 154
Cdd:PRK05851 78 GAAVSILPGPVRGADDGRWADATLTRFAGIGVRTVLSHGSHLERLRAV-DSSVTVHDLATAAHtnrSASLTPPDSGG--P 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 155 ALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSWLPCFHDMGMVgFLTIPMFFGAELVKVTPMDFLRD 234
Cdd:PRK05851 155 AVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLA-FLLTAALAGAPLWLAPTTAFSAS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 235 TLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQAkpgDFDLSTLRFALSGAEPVEPADVEDLLDAGKPFGLRPSAILPAY 314
Cdd:PRK05851 234 PFRWLSWLSDSRATLTAAPNFAYNLIGKYARRVS---DVDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 315 GMAETTLAVSFSECNAGLVVDEVdadllaalrrAVPATKGnTRRLATLGPLLQDLEARIIDEQGDV-MPARGVGVIELRG 393
Cdd:PRK05851 311 GLAESTCAVTVPVPGIGLRVDEV----------TTDDGSG-ARRHAVLGNPIPGMEVRISPGDGAAgVAGREIGEIEIRG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 394 ESLTPGYLtmgGFIPAqDEHGWYDTGDLGYLTEEGhVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLD 473
Cdd:PRK05851 380 ASMMSGYL---GQAPI-DPDDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTG 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 889038433 474 AGHSRESFAVAVESNAfEDPAEVRRiehQVAHEVVAEVDVRPRNVVVLGPGTIPKTPSGKLRR 536
Cdd:PRK05851 455 EGSARPGLVIAAEFRG-PDEAGARS---EVVQRVASECGVVPSDVVFVAPGSLPRTSSGKLRR 513
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
105-537 |
4.45e-89 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 285.36 E-value: 4.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 105 GMIE---AKAVIVSE---PFLVAIpILEQKGMQVLTVADLLASdPIGPIEVGE---DDLALMQLTSGSTGSPKAVQITHR 175
Cdd:PRK09192 122 GMLAsaqPAAIITPDellPWVNEA-THGNPLLHVLSHAWFKAL-PEADVALPRptpDDIAYLQYSSGSTRFPRGVIITHR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 176 NIYSNAEAMFVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMffgAELVKVTPM---DFLRDTLLWAKLIDKYQGTMTAA 252
Cdd:PRK09192 200 ALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPV---ATQLSVDYLptrDFARRPLQWLDLISRNRGTISYS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 253 PNFAYALLAKRLRRQAKpGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPFGLRPSAILPAYGMAETTLAVSFSECNAGL 332
Cdd:PRK09192 277 PPFGYELCARRVNSKDL-AELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEATLAVSFSPLGSGI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 333 VVDEVDADLLAALRRAVPAtKGNTRRLATL---GPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMGGFIPA 409
Cdd:PRK09192 356 VVEEVDRDRLEYQGKAVAP-GAETRRVRTFvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDV 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 410 QDEHGWYDTGDLGYLtEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDaGHSRESFAVAVESNA 489
Cdd:PRK09192 435 LAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAFSIA-QENGEKIVLLVQCRI 512
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 889038433 490 fEDPAEVRRIEHQVAHEVVAEVDVrPRNVVVLGPGTIPKTPSGKLRRA 537
Cdd:PRK09192 513 -SDEERRGQLIHALAALVRSEFGV-EAAVELVPPHSLPRTSSGKLSRA 558
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
110-537 |
1.24e-85 |
|
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: 275.31 E-value: 1.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 110 KAVIVSEPFLVAiPILEQ------KGMQVLTVADLL--ASDPIGPIeVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNA 181
Cdd:cd05906 119 SPVVLTDAELVA-EFAGLetlsglPGIRVLSIEELLdtAADHDLPQ-SRPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 182 EAMFVGAQYDvDKDVMVSWLPcFHDMGMVGFLTI-PMFFGAELVKVTPMDFLRDTLLWAKLIDKYQGTMTAAPNFAYALL 260
Cdd:cd05906 197 AGKIQHNGLT-PQDVFLNWVP-LDHVGGLVELHLrAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFAFALL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 261 AKRLRRQaKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPFGLRPSAILPAYGMAET----TLAVSFSECNAGlvvde 336
Cdd:cd05906 275 NDLLEEI-EDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETcsgvIYSRSFPTYDHS----- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 337 vDADLLAALRRAVPATkgntrrlatlgpllqdlEARIIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIpaqd 411
Cdd:cd05906 349 -QALEFVSLGRPIPGV-----------------SMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYynnpeANAEAFT---- 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 412 EHGWYDTGDLGYLtEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPG--CAVAVRlDAGHSRESFAV--AVES 487
Cdd:cd05906 407 EDGWFRTGDLGFL-DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVR-DPGAETEELAIffVPEY 484
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 889038433 488 NAFEDPAE-VRRIEHQVAHEVVaevdVRPRNVVVLGPGTIPKTPSGKLRRA 537
Cdd:cd05906 485 DLQDALSEtLRAIRSVVSREVG----VSPAYLIPLPKEEIPKTSLGKIQRS 531
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
155-537 |
1.33e-77 |
|
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: 251.65 E-value: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 155 ALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMDFLRd 234
Cdd:COG0318 103 ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPG-DVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPER- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 235 tllWAKLIDKYQGT-MTAAPNFAYALLakrlrRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpFGLRpsaILPA 313
Cdd:COG0318 181 ---VLELIERERVTvLFGVPTMLARLL-----RHPEFARYDLSSLRLVVSGGAPLPPELLERFEER---FGVR---IVEG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 314 YGMAETTLAVSFSECNAGLvvdevdadllaalrravpatkgntRRLATLGPLLQDLEARIIDEQGDVMPARGVGVIELRG 393
Cdd:COG0318 247 YGLTETSPVVTVNPEDPGE------------------------RRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 394 ESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLD 473
Cdd:COG0318 303 PNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDE 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889038433 474 AGHSRESFAVAVESNAFEDPAEVRRiehqVAHEVVAEVDVrPRNVVVLgpGTIPKTPSGKLRRA 537
Cdd:COG0318 383 KWGERVVAFVVLRPGAELDAEELRA----FLRERLARYKV-PRRVEFV--DELPRTASGKIDRR 439
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
152-536 |
2.97e-71 |
|
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: 236.23 E-value: 2.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMDF 231
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK-TKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 LRDTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQaKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPFGLRPSAIL 311
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPE-KANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAIL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 312 PAYGMAETTLAVSFSECNAGLVVDEVDADLLAALRRAVPATKGNTR--RLATLGPLLQDLEARIIDEQGDVMPARGVGVI 389
Cdd:cd05908 264 PVYGLAEASVGASLPKAQSPFKTITLGRRHVTHGEPEPEVDKKDSEclTFVEVGKPIDETDIRICDEDNKILPDGYIGHI 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 390 ELRGESLTPGYL-----TMGGFIPaqdeHGWYDTGDLGYLtEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRP 464
Cdd:cd05908 344 QIRGKNVTPGYYnnpeaTAKVFTD----DGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVEL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 465 GCAVA--VRLDAGHSRESFAVAVESNAFEDPAE-VRRIEHQV-------AHEVVaevdvrPRNVvvlgpgtIPKTPSGKL 534
Cdd:cd05908 419 GRVVAcgVNNSNTRNEEIFCFIEHRKSEDDFYPlGKKIKKHLnkrggwqINEVL------PIRR-------IPKTTSGKV 485
|
..
gi 889038433 535 RR 536
Cdd:cd05908 486 KR 487
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
131-537 |
2.68e-64 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 228.13 E-value: 2.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 131 QVLTVADL---LASDPIGPiEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDV-DKDVMVSWLPCFHD 206
Cdd:PRK05691 143 ELLCVDTLdpaLAEAWQEP-ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLnPDDVIVSWLPLYHD 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 207 MGMVGFLTIPMFFGAELVKVTPMDFLRDTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQAKPGdFDLSTLRFALSGAE 286
Cdd:PRK05691 222 MGLIGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALER-LDLSRWRVAYSGSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 287 PVEPADVEDLLDAGKPFGLRPSAILPAYGMAETTLAVSFSECNAGLVVDEVDADLLAAlRRAVPatkGNTRRLATLGPLL 366
Cdd:PRK05691 301 PIRQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALAR-NRAEP---GTGSVLMSCGRSQ 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 367 QDLEARIIDEQ-GDVMPARGVGVIELRGESLTPGY-----LTMGGFIpAQDEHGWYDTGDLGYLtEEGHVVVCGRVKDVI 440
Cdd:PRK05691 377 PGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYwrnpeASAKTFV-EHDGRTWLRTGDLGFL-RDGELFVTGRLKDML 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 441 IMAGRNIYPTDIERAAGR-VDGVRPG--CAVAVRLDAghsRESFAVAVE---SNAFEDPAE--VRRIEHQVAhEVVAEVd 512
Cdd:PRK05691 455 IVRGHNLYPQDIEKTVEReVEVVRKGrvAAFAVNHQG---EEGIGIAAEisrSVQKILPPQalIKSIRQAVA-EACQEA- 529
|
410 420
....*....|....*....|....*
gi 889038433 513 vrPRNVVVLGPGTIPKTPSGKLRRA 537
Cdd:PRK05691 530 --PSVVLLLNPGALPKTSSGKLQRS 552
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
146-537 |
1.22e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 219.22 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 146 PIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMVGFLtIPMFFGAELVK 225
Cdd:PRK07769 174 PPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQ-EGDRGVSWLPFFHDMGLITVL-LPALLGHYITF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 226 VTPMDFLRDTLLWAKLI----DKYQGTMTAAPNFAYALLAKR-LRRQAKPgDFDLSTLRFALSGAEPVEPADVEDLLDAG 300
Cdd:PRK07769 252 MSPAAFVRRPGRWIRELarkpGGTGGTFSAAPNFAFEHAAARgLPKDGEP-PLDLSNVKGLLNGSEPVSPASMRKFNEAF 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 301 KPFGLRPSAILPAYGMAETTLAVSFSECNAGLVVDEVDADLLAALRRA-VPATKGNTRRLATLGPLLQDLEARIID-EQG 378
Cdd:PRK07769 331 APYGLPPTAIKPSYGMAEATLFVSTTPMDEEPTVIYVDRDELNAGRFVeVPADAPNAVAQVSAGKVGVSEWAVIVDpETA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 379 DVMPARGVGVIELRGESLTPGYL------------TMGGFIP------AQDEHGWYDTGDLG-YLteEGHVVVCGRVKDV 439
Cdd:PRK07769 411 SELPDGQIGEIWLHGNNIGTGYWgkpeetaatfqnILKSRLSeshaegAPDDALWVRTGDYGvYF--DGELYITGRVKDL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 440 IIMAGRNIYPTDIERAAGRVD-GVRPGCAVA----------VRLDAGHSRESFAVAVESNAF----EDPAEVRRIEHQ-V 503
Cdd:PRK07769 489 VIIDGRNHYPQDLEYTAQEATkALRTGYVAAfsvpanqlpqVVFDDSHAGLKFDPEDTSEQLvivaERAPGAHKLDPQpI 568
|
410 420 430
....*....|....*....|....*....|....*....
gi 889038433 504 AHEVVAEVDVR----PRNVVVLGPGTIPKTPSGKL-RRA 537
Cdd:PRK07769 569 ADDIRAAIAVRhgvtVRDVLLVPAGSIPRTSSGKIaRRA 607
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
153-535 |
3.39e-63 |
|
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: 210.22 E-value: 3.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGMVGFLTiPMFFGAELVkvtpMDFL 232
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEG-DVFLSTLPLFHIGGLFGLLG-ALLAGGTVV----LLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 233 RDTLLWAKLIDKYQGTMTAAPNFAYAllakRLRRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPfglrpsAILP 312
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLA----RLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGI------KLVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 313 AYGMAETTLAVSFSecnaglVVDEVDadllaalrravpatkgntRRLATLGPLLQDLEARIIDEQGDVMPARGVGVIELR 392
Cdd:cd04433 145 GYGLTETGGTVATG------PPDDDA------------------RKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 393 GESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRl 472
Cdd:cd04433 201 GPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVP- 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889038433 473 DAGHSRESFAVAV-ESNAFEDPAEVRRIehqvAHEVVAEVDVrPRNVVVLGPgtIPKTPSGKLR 535
Cdd:cd04433 280 DPEWGERVVAVVVlRPGADLDAEELRAH----VRERLAPYKV-PRRVVFVDA--LPRTASGKID 336
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
137-540 |
8.97e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 215.58 E-value: 8.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 137 DLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDV-----MVSWLPCFHDMGMVG 211
Cdd:PRK05850 145 DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFGDTGGVPppdttVVSWLPFYHDMGLVL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 212 FLTIPMFFGAELVKVTPMDFLRDTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQAKPGdFDLSTLRFALSGAEPVEPA 291
Cdd:PRK05850 225 GVCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSDDDMAG-LDLGGVLGIISGSERVHPA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 292 DVEDLLDAGKPFGLRPSAILPAYGMAETTLAVSFSECNAGLVVDEVDADLLAAlRRAVPATKGNTRRLATLGpLLQDLEA 371
Cdd:PRK05850 304 TLKRFADRFAPFNLRETAIRPSYGLAEATVYVATREPGQPPESVRFDYEKLSA-GHAKRCETGGGTPLVSYG-SPRSPTV 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 372 RIIDEQGDV-MPARGVGVIELRGESLTPGY--------LTMGGFI----PAQDEHGWYDTGDLGYLTeEGHVVVCGRVKD 438
Cdd:PRK05850 382 RIVDPDTCIeCPAGTVGEIWVHGDNVAAGYwqkpeeteRTFGATLvdpsPGTPEGPWLRTGDLGFIS-EGELFIVGRIKD 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 439 VIIMAGRNIYPTDIER-----AAGRVdgvrpgCAVAVrldAGHSRESFAVAVESNAFEDPAEVRRIE-HQVAHEVVAEVD 512
Cdd:PRK05850 461 LLIVDGRNHYPDDIEAtiqeiTGGRV------AAISV---PDDGTEKLVAIIELKKRGDSDEEAMDRlRTVKREVTSAIS 531
|
410 420 430
....*....|....*....|....*....|..
gi 889038433 513 ----VRPRNVVVLGPGTIPKTPSGKLRRANSV 540
Cdd:PRK05850 532 kshgLSVADLVLVAPGSIPITTSGKIRRAACV 563
|
|
| FadD32_Coryne |
NF040633 |
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ... |
130-538 |
4.27e-58 |
|
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.
Pssm-ID: 468603 [Multi-domain] Cd Length: 613 Bit Score: 203.73 E-value: 4.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 130 MQVLTVADLLASDPIGPIevgeDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYdvdKDVM--VSWLPCFHDM 207
Cdd:NF040633 183 MATIEGQPLLAPAGTDPS----DDTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQL---KTPLrlVSWLPLHHDM 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 208 GMV--GFLTIpmfFGAELVKVTPMDFLRDTLLWAKLIDKYQGTM---TAAPNFAYAlLAKRLRRQAKPGDFDLSTLRFAL 282
Cdd:NF040633 256 GIIlaAFVTI---LGLEFELMSPRDFIQQPKRWVDQLSRREDDVnvyTVVPNFALE-LAARYANPEEGEDLDLSAVDGII 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 283 SGAEPVEPADVEDLLDAGKPFGLRPSAILPAYGMAETTLAVSFSECNAGLVVDEVDADLLAAlRRAVPATKG--NTRRLA 360
Cdd:NF040633 332 IGSEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERPLFTYFDREALAE-GRAVEVAEDseNAVPFA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 361 TLGPLLQDLEARIID-EQGDVMPARGVGVIELRGESLTPGYL------------TMGGFIPAQD------EHGWYDTGDL 421
Cdd:NF040633 411 SNGQVVRPQVLAIVDpETGQELPDGTVGEIWVHGDNMAAGYLdreeetaetfrnTLGERLAENSraegapEDNWMATGDL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 422 GYLTeEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRV-DGVRPGCAVAVRLdAGHSRESFAVAVESNAFEDPAEVRRIE 500
Cdd:NF040633 491 GVIV-DGELYITGRLKDLIVIAGRNHYPQDIEATVQEAsDHIRPDSVAAFAV-PGDDVEKLVILAERDDEADESGDAEAI 568
|
410 420 430
....*....|....*....|....*....|....*....
gi 889038433 501 HQVAHEVVAEVDVRPRNVVVLGPGTIPKTPSGKL-RRAN 538
Cdd:NF040633 569 EAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIaRRVN 607
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
88-537 |
5.69e-58 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 203.43 E-value: 5.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 88 TPRTDlAVWAEDTMTVIGMIEAKAVIVSEpFLVAIPILEQKGMQVLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSP 167
Cdd:PRK12476 131 AERLD-TALRDAEPTVVLTTTAAAEAVEG-FLRNLPRLRRPRVIAIDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 168 KAVQITHRNIYSNAEAMFVGAQYdVDKDVM-VSWLPCFHDMG--MVGFltiPMFFGAELVKVTPMDFLRDTLLWAKLID- 243
Cdd:PRK12476 209 VGVEITHRAVGTNLVQMILSIDL-LDRNTHgVSWLPLYHDMGlsMIGF---PAVYGGHSTLMSPTAFVRRPQRWIKALSe 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 244 --KYQGTMTAAPNFAYALLAKRlrRQAKPGD-FDLSTLRFaLSGAEPVEPADVEDLLDAGKPFGLRPSAILPAYGMAETT 320
Cdd:PRK12476 285 gsRTGRVVTAAPNFAYEWAAQR--GLPAEGDdIDLSNVVL-IIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEAT 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 321 LAVSFSECNAGLVVDEVDADLLAAlRRAVPATKGNTRRLA--TLGPLLQDLEARIIDE-QGDVMPARGVGVIELRGESLT 397
Cdd:PRK12476 362 LFVATIAPDAEPSVVYLDREQLGA-GRAVRVAADAPNAVAhvSCGQVARSQWAVIVDPdTGAELPDGEVGEIWLHGDNIG 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 398 PGY--------LTMGGFIPAQDEHG-----------WYDTGDLG-YLteEGHVVVCGRVKDVIIMAGRNIYPTDIERAAG 457
Cdd:PRK12476 441 RGYwgrpeeteRTFGAKLQSRLAEGshadgaaddgtWLRTGDLGvYL--DGELYITGRIADLIVIDGRNHYPQDIEATVA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 458 RVDG-VRPGCAVAVRLDAGHSRESFAVAvesnafEDPAEVRRIEHQVAHEVV-AEVD----VRPRNVVVLGPGTIPKTPS 531
Cdd:PRK12476 519 EASPmVRRGYVTAFTVPAEDNERLVIVA------ERAAGTSRADPAPAIDAIrAAVSrrhgLAVADVRLVPAGAIPRTTS 592
|
....*..
gi 889038433 532 GKL-RRA 537
Cdd:PRK12476 593 GKLaRRA 599
|
|
| FAAL_FadD32 |
NF038339 |
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ... |
132-537 |
1.48e-57 |
|
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.
Pssm-ID: 468483 [Multi-domain] Cd Length: 625 Bit Score: 202.64 E-value: 1.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 132 VLTVADLLASDPIGPiEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMVG 211
Cdd:NF038339 158 VDAVPDSVGSTWVRP-DADLDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELD-ENSRGVTWLPLFHDMGLLT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 212 FLtIPMFFGAELVKVTPMDFLRDTLLWAK---LIDKYQGTMTAAPNFAYALLAkrLRRQAKPGD-FDLSTLRFALSGAEP 287
Cdd:NF038339 236 VI-LPALGGKYITIMSPAAFVRRPGRWIRelaAVSDGAGTFAAAPNFAFEHAA--ARGLPKEGEpLDLSNVIGLINGSEP 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 288 VEPADVEDLLDAGKPFGLRPSAILPAYGMAETTLAVSFSECNAGLVVDEVDADLLAAlRRAVPATKGNTRRLATL--GPL 365
Cdd:NF038339 313 VTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAKVIYVDREELNA-GRIVEVDPDAPNAVAQVscGYV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 366 LQDLEARIID-EQGDVMPARGVGVIELRGESLTPGYL-----TMGGF-------IP-------AQDEHGWYDTGDLG-YL 424
Cdd:NF038339 392 ARSQWAVIVDpETGTELPDGQVGEIWLHGNNIGTGYWgrpeeTEETFhnklksrLEegshaegAPEDANWMRTGDYGvYY 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 425 teEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRV-DGVRPGCAVA-------------------VRLDAGHSRESFAVA 484
Cdd:NF038339 472 --DGELYITGRVKDLVIVDGRNHYPQDLEYSAQEAsKALRPGFVAAfsvpanqlpaevfenshsgLKYDADDSSEQLVIV 549
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 889038433 485 VESNAFEDPAEVRRIEHQVAHEVVAEVDVRPRNVVVLGPGTIPKTPSGKL-RRA 537
Cdd:NF038339 550 AERAPGAGKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIaRRA 603
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
108-441 |
8.97e-53 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 184.82 E-value: 8.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 108 EAKAVIVSEPFLVA--------------IPILEQ----KGMQVLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKA 169
Cdd:pfam00501 93 GAKVLITDDALKLEellealgklevvklVLVLDRdpvlKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 170 VQITHRNIYSNAEAMFVGAQYD---VDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMDFLrDTLLWAKLIDKYQ 246
Cdd:pfam00501 173 VMLTHRNLVANVLSIKRVRPRGfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAL-DPAALLELIERYK 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 247 GT-MTAAPNFAYALLakrlrRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGkpfglrPSAILPAYGMAETTLAVSF 325
Cdd:pfam00501 252 VTvLYGVPTLLNMLL-----EAGAPKRALLSSLRLVLSGGAPLPPELARRFRELF------GGALVNGYGLTETTGVVTT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 326 secnaglvvdevdadllaalrraVPATKGNTRRLATLGPLLQDLEARIIDEQ-GDVMPARGVGVIELRGESLTPGY---- 400
Cdd:pfam00501 321 -----------------------PLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYlndp 377
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 889038433 401 -LTMGGFipaqDEHGWYDTGDLGYLTEEGHVVVCGRVKDVII 441
Cdd:pfam00501 378 eLTAEAF----DEDGWYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
109-536 |
9.22e-49 |
|
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: 175.44 E-value: 9.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 109 AKAVIVSEPFlvaipileqkgmqvltvADLLASD--PIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAM-F 185
Cdd:cd05936 97 AKALIVAVSF-----------------TDLLAAGapLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIkA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 186 VGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVT---PMDFLrdtllwaKLIDKYQGT-MTAAPNFAYALLa 261
Cdd:cd05936 160 WLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPrfrPIGVL-------KEIRKHRVTiFPGVPTMYIALL- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 262 krlrRQAKPGDFDLSTLRFALSGAEPVEPADVEDLldaGKPFGLRpsaILPAYGMAETTLAVSFSECNAGlvvdevdadl 341
Cdd:cd05936 232 ----NAPEFKKRDFSSLRLCISGGAPLPVEVAERF---EELTGVP---IVEGYGLTETSPVVAVNPLDGP---------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 342 laalrravpatkgntRRLATLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMGGfipAQDEH---GWYDT 418
Cdd:cd05936 292 ---------------RKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPE---ETAEAfvdGWLRT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 419 GDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRlDAGHSRESFAVAV-ESNAFEDPAEVr 497
Cdd:cd05936 354 GDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVP-DPYSGEAVKAFVVlKEGASLTEEEI- 431
|
410 420 430
....*....|....*....|....*....|....*....
gi 889038433 498 rIEHqvAHEVVAEVDVrPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd05936 432 -IAF--CREQLAGYKV-PRQVEFR--DELPKSAVGKILR 464
|
|
| FAAL_FadD21 |
NF038337 |
fatty-acid--AMP ligase FAAL21/FadD21; |
150-540 |
2.92e-47 |
|
fatty-acid--AMP ligase FAAL21/FadD21;
Pssm-ID: 439631 [Multi-domain] Cd Length: 579 Bit Score: 173.52 E-value: 2.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 150 GEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFvgAQYDVDKD-------VMVSWLPCFHDMGMVGFLTIPMFFGAE 222
Cdd:NF038337 161 DAPSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLM--AAYFPDTNgvaprdtTIVSWLPFYHDMGLVLGVIAPILGGYR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 223 LVKVTPMDFLRDTLLWAKLIDKYQGTMTAAPNFAYAlLAKRLRRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKP 302
Cdd:NF038337 239 SELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFE-LAVRKTTDADLAGLDLGNVIGIVSGAERIHPATLDRFCKRFAP 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 303 FGLRPSAILPAYGMAETTLAV-SFSECNAGLVVDEVDADLLAALRRAVPATKGNtrrlatlgPLL-----QDLEARIID- 375
Cdd:NF038337 318 YNFREDMMQPSYGLAEATVYVaSRAEGGAPEVVHFEPEKLSEGSAQRCEARTGS--------PLLsygtpTSPTVRIVDp 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 376 EQGDVMPARGVGVIELRGESLTPGYL--------TMGGFI----PAQDEHGWYDTGDLGYLTeEGHVVVCGRVKDVIIMA 443
Cdd:NF038337 390 DTCIECPAGTVGEIWVHGDNVAEGYWqkpeetrrTFGGVLanpsPGTPEGPWLRTGDLGFIS-EDEMFIVGRMKDLLIVY 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 444 GRNIYPTDIERAAGRVDGVRPGcAVAVRLDaghSRESFAVAVE-SNAFEDPAEVRRIEHQVAHEVVAEVD----VRPRNV 518
Cdd:NF038337 469 GRNHYPEDIESTVQEITGGRVA-AISVPVD---ETEKLVTIIElKKRGDSDEEAMRKLDAVKNNVTAAISrshgLNVADL 544
|
410 420
....*....|....*....|..
gi 889038433 519 VVLGPGTIPKTPSGKLRRANSV 540
Cdd:NF038337 545 VLVPPGSIPTTTSGKIRRAACV 566
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
108-537 |
6.96e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 168.44 E-value: 6.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 108 EAKAVIVSEPFL-VAIPILEQ-----------------KGMQVLTVADLLA--SDPIGPIEVGEDDLALMQLTSGSTGSP 167
Cdd:PRK06187 103 EDRVVLVDSEFVpLLAAILPQlptvrtvivegdgpaapLAPEVGEYEELLAaaSDTFDFPDIDENDAAAMLYTSGTTGHP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 168 KAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMvGFLTIPMFFGAELVkvTPMDFLRDTLLwaKLIDKYQG 247
Cdd:PRK06187 183 KGVVLSHRNLFLHSLAVCAWLKLS-RDDVYLVIVPMFHVHAW-GLPYLALMAGAKQV--IPRRFDPENLL--DLIETERV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 248 TMT-AAPNFAYALLakrlrRQAKPGDFDLSTLRFALSGAEPVEPAdvedLLDAGKP-FGLRpsaILPAYGMAETTLAVSF 325
Cdd:PRK06187 257 TFFfAVPTIWQMLL-----KAPRAYFVDFSSLRLVIYGGAALPPA----LLREFKEkFGID---LVQGYGMTETSPVVSV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 326 secnaglvvdevdadllAALRRAVPAtkGNTRRLATlGPLLQDLEARIIDEQGDVMPARG--VGVIELRGESLTPGYLTM 403
Cdd:PRK06187 325 -----------------LPPEDQLPG--QWTKRRSA-GRPLPGVEARIVDDDGDELPPDGgeVGEIIVRGPWLMQGYWNR 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 404 ggfiPAQDE----HGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpgcAVAV--------- 470
Cdd:PRK06187 385 ----PEATAetidGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVA---EVAVigvpdekwg 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 889038433 471 -RLDAghsresfAVAVESNAFEDPAEVRriEHqvAHEVVAEVdVRPRNVVVLgpGTIPKTPSGK-LRRA 537
Cdd:PRK06187 458 eRPVA-------VVVLKPGATLDAKELR--AF--LRGRLAKF-KLPKRIAFV--DELPRTSVGKiLKRV 512
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
152-536 |
3.30e-41 |
|
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: 153.92 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGMvGFLTIPMFF-GAELVkvtPMD 230
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPD-DVLLVVAPLFHIGGL-GVFTLPTLLrGGTVV---ILR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 FLRDTLLWAkLIDKYQGTMT-AAPNFAYALLakrlrRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPFglrpsa 309
Cdd:cd17631 173 KFDPETVLD-LIERHRVTSFfLVPTMIQALL-----QHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKF------ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 310 iLPAYGMAETTLAVSFsecnagLVVDEVDADLLAAlRRAVPATkgntrrlatlgpllqdlEARIIDEQGDVMPARGVGVI 389
Cdd:cd17631 241 -VQGYGMTETSPGVTF------LSPEDHRRKLGSA-GRPVFFV-----------------EVRIVDPDGREVPPGEVGEI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 390 ELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpGCAVA 469
Cdd:cd17631 296 VVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVA-EVAVI 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 889038433 470 VRLDA--GHSRESFAVAVESNAfEDPAEVrrIEHqvAHEVVAEVDvRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd17631 375 GVPDEkwGEAVVAVVVPRPGAE-LDEDEL--IAH--CRERLARYK-IPKSVEFV--DALPRNATGKILK 435
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
152-536 |
5.37e-40 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 148.58 E-value: 5.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAeaMFVG-AQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMD 230
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNG--YFIGeRLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 FLRDTLlwaKLIDKYQGT-MTAAPNFAYALLakrlrRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpfgLRPSA 309
Cdd:cd05917 80 DPLAVL---EAIEKEKCTaLHGVPTMFIAEL-----EHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEV-----MNMKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 310 ILPAYGMAETTlAVSFsecnAGLVVDEVDadllaalrravpatkgntRRLATLGPLLQDLEARIIDEQGDVMPARGVgvi 389
Cdd:cd05917 147 VTIAYGMTETS-PVST----QTRTDDSIE------------------KRVNTVGRIMPHTEAKIVDPEGGIVPPVGV--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 390 elRGESLTPGYLTMGGFI-------PAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGV 462
Cdd:cd05917 201 --PGELCIRGYSVMKGYWndpektaEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKV 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 889038433 463 RPGCAVAVRlDAGHSRESFA-VAVESNAFEDPAEVRR-IEHQVAHEVVaevdvrPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd05917 279 SDVQVVGVP-DERYGEEVCAwIRLKEGAELTEEDIKAyCKGKIAHYKV------PRYVFFV--DEFPLTVSGKIQK 345
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
148-534 |
2.30e-38 |
|
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: 146.97 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 148 EVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAE--AMFVGAQYDVDkDVMVSWLPCFHDMGMVGFLTIpMFFGAELVk 225
Cdd:cd05911 142 KDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSqvQTFLYGNDGSN-DVILGFLPLYHIYGLFTTLAS-LLNGATVI- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 226 VTPmDFlrDTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQAkpgdFDLSTLRFALSGAEPVEpADVEDLLDAGKPfgl 305
Cdd:cd05911 219 IMP-KF--DSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDK----YDLSSLRVILSGGAPLS-KELQELLAKRFP--- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 306 rPSAILPAYGMAETTLAVSfsecnaglvvdevdadllaalrravpATKGNTRRLATLGPLLQDLEARIIDEQG-DVMPAR 384
Cdd:cd05911 288 -NATIKQGYGMTETGGILT--------------------------VNPDGDDKPGSVGRLLPNVEAKIVDDDGkDSLGPN 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 385 GVGVIELRGESLTPGYL-----TMGgfipAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRV 459
Cdd:cd05911 341 EPGEICVRGPQVMKGYYnnpeaTKE----TFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEH 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 460 DGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRR-IEHQVAH------EVVAeVDvrprnvvvlgpgTIPKTPSG 532
Cdd:cd05911 417 PGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDyVAKKVASykqlrgGVVF-VD------------EIPKSASG 483
|
..
gi 889038433 533 KL 534
Cdd:cd05911 484 KI 485
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
138-536 |
1.21e-35 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 138.50 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 138 LLASDPigpievgeDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFvGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPM 217
Cdd:cd05907 81 LFVEDP--------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALA-ERLPATEGDRHLSFLPLAHVFERRAGLYVPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 218 FFGAELVKVTPMDFLRDTL-------------LWAKLIDKYQgtMTAAPNFAYALLAKRLrrqakpgdfdLSTLRFALSG 284
Cdd:cd05907 152 LAGARIYFASSAETLLDDLsevrptvflavprVWEKVYAAIK--VKAVPGLKRKLFDLAV----------GGRLRFAASG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 285 AEPVEPADVEDLLDAGKPfglrpsaILPAYGMAETTLAVSFSEcnaglvvdevdadllaalrravpatkGNTRRLATLGP 364
Cdd:cd05907 220 GAPLPAELLHFFRALGIP-------VYEGYGLTETSAVVTLNP--------------------------PGDNRIGTVGK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 365 LLQDLEARIIDEqgdvmpargvGVIELRGESLTPGYLTM-GGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMA 443
Cdd:cd05907 267 PLPGVEVRIADD----------GEILVRGPNVMLGYYKNpEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 444 -GRNIYPTDIERAAGRV----------DGvRPGCAVAVRLDAghsrESFAVAVESN--AFEDPAEVRRIEHQVAH--EVV 508
Cdd:cd05907 337 gGKNISPEPIENALKASplisqavvigDG-RPFLVALIVPDP----EALEAWAEEHgiAYTDVAELAANPAVRAEieAAV 411
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 889038433 509 AEVDVR------PRNVVVLG------PGTIpkTPSGKLRR 536
Cdd:cd05907 412 EAANARlsryeqIKKFLLLPepftieNGEL--TPTLKLKR 449
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
151-536 |
9.47e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 136.42 E-value: 9.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMD 230
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG-KGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 FLRdtllwAKLIDKYQGTMTAAPNFAYALLAKR--------------LRRQAKPGDFDLSTL-------------RFALS 283
Cdd:cd05914 167 SAK-----IIALAFAQVTPTLGVPVPLVIEKIFkmdiipkltlkkfkFKLAKKINNRKIRKLafkkvheafggniKEFVI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 284 GAEPVEPADVEDLLDAGKPFGLrpsailpAYGMAETTLAVSFSecnaglvvdevdadllaalrraVPatkgNTRRLATLG 363
Cdd:cd05914 242 GGAKINPDVEEFLRTIGFPYTI-------GYGMTETAPIISYS----------------------PP----NRIRLGSAG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 364 PLLQDLEARIIDEQgdvmPARGVGVIELRGESLTPGY-----LTMGGFipaqDEHGWYDTGDLGYLTEEGHVVVCGRVKD 438
Cdd:cd05914 289 KVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYyknpeATAEAF----DKDGWFHTGDLGKIDAEGYLYIRGRKKE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 439 VIIM-AGRNIYPTDIERAagrvdgVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAE--VRRIEHQVAHEVVAEVDVRP 515
Cdd:cd05914 361 MIVLsSGKNIYPEEIEAK------INNMPFVLESLVVVQEKKLVALAYIDPDFLDVKAlkQRNIIDAIKWEVRDKVNQKV 434
|
410 420
....*....|....*....|....*.
gi 889038433 516 RNV-----VVLGPGTIPKTPSGKLRR 536
Cdd:cd05914 435 PNYkkiskVKIVKEEFEKTPKGKIKR 460
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
138-536 |
2.69e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 136.67 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 138 LLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeAM---FVGAQYDvDKDVMVSWLPCFHDMGMVGFLT 214
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-AQgkaWVPGLGD-GPERVLAALPMFHAYGLTLCLT 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 215 IPMFFGAELVkVTP---MDflrdtlLWAKLIDKYQGT-MTAAPNfayalLAKRLRRQAKPGDFDLSTLRFALSGAEPVEP 290
Cdd:PRK05605 283 LAVSIGGELV-LLPapdID------LILDAMKKHPPTwLPGVPP-----LYEKIAEAAEERGVDLSGVRNAFSGAMALPV 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 291 ADVEDLLDAGKpfGLrpsaILPAYGMAETTlavsfsecnaglvvdevdadllaalrravPATKGN----TRRLATLGPLL 366
Cdd:PRK05605 351 STVELWEKLTG--GL----LVEGYGLTETS-----------------------------PIIVGNpmsdDRRPGYVGVPF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 367 QDLEARIIDEQ--GDVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAG 444
Cdd:PRK05605 396 PDTEVRIVDPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGG 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 445 RNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRriehQVAHEVVAEVDVrPRNVVVLgpG 524
Cdd:PRK05605 476 FNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLR----AYCREHLTRYKV-PRRFYHV--D 548
|
410
....*....|..
gi 889038433 525 TIPKTPSGKLRR 536
Cdd:PRK05605 549 ELPRDQLGKVRR 560
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
151-536 |
3.63e-34 |
|
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: 135.13 E-value: 3.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAmfVGAQYDV-DKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVkvTPM 229
Cdd:cd05926 148 PDDLALILHTSGTTGRPKGVPLTHRNLAASATN--ITNTYKLtPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVV--LPP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 230 DFlRDTLLWaKLIDKYQGT-MTAAPNFAYALLAkrlRRQAKPGDfDLSTLRFALSGAEPVEPADVEDLldaGKPFGlrpS 308
Cdd:cd05926 224 RF-SASTFW-PDVRDYNATwYTAVPTIHQILLN---RPEPNPES-PPPKLRFIRSCSASLPPAVLEAL---EATFG---A 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 309 AILPAYGMAETTLAVSfseCNAglvvdevdadllaalrraVPATKgntRRLATLGPLlQDLEARIIDEQGDVMPARGVGV 388
Cdd:cd05926 292 PVLEAYGMTEAAHQMT---SNP------------------LPPGP---RKPGSVGKP-VGVEVRILDEDGEILPPGVVGE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 389 IELRGESLTPGYL-----TMGGFipaqDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVR 463
Cdd:cd05926 347 ICLRGPNVTRGYLnnpeaNAEAA----FKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVL 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 889038433 464 PGCAVAVRlDAGHSRESFAVAV-ESNAFEDPAEVRRiehQVAHEVVA-EVdvrPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd05926 423 EAVAFGVP-DEKYGEEVAAAVVlREGASVTEEELRA---FCRKHLAAfKV---PKKVYFV--DELPKTATGKIQR 488
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
151-534 |
6.53e-34 |
|
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: 134.38 E-value: 6.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGMVGFLTIPMFFGAELV-KVTPM 229
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPE-DVVFGALPFFHSFGLTGCLWLPLLSGIKVVfHPNPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 230 DFLRdtllWAKLIDKYQGT-MTAAPNF--AYAllakrlrRQAKPGDFdlSTLRFALSGAEPVEPADVEDLLDAgkpFGLR 306
Cdd:cd05909 225 DYKK----IPELIYDKKATiLLGTPTFlrGYA-------RAAHPEDF--SSLRLVVAGAEKLKDTLRQEFQEK---FGIR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 307 psaILPAYGMAETTLAVSfseCNaglvvdevdadllaalrravpaTKGNTRRLATLGPLLQDLEARIIDEQGDVMPARGV 386
Cdd:cd05909 289 ---ILEGYGTTECSPVIS---VN----------------------TPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 387 -GVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPG 465
Cdd:cd05909 341 gGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNE 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 889038433 466 CAVAVRLDAGHSRESFAVAVESNAfeDPAEVRRI--EHQVAHEVVaevdvrPRNVVVLgpGTIPKTPSGKL 534
Cdd:cd05909 421 VAVVSVPDGRKGEKIVLLTTTTDT--DPSSLNDIlkNAGISNLAK------PSYIHQV--EEIPLLGTGKP 481
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
78-536 |
7.79e-34 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 135.85 E-value: 7.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 78 GASLTMLHQPTPRTDLAvwaEDTMTVIGMIEA-KAVI-------VSEPFLVAIPILEQK-GMQVLTVADLLASDP----I 144
Cdd:PRK07529 129 GAKVLVTLGPFPGTDIW---QKVAEVLAALPElRTVVevdlaryLPGPKRLAVPLIRRKaHARILDFDAELARQPgdrlF 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 145 GPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGMVGFLTIPMFFGAELV 224
Cdd:PRK07529 206 SGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPG-DTVFCGLPLFHVNALLVTGLAPLARGAHVV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 225 KVTPMDFLRDTL---LWaKLIDKYQ-GTMTAAPNfAYALLAKRlrrqaKPGDFDLSTLRFALSGAEPVEPADVEDLLDAG 300
Cdd:PRK07529 285 LATPQGYRGPGVianFW-KIVERYRiNFLSGVPT-VYAALLQV-----PVDGHDISSLRYALCGAAPLPVEVFRRFEAAT 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 301 kpfGLRpsaILPAYGMAETTLAVSfseCNaglvvdevdadllaalrravPAtkGNTRRLATLGPLL--QDLEARIIDEQG 378
Cdd:PRK07529 358 ---GVR---IVEGYGLTEATCVSS---VN--------------------PP--DGERRIGSVGLRLpyQRVRVVILDDAG 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 379 DVM---PARGVGVIELRGESLTPGYLTmggfiPAQD-----EHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPT 450
Cdd:PRK07529 407 RYLrdcAVDEVGVLCIAGPNVFSGYLE-----AAHNkglwlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPA 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 451 DIERAAGRVDGVRPGCAVAvRLDAgHSRESFAVAVE--SNAFEDPAEVRriEHQVAHevVAEVDVRPRNVVVLGPgtIPK 528
Cdd:PRK07529 482 AIEEALLRHPAVALAAAVG-RPDA-HAGELPVAYVQlkPGASATEAELL--AFARDH--IAERAAVPKHVRILDA--LPK 553
|
490
....*....|...
gi 889038433 529 TPSGK-----LRR 536
Cdd:PRK07529 554 TAVGKifkpaLRR 566
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
152-533 |
8.80e-34 |
|
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: 131.45 E-value: 8.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMDF 231
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPD-DVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 LRDTL---LWaKLIDKYQGTMTAAPNFAYALLAKRlrrqakPGDFDLSTLRFALSGAEPVePADVEDLLDAGKpfGLRps 308
Cdd:cd05944 81 RNPGLfdnFW-KLVERYRITSLSTVPTVYAALLQV------PVNADISSLRFAMSGAAPL-PVELRARFEDAT--GLP-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 309 aILPAYGMAETTLAVSfsecnaglvvdevdadllaalrRAVPATKgntRRLATLGPLLQDLEARIIDEQGDVMPARG--- 385
Cdd:cd05944 149 -VVEGYGLTEATCLVA----------------------VNPPDGP---KRPGSVGLRLPYARVRIKVLDGVGRLLRDcap 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 386 --VGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVr 463
Cdd:cd05944 203 deVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV- 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 889038433 464 pGCAVAVRLDAGHSRESFAVAVE--SNAFEDPAEVrrIEHQVAHevVAEVDVRPRNVVVLGPgtIPKTPSGK 533
Cdd:cd05944 282 -AFAGAVGQPDAHAGELPVAYVQlkPGAVVEEEEL--LAWARDH--VPERAAVPKHIEVLEE--LPVTAVGK 346
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
77-536 |
1.07e-33 |
|
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: 133.90 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 77 RGASLTMLHQPTPRTDLAVWAEDTMTVIGMIEAKAVIVSEPFLVAIPILEQKGMQVLTVADLLASDPIGPI---EVGEDD 153
Cdd:cd05904 80 LGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPpvvVIKQDD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 154 LALMQLTSGSTGSPKAVQITHRNIYSNAEA--MFVGAQYDVDkDVMVSWLPCFHDMGMVGFLTIPMFFGAELVkVTPMDF 231
Cdd:cd05904 160 VAALLYSSGTTGRSKGVMLTHRNLIAMVAQfvAGEGSNSDSE-DVFLCVLPMFHIYGLSSFALGLLRLGATVV-VMPRFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 LRDTLlwaKLIDKYQGT-MTAAPNFAYALLakrlrRQAKPGDFDLSTLRFALSGAEPVEPadveDLLDAgkpFGLR-PSA 309
Cdd:cd05904 238 LEELL---AAIERYKVThLPVVPPIVLALV-----KSPIVDKYDLSSLRQIMSGAAPLGK----ELIEA---FRAKfPNV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 310 -ILPAYGMAETTLAVSfsecnaglvvdevdadllaalrrAVPATKGNTRRLATLGPLLQDLEARIID-EQGDVMPARGVG 387
Cdd:cd05904 303 dLGQGYGMTESTGVVA-----------------------MCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 388 VIELRGESLTPGYL-----TMGGFipaqDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIEraagrvdGV 462
Cdd:cd05904 360 ELWIRGPSIMKGYLnnpeaTAATI----DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELE-------AL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 463 ---RPG---CAVAVRLD--AGHSRESFAV-AVESNAFEDpaEVRR-IEHQVAHEvvaevdVRPRNVVVLgpGTIPKTPSG 532
Cdd:cd05904 429 llsHPEildAAVIPYPDeeAGEVPMAFVVrKPGSSLTED--EIMDfVAKQVAPY------KKVRKVAFV--DAIPKSPSG 498
|
....*
gi 889038433 533 K-LRR 536
Cdd:cd05904 499 KiLRK 503
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
152-536 |
1.13e-33 |
|
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: 132.60 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMDf 231
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLT-PSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWD- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 lRDTLLwaKLIDKYQGTM-TAAPNFAYALLAkrlrrQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpFGLRpsaI 310
Cdd:cd05935 162 -RETAL--ELIEKYKVTFwTNIPTMLVDLLA-----TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKL---TGLR---F 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 311 LPAYGMAETtlavsfsecnaglvvdevdadllaalrraVPATKGN---TRRLATLGPLLQDLEARIID-EQGDVMPARGV 386
Cdd:cd05935 228 VEGYGLTET-----------------------------MSQTHTNpplRPKLQCLGIP*FGVDARVIDiETGRELPPNEV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 387 GVIELRGESLTPGYLTMggfiPAQDEHGW--------YDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGR 458
Cdd:cd05935 279 GEIVVRGPQIFKGYWNR----PEETEESFieikgrrfFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYK 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889038433 459 VDGVRPGCAVAVRlDAGHSRESFAVAVESNAFEDPAEVRRIEhQVAHEVVAEVDvRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd05935 355 HPAI*EVCVISVP-DERVGEEVKAFIVLRPEYRGKVTEEDII-EWAREQMAAYK-YPREVEFV--DELPRSASGKILW 427
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
109-462 |
2.46e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 133.11 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 109 AKAVIVSEPFL-------VAIPILE-----------QKGMQVLTVADLLAS--DPIGPIEVGEDDLALMQLTSGSTGSPK 168
Cdd:PRK07656 103 AKALFVLGLFLgvdysatTRLPALEhvviceteeddPHTEKMKTFTDFLAAgdPAERAPEVDPDDVADILFTSGTTGRPK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 169 AVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGM-VGFLTiPMFFGAELVKVtpMDFLRDTLLwaKLIDKYQG 247
Cdd:PRK07656 183 GAMLTHRQLLSNAADWAEYLGLTEG-DRYLAANPFFHVFGYkAGVNA-PLMRGATILPL--PVFDPDEVF--RLIETERI 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 248 TMTAAP----NFAYALLAKRlrrqakpgDFDLSTLRFALSGAEPVEPADVEDLLDAgkpfgLRPSAILPAYGMAETTLAV 323
Cdd:PRK07656 257 TVLPGPptmyNSLLQHPDRS--------AEDLSSLRLAVTGAASMPVALLERFESE-----LGVDIVLTGYGLSEASGVT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 324 SFseCNAGlvvDEvdadllaalrRAVPATkgntrrlaTLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTM 403
Cdd:PRK07656 324 TF--NRLD---DD----------RKTVAG--------TIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDD 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889038433 404 ggfiP-----AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGV 462
Cdd:PRK07656 381 ----PeataaAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAV 440
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
152-536 |
6.63e-33 |
|
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: 130.58 E-value: 6.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFvgAQYDVD-KDVMVSWLPCFHDMGMVGFLTIPMFFGAelvkvtPMD 230
Cdd:cd05903 93 DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYA--ERLGLGpGDVFLVASPMAHQTGFVYGFTLPLLLGA------PVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 FLRD-TLLWAKLIDKYQG--TMTAAPNFAYALLakrlrRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPFglrp 307
Cdd:cd05903 165 LQDIwDPDKALALMREHGvtFMMGATPFLTDLL-----NAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAK---- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 308 saILPAYGMAETTLAVSFSEcnaglvVDEVDadllaalrravpatkgntRRLATLGPLLQDLEARIIDEQGDVMPARGVG 387
Cdd:cd05903 236 --VCSAYGSTECPGAVTSIT------PAPED------------------RRLYTDGRPLPGVEIKVVDDTGATLAPGVEG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 388 VIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCA 467
Cdd:cd05903 290 ELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 889038433 468 VAVRlDAGHSRESFAVAV-ESNAFEDPAEVRRI--EHQVAHEVVaevdvrPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd05903 370 VALP-DERLGERACAVVVtKSGALLTFDELVAYldRQGVAKQYW------PERLVHV--DDLPRTPSGKVQK 432
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
111-534 |
8.80e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 128.92 E-value: 8.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 111 AVIVSEPFLVAIPILEQKGMQVLTVADLLAS-DPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeamfVGAQ 189
Cdd:PRK08314 148 EIAVPAWLRAEPPLQALAPGGVVAWKEALAAgLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA----VGSV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 190 YDVD---KDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMDflRDTLlwAKLIDKYQGTM-TAAPNFAYALLAkrlr 265
Cdd:PRK08314 224 LWSNstpESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWD--REAA--ARLIERYRVTHwTNIPTMVVDFLA---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 266 rQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpFGLRpsaILPAYGMAETtlaVSFSECNAglvvdevdadllaal 345
Cdd:PRK08314 296 -SPGLAERDLSSLRYIGGGGAAMPEAVAERLKEL---TGLD---YVEGYGLTET---MAQTHSNP--------------- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 346 rRAVPatkgntrRLATLGPLLQDLEARIID-EQGDVMPARGVGVIELRGESLTPGYL-----TMGGFIPAqDEHGWYDTG 419
Cdd:PRK08314 351 -PDRP-------KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWnrpeaTAEAFIEI-DGKRFFRTG 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 420 DLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRlDAGHSRESFAVAVESNAFEDPAEVRRI 499
Cdd:PRK08314 422 DLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP-DPRRGETVKAVVVLRPEARGKTTEEEI 500
|
410 420 430
....*....|....*....|....*....|....*
gi 889038433 500 EhQVAHEVVAEVDVrPRNVVVLgpGTIPKTPSGKL 534
Cdd:PRK08314 501 I-AWAREHMAAYKY-PRIVEFV--DSLPKSGSGKI 531
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
153-538 |
1.30e-30 |
|
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: 123.94 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHRNI----YSNAEAMFVGaqydvDKDVMVSWLPCFHdMGMVGFLTIPMFF-GAELV--- 224
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLtfagYYSARRFGLG-----EDDVYLTVLPLFH-INAQAVSVLAALSvGATLVllp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 225 KVTPMDFLRDtllwaklIDKYQGTMTaapNFAYALLAKRLRRQAKPGDFDlSTLRFALSGAEPvePADVEDLLDAgkpFG 304
Cdd:cd05934 156 RFSASRFWSD-------VRRYGATVT---NYLGAMLSYLLAQPPSPDDRA-HRLRAAYGAPNP--PELHEEFEER---FG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 305 LRpsaILPAYGMAETTlavsfsecnaglvvdevdadllaalrRAVPATKGNTRRLATLGPLLQDLEARIIDEQGDVMPAR 384
Cdd:cd05934 220 VR---LLEGYGMTETI--------------------------VGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 385 GVGVIELRGE---SLTPGYLTMggfiPAQD----EHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAG 457
Cdd:cd05934 271 EPGELVIRGLrgwGFFKGYYNM----PEATaeamRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 458 RVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRR-IEHQVAHEVVaevdvrPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd05934 347 RHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAfCEGQLAYFKV------PRYIRFV--DDLPKTPTEKVAK 418
|
..
gi 889038433 537 AN 538
Cdd:cd05934 419 AQ 420
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
147-537 |
1.48e-30 |
|
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: 123.90 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 147 IEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAM----FVGAQ--------YDVDKDVMvSWLPCfhdmgmvgfLT 214
Cdd:cd05945 92 LIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMlsdfPLGPGdvflnqapFSFDLSVM-DLYPA---------LA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 215 IpmffGAELVKVtPMDFLRDTLLWAKLIDKYQGTM-TAAPNFAYALLAKRLRRQAKpgdfdLSTLRFALSGAEPVEPADV 293
Cdd:cd05945 162 S----GATLVPV-PRDATADPKQLFRFLAEHGITVwVSTPSFAAMCLLSPTFTPES-----LPSLRHFLFCGEVLPHKTA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 294 EDLLDAgkpfgLRPSAILPAYGMAETTLAVSFsecnaglvvDEVDADLLAALRRaVPatkgntrrlatLGPLLQDLEARI 373
Cdd:cd05945 232 RALQQR-----FPDARIYNTYGPTEATVAVTY---------IEVTPEVLDGYDR-LP-----------IGYAKPGAKLVI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 374 IDEQGDVMPARGVGVIELRGESLTPGYL-----TMGGFIPAqDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIY 448
Cdd:cd05945 286 LDEDGRPVPPGEKGELVISGPSVSKGYLnnpekTAAAFFPD-EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 449 PTDIERAAGRVDGVRPgcAVAVRLDAGHSRESFAVAVESNAFEDPAEVRRIEHQVAHEVVAEvdVRPRNVVVLgpGTIPK 528
Cdd:cd05945 365 LEEIEAALRQVPGVKE--AVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIKAELAERLPPY--MIPRRFVYL--DELPL 438
|
410
....*....|
gi 889038433 529 TPSGKL-RRA 537
Cdd:cd05945 439 NANGKIdRKA 448
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
133-536 |
2.04e-30 |
|
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: 122.84 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 133 LTVADLLasDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeamfVGAQYDV---DKDVMVSWLPCFHdmgm 209
Cdd:cd05912 60 LTPNELA--FQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSA----IGSALNLgltEDDNWLCALPLFH---- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 210 VGFLTIPMFFGAELVKVTPMD-FLRDTLLwaKLIDKYQGTMTAapnfayaLLAKRLRRQAK--PGDFDlSTLRFALSGAE 286
Cdd:cd05912 130 ISGLSILMRSVIYGMTVYLVDkFDAEQVL--HLINSGKVTIIS-------VVPTMLQRLLEilGEGYP-NNLRCILLGGG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 287 PVEPADVEDLLDAGKPfglrpsaILPAYGMAETtlavsFSEcnaglVVDEVDADLLAalrravpatkgntrRLATLGPLL 366
Cdd:cd05912 200 PAPKPLLEQCKEKGIP-------VYQSYGMTET-----CSQ-----IVTLSPEDALN--------------KIGSAGKPL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 367 QDLEARIIDEQGdvmPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRN 446
Cdd:cd05912 249 FPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGEN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 447 IYPTDIERAAGRVDGVRPgCAVAVRLDA--GHSRESFAVAvesnafEDPAEVRRIEHQVAhEVVAEVDvRPRNVVVLgpG 524
Cdd:cd05912 326 IYPAEIEEVLLSHPAIKE-AGVVGIPDDkwGQVPVAFVVS------ERPISEEELIAYCS-EKLAKYK-VPKKIYFV--D 394
|
410
....*....|..
gi 889038433 525 TIPKTPSGKLRR 536
Cdd:cd05912 395 ELPRTASGKLLR 406
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
151-537 |
1.17e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 122.83 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLALMQLTSGSTGSPKAVQITHRNIYSNAeamFVGAQYDVD----KDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKV 226
Cdd:PRK06710 205 ENDLALLQYTGGTTGFPKGVMLTHKNLVSNT---LMGVQWLYNckegEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 227 TPMDFlrdtLLWAKLIDKYQGTM-TAAPNFAYALLAKRLRRQakpgdFDLSTLRFALSGAEPVePADVEDLLDAgkpfgL 305
Cdd:PRK06710 282 PKFDM----KMVFEAIKKHKVTLfPGAPTIYIALLNSPLLKE-----YDISSIRACISGSAPL-PVEVQEKFET-----V 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 306 RPSAILPAYGMAETTlavsfsecnaglvvdevdadllaalrravPATKGN----TRRLATLGPLLQDLEARIID-EQGDV 380
Cdd:PRK06710 347 TGGKLVEGYGLTESS-----------------------------PVTHSNflweKRVPGSIGVPWPDTEAMIMSlETGEA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 381 MPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVD 460
Cdd:PRK06710 398 LPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 461 GVRPGCAVAVRLD-AGHSRESFAVAVESNAFEDpAEVRRI--EHQVAHEVVAEVDVRPRnvvvlgpgtIPKTPSGK-LRR 536
Cdd:PRK06710 478 KVQEVVTIGVPDPyRGETVKAFVVLKEGTECSE-EELNQFarKYLAAYKVPKVYEFRDE---------LPKTTVGKiLRR 547
|
.
gi 889038433 537 A 537
Cdd:PRK06710 548 V 548
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
136-536 |
1.28e-29 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 122.47 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 136 ADLLASDPIGPievgeDDLALMQLTSGSTGSPKAVQITHRNIYSN----AEAMFVGAQydvdkDVMVSWLPCFHDMGMVG 211
Cdd:PRK13295 186 PAILARLRPGP-----DDVTQLIYTSGTTGEPKGVMHTANTLMANivpyAERLGLGAD-----DVILMASPMAHQTGFMY 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 212 FLTIPMFFGAELVkvtpmdfLRDT---LLWAKLIDKYQGTMTAApnfAYALLAKRLRRQAKPGDfDLSTLRFALSGAEPV 288
Cdd:PRK13295 256 GLMMPVMLGATAV-------LQDIwdpARAAELIRTEGVTFTMA---STPFLTDLTRAVKESGR-PVSSLRTFLCAGAPI 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 289 EPADVEDlldAGKPFGLRpsaILPAYGMaettlavsfSECNAGLVVDEVDADLLAALRRAVPatkgntrrlatlgplLQD 368
Cdd:PRK13295 325 PGALVER---ARAALGAK---IVSAWGM---------TENGAVTLTKLDDPDERASTTDGCP---------------LPG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 369 LEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMggfiP---AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGR 445
Cdd:PRK13295 375 VEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKR----PqlnGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 446 NIYPTDIERAAGRVDGVRPGCAVAV---RLdaGHSRESFAVAVESNAFEDPAEVRRI-EHQVAHEVVAEvdvrpRNVVVl 521
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQVAIVAYpdeRL--GERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPE-----RLVVR- 522
|
410
....*....|....*
gi 889038433 522 gpGTIPKTPSGKLRR 536
Cdd:PRK13295 523 --DALPRTPSGKIQK 535
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
152-453 |
1.73e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 122.19 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAeAMFVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVkvTPMDF 231
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHNILNNG-YFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLV--YPNEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 LrDTLLWAKLIDKYQGT-MTAAPNFAYALLAKRLRrqakpGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpfgLRPSAI 310
Cdd:PRK12583 278 F-DPLATLQAVEEERCTaLYGVPTMFIAELDHPQR-----GNFDLSSLRTGIMAGAPCPIEVMRRVMDE-----MHMAEV 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 311 LPAYGMAETTlAVSFSECNAglvvDEVDadllaalrravpatkgntRRLATLGPLLQDLEARIIDEQGDVMPARGVGVIE 390
Cdd:PRK12583 347 QIAYGMTETS-PVSLQTTAA----DDLE------------------RRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889038433 391 LRGESLTPGYLTMG-GFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIE 453
Cdd:PRK12583 404 TRGYSVMKGYWNNPeATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIE 467
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
94-537 |
1.90e-29 |
|
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: 121.01 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 94 AVWAEDTMTVIGMIEAKAVIVSEPFLV-----AIPILEQKGMQVLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPK 168
Cdd:cd05922 54 PTLKESVLRYLVADAGGRIVLADAGAAdrlrdALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 169 AVQITHRNIYSNAEAMfvgAQY-DVDK-DVMVSWLPCFHDMGMvGFLTIPMFFGAELVkVTPmDFLRDTLLWaKLIDKYQ 246
Cdd:cd05922 134 LVRLSHQNLLANARSI---AEYlGITAdDRALTVLPLSYDYGL-SVLNTHLLRGATLV-LTN-DGVLDDAFW-EDLREHG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 247 GTMTAAPNFAYALLAKRLRRQAKpgdfdLSTLRFALSGAEPVEPADVEDLLDAGkpfglRPSAILPAYGMAETTLAVSFs 326
Cdd:cd05922 207 ATGLAGVPSTYAMLTRLGFDPAK-----LPSLRYLTQAGGRLPQETIARLRELL-----PGAQVYVMYGQTEATRRMTY- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 327 ecnaglvvdeVDADLLAalrravpatkgntRRLATLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMGGF 406
Cdd:cd05922 276 ----------LPPERIL-------------EKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 407 IPAQDEHG---WydTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGhsrESFAV 483
Cdd:cd05922 333 RRKEGRGGgvlH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLG---EKLAL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 889038433 484 AVESNAFEDPAEVRRIEHQVAHEVVAEVDVRPRNvvvlgpgTIPKTPSGKLRRA 537
Cdd:cd05922 408 FVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVD-------ELPLTASGKVDYA 454
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
152-537 |
1.96e-29 |
|
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: 120.64 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKvtpMDF 231
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVL---NPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 LRDTLLWAKLIDKYQGT-MTAAPNFaYAllakRLRRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpFGLrpsAI 310
Cdd:cd05919 168 WPTAERVLATLARFRPTvLYGVPTF-YA----NLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEH---FGG---PI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 311 LPAYGMAETtlaVSFSECNAglvVDEVdadllaalrravpatkgntrRLATLGPLLQDLEARIIDEQGDVMPARGVGVIE 390
Cdd:cd05919 237 LDGIGATEV---GHIFLSNR---PGAW--------------------RLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 391 LRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAV 470
Cdd:cd05919 291 VRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAV 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 889038433 471 RLDAGHSRESFAVAVESNAFEDPAEVRRIEHQVAHEVVAEvdVRPRNVVVLgpGTIPKTPSGKLRRA 537
Cdd:cd05919 371 PESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAH--KVPRRIAFV--DELPRTATGKLQRF 433
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
118-462 |
2.68e-29 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 120.25 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 118 FLVAIPILEQKGMQVLTVADLLASDPiGPIEVGE----DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvD 193
Cdd:TIGR01923 74 LLLTDSLLEEKDFQADSLDRIEAAGR-YETSLSAsfnmDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFT-E 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 194 KDVMVSWLPCFHDMGmVGFLTIPMFFGAELVKVTPM-DFLRDtllwaklIDKYQGTM-TAAPNFAYALLAKRLRRQakpg 271
Cdd:TIGR01923 152 DDNWLLSLPLYHISG-LSILFRWLIEGATLRIVDKFnQLLEM-------IANERVTHiSLVPTQLNRLLDEGGHNE---- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 272 dfdlsTLRFALSGAEPVEPADVEDLLDAGKPfglrpsaILPAYGMAETTLAVSFSEcnaglvvDEVDADLLAAlrravpa 351
Cdd:TIGR01923 220 -----NLRKILLGGSAIPAPLIEEAQQYGLP-------IYLSYGMTETCSQVTTAT-------PEMLHARPDV------- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 352 tkgntrrlatlGPLLQDLEARIideqgDVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVV 431
Cdd:TIGR01923 274 -----------GRPLAGREIKI-----KVDNKEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLY 337
|
330 340 350
....*....|....*....|....*....|.
gi 889038433 432 VCGRVKDVIIMAGRNIYPTDIERAAGRVDGV 462
Cdd:TIGR01923 338 VLGRRDDLIISGGENIYPEEIETVLYQHPGI 368
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
153-537 |
2.70e-29 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 118.20 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHRNIYSNAEamfvGAQYDVDKDVMVSWL---PCFHDMGMvGFLTIPMFFGAELVKVTPm 229
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAA----GLHSRLGFGGGDSWLlslPLYHVGGL-AILVRSLLAGAELVLLER- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 230 dflrdtlLWAKLIDKYQGTMTAApnfayALLAKRLRR--QAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPfglrp 307
Cdd:cd17630 75 -------NQALAEDLAPPGVTHV-----SLVPTQLQRllDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIP----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 308 saILPAYGMAETTLAVsfsecnAGLVVDEVDAdllaalrravpatkgntrrlATLGPLLQDLEARIIDEqgdvmpargvG 387
Cdd:cd17630 138 --LYTTYGMTETASQV------ATKRPDGFGR--------------------GGVGVLLPGRELRIVED----------G 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 388 VIELRGESLTPGYLtMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCA 467
Cdd:cd17630 180 EIWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 468 VAVrldaGHSR--ESFAVAVESNAFEDPAEVR--------RIEHQVAHEVVAEvdvrprnvvvlgpgtIPKTPSGKLRRA 537
Cdd:cd17630 259 VGV----PDEElgQRPVAVIVGRGPADPAELRawlkdklaRFKLPKRIYPVPE---------------LPRTGGGKVDRR 319
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
108-453 |
2.81e-29 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 122.13 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 108 EAKAVIVSE--------------PFLVAIPILEQKGM----QVLTVADLLA--SDPIGPIEV-------GEDDLALMQLT 160
Cdd:COG1022 112 GAKVLFVEDqeqldkllevrdelPSLRHIVVLDPRGLrddpRLLSLDELLAlgREVADPAELearraavKPDDLATIIYT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 161 SGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMG-MVGFLTipMFFGAELVKVTPMDFLRDTL--- 236
Cdd:COG1022 192 SGTTGRPKGVMLTHRNLLSNARALLERLPLG-PGDRTLSFLPLAHVFErTVSYYA--LAAGATVAFAESPDTLAEDLrev 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 237 ----------LWAKLIDKYQGTMTAAPN-----FAYAL-LAKRLRRQAKPGD------------FDL-----------ST 277
Cdd:COG1022 269 kptfmlavprVWEKVYAGIQAKAEEAGGlkrklFRWALaVGRRYARARLAGKspslllrlkhalADKlvfsklrealgGR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 278 LRFALSGAEPVEPaDVEDLLDAgkpFGLRpsaILPAYGMAETTLAVSfseCNaglVVDEVdadllaalrravpatkgntr 357
Cdd:COG1022 349 LRFAVSGGAALGP-ELARFFRA---LGIP---VLEGYGLTETSPVIT---VN---RPGDN-------------------- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 358 RLATLGPLLQDLEARIIDEqgdvmpargvGVIELRGESLTPGYLTMggfiPAQ-----DEHGWYDTGDLGYLTEEGHVVV 432
Cdd:COG1022 396 RIGTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKN----PEAtaeafDADGWLHTGDIGELDEDGFLRI 461
|
410 420
....*....|....*....|..
gi 889038433 433 CGRVKDVIIMA-GRNIYPTDIE 453
Cdd:COG1022 462 TGRKKDLIVTSgGKNVAPQPIE 483
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
136-544 |
2.61e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 118.04 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 136 ADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeamfVGAQYDVD---KDVMVSWLPCFHdMGMVGF 212
Cdd:PRK06839 133 KEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNA----LNNTFAIDltmHDRSIVLLPLFH-IGGIGL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 213 LTIPMFFGAELVkVTPMDFLRDTLLwaKLIDKYQGTMTaapnFAYALLAKRLRRQAKPGDFDLSTLRFALSGAEPVEPAD 292
Cdd:PRK06839 208 FAFPTLFAGGVI-IVPRKFEPTKAL--SMIEKHKVTVV----MGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEEL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 293 VEDLLDAGKPFGlrpsailPAYGMAETTLAVsfsecnagLVVDEVDAdllaalrravpatkgnTRRLATLGPLLQDLEAR 372
Cdd:PRK06839 281 MREFIDRGFLFG-------QGFGMTETSPTV--------FMLSEEDA----------------RRKVGSIGKPVLFCDYE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 373 IIDEQGDVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDI 452
Cdd:PRK06839 330 LIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEV 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 453 ERAAGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRriEHQVAHevVAEVDVrPRNVVVLgpGTIPKTPSG 532
Cdd:PRK06839 410 EQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVI--EHCRLF--LAKYKI-PKEIVFL--KELPKNATG 482
|
410
....*....|..
gi 889038433 533 KLRRANSVTLVT 544
Cdd:PRK06839 483 KIQKAQLVNQLK 494
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
85-469 |
3.03e-28 |
|
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: 116.60 E-value: 3.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 85 HQPTPRTDlavwaedtmTVIGMIEAKAVIVSEPFL-----VAIPILEQKGMQVLTVADLLASDPiGPIEVGEDDLALMQL 159
Cdd:TIGR01733 58 AYPAERLA---------FILEDAGARLLLTDSALAsrlagLVLPVILLDPLELAALDDAPAPPP-PDAPSGPDDLAYVIY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 160 TSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVD-KDVMVSWLPCFHDMGMVGFLTiPMFFGAELVKVTPMDFLRDTLLW 238
Cdd:TIGR01733 128 TSGSTGRPKGVVVTHRSLVNLLAWL--ARRYGLDpDDRVLQFASLSFDASVEEIFG-ALLAGATLVVPPEDEERDDAALL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 239 AKLIDKYQGT-MTAAPNFAYALLAkrlrrqakPGDFDLSTLRFALSGAEPVEPADVEDLLDAGkpfglRPSAILPAYGMA 317
Cdd:TIGR01733 205 AALIAEHPVTvLNLTPSLLALLAA--------ALPPALASLRLVILGGEALTPALVDRWRARG-----PGARLINLYGPT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 318 ETTLAVSFSECNAglvvdevdadllAALRRAVPatkgntrrlATLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLT 397
Cdd:TIGR01733 272 ETTVWSTATLVDP------------DDAPRESP---------VPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 398 PGYLTMGG-----FIP----AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpgCAV 468
Cdd:TIGR01733 331 RGYLNRPEltaerFVPdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVR--EAV 408
|
.
gi 889038433 469 A 469
Cdd:TIGR01733 409 V 409
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
153-468 |
6.82e-28 |
|
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: 116.24 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYdVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVkVTPmDFl 232
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRW-TEDDVLLHVLPLHHVHGLVNALLCPLFAGASVE-FLP-KF- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 233 rDTLLWAKLIDKYQGTM-TAAPNFaYALLAKRLRRQAKPGDFDLS----TLRFALSGAEPVePADVEDLLDAgkPFGLRp 307
Cdd:cd05941 166 -DPKEVAISRLMPSITVfMGVPTI-YTRLLQYYEAHFTDPQFARAaaaeRLRLMVSGSAAL-PVPTLEEWEA--ITGHT- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 308 saILPAYGMAETTLAVSfsecnaglvvdevdadllaalrraVPATkgNTRRLATLGPLLQDLEARIIDEQ-GDVMPARGV 386
Cdd:cd05941 240 --LLERYGMTEIGMALS------------------------NPLD--GERRPGTVGMPLPGVQARIVDEEtGEPLPRGEV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 387 GVIELRGESLTPGYLTMggfiP-----AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMA-GRNIYPTDIERAAGRVD 460
Cdd:cd05941 292 GEIQVRGPSVFKEYWNK----PeatkeEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHP 367
|
....*...
gi 889038433 461 GVRPgCAV 468
Cdd:cd05941 368 GVSE-CAV 374
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
133-536 |
7.75e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 117.16 E-value: 7.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 133 LTVADLLAS-DPIG-PIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSnAEAMFVGAQYDVDKDVMVSWLPCFHDMGMV 210
Cdd:PRK06087 166 LSLSQIIADyEPLTtAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILA-SERAYCARLNLTWQDVFMMPAPLGHATGFL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 211 GFLTIPMFFGAELVKVTpmDFLRDTLLwaKLIDKYQGT--MTAAPnFAYALLakRLRRQAKPgdfDLSTLRFALSGAEPV 288
Cdd:PRK06087 245 HGVTAPFLIGARSVLLD--IFTPDACL--ALLEQQRCTcmLGATP-FIYDLL--NLLEKQPA---DLSALRFFLCGGTTI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 289 EPADVEDLLDAGkpfglrpSAILPAYGMAETTLAVsfsecnaglvvdevdadllaalrrAVPATKGNTRRLATLGPLLQD 368
Cdd:PRK06087 315 PKKVARECQQRG-------IKLLSVYGSTESSPHA------------------------VVNLDDPLSRFMHTDGYAAAG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 369 LEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMggfiP-----AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMA 443
Cdd:PRK06087 364 VEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDE----PeltarALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRG 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 444 GRNIYPTDIERAAGRVDGVRPGCAVAV---RLdaGHSRESFAVAVESNAFEDPAEVrriehqVAHEVVAEVDVR--PRNV 518
Cdd:PRK06087 440 GENISSREVEDILLQHPKIHDACVVAMpdeRL--GERSCAYVVLKAPHHSLTLEEV------VAFFSRKRVAKYkyPEHI 511
|
410
....*....|....*...
gi 889038433 519 VVLgpGTIPKTPSGKLRR 536
Cdd:PRK06087 512 VVI--DKLPRTASGKIQK 527
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
110-534 |
8.05e-28 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 116.96 E-value: 8.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 110 KAVIVsepFLVAIPILEQKGMQVLTVADLLA--SDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeamFVG 187
Cdd:cd12119 122 EHVVV---MTDDAAMPEPAGVGVLAYEELLAaeSPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHA---MAA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 188 AQYDV----DKDVMVSWLPCFH----DMGMVGFLTipmffGAELVkvTPMDFLRDTLLwAKLIDKYQGTMTAA-PNFAYA 258
Cdd:cd12119 196 LLTDGlglsESDVVLPVVPMFHvnawGLPYAAAMV-----GAKLV--LPGPYLDPASL-AELIEREGVTFAAGvPTVWQG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 259 LLAKRLRRQAkpgdfDLSTLRFALSGAEPVEPADVEDLLDAGKPfglrpsaILPAYGMAETTLAVSFSECNAGLVVDEVD 338
Cdd:cd12119 268 LLDHLEANGR-----DLSSLRRVVIGGSAVPRSLIEAFEERGVR-------VIHAWGMTETSPLGTVARPPSEHSNLSED 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 339 ADLlaalrravpatkgntRRLATLGPLLQDLEARIIDEQGDVMPARG--VGVIELRGESLTPGYLTMGGFIPAQDEHGWY 416
Cdd:cd12119 336 EQL---------------ALRAKQGRPVPGVELRIVDDDGRELPWDGkaVGELQVRGPWVTKSYYKNDEESEALTEDGWL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 417 DTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEV 496
Cdd:cd12119 401 RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEEL 480
|
410 420 430
....*....|....*....|....*....|....*....
gi 889038433 497 R-RIEHQVAHEVVaevdvrPRNVVVLgpGTIPKTPSGKL 534
Cdd:cd12119 481 LeFLADKVAKWWL------PDDVVFV--DEIPKTSTGKI 511
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
136-536 |
2.80e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 115.59 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 136 ADLLA--SDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeAMFVGAQYDV-DKDVMvsWlpCFHDMG-MVG 211
Cdd:COG0365 166 DELLAaaSAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHA-ATTAKYVLDLkPGDVF--W--CTADIGwATG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 212 ---FLTIPMFFGAELV----KVTPMDFLRdtllWAKLIDKYQGT-MTAAPNfAYALLAKrlRRQAKPGDFDLSTLRFALS 283
Cdd:COG0365 241 hsyIVYGPLLNGATVVlyegRPDFPDPGR----LWELIEKYGVTvFFTAPT-AIRALMK--AGDEPLKKYDLSSLRLLGS 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 284 GAEPVEPADVEDLLDAgkpFGLRpsaILPAYGMAETTLAVSfsecnAGLVVDEVdadllaalrraVPATKGntrrLATLG 363
Cdd:COG0365 314 AGEPLNPEVWEWWYEA---VGVP---IVDGWGQTETGGIFI-----SNLPGLPV-----------KPGSMG----KPVPG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 364 pllqdLEARIIDEQGDVMPARGVGVIELRGE--SLTPGYL--------TMGGFIPaqdehGWYDTGDLGYLTEEGHVVVC 433
Cdd:COG0365 368 -----YDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWndperyreTYFGRFP-----GWYRTGDGARRDEDGYFWIL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 434 GRVKDVIIMAGRNIYPTDIERAAGRVDGVRPgCAVA--------------VRLDAGHSresfavavesnafEDPAEVRRI 499
Cdd:COG0365 438 GRSDDVINVSGHRIGTAEIESALVSHPAVAE-AAVVgvpdeirgqvvkafVVLKPGVE-------------PSDELAKEL 503
|
410 420 430
....*....|....*....|....*....|....*....
gi 889038433 500 EHQVAHEV--VAevdvRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:COG0365 504 QAHVREELgpYA----YPREIEFV--DELPKTRSGKIMR 536
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
147-458 |
4.38e-27 |
|
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: 114.38 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 147 IEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDM-----------GMVGFLTI 215
Cdd:cd17640 83 VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG-DRFLSILPIWHSYersaeyfifacGCSQAYTS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 216 PMFFGAELVKVTPMDFLRDTLLWAKLIDKYQGTMTAAPNFAyallaKRLRRQAKPGdfdlSTLRFALSGAEPVePADVED 295
Cdd:cd17640 162 IRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIK-----QFLFLFFLSG----GIFKFGISGGGAL-PPHVDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 296 LLDAgkpFGLRpsaILPAYGMAETTLAVSfsecnaglvvdevdadllaaLRRavpaTKGNTRrlATLGPLLQDLEARIID 375
Cdd:cd17640 232 FFEA---IGIE---VLNGYGLTETSPVVS--------------------ARR----LKCNVR--GSVGRPLPGTEIKIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 376 EQGD-VMPARGVGVIELRGESLTPGYLTMggfiPAQ-----DEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMA-GRNIY 448
Cdd:cd17640 280 PEGNvVLPPGEKGIVWVRGPQVMKGYYKN----PEAtskvlDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVE 355
|
330
....*....|
gi 889038433 449 PTDIERAAGR 458
Cdd:cd17640 356 PQPIEEALMR 365
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
133-462 |
5.14e-26 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 111.51 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 133 LTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvgAQY--DVDKDVMVSWLPCFHDMGMV 210
Cdd:PRK07514 137 LLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTL---VDYwrFTPDDVLIHALPIFHTHGLF 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 211 GFLTIPMFFGAelvkvtPMDFLR--DTllwAKLIDKY-QGT-MTAAPNFAYALLA-KRLRRQAkpgdfdLSTLRFALSGA 285
Cdd:PRK07514 214 VATNVALLAGA------SMIFLPkfDP---DAVLALMpRATvMMGVPTFYTRLLQePRLTREA------AAHMRLFISGS 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 286 EPVepadvedLLDAGKPFGLRPS-AILPAYGMAETTLAVSfsecnaglvvDEVDADllaalrravpatkgntRRLATLGP 364
Cdd:PRK07514 279 APL-------LAETHREFQERTGhAILERYGMTETNMNTS----------NPYDGE----------------RRAGTVGF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 365 LLQDLEARIID-EQGDVMPARGVGVIELRGESLTPGYLTMggfiP---AQD--EHGWYDTGDLGYLTEEGHVVVCGRVKD 438
Cdd:PRK07514 326 PLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRM----PektAEEfrADGFFITGDLGKIDERGYVHIVGRGKD 401
|
330 340
....*....|....*....|....
gi 889038433 439 VIIMAGRNIYPTDIERAAGRVDGV 462
Cdd:PRK07514 402 LIISGGYNVYPKEVEGEIDELPGV 425
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
153-536 |
6.50e-25 |
|
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: 105.81 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAelvKVTPMDFL 232
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGL---CVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 233 RDTLLWaKLIDKYQGTMTAAPNFAYALLAKRLRRQAKpgdfDLSTLRFALSGAEPVEPADVEDLLDAGKpfglrpSAILP 312
Cdd:cd17635 79 TYKSLF-KILTTNAVTTTCLVPTLLSKLVSELKSANA----TVPSLRLIGYGGSRAIAADVRFIEATGL------TNTAQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 313 AYGMAETTLAVSFSECNaglvvDEVDADllaalrravpatkgntrrlaTLGPLLQDLEARIIDEQGDVMPARGVGVIELR 392
Cdd:cd17635 148 VYGLSETGTALCLPTDD-----DSIEIN--------------------AVGRPYPGVDVYLAATDGIAGPSASFGTIWIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 393 GESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPgCAVAVRL 472
Cdd:cd17635 203 SPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQE-CACYEIS 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889038433 473 DAGHSrESFAVAVESNAFEDPAEVRRIEHQVAHEVvaEVDVRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd17635 282 DEEFG-ELVGLAVVASAELDENAIRALKHTIRREL--EPYARPSTIVIV--TDIPRTQSGKVKR 340
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
152-435 |
8.19e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 109.24 E-value: 8.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEA--MFVGAQydvDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVT-P 228
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQisDVFNLR---NDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPdP 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 229 MdflrDTLLWAKLIDKYQGT-MTAAPNF--AYAllakRLRRqAKPGDFdlSTLRFALSGAEPVePADVEDllDAGKPFGL 305
Cdd:PRK08633 859 T----DALGIAKLVAKHRATiLLGTPTFlrLYL----RNKK-LHPLMF--ASLRLVVAGAEKL-KPEVAD--AFEEKFGI 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 306 RPsaiLPAYGMAETTLAVSfseCNaglVVDEVDADllaalrraVPATKGNtrRLATLGPLLQDLEARIID-EQGDVMPAR 384
Cdd:PRK08633 925 RI---LEGYGATETSPVAS---VN---LPDVLAAD--------FKRQTGS--KEGSVGMPLPGVAVRIVDpETFEELPPG 985
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 889038433 385 GVGVIELRGESLTPGYL----TMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGR 435
Cdd:PRK08633 986 EDGLILIGGPQVMKGYLgdpeKTAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
152-537 |
5.22e-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: 104.70 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRniysNAEAMFVGAQYDVDKDVMVSWLpCFHDMGM---VGFLTIPMFFGAELVkVTP 228
Cdd:cd17643 93 DDLAYVIYTSGSTGRPKGVVVSHA----NVLALFAATQRWFGFNEDDVWT-LFHSYAFdfsVWEIWGALLHGGRLV-VVP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 229 MDFLRD-TLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRqakpgDFDLSTLRFALSGAEPVEPADVEDLldaGKPFGLRP 307
Cdd:cd17643 167 YEVARSpEDFARLLRDEGVTVLNQTPSAFYQLVEAADRD-----GRDPLALRYVIFGGEALEAAMLRPW---AGRFGLDR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 308 SAILPAYGMAETTLAVSFSEcnaglvVDEVDADLLAAlrravpatkgntrrlATLGPLLQDLEARIIDEQGDVMPARGVG 387
Cdd:cd17643 239 PQLVNMYGITETTVHVTFRP------LDAADLPAAAA---------------SPIGRPLPGLRVYVLDADGRPVPPGVVG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 388 VIELRGESLTPGYL-----TMGGFIPAQDEHG---WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRV 459
Cdd:cd17643 298 ELYVSGAGVARGYLgrpelTAERFVANPFGGPgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATH 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 460 DGVRPGcAVAVRLDA-GHSRESFAVAVESNAFEDPAEVRRI--EHQVAHevvaevdVRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd17643 378 PSVRDA-AVIVREDEpGDTRLVAYVVADDGAAADIAELRALlkELLPDY-------MVPARYVPL--DALPLTVNGKLDR 447
|
.
gi 889038433 537 A 537
Cdd:cd17643 448 A 448
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
153-517 |
9.07e-24 |
|
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: 102.19 E-value: 9.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSwLPCFHDMGMVGFLTIPMFFGAELVkvtPMDFL 232
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLII-NPFFHTFGYKAGIVACLLTGATVV---PVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 233 rDTLLWAKLIDKYQGTMT-AAPNFAYALLAKRLRRqakpgDFDLSTLRFALSGAEPVEPADVEDLLDAgkpfgLRPSAIL 311
Cdd:cd17638 77 -DVDAILEAIERERITVLpGPPTLFQSLLDHPGRK-----KFDLSSLRAAVTGAATVPVELVRRMRSE-----LGFETVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 312 PAYGMAEttlAVSFSECNAGlvvdeVDADLLAAlrravpatkgntrrlaTLGPLLQDLEARIIDeQGDVMpargvgvieL 391
Cdd:cd17638 146 TAYGLTE---AGVATMCRPG-----DDAETVAT----------------TCGRACPGFEVRIAD-DGEVL---------V 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 392 RGESLTPGYLT-MGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAV 470
Cdd:cd17638 192 RGYNVMQGYLDdPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGV 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 889038433 471 ---RLdaGHSRESFAVAVESNAFEDPAEVRRIEHQVAH----EVVAEVDVRPRN 517
Cdd:cd17638 272 pdeRM--GEVGKAFVVARPGVTLTEEDVIAWCRERLANykvpRFVRFLDELPRN 323
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
152-453 |
9.58e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 104.89 E-value: 9.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAeaMFVG-AQYDVDKDVMVSWLPCFHDMGMV-GFLTIpMFFGAELVKVTPm 229
Cdd:PRK08315 199 DDPINIQYTSGTTGFPKGATLTHRNILNNG--YFIGeAMKLTEEDRLCIPVPLYHCFGMVlGNLAC-VTHGATMVYPGE- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 230 DFlrDTLLWAKLIDK------YqG--TMTAA----PNFAyallakrlrrqakpgDFDLSTLRFA-LSGAE-PVEPA-DVE 294
Cdd:PRK08315 275 GF--DPLATLAAVEEerctalY-GvpTMFIAeldhPDFA---------------RFDLSSLRTGiMAGSPcPIEVMkRVI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 295 DLLDAgkpfglrpSAILPAYGMAETTlAVSFSEcnaglvvdEVDADLlaalrravpatkgnTRRLATLGPLLQDLEARII 374
Cdd:PRK08315 337 DKMHM--------SEVTIAYGMTETS-PVSTQT--------RTDDPL--------------EKRVTTVGRALPHLEVKIV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 375 D-EQGDVMPaRGVgvielRGESLTPGYLTMGGF--IPAQ-----DEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRN 446
Cdd:PRK08315 386 DpETGETVP-RGE-----QGELCTRGYSVMKGYwnDPEKtaeaiDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGEN 459
|
....*..
gi 889038433 447 IYPTDIE 453
Cdd:PRK08315 460 IYPREIE 466
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
152-537 |
1.36e-23 |
|
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: 103.38 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVD-KDVMVSWLPCFHDMGMVGFLTiPMFFGAELVkVTPMD 230
Cdd:cd05930 93 DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM--QEAYPLTpGDRVLQFTSFSFDVSVWEIFG-ALLAGATLV-VLPEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 FLRDTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQakpgdfDLSTLRFALSGAEPVEPADVEDLLDAgkpfgLRPSAI 310
Cdd:cd05930 169 VRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA------ALPSLRLVLVGGEALPPDLVRRWREL-----LPGARL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 311 LPAYGMAETTLAVSFSECNAGlvvdevdadllAALRRAVPatkgntrrlatLGPLLQDLEARIIDEQGDVMPARGVGVIE 390
Cdd:cd05930 238 VNLYGPTEATVDATYYRVPPD-----------DEEDGRVP-----------IGRPIPNTRVYVLDENLRPVPPGVPGELY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 391 LRGESLTPGY-----LTMGGFIPAQDEHG--WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVR 463
Cdd:cd05930 296 IGGAGLARGYlnrpeLTAERFVPNPFGPGerMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVR 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 889038433 464 pGCAVAVRLD-AGHSRESFAVAVESNAFEDPAEVRriehQVAHEVVAEVDVrPRNVVVLgpGTIPKTPSGKL-RRA 537
Cdd:cd05930 376 -EAAVVAREDgDGEKRLVAYVVPDEGGELDEEELR----AHLAERLPDYMV-PSAFVVL--DALPLTPNGKVdRKA 443
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
141-536 |
2.13e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 103.77 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 141 SDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAM--FVGAQYDVD--KDVMVSWLPCFHDMGMVGFLTIP 216
Cdd:PLN02574 187 FDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFvrFEASQYEYPgsDNVYLAALPMFHIYGLSLFVVGL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 217 MFFGAELVKVTPMDfLRDTLlwaKLIDKYQgtMTAAPNFAYALLAkrLRRQAKP-GDFDLSTLRFALSGAEPVEPADVED 295
Cdd:PLN02574 267 LSLGSTIVVMRRFD-ASDMV---KVIDRFK--VTHFPVVPPILMA--LTKKAKGvCGEVLKSLKQVSCGAAPLSGKFIQD 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 296 LLDAgkpfgLRPSAILPAYGMAETTlavsfsecnaglvvdevdadllaalrrAVpATKG-NTRRL---ATLGPLLQDLEA 371
Cdd:PLN02574 339 FVQT-----LPHVDFIQGYGMTEST---------------------------AV-GTRGfNTEKLskySSVGLLAPNMQA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 372 RIID-EQGDVMPARGVGVIELRGESLTPGYLTMG-GFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYP 449
Cdd:PLN02574 386 KVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPkATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAP 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 450 TDIERA----AGRVDGvrpGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRRIEHQVA-HEVVaevdvrpRNVVVLGPg 524
Cdd:PLN02574 466 ADLEAVlishPEIIDA---AVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVApYKKV-------RKVVFVQS- 534
|
410
....*....|...
gi 889038433 525 tIPKTPSGK-LRR 536
Cdd:PLN02574 535 -IPKSPAGKiLRR 546
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
119-537 |
9.62e-23 |
|
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: 100.87 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 119 LVAIPILEQkgmqvLTVADLL----ASDPiGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYsnaeAMFVGAQYDVD- 193
Cdd:cd05972 50 AVYVPLTTL-----LGPKDIEyrleAAGA-KAIVTDAEDPALIYFTSGTTGLPKGVLHTHSYPL----GHIPTAAYWLGl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 194 --KDVMvsWlpCFHDMGMVGFLTIPmFFGAELVKVTPMDFLR---DTLLWAKLIDKYQGTMTAAPNFAYallakRLRRQA 268
Cdd:cd05972 120 rpDDIH--W--NIADPGWAKGAWSS-FFGPWLLGATVFVYEGprfDAERILELLERYGVTSFCGPPTAY-----RMLIKQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 269 KPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPfglrpsAILPAYGMAETTLAVSFSecnaglvvdevdadllaalrRA 348
Cdd:cd05972 190 DLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGL------PIRDGYGQTETGLTVGNF--------------------PD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 349 VPATKGNTRRlATLGpllqdLEARIIDEQGDVMPARGVGVIELRGE--SLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTE 426
Cdd:cd05972 244 MPVKPGSMGR-PTPG-----YDVAIIDDDGRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 427 EGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPgCAVAVRLDAGHSRESFAVAVESNAFEDPAE-VRRIEHQV-- 503
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAE-AAVVGSPDPVRGEVVKAFVVLTSGYEPSEElAEELQGHVkk 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 889038433 504 ---AHEVVAEVDVRPrnvvvlgpgTIPKTPSGKLRRA 537
Cdd:cd05972 397 vlaPYKYPREIEFVE---------ELPKTISGKIRRV 424
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
108-453 |
1.38e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 100.81 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 108 EAKAVIVSEPFLVaipilEQKGMQVLTVADLLASD--PIGPIE-VGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeam 184
Cdd:PRK03640 99 EVKCLITDDDFEA-----KLIPGISVKFAELMNGPkeEAEIQEeFDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSA--- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 185 fVGAQYDV---DKDvmvSWL---PCFHdmgmVGFLTIPM---FFGAELVKVTPMDFLRDTLLwakLIDKYQGTMTAAPNF 255
Cdd:PRK03640 171 -VGSALNLgltEDD---CWLaavPIFH----ISGLSILMrsvIYGMRVVLVEKFDAEKINKL---LQTGGVTIISVVSTM 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 256 AYALLAkRLRRQAKPgdfdlSTLRFALSGAEPVEPADVEDLLDAGKPfglrpsaILPAYGMAETtlavsfsecnaglvvd 335
Cdd:PRK03640 240 LQRLLE-RLGEGTYP-----SSFRCMLLGGGPAPKPLLEQCKEKGIP-------VYQSYGMTET---------------- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 336 evdADLLAALRRAVPATKgntrrLATLGPLLQDLEARIIDeQGDVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGW 415
Cdd:PRK03640 291 ---ASQIVTLSPEDALTK-----LGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGW 361
|
330 340 350
....*....|....*....|....*....|....*...
gi 889038433 416 YDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIE 453
Cdd:PRK03640 362 FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE 399
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
106-537 |
4.73e-22 |
|
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: 100.70 E-value: 4.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 106 MIE---AKAVIVSEPFLVAIPileQKGMQVLTV-ADLLASDPIG--PIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYS 179
Cdd:COG1020 568 MLEdagARLVLTQSALAARLP---ELGVPVLALdALALAAEPATnpPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVN 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 180 NAEAMfvGAQYDVD-KDVMVSWLPCFHDMGMVGFLTiPMFFGAELVkVTPMDFLRDTLLWAKLIDKYQGT-MTAAPNFAY 257
Cdd:COG1020 645 LLAWM--QRRYGLGpGDRVLQFASLSFDASVWEIFG-ALLSGATLV-LAPPEARRDPAALAELLARHRVTvLNLTPSLLR 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 258 ALLAKRLRrqakpgdfDLSTLRFALSGAEPVEPADVEDLLDAgkpfgLRPSAILPAYGMAETTLAVSFSECNAGlvvdev 337
Cdd:COG1020 721 ALLDAAPE--------ALPSLRLVLVGGEALPPELVRRWRAR-----LPGARLVNLYGPTETTVDSTYYEVTPP------ 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 338 dadllAALRRAVPatkgntrrlatLGPLLQDLEARIIDEQGDVMPargVGVI-EL--RGESLTPGY-----LTMGGFIP- 408
Cdd:COG1020 782 -----DADGGSVP-----------IGRPIANTRVYVLDAHLQPVP---VGVPgELyiGGAGLARGYlnrpeLTAERFVAd 842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 409 --AQDEHGWYDTGDLGYLTEEGHVVVCGR----VKdviIMaGRNIYPTDIERAAGRVDGVRpGCAVAVRLDAGHSRESFA 482
Cdd:COG1020 843 pfGFPGARLYRTGDLARWLPDGNLEFLGRaddqVK---IR-GFRIELGEIEAALLQHPGVR-EAVVVAREDAPGDKRLVA 917
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 889038433 483 VAVESNAFEDPAEVRRiehQVAHEVVAEVDVRPRNVVVLGPgtiPKTPSGKLRRA 537
Cdd:COG1020 918 YVVPEAGAAAAAALLR---LALALLLPPYMVPAAVVLLLPL---PLTGNGKLDRL 966
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
112-536 |
5.55e-22 |
|
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: 99.37 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 112 VIVSEPflvaipilEQKGMQVLTVADLLA--SDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQ 189
Cdd:cd05959 129 LIVSGG--------AGPEAGALLLAELVAaeAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 190 YDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELV----KVTPMDFLrdtllwaKLIDKYQGTMT-AAPNFAYALLAkrl 264
Cdd:cd05959 201 GIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVlmpeRPTPAAVF-------KRIRRYRPTVFfGVPTLYAAMLA--- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 265 rrQAKPGDFDLSTLRFALSGAEPVePADVEDLLDAgkPFGLRpsaILPAYGMAEtTLAVsfsecnaglvvdevdadLLAA 344
Cdd:cd05959 271 --APNLPSRDLSSLRLCVSAGEAL-PAEVGERWKA--RFGLD---ILDGIGSTE-MLHI-----------------FLSN 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 345 LRRAVpatkgntrRLATLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYL--------TMGGfipaqdehGWY 416
Cdd:cd05959 325 RPGRV--------RYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWnnrdktrdTFQG--------EWT 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 417 DTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHSRESfAVAVESNAFEDPAEV 496
Cdd:cd05959 389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPK-AFVVLRPGYEDSEAL 467
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 889038433 497 RRIEHQVAHEVVAEVDvRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd05959 468 EEELKEFVKDRLAPYK-YPRWIVFV--DELPKTATGKIQR 504
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
109-537 |
4.93e-21 |
|
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: 96.19 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 109 AKAVIVSEPFLVAIPILEQkgMQVLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGA 188
Cdd:cd12114 85 ARLVLTDGPDAQLDVAVFD--VLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI--NR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 189 QYDVD-KDVMVSWLPCFHDMGMVGFLTiPMFFGAELVKVTPMDfLRDTLLWAKLIDKYQGTMTaapNFAYALLAKRLRRQ 267
Cdd:cd12114 161 RFAVGpDDRVLALSSLSFDLSVYDIFG-ALSAGATLVLPDEAR-RRDPAHWAELIERHGVTLW---NSVPALLEMLLDVL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 268 AKPGDfDLSTLRFA-LSGaepvepadveDLLDAGKPFGLR---PSAILPAYGMA-ETTLAVSFSEcnaglvVDEVDADLl 342
Cdd:cd12114 236 EAAQA-LLPSLRLVlLSG----------DWIPLDLPARLRalaPDARLISLGGAtEASIWSIYHP------IDEVPPDW- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 343 aalrRAVPatkgntrrlatLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIPAQDEHGWYD 417
Cdd:cd12114 298 ----RSIP-----------YGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYlgdpeLTAARFVTHPDGERLYR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 418 TGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVR 497
Cdd:cd12114 363 TGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALR 442
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 889038433 498 riehQVAHEVVAeVDVRPRNVVVLgpGTIPKTPSGKLRRA 537
Cdd:cd12114 443 ----AFLAQTLP-AYMIPSRVIAL--EALPLTANGKVDRA 475
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
152-440 |
8.07e-21 |
|
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: 95.07 E-value: 8.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNI---YSNAEA-MFVGAQYDVDKDVMVSWLPCFHDMgmvgFLTIpmFFGAELVKVT 227
Cdd:cd17653 105 DDLAYIIFTSGSTGIPKGVMVPHRGVlnyVSQPPArLDVGPGSRVAQVLSIAFDACIGEI----FSTL--CNGGTLVLAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 228 PMDFlrdtllWAKLIDKYQGTMtAAPNFayalLAKrLRRQakpgdfDLSTLRFALSGAEPVEPadveDLLDAGKPfglRP 307
Cdd:cd17653 179 PSDP------FAHVARTVDALM-STPSI----LST-LSPQ------DFPNLKTIFLGGEAVPP----SLLDRWSP---GR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 308 SaILPAYGMAETTLAVSFSECNAGLVVdevdadllaalrravpatkgntrrlaTLGPLLQDLEARIIDEQGDVMPARGVG 387
Cdd:cd17653 234 R-LYNAYGPTECTISSTMTELLPGQPV--------------------------TIGKPIPNSTCYILDADLQPVPEGVVG 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 388 VIELRGESLTPGYL-----TMGGFIPAQDEHGW--YDTGDLGYLTEEGHVVVCGRVKDVI 440
Cdd:cd17653 287 EICISGVQVARGYLgnpalTASKFVPDPFWPGSrmYRTGDYGRWTEDGGLEFLGREDNQV 346
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
114-497 |
1.12e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 95.49 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 114 VSEPFLVAIPILEQKGMQVLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRN-IYSNAEAMFVGAQYDV 192
Cdd:PRK06178 171 LPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 193 DkDVMVSWLPCF----HDMGMVgfltIPMFFGAELVKVTpmdflR-DTLLWAKLIDKYQGTMTAAP--NFAYALLAKRLr 265
Cdd:PRK06178 251 D-SVFLSFLPEFwiagENFGLL----FPLFSGATLVLLA-----RwDAVAFMAAVERYRVTRTVMLvdNAVELMDHPRF- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 266 rqakpGDFDLSTLRF--ALSGAEPVEPADVEDLLDAgkpfglrPSAIL--PAYGMAETTLAVSFSecnAGLVVDevDADL 341
Cdd:PRK06178 320 -----AEYDLSSLRQvrVVSFVKKLNPDYRQRWRAL-------TGSVLaeAAWGMTETHTCDTFT---AGFQDD--DFDL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 342 LAA---LRRAVPATkgntrrlatlgpllqdlEARIID-EQGDVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYD 417
Cdd:PRK06178 383 LSQpvfVGLPVPGT-----------------EFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLH 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 418 TGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpGCAVAVRLDAGHSRESFA-VAVESNAFEDPAEV 496
Cdd:PRK06178 446 TGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVL-GSAVVGRPDPDKGQVPVAfVQLKPGADLTAAAL 524
|
.
gi 889038433 497 R 497
Cdd:PRK06178 525 Q 525
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
151-453 |
1.84e-20 |
|
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: 94.52 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLALMQLTSGSTGSPKAVQITHRNI---YSNAEAMFVGAQYDVDKDVMvSWLPCFHDMGM---VGFLTIpmffGAELV 224
Cdd:cd17642 183 DEQVALIMNSSGSTGLPKGVQLTHKNIvarFSHARDPIFGNQIIPDTAIL-TVIPFHHGFGMfttLGYLIC----GFRVV 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 225 KVTPMD---FLRDtllwaklIDKYQGTMTAAPNFAYALLAKrlrrQAKPGDFDLSTLRFALSGAEPVEpADVEDLLdaGK 301
Cdd:cd17642 258 LMYKFEeelFLRS-------LQDYKVQSALLVPTLFAFFAK----STLVDKYDLSNLHEIASGGAPLS-KEVGEAV--AK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 302 PFGLrpSAILPAYGMAETTLAVsfsecnagLVVDEVDAdllaalrravpatkgntrRLATLGPLLQDLEARIIDeqgdvm 381
Cdd:cd17642 324 RFKL--PGIRQGYGLTETTSAI--------LITPEGDD------------------KPGAVGKVVPFFYAKVVD------ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 382 PARG--VGVIElRGESLTPGYLTMGGFI-------PAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDI 452
Cdd:cd17642 370 LDTGktLGPNE-RGELCVKGPMIMKGYVnnpeatkALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAEL 448
|
.
gi 889038433 453 E 453
Cdd:cd17642 449 E 449
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
136-470 |
1.86e-20 |
|
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: 94.83 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 136 ADLLASD-PIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGMV--GF 212
Cdd:COG1021 167 DALLAAPaDLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDAD-TVYLAALPAAHNFPLSspGV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 213 LTiPMFFGAELVKVT---PMDFLrdtllwaKLIDKYQGTMTAA-PNFAYALLAKRLRRqakpgDFDLSTLRFALSGAEPV 288
Cdd:COG1021 246 LG-VLYAGGTVVLAPdpsPDTAF-------PLIERERVTVTALvPPLALLWLDAAERS-----RYDLSSLRVLQVGGAKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 289 EPADVEDLLDAgkpFGLRPSAIlpaYGMAEttlavsfsecnaGLVV-----DEVDadllaalrravpatkgntRRLATLG 363
Cdd:COG1021 313 SPELARRVRPA---LGCTLQQV---FGMAE------------GLVNytrldDPEE------------------VILTTQG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 364 -PLLQDLEARIIDEQG-DVMPargvGVIelrGESLTPGYLTMGGFIPAqDEH--------GWYDTGDLGYLTEEGHVVVC 433
Cdd:COG1021 357 rPISPDDEVRIVDEDGnPVPP----GEV---GELLTRGPYTIRGYYRA-PEHnaraftpdGFYRTGDLVRRTPDGYLVVE 428
|
330 340 350
....*....|....*....|....*....|....*..
gi 889038433 434 GRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAV 470
Cdd:COG1021 429 GRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAM 465
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
129-537 |
3.13e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 93.72 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 129 GMQVLTVADLLAS-DPIGPIE---VGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSwLPCF 204
Cdd:PRK09088 108 RTDVEDLAAFIASaDALEPADtpsIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCD-APMF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 205 HDMGMVGFLTiPMFFGAELVKVTPMDFLRDTLLWakLIDKyqgTMTAAPNFAYALLAKRLRRQakPGdFDLSTLRF---A 281
Cdd:PRK09088 187 HIIGLITSVR-PVLAVGGSILVSNGFEPKRTLGR--LGDP---ALGITHYFCVPQMAQAFRAQ--PG-FDAAALRHltaL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 282 LSGAEPVEPADVEDLLDAGKPfglrpsaILPAYGMAEttlavsfsecnAGLVVD-EVDADLLAAlrravpatkgntrRLA 360
Cdd:PRK09088 258 FTGGAPHAAEDILGWLDDGIP-------MVDGFGMSE-----------AGTVFGmSVDCDVIRA-------------KAG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 361 TLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMggfiP-----AQDEHGWYDTGDLGYLTEEGHVVVCGR 435
Cdd:PRK09088 307 AAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRR----PqatarAFTGDGWFRTGDIARRDADGFFWVVDR 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 436 VKDVIIMAGRNIYPTDIERAAGRVDGVRPgCAVAVRLDA-----GHsresFAVAVESNAFEDPAEVR-RIEHQVAHEVVa 509
Cdd:PRK09088 383 KKDMFISGGENVYPAEIEAVLADHPGIRE-CAVVGMADAqwgevGY----LAIVPADGAPLDLERIRsHLSTRLAKYKV- 456
|
410 420
....*....|....*....|....*...
gi 889038433 510 evdvrPRNVVVLgpGTIPKTPSGKLRRA 537
Cdd:PRK09088 457 -----PKHLRLV--DALPRTASGKLQKA 477
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
153-533 |
3.70e-20 |
|
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: 93.55 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHR----NIYSNAEAMFVGAQydvdkDVMVSWLPCFHDM-----GMVGFLTipmfFGAEL 223
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNdyayNVRASAEVCGLDQD-----TVYLAVLPAAHNFplacpGVLGTLL----AGGRV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 224 VKVTPMDflRDTLLwaKLIDKYQGTMTAA-PNFAYALLAKRLRRQAkpgdfDLSTLRFALSGAEPVEPADVEDlldAGKP 302
Cdd:cd05920 211 VLAPDPS--PDAAF--PLIEREGVTVTALvPALVSLWLDAAASRRA-----DLSSLRLLQVGGARLSPALARR---VPPV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 303 FGLRpsaILPAYGMAEttlavsfsecnaGLV----VDEVDADLLAalrravpaTKGNtrrlatlgPLLQDLEARIIDEQG 378
Cdd:cd05920 279 LGCT---LQQVFGMAE------------GLLnytrLDDPDEVIIH--------TQGR--------PMSPDDEIRVVDEEG 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 379 dvmpaRGVGVIELrGESLTPGYLTMGGFIPAQ-------DEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTD 451
Cdd:cd05920 328 -----NPVPPGEE-GELLTRGPYTIRGYYRAPehnarafTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEE 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 452 IERAAGRVDGVRPGCAVAVRlDAGHSRESFAVAVESNAFEDPAEVRRIEHQVAhevVAEVDVrPRNVVVLgpGTIPKTPS 531
Cdd:cd05920 402 VENLLLRHPAVHDAAVVAMP-DELLGERSCAFVVLRDPPPSAAQLRRFLRERG---LAAYKL-PDRIEFV--DSLPLTAV 474
|
..
gi 889038433 532 GK 533
Cdd:cd05920 475 GK 476
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
131-534 |
4.17e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 93.46 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 131 QVLTVADLLASDPIGP--IEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMG 208
Cdd:PRK08316 148 GWLDFADWAEAGSVAEpdVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSAD-DIPLHALPLYHCAQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 209 MVGFLTIPMFFGAELVKV---TPMDFLRdtllwakLIDKYQGTMT-AAPNFAYALLakrlrRQAKPGDFDLSTLRFALSG 284
Cdd:PRK08316 227 LDVFLGPYLYVGATNVILdapDPELILR-------TIEAERITSFfAPPTVWISLL-----RHPDFDTRDLSSLRKGYYG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 285 AE--PVEPadVEDLLDAgkpfglrpsaiLPA------YGMAETtlavsfsecnaglvvdevdADLLAALRravpaTKGNT 356
Cdd:PRK08316 295 ASimPVEV--LKELRER-----------LPGlrfyncYGQTEI-------------------APLATVLG-----PEEHL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 357 RRLATLG-PLLqDLEARIIDEQGDVMPARGVGVIELRGESLTPGYL-----TMGGFipaqdEHGWYDTGDLGYLTEEGHV 430
Cdd:PRK08316 338 RRPGSAGrPVL-NVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWddpekTAEAF-----RGGWFHSGDLGVMDEEGYI 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 431 VVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpgcAVAVrLDAGHSR--ESFAVAVesnafedpaeVRRIEHQV-AHEV 507
Cdd:PRK08316 412 TVVDRKKDMIKTGGENVASREVEEALYTHPAVA---EVAV-IGLPDPKwiEAVTAVV----------VPKAGATVtEDEL 477
|
410 420 430
....*....|....*....|....*....|...
gi 889038433 508 VAEVDVR------PRNVVVLgpGTIPKTPSGKL 534
Cdd:PRK08316 478 IAHCRARlagfkvPKRVIFV--DELPRNPSGKI 508
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
146-466 |
9.46e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 92.64 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 146 PIEVGEDDlALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVK 225
Cdd:PRK05852 171 PEGLRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLS-PRDATVAVMPLYHGHGLIAALLATLASGGAVLL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 226 VTPMDFLRDTlLWAKLIDKYQGTMTAAPNFAYALLAkrlRRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpFGl 305
Cdd:PRK05852 249 PARGRFSAHT-FWDDIKAVGATWYTAVPTIHQILLE---RAATEPSGRKPAALRFIRSCSAPLTAETAQALQTE---FA- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 306 rpSAILPAYGMAETTLAVsfsecnaglvvdevdadllaALRRAVPATKGNTRRlATLGPLLQD--LEARIIDEQGDVMPA 383
Cdd:PRK05852 321 --APVVCAFGMTEATHQV--------------------TTTQIEGIGQTENPV-VSTGLVGRStgAQIRIVGSDGLPLPA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 384 RGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTdieraagRVDGVR 463
Cdd:PRK05852 378 GAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPE-------RVEGVL 450
|
...
gi 889038433 464 PGC 466
Cdd:PRK05852 451 ASH 453
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
133-538 |
1.23e-19 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 91.97 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 133 LTVADLLASD--PIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNaeamfVGAQYDVD--------KDVMVSWLP 202
Cdd:PLN02246 158 LHFSELTQADenELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTS-----VAQQVDGEnpnlyfhsDDVILCVLP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 203 CFHDMGMVGFLTIPMFFGAELVkVTPmDFLRDTLLwaKLIDKYQgtMTAAPNFAYALLAkrLRRQAKPGDFDLSTLRFAL 282
Cdd:PLN02246 233 MFHIYSLNSVLLCGLRVGAAIL-IMP-KFEIGALL--ELIQRHK--VTIAPFVPPIVLA--IAKSPVVEKYDLSSIRMVL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 283 SGAEPVEpadvEDLLDAgkpFGLR-PSAIL-PAYGMAEttlavsfsecnAGLVVdevdADLLAALRRAVPATKGntrrla 360
Cdd:PLN02246 305 SGAAPLG----KELEDA---FRAKlPNAVLgQGYGMTE-----------AGPVL----AMCLAFAKEPFPVKSG------ 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 361 TLGPLLQDLEARIID-EQGDVMPARGVGVIELRGESLTPGYL-----TMGGFipaqDEHGWYDTGDLGYLTEEGHVVVCG 434
Cdd:PLN02246 357 SCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLndpeaTANTI----DKDGWLHTGDIGYIDDDDELFIVD 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 435 RVKDVIIMAGRNIYPTDIER---AAGRVDgvrpGCAVAVRLD--AGHSRESFAVAVE-SNAFEDpaevrRIEHQVAHEVV 508
Cdd:PLN02246 433 RLKELIKYKGFQVAPAELEAlliSHPSIA----DAAVVPMKDevAGEVPVAFVVRSNgSEITED-----EIKQFVAKQVV 503
|
410 420 430
....*....|....*....|....*....|
gi 889038433 509 aeVDVRPRNVVVLgpGTIPKTPSGKLRRAN 538
Cdd:PLN02246 504 --FYKRIHKVFFV--DSIPKAPSGKILRKD 529
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
131-536 |
1.33e-19 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 91.96 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 131 QVLTVADLlASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSN-AEAMF-VGAQYdVDKDVMVSWLPCFHDMG 208
Cdd:PLN02330 164 ELLEAADR-AGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFsVGPEM-IGQVVTLGLIPFFHIYG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 209 MVGFLTIPMFFGAELVKVTPMDfLRdTLLWAKLIDKyqgtMTAAPNFAYALLAkrLRRQAKPGDFDLSTLRF--ALSGAE 286
Cdd:PLN02330 242 ITGICCATLRNKGKVVVMSRFE-LR-TFLNALITQE----VSFAPIVPPIILN--LVKNPIVEEFDLSKLKLqaIMTAAA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 287 PVEPadveDLLDA--GKPFGLRpsaILPAYGMAETTlavsfseCnaglvvdevdadllAALRRAVPATKGNTRRLATLGP 364
Cdd:PLN02330 314 PLAP----ELLTAfeAKFPGVQ---VQEAYGLTEHS-------C--------------ITLTHGDPEKGHGIAKKNSVGF 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 365 LLQDLEARIID-EQGDVMPARGVGVIELRGESLTPGYLTMGGFIPAQ-DEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIM 442
Cdd:PLN02330 366 ILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTiDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 443 AGRNIYPTDIEraagrvdgvrpgcavAVRLdaGH-SRESFAVA--VESNAFEDPA-------EVRRIEHQVAHEVVAEVD 512
Cdd:PLN02330 446 KGFQVAPAELE---------------AILL--THpSVEDAAVVplPDEEAGEIPAacvvinpKAKESEEDILNFVAANVA 508
|
410 420
....*....|....*....|....
gi 889038433 513 VRPRNVVVLGPGTIPKTPSGKLRR 536
Cdd:PLN02330 509 HYKKVRVVQFVDSIPKSLSGKIMR 532
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
25-536 |
2.08e-19 |
|
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: 91.21 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 25 HMPVRHTWGEVHERARCIAGGLAAAGVGLGDVVGVlagfpveIAPTAQALW-------MRGASLTMLHQptpRTDlavwa 97
Cdd:cd12118 25 YGDRRYTWRQTYDRCRRLASALAALGISRGDTVAV-------LAPNTPAMYelhfgvpMAGAVLNALNT---RLD----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 98 EDTMTVI-GMIEAKAVIVSEPFlvaipileqkgmqvlTVADLLAS-----DPIGPieVGEDDLALMQLTSGSTGSPKAVQ 171
Cdd:cd12118 90 AEEIAFIlRHSEAKVLFVDREF---------------EYEDLLAEgdpdfEWIPP--ADEWDPIALNYTSGTTGRPKGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 172 ITHRNIYSNAEAMFVGaqYDVDKDVMVSW-LPCFHDMGMVGFLTIPMFFGAE--LVKVTPmdflrdTLLWaKLIDKYQGT 248
Cdd:cd12118 153 YHHRGAYLNALANILE--WEMKQHPVYLWtLPMFHCNGWCFPWTVAAVGGTNvcLRKVDA------KAIY-DLIEKHKVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 249 -MTAAPNfAYALLAKRLRRQAKPGDfdlSTLRFALSGAEPvePADVedlLDAGKPFGLRPSAilpAYGMAETTLAVSFSE 327
Cdd:cd12118 224 hFCGAPT-VLNMLANAPPSDARPLP---HRVHVMTAGAPP--PAAV---LAKMEELGFDVTH---VYGLTETYGPATVCA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 328 CNAGLvvDEVDADLLAAL--RRAVpatkgntrRLATLGPLlqdleaRIIDEQG-DVMPARG--VGVIELRGESLTPGYL- 401
Cdd:cd12118 292 WKPEW--DELPTEERARLkaRQGV--------RYVGLEEV------DVLDPETmKPVPRDGktIGEIVFRGNIVMKGYLk 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 402 ----TMGGFipaqdEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPgCAVAVRLDA--G 475
Cdd:cd12118 356 npeaTAEAF-----RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLE-AAVVARPDEkwG 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889038433 476 HSRESFaVAVESNAFEDPAEVrrIEH---QVAHEVVaevdvrPRNVVVlgpGTIPKTPSGKLRR 536
Cdd:cd12118 430 EVPCAF-VELKEGAKVTEEEI--IAFcreHLAGFMV------PKTVVF---GELPKTSTGKIQK 481
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
152-459 |
2.51e-19 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 91.70 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYdVDKDVMVSWLPCFHDMGM-VGFLTiPMFFGAELV------ 224
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADF-TPNDRFMSALPLFHSFGLtVGLFT-PLLTGAEVFlypspl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 225 --KVTP-MDFLRD-TLLWaklidkyqGTMTAAPNFAyallakrlrRQAKPGDFdlSTLRFALSGAEPVEPADVEDLLDAg 300
Cdd:PRK08043 443 hyRIVPeLVYDRNcTVLF--------GTSTFLGNYA---------RFANPYDF--ARLRYVVAGAEKLQESTKQLWQDK- 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 301 kpFGLRpsaILPAYGMAETTLAVSFSecnaglvvdevdadllaalrraVP-ATKgntrrLATLGPLLQDLEARIID---- 375
Cdd:PRK08043 503 --FGLR---ILEGYGVTECAPVVSIN----------------------VPmAAK-----PGTVGRILPGMDARLLSvpgi 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 376 EQGdvmpargvGVIELRGESLTPGYLTMG--GFI--PAQD------EHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGR 445
Cdd:PRK08043 551 EQG--------GRLQLKGPNIMNGYLRVEkpGVLevPTAEnargemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGE 622
|
330
....*....|....
gi 889038433 446 NIYPTDIERAAGRV 459
Cdd:PRK08043 623 MVSLEMVEQLALGV 636
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
109-537 |
2.62e-19 |
|
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: 90.72 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 109 AKAVIVSEPFLVAIPILEqkgMQVLTVADLLASDPIGP-IEVGEDDLALMQLTSGSTGSPKAVQITHRNI---YSNAEAM 184
Cdd:cd12117 95 AKVLLTDRSLAGRAGGLE---VAVVIDEALDAGPAGNPaVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVvrlVKNTNYV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 185 FVGAQydvdkDVMVSWLPCFHDMGMvgfLTI--PMFFGAELVkVTPMDFLRDTLLWAKLIDKYQGT---MTAApnfAYAL 259
Cdd:cd12117 172 TLGPD-----DRVLQTSPLAFDAST---FEIwgALLNGARLV-LAPKGTLLDPDALGALIAEEGVTvlwLTAA---LFNQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 260 LAkrlrrQAKPGDFdlSTLRFALSGAEPVEPADVEDLLDAGKPfgLRpsaILPAYGMAETTLavsFSECnagLVVDEVDA 339
Cdd:cd12117 240 LA-----DEDPECF--AGLRELLTGGEVVSPPHVRRVLAACPG--LR---LVNGYGPTENTT---FTTS---HVVTELDE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 340 DllaalRRAVPATK--GNTRrlatlgpllqdleARIIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIPAQDE 412
Cdd:cd12117 302 V-----AGSIPIGRpiANTR-------------VYVLDEDGRPVPPGVPGELYVGGDGLALGYlnrpaLTAERFVADPFG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 413 HG--WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpGCAVAVRLDAGHSRESFAvAVESNAF 490
Cdd:cd12117 364 PGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVR-EAVVVVREDAGGDKRLVA-YVVAEGA 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 889038433 491 EDPAEVRRIehqvAHEVVAEVDVrPRNVVVLgpGTIPKTPSGKL-RRA 537
Cdd:cd12117 442 LDAAELRAF----LRERLPAYMV-PAAFVVL--DELPLTANGKVdRRA 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
140-536 |
4.05e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.94 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 140 ASDPIGPIEvgEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFF 219
Cdd:PRK12316 4684 AHDPAVRLH--PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT--GERYELTPDDRVLQFMSFSFDGSHEGLYHPLIN 4759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 220 GAELVKVTPMDFLRDTLLwaKLIDKYQGTMTAAPNFAYALLAKRLRRQAKPGdfdlsTLRFALSGAEPVEPADVEDLLDA 299
Cdd:PRK12316 4760 GASVVIRDDSLWDPERLY--AEIHEHRVTVLVFPPVYLQQLAEHAERDGEPP-----SLRVYCFGGEAVAQASYDLAWRA 4832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 300 gkpfgLRPSAILPAYGMAETTLAVSFSECNAGLVvdevdadllaALRRAVPatkgntrrlatLGPLLQDLEARIIDEQGD 379
Cdd:PRK12316 4833 -----LKPVYLFNGYGPTETTVTVLLWKARDGDA----------CGAAYMP-----------IGTPLGNRSGYVLDGQLN 4886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 380 VMPARGVGVIELRGESLTPGY-----LTMGGFIPAQ-DEHG--WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTD 451
Cdd:PRK12316 4887 PLPVGVAGELYLGGEGVARGYlerpaLTAERFVPDPfGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGE 4966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 452 IERAAGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDP---AEVRRIEHQVAHEVVAEVDVrPRNVVVLgpGTIPK 528
Cdd:PRK12316 4967 IEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADeaqAELRDELKAALRERLPEYMV-PAHLVFL--ARMPL 5043
|
....*...
gi 889038433 529 TPSGKLRR 536
Cdd:PRK12316 5044 TPNGKLDR 5051
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
152-501 |
4.56e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 91.18 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAmfVGAQYDVD-KDVMVSWLPCFHDMGMVGFLTIPMFFGaelVKVtpmd 230
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRAQ--VAARIDFSpEDKVFNALPVFHSFGLTGGLVLPLLSG---VKV---- 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 FLRDTLLWAKLIDK--YQ-------GTMTAAPNFAyallakrlrRQAKPgdFDLSTLRFALSGAEPVEPADVEDLLDAgk 301
Cdd:PRK06814 864 FLYPSPLHYRIIPEliYDtnatilfGTDTFLNGYA---------RYAHP--YDFRSLRYVFAGAEKVKEETRQTWMEK-- 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 302 pFGLRpsaILPAYGMAETtlavsfsecnaglvvdevdADLLAAlrravpatkgNT---RRLATLGPLLQDLEARI----- 373
Cdd:PRK06814 931 -FGIR---ILEGYGVTET-------------------APVIAL----------NTpmhNKAGTVGRLLPGIEYRLepvpg 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 374 IDEQGDVMpargvgvieLRGESLTPGYLTM---GGFIPAQDehGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPT 450
Cdd:PRK06814 978 IDEGGRLF---------VRGPNVMLGYLRAenpGVLEPPAD--GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLA 1046
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 889038433 451 DIERAAGRVDGVRPGCAVAV-------RL-----DAGHSRESFAVAVESNAFED---PAEVRRIEH 501
Cdd:PRK06814 1047 AVEELAAELWPDALHAAVSIpdarkgeRIillttASDATRAAFLAHAKAAGASElmvPAEIITIDE 1112
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
152-455 |
5.00e-19 |
|
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: 89.48 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAeamFVGAQ-YDVDKDVMVsWlpCFHD----MGMVGFLTIPMFFGAELVkV 226
Cdd:cd05969 89 EDPTLLHYTSGTTGTPKGVLHVHDAMIFYY---FTGKYvLDLHPDDIY-W--CTADpgwvTGTVYGIWAPWLNGVTNV-V 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 227 TPMDFlrDTLLWAKLIDKYQGT-MTAAPNfayallakRLRRQAKPGD-----FDLSTLRFALSGAEPVEPadvEDLLDAG 300
Cdd:cd05969 162 YEGRF--DAESWYGIIERVKVTvWYTAPT--------AIRMLMKEGDelarkYDLSSLRFIHSVGEPLNP---EAIRWGM 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 301 KPFGLRpsaILPAYGMAETtlavsfsecnaglvvdevdADLLAALRRAVPATKGntrrlaTLGPLLQDLEARIIDEQGDV 380
Cdd:cd05969 229 EVFGVP---IHDTWWQTET-------------------GSIMIANYPCMPIKPG------SMGKPLPGVKAAVVDENGNE 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 889038433 381 MPARGVGVIELRGE--SLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERA 455
Cdd:cd05969 281 LPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESA 357
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
146-536 |
9.34e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 89.69 E-value: 9.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 146 PIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQY------DVDKDVMVSWLPCFHdmgmVGFLTIPMFF 219
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPafekkpRPDQLNFVCALPLYH----IFALTVCGLL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 220 GaelVKVTPMDFL----RDTLLWAKLIDKYQGTMTAAPNFAY-ALLAKRLRRQakpgdFDLSTLRFALSGAEPVEPADVE 294
Cdd:PRK07059 274 G---MRTGGRNILipnpRDIPGFIKELKKYQVHIFPAVNTLYnALLNNPDFDK-----LDFSKLIVANGGGMAVQRPVAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 295 DLLDagkpfgLRPSAILPAYGMAETTLAVSfseCNAglvvdeVDADLLAAlrravpatkgntrrlaTLGPLLQDLEARII 374
Cdd:PRK07059 346 RWLE------MTGCPITEGYGLSETSPVAT---CNP------VDATEFSG----------------TIGLPLPSTEVSIR 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 375 DEQGDVMPARGVGVIELRGESLTPGYLTMggfipaQDE-------HGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNI 447
Cdd:PRK07059 395 DDDGNDLPLGEPGEICIRGPQVMAGYWNR------PDEtakvmtaDGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNV 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 448 YPTDIERAAGRVDGVRPGCAVAVrlDAGHSRES---FAVAvesnafEDPA--EVRRIEHqvAHEVVAEVDvRPRNVVVLg 522
Cdd:PRK07059 469 YPNEIEEVVASHPGVLEVAAVGV--PDEHSGEAvklFVVK------KDPAltEEDVKAF--CKERLTNYK-RPKFVEFR- 536
|
410
....*....|....*
gi 889038433 523 pGTIPKTPSGK-LRR 536
Cdd:PRK07059 537 -TELPKTNVGKiLRR 550
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
160-455 |
1.19e-18 |
|
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: 89.34 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 160 TSGSTGSPKAVQITHRNI-----YSNAEAMFVGAqyDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAE------------ 222
Cdd:cd05933 158 TSGTTGMPKGVMLSHDNItwtakAASQHMDLRPA--TVGQESVVSYLPLSHIAAQILDIWLPIKVGGQvyfaqpdalkgt 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 223 ----LVKVTPMDFL------------------------RDTLLWAKLI--DKYQGTMTA-APNFAYALLAKRLR----RQ 267
Cdd:cd05933 236 lvktLREVRPTAFMgvprvwekiqekmkavgaksgtlkRKIASWAKGVglETNLKLMGGeSPSPLFYRLAKKLVfkkvRK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 268 AkpgdFDLSTLRFALSGAEPVEPADVEDLLDAGKPfglrpsaILPAYGMAETTLAVSFSECNAglvvdevdadllaalrr 347
Cdd:cd05933 316 A----LGLDRCQKFFTGAAPISRETLEFFLSLNIP-------IMELYGMSETSGPHTISNPQA----------------- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 348 avpatkgntRRLATLGPLLQDLEARIIDEQGDvmparGVGVIELRGESLTPGYLTMggfiP-----AQDEHGWYDTGDLG 422
Cdd:cd05933 368 ---------YRLLSCGKALPGCKTKIHNPDAD-----GIGEICFWGRHVFMGYLNM----EdkteeAIDEDGWLHSGDLG 429
|
330 340 350
....*....|....*....|....*....|....
gi 889038433 423 YLTEEGHVVVCGRVKDVIIMA-GRNIYPTDIERA 455
Cdd:cd05933 430 KLDEDGFLYITGRIKELIITAgGENVPPVPIEDA 463
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
132-537 |
1.87e-18 |
|
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: 88.10 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 132 VLTVADLLASDPIGPI-EVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVD-KDVMVSWLPCFHDMGM 209
Cdd:cd17646 117 LLGDEALAAPPATPPLvPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWM--QDEYPLGpGDRVLQKTPLSFDVSV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 210 VGFLtIPMFFGAELVKVTPmDFLRDTLLWAKLIDKYQGTMTaapNFAYALLAKRLrrqAKPGDFDLSTLRFALSGAEPVe 289
Cdd:cd17646 195 WELF-WPLVAGARLVVARP-GGHRDPAYLAALIREHGVTTC---HFVPSMLRVFL---AEPAAGSCASLRRVFCSGEAL- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 290 PADVEDLldagkpFGLRPSAIL-PAYGMAETTLAVSFSECNAGLVVDEVdadllaALRRAVPatkgNTRrlatlgpllqd 368
Cdd:cd17646 266 PPELAAR------FLALPGAELhNLYGPTEAAIDVTHWPVRGPAETPSV------PIGRPVP----NTR----------- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 369 leARIIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIPAQDEHG--WYDTGDLGYLTEEGHVVVCGRVKDVII 441
Cdd:cd17646 319 --LYVLDDALRPVPVGVPGELYLGGVQLARGYlgrpaLTAERFVPDPFGPGsrMYRTGDLARWRPDGALEFLGRSDDQVK 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 442 MAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHSR-ESFAVAVESNAFEDPAEVRR--IEHQVAHEVVAEVDVRPRnv 518
Cdd:cd17646 397 IRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARlVGYVVPAAGAAGPDTAALRAhlAERLPEYMVPAAFVVLDA-- 474
|
410
....*....|....*....
gi 889038433 519 vvlgpgtIPKTPSGKLRRA 537
Cdd:cd17646 475 -------LPLTANGKLDRA 486
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
148-536 |
2.22e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 88.19 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 148 EVGEDDLALMQLTSGSTGSPKAVQITHRNIYSN---AEAMFvGAQYDVDKDVMVSWLPCFHdmgmVGFLTIP----MFFG 220
Cdd:PRK08974 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqAKAAY-GPLLHPGKELVVTALPLYH----IFALTVNcllfIELG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 221 AELVKVT-PmdflRDTLLWAKLIDKYQGT-MTAAPNFAYALLAKRlrrqakpgDF---DLSTLRFALSGAEPVEPADVEd 295
Cdd:PRK08974 277 GQNLLITnP----RDIPGFVKELKKYPFTaITGVNTLFNALLNNE--------EFqelDFSSLKLSVGGGMAVQQAVAE- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 296 lldagKPFGLRPSAILPAYGMAETTLAVSfseCNAglvVDEVDADllAALRRAVPATkgntrrlatlgpllqdlEARIID 375
Cdd:PRK08974 344 -----RWVKLTGQYLLEGYGLTECSPLVS---VNP---YDLDYYS--GSIGLPVPST-----------------EIKLVD 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 376 EQGDVMPARGVGVIELRGESLTPGYLTMggfiP-AQDE---HGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTD 451
Cdd:PRK08974 394 DDGNEVPPGEPGELWVKGPQVMLGYWQR----PeATDEvikDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 452 IERAAGRVDGVRPGCAVAVRLDA-GHSRESFAVAVESNAFEDpaEVRRI--EHQVAHEVVAEVDVRPRnvvvlgpgtIPK 528
Cdd:PRK08974 470 IEDVVMLHPKVLEVAAVGVPSEVsGEAVKIFVVKKDPSLTEE--ELITHcrRHLTGYKVPKLVEFRDE---------LPK 538
|
....*....
gi 889038433 529 TPSGK-LRR 536
Cdd:PRK08974 539 SNVGKiLRR 547
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
146-470 |
2.52e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 88.01 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 146 PIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEA----MFVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGA 221
Cdd:PRK08751 202 TLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQahqwLAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGG 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 222 --ELVKvTPmdflRDTLLWAKLIDKYQGTMTAAPNFAYALLAKrlrrqaKPG--DFDLSTLRFALSGAEPVEPADVEDLl 297
Cdd:PRK08751 282 cnHLIS-NP----RDMPGFVKELKKTRFTAFTGVNTLFNGLLN------TPGfdQIDFSSLKMTLGGGMAVQRSVAERW- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 298 daGKPFGLrpsAILPAYGMAETTLAVsfseCNAGLVVDEVDAdllaALRRAVPATkgntrrlatlgpllqdlEARIIDEQ 377
Cdd:PRK08751 350 --KQVTGL---TLVEAYGLTETSPAA----CINPLTLKEYNG----SIGLPIPST-----------------DACIKDDA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 378 GDVMPARGVGVIELRGESLTPGYLTMGGFIP-AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAA 456
Cdd:PRK08751 400 GTVLAIGEIGELCIKGPQVMKGYWKRPEETAkVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVI 479
|
330
....*....|....
gi 889038433 457 GRVDGVRPGCAVAV 470
Cdd:PRK08751 480 AMMPGVLEVAAVGV 493
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
103-536 |
2.77e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 87.63 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 103 VIGMIEAKAVIVSEPFlVAIPILEQKgmQVLTVADLLAS--------DPIGPIEV-GEDDLALMQLTSGSTGSPKAVQIT 173
Cdd:PRK06145 94 ILGDAGAKLLLVDEEF-DAIVALETP--KIVIDAAAQADsrrlaqggLEIPPQAAvAPTDLVRLMYTSGTTDRPKGVMHS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 174 HRNIYSNAEAMFVGAQYDVDKDVMVSWlPCFHdmgmVGFLTIPmffGAELVKVTPM-----DFLRDTLLWAKLIDKYQGT 248
Cdd:PRK06145 171 YGNLHWKSIDHVIALGLTASERLLVVG-PLYH----VGAFDLP---GIAVLWVGGTlrihrEFDPEAVLAAIERHRLTCA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 249 MTAApnfayaLLAKRLRRQAKPGDFDLSTLRFALSGAEPVEPADVEDLldaGKPFglRPSAILPAYGMAETTLAVSFSEc 328
Cdd:PRK06145 243 WMAP------VMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDF---TRVF--TRARYIDAYGLTETCSGDTLME- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 329 nAGLVVDEVdadllaalrravpatkGNTRRLatlgplLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMGGFIP 408
Cdd:PRK06145 311 -AGREIEKI----------------GSTGRA------LAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 409 AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRlDAGHSRESFAVAV--E 486
Cdd:PRK06145 368 EAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVH-DDRWGERITAVVVlnP 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 889038433 487 SNAFEDPAEVRRIEHQVAHEVVaevdvrPRNVVVLgpGTIPKTPSGK-LRR 536
Cdd:PRK06145 447 GATLTLEALDRHCRQRLASFKV------PRQLKVR--DELPRNPSGKvLKR 489
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
146-536 |
3.41e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 87.96 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 146 PIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVG-AQYDVD--------KDVMVSWLPCFHDMGMVGFLTIP 216
Cdd:PRK12492 201 PVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRAClSQLGPDgqplmkegQEVMIAPLPLYHIYAFTANCMCM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 217 MFFGAELVKVT-PmdflRDTLLWAKLIDKYQGTMTAAPNFAYALLakrlrrQAKPG--DFDLSTLRFALSGAEPVEPADV 293
Cdd:PRK12492 281 MVSGNHNVLITnP----RDIPGFIKELGKWRFSALLGLNTLFVAL------MDHPGfkDLDFSALKLTNSGGTALVKATA 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 294 EdlldagKPFGLRPSAILPAYGMAETTLAVSfsecnaglvvdevdadllaalrrAVPatKGNTRRLATLGPLLQDLEARI 373
Cdd:PRK12492 351 E------RWEQLTGCTIVEGYGLTETSPVAS-----------------------TNP--YGELARLGTVGIPVPGTALKV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 374 IDEQGDVMPARGVGVIELRGESLTPGYLTM-GGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDI 452
Cdd:PRK12492 400 IDDDGNELPLGERGELCIKGPQVMKGYWQQpEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEI 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 453 ERAAGRVDGVRPGCAVAVRLD-AGHSRESFAVAVESNAFEDPAEVRRIEHQVAHEVvaevdvrPRNVVVlgPGTIPKTPS 531
Cdd:PRK12492 480 EDVVMAHPKVANCAAIGVPDErSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKV-------PKHIVL--RDSLPMTPV 550
|
....*.
gi 889038433 532 GK-LRR 536
Cdd:PRK12492 551 GKiLRR 556
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
108-537 |
3.45e-18 |
|
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: 87.56 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 108 EAKAVIVSEPFLVAiPILEQKGMQVLTVADLL-------ASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSN 180
Cdd:cd05923 100 EMTAAVIAVDAQVM-DAIFQSGVRVLALSDLVglgepesAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 181 AEAMFVGAQYDV-DKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTpmDFLRDTLLwaKLIDKYQGT-MTAAPNFAYA 258
Cdd:cd05923 179 VLFMSTQAGLRHgRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVE--EFDPADAL--KLIEQERVTsLFATPTHLDA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 259 LLAKRLRRQAKpgdfdLSTLRfALSGAEPVEPADVEDLLDAGKPfglrpSAILPAYGMAETTLAVSFSECNAGlvvdevd 338
Cdd:cd05923 255 LAAAAEFAGLK-----LSSLR-HVTFAGATMPDAVLERVNQHLP-----GEKVNIYGTTEAMNSLYMRDARTG------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 339 ADLLAALRRAVpatkgntrRLATLGPLLQDLEAriIDEQGDVmpargvgVIELRGESLTPGYLTMGGFIPAQDEHGWYDT 418
Cdd:cd05923 317 TEMRPGFFSEV--------RIVRIGGSPDEALA--NGEEGEL-------IVAAAADAAFTGYLNQPEATAKKLQDGWYRT 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 419 GDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDA-GHSRESFAVAVESNAFEDPAEVR 497
Cdd:cd05923 380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSVTACVVPREGTLSADELDQF 459
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 889038433 498 RIEHQVAHEvvaevdVRPRNVVVLgpGTIPKTPSGK-LRRA 537
Cdd:cd05923 460 CRASELADF------KRPRRYFFL--DELPKNAMNKvLRRQ 492
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
143-536 |
7.09e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 86.74 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 143 PIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSN---AEAMfVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFF 219
Cdd:PRK05677 198 PVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRAL-MGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLI 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 220 GAELVKVT-PmdflRDTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQakpgDFDLSTLRFALSGAEPVEPADVEdlld 298
Cdd:PRK05677 277 GNHNILISnP----RDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFR----KLDFSALKLTLSGGMALQLATAE---- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 299 agKPFGLRPSAILPAYGMAETTLAVSFSECNAglvvdevdadllaalrravpatkgntRRLATLGPLLQDLEARIIDEQG 378
Cdd:PRK05677 345 --RWKEVTGCAICEGYGMTETSPVVSVNPSQA--------------------------IQVGTIGIPVPSTLCKVIDDDG 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 379 DVMPARGVGVIELRGESLTPGYLT-MGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAG 457
Cdd:PRK05677 397 NELPLGEVGELCVKGPQVMKGYWQrPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 458 RVDGVRPGCAVAVRLDA-GHSRESFAVaVESNAFEDPAEVRRIEHQ--VAHEVVAEVDVRPRnvvvlgpgtIPKTPSGK- 533
Cdd:PRK05677 477 ALPGVLQCAAIGVPDEKsGEAIKVFVV-VKPGETLTKEQVMEHMRAnlTGYKVPKAVEFRDE---------LPTTNVGKi 546
|
...
gi 889038433 534 LRR 536
Cdd:PRK05677 547 LRR 549
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
132-534 |
1.19e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 85.98 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 132 VLTVADLLASD--PIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDvmvswlpcfhdmgm 209
Cdd:PRK07786 152 VLGYEDLLAEAgpAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSD-------------- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 210 VGFLTIPMFFGAELVKVTPMDFL-RDTLLW-------AKLIDKYQG----TMTAAPNFAYALLAKrlrRQAKPGDFdlsT 277
Cdd:PRK07786 218 VGFVGVPLFHIAGIGSMLPGLLLgAPTVIYplgafdpGQLLDVLEAekvtGIFLVPAQWQAVCAE---QQARPRDL---A 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 278 LRFALSGAEPVEPADVEDLLDAgkpfgLRPSAILPAYGMAEttlaVSFSECnaglVVDEVDAdllaalrravpatkgnTR 357
Cdd:PRK07786 292 LRVLSWGAAPASDTLLRQMAAT-----FPEAQILAAFGQTE----MSPVTC----MLLGEDA----------------IR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 358 RLATLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVK 437
Cdd:PRK07786 343 KLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 438 DVIIMAGRNIYPTDIERA-AGRVDGVRpgCAVAVRLDAGHSRESFAVAVESNAfEDPAEVRRIEhQVAHEVVAEVDvRPR 516
Cdd:PRK07786 423 DMIISGGENIYCAEVENVlASHPDIVE--VAVIGRADEKWGEVPVAVAAVRND-DAALTLEDLA-EFLTDRLARYK-HPK 497
|
410
....*....|....*...
gi 889038433 517 NVVVLgpGTIPKTPSGKL 534
Cdd:PRK07786 498 ALEIV--DALPRNPAGKV 513
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
121-470 |
1.61e-17 |
|
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: 85.20 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 121 AIPILEQKGMQVLTVADLLA-SDPIGPIEVGE-DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAM---FVGAQYDVDkd 195
Cdd:cd05910 52 AVPVLIDPGMGRKNLKQCLQeAEPDAFIGIPKaDEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALrqlYGIRPGEVD-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 196 vmvswLPCFhdmgmvgfltiPMF--FGAEL---VKVTPMDFLR----DTLLWAKLIDKYQGTMTaapnFAYALLAKRLRR 266
Cdd:cd05910 130 -----LATF-----------PLFalFGPALgltSVIPDMDPTRparaDPQKLVGAIRQYGVSIV----FGSPALLERVAR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 267 QAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpfgLRPSA-ILPAYGMAETtlavsfsecnagLVVDEVDADLLAAL 345
Cdd:cd05910 190 YCAQHGITLPSLRRVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEA------------LPVSSIGSRELLAT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 346 RRAVPATKGNTrrlaTLGPLLQDLEARIID---------EQGDVMPARGVGVIELRGESLTPGYL-----TMGGFIPAQD 411
Cdd:cd05910 253 TTAATSGGAGT----CVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVnrpvaTALAKIDDNS 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 889038433 412 EHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAV 470
Cdd:cd05910 329 EGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
134-454 |
2.06e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.34 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 134 TVADLLASDPIGPIE---VGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAmfVGAQY-----DVDkdvmvswLPCFh 205
Cdd:PRK09274 153 TLATLLRDGAAAPFPmadLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA--LREDYgiepgEID-------LPTF- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 206 dmgmvgfltiPMF--FGAEL----VkVTPMDFLR------DTLLWAklIDKYQ-GTMTAAPnfayALLaKRLRRQAKPGD 272
Cdd:PRK09274 223 ----------PLFalFGPALgmtsV-IPDMDPTRpatvdpAKLFAA--IERYGvTNLFGSP----ALL-ERLGRYGEANG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 273 FDLSTLRFALSGAEPVEPADVEDLLDAgkpfgLRPSA-ILPAYGMAETtLAVSFSECNAglvvdevdadLLAALRRAVPA 351
Cdd:PRK09274 285 IKLPSLRRVISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEA-LPISSIESRE----------ILFATRAATDN 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 352 TKGntrrlATLGPLLQDLEARIID---------EQGDVMPARGVGVIELRGESLTPGYL-----TMGGFIPAQDEHGWYD 417
Cdd:PRK09274 349 GAG-----ICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRSYYnrpeaTRLAKIPDGQGDVWHR 423
|
330 340 350
....*....|....*....|....*....|....*..
gi 889038433 418 TGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIER 454
Cdd:PRK09274 424 MGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCER 460
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
127-453 |
5.92e-17 |
|
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: 83.80 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 127 QKGMQVLTVADLL---ASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSN---AEAMFVGAQYDVDKDVMVSW 200
Cdd:cd05927 86 DAGVKVYSLEEFEklgKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNvagVFKILEILNKINPTDVYISY 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 201 LP------------CFHDMGMVGFltipmFFGaeLVKVTPMDF--LRDTL------LWAKLIDKYQGTMTAAP------- 253
Cdd:cd05927 166 LPlahifervvealFLYHGAKIGF-----YSG--DIRLLLDDIkaLKPTVfpgvprVLNRIYDKIFNKVQAKGplkrklf 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 254 NFAYALLAKRLRRQAKPGD--FD-----------LSTLRFALSGAEPVePADVEDLLDAGkpFGlrpSAILPAYGMAETT 320
Cdd:cd05927 239 NFALNYKLAELRSGVVRASpfWDklvfnkikqalGGNVRLMLTGSAPL-SPEVLEFLRVA--LG---CPVLEGYGQTECT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 321 LAVSFSEcnaglvVDEVDAdllaalrravpatkgntrrlATLGPLLQDLEARIID--EQG-DVMPARGVGVIELRGESLT 397
Cdd:cd05927 313 AGATLTL------PGDTSV--------------------GHVGGPLPCAEVKLVDvpEMNyDAKDPNPRGEVCIRGPNVF 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 889038433 398 PGYLtmggFIPAQ-----DEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMA-GRNIYPTDIE 453
Cdd:cd05927 367 SGYY----KDPEKtaealDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYVAPEKIE 424
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
143-537 |
7.90e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 83.27 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 143 PIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIY----SNAEAMFVGAqydvdKDVMVSWLPCFHDMGMVGFLTIpMF 218
Cdd:PRK06155 171 PAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYwwgrNSAEDLEIGA-----DDVLYTTLPLFHTNALNAFFQA-LL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 219 FGAELVkVTPMdfLRDTLLWAKLIdKYQGTMTaapnfaY---ALLAKRLRRQAKPGDFDlSTLRFALSGAEPvePADVED 295
Cdd:PRK06155 245 AGATYV-LEPR--FSASGFWPAVR-RHGATVT------YllgAMVSILLSQPARESDRA-HRVRVALGPGVP--AALHAA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 296 LLDAgkpFGLrpsAILPAYGMAETTlavsfsecnaglvvdevdadllaalrrAVPATKGNTRRLATLGPLLQDLEARIID 375
Cdd:PRK06155 312 FRER---FGV---DLLDGYGSTETN---------------------------FVIAVTHGSQRPGSMGRLAPGFEARVVD 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 376 EQGDVMPARGVGVIELRGE---SLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDI 452
Cdd:PRK06155 359 EHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEV 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 453 ERAAGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAE-VRRIEHQVAHEVVaevdvrPRNVVVLgpGTIPKTPS 531
Cdd:PRK06155 439 EQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVAlVRHCEPRLAYFAV------PRYVEFV--AALPKTEN 510
|
....*.
gi 889038433 532 GKLRRA 537
Cdd:PRK06155 511 GKVQKF 516
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
111-537 |
1.37e-16 |
|
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: 82.34 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 111 AVIVSEPFLVAIPILeqkgmQVLTVADLLASDPIGPIEVGE----DDLALMQLTSGSTGSPKAVQITHRNI----YSNAE 182
Cdd:cd12116 86 ALVLTDDALPDRLPA-----GLPVLLLALAAAAAAPAAPRTpvspDDLAYVIYTSGSTGRPKGVVVSHRNLvnflHSMRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 183 AMFVGAQydvDKDVMVSwLPCFhDMGMVGFLtIPMFFGAELVkVTPMDFLRDTLLWAKLIDKYQGT-MTAAPNFAYALLA 261
Cdd:cd12116 161 RLGLGPG---DRLLAVT-TYAF-DISLLELL-LPLLAGARVV-IAPRETQRDPEALARLIEAHSITvMQATPATWRMLLD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 262 KrlrrqakpGDFDLSTLRfALSGAEPVEPADVEDLLDagkpfglRPSAILPAYGMAETTLAVSFSECNAGLvvdevdadl 341
Cdd:cd12116 234 A--------GWQGRAGLT-ALCGGEALPPDLAARLLS-------RVGSLWNLYGPTETTIWSTAARVTAAA--------- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 342 laalrRAVPATK--GNTRrlatlgpllqdleARIIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIP---AQD 411
Cdd:cd12116 289 -----GPIPIGRplANTQ-------------VYVLDAALRPVPPGVPGELYIGGDGVAQGYlgrpaLTAERFVPdpfAGP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 412 EHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPgCAVAVRLDAGHSR-ESFAVAVESNAF 490
Cdd:cd12116 351 GSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQ-AAVVVREDGGDRRlVAYVVLKAGAAP 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 889038433 491 eDPAEVRriEHQVAHEVVAEVdvrPRNVVVLgpGTIPKTPSGKLRRA 537
Cdd:cd12116 430 -DAAALR--AHLRATLPAYMV---PSAFVRL--DALPLTANGKLDRK 468
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
132-536 |
1.41e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 83.16 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 132 VLTVADLLA-SDPIGPIE---VGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSWLPCFHDM 207
Cdd:PRK06060 121 VAEAAELMSeAARVAPGGyepMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 208 GMVGFLTIPMFFGAELVkVTPMDFLRDTLlwAKLIDKYQ-GTMTAAPNFaYAllakRLRRQAKPGDFdlSTLRFALSGAE 286
Cdd:PRK06060 201 GLGNSVWFPLATGGSAV-INSAPVTPEAA--AILSARFGpSVLYGVPNF-FA----RVIDSCSPDSF--RSLRCVVSAGE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 287 PVEPADVEDLLDAgkpFGLRPsaILPAYGMaettlavsfSECNAGLVVDEVDadllaalrravpatkgnTRRLATLGPLL 366
Cdd:PRK06060 271 ALELGLAERLMEF---FGGIP--ILDGIGS---------TEVGQTFVSNRVD-----------------EWRLGTLGRVL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 367 QDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMGGfiPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRN 446
Cdd:PRK06060 320 PPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD--SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 447 IYPTDIERAAGRVDGVRPGCAVAVRLDAGHSR-ESFAVAVeSNAFEDPAEVRRIEHQVAHEVVAeVDVRPRNVVVlgpGT 525
Cdd:PRK06060 398 VDPREVERLIIEDEAVAEAAVVAVRESTGASTlQAFLVAT-SGATIDGSVMRDLHRGLLNRLSA-FKVPHRFAVV---DR 472
|
410
....*....|.
gi 889038433 526 IPKTPSGKLRR 536
Cdd:PRK06060 473 LPRTPNGKLVR 483
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
152-538 |
2.30e-16 |
|
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: 82.01 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVKVTPMDF 231
Cdd:cd05905 149 GDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELY-ESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 LRDTLLWAKLIDKYQGTMTAAP----NFAYALLAKRLRrQAKPGDFDLSTLRFALSGAEPvEP--ADVEDLLDAGKPFGL 305
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKlrtlHWCLKDLSSTLA-SLKNRDVNLSSLRMCMVPCEN-RPriSSCDSFLKLFQTLGL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 306 RPSAILPAYGmaetTLAVSF-------SECNAGLVVDevdadlLAALR--RAVPATKGNTRRLATL--GPLLQDLEARII 374
Cdd:cd05905 306 SPRAVSTEFG----TRVNPFicwqgtsGPEPSRVYLD------MRALRhgVVRLDERDKPNSLPLQdsGKVLPGAQVAIV 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 375 DEQGDVMPARG-VGVIELRGESLTPGYLTMGGFIPAQDEH-------------GWYDTGDLGYL----------TEEGHV 430
Cdd:cd05905 376 NPETKGLCKDGeIGEIWVNSPANASGYFLLDGETNDTFKVfpstrlstgitnnSYARTGLLGFLrptkctdlnvEEHDLL 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 431 VVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVA---------VRLDAGHSRESFAVAvesnafedPAEVRRI-- 499
Cdd:cd05905 456 FVVGSIDETLEVRGLRHHPSDIEATVMRVHPYRGRCAVFsitglvvvvAEQPPGSEEEALDLV--------PLVLNAIle 527
|
410 420 430
....*....|....*....|....*....|....*....
gi 889038433 500 EHQVAHEVVAEVDvrprnvvvlgPGTIPKTPSGKLRRAN 538
Cdd:cd05905 528 EHQVIVDCVALVP----------PGSLPKNPLGEKQRME 556
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
94-536 |
2.57e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 81.57 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 94 AVWAEDTMT----VIGMIEAKAVIV-----------------SEPFLV-AIPILEQKGMQVLTVaDLLASDPIGPIEVGE 151
Cdd:PRK07787 49 AVLATPTLAtvlaVVGALIAGVPVVpvppdsgvaerrhiladSGAQAWlGPAPDDPAGLPHVPV-RLHARSWHRYPEPDP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGMVGFLTIPMFFGAELV---KVTP 228
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTAD-DVLVHGLPLFHVHGLVLGVLGPLRIGNRFVhtgRPTP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 229 MDFLRDTLLWAKLidkYQG--TM----TAAPNFAYALlakrlrrqakpgdfdlSTLRFALSGAEPVEPADVEDLLDAGkp 302
Cdd:PRK07787 207 EAYAQALSEGGTL---YFGvpTVwsriAADPEAARAL----------------RGARLLVSGSAALPVPVFDRLAALT-- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 303 fGLRPsaiLPAYGMAETTLAVSfsecnaglvvdeVDADllaalrravpatkgNTRRLATLGPLLQDLEARIIDEQGDVMP 382
Cdd:PRK07787 266 -GHRP---VERYGMTETLITLS------------TRAD--------------GERRPGWVGLPLAGVETRLVDEDGGPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 383 ARG--VGVIELRGESLTPGYL-----TMGGFipaqDEHGWYDTGDLGYLTEEGHVVVCGRVK-DVIIMAGRNIYPTDIER 454
Cdd:PRK07787 316 HDGetVGELQVRGPTLFDGYLnrpdaTAAAF----TADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 455 AAGRVDGVRPGCAVAV-RLDAGHSRESFAVAVesnafEDPAEVRRIEHqVAHEVvaEVDVRPRNVVVLgpGTIPKTPSGK 533
Cdd:PRK07787 392 ALLGHPGVREAAVVGVpDDDLGQRIVAYVVGA-----DDVAADELIDF-VAQQL--SVHKRPREVRFV--DALPRNAMGK 461
|
...
gi 889038433 534 LRR 536
Cdd:PRK07787 462 VLK 464
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
136-537 |
2.90e-16 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 81.36 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 136 ADLLASDPigpievgeDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVD-KDVMVSWLPCFHDMGMVGFLT 214
Cdd:cd17650 85 AKLLLTQP--------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW--RREYELDsFPVRLLQMASFSFDVFAGDFA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 215 IPMFFGAELVkVTPMDFLRDTLLWAKLIDKYQGT-MTAAPNFAYALLAKRLRRQakpgdFDLSTLRFALSGAEPVEPADV 293
Cdd:cd17650 155 RSLLNGGTLV-ICPDEVKLDPAALYDLILKSRITlMESTPALIRPVMAYVYRNG-----LDLSAMRLLIVGSDGCKAQDF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 294 EDLLDAgkpFGLRpSAILPAYGMAETTLAVSFSECNAGLVVDEvdadllaalrRAVPatkgntrrlatLGPLLQDLEARI 373
Cdd:cd17650 229 KTLAAR---FGQG-MRIINSYGVTEATIDSTYYEEGRDPLGDS----------ANVP-----------IGRPLPNTAMYV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 374 IDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIPAQDEHG--WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRN 446
Cdd:cd17650 284 LDERLQPQPVGVAGELYIGGAGVARGYlnrpeLTAERFVENPFAPGerMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 447 IYPTDIERAAGRVDGVRPGcAVAVRLDAGHSRESFAVAVESnAFEDPAEVRriEHQVAHEVVAEVdvrPRNVVVLgpGTI 526
Cdd:cd17650 364 IELGEIESQLARHPAIDEA-VVAVREDKGGEARLCAYVVAA-ATLNTAELR--AFLAKELPSYMI---PSYYVQL--DAL 434
|
410
....*....|.
gi 889038433 527 PKTPSGKLRRA 537
Cdd:cd17650 435 PLTPNGKVDRR 445
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
148-436 |
7.31e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 80.25 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 148 EVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFvgAQYD-VDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVkv 226
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACL--KFFSpKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVV-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 227 tpmdFLRDTLLWAK---LIDKYQGTMTAAPN--FAYALlakrlrRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGK 301
Cdd:PRK06334 255 ----FAYNPLYPKKiveMIDEAKVTFLGSTPvfFDYIL------KTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFP 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 302 PFGLRpsailPAYGmaeTTlavsfsECNAGLVVDevdadllaalrravpaTKGNTRRLATLGPLLQDLEARIIDEQGDVM 381
Cdd:PRK06334 325 HIQLR-----QGYG---TT------ECSPVITIN----------------TVNSPKHESCVGMPIRGMDVLIVSEETKVP 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 889038433 382 PARG-VGVIELRGESLTPGYLTMG---GFIPAQDEHgWYDTGDLGYLTEEGHVVVCGRV 436
Cdd:PRK06334 375 VSSGeTGLVLTRGTSLFSGYLGEDfgqGFVELGGET-WYVTGDLGYVDRHGELFLKGRL 432
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
108-453 |
7.39e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 80.33 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 108 EAKAVIVSEPFL-VAIPILE--QKGMQVLTV-----------ADLLASDPIGPIEvGEDDLALMQLTSGSTGSPKAV--Q 171
Cdd:PRK08276 83 GAKVLIVSAALAdTAAELAAelPAGVPLLLVvagpvpgfrsyEEALAAQPDTPIA-DETAGADMLYSSGTTGRPKGIkrP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 172 ITHRNIYSNAEAM--FVGAQYDVDKD-VMVSWLPCFHDMGMVgFLTIPMFFGAELV---KVTPMDFLRdtllwakLIDKY 245
Cdd:PRK08276 162 LPGLDPDEAPGMMlaLLGFGMYGGPDsVYLSPAPLYHTAPLR-FGMSALALGGTVVvmeKFDAEEALA-------LIERY 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 246 QGT-----------MTAAPNfayallAKRLRrqakpgdFDLSTLRFALSGAEPVePADV-EDLLDAGKPfglrpsaILPA 313
Cdd:PRK08276 234 RVThsqlvptmfvrMLKLPE------EVRAR-------YDVSSLRVAIHAAAPC-PVEVkRAMIDWWGP-------IIHE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 314 YGMAettlavsfSECNAGLVVDEVDAdllaaLRRavPATKGntrrLATLGpllqdlEARIIDEQGDVMPARGVGVIELRG 393
Cdd:PRK08276 293 YYAS--------SEGGGVTVITSEDW-----LAH--PGSVG----KAVLG------EVRILDEDGNELPPGEIGTVYFEM 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 889038433 394 ESLTPGYL-----TMGgfipAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIE 453
Cdd:PRK08276 348 DGYPFEYHndpekTAA----ARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIE 408
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
129-538 |
8.86e-16 |
|
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: 80.08 E-value: 8.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 129 GMQVLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIysnaeAMFVGAQ---YDVDKDVMVSwlpcfh 205
Cdd:cd17651 113 VTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSL-----ANLVAWQaraSSLGPGARTL------ 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 206 DMGMVGF------LTIPMFFGAELVkVTPMDFLRDTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQAKPgdfdLSTLR 279
Cdd:cd17651 182 QFAGLGFdvsvqeIFSTLCAGATLV-LPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVR----LAALR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 280 FALSGAEPVEPADVEDLLDAGKPfGLRpsaILPAYGMAETTLAVSfsecnaglvvdevdadllaalrRAVPATKGNTRRL 359
Cdd:cd17651 257 YLLTGGEQLVLTEDLREFCAGLP-GLR---LHNHYGPTETHVVTA----------------------LSLPGDPAAWPAP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 360 ATLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMGG-----FIPAQDEHG--WYDTGDLGYLTEEGHVVV 432
Cdd:cd17651 311 PPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPEltaerFVPDPFVPGarMYRTGDLARWLPDGELEF 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 433 CGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpGCAVAVRLDAGHSRESFA-VAVESNAFEDPAEVRRiehQVAHEVVAEv 511
Cdd:cd17651 391 LGRADDQVKIRGFRIELGEIEAALARHPGVR-EAVVLAREDRPGEKRLVAyVVGDPEAPVDAAELRA---ALATHLPEY- 465
|
410 420
....*....|....*....|....*..
gi 889038433 512 dVRPRNVVVLgpGTIPKTPSGKLRRAN 538
Cdd:cd17651 466 -MVPSAFVLL--DALPLTPNGKLDRRA 489
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
152-536 |
1.15e-15 |
|
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: 79.44 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELV---KVTP 228
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVlleEATP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 229 MDFLrdtllwaKLIDKYQGT-MTAAPNFAYALLAKrlrrqAKPGDFDLSTLRFALSGAEPVePADVEDLLDAGkpFGlrp 307
Cdd:cd05958 177 DLLL-------SAIARYKPTvLFTAPTAYRAMLAH-----PDAAGPDLSSLRKCVSAGEAL-PAALHRAWKEA--TG--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 308 SAILPAYGMAEttlavsfsecnaglvvdevdadllaALRRAVPATKGNTRrLATLGPLLQDLEARIIDEQGDVMPARGVG 387
Cdd:cd05958 239 IPIIDGIGSTE-------------------------MFHIFISARPGDAR-PGATGKPVPGYEAKVVDDEGNPVPDGTIG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 388 VIELRGESltpGYltMGGFIPAQDEH---GWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRP 464
Cdd:cd05958 293 RLAVRGPT---GC--RYLADKRQRTYvqgGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAE 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 889038433 465 GCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRRIEHQVAHEVVAEvdVRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd05958 368 CAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPY--KYPRAIEFV--TELPRTATGKLQR 435
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
125-536 |
1.46e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 79.59 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 125 LEQKGMQVLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvgaqydVD------KDVMV 198
Cdd:PRK07788 180 DEPSGSTDETLDDLIAGSSTAPLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGL-------LSrvpfraGETTL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 199 SWLPCFHDMGmVGFLTIPMFFGAELV---KVTPMDFLRDtllwaklIDKYQGT-MTAAPNFayallakrLRRQAK----- 269
Cdd:PRK07788 253 LPAPMFHATG-WAHLTLAMALGSTVVlrrRFDPEATLED-------IAKHKATaLVVVPVM--------LSRILDlgpev 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 270 PGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpFGlrpSAILPAYGMAETTLAVSFSEcnaglvvdevdADLLAAlrrav 349
Cdd:PRK07788 317 LAKYDTSSLKIIFVSGSALSPELATRALEA---FG---PVLYNLYGSTEVAFATIATP-----------EDLAEA----- 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 350 PATKGNTRRLATLgpllqdleaRIIDEQGDVMPARGVGVIELRGESLTPGYlTMGGfiPAQDEHGWYDTGDLGYLTEEGH 429
Cdd:PRK07788 375 PGTVGRPPKGVTV---------KILDENGNEVPRGVVGRIFVGNGFPFEGY-TDGR--DKQIIDGLLSSGDVGYFDEDGL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 430 VVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRRI--EHQVAHEV 507
Cdd:PRK07788 443 LFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYvrDNLARYKV 522
|
410 420 430
....*....|....*....|....*....|
gi 889038433 508 vaevdvrPRNVVVLgpGTIPKTPSGK-LRR 536
Cdd:PRK07788 523 -------PRDVVFL--DELPRNPTGKvLKR 543
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
152-537 |
1.61e-15 |
|
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: 78.95 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAmfVGAQYDVD-KDVMVSWLPCFHDMGMVGFLTiPMFFGAELVkvtpmd 230
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA--TAERYGLTpGDRELQFASFNFDGAHEQLLP-PLICGACVV------ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 fLRDTLLW------AKLIDKYQGTMTAAPNFAYALLAKRLRRQakpGDFDLSTLRFALSGAEPVepaDVEDLLDAGKPfg 304
Cdd:cd17649 165 -LRPDELWasadelAEMVRELGVTVLDLPPAYLQQLAEEADRT---GDGRPPSLRLYIFGGEAL---SPELLRRWLKA-- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 305 lrPSAILPAYGMAETTLAVSFSECNAGLvvdevdadllaalRRAVPAtkgntrrlATLGPLLQDLEARIIDEQGDVMPAR 384
Cdd:cd17649 236 --PVRLFNAYGPTEATVTPLVWKCEAGA-------------ARAGAS--------MPIGRPLGGRSAYILDADLNPVPVG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 385 GVGVIELRGESLTPGY-----LTMGGFIPaqDEHG-----WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIER 454
Cdd:cd17649 293 VTGELYIGGEGLARGYlgrpeLTAERFVP--DPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 455 AAGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAF-EDPAEVRR--IEHQVAHEVvaevdvrPRNVVVLgpGTIPKTPS 531
Cdd:cd17649 371 ALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQpELRAQLRTalRASLPDYMV-------PAHLVFL--ARLPLTPN 441
|
....*.
gi 889038433 532 GKLRRA 537
Cdd:cd17649 442 GKLDRK 447
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
129-536 |
2.39e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 78.87 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 129 GMQVLTVADLLASDPIGPIEVGeDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFvgAQYDVDKDV-MVSWLPCFHDM 207
Cdd:PRK06188 146 GVDLLAAAAKFGPAPLVAAALP-PDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQL--AEWEWPADPrFLMCTPLSHAG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 208 GMvgFLTIPMFFGAELV---KVTPMDFLRdtllwakLIDKYQGTMT-AAPNFAYALL-AKRLRRQakpgdfDLSTLRFAL 282
Cdd:PRK06188 223 GA--FFLPTLLRGGTVIvlaKFDPAEVLR-------AIEEQRITATfLVPTMIYALLdHPDLRTR------DLSSLETVY 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 283 SGAEPVEPADvedLLDAGKPFGlrpSAILPAYGMAETTLAVSfsecnaglVVDEVDADLlaalrravpatkGNTRRLATL 362
Cdd:PRK06188 288 YGASPMSPVR---LAEAIERFG---PIFAQYYGQTEAPMVIT--------YLRKRDHDP------------DDPKRLTSC 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 363 GPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMggfiPAQDE----HGWYDTGDLGYLTEEGHVVVCGRVKD 438
Cdd:PRK06188 342 GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNR----PEETAeafrDGWLHTGDVAREDEDGFYYIVDRKKD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 439 VIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDA-GHSRESFAVAvESNAFEDPAEVrrIEHQVAHEVVAEVdvrPRN 517
Cdd:PRK06188 418 MIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEAVTAVVVL-RPGAAVDAAEL--QAHVKERKGSVHA---PKQ 491
|
410
....*....|....*....
gi 889038433 518 VVVLgpGTIPKTPSGKLRR 536
Cdd:PRK06188 492 VDFV--DSLPLTALGKPDK 508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
147-536 |
2.97e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 79.62 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 147 IEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSWLPCFhDMGMVGFLtIPMFFGAELVkV 226
Cdd:PRK12316 650 TELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSF-DVSVWEFF-WPLMSGARLV-V 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 227 TPMDFLRDTLLWAKLIDKYQ-GTMTAAPNFAYALLakrlrrqAKPGDFDLSTLRFALSGAEPVEPADVEDLldagkpFGL 305
Cdd:PRK12316 727 AAPGDHRDPAKLVELINREGvDTLHFVPSMLQAFL-------QDEDVASCTSLRRIVCSGEALPADAQEQV------FAK 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 306 RPSA-ILPAYGMAETTLAVSFSECnaglvVDEVdadllaalRRAVPatkgntrrlatLGPLLQDLEARIIDEQGDVMPAR 384
Cdd:PRK12316 794 LPQAgLYNLYGPTEAAIDVTHWTC-----VEEG--------GDSVP-----------IGRPIANLACYILDANLEPVPVG 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 385 GVGVIELRGESLTPGY-----LTMGGFIPAQDEHG--WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAG 457
Cdd:PRK12316 850 VLGELYLAGRGLARGYhgrpgLTAERFVPSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLL 929
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 889038433 458 RVDGVRPGCAVAVrldAGHSRESFAVAvesnafEDPAEVRRIEHQVAHEVVAEVDVRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:PRK12316 930 EHPWVREAAVLAV---DGKQLVGYVVL------ESEGGDWREALKAHLAASLPEYMVPAQWLAL--ERLPLTPNGKLDR 997
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
157-468 |
4.59e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 77.82 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 157 MQLTSGSTGSPKAVQithRNIYSNAEAMFVGaqydvDKDVMVSWLPcfhdMGMVGFLTIPMF-------------FGAEL 223
Cdd:PRK12406 157 MIYTSGTTGHPKGVR---RAAPTPEQAAAAE-----QMRALIYGLK----PGIRALLTGPLYhsapnayglragrLGGVL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 224 V---KVTPMDFLrdtllwaKLIDKYQ-GTMTAAPNFAYALLAKRLRRQAKpgdFDLSTLRFALSGAEPVePADV-EDLLD 298
Cdd:PRK12406 225 VlqpRFDPEELL-------QLIERHRiTHMHMVPTMFIRLLKLPEEVRAK---YDVSSLRHVIHAAAPC-PADVkRAMIE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 299 AGKPfglrpsAILPAYGMAETtlavsfsecnaGLVVDEVDADLLaalrravpatkgntRRLATLGPLLQDLEARIIDEQG 378
Cdd:PRK12406 294 WWGP------VIYEYYGSTES-----------GAVTFATSEDAL--------------SHPGTVGKAAPGAELRFVDEDG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 379 DVMPARGVGVIELRGESLTP-GYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAG 457
Cdd:PRK12406 343 RPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLH 422
|
330
....*....|.
gi 889038433 458 RVDGVRpGCAV 468
Cdd:PRK12406 423 AVPGVH-DCAV 432
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
91-536 |
6.07e-15 |
|
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: 77.51 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 91 TDLAVWAEDTMTV----------IGMI----EAKAVIV--------------SEPFLVAIPILEQKGMQvLTVADLLASD 142
Cdd:cd05932 47 TDLAIWMAGHISVplyptlnpdtIRYVlehsESKALFVgklddwkamapgvpEGLISISLPPPSAANCQ-YQWDDLIAQH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 143 P--IGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMF--VGAQYDvdkDVMVSWLPCFH-------DMGMV- 210
Cdd:cd05932 126 PplEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIehIGTEEN---DRMLSYLPLAHvtervfvEGGSLy 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 211 -GFLTipMF------FGAELVKVTPMDFLRDTLLWAKLidkYQGTMTAAPNFAYALLAK-----RLRRQAKPGDFDLSTL 278
Cdd:cd05932 203 gGVLV--AFaesldtFVEDVQRARPTLFFSVPRLWTKF---QQGVQDKIPQQKLNLLLKipvvnSLVKRKVLKGLGLDQC 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 279 RFALSGAEPVEPAdvedLLDAGKPFGLRpsaILPAYGMAETtLAVSFsecnaglvvdevdadllaalrravpATKGNTRR 358
Cdd:cd05932 278 RLAGCGSAPVPPA----LLEWYRSLGLN---ILEAYGMTEN-FAYSH-------------------------LNYPGRDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 359 LATLGPLLQDLEARIiDEQGDVMpargvgvieLRGESLTPGYL-----TMGGFipaqDEHGWYDTGDLGYLTEEGHVVVC 433
Cdd:cd05932 325 IGTVGNAGPGVEVRI-SEDGEIL---------VRSPALMMGYYkdpeaTAEAF----TADGFLRTGDKGELDADGNLTIT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 434 GRVKDVIIMA-GRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHS---RESFAVAVESNAFEdpAEVRRIEHQVAHEVVA 509
Cdd:cd05932 391 GRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLAlvvLSEEARLRADAFAR--AELEASLRAHLARVNS 468
|
490 500 510
....*....|....*....|....*....|...
gi 889038433 510 EVDVRPR---NVVVLGPGTIPK---TPSGKLRR 536
Cdd:cd05932 469 TLDSHEQlagIVVVKDPWSIDNgilTPTLKIKR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
133-538 |
6.69e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.46 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 133 LTVADLLASDPIG--PIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVD-KDVMVSWLPCFHDMGM 209
Cdd:PRK12316 2125 LDRDAEWADYPDTapAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAA--GERYELSpADCELQFMSFSFDGAH 2202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 210 VGFLTiPMFFGAELVkvtpmdfLRDTLLW-----AKLIDKYQGTMTAAPNFAYALLAKRLRRQAKPgdfdlSTLRFALSG 284
Cdd:PRK12316 2203 EQWFH-PLLNGARVL-------IRDDELWdpeqlYDEMERHGVTILDFPPVYLQQLAEHAERDGRP-----PAVRVYCFG 2269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 285 AEPVEPADVEDLLDAgkpfgLRPSAILPAYGMAETTLAVSFSECnaglvvdevdadllaalRRAVPATKGNtrrlATLGP 364
Cdd:PRK12316 2270 GEAVPAASLRLAWEA-----LRPVYLFNGYGPTEAVVTPLLWKC-----------------RPQDPCGAAY----VPIGR 2323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 365 LLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIPAQDEHG---WYDTGDLGYLTEEGHVVVCGRV 436
Cdd:PRK12316 2324 ALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYlnrpgLTAERFVPDPFSASgerLYRTGDLARYRADGVVEYLGRI 2403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 437 KDVIIMAGRNIYPTDIERAAGRVDGVRPgcAVAVRLDAGHSRESFAVAVEsnafEDPAEVRRIEHQVAHEVVAEVDVRPR 516
Cdd:PRK12316 2404 DHQVKIRGFRIELGEIEARLQAHPAVRE--AVVVAQDGASGKQLVAYVVP----DDAAEDLLAELRAWLAARLPAYMVPA 2477
|
410 420
....*....|....*....|..
gi 889038433 517 NVVVLgpGTIPKTPSGKLRRAN 538
Cdd:PRK12316 2478 HWVVL--ERLPLNPNGKLDRKA 2497
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
92-536 |
8.14e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 76.86 E-value: 8.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 92 DLAVWAEDTMTVIGMIEAKAVIVSEPFLvaipiLEQKGMQVLTVADLLASDPIGPIE-----VGEDDLALMQLTSGSTGS 166
Cdd:PRK04813 83 DVSSPAERIEMIIEVAKPSLIIATEELP-----LEILGIPVITLDELKDIFATGNPYdfdhaVKGDDNYYIIFTSGTTGK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 167 PKAVQITHRNIYSNAEAM-----------FVG-AQYDVDKDVMvSWLPCfhdmgmvgfLTIpmffGAELVKVtPMDFLRD 234
Cdd:PRK04813 158 PKGVQISHDNLVSFTNWMledfalpegpqFLNqAPYSFDLSVM-DLYPT---------LAS----GGTLVAL-PKDMTAN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 235 -TLLWAKLIDKYQGTMTAAPNFA-YALLAKrlrrqakpgDFDLSTL----RFALSGAE-PVEPAdvEDLLDAgkpFglrP 307
Cdd:PRK04813 223 fKQLFETLPQLPINVWVSTPSFAdMCLLDP---------SFNEEHLpnltHFLFCGEElPHKTA--KKLLER---F---P 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 308 SA-ILPAYGMAETTLAVSfsecnaGLvvdEVDADLLAALRRaVPAtkGNTRrlatlgpllQDLEARIIDEQGDVMPARGV 386
Cdd:PRK04813 286 SAtIYNTYGPTEATVAVT------SI---EITDEMLDQYKR-LPI--GYAK---------PDSPLLIIDEEGTKLPDGEQ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 387 GVIELRGESLTPGYL-----TMGGFIpAQDEHGWYDTGDLGYLtEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDG 461
Cdd:PRK04813 345 GEIVISGPSVSKGYLnnpekTAEAFF-TFDGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSY 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 462 VRPgcAVAVRLDAGHSRESFAVAVESNA--FEDpaevrriEHQVAHEVVAEVDVR------PRNVVVLgpGTIPKTPSGK 533
Cdd:PRK04813 423 VES--AVVVPYNKDHKVQYLIAYVVPKEedFER-------EFELTKAIKKELKERlmeymiPRKFIYR--DSLPLTPNGK 491
|
...
gi 889038433 534 LRR 536
Cdd:PRK04813 492 IDR 494
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
152-440 |
8.31e-15 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 76.87 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVG-AQYDVDKDVMVSWLPCFHDM------------GMVGF-----L 213
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRvPELLGPDDRYLAYLPLAHIFelaaenvclyrgGTIGYgsprtL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 214 TIPMFFG-------------------------AELVKVTPMDFLRDTLLW------AKLIDKYQGTMtaapnFAYALLAK 262
Cdd:cd17639 168 TDKSKRGckgdltefkptlmvgvpaiwdtirkGVLAKLNPMGGLKRTLFWtayqskLKALKEGPGTP-----LLDELVFK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 263 RLrRQAKPGDfdlstLRFALSGAEPVEPADVEDLLDAGKPfglrpsaILPAYGMAETtlavsfseCNAGLVVDEvdADLl 342
Cdd:cd17639 243 KV-RAALGGR-----LRYMLSGGAPLSADTQEFLNIVLCP-------VIQGYGLTET--------CAGGTVQDP--GDL- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 343 aalrravpatkgntrRLATLGPLLQDLEARIID--EQG---DVMPARgvGVIELRGESLTPGY-----LTMGGFipaqDE 412
Cdd:cd17639 299 ---------------ETGRVGPPLPCCEIKLVDweEGGystDKPPPR--GEILIRGPNVFKGYyknpeKTKEAF----DG 357
|
330 340
....*....|....*....|....*...
gi 889038433 413 HGWYDTGDLGYLTEEGHVVVCGRVKDVI 440
Cdd:cd17639 358 DGWFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
152-453 |
8.96e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 77.15 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRN--IYSNAEAMFVGaqYDVDkDVMVSWLPCFH--------DMGMVG--FLTIPMFf 219
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSAliVQSLAKIAIVG--YGED-DVYLHTAPLCHigglssalAMLMVGacHVLLPKF- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 220 gaelvkvtpmdflrDTLLWAKLIDKYQGT-MTAAPnfayALLAKRLRRQAKPGDFDL-STLRFALSGAEPVePADVedLL 297
Cdd:PLN02860 248 --------------DAKAALQAIKQHNVTsMITVP----AMMADLISLTRKSMTWKVfPSVRKILNGGGSL-SSRL--LP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 298 DAGKPFglrPSA-ILPAYGMAETTLAVSFsecnaglvvdevdadllaaLRRAVPatkgntrrlaTLGPLLQDLEARIIDE 376
Cdd:PLN02860 307 DAKKLF---PNAkLFSAYGMTEACSSLTF-------------------MTLHDP----------TLESPKQTLQTVNQTK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 377 QGDVMPARGVGV------IELR---------GESLTPGYLTMGGF---IPAQDE----HGWYDTGDLGYLTEEGHVVVCG 434
Cdd:PLN02860 355 SSSVHQPQGVCVgkpaphVELKigldessrvGRILTRGPHVMLGYwgqNSETASvlsnDGWLDTGDIGWIDKAGNLWLIG 434
|
330
....*....|....*....
gi 889038433 435 RVKDVIIMAGRNIYPTDIE 453
Cdd:PLN02860 435 RSNDRIKTGGENVYPEEVE 453
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
126-497 |
1.14e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 76.45 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 126 EQKGMQVLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAE---AMFVGAQYDvdkdvmvSWL- 201
Cdd:PRK09029 109 GENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEgvlSLMPFTAQD-------SWLl 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 202 --PCFHDMGMvGFLTIPMFFGAELVkvtpmdfLRDTllwAKLIDKYQGTMTAApnfayaLLAKRLRRQAKPGDFDLSTLR 279
Cdd:PRK09029 182 slPLFHVSGQ-GIVWRWLYAGATLV-------VRDK---QPLEQALAGCTHAS------LVPTQLWRLLDNRSEPLSLKA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 280 FALSGAE-PVEpadvedLLDAGKPFGLRPSAilpAYGMAE---TTLAVsfsecnaglvvdEVDAdllaalrravpatkgn 355
Cdd:PRK09029 245 VLLGGAAiPVE------LTEQAEQQGIRCWC---GYGLTEmasTVCAK------------RADG---------------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 356 trrLATLGPLLQDLEARIIDEQgdvmpargvgvIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLtEEGHVVVCGR 435
Cdd:PRK09029 288 ---LAGVGSPLPGREVKLVDGE-----------IWLRGASLALGYWRQGQLVPLVNDEGWFATRDRGEW-QNGELTILGR 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 889038433 436 VKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRlDA--GHsResfAVAV-ESNAFEDPAEVR 497
Cdd:PRK09029 353 LDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVA-DAefGQ-R---PVAVvESDSEAAVVNLA 412
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
146-536 |
2.06e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 76.74 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 146 PIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDkDVMVSWLPCFHDMGMVGFLTiPMFFGAELVk 225
Cdd:PRK12467 650 EVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAAD-DSMLMVSTFAFDLGVTELFG-ALASGATLH- 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 226 VTPMDFLRDTLLWAKLIDKYQ-GTMTAAPNFAYALLakRLRRQAKPgdfdlSTLRFALSGAEPVEPADVEdlldagKPFG 304
Cdd:PRK12467 727 LLPPDCARDAEAFAALMADQGvTVLKIVPSHLQALL--QASRVALP-----RPQRALVCGGEALQVDLLA------RVRA 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 305 LRPSA-ILPAYGMAETTLAVSFSECNaglvvdevdadLLAALRRAVPatkgntrrlatLGPLLQDLEARIIDEQGDVMPA 383
Cdd:PRK12467 794 LGPGArLINHYGPTETTVGVSTYELS-----------DEERDFGNVP-----------IGQPLANLGLYILDHYLNPVPV 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 384 RGVGVIELRGESLTPGYLTMGG-----FIP---AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERA 455
Cdd:PRK12467 852 GVVGELYIGGAGLARGYHRRPAltaerFVPdpfGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEAR 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 456 AGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRRIEHQVAHEVVAEVDVrPRNVVVLgpGTIPKTPSGKLR 535
Cdd:PRK12467 932 LLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQATRDELKAQLRQVLPDYMV-PAHLLLL--DSLPLTPNGKLD 1008
|
.
gi 889038433 536 R 536
Cdd:PRK12467 1009 R 1009
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
160-455 |
2.54e-14 |
|
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: 74.23 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 160 TSGSTGSPKAVQITHRN-IYSNAEAMFVgaqYDVDK-DVMVSWLPCFHDMGMVGFLTIPMFFGAELVkvtpMD-FlrDTL 236
Cdd:cd17637 8 TAAVAGRPRGAVLSHGNlIAANLQLIHA---MGLTEaDVYLNMLPLFHIAGLNLALATFHAGGANVV----MEkF--DPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 237 LWAKLIDKYQGT-MTAAPNFAYALLAkrlrrQAKPGDFDLSTLRfALSGAEpvEPADVEDLLdagkpfGLRPSAILPAYG 315
Cdd:cd17637 79 EALELIEEEKVTlMGSFPPILSNLLD-----AAEKSGVDLSSLR-HVLGLD--APETIQRFE------ETTGATFWSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 316 MAETTLAVSFSECnaglvvdevdadllaalrRAVPATKGNTRRLATLgpllqdleaRIIDEQGDVMPARGVGVIELRGES 395
Cdd:cd17637 145 QTETSGLVTLSPY------------------RERPGSAGRPGPLVRV---------RIVDDNDRPVPAGETGEIVVRGPL 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 889038433 396 LTPGYLTMggfiPAQDEH----GWYDTGDLGYLTEEGHVVVCGRV--KDVIIMAGRNIYPTDIERA 455
Cdd:cd17637 198 VFQGYWNL----PELTAYtfrnGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKV 259
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
143-537 |
2.58e-14 |
|
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: 75.61 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 143 PIGPIEVGEDDLALMQLTSGSTGSPKAVQitHRNIYSNAEamFVGAQY--DVDKDVM------VSWLPCfhdmgMVGFLT 214
Cdd:cd05970 176 PTANSYPCGEDILLVYFSSGTTGMPKMVE--HDFTYPLGH--IVTAKYwqNVREGGLhltvadTGWGKA-----VWGKIY 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 215 IPMFFGAElVKVTPMD-FLRDTLLwaKLIDKYQGTMTAAPNFAYALLAKrlrrqAKPGDFDLSTLRFALSGAEPVEPADV 293
Cdd:cd05970 247 GQWIAGAA-VFVYDYDkFDPKALL--EKLSKYGVTTFCAPPTIYRFLIR-----EDLSRYDLSSLRYCTTAGEALNPEVF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 294 EDLLDAGkpfGLRpsaILPAYGMAETTLAVSFSECnaglvvdevdadllaalRRAVPATKGNtrrlatlgPLLQdLEARI 373
Cdd:cd05970 319 NTFKEKT---GIK---LMEGFGQTETTLTIATFPW-----------------MEPKPGSMGK--------PAPG-YEIDL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 374 IDEQGDVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEH-----GWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIY 448
Cdd:cd05970 367 IDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEKTAevwhdGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIG 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 449 PTDIERAAGRVDGVRPgCAVAVRLDAGHSRESFAVAVESNAFEdPAEVRRIEHQVAHEVVAEVDVRPRNVVVLgpGTIPK 528
Cdd:cd05970 447 PFEVESALIQHPAVLE-CAVTGVPDPIRGQVVKATIVLAKGYE-PSEELKKELQDHVKKVTAPYKYPRIVEFV--DELPK 522
|
....*....
gi 889038433 529 TPSGKLRRA 537
Cdd:cd05970 523 TISGKIRRV 531
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
143-537 |
3.26e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 75.04 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 143 PIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYS-----NAEAMfvgAQYD-VDKDVMVSWLPCFHDMGMVGFLTIP 216
Cdd:PRK05857 160 LAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpdilQKEGL---NWVTwVVGETTYSPLPATHIGGLWWILTCL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 217 MFFGAELVKVTPMDFLRDTLlwaklIDKYQGTMTAAPNfayalLAKRLRRQAKPGDFDLSTLRFALSGAEPVEPADVEdL 296
Cdd:PRK05857 237 MHGGLCVTGGENTTSLLEIL-----TTNAVATTCLVPT-----LLSKLVSELKSANATVPSLRLVGYGGSRAIAADVR-F 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 297 LDAGkpfGLRPSAIlpaYGMAETTlavsfseCNAglvvdevdadllaalrRAVPATKGNTRRL--ATLGPLLQDLEARII 374
Cdd:PRK05857 306 IEAT---GVRTAQV---YGLSETG-------CTA----------------LCLPTDDGSIVKIeaGAVGRPYPGVDVYLA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 375 DEQG------DVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIY 448
Cdd:PRK05857 357 ATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 449 PTDIERAAGRVDGVRPgcAVAVRLDAGHSRESFAVAVESNAFEDPAEVRRIEHQVA--HEVVAEVDVRPRNVVVLgpGTI 526
Cdd:PRK05857 437 PDEVDRIAEGVSGVRE--AACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAarFRRESEPMARPSTIVIV--TDI 512
|
410
....*....|.
gi 889038433 527 PKTPSGKLRRA 537
Cdd:PRK05857 513 PRTQSGKVMRA 523
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
136-537 |
3.41e-14 |
|
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: 75.43 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 136 ADLLAS-DPIGPIEVGEDDLALMQLTSGSTGSPKAVQithRNI--YSNAEAMFVGAQYDVdKDVMVSWlpCFHDMG-MVG 211
Cdd:cd05967 213 SELLAKaEPVDCVPVAATDPLYILYTSGTTGKPKGVV---RDNggHAVALNWSMRNIYGI-KPGDVWW--AASDVGwVVG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 212 FLTI---PMFFGAELV------KVTPmdflrDTLLWAKLIDKYQGT-MTAAPNfayallAKRLRRQAKPG-----DFDLS 276
Cdd:cd05967 287 HSYIvygPLLHGATTVlyegkpVGTP-----DPGAFWRVIEKYQVNaLFTAPT------AIRAIRKEDPDgkyikKYDLS 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 277 TLR-FALSGaepvEPADVEDLLDAGKPFGlRPsaILPAYGMAETTLAVSfseCNA-GLVvdevdadllaalRRAVPAtkg 354
Cdd:cd05967 356 SLRtLFLAG----ERLDPPTLEWAENTLG-VP--VIDHWWQTETGWPIT---ANPvGLE------------PLPIKA--- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 355 ntrrlATLGPLLQDLEARIIDEQGDVMPARGVGVIELRGeSLTPGYLTM-----GGFIPA--QDEHGWYDTGDLGYLTEE 427
Cdd:cd05967 411 -----GSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTlwkndERFKKLylSKFPGYYDTGDAGYKDED 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 428 GHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPgCAVAVRLDA--GHSRESFAVAVESnafedpaeVRRIEHQVAH 505
Cdd:cd05967 485 GYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE-CAVVGVRDElkGQVPLGLVVLKEG--------VKITAEELEK 555
|
410 420 430
....*....|....*....|....*....|....*....
gi 889038433 506 EVVAEVD------VRPRNVVVLgpGTIPKTPSGK-LRRA 537
Cdd:cd05967 556 ELVALVReqigpvAAFRLVIFV--KRLPKTRSGKiLRRT 592
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
103-453 |
5.76e-14 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 74.33 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 103 VIGMIEAKAVIVSEPFLVAIPILEQKGMQVLTvaDLLASDPIGPIEVG----------------------EDDLALMQLT 160
Cdd:PRK08008 104 ILQNSQASLLVTSAQFYPMYRQIQQEDATPLR--HICLTRVALPADDGvssftqlkaqqpatlcyapplsTDDTAEILFT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 161 SGSTGSPKAVQITHRNI-----YSNAEAMFVgaqydvDKDVMVSWLPCFHdmgmVGF---LTIPMF-FGAELVKVTPMDF 231
Cdd:PRK08008 182 SGTTSRPKGVVITHYNLrfagyYSAWQCALR------DDDVYLTVMPAFH----IDCqctAAMAAFsAGATFVLLEKYSA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 LRdtlLWaKLIDKYQGTMTAApnfaYALLAKRLRRQ-AKPGDFD--LSTLRFALsgaepvePADVEDLLDAGKPFGLRps 308
Cdd:PRK08008 252 RA---FW-GQVCKYRATITEC----IPMMIRTLMVQpPSANDRQhcLREVMFYL-------NLSDQEKDAFEERFGVR-- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 309 aILPAYGMAETTLavsfsecnaGLVVDevdadllaalrravpaTKGNTRRLATLGPLLQDLEARIIDEQGDVMPARGVGV 388
Cdd:PRK08008 315 -LLTSYGMTETIV---------GIIGD----------------RPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGE 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 889038433 389 IELRGEsltPGYLTMGGFI-------PAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIE 453
Cdd:PRK08008 369 ICIKGV---PGKTIFKEYYldpkataKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELE 437
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
356-537 |
7.07e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 74.05 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 356 TRRLATLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGR 435
Cdd:PRK07638 303 ERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGR 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 436 VKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHSResfAVAVesnaFEDPAEVRRIEHQVAHEVVAEvdVRP 515
Cdd:PRK07638 383 EKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEK---PVAI----IKGSATKQQLKSFCLQRLSSF--KIP 453
|
170 180
....*....|....*....|..
gi 889038433 516 RNVVVLgpGTIPKTPSGKLRRA 537
Cdd:PRK07638 454 KEWHFV--DEIPYTNSGKIARM 473
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
132-536 |
8.39e-14 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 73.26 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 132 VLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHR--NIYSNAEAMFVGAQYDVDKDVMVSwlpCF-HDMG 208
Cdd:COG1541 63 FTTKEDLRDNYPFGLFAVPLEEIVRIHASSGTTGKPTVVGYTRKdlDRWAELFARSLRAAGVRPGDRVQN---AFgYGLF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 209 MVGFLtipMFFGAELV--KVTPMDFLRDTLLWaKLIDKYQGT-MTAAPNFAYaLLAKRLRRQAKpgDFDLSTLRFALSGA 285
Cdd:COG1541 140 TGGLG---LHYGAERLgaTVIPAGGGNTERQL-RLMQDFGPTvLVGTPSYLL-YLAEVAEEEGI--DPRDLSLKKGIFGG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 286 EPVEPA---DVEDLLDAgkpfglrpsAILPAYGMAETTLAVSF-SECNAGLVVDEvdADLLaalrravpatkgntrrlat 361
Cdd:COG1541 213 EPWSEEmrkEIEERWGI---------KAYDIYGLTEVGPGVAYeCEAQDGLHIWE--DHFL------------------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 362 lgpllqdLEarIID-EQGDVMPARGVGviELrgeSLTPgyLTMGGF--IPaqdehgwYDTGDLGYLTEE----------- 427
Cdd:COG1541 263 -------VE--IIDpETGEPVPEGEEG--EL---VVTT--LTKEAMplIR-------YRTGDLTRLLPEpcpcgrthpri 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 428 GHVVvcGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPgCAVAVrLDAGHSRESFAVAVESnafEDPAEVRRIEHQVAHEV 507
Cdd:COG1541 320 GRIL--GRADDMLIIRGVNVFPSQIEEVLLRIPEVGP-EYQIV-VDREGGLDELTVRVEL---APGASLEALAEAIAAAL 392
|
410 420
....*....|....*....|....*....
gi 889038433 508 VAEVDVRPRnVVVLGPGTIPKTPsGKLRR 536
Cdd:COG1541 393 KAVLGLRAE-VELVEPGSLPRSE-GKAKR 419
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
151-536 |
9.60e-14 |
|
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: 73.32 E-value: 9.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLALMQLTSGSTGSPKAVQITHRNIysnaeAMFVGAQ-YDVD-KDVMVSWlpCFHDMGMVgfltipmfFGAELVKVTP 228
Cdd:cd05973 87 DSDPFVMMFTSGTTGLPKGVPVPLRAL-----AAFGAYLrDAVDlRPEDSFW--NAADPGWA--------YGLYYAITGP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 229 MDFLRDTLLWA---------KLIDKYQGT-MTAAPNFAYALLAKRLRRQAKPGdfdlSTLRFALSGAEPVEPaDVEDLLD 298
Cdd:cd05973 152 LALGHPTILLEggfsvestwRVIERLGVTnLAGSPTAYRLLMAAGAEVPARPK----GRLRRVSSAGEPLTP-EVIRWFD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 299 AGkpFGLrpsAILPAYGMAETTLAVsfseCNAGLVVDEVDAdllAALRRAVPATKGNtrrlatlgpllqdlearIIDEQG 378
Cdd:cd05973 227 AA--LGV---PIHDHYGQTELGMVL----ANHHALEHPVHA---GSAGRAMPGWRVA-----------------VLDDDG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 379 DVMPARGVGV--IELRGESLT--PGYLTMGgfIPAQDEHgWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIER 454
Cdd:cd05973 278 DELGPGEPGRlaIDIANSPLMwfRGYQLPD--TPAIDGG-YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVES 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 455 AAGRVDGVRPgCAVAVRLDAGHSRESFAVAVESNAFE-DPAEVRRIEHQVAHEVVAEvdVRPRNVVVLgpGTIPKTPSGK 533
Cdd:cd05973 355 ALIEHPAVAE-AAVIGVPDPERTEVVKAFVVLRGGHEgTPALADELQLHVKKRLSAH--AYPRTIHFV--DELPKTPSGK 429
|
...
gi 889038433 534 LRR 536
Cdd:cd05973 430 IQR 432
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
129-536 |
2.09e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.45 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 129 GMQVLTV--ADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVDKDVMVSWLPCFHD 206
Cdd:PRK12316 3171 GVQVLDLdrGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWM--QQAYGLGVGDRVLQFTTFSF 3248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 207 MGMVGFLTIPMFFGAELVKVTPMDFLRDTLLWAKLIDKYQGTMTAAPNFAYALLakrlrrqAKPGDFDLSTLRFALSGAE 286
Cdd:PRK12316 3249 DVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL-------EEEDAHRCTSLKRIVCGGE 3321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 287 PVePADVEDLLDAGKPfglrpsaILPAYGMAETTLAVSFSECNAglvvdevdadllaalrravpatkgNTRRLATLGPLL 366
Cdd:PRK12316 3322 AL-PADLQQQVFAGLP-------LYNLYGPTEATITVTHWQCVE------------------------EGKDAVPIGRPI 3369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 367 QDLEARIIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIPAQDEHG--WYDTGDLGYLTEEGHVVVCGRVKDV 439
Cdd:PRK12316 3370 ANRACYILDGSLEPVPVGALGELYLGGEGLARGYhnrpgLTAERFVPDPFVPGerLYRTGDLARYRADGVIEYIGRVDHQ 3449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 440 IIMAGRNIYPTDIERAAGRVDGVRPGCAVAVrldagHSRESFAVAVESnafEDPAEVRRIEHQVAHEVVAEVDVrPRNVV 519
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLAV-----DGRQLVAYVVPE---DEAGDLREALKAHLKASLPEYMV-PAHLL 3520
|
410
....*....|....*..
gi 889038433 520 VLgpGTIPKTPSGKLRR 536
Cdd:PRK12316 3521 FL--ERMPLTPNGKLDR 3535
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
354-462 |
2.57e-13 |
|
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: 70.90 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 354 GNTRRLATLGPLLQDLEARIIDEQGDvmparGVGVIELRGESLTPGYLTMGGFipaqDEHGWYDTGDLGYLTEEGHVVVC 433
Cdd:cd17633 157 QESRPPNSVGRPFPNVEIEIRNADGG-----EIGKIFVKSEMVFSGYVRGGFS----NPDGWMSVGDIGYVDEEGYLYLV 227
|
90 100
....*....|....*....|....*....
gi 889038433 434 GRVKDVIIMAGRNIYPTDIERAAGRVDGV 462
Cdd:cd17633 228 GRESDMIIIGGINIFPTEIESVLKAIPGI 256
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
151-456 |
2.82e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 72.09 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLALMQLTSGSTGSPKAVQITHR-NIYSNAEAMFVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFfGAELVkvtpM 229
Cdd:PRK06018 176 ENTAAGMCYTSGTTGDPKGVLYSHRsNVLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSM-GTKLV----M 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 230 DFLR-DTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQakpgDFDLSTLRFALSGAEPVEPADVEDLLDAGkpfglrpS 308
Cdd:PRK06018 251 PGAKlDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKE----GLKLPHLKMVVCGGSAMPRSMIKAFEDMG-------V 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 309 AILPAYGMAETTLAVSFSECNAGLVVDEVDADLLAALRRAVPatkgntrrlatlgPLLqdLEARIIDEQGDVMPARG--V 386
Cdd:PRK06018 320 EVRHAWGMTEMSPLGTLAALKPPFSKLPGDARLDVLQKQGYP-------------PFG--VEMKITDDAGKELPWDGktF 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 387 GVIELRGESLTPGYLTMGGFIpaQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAA 456
Cdd:PRK06018 385 GRLKVRGPAVAAAYYRVDGEI--LDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLA 452
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
150-536 |
4.45e-13 |
|
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: 71.31 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 150 GEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeamfVGAQYDVD---KDVMVSWLPCfhDMGMVGFL---TIP-MFFGAE 222
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLLGHL----PGVQFPFNlfpRDGDLYWTPA--DWAWIGGLldvLLPsLYFGVP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 223 LVKVTPMDFLRDTLLwaKLIDKYQGTMTAAPnfAYALlaKRLRRQAKPGDFDLSTLRFALSGAEPvepADVEDLLDAGKP 302
Cdd:cd05971 160 VLAHRMTKFDPKAAL--DLMSRYGVTTAFLP--PTAL--KMMRQQGEQLKHAQVKLRAIATGGES---LGEELLGWAREQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 303 FGLrpsAILPAYGMAETTLAVSfsECNAGLVVDEvdadllAALRRAVPATKgntrrlatlgpllqdleARIIDEQGDVMP 382
Cdd:cd05971 231 FGV---EVNEFYGQTECNLVIG--NCSALFPIKP------GSMGKPIPGHR-----------------VAIVDDNGTPLP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 383 ARGVGVIELRgeslTPGYLTMGGFI--PAQDEH----GWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIER-- 454
Cdd:cd05971 283 PGEVGEIAVE----LPDPVAFLGYWnnPSATEKkmagDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEEcl 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 455 ----------AAGRVDGVRPGCAVA-VRLDAGHSrESFAVAVESNAFedpaeVRRIEHqvAHEvvaevdvRPRNVVVlgP 523
Cdd:cd05971 359 lkhpavlmaaVVGIPDPIRGEIVKAfVVLNPGET-PSDALAREIQEL-----VKTRLA--AHE-------YPREIEF--V 421
|
410
....*....|...
gi 889038433 524 GTIPKTPSGKLRR 536
Cdd:cd05971 422 NELPRTATGKIRR 434
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
139-534 |
1.11e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 139 LASDPIGpievgeddlALMQLTSGSTGSPKAVQ--ITHRNIYSNAEAM--FVGAQYDV-DKDVMVSWLPCFHDM-----G 208
Cdd:PRK13390 144 LTEQPCG---------AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIvaIARAFYDIsESDIYYSSAPIYHAAplrwcS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 209 MVGFLtipmffGAELVKVTPMDfLRDTLlwaKLIDKYQGTMTA-APNFAYALLakRLRRQAKpGDFDLSTLRFALSGAEP 287
Cdd:PRK13390 215 MVHAL------GGTVVLAKRFD-AQATL---GHVERYRITVTQmVPTMFVRLL--KLDADVR-TRYDVSSLRAVIHAAAP 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 288 VePADVED-LLDAGKPFGLRPSAILPAYGMAettlavsfsecnaglVVDEvdADLLAAlrravPATKGNTrrlaTLGPLl 366
Cdd:PRK13390 282 C-PVDVKHaMIDWLGPIVYEYYSSTEAHGMT---------------FIDS--PDWLAH-----PGSVGRS----VLGDL- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 367 qdleaRIIDEQGDVMPARGVGVIELRGESLTPGYL-----TMGGFIPAQDehGWYDTGDLGYLTEEGHVVVCGRVKDVII 441
Cdd:PRK13390 334 -----HICDDDGNELPAGRIGTVYFERDRLPFRYLndpekTAAAQHPAHP--FWTTVGDLGSVDEDGYLYLADRKSFMII 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 442 MAGRNIYPTDIERAAGRVDGVRPGCAVAVRlDAGHSRESFAVaVESNAFEDPAEvrriehQVAHEVVAEVDVR------P 515
Cdd:PRK13390 407 SGGVNIYPQETENALTMHPAVHDVAVIGVP-DPEMGEQVKAV-IQLVEGIRGSD------ELARELIDYTRSRiahykaP 478
|
410
....*....|....*....
gi 889038433 516 RNVVVLgpGTIPKTPSGKL 534
Cdd:PRK13390 479 RSVEFV--DELPRTPTGKL 495
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
132-536 |
1.14e-12 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 69.96 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 132 VLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAM---FVGAqyDVDKDVMVswlpcfHDMG 208
Cdd:cd05913 58 FTTKEDLRDNYPFGLFAVPREKVVRIHASSGTTGKPTVVGYTKNDLDVWAELVarcLDAA--GVTPGDRV------QNAY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 209 MVGFLT--IPMFFGAELVKVT--PMDFLRdTLLWAKLIDKYQGTM-TAAPNFAyALLAKRLRRQAkpGDFDLSTLRFALS 283
Cdd:cd05913 130 GYGLFTggLGFHYGAERLGALviPAGGGN-TERQLQLIKDFGPTVlCCTPSYA-LYLAEEAEEEG--IDPRELSLKVGIF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 284 GAEPVEPAD---VEDLLDAGkpfglrpsaILPAYGMAETTL-AVSFSECNA-GLVVDEvdaDLLAAlrravpatkgntrr 358
Cdd:cd05913 206 GAEPWTEEMrkrIERRLGIK---------AYDIYGLTEIIGpGVAFECEEKdGLHIWE---DHFIP-------------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 359 latlgpllqdleaRIID-EQGDVMPARGVGviELRGESLTPGYLTMggfIpaqdehgWYDTGDLGYLTEE----GHVV-- 431
Cdd:cd05913 260 -------------EIIDpETGEPVPPGEVG--ELVFTTLTKEAMPL---I-------RYRTRDITRLLPGpcpcGRTHrr 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 432 ---VCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGC-AVAVRLDAGHSREsfaVAVE-SNAFEDPAEVRRIEHQVAHE 506
Cdd:cd05913 315 idrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYqLILTRQEHLDELT---IKVEvRPEADDDEKLEALKQRLERH 391
|
410 420 430
....*....|....*....|....*....|
gi 889038433 507 VVAEVDVRPRnVVVLGPGTIPKTPsGKLRR 536
Cdd:cd05913 392 IKSVLGVTVE-VELVEPGSLPRSE-GKAKR 419
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
151-454 |
1.16e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 70.43 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKdVMVSWLPCFHDMGMVGFLTIPMFFGAELV--KVTP 228
Cdd:PLN03102 185 EHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCP-VYLWTLPMFHCNGWTFTWGTAARGGTSVCmrHVTA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 229 MDFLRDtllwaklIDKYQGT-MTAAPN-FAYALLAKRLRRQAKPGDFDLstlrfaLSGAEPVEPADVEDLLDAGkpfglr 306
Cdd:PLN03102 264 PEIYKN-------IEMHNVThMCCVPTvFNILLKGNSLDLSPRSGPVHV------LTGGSPPPAALVKKVQRLG------ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 307 pSAILPAYGMAETTLAVSFSECNaglvvDEVDAdLLAALRRAVPATKGntrrLATLGplLQDLEARIIDEQGDVmPARG- 385
Cdd:PLN03102 325 -FQVMHAYGLTEATGPVLFCEWQ-----DEWNR-LPENQQMELKARQG----VSILG--LADVDVKNKETQESV-PRDGk 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 386 -VGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIER 454
Cdd:PLN03102 391 tMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVEN 460
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
135-453 |
1.40e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 70.07 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 135 VADLLASD---PIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRN---IYSNAEAMFVGAQYDVDKDVMVSwlPCFHDMG 208
Cdd:PRK07470 143 YEALVARHlgaRVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQmafVITNHLADLMPGTTEQDASLVVA--PLSHGAG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 209 MVGFLTIPMffGAELVkVTPMDFLRDTLLWAkLIDKYQGTmtaapN-FAYALLAKRLRRQAKPGDFDLSTLRFALSGAEP 287
Cdd:PRK07470 221 IHQLCQVAR--GAATV-LLPSERFDPAEVWA-LVERHRVT-----NlFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 288 VEPADVEDLLDA-GKpfglrpsAILPAYGMAETTLAVSFsecnaglvvdevdadLLAALRRAVPatkGNTRRLATLGPLL 366
Cdd:PRK07470 292 MYRADQKRALAKlGK-------VLVQYFGLGEVTGNITV---------------LPPALHDAED---GPDARIGTCGFER 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 367 QDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMggfiPAQDE----HGWYDTGDLGYLTEEGHVVVCGRVKDVIIM 442
Cdd:PRK07470 347 TGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNN----PEANAkafrDGWFRTGDLGHLDARGFLYITGRASDMYIS 422
|
330
....*....|.
gi 889038433 443 AGRNIYPTDIE 453
Cdd:PRK07470 423 GGSNVYPREIE 433
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
129-497 |
1.88e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 69.77 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 129 GMQVLTVADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLP-Cfhdm 207
Cdd:PRK06164 158 RVQLFALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYD-PGAVLLAALPfC---- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 208 GMVGFLTIPMFF--GAELVkvtpMDFLRDTLLWAKLIDKYQGTMTAAPNFAYALLAkrlrrQAKPGDFDLSTLR------ 279
Cdd:PRK06164 233 GVFGFSTLLGALagGAPLV----CEPVFDAARTARALRRHRVTHTFGNDEMLRRIL-----DTAGERADFPSARlfgfas 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 280 FALSGAEPVEPADVEDLLDAGkpfglrpsailpAYGMAEttlavsfsecnaglvvdeVDAdLLAALRRAVPATkgnTRRL 359
Cdd:PRK06164 304 FAPALGELAALARARGVPLTG------------LYGSSE------------------VQA-LVALQPATDPVS---VRIE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 360 ATLGPLLQDLEARIIDEQGD-VMPARGVGVIELRGESLTPGYL-----TMGGFIPaqdeHGWYDTGDLGYLTEEGHVVVC 433
Cdd:PRK06164 350 GGGRPASPEARVRARDPQDGaLLPDGESGEIEIRAPSLMRGYLdnpdaTARALTD----DGYFRTGDLGYTRGDGQFVYQ 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889038433 434 GRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDaGHSRESFAVAVESNAFEDPAEVR 497
Cdd:PRK06164 426 TRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD-GKTVPVAFVIPTDGASPDEAGLM 488
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
31-537 |
3.16e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 69.02 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 31 TWGEVHERARCIAGGLAAAGVGLGDVVGVLA----GFpVEIAPTAQALwmrGASLTMLHqptprTDLAvwAEDTMTVIGM 106
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCrnhrGF-VEALLAANRI---GADILLLN-----TSFA--GPALAEVVTR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 107 IEAKAVIVSEPFLVAIP-----------ILEQKGMQVLTVADLLASDPIG-PIEVGEDDLALMQLTSGSTGSPKAVQITH 174
Cdd:PRK13382 139 EGVDTVIYDEEFSATVDraladcpqatrIVAWTDEDHDLTVEVLIAAHAGqRPEPTGRKGRVILLTSGTTGTPKGARRSG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 175 RNIYSNAEAMFVGAQYDVDKDVMVSwLPCFHDMGMVGFLtipmfFGAEL--VKVTPMDFLRDTLLwaKLIDKYQGTmtaa 252
Cdd:PRK13382 219 PGGIGTLKAILDRTPWRAEEPTVIV-APMFHAWGFSQLV-----LAASLacTIVTRRRFDPEATL--DLIDRHRAT---- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 253 pnfAYALLAKRLRRQAK-PGD----FDLSTLRFALSGAEPVEPADVEDLLDAgkpFGlrpSAILPAYGMAEttlavsfse 327
Cdd:PRK13382 287 ---GLAVVPVMFDRIMDlPAEvrnrYSGRSLRFAAASGSRMRPDVVIAFMDQ---FG---DVIYNNYNATE--------- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 328 cnAGLVVDEVDADLlaalrRAVPATKGnTRRLATlgpllqdlEARIIDEQGDVMPARGVGVIELRGESLTPGYlTMGGfi 407
Cdd:PRK13382 349 --AGMIATATPADL-----RAAPDTAG-RPAEGT--------EIRILDQDFREVPTGEVGTIFVRNDTQFDGY-TSGS-- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 408 pAQDEH-GWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDA-GHSRESFAV-A 484
Cdd:PRK13382 410 -TKDFHdGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQyGQRLAAFVVlK 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 889038433 485 VESNAFEDPAEVRRIEHQVAHEVvaevdvrPRNVVVLgpGTIPKTPSGKLRRA 537
Cdd:PRK13382 489 PGASATPETLKQHVRDNLANYKV-------PRDIVVL--DELPRGATGKILRR 532
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
156-536 |
4.83e-12 |
|
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: 68.17 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 156 LMQLTSGSTGSPKAVQ--ITHRNIYSNAEAMFVGAQYDVDKDVMVSWLPCFHDMGMVGFLTIpMFFGAELV---KVTPMD 230
Cdd:cd05929 129 KMLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTA-LFMGGTLVlmeKFDPEE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 FLRdtllwakLIDKYQGTMTaapNFAYALLAKRLR-RQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGkpfglrPSA 309
Cdd:cd05929 208 FLR-------LIERYRVTFA---QFVPTMFVRLLKlPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWG------GPI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 310 ILPAYGMAEttlAVSFSECNAglvvdevdADLLAAlrravpatKGNTRRlATLGpllqdlEARIIDEQGDVMPARGVGVI 389
Cdd:cd05929 272 IWEYYGGTE---GQGLTIING--------EEWLTH--------PGSVGR-AVLG------KVHILDEDGNEVPPGEIGEV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 390 ELRGeslTPGYLTMG---GFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpGC 466
Cdd:cd05929 326 YFAN---GPGFEYTNdpeKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVL-DA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 467 AVAVRLDAGHSRESFAV---AVESNAFEDPAE---------VRRIEHQVAHEVVAEvdvrprnvvvlgpgtIPKTPSGKL 534
Cdd:cd05929 402 AVVGVPDEELGQRVHAVvqpAPGADAGTALAEeliaflrdrLSRYKCPRSIEFVAE---------------LPRDDTGKL 466
|
..
gi 889038433 535 RR 536
Cdd:cd05929 467 YR 468
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
152-536 |
6.34e-12 |
|
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: 67.74 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIySNAEAMFVGAQYDVDKDVMVSWLPCFHDMGmVGFLTIPMFFGAELV---KVTP 228
Cdd:cd17655 137 DDLAYVIYTSGSTGKPKGVMIEHRGV-VNLVEWANKVIYQGEHLRVALFASISFDAS-VTEIFASLLSGNTLYivrKETV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 229 MDFlrDTLLwaKLIDKYQGTMTAAPNFAYALLAKRlrrqakpGDFDLSTLRFALSGAEPVEPADVEDLldaGKPFGLRPs 308
Cdd:cd17655 215 LDG--QALT--QYIRQNRITIIDLTPAHLKLLDAA-------DDSEGLSLKHLIVGGEALSTELAKKI---IELFGTNP- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 309 AILPAYGMAETTLAVSFSECNAGLVVDEvdadllaalrrAVPatkgntrrlatLGPLLQDLEARIIDEQGDVMPARGVGV 388
Cdd:cd17655 280 TITNAYGPTETTVDASIYQYEPETDQQV-----------SVP-----------IGKPLGNTRIYILDQYGRPQPVGVAGE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 389 IELRGESLTPGY-----LTMGGFIPAQDEHG--WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDG 461
Cdd:cd17655 338 LYIGGEGVARGYlnrpeLTAEKFVDDPFVPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPD 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 889038433 462 VRPGcAVAVRLDAGHSRESFAVAVESNAFeDPAEVR-RIEHQVAHEVVaevdvrPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd17655 418 IKEA-VVIARKDEQGQNYLCAYIVSEKEL-PVAQLReFLARELPDYMI------PSYFIKL--DEIPLTPNGKVDR 483
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
152-453 |
6.84e-12 |
|
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: 67.83 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNaEAMFVGAQYDVDKDVMVSWLPCFHDM-------------GMVGFLTIPMF 218
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGNFLGH-CAAYLAADPLGPGDEYVSVLPLPWIGeqmysvgqalvcgFIVNFPEEPET 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 219 FGAELVKVTPMDFLRDTLLWAKLIDKYQGTMTAAPNF-----------------------------------AYALLAKR 263
Cdd:cd17641 237 MMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFkrfmfelgmklglraldrgkrgrpvslwlrlaswlADALLFRP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 264 LRRQakpgdFDLSTLRFALSGAEPVEPaDVEDLLDA-GKPfglrpsaILPAYGMAETtlavsfsecnAGLVVDEVDADLl 342
Cdd:cd17641 317 LRDR-----LGFSRLRSAATGGAALGP-DTFRFFHAiGVP-------LKQLYGQTEL----------AGAYTVHRDGDV- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 343 aalrravpatkgntrRLATLGPLLQDLEARIIDeqgdvmpargVGVIELRGESLTPGYLTMG-GFIPAQDEHGWYDTGDL 421
Cdd:cd17641 373 ---------------DPDTVGVPFPGTEVRIDE----------VGEILVRSPGVFVGYYKNPeATAEDFDEDGWLHTGDA 427
|
330 340 350
....*....|....*....|....*....|...
gi 889038433 422 GYLTEEGHVVVCGRVKDVIIMA-GRNIYPTDIE 453
Cdd:cd17641 428 GYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIE 460
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
141-536 |
8.12e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 68.65 E-value: 8.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 141 SDPIgpIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFG 220
Cdd:PRK12467 1709 SNPA--VNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCAT--QEAYQLSAADVVLQFTSFAFDVSVWELFWPLING 1784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 221 AELVkVTPMDFLRDTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQAKPgdfdlSTLRFALSGAEPVEPADVEDLLDAg 300
Cdd:PRK12467 1785 ARLV-IAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHP-----LSLRRVVCGGEALEVEALRPWLER- 1857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 301 kpfgLRPSAILPAYGMAETTLAVSFSECNAGlvvDEVDADllaalrrAVPatkgntrrlatLGPLLQDLEARIIDEQGDV 380
Cdd:PRK12467 1858 ----LPDTGLFNLYGPTETAVDVTHWTCRRK---DLEGRD-------SVP-----------IGQPIANLSTYILDASLNP 1912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 381 MPARGVGVIELRGESLTPGY-----LTMGGFIPAQDEHG---WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDI 452
Cdd:PRK12467 1913 VPIGVAGELYLGGVGLARGYlnrpaLTAERFVADPFGTVgsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 1992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 453 ERAAGRVDGVRPgcAVAVRLDAGHSRESFAVAVESNA-----FEDPAEVRRIEHQVAHEVVAEVDVrPRNVVVLgpGTIP 527
Cdd:PRK12467 1993 EARLREQGGVRE--AVVIAQDGANGKQLVAYVVPTDPglvddDEAQVALRAILKNHLKASLPEYMV-PAHLVFL--ARMP 2067
|
....*....
gi 889038433 528 KTPSGKLRR 536
Cdd:PRK12467 2068 LTPNGKLDR 2076
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
124-537 |
1.06e-11 |
|
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: 67.18 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 124 ILEQKGMQVLtvadlLASDPigpievgeDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVDKDVMV----- 198
Cdd:cd05918 91 ILQDTGAKVV-----LTSSP--------SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAH--GRALGLTSESRVlqfas 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 199 -SWLPCFHDMgmvgFLTipMFFGAELvkVTPMDFLRDTLLwAKLIDKYQGTmtaapnfaYALLAKRLRRQAKPGDFdlST 277
Cdd:cd05918 156 yTFDVSILEI----FTT--LAAGGCL--CIPSEEDRLNDL-AGFINRLRVT--------WAFLTPSVARLLDPEDV--PS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 278 LRFALSGAEPVEPADVEDLLDagkpfGLRpsaILPAYGMAETTLAVSFSECnaglvVDEVDADLLAalrRAVPAT----- 352
Cdd:cd05918 217 LRTLVLGGEALTQSDVDTWAD-----RVR---LINAYGPAECTIAATVSPV-----VPSTDPRNIG---RPLGATcwvvd 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 353 KGNTRRLATLGpllqdleariideqgdvmparGVG--VIElrGESLTPGYL-----TMGGFIP----AQDEHGW-----Y 416
Cdd:cd05918 281 PDNHDRLVPIG---------------------AVGelLIE--GPILARGYLndpekTAAAFIEdpawLKQEGSGrgrrlY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 417 DTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGHSRESFAVAV-----ESNAFE 491
Cdd:cd05918 338 RTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFvvldgSSSGSG 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 889038433 492 DPAEVRRIEHQVAHEVVAEVDVR----------PRNVVVLgpGTIPKTPSGKL-RRA 537
Cdd:cd05918 418 DGDSLFLEPSDEFRALVAELRSKlrqrlpsymvPSVFLPL--SHLPLTASGKIdRRA 472
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
152-537 |
1.25e-11 |
|
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: 66.51 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVDKDVMVSWlpcFHDMGM-VGFLTIPMFF--GAELVKVTP 228
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ--IAAFDVGPGSRVLQ---FASPSFdASVWELLMALlaGATLVLAPA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 229 MDFLRDTLLwAKLIDKYQGTMTAAPNFAYALLakrlrrqakPGDfDLSTLRFALSGAEPVePADVEDLLDAGKPFglrps 308
Cdd:cd17652 168 EELLPGEPL-ADLLREHRITHVTLPPAALAAL---------PPD-DLPDLRTLVVAGEAC-PAELVDRWAPGRRM----- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 309 aiLPAYGMAETTLAVSFSECNAGlvvdevdadllaalrRAVPatkgntrrlaTLGPLLQDLEARIIDEQGDVMPARGVGV 388
Cdd:cd17652 231 --INAYGPTETTVCATMAGPLPG---------------GGVP----------PIGRPVPGTRVYVLDARLRPVPPGVPGE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 389 IELRGESLTPGY-----LTMGGFIP---AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVD 460
Cdd:cd17652 284 LYIAGAGLARGYlnrpgLTAERFVAdpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHP 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 889038433 461 GVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRriEHqvAHEVVAEVDVrPRNVVVLgpGTIPKTPSGKLRRA 537
Cdd:cd17652 364 GVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELR--AH--LAERLPGYMV-PAAFVVL--DALPLTPNGKLDRR 433
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
108-534 |
2.89e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 65.74 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 108 EAKAVIVSEPF--LVAIPILEQKGMQVLTVADLLASDPIGPiEVGEDD-----------------------LALmQLTSG 162
Cdd:PRK08162 115 EAKVLIVDTEFaeVAREALALLPGPKPLVIDVDDPEYPGGR-FIGALDyeaflasgdpdfawtlpadewdaIAL-NYTSG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 163 STGSPKAVQITHRNIYSNAEAMFVgaQYDVDKDVMVSW-LPCFHDMGMVGFLTIPMFFGAE--LVKVTPmdflrdTLLWa 239
Cdd:PRK08162 193 TTGNPKGVVYHHRGAYLNALSNIL--AWGMPKHPVYLWtLPMFHCNGWCFPWTVAARAGTNvcLRKVDP------KLIF- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 240 KLIDKYQGT-MTAAPnFAYALLAKrLRRQAKPGdFDlSTLRFALSGAEPvePADVedlLDAGKPFGLRpsaILPAYGMAE 318
Cdd:PRK08162 264 DLIREHGVThYCGAP-IVLSALIN-APAEWRAG-ID-HPVHAMVAGAAP--PAAV---IAKMEEIGFD---LTHVYGLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 319 TTLAVSFSECNAGlvVDEVDADLLAAL--RRAVPAtkgntrrlatlgpLLQDlEARIID-EQGDVMPARG--VGVIELRG 393
Cdd:PRK08162 332 TYGPATVCAWQPE--WDALPLDERAQLkaRQGVRY-------------PLQE-GVTVLDpDTMQPVPADGetIGEIMFRG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 394 ESLTPGYL-----TMGGFipaqdEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpGCAV 468
Cdd:PRK08162 396 NIVMKGYLknpkaTEEAF-----AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVL-VAAV 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889038433 469 AVRLDA--GHSRESFaVAVESNAFEDPAEVrrIEHQVAHevVAEVDVrPRNVVVlgpGTIPKTPSGKL 534
Cdd:PRK08162 470 VAKPDPkwGEVPCAF-VELKDGASATEEEI--IAHCREH--LAGFKV-PKAVVF---GELPKTSTGKI 528
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
140-455 |
3.01e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 66.07 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 140 ASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHrniysnaEAM---FVGAQYDVD-KDVMVSWlpCFHDMGMV----- 210
Cdd:PRK04319 193 ASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH-------NAMlqhYQTGKYVLDlHEDDVYW--CTADPGWVtgtsy 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 211 GFLTiPMFFGAELVkVTPMDFlrDTLLWAKLIDKYQGTM-----TAapnfayallakrLRRQAKPGD-----FDLSTLRF 280
Cdd:PRK04319 264 GIFA-PWLNGATNV-IDGGRF--SPERWYRILEDYKVTVwytapTA------------IRMLMGAGDdlvkkYDLSSLRH 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 281 ALSGAEPVEPadvEDLLDAGKPFGLRpsaILPAYGMAETtlavsfsecNAGLVVDEVDADLlaalrravpatkgntrRLA 360
Cdd:PRK04319 328 ILSVGEPLNP---EVVRWGMKVFGLP---IHDNWWMTET---------GGIMIANYPAMDI----------------KPG 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 361 TLGPLLQDLEARIIDEQGDVMPARGVGVIELRgesltPGYLTMGGFIPAQDEH-------GWYDTGDLGYLTEEGHVVVC 433
Cdd:PRK04319 377 SMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-----KGWPSMMRGIWNNPEKyesyfagDWYVSGDSAYMDEDGYFWFQ 451
|
330 340
....*....|....*....|..
gi 889038433 434 GRVKDVIIMAGRNIYPTDIERA 455
Cdd:PRK04319 452 GRVDDVIKTSGERVGPFEVESK 473
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
156-532 |
3.90e-11 |
|
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: 64.63 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 156 LMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKdVMVSWLPCFHdMGMVGFLTIPMFFGAELVkvtpmdFLR-- 233
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGT-VFLNSGPLFH-IGTLMFTLATFHAGGTNV------FVRrv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 234 DTLLWAKLI--DKYQGTMTAAPNFAyallakRLRRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAGKPFGlrpsail 311
Cdd:cd17636 76 DAEEVLELIeaERCTHAFLLPPTID------QIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGG------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 312 paYGMAETTlavsfsecnaGLVVdevdadlLAALrrAVPATKGNTRRlatlGPLLQdleARIIDEQGDVMPARGVGVIEL 391
Cdd:cd17636 143 --YGQTEVM----------GLAT-------FAAL--GGGAIGGAGRP----SPLVQ---VRILDEDGREVPDGEVGEIVA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 392 RGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVR 471
Cdd:cd17636 195 RGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVP 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 889038433 472 LDAGHSRESFAVAVESNAFEDPAEVrrIEHQVAHevVAEVDvRPRNVVVLGPgtIPKTPSG 532
Cdd:cd17636 275 DPRWAQSVKAIVVLKPGASVTEAEL--IEHCRAR--IASYK-KPKSVEFADA--LPRTAGG 328
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
140-537 |
4.82e-11 |
|
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: 65.18 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 140 ASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRniySNAEAMFVGAQYDVD---KDVMvsWlpCFHDMGMV----GF 212
Cdd:cd05928 162 ASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHS---SLGLGLKVNGRYWLDltaSDIM--W--NTSDTGWIksawSS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 213 LTIPMFFGA-----ELVKVTPMDFLrDTLLwaklidKYQ-GTMTAAPNFAYALLAKRLRRqakpgdFDLSTLRFALSGAE 286
Cdd:cd05928 235 LFEPWIQGAcvfvhHLPRFDPLVIL-KTLS------SYPiTTFCGAPTVYRMLVQQDLSS------YKFPSLQHCVTGGE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 287 PVEPADVEDLLDAGkpfGLRpsaILPAYGMAETTLAVSFSecnaglvvdevdadllaalrravpatKGNTRRLATLGPLL 366
Cdd:cd05928 302 PLNPEVLEKWKAQT---GLD---IYEGYGQTETGLICANF--------------------------KGMKIKPGSMGKAS 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 367 QDLEARIIDEQGDVMPARGVGVIELRGESLTPGYLTMGgFI-----PAQDEHG-WYDTGDLGYLTEEGHVVVCGRVKDVI 440
Cdd:cd05928 350 PPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSG-YVdnpekTAATIRGdFYLTGDRGIMDEDGYFWFMGRADDVI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 441 IMAGRNIYPTDIERAAGRVDGVRPGCAVA----VRldaGHSRESFAVAVESNAFEDPAEVRRIEHQVAHEVVAEVDVrPR 516
Cdd:cd05928 429 NSSGYRIGPFEVESALIEHPAVVESAVVSspdpIR---GEVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKY-PR 504
|
410 420
....*....|....*....|.
gi 889038433 517 NVVVLgpGTIPKTPSGKLRRA 537
Cdd:cd05928 505 KVEFV--QELPKTVTGKIQRN 523
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
127-453 |
6.08e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 65.12 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 127 QKGMQVLTVADLLA---SDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeamfVGAQYDVD---KDVMVSW 200
Cdd:PLN02736 193 GTGVEIVTYSKLLAqgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANV----AGSSLSTKfypSDVHISY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 201 LP------------CFHDMGMVGFltipmFFGAELVKVTPMDFLRDTL------LWAKLIDKYQGTMTAAP-------NF 255
Cdd:PLN02736 269 LPlahiyervnqivMLHYGVAVGF-----YQGDNLKLMDDLAALRPTIfcsvprLYNRIYDGITNAVKESGglkerlfNA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 256 AYALLAKRLRRQAKPGD------FDL------STLRFALSGAEPVEPaDVEDLLDAGkpFGLRpsaILPAYGMAETTLAV 323
Cdd:PLN02736 344 AYNAKKQALENGKNPSPmwdrlvFNKikaklgGRVRFMSSGASPLSP-DVMEFLRIC--FGGR---VLEGYGMTETSCVI 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 324 SfsecnaglVVDEVDaDLLAALRRAVPATkgntrrlatlgpllqdlEARIID--EQG----DVMPARgvGVIELRGESLT 397
Cdd:PLN02736 418 S--------GMDEGD-NLSGHVGSPNPAC-----------------EVKLVDvpEMNytseDQPYPR--GEICVRGPIIF 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 889038433 398 PGYL-----TMGGFipaqDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMA-GRNIYPTDIE 453
Cdd:PLN02736 470 KGYYkdevqTREVI----DEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIE 527
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
149-537 |
7.14e-11 |
|
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: 64.26 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 149 VGEDDLALMQLTSGSTGSPKAVQITHRNiysnAEAMFVGAQYDVDKDVMVSWLP----CFhDMGmVGFLTIPMFFGAELV 224
Cdd:cd12115 102 TDPDDLAYVIYTSGSTGRPKGVAIEHRN----AAAFLQWAAAAFSAEELAGVLAstsiCF-DLS-VFELFGPLATGGKVV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 225 KVTPMDFLRD--TLLWAKLIDkyqgtmtAAPNFAYALLakrlRRQAKPGDfdLSTLRFAlsgAEPVEPADVEDLldAGKP 302
Cdd:cd12115 176 LADNVLALPDlpAAAEVTLIN-------TVPSAAAELL----RHDALPAS--VRVVNLA---GEPLPRDLVQRL--YARL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 303 FGLRpsaILPAYGMAETTLAVSFSECNAGlvvdevdadllaalrravpatkgnTRRLATLGPLLQDLEARIIDEQGDVMP 382
Cdd:cd12115 238 QVER---VVNLYGPSEDTTYSTVAPVPPG------------------------ASGEVSIGRPLANTQAYVLDRALQPVP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 383 ARGVGVIELRGESLTPGYL-----TMGGFIPAQDEHG--WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERA 455
Cdd:cd12115 291 LGVPGELYIGGAGVARGYLgrpglTAERFLPDPFGPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 456 AGRVDGVRPGCAVAVRLDAGHSRESFAVAVESNAFEDPAEVRR-IEHQVAHEVVaevdvrPRNVVVLGpgTIPKTPSGKL 534
Cdd:cd12115 371 LRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRhLGTRLPAYMV------PSRFVRLD--ALPLTPNGKI 442
|
...
gi 889038433 535 RRA 537
Cdd:cd12115 443 DRS 445
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
418-536 |
1.41e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.13 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 418 TGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPgcAVAVRLDAGHSRESFAVAVESNAFEDPAEVR 497
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQE--AVVYRGKDPVAGERVKAKVISHEEIDPVQLR 372
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 889038433 498 R------IEHQVAHEV--VAEvdvrprnvvvlgpgtIPKTPSGKLRR 536
Cdd:PRK08308 373 EwciqhlAPYQVPHEIesVTE---------------IPKNANGKVSR 404
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
361-536 |
1.73e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 63.48 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 361 TLGPLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGYlTMGGFIPAQDehGWYDTGDLGYLTEEGHVVVCGRVKDVI 440
Cdd:PRK13383 346 TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY-TDGGGKAVVD--GMTSTGDMGYLDNAGRLFIVGREDDMI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 441 IMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDA-GHSRESFAVA-----VESNAFED--PAEVRRIEhqvahevvaevd 512
Cdd:PRK13383 423 ISGGENVYPRAVENALAAHPAVADNAVIGVPDERfGHRLAAFVVLhpgsgVDAAQLRDylKDRVSRFE------------ 490
|
170 180
....*....|....*....|....
gi 889038433 513 vRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:PRK13383 491 -QPRDINIV--SSIPRNPTGKVLR 511
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
94-208 |
2.60e-10 |
|
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: 62.83 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 94 AVWAEDTMTVIGMIEAkavivsePFLVAIPIL----EQKGMQVLTVADLLASDPIGPIE-----VGEDDLALMQLTSGST 164
Cdd:cd05921 105 LVFAQDAAPFARALAA-------IFPLGTPLVvsrnAVAGRGAISFAELAATPPTAAVDaafaaVGPDTVAKFLFTSGST 177
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 889038433 165 GSPKAVQITHRNIYSNAEAMF-VGAQYDVDKDVMVSWLPCFHDMG 208
Cdd:cd05921 178 GLPKAVINTQRMLCANQAMLEqTYPFFGEEPPVLVDWLPWNHTFG 222
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
129-537 |
4.61e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 62.75 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 129 GMQVLTVADLLASDPIGPIEVGE-DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVD-KDVMVSWLPCFHD 206
Cdd:PRK10252 574 DLTSLCYNAPLAPQGAAPLQLSQpHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM--QNHYPLTaDDVVLQKTPCSFD 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 207 MGMVGFLtIPMFFGAELVkVTPMDFLRDTLLWAKLIDKYQGTMTA-APNFAYALLAKRLRRQAkpgDFDLSTLRFALSGA 285
Cdd:PRK10252 652 VSVWEFF-WPFIAGAKLV-MAEPEAHRDPLAMQQFFAEYGVTTTHfVPSMLAAFVASLTPEGA---RQSCASLRQVFCSG 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 286 EPVePADVEDLldagkpFGLRPSAIL-PAYGMAETtlAVSFSECNAGlvvdevdADLLAALR-RAVPAtkG----NTRrl 359
Cdd:PRK10252 727 EAL-PADLCRE------WQQLTGAPLhNLYGPTEA--AVDVSWYPAF-------GEELAAVRgSSVPI--GypvwNTG-- 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 360 atlgpllqdleARIIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFI--PAQDEHGWYDTGDLGYLTEEGHVVV 432
Cdd:PRK10252 787 -----------LRILDARMRPVPPGVAGDLYLTGIQLAQGYlgrpdLTASRFIadPFAPGERMYRTGDVARWLDDGAVEY 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 433 CGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLD-----AGHSRESFAVAV-ESNAFEDPAEVR-RIEHQV-A 504
Cdd:PRK10252 856 LGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINqaaatGGDARQLVGYLVsQSGLPLDTSALQaQLRERLpP 935
|
410 420 430
....*....|....*....|....*....|...
gi 889038433 505 HEVvaevdvrPrnVVVLGPGTIPKTPSGKLRRA 537
Cdd:PRK10252 936 HMV-------P--VVLLQLDQLPLSANGKLDRK 959
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
148-470 |
4.97e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 61.97 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 148 EVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFvgAQYDVDK-DVMVSWLPCFHDMGMVGFLTIPMFFGAELV-- 224
Cdd:PRK13388 146 EVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALT--ERFGLTRdDVCYVSMPLFHSNAVMAGWAPAVASGAAVAlp 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 225 -KVTPMDFLRDtllwaklIDKYQGTMTaapNFAYALLAKRLRRQAKPGDFDlSTLRFALsGAEpvepADVEDLLDAGKPF 303
Cdd:PRK13388 224 aKFSASGFLDD-------VRRYGATYF---NYVGKPLAYILATPERPDDAD-NPLRVAF-GNE----ASPRDIAEFSRRF 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 304 GLRpsaILPAYGMAEttlavsfsecNAGLVVDEVDADlLAALRRAVPAtkgntrrLATLGP-LLQDLEARIIDEQGDVM- 381
Cdd:PRK13388 288 GCQ---VEDGYGSSE----------GAVIVVREPGTP-PGSIGRGAPG-------VAIYNPeTLTECAVARFDAHGALLn 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 382 PARGVG-VIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVD 460
Cdd:PRK13388 347 ADEAIGeLVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHP 426
|
330
....*....|
gi 889038433 461 GVRpgcAVAV 470
Cdd:PRK13388 427 AIN---RVAV 433
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
126-208 |
9.74e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 61.05 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 126 EQKGMQVLTVADLLASDPIGPIE-----VGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvgAQ-YDVDKD---V 196
Cdd:PRK08180 178 AVPGRAATPFAALLATPPTAAVDaahaaVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQML---AQtFPFLAEeppV 254
|
90
....*....|..
gi 889038433 197 MVSWLPCFHDMG 208
Cdd:PRK08180 255 LVDWLPWNHTFG 266
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
152-537 |
1.01e-09 |
|
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: 60.91 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFvgAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVkVTPMDF 231
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLI--KEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLV-LRPEEM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 LRDTLLWAKLIDKYQGTMTAAPNFAYALLAKRLRRQAKPGDfdlSTLRFALSGAEPVEPADVEDLLDAGKPFglrpSAIL 311
Cdd:cd17644 183 RSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLP---SSLRLVIVGGEAVQPELVRQWQKNVGNF----IQLI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 312 PAYGMAETTLAVSFSECNaglvvdevdaDLLAALRRAVPatkgntrrlatLGPLLQDLEARIIDEQGDVMPARGVGVIEL 391
Cdd:cd17644 256 NVYGPTEATIAATVCRLT----------QLTERNITSVP-----------IGRPIANTQVYILDENLQPVPVGVPGELHI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 392 RGESLTPGY-----LTMGGFIPAQDEHG----WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGV 462
Cdd:cd17644 315 GGVGLARGYlnrpeLTAEKFISHPFNSSeserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 463 RPGCaVAVRLDAGHSRESFAVAV-ESNAFEDPAEVRRI------EHQVahevvaevdvrPRNVVVLgpGTIPKTPSGKL- 534
Cdd:cd17644 395 KTAV-VIVREDQPGNKRLVAYIVpHYEESPSTVELRQFlkaklpDYMI-----------PSAFVVL--EELPLTPNGKId 460
|
...
gi 889038433 535 RRA 537
Cdd:cd17644 461 RRA 463
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
136-470 |
1.74e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 60.08 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 136 ADLLAS---DPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVDKD--VMVSwLPCFHDMGMV 210
Cdd:PRK07867 133 ADELAAhrdAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVML--AQRFGLGPDdvCYVS-MPLFHSNAVM 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 211 GFLTIPMFFGAELV---KVTPMDFLRDtllwaklIDKYQGTMTaapNFAYALLAKRLRRQAKPGDFDlSTLRFALsGAEP 287
Cdd:PRK07867 210 AGWAVALAAGASIAlrrKFSASGFLPD-------VRRYGATYA---NYVGKPLSYVLATPERPDDAD-NPLRIVY-GNEG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 288 VePADVEDLldaGKPFGLRpsaILPAYGMAETTLAVSfsecnaglvvdevdadllaalrrAVPATkgntrRLATLGPLLQ 367
Cdd:PRK07867 278 A-PGDIARF---ARRFGCV---VVDGFGSTEGGVAIT-----------------------RTPDT-----PPGALGPLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 368 DLEAR-----------IIDEQGDVMPARGVG-VIELRGESLTPGYLTMggfiPAQDE----HGWYDTGDLGYLTEEGHVV 431
Cdd:PRK07867 323 GVAIVdpdtgtecppaEDADGRLLNADEAIGeLVNTAGPGGFEGYYND----PEADAermrGGVYWSGDLAYRDADGYAY 398
|
330 340 350
....*....|....*....|....*....|....*....
gi 889038433 432 VCGRVKDVIIMAGRNIYPTDIERAAGRVDGVrpgCAVAV 470
Cdd:PRK07867 399 FAGRLGDWMRVDGENLGTAPIERILLRYPDA---TEVAV 434
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
275-462 |
3.66e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 58.85 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 275 LSTLRFALSGAEPVEPAdvedLLDAGKPFGLRpsaILPAYGMAETtlavsfsecnAGLVVDEVDADLLAalrravpatkG 354
Cdd:PRK07445 229 LAQFRTILLGGAPAWPS----LLEQARQLQLR---LAPTYGMTET----------ASQIATLKPDDFLA----------G 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 355 NTrrlaTLGPLLQdlEARIIDEQGDVmpargvGVIELRGESLTPGYltmggFIPAQDEHGWYDTGDLGYLTEEGHVVVCG 434
Cdd:PRK07445 282 NN----SSGQVLP--HAQITIPANQT------GNITIQAQSLALGY-----YPQILDSQGIFETDDLGYLDAQGYLHILG 344
|
170 180 190
....*....|....*....|....*....|.
gi 889038433 435 RVKDVIIMAGRNIYPTDIE---RAAGRVDGV 462
Cdd:PRK07445 345 RNSQKIITGGENVYPAEVEaaiLATGLVQDV 375
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
140-534 |
4.28e-09 |
|
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: 59.13 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 140 ASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNiYSNAEAMFVGAQYDVDKDVMVsWlpCFHDMG-MVG---FLTI 215
Cdd:cd17634 220 ASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGG-YLVYAATTMKYVFDYGPGDIY-W--CTADVGwVTGhsyLLYG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 216 PMFFGAELVKVTPMDFLRDTLLWAKLIDKYQGT-MTAAPNFAYALLAKRLRRQAKpgdFDLSTLRFALSGAEPVEPAD-- 292
Cdd:cd17634 296 PLACGATTLLYEGVPNWPTPARMWQVVDKHGVNiLYTAPTAIRALMAAGDDAIEG---TDRSSLRILGSVGEPINPEAye 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 293 --VEDLLDAGKPfglrpsaILPAYGMAETTLAVsfsecnaglvvdevdadlLAALRRAVPATKGNTRRlATLGpllqdLE 370
Cdd:cd17634 373 wyWKKIGKEKCP-------VVDTWWQTETGGFM------------------ITPLPGAIELKAGSATR-PVFG-----VQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 371 ARIIDEQGDVMPARGVGVIELrGESLTPGYLTMGGFIPAQDE------HGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAG 444
Cdd:cd17634 422 PAVVDNEGHPQPGGTEGNLVI-TDPWPGQTRTLFGDHERFEQtyfstfKGMYFSGDGARRDEDGYYWITGRSDDVINVAG 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 445 RNIYPTDIERAAGRVDGVRPGCAVAVRlDAGHSRESFAVAVESNAFEDPAEVR-RIEHQVAHEVVAEvdVRPRNVVVLgp 523
Cdd:cd17634 501 HRLGTAEIESVLVAHPKVAEAAVVGIP-HAIKGQAPYAYVVLNHGVEPSPELYaELRNWVRKEIGPL--ATPDVVHWV-- 575
|
410
....*....|.
gi 889038433 524 GTIPKTPSGKL 534
Cdd:cd17634 576 DSLPKTRSGKI 586
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
136-536 |
4.99e-09 |
|
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: 59.04 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 136 ADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAeAMFVGAQYDVDKDVMVSWlpcFHDMG-MVGFLT 214
Cdd:cd05968 220 DEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKA-AQDMYFQFDLKPGDLLTW---FTDLGwMMGPWL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 215 IpmfFGAELVKVTPM------DFLRDTLLWaKLIDKYQGT-MTAAPNFAYALLAkrlRRQAKPGDFDLSTLRFALSGAEP 287
Cdd:cd05968 296 I---FGGLILGATMVlydgapDHPKADRLW-RMVEDHEIThLGLSPTLIRALKP---RGDAPVNAHDLSSLRVLGSTGEP 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 288 VEPAD----VEDLLDAGKPfglrpsaILPAYGMAETTLAVSfsecnAGLVVDEVDAdllAALRRAVPATKgntrrlatlg 363
Cdd:cd05968 369 WNPEPwnwlFETVGKGRNP-------IINYSGGTEISGGIL-----GNVLIKPIKP---SSFNGPVPGMK---------- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 364 pllqdleARIIDEQGDvmPARG-VGviELRGESLTPGyLTMGGFipaQDEHGWYDT-----------GDLGYLTEEGHVV 431
Cdd:cd05968 424 -------ADVLDESGK--PARPeVG--ELVLLAPWPG-MTRGFW---RDEDRYLETywsrfdnvwvhGDFAYYDEEGYFY 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 432 VCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDA-GHSRESFAVaVESNAFEDPAevrrIEHQVAHEVVAE 510
Cdd:cd05968 489 ILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVkGEAIVCFVV-LKPGVTPTEA----LAEELMERVADE 563
|
410 420
....*....|....*....|....*...
gi 889038433 511 VD--VRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:cd05968 564 LGkpLSPERILFV--KDLPKTRNAKVMR 589
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
116-453 |
7.23e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 58.16 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 116 EPFLVAIPILEQKGMQvlTVADLLASDPIGPIEvGEDDLALMQLTSGSTGSPKAV--QITHRNIYSNAE-AMFVGAQYDV 192
Cdd:PRK13391 121 RHRLVLDGDGELEGFV--GYAEAVAGLPATPIA-DESLGTDMLYSSGTTGRPKGIkrPLPEQPPDTPLPlTAFLQRLWGF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 193 DKD-VMVSWLPCFHDMGMVGFLTIPMFFGAELV--KVTPMDFLRdtllwakLIDKYQGTMTaapNFAYALLAKRLR-RQA 268
Cdd:PRK13391 198 RSDmVYLSPAPLYHSAPQRAVMLVIRLGGTVIVmeHFDAEQYLA-------LIEEYGVTHT---QLVPTMFSRMLKlPEE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 269 KPGDFDLSTLRFALSGAEPVePADV-EDLLDAGKPFglrpsaILPAYGMAEttlAVSFSECNAglvvdevdADLLAAlrr 347
Cdd:PRK13391 268 VRDKYDLSSLEVAIHAAAPC-PPQVkEQMIDWWGPI------IHEYYAATE---GLGFTACDS--------EEWLAH--- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 348 avPATKGNtrrlatlgPLLQDLeaRIIDEQGDVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHG-WYDTGDLGYLTE 426
Cdd:PRK13391 327 --PGTVGR--------AMFGDL--HILDDDGAELPPGEPGTIWFEGGRPFEYLNDPAKTAEARHPDGtWSTVGDIGYVDE 394
|
330 340
....*....|....*....|....*..
gi 889038433 427 EGHVVVCGRVKDVIIMAGRNIYPTDIE 453
Cdd:PRK13391 395 DGYLYLTDRAAFMIISGGVNIYPQEAE 421
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
117-468 |
7.93e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 57.36 E-value: 7.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 117 PFLVAIPILEQKGMQVLTVAdLLASDPIgpievgEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAM--FVGAQydvdk 194
Cdd:PRK07824 7 PALLPVPAQDERRAALLRDA-LRVGEPI------DDDVALVVATSGTTGTPKGAMLTAAALTASADAThdRLGGP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 195 dvmVSWL---PCFHDMGMvGFLTIPMFFGAE-LVKVTPMDFLRDTLlwAKLIDKYQGTMTAAPNFAyALLAKRLRRQAkp 270
Cdd:PRK07824 75 ---GQWLlalPAHHIAGL-QVLVRSVIAGSEpVELDVSAGFDPTAL--PRAVAELGGGRRYTSLVP-MQLAKALDDPA-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 271 GDFDLSTLRFALSGAEPVePADVedlLDAGKPFGLRpsaILPAYGMAETTlavsfsecnAGLVVDevdadllaalrrAVP 350
Cdd:PRK07824 146 ATAALAELDAVLVGGGPA-PAPV---LDAAAAAGIN---VVRTYGMSETS---------GGCVYD------------GVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 351 atkgntrrlatlgplLQDLEARIIDEQgdvmpargvgvIELRGESLTPGYLTMGGFiPAQDEHGWYDTGDLGYLTEeGHV 430
Cdd:PRK07824 198 ---------------LDGVRVRVEDGR-----------IALGGPTLAKGYRNPVDP-DPFAEPGWFRTDDLGALDD-GVL 249
|
330 340 350
....*....|....*....|....*....|....*...
gi 889038433 431 VVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRpGCAV 468
Cdd:PRK07824 250 TVLGRADDAISTGGLTVLPQVVEAALATHPAVA-DCAV 286
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
28-536 |
1.03e-08 |
|
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: 57.83 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 28 VRHTWGEVheRARCIAGGLAAAGVGLGDVVGVLAgfpveIAPTAQALW-------MRGASLTMLHQPTPRTDLAVWAEDT 100
Cdd:cd05915 23 HRTTYAEV--YQRARRLMGGLRALGVGVGDRVAT-----LGFNHFRHLeayfavpGMGAVLHTANPRLSPKEIAYILNHA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 101 MTVIGMIEAKAVIVSEPFLVAI------PILEQKGMQVltvADLLAS-----DPIGPIEvgEDDLALMQLTSGSTGSPKA 169
Cdd:cd05915 96 EDKVLLFDPNLLPLVEAIRGELktvqhfVVMDEKAPEG---YLAYEEalgeeADPVRVP--ERAACGMAYTTGTTGLPKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 170 VQITHRNIYSNAEAmfVGAQYDVDKDVMVSWL---PCFHDMGMVGFLTIPMFFGaelVKVTPMDFLRDTLLWAKLIDKYQ 246
Cdd:cd05915 171 VVYSHRALVLHSLA--ASLVDGTALSEKDVVLpvvPMFHVNAWCLPYAATLVGA---KQVLPGPRLDPASLVELFDGEGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 247 GTMTAAPNFAYALL-AKRLRRQAKPGdfdlsTLRFALSGAEPVEPadvedLLDAGKpfgLRPSAILPAYGMAETtlavsF 325
Cdd:cd05915 246 TFTAGVPTVWLALAdYLESTGHRLKT-----LRRLVVGGSAAPRS-----LIARFE---RMGVEVRQGYGLTET-----S 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 326 SECNAGLVVDEVDadllaalrrAVPATKgnTRRLATLGPLLQDLEA-RIIDEQGDVMPARG--VGVIELRGESLTPGYLT 402
Cdd:cd05915 308 PVVVQNFVKSHLE---------SLSEEE--KLTLKAKTGLPIPLVRlRVADEEGRPVPKDGkaLGEVQLKGPWITGGYYG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 403 MGGFIPAQD-EHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAvRLDA--GHSRE 479
Cdd:cd05915 377 NEEATRSALtPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA-IPHPkwQERPL 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 889038433 480 SFAVAVESNAFEDPAevrrIEhqVAHEVVAEVDVRPRNVVVlgPGTIPKTPSGKLRR 536
Cdd:cd05915 456 AVVVPRGEKPTPEEL----NE--HLLKAGFAKWQLPDAYVF--AEEIPRTSAGKFLK 504
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
89-536 |
1.35e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 58.25 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 89 PRTDLAVWAEDTmtviGMieaKAVIVSEPFLVAIPILeqKGMQVLTVaDLLASDPIGP----IEVGEDDLALMQLTSGST 164
Cdd:PRK12467 3180 PRERLAYMIEDS----GV---KLLLTQAHLLEQLPAP--AGDTALTL-DRLDLNGYSEnnpsTRVMGENLAYVIYTSGST 3249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 165 GSPKAVQITHRNIYSNAEAMfvGAQYDVDKDVMVSWLPCFHDMGMVGFLTIPMFFGAELVkVTPMDFLRDTLLWAKLidK 244
Cdd:PRK12467 3250 GKPKGVGVRHGALANHLCWI--AEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLV-VRDNDLWDPEELWQAI--H 3324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 245 YQGTMTAapNFAYALLaKRLRRQAKPGdfDLSTLRFALSGAEPVEPADVEDLLDAGKPFGLrpsaiLPAYGMAETTLAVS 324
Cdd:PRK12467 3325 AHRISIA--CFPPAYL-QQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKLKPRGL-----TNGYGPTEAVVTVT 3394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 325 FSECNaglvvdeVDADLLAAlrrAVPAtkgnTRRLATLGpllqdleARIIDEQGDVMPARGVGVIELRGESLTPGY---- 400
Cdd:PRK12467 3395 LWKCG-------GDAVCEAP---YAPI----GRPVAGRS-------IYVLDGQLNPVPVGVAGELYIGGVGLARGYhqrp 3453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 401 -LTMGGFIPAQ-DEHG--WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRLDAGH 476
Cdd:PRK12467 3454 sLTAERFVADPfSGSGgrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGK 3533
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 889038433 477 SRESFAVAvesnafEDPAEVRRIehQVAHEVVAEVD--VRPRNVVVLgpGTIPKTPSGKLRR 536
Cdd:PRK12467 3534 QLVAYVVP------ADPQGDWRE--TLRDHLAASLPdyMVPAQLLVL--AAMPLGPNGKVDR 3585
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
152-453 |
3.94e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 55.77 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVMVSwLPCFHDMGMVGFLTIPMFFGAELVKVTPMDf 231
Cdd:PRK10946 182 DEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCA-LPAAHNYPMSSPGALGVFLAGGTVVLAPDP- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 232 lrDTLLWAKLIDKYQGTMTAAPNFAYALLakrLRRQAKPGDFD-LSTLRFALSGaepvepadvedlldaGKPFGLRPSAI 310
Cdd:PRK10946 260 --SATLCFPLIEKHQVNVTALVPPAVSLW---LQAIAEGGSRAqLASLKLLQVG---------------GARLSETLARR 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 311 LPA---------YGMAEttlavsfsecnaGLV----VDEVDadllaalrravpatkgnTRRLATLG-PLLQDLEARIIDE 376
Cdd:PRK10946 320 IPAelgcqlqqvFGMAE------------GLVnytrLDDSD-----------------ERIFTTQGrPMSPDDEVWVADA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 377 QGDVMPARGVGVIELRGESLTPGYLTMggfiPAQ-----DEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTD 451
Cdd:PRK10946 371 DGNPLPQGEVGRLMTRGPYTFRGYYKS----PQHnasafDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEE 446
|
..
gi 889038433 452 IE 453
Cdd:PRK10946 447 IE 448
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
152-537 |
4.03e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 152 DDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMfvGAQYDVD-KDVMVSWLPCFHDMGmVGFLTIPMFFGAELVKVTPMD 230
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM--QATYALDdSDVLMQKAPISFDVS-VWECFWPLITGCRLVLAGPGE 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 FlRDTLLWAKLIDKYQGTMTaapNFAYALLAKRLRrqaKPGDFDLSTLRFALSGAEPVePADVEDlldagkpfglRPSAI 310
Cdd:PRK05691 1350 H-RDPQRIAELVQQYGVTTL---HFVPPLLQLFID---EPLAAACTSLRRLFSGGEAL-PAELRN----------RVLQR 1411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 311 LPA------YGMAETTLAVSFSECNAglvvdevdadllaalrravpatkGNTRRlATLGPLLQDLEARIIDEQGDVMPAR 384
Cdd:PRK05691 1412 LPQvqlhnrYGPTETAINVTHWQCQA-----------------------EDGER-SPIGRPLGNVLCRVLDAELNLLPPG 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 385 GVGVIELRGESLTPGYL-----TMGGFIP---AQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAA 456
Cdd:PRK05691 1468 VAGELCIGGAGLARGYLgrpalTAERFVPdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARL 1547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 457 GRVDGVRPGcAVAVRLDAGHSResfAVAVESNAFEDPAEVRRIEHQVAHEVVAEvdVRPRNVVVLgpGTIPKTPSGKL-R 535
Cdd:PRK05691 1548 LAQPGVAQA-AVLVREGAAGAQ---LVGYYTGEAGQEAEAERLKAALAAELPEY--MVPAQLIRL--DQMPLGPSGKLdR 1619
|
..
gi 889038433 536 RA 537
Cdd:PRK05691 1620 RA 1621
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
153-497 |
7.13e-08 |
|
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: 55.05 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHRNIYsNAEAMFVGAQYDVDKDVMVSWLPCFHDMG-MVGFLTIPMfFGAELV---KVTP 228
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAW-RGGAFFAGSGGALPSDVLYTCLPLYHSTAlIVGWSACLA-SGATLVirkKFSA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 229 MDFLRDtllwaklIDKYQGTMtaapnFAYAllakrlrrqakpGDfdlsTLRFALsgAEPVEPADVEDLLDAGKPFGLRPS 308
Cdd:cd05940 160 SNFWDD-------IRKYQATI-----FQYI------------GE----LCRYLL--NQPPKPTERKHKVRMIFGNGLRPD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 309 A---ILPAYGMAETTLAVSFSECNAGLV-VDEVDadllaalrRAVPATKGNTRRLATLGPLLQDLE--ARIIDEQGDVMP 382
Cdd:cd05940 210 IweeFKERFGVPRIAEFYAATEGNSGFInFFGKP--------GAIGRNPSLLRKVAPLALVKYDLEsgEPIRDAEGRCIK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 383 ArGVG-VIELRGEsLTPGYLTMGGFIPAQDEH-----------GWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPT 450
Cdd:cd05940 282 V-PRGePGLLISR-INPLEPFDGYTDPAATEKkilrdvfkkgdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTT 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 889038433 451 DIERAAGRVDGV---------------RPGCA-VAVRLDAGHSRESFAVAVESN--AFEDPAEVR 497
Cdd:cd05940 360 EVAAVLGAFPGVeeanvygvqvpgtdgRAGMAaIVLQPNEEFDLSALAAHLEKNlpGYARPLFLR 424
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
381-536 |
9.31e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 54.85 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 381 MPARG--VGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGR 458
Cdd:PLN02479 395 VPADGktMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYT 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 459 VDGVRPGCAVAvRLDA--GHSRESFAVAvesnafeDPAEVRRIEHQVAHEVVAEVDVR------PRNvVVLGPgtIPKTP 530
Cdd:PLN02479 475 HPAVLEASVVA-RPDErwGESPCAFVTL-------KPGVDKSDEAALAEDIMKFCRERlpaywvPKS-VVFGP--LPKTA 543
|
....*.
gi 889038433 531 SGKLRR 536
Cdd:PLN02479 544 TGKIQK 549
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
160-456 |
2.84e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 53.17 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 160 TSGSTGSPKAVQITHRNI----YSNA--EAMFVGAQydvdkDVMVSWLPCFHdmgmVGFLTIPM---FFGAELVkvTPMD 230
Cdd:PRK07008 184 TSGTTGNPKGALYSHRSTvlhaYGAAlpDAMGLSAR-----DAVLPVVPMFH----VNAWGLPYsapLTGAKLV--LPGP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 231 FLRDTLLWaKLIDKYQGTMTAA-PNFAYALLakrlrRQAKPGDFDLSTLRFALSGAEPVEPADVEDLLDAgkpFGLRpsa 309
Cdd:PRK07008 253 DLDGKSLY-ELIEAERVTFSAGvPTVWLGLL-----NHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDE---YGVE--- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 310 ILPAYGMAETTLAVSFSECNAglvvdEVDADLLAALRRavpatkgntrRLATLGPLLQDLEARIIDEQGDVMPARGV--G 387
Cdd:PRK07008 321 VIHAWGMTEMSPLGTLCKLKW-----KHSQLPLDEQRK----------LLEKQGRVIYGVDMKIVGDDGRELPWDGKafG 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 889038433 388 VIELRGESLTPGYLTmGGFIPAQDehGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAA 456
Cdd:PRK07008 386 DLQVRGPWVIDRYFR-GDASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVA 451
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
125-437 |
3.03e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 53.44 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 125 LEQKGMQVLTVADLLA------SDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAM------FVGaQYDV 192
Cdd:PTZ00216 231 VDTEGCRLVAWTDVVAkghsagSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALedrlndLIG-PPEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 193 DkDVMVSWLPCFHDMGMvGFLTIPMFFGAELVKVTPM-----------DFL--RDTLLWA--KLIDKYQGTMTA--AP-- 253
Cdd:PTZ00216 310 D-ETYCSYLPLAHIMEF-GVTNIFLARGALIGFGSPRtltdtfarphgDLTefRPVFLIGvpRIFDTIKKAVEAklPPvg 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 254 -------NFAYallAKRLRRQAKPGD--------FDL------STLRFALSGAEPVEPAdVEDLLDAgkPFGLrpsaILP 312
Cdd:PTZ00216 388 slkrrvfDHAY---QSRLRALKEGKDtpywnekvFSApravlgGRVRAMLSGGGPLSAA-TQEFVNV--VFGM----VIQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 313 AYGMAETTlavsfseCNAGlvvdevdadllaalrravpatkgnTRRLATL-----GPLLQDLEARIIDEQG----DVMPA 383
Cdd:PTZ00216 458 GWGLTETV-------CCGG------------------------IQRTGDLepnavGQLLKGVEMKLLDTEEykhtDTPEP 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 889038433 384 RgvGVIELRGESLTPGY-----LTMggfiPAQDEHGWYDTGDLGYLTEEGHVVVCGRVK 437
Cdd:PTZ00216 507 R--GEILLRGPFLFKGYykqeeLTR----EVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
151-495 |
3.05e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 53.31 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLALMQLTSGSTGSPKAVQITHRNI----YSNAEAMFVGAQYDVDKDVMVSWLP------------CFHDMGMVGFLT 214
Cdd:PLN02861 219 KTDICTIMYTSGTTGEPKGVILTNRAIiaevLSTDHLLKVTDRVATEEDSYFSYLPlahvydqvietyCISKGASIGFWQ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 215 IPMFFGAELVKV--------TPMDFLRdtlLWAKLIDKYQ-GTMTAAPNFAYAL------LAKRLRRQAKPGDFDL---- 275
Cdd:PLN02861 299 GDIRYLMEDVQAlkptifcgVPRVYDR---IYTGIMQKISsGGMLRKKLFDFAYnyklgnLRKGLKQEEASPRLDRlvfd 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 276 -------STLRFALSGAEPVePADVEDLLDAgkpfgLRPSAILPAYGMAE------TTLAVSFSecnaglvvdevdadll 342
Cdd:PLN02861 376 kikeglgGRVRLLLSGAAPL-PRHVEEFLRV-----TSCSVLSQGYGLTEscggcfTSIANVFS---------------- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 343 aalrravpatkgntrRLATLGPLLQDLEARI--IDEQG-DVMPARGVGVIELRGESLTPGYLTMGGFIPAQDEHGWYDTG 419
Cdd:PLN02861 434 ---------------MVGTVGVPMTTIEARLesVPEMGyDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTG 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 420 DLGYLTEEGHVVVCGRVKDVIIMA-GRNIYPTDIERAAGRvdgvrpgCA-VAVRLDAGHSRESFAVAV---ESNAFEDPA 494
Cdd:PLN02861 499 DIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTYSR-------CPlIASIWVYGNSFESFLVAVvvpDRQALEDWA 571
|
.
gi 889038433 495 E 495
Cdd:PLN02861 572 A 572
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
153-485 |
1.01e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 51.56 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHRNIYSNAEAM--FVGAQYD--VDKDVMVSWLP-----------CFHDMG-MVGF---- 212
Cdd:PLN02614 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVirLLKSANAalTVKDVYLSYLPlahifdrvieeCFIQHGaAIGFwrgd 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 213 ----------LTIPMFFGAELV----------KVTPMDFLR----DTLLWAKL--IDKYQGTMTAAPNFAYALLAKRlrR 266
Cdd:PLN02614 304 vklliedlgeLKPTIFCAVPRVldrvysglqkKLSDGGFLKkfvfDSAFSYKFgnMKKGQSHVEASPLCDKLVFNKV--K 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 267 QAKPGDfdlstLRFALSGAEPVePADVEDLLDAgkpfgLRPSAILPAYGMAETTlAVSFSEcnaglVVDEVDAdllaalr 346
Cdd:PLN02614 382 QGLGGN-----VRIILSGAAPL-ASHVESFLRV-----VACCHVLQGYGLTESC-AGTFVS-----LPDELDM------- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 347 ravpatkgntrrLATLGPLLQDLEAR---IIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIpaqdeHGWYDT 418
Cdd:PLN02614 438 ------------LGTVGPPVPNVDIRlesVPEMEYDALASTPRGEICIRGKTLFSGYykredLTKEVLI-----DGWLHT 500
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889038433 419 GDLGYLTEEGHVVVCGRVKDVIIMA-GRNIYPTDIERAAGRVDGVRpgcAVAVRldaGHSRESFAVAV 485
Cdd:PLN02614 501 GDVGEWQPNGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVD---SVWVY---GNSFESFLVAI 562
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
151-533 |
1.22e-06 |
|
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: 50.84 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 151 EDDLaLMQLTSGSTGSPKAVQITHRNIYSnaeAMFVGAQYDVDKDVMVSWL----------------PCFHDMGMVGFLT 214
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQEDIFR---MLMGGADFGTGEFTPSEDAhkaaaaaagtvmfpapPLMHGTGSWTAFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 215 IpmFFGAELVkVTPMDFLRDTLLWaKLIDKYQGTMTAAPNFAYAL-LAKRLRRqakPGDFDLSTLRFALSGAEPVEPADV 293
Cdd:cd05924 79 G--LLGGQTV-VLPDDRFDPEEVW-RTIEKHKVTSMTIVGDAMARpLIDALRD---AGPYDLSSLFAISSGGALLSPEVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 294 EDLLDagkpfgLRPSAILP-AYGMAETtlavsfsecnaglvvdevdadllAALRRAVPATKGN-TRRLATLGPLLQdlea 371
Cdd:cd05924 152 QGLLE------LVPNITLVdAFGSSET-----------------------GFTGSGHSAGSGPeTGPFTRANPDTV---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 372 rIIDEQGDVMP--ARGVGVIELRGesLTP-GYL-----TMGGFIPAQDEHgWYDTGDLGYLTEEGHVVVCGRVKDVIIMA 443
Cdd:cd05924 199 -VLDDDGRVVPpgSGGVGWIARRG--HIPlGYYgdeakTAETFPEVDGVR-YAVPGDRATVEADGTVTLLGRGSVCINTG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 444 GRNIYPTDIERAAGRVDGVRpGCAVAVRLDAGHSRESFAVAvesnAFEDPAEVRRIEHQvahEVVAEVDVR---PRNVVV 520
Cdd:cd05924 275 GEKVFPEEVEEALKSHPAVY-DVLVVGRPDERWGQEVVAVV----QLREGAGVDLEELR---EHCRTRIARyklPKQVVF 346
|
410
....*....|...
gi 889038433 521 LgpGTIPKTPSGK 533
Cdd:cd05924 347 V--DEIERSPAGK 357
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
135-440 |
2.76e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 50.12 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 135 VADLLASDPIGPIEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEA-MFVGAQYDvDKDVMVSWLPCFHDMGMVGFL 213
Cdd:PLN02387 233 VEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGvMTVVPKLG-KNDVYLAYLPLAHILELAAES 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 214 TIpMFFGAELVKVTPMDfLRDTllwAKLIDKyqGT-----------MTAAPNF-------------AYALLAKRL----- 264
Cdd:PLN02387 312 VM-AAVGAAIGYGSPLT-LTDT---SNKIKK--GTkgdasalkptlMTAVPAIldrvrdgvrkkvdAKGGLAKKLfdiay 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 265 -RRQAKP-----GDFDLSTL------------------RFALSGAEPVEPaDVEDLLDA--GKPFGlrpsailPAYGMAE 318
Cdd:PLN02387 385 kRRLAAIegswfGAWGLEKLlwdalvfkkiravlggriRFMLSGGAPLSG-DTQRFINIclGAPIG-------QGYGLTE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 319 TTLAVSFSECNaGLVVDEVDADLLAALRRAVPATKGntrrlatlGPLLQDleariideqgDVMPargvgvielRGESLTP 398
Cdd:PLN02387 457 TCAGATFSEWD-DTSVGRVGPPLPCCYVKLVSWEEG--------GYLISD----------KPMP---------RGEIVIG 508
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 889038433 399 GY-LTMGGF--------IPAQDEHG--WYDTGDLGYLTEEGHVVVCGRVKDVI 440
Cdd:PLN02387 509 GPsVTLGYFknqektdeVYKVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIV 561
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
147-453 |
3.49e-06 |
|
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: 49.78 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 147 IEVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVM----VSWLPCFHDMgmvgFLTIpmFFGAE 222
Cdd:cd17656 123 YINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLqfatCSFDVCYQEI----FSTL--LSGGT 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 223 LvKVTPMDFLRDTLLWAKLIDKYQGTMTAAPNFAYALLAKrlRRQAKPGDFDlsTLRFALSGAEPVEpadVEDLLDagKP 302
Cdd:cd17656 197 L-YIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS--EREFINRFPT--CVKHIITAGEQLV---ITNEFK--EM 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 303 FGLRPSAILPAYGMAETTLaVSFSECNAGLVVDEvdadllaalrravpatkgntrrLATLGPLLQDLEARIIDEQGDVMP 382
Cdd:cd17656 267 LHEHNVHLHNHYGPSETHV-VTTYTINPEAEIPE----------------------LPPIGKPISNTWIYILDQEQQLQP 323
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889038433 383 ARGVGVIELRGESLTPGY-----LTMGGFI--PAQDEHGWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIE 453
Cdd:cd17656 324 QGIVGELYISGASVARGYlnrqeLTAEKFFpdPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIE 401
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
148-453 |
3.54e-06 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 49.78 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 148 EVGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDVDKDVmvSWL---PCFHDMG----MVGFLT-IPMFF 219
Cdd:PRK05620 177 ELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHGE--SFLccvPIYHVLSwgvpLAAFMSgTPLVF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 220 -GAELVKVTPMDFLRDTL---------LWAKLIDKYqgtMTAAPnfayallaKRLrrqakpgdfdlsTLRFALSGAEPVE 289
Cdd:PRK05620 255 pGPDLSAPTLAKIIATAMprvahgvptLWIQLMVHY---LKNPP--------ERM------------SLQEIYVGGSAVP 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 290 PAdvedLLDAGKP-FGLRpsaILPAYGMAETTLAVSFSECNAGLvvdevdadllaalrravpatKGNTRRL--ATLGPLL 366
Cdd:PRK05620 312 PI----LIKAWEErYGVD---VVHVWGMTETSPVGTVARPPSGV--------------------SGEARWAyrVSQGRFP 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 367 QDLEARIIDEqGDVMPA--RGVGVIELRGESLTPGYL-----TMGGFIPAQDEH------------GWYDTGDLGYLTEE 427
Cdd:PRK05620 365 ASLEYRIVND-GQVMEStdRNEGEIQVRGNWVTASYYhspteEGGGAASTFRGEdvedandrftadGWLRTGDVGSVTRD 443
|
330 340
....*....|....*....|....*.
gi 889038433 428 GHVVVCGRVKDVIIMAGRNIYPTDIE 453
Cdd:PRK05620 444 GFLTIHDRARDVIRSGGEWIYSAQLE 469
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
117-208 |
1.42e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 47.73 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 117 PFLVAIPILEQKGMQVLTV------------ADLLASDPIGPIE-----VGEDDLALMQLTSGSTGSPKAVQITHRNIYS 179
Cdd:PRK12582 168 PFARALAALDLLDVTVVHVtgpgegiasiafADLAATPPTAAVAaaiaaITPDTVAKYLFTSGSTGMPKAVINTQRMMCA 247
|
90 100 110
....*....|....*....|....*....|..
gi 889038433 180 NAeAMFVGAQYDVDKD---VMVSWLPCFHDMG 208
Cdd:PRK12582 248 NI-AMQEQLRPREPDPpppVSLDWMPWNHTMG 278
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
104-210 |
2.74e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 46.79 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 104 IGMIEAKAVIVSE-----------------PFLVAIPILEQKGMQVLTVADLLASDPIGPIEVGE----DDLALMQLTSG 162
Cdd:PRK08279 130 LNLVDAKHLIVGEelveafeearadlarppRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSgvtaKDTAFYIYTSG 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 889038433 163 STGSPKAVQITHRNI--YSNAEAMFVGAQydvDKDVMVSWLPCFHDMGMV 210
Cdd:PRK08279 210 TTGLPKAAVMSHMRWlkAMGGFGGLLRLT---PDDVLYCCLPLYHNTGGT 256
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
150-536 |
2.76e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.47 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 150 GEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAMFVGAQYDvDKDVMVSWLPCFHDMGMVGFLTIPMfFGAElVKVTPM 229
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALS-EADVIAQTASQSFDISVWQFLAAPL-FGAR-VEIVPN 3943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 230 DFLRD-TLLWAKLIDKYQGTMTAAPNFAYALLAKrlRRQAkpgdfdLSTLRFALSGAEPVEPADVEDLLDAGKPFGLrps 308
Cdd:PRK05691 3944 AIAHDpQGLLAHVQAQGITVLESVPSLIQGMLAE--DRQA------LDGLRWMLPTGEAMPPELARQWLQRYPQIGL--- 4012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 309 aiLPAYGMAETTLAVSFsecnagLVVDevdadlLAALRRA-VP-ATKGNTRRLATLgpllqdleariiDEQGDVMPARGV 386
Cdd:PRK05691 4013 --VNAYGPAECSDDVAF------FRVD------LASTRGSyLPiGSPTDNNRLYLL------------DEALELVPLGAV 4066
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 387 GVIELRGESLTPGYL-----TMGGFIP----AQDEHgWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAG 457
Cdd:PRK05691 4067 GELCVAGTGVGRGYVgdplrTALAFVPhpfgAPGER-LYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLH 4145
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 458 RVDGVRPGcAVAVRlDAGHSRESFAVAVESNAFEDPAEVRrieHQVAHEVVAEVdvrPRNVVVLGPG---TIPKTPSGKL 534
Cdd:PRK05691 4146 EQAEVREA-AVAVQ-EGVNGKHLVGYLVPHQTVLAQGALL---ERIKQRLRAEL---PDYMVPLHWLwldRLPLNANGKL 4217
|
..
gi 889038433 535 RR 536
Cdd:PRK05691 4218 DR 4219
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
444-536 |
3.03e-05 |
|
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: 434024 [Multi-domain] Cd Length: 96 Bit Score: 42.85 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 444 GRNIYPTDIERAAGRVDGVRPgcAVAVRLDAGHSRESFAVAVE--SNAFEDPAEVRRIEHQVAHEVVAEVDVRPRnVVVL 521
Cdd:pfam14535 1 GVNVFPSQIEEVLLEIPGVGP--EYQIIVTREGGLDELEVKVEvaEGFSDEIKDLEALEKRIAKELKSVLGVSVK-VELV 77
|
90
....*....|....*
gi 889038433 522 GPGTIPKTPsGKLRR 536
Cdd:pfam14535 78 EPGTLPRSE-GKAKR 91
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
416-537 |
4.64e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 46.10 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 416 YDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVRPGCAVAVRlDA--GHSRESFAVAVESNAFEDP 493
Cdd:PRK10524 475 YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVK-DAlkGQVAVAFVVPKDSDSLADR 553
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 889038433 494 AEVRRIEHQVAHEVVAEVD--VRPRNVVVlgPGTIPKTPSGK-LRRA 537
Cdd:PRK10524 554 EARLALEKEIMALVDSQLGavARPARVWF--VSALPKTRSGKlLRRA 598
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
109-213 |
2.01e-04 |
|
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: 44.20 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 109 AKAVIVSEPFLVAI----PILEQKGMQVL------------TVADLLASDPIGPI------EVGEDDLALMQLTSGSTGS 166
Cdd:cd05938 79 AKVLVVAPELQEAVeevlPALRADGVSVWylshtsntegviSLLDKVDAASDEPVpaslraHVTIKSPALYIYTSGTTGL 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 889038433 167 PKAVQITH-RNIYSNAEAMFVGAQYDvdkDVMVSWLPCFHDMG-MVGFL 213
Cdd:cd05938 159 PKAARISHlRVLQCSGFLSLCGVTAD---DVIYITLPLYHSSGfLLGIG 204
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
138-537 |
2.73e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 138 LLASDPIGPIE--VGEDDLALMQLTSGSTGSPKAVQITHRNIYSNAEAmfVGAQYDVDKDvmvswlPCFHDMGMVGF--- 212
Cdd:PRK05691 2317 ALAAYSDAPLPflSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQA--VIERFGMRAD------DCELHFYSINFdaa 2388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 213 ---LTIPMFFGAELVkvtpmdfLRDTLLW-----AKLIDKYQGTMTA-APNFAyALLAKRLRRQAkpgdfDLSTLRFALS 283
Cdd:PRK05691 2389 serLLVPLLCGARVV-------LRAQGQWgaeeiCQLIREQQVSILGfTPSYG-SQLAQWLAGQG-----EQLPVRMCIT 2455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 284 GAEPVEPADVEDLLDAgkpfgLRPSAILPAYGMAETTlaVSFSECNAGLVVDEVDAdllaalrrAVPatkgntrrlatLG 363
Cdd:PRK05691 2456 GGEALTGEHLQRIRQA-----FAPQLFFNAYGPTETV--VMPLACLAPEQLEEGAA--------SVP-----------IG 2509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 364 PLLQDLEARIIDEQGDVMPARGVGVIELRGESLTPGY-----LTMGGFIP---AQDEHGWYDTGDLGYLTEEGHVVVCGR 435
Cdd:PRK05691 2510 RVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYhdrpgLTAERFVAdpfAADGGRLYRTGDLVRLRADGLVEYVGR 2589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 436 VKDVIIMAGRNIYPTDIERAAGRVDGVRPgcAVAVRLDAGHSRESFAVAVESNAFEDPAEVRRIEHQVAHEVVAEVD--V 513
Cdd:PRK05691 2590 IDHQVKIRGFRIELGEIESRLLEHPAVRE--AVVLALDTPSGKQLAGYLVSAVAGQDDEAQAALREALKAHLKQQLPdyM 2667
|
410 420
....*....|....*....|....*
gi 889038433 514 RPRNVVVLgpGTIPKTPSGKL-RRA 537
Cdd:PRK05691 2668 VPAHLILL--DSLPLTANGKLdRRA 2690
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
153-534 |
3.53e-04 |
|
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: 43.16 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 153 DLALMQLTSGSTGSPKAVQITHR---NIYSNAEAMFVGAQYDvDKDVMV--SWLPCFHdmgmVGFLTIPMFFGAELVkVT 227
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGsvvNLRTSLSERYFGRDNG-DEAVLFfsNYVFDFF----VEQMTLALLNGQKLV-VP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 228 PMDFLRDTLLWAKLIDKYQ-----GTMTAAPNFAYALLAKrLRRQAKPGDfDLSTLRFAlsgaepvepadvedlldagKP 302
Cdd:cd17648 169 PDEMRFDPDRFYAYINREKvtylsGTPSVLQQYDLARLPH-LKRVDAAGE-EFTAPVFE-------------------KL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 303 FGLRPSAILPAYGMAETTLAVSFSECNAGLVVDEvdadllaALRRAVPATKgntrrLATLGPLLQDLeariideqgdvmP 382
Cdd:cd17648 228 RSRFAGLIINAYGPTETTVTNHKRFFPGDQRFDK-------SLGRPVRNTK-----CYVLNDAMKRV------------P 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 383 ARGVGVIELRGESLTPGY-----LTMGGFIP-----AQDEHG-----WYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNI 447
Cdd:cd17648 284 VGAVGELYLGGDGVARGYlnrpeLTAERFLPnpfqtEQERARgrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 448 YPTDIERAAGRVDGVRPgCAVAVRLDAGHSREsfavavesnafedpaevRRIEHQVAH-----EVVAEVDVR-------P 515
Cdd:cd17648 364 EPGEVEAALASYPGVRE-CAVVAKEDASQAQS-----------------RIQKYLVGYylpepGHVPESDLLsflraklP 425
|
410 420
....*....|....*....|..
gi 889038433 516 RNVV---VLGPGTIPKTPSGKL 534
Cdd:cd17648 426 RYMVparLVRLEGIPVTINGKL 447
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
414-536 |
1.17e-03 |
|
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: 41.78 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889038433 414 GWYDTGDLGYLTEEGHVVVCGRVKDVIIMAGRNIYPTDIERAAGRVDGVrPGCAVAVRLDA--GHSRESFAVAVESNAFE 491
Cdd:cd05966 469 GYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAV-AEAAVVGRPHDikGEAIYAFVTLKDGEEPS 547
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 889038433 492 DP--AEVRrieHQVAHEV--VAevdvRPRNVVVlGPGtIPKTPSGK-LRR 536
Cdd:cd05966 548 DElrKELR---KHVRKEIgpIA----TPDKIQF-VPG-LPKTRSGKiMRR 588
|
|
| |
