|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1-577 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 882.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 1 MSRFVDTLVATAtkRGQQRGMVTGEPKEPVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAG 80
Cdd:PRK07768 1 MSRFTEKMYANA--RTSPRGMVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 81 GSVTMLHQPTPRTDLAEWAEDTVRVLGMIGSDqdalggpgglaprpgsgagprnvTVLLGEPFDQLAPVLEQKGIGFQLI 160
Cdd:PRK07768 79 ASLTMLHQPTPRTDLAVWAEDTLRVIGMIGAK-----------------------AVVVGEPFLAAAPVLEEKGIRVLTV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 161 TELAAAEPlPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSWLPTFHDMGMVGFLT 240
Cdd:PRK07768 136 ADLLAADP-IDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 241 VPMTFGVELVKITPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQ 320
Cdd:PRK07768 215 VPMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKPGAFDLSSLRFALNGAEPIDPADVE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 321 TFVDAGARFKMPAECVFPAYGMAEATLAVSFAPLFTGLTLDVVEADALEAENRAVPVPEGdprrgtdGVRSFALLGRPLD 400
Cdd:PRK07768 295 DLLDAGARFGLRPEAILPAYGMAEATLAVSFSPCGAGLVVDEVDADLLAALRRAVPATKG-------NTRRLATLGPPLP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 401 GLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYLVD-GQIVICGRRKDVIIMGGRNL 479
Cdd:PRK07768 368 GLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEeGEVVVCGRVKDVIIMAGRNI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 480 YPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVRDAVDMRPYAVVVLPAGSLP 559
Cdd:PRK07768 448 YPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIP 527
|
570
....*....|....*...
gi 300790052 560 KTPSGKVKRAATAQQFAD 577
Cdd:PRK07768 528 KTPSGKLRRANAAELVTP 545
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
20-577 |
4.36e-174 |
|
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: 504.47 E-value: 4.36e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 20 GMVTGEPKEPVRRTWAEVHEEARRIAGGLVAGGfERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRtdlaEWA 99
Cdd:cd05931 13 TFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPG----RHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 100 EDTVRVLGmigsdqDAlgGPGGLAPRPGSGAGPRNVTVLLgepfdqlapvlEQKGIGFQLITELAAAEPLPDVVVT--DE 177
Cdd:cd05931 88 ERLAAILA------DA--GPRVVLTTAAALAAVRAFAASR-----------PAAGTPRLLVVDLLPDTSAADWPPPspDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 178 GDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFGVELVKITPVEF 257
Cdd:cd05931 149 DDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPG-DVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 258 LSGPLIWPELITKYHGTTTAAPNFAYAIVGRRMARVDEDDaYDLSKLRIALNGAEPIDETAVQTFVDAGARFKMPAECVF 337
Cdd:cd05931 228 LRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEG-LDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 338 PAYGMAEATLAVSFAPLFTGLTLDVVEADALEaeNRAVPVPEGDPrrgtdGVRSFALLGRPLDGLEAEIVDDAGKR-VDE 416
Cdd:cd05931 307 PSYGLAEATLFVSGGPPGTGPVVLRVDRDALA--GRAVAVAADDP-----AARELVSCGRPLPDQEVRIVDPETGReLPD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 417 REVGEIRLRGEAVTPGYLTMD-------GPLATQDEDGWLNTGDLGYLVDGQIVICGRRKDVIIMGGRNLYPTDIERAAT 489
Cdd:cd05931 380 GEVGEIWVRGPSVASGYWGRPeataetfGALAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 490 SVEGV-RAGNAVAVRLDAGSrRERFAVVLESKLAGDAEAEKNLMKQVSARVRDAVDMRPYAVVVLPAGSLPKTPSGKVKR 568
Cdd:cd05931 460 EAHPAlRPGCVAAFSVPDDG-EERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQR 538
|
....*....
gi 300790052 569 AATAQQFAD 577
Cdd:cd05931 539 RACRAAYLD 547
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
30-574 |
8.67e-104 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 323.26 E-value: 8.67e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 30 VRRTWAEVHEEARRIAGGLVAGGfeRGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDTVRVLGMI 109
Cdd:PRK05851 30 RRHPWPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAAVSILPGPVRGADDGRWADATLTRFAGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 GSDqdalggpgglaprpgsgagprnvTVL-LGEPFDQLAPVleQKGIGFQLITELAAAEPLPDVVVTDEGDTALLQLTSG 188
Cdd:PRK05851 108 GVR-----------------------TVLsHGSHLERLRAV--DSSVTVHDLATAAHTNRSASLTPPDSGGPAVLQGTAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 189 STADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSWLPTFHDMGMVGFLTVPMTfGVELVKITPVEFLSGPLIWPELI 268
Cdd:PRK05851 163 STGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAFLLTAALA-GAPLWLAPTTAFSASPFRWLSWL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 269 TKYHGTTTAAPNFAYAIVGRRMARVDEddaYDLSKLRIALNGAEPIDETAVQTFVDAGARFKMPAECVFPAYGMAEATLA 348
Cdd:PRK05851 242 SDSRATLTAAPNFAYNLIGKYARRVSD---VDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAESTCA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 349 VSFAPLFTGLTLDVVEADAleaenravpvpegdprrgTDGVRSFALLGRPLDGLEAEIVDDAGKR-VDEREVGEIRLRGE 427
Cdd:PRK05851 319 VTVPVPGIGLRVDEVTTDD------------------GSGARRHAVLGNPIPGMEVRISPGDGAAgVAGREIGEIEIRGA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 428 AVTPGYLTMDgPLatqDEDGWLNTGDLGYLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAG 507
Cdd:PRK05851 381 SMMSGYLGQA-PI---DPDDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEG 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300790052 508 SRRERFAVVLESKLAGDAEAEKNLMKQVSARvrdaVDMRPYAVVVLPAGSLPKTPSGKVKRAATAQQ 574
Cdd:PRK05851 457 SARPGLVIAAEFRGPDEAGARSEVVQRVASE----CGVVPSDVVFVAPGSLPRTSSGKLRRLAVKRS 519
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
34-575 |
5.97e-100 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 315.02 E-value: 5.97e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 34 WAEVHEEARRIAGGLVAGGFERGTAVGvlaaapvLIAPT----VQAVW---LAGGSVTMLHQPTPRTDLAEWAEdtvRVL 106
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVA-------LIAETdgdfVEAFFacqYAGLVPVPLPLPMGFGGRESYIA---QLR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 107 GMIGSDQ-DALGGPGGLAPRPGSGAGPRN-VTVLLGEPFDQLApvleqkgigfqlitelAAAEPLPDVvvtDEGDTALLQ 184
Cdd:PRK09192 122 GMLASAQpAAIITPDELLPWVNEATHGNPlLHVLSHAWFKALP----------------EADVALPRP---TPDDIAYLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 185 LTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSWLPTFHDMGMVGFLTVPMTFGVELVKITPVEFLSGPLIW 264
Cdd:PRK09192 183 YSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 265 PELITKYHGTTTAAPNFAYAIVGRRMARVDEDDaYDLSKLRIALNGAEPIDETAVQTFVDAGARFKMPAECVFPAYGMAE 344
Cdd:PRK09192 263 LDLISRNRGTISYSPPFGYELCARRVNSKDLAE-LDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 345 ATLAVSFAPLFTGLTLDVVEADALEAENRAVPvPEGDPRRgtdgVRSFALLGRPLDGLEAEIVDDAGKRVDEREVGEIRL 424
Cdd:PRK09192 342 ATLAVSFSPLGSGIVVEEVDRDRLEYQGKAVA-PGAETRR----VRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 425 RGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRL 504
Cdd:PRK09192 417 RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAFSI 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300790052 505 DAGSrRERFAVVLESKLaGDAEAEKNLMKQVSARVRDAVDMrPYAVVVLPAGSLPKTPSGKVKRAATAQQF 575
Cdd:PRK09192 497 AQEN-GEKIVLLVQCRI-SDEERRGQLIHALAALVRSEFGV-EAAVELVPPHSLPRTSSGKLSRAKAKKRY 564
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-578 |
1.07e-84 |
|
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: 271.30 E-value: 1.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 4 FVDTLVATATKRGQQRGMVTGEpkepVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSV 83
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGG----RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 84 TMLHQPTPRTDLAEWAEDtvrvlgmigsdqdalggpgglaprpgsgAGPRnvtvllgepfdqlapvleqkgigfqlitel 163
Cdd:COG0318 77 VPLNPRLTAEELAYILED----------------------------SGAR------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 164 aaaeplpdVVVTdegdtALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPM 243
Cdd:COG0318 99 --------ALVT-----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPG-DVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 244 TFGVELV---KITPVEFLsgpliwpELITKYHGT-TTAAPNFAYaivgrRMARVDEDDAYDLSKLRIALNGAEPIDETAV 319
Cdd:COG0318 165 LAGATLVllpRFDPERVL-------ELIERERVTvLFGVPTMLA-----RLLRHPEFARYDLSSLRLVVSGGAPLPPELL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 320 QTFVDagaRFKMPaecVFPAYGMAEATLAVSFAPlftgltldvveadaleaenravpVPEGDPRRGTdgvrsfalLGRPL 399
Cdd:COG0318 233 ERFEE---RFGVR---IVEGYGLTETSPVVTVNP-----------------------EDPGERRPGS--------VGRPL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 400 DGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYLV-DGQIVICGRRKDVIIMGGRN 478
Cdd:COG0318 276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDeDGYLYIVGRKKDMIISGGEN 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 479 LYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAeknLMKQVSARVRDAvdMRPYAVVVLPAgsL 558
Cdd:COG0318 356 VYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEE---LRAFLRERLARY--KVPRRVEFVDE--L 428
|
570 580
....*....|....*....|
gi 300790052 559 PKTPSGKVKRAATAQQFADR 578
Cdd:COG0318 429 PRTASGKIDRRALRERYAAG 448
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
159-575 |
2.52e-81 |
|
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: 263.97 E-value: 2.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 159 LITELAAAEPLPDVVvtdegdtALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGF 238
Cdd:cd05908 94 LITEEEVLCELADEL-------AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK-DRILSWMPLTHDMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 239 LTVPMTFGVELVKITPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGRRMARVDEDDaYDLSKLRIALNGAEPIDETA 318
Cdd:cd05908 166 HLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKAND-WDLSSIRMILNGAEPIDYEL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 319 VQTFVDAGARFKMPAECVFPAYGMAEATLAVSFAPL---FTGLTLDvveadaLEAENRAVPVPEGDpRRGTDGVRsFALL 395
Cdd:cd05908 245 CHEFLDHMSKYGLKRNAILPVYGLAEASVGASLPKAqspFKTITLG------RRHVTHGEPEPEVD-KKDSECLT-FVEV 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYltMDGPLATQD---EDGWLNTGDLGYLVDGQIVICGRRKDVI 472
Cdd:cd05908 317 GKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGY--YNNPEATAKvftDDGWLKTGDLGFIRNGRLVITGREKDII 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 473 IMGGRNLYPTDIERAATSVEGVRAGNAVAVRL-DAGSRRER-FAVVLESKLAGD-AEAEKNLMKQVSARVRDAVDMrpya 549
Cdd:cd05908 395 FVNGQNVYPHDIERIAEELEGVELGRVVACGVnNSNTRNEEiFCFIEHRKSEDDfYPLGKKIKKHLNKRGGWQINE---- 470
|
410 420
....*....|....*....|....*.
gi 300790052 550 vvVLPAGSLPKTPSGKVKRAATAQQF 575
Cdd:cd05908 471 --VLPIRRIPKTTSGKVKRYELAQRY 494
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
8-575 |
3.84e-77 |
|
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: 254.13 E-value: 3.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 8 LVATATKRGQQRGMVT-GEPKEPVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTML 86
Cdd:cd05906 15 LLLRAAERGPTKGITYiDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 87 hqPTPRTDlaEWAEDTVRVLgmigsdqdalggpgglaprpgsgagpRNVTVLLGEPF--------DQLAPVLEQKGI-GF 157
Cdd:cd05906 95 --TVPPTY--DEPNARLRKL--------------------------RHIWQLLGSPVvltdaelvAEFAGLETLSGLpGI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 158 QLIT--ELAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGM 235
Cdd:cd05906 145 RVLSieELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ-DVFLNWVPLDHVGGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 236 VGFLTVPMTFGVELVKITPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGRRMARvDEDDAYDLSKLRIALNGAEPID 315
Cdd:cd05906 224 VELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEE-IEDGTWDLSSLRYLVNAGEAVV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 316 ETAVQTFVDAGARFKMPAECVFPAYGMAEaTLAvsfaplftGLTLDVVeadaleaenravpvpegDPRRGTDGVRSFALL 395
Cdd:cd05906 303 AKTIRRLLRLLEPYGLPPDAIRPAFGMTE-TCS--------GVIYSRS-----------------FPTYDHSQALEFVSL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQD---EDGWLNTGDLGYLVDGQIVICGRRKDVI 472
Cdd:cd05906 357 GRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYY--NNPEANAEaftEDGWFRTGDLGFLDNGNLTITGRTKDTI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 473 IMGGRNLYPTDIERAATSVEGVRAG--NAVAVRlDAGSRRERFAVVLESKLAGDAEAEKnLMKQVSARVRDAVDMRPYAV 550
Cdd:cd05906 435 IVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVR-DPGAETEELAIFFVPEYDLQDALSE-TLRAIRSVVSREVGVSPAYL 512
|
570 580
....*....|....*....|....*
gi 300790052 551 VVLPAGSLPKTPSGKVKRAATAQQF 575
Cdd:cd05906 513 IPLPKEEIPKTSLGKIQRSKLKAAF 537
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
176-577 |
3.35e-66 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 235.06 E-value: 3.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 176 DEGDTALLQLTSGSTADPKAVRITYGNLYSNvkAMVERAEFDFDV---DVMVSWLPTFHDMGMVGFLTVPMTFGVELVKI 252
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVAN--EQLIRHGFGIDLnpdDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 253 TPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGrrmARVDED--DAYDLSKLRIALNGAEPIDETAVQTFVDAGARFK 330
Cdd:PRK05691 242 SPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCS---ERVSESalERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 331 MPAECVFPAYGMAEATLAVSFAPLFTGLTLDVVEADALeAENRAVPvPEGDPRRGTdgvrsfallGRPLDGLEAEIVDDA 410
Cdd:PRK05691 319 FDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEAL-ARNRAEP-GTGSVLMSC---------GRSQPGHAVLIVDPQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 411 -GKRVDEREVGEIRLRGEAVTPGYLTmdGPLATQ----DEDG--WLNTGDLGYLVDGQIVICGRRKDVIIMGGRNLYPTD 483
Cdd:PRK05691 388 sLEVLGDNRVGEIWASGPSIAHGYWR--NPEASAktfvEHDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQD 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 484 IERAATS-VEGVRAGN--AVAVRLDAgsrRERFAVVLE-SKLAGDAEAEKNLMKQVSARVRDAVDMRPYAVVVLPAGSLP 559
Cdd:PRK05691 466 IEKTVEReVEVVRKGRvaAFAVNHQG---EEGIGIAAEiSRSVQKILPPQALIKSIRQAVAEACQEAPSVVLLLNPGALP 542
|
410
....*....|....*...
gi 300790052 560 KTPSGKVKRAATAQQFAD 577
Cdd:PRK05691 543 KTSSGKLQRSACRLRLAD 560
|
|
| FadD32_Coryne |
NF040633 |
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ... |
178-577 |
3.54e-62 |
|
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: 216.06 E-value: 3.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 178 GDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDvMVSWLPTFHDMGMV--GFLTVpmtFGVELVKITPV 255
Cdd:NF040633 201 DDTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLR-LVSWLPLHHDMGIIlaAFVTI---LGLEFELMSPR 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 256 EFLSGPLIWPELITKYHG---TTTAAPNFAYAIVGrRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGARFKMP 332
Cdd:NF040633 277 DFIQQPKRWVDQLSRREDdvnVYTVVPNFALELAA-RYANPEEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLR 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 333 AECVFPAYGMAEATLAVSFA-----PLFTgltldVVEADALeAENRAVPVPEGDPrrgtDGVrSFALLGRPLDGLEAEIV 407
Cdd:NF040633 356 RTALRPSYGLAEASLLVTTPqteerPLFT-----YFDREAL-AEGRAVEVAEDSE----NAV-PFASNGQVVRPQVLAIV 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 408 DDA-GKRVDEREVGEIRLRGEAVTPGYL------------TMDGPLATQD------EDGWLNTGDLGYLVDGQIVICGRR 468
Cdd:NF040633 425 DPEtGQELPDGTVGEIWVHGDNMAAGYLdreeetaetfrnTLGERLAENSraegapEDNWMATGDLGVIVDGELYITGRL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 469 KDVIIMGGRNLYPTDIERAA-TSVEGVRAGnAVAVRLDAGSRRERFAVVLESKL----AGDAEAEknlmKQVSARVRDAV 543
Cdd:NF040633 505 KDLIVIAGRNHYPQDIEATVqEASDHIRPD-SVAAFAVPGDDVEKLVILAERDDeadeSGDAEAI----EAIRAAVTSAH 579
|
410 420 430
....*....|....*....|....*....|....
gi 300790052 544 DMRPYAVVVLPAGSLPKTPSGKVKRAATAQQFAD 577
Cdd:NF040633 580 GVVPADIRIVAPGEIARSSSGKIARRVNAKAYLE 613
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
179-567 |
1.29e-61 |
|
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: 207.14 E-value: 1.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHdMGMVGFLTVPMTFGVELVKITPVEfl 258
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEG-DVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPKFD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 259 sgPLIWPELITKYHGTTTAAPNFAYaivgRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFVdagARFKMPaecVFP 338
Cdd:cd04433 77 --PEAALELIEREKVTILLGVPTLL----ARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFE---EAPGIK---LVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 339 AYGMAEATLAVSFAPlftgltldvveadaleaenravpVPEGDPRRGTdgvrsfalLGRPLDGLEAEIVDDAGKRVDERE 418
Cdd:cd04433 145 GYGLTETGGTVATGP-----------------------PDDDARKPGS--------VGRPVPGVEVRIVDPDGGELPPGE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 419 VGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAg 497
Cdd:cd04433 194 IGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE- 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300790052 498 nAVAVRLDAGSRRERFAVVLESKLAGDAEAEknlmkQVSARVRDavDMRPYAV--VVLPAGSLPKTPSGKVK 567
Cdd:cd04433 273 -AAVVGVPDPEWGERVVAVVVLRPGADLDAE-----ELRAHVRE--RLAPYKVprRVVFVDALPRTASGKID 336
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
173-577 |
1.31e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 214.98 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 173 VVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLtVPMTFGVELVKI 252
Cdd:PRK07769 175 PEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEG-DRGVSWLPFFHDMGLITVL-LPALLGHYITFM 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 253 TPVEFLSGPLIW-PELITKYH---GTTTAAPNFAYAIVGRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGAR 328
Cdd:PRK07769 253 SPAAFVRRPGRWiRELARKPGgtgGTFSAAPNFAFEHAAARGLPKDGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFAP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 329 FKMPAECVFPAYGMAEATLAVSFAPLFTGLTLDVVEADALeAENRAVPVPEGDPRR------GTDGVRSFALlgrpldgl 402
Cdd:PRK07769 333 YGLPPTAIKPSYGMAEATLFVSTTPMDEEPTVIYVDRDEL-NAGRFVEVPADAPNAvaqvsaGKVGVSEWAV-------- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 403 eaeIVD-DAGKRVDEREVGEIRLRGEAVTPGYL------------TMDGPLA------TQDEDGWLNTGDLGYLVDGQIV 463
Cdd:PRK07769 404 ---IVDpETASELPDGQIGEIWLHGNNIGTGYWgkpeetaatfqnILKSRLSeshaegAPDDALWVRTGDYGVYFDGELY 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 464 ICGRRKDVIIMGGRNLYPTDIERAA-TSVEGVRAGNAVA-------------------VRLDAGSRRERFAVVLEsKLAG 523
Cdd:PRK07769 481 ITGRVKDLVIIDGRNHYPQDLEYTAqEATKALRTGYVAAfsvpanqlpqvvfddshagLKFDPEDTSEQLVIVAE-RAPG 559
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 300790052 524 DAEAEknlMKQVSARVRDAVDMR----PYAVVVLPAGSLPKTPSGKVKRAATAQQFAD 577
Cdd:PRK07769 560 AHKLD---PQPIADDIRAAIAVRhgvtVRDVLLVPAGSIPRTSSGKIARRACRAAYLD 614
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
170-575 |
5.89e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 211.72 E-value: 5.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 170 PDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDV-----MVSWLPTFHDMGMVGFLTVPMT 244
Cdd:PRK05850 152 SDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYFGDTGGVPppdttVVSWLPFYHDMGLVLGVCAPIL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 245 FGVELVKITPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGRRMArvDEDDA-YDLSKLRIALNGAEPIDETAVQTFV 323
Cdd:PRK05850 232 GGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTS--DDDMAgLDLGGVLGIISGSERVHPATLKRFA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 324 DAGARFKMPAECVFPAYGMAEATLAVSFAPlfTGLTLDVVEADALE-AENRAVPVPEGDprrGTDGVRsfalLGRPLDGL 402
Cdd:PRK05850 310 DRFAPFNLRETAIRPSYGLAEATVYVATRE--PGQPPESVRFDYEKlSAGHAKRCETGG---GTPLVS----YGSPRSPT 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 403 eAEIVD-DAGKRVDEREVGEIRLRGEAVTPGYL------------TMDGPLATQDEDGWLNTGDLGYLVDGQIVICGRRK 469
Cdd:PRK05850 381 -VRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWqkpeetertfgaTLVDPSPGTPEGPWLRTGDLGFISEGELFIVGRIK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 470 DVIIMGGRNLYPTDIEraATsVEGVRAGNAVAVRLDAGSrRERFAVVLESKLAGDAEAE-----KNLMKQVSARVRDAVD 544
Cdd:PRK05850 460 DLLIVDGRNHYPDDIE--AT-IQEITGGRVAAISVPDDG-TEKLVAIIELKKRGDSDEEamdrlRTVKREVTSAISKSHG 535
|
410 420 430
....*....|....*....|....*....|.
gi 300790052 545 MRPYAVVVLPAGSLPKTPSGKVKRAATAQQF 575
Cdd:PRK05850 536 LSVADLVLVAPGSIPITTSGKIRRAACVEQY 566
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
176-577 |
3.54e-57 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 202.28 E-value: 3.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 176 DEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFdFDVDVM-VSWLPTFHDMG--MVGFltvPMTFGVELVKI 252
Cdd:PRK12476 191 DTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDL-LDRNTHgVSWLPLYHDMGlsMIGF---PAVYGGHSTLM 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 253 TPVEFLSGPLIWPELIT---KYHGTTTAAPNFAYAIVGRRmARVDEDDAYDLSKLrIALNGAEPIDETAVQTFVDAGARF 329
Cdd:PRK12476 267 SPTAFVRRPQRWIKALSegsRTGRVVTAAPNFAYEWAAQR-GLPAEGDDIDLSNV-VLIIGSEPVSIDAVTTFNKAFAPY 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 330 KMPAECVFPAYGMAEATLAVSFAPLFTGLTLDVVEADALEAeNRAVPVPEGDPRrgtdgVRSFALLGRPLDGLEAEIVD- 408
Cdd:PRK12476 345 GLPRTAFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGA-GRAVRVAADAPN-----AVAHVSCGQVARSQWAVIVDp 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 409 DAGKRVDEREVGEIRLRGEAVTPGY--------LTMDGPLATQDEDG-----------WLNTGDLGYLVDGQIVICGRRK 469
Cdd:PRK12476 419 DTGAELPDGEVGEIWLHGDNIGRGYwgrpeeteRTFGAKLQSRLAEGshadgaaddgtWLRTGDLGVYLDGELYITGRIA 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 470 DVIIMGGRNLYPTDIE-RAATSVEGVRAGNAVAVRLDaGSRRERFAVVLEsKLAGDAEAEKN-LMKQVSARVRDAVDMRP 547
Cdd:PRK12476 499 DLIVIDGRNHYPQDIEaTVAEASPMVRRGYVTAFTVP-AEDNERLVIVAE-RAAGTSRADPApAIDAIRAAVSRRHGLAV 576
|
410 420 430
....*....|....*....|....*....|
gi 300790052 548 YAVVVLPAGSLPKTPSGKVKRAATAQQFAD 577
Cdd:PRK12476 577 ADVRLVPAGAIPRTTSGKLARRACRAQYLD 606
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
28-475 |
8.85e-56 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 193.68 E-value: 8.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 28 EPVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAA--APVLIAptVQAVWLAGG-SVTMLHQPTPRtDLAEWAEDT-V 103
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPnsPEWVVA--FLACLKAGAvYVPLNPRLPAE-ELAYILEDSgA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 104 RVLgmIGSDQDALGGpggLAPRPGSGAGPRNVTVLLGEPFDQLAPVLEqkgigfqliTELAAAEPLPDVVVTDEGDTALL 183
Cdd:pfam00501 95 KVL--ITDDALKLEE---LLEALGKLEVVKLVLVLDRDPVLKEEPLPE---------EAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 184 QLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDV---DVMVSWLPTFHDMGMVGFLTVPMTFGVELVKITPVEFLSg 260
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLgpdDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 261 PLIWPELITKYHGTTTAAPNFAYaivgRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGARfkmpaeCVFPAY 340
Cdd:pfam00501 240 PAALLELIERYKVTVLYGVPTLL----NMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG------ALVNGY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 341 GMAEATLAVSFAPlftgltldvveadaleaenravPVPEGDPRRGTdgvrsfalLGRPLDGLEAEIVDDA-GKRVDEREV 419
Cdd:pfam00501 310 GLTETTGVVTTPL----------------------PLDEDLRSLGS--------VGRPLPGTEVKIVDDEtGEPVPPGEP 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 420 GEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGDLGYLV-DGQIVICGRRKDVIIMG 475
Cdd:pfam00501 360 GELCVRGPGVMKGYL--NDPELTAeafDEDGWYRTGDLGRRDeDGYLEIVGRKKDQIKLG 417
|
|
| FAAL_FadD32 |
NF038339 |
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ... |
165-577 |
3.22e-52 |
|
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: 189.16 E-value: 3.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 165 AAEPLPDVV-------VTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMvg 237
Cdd:NF038339 157 AVDAVPDSVgstwvrpDADLDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDEN-SRGVTWLPLFHDMGL-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 238 fLTV--PMTFGVELVKITPVEFLSGPLIW-PELITK--YHGTTTAAPNFAYAIVGRRmARVDEDDAYDLSKLRIALNGAE 312
Cdd:NF038339 234 -LTVilPALGGKYITIMSPAAFVRRPGRWiRELAAVsdGAGTFAAAPNFAFEHAAAR-GLPKEGEPLDLSNVIGLINGSE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 313 PIDETAVQTFVDAGARFKMPAECVFPAYGMAEATLAVSFAPLFTGLTLDVVEADALEAeNRAVPVPEGDPrrgtDGVRSF 392
Cdd:NF038339 312 PVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAKVIYVDREELNA-GRIVEVDPDAP----NAVAQV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 393 AlLGRPLDGLEAEIVD-DAGKRVDEREVGEIRLRGEAVTPGYL--------TMDGPLATQDEDG-----------WLNTG 452
Cdd:NF038339 387 S-CGYVARSQWAVIVDpETGTELPDGQVGEIWLHGNNIGTGYWgrpeeteeTFHNKLKSRLEEGshaegapedanWMRTG 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 453 DLGYLVDGQIVICGRRKDVIIMGGRNLYPTDIER--------------AATSV------EGVRAGNAVAVRLDAGSRRER 512
Cdd:NF038339 466 DYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYsaqeaskalrpgfvAAFSVpanqlpAEVFENSHSGLKYDADDSSEQ 545
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300790052 513 FAVVLEsKLAGDAEAEKnlmKQVSARVRDAVDMR----PYAVVVLPAGSLPKTPSGKVKRAATAQQFAD 577
Cdd:NF038339 546 LVIVAE-RAPGAGKADP---QPIADAVRAAIAVRhgvtVRDVLLVPAGSIPRTSSGKIARRACKAAYID 610
|
|
| FAAL_FadD21 |
NF038337 |
fatty-acid--AMP ligase FAAL21/FadD21; |
170-575 |
1.09e-49 |
|
fatty-acid--AMP ligase FAAL21/FadD21;
Pssm-ID: 439631 [Multi-domain] Cd Length: 579 Bit Score: 181.23 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 170 PDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVerAEFDFDVD-------VMVSWLPTFHDMGMVGFLTVP 242
Cdd:NF038337 155 PSIRISDAPSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLM--AAYFPDTNgvaprdtTIVSWLPFYHDMGLVLGVIAP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 243 MTFGVELVKITPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGRRMARVDEDDAyDLSKLRIALNGAEPIDETAVQTF 322
Cdd:NF038337 233 ILGGYRSELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAVRKTTDADLAGL-DLGNVIGIVSGAERIHPATLDRF 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 323 VDAGARFKMPAECVFPAYGMAEATLAVsfaplftgltldvveadALEAENRAVPVPEGDPRRGTDGV--RSFALLGRPLD 400
Cdd:NF038337 312 CKRFAPYNFREDMMQPSYGLAEATVYV-----------------ASRAEGGAPEVVHFEPEKLSEGSaqRCEARTGSPLL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 401 GLEA------EIVD-DAGKRVDEREVGEIRLRGEAVTPGYL------------TMDGPLATQDEDGWLNTGDLGYLVDGQ 461
Cdd:NF038337 375 SYGTptsptvRIVDpDTCIECPAGTVGEIWVHGDNVAEGYWqkpeetrrtfggVLANPSPGTPEGPWLRTGDLGFISEDE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 462 IVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGnAVAVRLDagsRRERFAVVLESKLAGDAEAEKN-----LMKQVS 536
Cdd:NF038337 455 MFIVGRMKDLLIVYGRNHYPEDIESTVQEITGGRVA-AISVPVD---ETEKLVTIIELKKRGDSDEEAMrkldaVKNNVT 530
|
410 420 430
....*....|....*....|....*....|....*....
gi 300790052 537 ARVRDAVDMRPYAVVVLPAGSLPKTPSGKVKRAATAQQF 575
Cdd:NF038337 531 AAISRSHGLNVADLVLVPPGSIPTTTSGKIRRAACVEQY 569
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
30-568 |
1.15e-47 |
|
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: 173.13 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 30 VRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLA--AAPVLIAptVQAVWLAGGSVTMLH-QPTPRtDLAEWAEDtvrvl 106
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLpnCPQFPIA--YFGALKAGAVVVPLNpLYTPR-ELEHILND----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 107 gmigsdqdalggpgglaprpgSGAgprnVTVLLGEPFDQLapvleqkgigfqliteLAAAEPLPDVVVTDEGDTALLQLT 186
Cdd:cd05936 95 ---------------------SGA----KALIVAVSFTDL----------------LAAGAPLGERVALTPEDVAVLQYT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 187 SGSTADPKAVRITYGNLYSNVKAMVERAEFDFDV-DVMVSWLPTFHDMGMVGFLTVPMTFGVELVKIT---PVEFLsgpl 262
Cdd:cd05936 134 SGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGdDVVLAALPLFHVFGLTVALLLPLALGATIVLIPrfrPIGVL---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 263 iwpELITKYHGTTTAAPNFAYAIvgrrMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFvdaGARFKMPaecVFPAYGM 342
Cdd:cd05936 210 ---KEIRKHRVTIFPGVPTMYIA----LLNAPEFKKRDFSSLRLCISGGAPLPVEVAERF---EELTGVP---IVEGYGL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 343 AEATLAVSFAPlftgltldvveadaleaenravpvPEGDPRRGTdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEI 422
Cdd:cd05936 277 TETSPVVAVNP------------------------LDGPRKPGS--------IGIPLPGTEVKIVDDDGEELPPGEVGEL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 423 RLRGEAVTPGYLTMdgPLATQD--EDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNA 499
Cdd:cd05936 325 WVRGPQVMKGYWNR--PEETAEafVDGWLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAV 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300790052 500 VAVRLDAGSRRERFAVVLESklaGDAEAEKNLMKQvsARVRDAVDMRPYAVVVLPAgsLPKTPSGKVKR 568
Cdd:cd05936 403 VGVPDPYSGEAVKAFVVLKE---GASLTEEEIIAF--CREQLAGYKVPRQVEFRDE--LPKSAVGKILR 464
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
30-566 |
1.29e-43 |
|
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: 161.24 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 30 VRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGgsvTMLHQPTPRTDLAEWAEdtvrvlgmI 109
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLG---AVFVPLNFRLTPPEVAY--------I 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 GSDQDAlggpgglaprpgsgagprnvTVLLGepfdqlapvleqkgigfqlitelaaaeplpdvvvtdegDTALLQLTSGS 189
Cdd:cd17631 88 LADSGA--------------------KVLFD--------------------------------------DLALLMYTSGT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 190 TADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFGVELV---KITPVEFLSgpliwpe 266
Cdd:cd17631 110 TGRPKGAMLTHRNLLWNAVNALAALDLGPD-DVLLVVAPLFHIGGLGVFTLPTLLRGGTVVilrKFDPETVLD------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 267 LITKYHGTTT-AAPNFAYAivgrrMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGARFKMpaecvfpAYGMAEA 345
Cdd:cd17631 182 LIERHRVTSFfLVPTMIQA-----LLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQ-------GYGMTET 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 346 TLAVSFAPlftgltldvvEADALEaenravpvpegdpRRGTdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLR 425
Cdd:cd17631 250 SPGVTFLS----------PEDHRR-------------KLGS--------AGRPVFFVEVRIVDPDGREVPPGEVGEIVVR 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 426 GEAVTPGYLtmDGPLATQD--EDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRagnAVAV 502
Cdd:cd17631 299 GPHVMAGYW--NRPEATAAafRDGWFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVA---EVAV 373
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 503 rldAGSRRERF------AVVLESklaGDAEAEKNLMKQVSARVrdAVDMRPYAVVVLPAgsLPKTPSGKV 566
Cdd:cd17631 374 ---IGVPDEKWgeavvaVVVPRP---GAELDEDELIAHCRERL--ARYKIPKSVEFVDA--LPRNATGKI 433
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
163-577 |
1.68e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 157.27 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 163 LAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMvGFLTVP 242
Cdd:PRK06187 152 LAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRD-DVYLVIVPMFHVHAW-GLPYLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 243 MTFGVELVkiTPVEFLSGPLIwpELITKyHGTTT--AAPNFAYAIVGRRMARvdeddAYDLSKLRIALNGAEPIDETAVQ 320
Cdd:PRK06187 230 LMAGAKQV--IPRRFDPENLL--DLIET-ERVTFffAVPTIWQMLLKAPRAY-----FVDFSSLRLVIYGGAALPPALLR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 321 TFVDagaRFKMPaecVFPAYGMAEATLAVSFAPLftgltldvveadalEAEnravpVPEGDPRRGTdgvrsfalLGRPLD 400
Cdd:PRK06187 300 EFKE---KFGID---LVQGYGMTETSPVVSVLPP--------------EDQ-----LPGQWTKRRS--------AGRPLP 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 401 GLEAEIVDDAGKRV--DEREVGEIRLRGEAVTPGYLTMdgPLATQD--EDGWLNTGDLGYL-VDGQIVICGRRKDVIIMG 475
Cdd:PRK06187 347 GVEARIVDDDGDELppDGGEVGEIIVRGPWLMQGYWNR--PEATAEtiDGGWLHTGDVGYIdEDGYLYITDRIKDVIISG 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 476 GRNLYPTDIERAATSVEGVRAgnaVAV------RLDagsrrER-FAVVlesKLAGDAEA-EKNLMKQVSARVRDAVdmRP 547
Cdd:PRK06187 425 GENIYPRELEDALYGHPAVAE---VAVigvpdeKWG-----ERpVAVV---VLKPGATLdAKELRAFLRGRLAKFK--LP 491
|
410 420 430
....*....|....*....|....*....|
gi 300790052 548 YAVVVLPAgsLPKTPSGKVKRAATAQQFAD 577
Cdd:PRK06187 492 KRIAFVDE--LPRTSVGKILKRVLREQYAE 519
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
33-566 |
7.20e-40 |
|
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: 151.98 E-value: 7.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHqP--TPRTdLAEWAEDT-VRVLGMI 109
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAAN-PiyTADE-LAHQLKISkPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 GSDQDALggpggLAPRPGSGAGPRnVTVLLGEPFDQLAPvleqkgIGFQLITELAAAEPLPDVVVTDEGDTALLQLTSGS 189
Cdd:cd05911 90 PDGLEKV-----KEAAKELGPKDK-IIVLDDKPDGVLSI------EDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 190 TADPKAVRITYGNLYSNVKaMVERAEFDFDV--DVMVSWLPTFHDMGMVGFLTVpMTFGVELV---KITPVEFLsgpliw 264
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLS-QVQTFLYGNDGsnDVILGFLPLYHIYGLFTTLAS-LLNGATVIimpKFDSELFL------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 265 pELITKYHGTTTA-APNFAYAivgrrMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFvdaGARFkmPAECVFPAYGMA 343
Cdd:cd05911 230 -DLIEKYKITFLYlVPPIAAA-----LAKSPLLDKYDLSSLRVILSGGAPLSKELQELL---AKRF--PNATIKQGYGMT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 344 EATLAVSFAPlftgltldvveadaleaenravpvpEGDPRRGTdgvrsfalLGRPLDGLEAEIVDDAGKRVDE-REVGEI 422
Cdd:cd05911 299 ETGGILTVNP-------------------------DGDDKPGS--------VGRLLPNVEAKIVDDDGKDSLGpNEPGEI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 423 RLRGEAVTPGYLtmDGPLAT---QDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGN 498
Cdd:cd05911 346 CVRGPQVMKGYY--NNPEATketFDEDGWLHTGDIGYFdEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAA 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300790052 499 AVAVRLDAGSRRERFAVVLEsklAGDAEAEKNLMKQVSARVRDAVDMRPyAVVVLPAgsLPKTPSGKV 566
Cdd:cd05911 424 VIGIPDEVSGELPRAYVVRK---PGEKLTEKEVKDYVAKKVASYKQLRG-GVVFVDE--IPKSASGKI 485
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3-579 |
6.04e-39 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 151.02 E-value: 6.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 3 RFVDTLVATATKRGQQRGMVTGEPKEPVRRTWAEVHEEARRIAGGLVAGGFERGTAVGvlaaapvLIAPTV-------QA 75
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVA-------ILSDNRpewviadLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 76 VWLAGGSVTMLHQPTPRTDLAEWAEDT-VRVLgmIGSDQDALGGpggLAPRPGSGAGPRNVTVllgepFDQLAPVLEQKG 154
Cdd:COG1022 85 ILAAGAVTVPIYPTSSAEEVAYILNDSgAKVL--FVEDQEQLDK---LLEVRDELPSLRHIVV-----LDPRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 155 IGFQLITELAAAEPLPDVV-----VTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPT 229
Cdd:COG1022 155 LSLDELLALGREVADPAELearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPG-DRTLSFLPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 230 FH-----------DMGM-VGFLTVPMTFGVELVKITPVEFLSGPLIWPELITKYHGTTTAAPN-----FAYAI-VGRRMA 291
Cdd:COG1022 234 AHvfertvsyyalAAGAtVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGlkrklFRWALaVGRRYA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 292 RVDEDD------------AYD---LSKLR--------IALNGAEPIDETAVQTFVDAGarfkMPaecVFPAYGMAEATLA 348
Cdd:COG1022 314 RARLAGkspslllrlkhaLADklvFSKLRealggrlrFAVSGGAALGPELARFFRALG----IP---VLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 349 VSFaplftgltldvveadaleaeNRavpvpEGDPRRGTdgvrsfalLGRPLDGLEAEIVDDagkrvderevGEIRLRGEA 428
Cdd:COG1022 387 ITV--------------------NR-----PGDNRIGT--------VGPPLPGVEVKIAED----------GEILVRGPN 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 429 VTPGYLtmDGPLATQ---DEDGWLNTGDLGYLV-DGQIVICGRRKDVIIM-GGRNLYPTDIERAATSVEGVraGNAVAVr 503
Cdd:COG1022 424 VMKGYY--KNPEATAeafDADGWLHTGDIGELDeDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLI--EQAVVV- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 504 ldaGSRR--------------ERFAVVLESKLAGDAEAEKNlmKQVSARVRDAVDM---------RPYAVVVLPA----- 555
Cdd:COG1022 499 ---GDGRpflaalivpdfealGEWAEENGLPYTSYAELAQD--PEVRALIQEEVDRanaglsraeQIKRFRLLPKeftie 573
|
650 660
....*....|....*....|....*
gi 300790052 556 -GSLpkTPSGKVKRAATAQQFADRI 579
Cdd:COG1022 574 nGEL--TPTLKLKRKVILEKYADLI 596
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
33-570 |
2.34e-37 |
|
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: 144.28 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAApvliaptvQAVWLAggsvtmlhqptprTDLAEWAedtvrvLGMIgsd 112
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRN--------RPEWTI-------------ADLAILA------IGAV--- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 qdalggpgglaprpgsgagprNVTVLLGEPFDQLAPVLEQKGIgfqlitelaaaeplpDVVVTDEG-DTALLQLTSGSTA 191
Cdd:cd05907 57 ---------------------PVPIYPTSSAEQIAYILNDSEA---------------KALFVEDPdDLATIIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 192 DPKAVRITYGNLYSNVKAMVERAEFDfDVDVMVSWLPTFHDMGMVGFLTVPMTFGVELV-------------KITPVEFL 258
Cdd:cd05907 101 RPKGVMLSHRNILSNALALAERLPAT-EGDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetllddlsEVRPTVFL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 259 SGPLIWPELITKYHGttTAAPNFAYAIVGRRMarvdeddaydLSKLRIALNGAEPIDETAVQTFVDAGarfkMPaecVFP 338
Cdd:cd05907 180 AVPRVWEKVYAAIKV--KAVPGLKRKLFDLAV----------GGRLRFAASGGAPLPAELLHFFRALG----IP---VYE 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 339 AYGMAEATLAVSFAPLftgltldvveadaleaenravpvpeGDPRRGTdgvrsfalLGRPLDGLEAEIVDDagkrvdere 418
Cdd:cd05907 241 GYGLTETSAVVTLNPP-------------------------GDNRIGT--------VGKPLPGVEVRIADD--------- 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 419 vGEIRLRGEAVTPGYLTMDGPLATQ-DEDGWLNTGDLGYL-VDGQIVICGRRKDVIIM-GGRNLYPTDIERAATSVEGV- 494
Cdd:cd05907 279 -GEILVRGPNVMLGYYKNPEATAEAlDADGWLHTGDLGEIdEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLIs 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 495 --------RAGNAVAVRLDAGS-----RRERFAVVLESKLAGDAEAEKNL---MKQVSARVRDAVDMRPYAVVVLP---- 554
Cdd:cd05907 358 qavvigdgRPFLVALIVPDPEAleawaEEHGIAYTDVAELAANPAVRAEIeaaVEAANARLSRYEQIKKFLLLPEPftie 437
|
570
....*....|....*.
gi 300790052 555 AGSLpkTPSGKVKRAA 570
Cdd:cd05907 438 NGEL--TPTLKLKRPV 451
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
162-573 |
1.11e-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: 137.06 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 162 ELAAAEPLPDVVVT----DEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVG 237
Cdd:cd05926 129 SLSNLLADKKNAKSegvpLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPD-DRTLVVMPLFHVHGLVA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 238 FLTVPMTFGVELVkiTPVEFlSGPLIWPElITKYHGT-TTAAPNFAYAIvgrrMARVDEDDAYDLSKLRIALNGAEPIDE 316
Cdd:cd05926 208 SLLSTLAAGGSVV--LPPRF-SASTFWPD-VRDYNATwYTAVPTIHQIL----LNRPEPNPESPPPKLRFIRSCSASLPP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 317 tavQTFVDAGARFKMPaecVFPAYGMAEATLAVSFAPLftgltldvveadaleaenravpvPEGDPRRGTdgvrsfalLG 396
Cdd:cd05926 280 ---AVLEALEATFGAP---VLEAYGMTEAAHQMTSNPL-----------------------PPGPRKPGS--------VG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 397 RPlDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQD---EDGWLNTGDLGYL-VDGQIVICGRRKDVI 472
Cdd:cd05926 323 KP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYL--NNPEANAEaafKDGWFRTGDLGYLdADGYLFLTGRIKELI 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 473 IMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQ------VSARVRdAVDmr 546
Cdd:cd05926 400 NRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKhlaafkVPKKVY-FVD-- 476
|
410 420
....*....|....*....|....*..
gi 300790052 547 pyavvvlpagSLPKTPSGKVKRAATAQ 573
Cdd:cd05926 477 ----------ELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
5-574 |
1.41e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 137.34 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 5 VDTLVATATKRGQQRGMVTGEpkepVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAA--APVLIAptVQAVWLAGGS 82
Cdd:PRK07656 8 PELLARAARRFGDKEAYVFGD----QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPnsPHWVIA--ALGALKAGAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 83 VTMLHqptPRTDLAEWAEDTVRvlgmigSDQDALGGPGGLAP--RPGSGAGP--RNVTVLLGEPfdqlapvLEQKGIGFQ 158
Cdd:PRK07656 82 VVPLN---TRYTADEAAYILAR------GDAKALFVLGLFLGvdYSATTRLPalEHVVICETEE-------DDPHTEKMK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 159 LITE-LAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGM-V 236
Cdd:PRK07656 146 TFTDfLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEG-DRYLAANPFFHVFGYkA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 237 GFLTVPMTFG--VELVKITPVEFLsgpliwpELITKYHGTTTAAP----NFAYAIVGRrmarvdedDAYDLSKLRIALNG 310
Cdd:PRK07656 225 GVNAPLMRGAtiLPLPVFDPDEVF-------RLIETERITVLPGPptmyNSLLQHPDR--------SAEDLSSLRLAVTG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 311 AEPIDETAVQTFvdagaRFKMPAECVFPAYGMAEATLAVSFAPLftgltldvveadaleaenravpvpeGDPRRGTDGVr 390
Cdd:PRK07656 290 AASMPVALLERF-----ESELGVDIVLTGYGLSEASGVTTFNRL-------------------------DDDRKTVAGT- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 391 sfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMdgPLATQ---DEDGWLNTGDLGYL-VDGQIVICG 466
Cdd:PRK07656 339 ----IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDD--PEATAaaiDADGWLHTGDLGRLdEEGYLYIVD 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 467 RRKDVIIMGGRNLYPTDIER--------AATSVEGV---RAGNAVavrldagsrreRFAVVLESKLAGDAEAeknLMKQv 535
Cdd:PRK07656 413 RKKDMFIVGGFNVYPAEVEEvlyehpavAEAAVIGVpdeRLGEVG-----------KAYVVLKPGAELTEEE---LIAY- 477
|
570 580 590
....*....|....*....|....*....|....*....
gi 300790052 536 sARVRDAVDMRPYAVVVLPAgsLPKTPSGKVKRAATAQQ 574
Cdd:PRK07656 478 -CREHLAKYKVPRSIEFLDE--LPKNATGKVLKRALREK 513
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
31-568 |
5.71e-34 |
|
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: 134.05 E-value: 5.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 31 RRTWAEVHEEARRIAGGLVAGGFERGTAVGVLaaapvliaptvqavwlaggsvtmlhqptprtdLAEWAEDTVRVLGmig 110
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQ--------------------------------LPNWWEFAVLYLA--- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 111 sdqdalggpgglaprpgsgagprnvTVLLGEPFDQLAPVLEQKGIGFQLITELAAAEPLPDV-----VVTDEGDTALLQL 185
Cdd:cd05903 46 -------------------------CLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERfrqfdPAAMPDAVALLLF 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 186 TSGSTADPKAVRITYGNLYSNVKAMVERAEFDF-DVDVMVSwlPTFHDMGMVGFLTVPMTFGvelvkiTPVEFLSgplIW 264
Cdd:cd05903 101 TSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPgDVFLVAS--PMAHQTGFVYGFTLPLLLG------APVVLQD---IW 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 265 P-----ELITKYHGTTT-AAPNFAYAIVgrrmaRVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGARFkmpaecVFP 338
Cdd:cd05903 170 DpdkalALMREHGVTFMmGATPFLTDLL-----NAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAK------VCS 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 339 AYGMAEATLAVSfaplftgltldvveadaleaenrAVPVPEGDPRRGTDGvrsfallgRPLDGLEAEIVDDAGKRVDERE 418
Cdd:cd05903 239 AYGSTECPGAVT-----------------------SITPAPEDRRLYTDG--------RPLPGVEIKVVDDTGATLAPGV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 419 VGEIRLRGEAVTPGYLtmDGPLATQD--EDGWLNTGDLGYLVD-GQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVR 495
Cdd:cd05903 288 EGELLSRGPSVFLGYL--DRPDLTADaaPEGWFRTGDLARLDEdGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVI 365
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300790052 496 AGNAVAV---RLdaGSRRERFaVVLESKLAGDAEAeknlMKQVSARVRDAVDMRPYAVVVLPAgsLPKTPSGKVKR 568
Cdd:cd05903 366 EAAVVALpdeRL--GERACAV-VVTKSGALLTFDE----LVAYLDRQGVAKQYWPERLVHVDD--LPRTPSGKVQK 432
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
28-566 |
8.52e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 133.16 E-value: 8.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 28 EPVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLA------------------AAPV--LIAPTVQAVWL--AGGSVTM 85
Cdd:PRK07529 55 RPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLpnlpethfalwggeaagiANPInpLLEPEQIAELLraAGAKVLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 86 LHQPTPRTDLAEWAEDTVR----VLGMIGSD-QDALGGPGGLAPRPGSGAGPRNVtvllgepFDQLAPVLEQKGigfqli 160
Cdd:PRK07529 135 TLGPFPGTDIWQKVAEVLAalpeLRTVVEVDlARYLPGPKRLAVPLIRRKAHARI-------LDFDAELARQPG------ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 161 TELAAAEPLpdvvvtDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLT 240
Cdd:PRK07529 202 DRLFSGRPI------GPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPG-DTVFCGLPLFHVNALLVTGL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 241 VPMTFGVELVKITPVEFlSGPL----IWpELITKYHGTTTAAPNFAYAIVGRRMArvdedDAYDLSKLRIALNGAEPIDE 316
Cdd:PRK07529 275 APLARGAHVVLATPQGY-RGPGvianFW-KIVERYRINFLSGVPTVYAALLQVPV-----DGHDISSLRYALCGAAPLPV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 317 TAVQTFVDA-GARfkmpaecVFPAYGMAEATLAVSFAPlftgltldvveadaleaenravpvPEGDPRRGTdgvrsfalL 395
Cdd:PRK07529 348 EVFRRFEAAtGVR-------IVEGYGLTEATCVSSVNP------------------------PDGERRIGS--------V 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIV--DDAGKRVDE---REVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRK 469
Cdd:PRK07529 389 GLRLPYQRVRVVilDDAGRYLRDcavDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIdADGYFWLTGRAK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 470 DVIIMGGRNLYPTDIERAATSVEGVRAGNAVAvRLDAGSRRERFAVVlesKLAGDAEA-EKNLMKQVSARV--RDAVdmr 546
Cdd:PRK07529 469 DLIIRGGHNIDPAAIEEALLRHPAVALAAAVG-RPDAHAGELPVAYV---QLKPGASAtEAELLAFARDHIaeRAAV--- 541
|
570 580
....*....|....*....|
gi 300790052 547 PYAVVVLPAgsLPKTPSGKV 566
Cdd:PRK07529 542 PKHVRILDA--LPKTAVGKI 559
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
172-568 |
2.91e-32 |
|
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: 129.87 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 172 VVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAmVERAEFDFDVDVMVSWLPTFHDMGMVGFLTVPMTFGVELVK 251
Cdd:cd05914 83 IFVSDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDG-VKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 252 ITPvefLSGPLIwpELITKYHGTTTAAPNFAYAIVGRRmaRVDEDDAYDLSKLRIALNG---AEPIDETAVQTFVDA-GA 327
Cdd:cd05914 162 LDK---IPSAKI--IALAFAQVTPTLGVPVPLVIEKIF--KMDIIPKLTLKKFKFKLAKkinNRKIRKLAFKKVHEAfGG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 328 RFK--------MPAE----------CVFPAYGMAEATLAVSFAPlftgltldvveadaleaENRAVpvpegdprrgtdgv 389
Cdd:cd05914 235 NIKefviggakINPDveeflrtigfPYTIGYGMTETAPIISYSP-----------------PNRIR-------------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 390 rsFALLGRPLDGLEAEIVDDAGKRVDerevGEIRLRGEAVTPGYltMDGPLATQ---DEDGWLNTGDLGYLV-DGQIVIC 465
Cdd:cd05914 284 --LGSAGKVIDGVEVRIDSPDPATGE----GEIIVRGPNVMKGY--YKNPEATAeafDKDGWFHTGDLGKIDaEGYLYIR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 466 GRRKDVIIMG-GRNLYPTDIE-------RAATSVEGVRAGNAVA-VRLDAGSrrerfavvLESKLAGDAEAEKNLMKQVS 536
Cdd:cd05914 356 GRKKEMIVLSsGKNIYPEEIEakinnmpFVLESLVVVQEKKLVAlAYIDPDF--------LDVKALKQRNIIDAIKWEVR 427
|
410 420 430
....*....|....*....|....*....|...
gi 300790052 537 ARV-RDAVDMRPYAVVVLPAGSLPKTPSGKVKR 568
Cdd:cd05914 428 DKVnQKVPNYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
179-568 |
5.01e-32 |
|
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: 128.23 E-value: 5.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDfDVDVMVSWLPTFHdmgmVGFLTVPMTFGVELVKITPVEFL 258
Cdd:cd05912 78 DIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT-EDDNWLCALPLFH----ISGLSILMRSVIYGMTVYLVDKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 259 SGPLIwPELITKYHGTTTAApnfAYAIVGRRMARVDEDDAYDLsklRIALNGAEPIDETAVQTFVDAGarfkMPaecVFP 338
Cdd:cd05912 153 DAEQV-LHLINSGKVTIISV---VPTMLQRLLEILGEGYPNNL---RCILLGGGPAPKPLLEQCKEKG----IP---VYQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 339 AYGMAE-ATLAVSFAPLFTGLTLDVVeadaleaenravpvpegdprrgtdgvrsfallGRPLDGLEAEIVDDAGKrvdER 417
Cdd:cd05912 219 SYGMTEtCSQIVTLSPEDALNKIGSA--------------------------------GKPLFPVELKIEDDGQP---PY 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 418 EVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRA 496
Cdd:cd05912 264 EVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKE 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300790052 497 GNAVAVRLDAGSRRERFAVVLESKLagdaeAEKNLMKQVSARVrdAVDMRPYAVVVLpaGSLPKTPSGKVKR 568
Cdd:cd05912 344 AGVVGIPDDKWGQVPVAFVVSERPI-----SEEELIAYCSEKL--AKYKVPKKIYFV--DELPRTASGKLLR 406
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
33-570 |
2.55e-31 |
|
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: 126.41 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDtvrvlgmigSD 112
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLED---------LD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 QDALggpggLAPRPgsgagprnvtvllgepfdqlapvLEQKGIGFQLITELAAAEPLPDVVVTDEG--DTALLQLTSGST 190
Cdd:TIGR01923 72 VQLL-----LTDSL-----------------------LEEKDFQADSLDRIEAAGRYETSLSASFNmdQIATLMFTSGTT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 191 ADPKAVRITYGNLYSNVKAMVERAEFDfDVDVMVSWLPTFHDMGmVGFLTVPMTFGVELVKITPVEFLSgpliwpELITk 270
Cdd:TIGR01923 124 GKPKAVPHTFRNHYASAVGSKENLGFT-EDDNWLLSLPLYHISG-LSILFRWLIEGATLRIVDKFNQLL------EMIA- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 271 yHGTTTAApnfayAIVGRRMARVDEDDAYDLSkLRIALNGAEPIDETAVQTFVDAGarfkMPaecVFPAYGMAEATLAVS 350
Cdd:TIGR01923 195 -NERVTHI-----SLVPTQLNRLLDEGGHNEN-LRKILLGGSAIPAPLIEEAQQYG----LP---IYLSYGMTETCSQVT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 351 FAPlftgltldvveadaleaenravpvPEGDPRRGTdgvrsfalLGRPLDGLEAEIvddagKRVDEREVGEIRLRGEAVT 430
Cdd:TIGR01923 261 TAT------------------------PEMLHARPD--------VGRPLAGREIKI-----KVDNKEGHGEIMVKGANLM 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 431 PGYLTmDGPL-ATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGS 508
Cdd:TIGR01923 304 KGYLY-QGELtPAFEQQGWFNTGDIGELdGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWG 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300790052 509 RRERFAVVLESKLAgDAEAEKNLMKQVsARVRdavdmRPYAVVVLPagSLPKTPSGKVKRAA 570
Cdd:TIGR01923 383 QVPVAYIVSESDIS-QAKLIAYLTEKL-AKYK-----VPIAFEKLD--ELPYNASGKILRNQ 435
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
163-570 |
3.74e-31 |
|
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: 126.21 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 163 LAAAEPlpDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVER------------AEFDFDVDVMvSWLPTf 230
Cdd:cd05945 84 LDAAKP--ALLIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDfplgpgdvflnqAPFSFDLSVM-DLYPA- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 231 hdmgmvgfLTVPMTfgvelVKITPVEFLSGPLIWPELITKyHGTT--TAAPNFAyaivgrRMARVDEDDAYD-LSKLRIA 307
Cdd:cd05945 160 --------LASGAT-----LVPVPRDATADPKQLFRFLAE-HGITvwVSTPSFA------AMCLLSPTFTPEsLPSLRHF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 308 LNGAEPIDETAVQTFVdagARFkmPAECVFPAYGMAEATLAVsfaplftglTLDVVEADALEAENRaVPVpegdprrgtd 387
Cdd:cd05945 220 LFCGEVLPHKTARALQ---QRF--PDARIYNTYGPTEATVAV---------TYIEVTPEVLDGYDR-LPI---------- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 388 gvrsfallGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQ------DEDGWLNTGDLGYLV-DG 460
Cdd:cd05945 275 --------GYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYL--NNPEKTAaaffpdEGQRAYRTGDLVRLEaDG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 461 QIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAgnAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVR 540
Cdd:cd05945 345 LLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKE--AVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIKAELAERLP 422
|
410 420 430
....*....|....*....|....*....|
gi 300790052 541 DAvdMRPYAVVVLPagSLPKTPSGKVKRAA 570
Cdd:cd05945 423 PY--MIPRRFVYLD--ELPLNANGKIDRKA 448
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
22-569 |
1.44e-29 |
|
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: 122.74 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 22 VTGEPKEPVRR-TWAEVHEEARRIAGGLVAGGFERGTAVGVLA-----------AAPVLiaptvqavwlagGSVtmLHQP 89
Cdd:cd12119 15 VSRTHEGEVHRyTYAEVAERARRLANALRRLGVKPGDRVATLAwnthrhlelyyAVPGM------------GAV--LHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 90 TPR--TDLAEW----AEDtvRVLgMIGSDQDALGGPggLAPRPGSGAGPRNVTVLLGEPFDQLAPVLEQKgigfqliTEL 163
Cdd:cd12119 81 NPRlfPEQIAYiinhAED--RVV-FVDRDFLPLLEA--IAPRLPTVEHVVVMTDDAAMPEPAGVGVLAYE-------ELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 164 AAAEPLPDVVVTDEGDTALLQLTSGSTADPKAV----RITY----GNLYSNVKAMVERaefdfdvDVMVSWLPTFHDMGM 235
Cdd:cd12119 149 AAESPEYDWPDFDENTAAAICYTSGTTGNPKGVvyshRSLVlhamAALLTDGLGLSES-------DVVLPVVPMFHVNAW 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 236 VGFLTVPMTfGVELVkitpvefLSGPLIWP----ELITKYHGTTTAA-PNFAYAIvgrrMARVDEDDaYDLSKLRIALNG 310
Cdd:cd12119 222 GLPYAAAMV-GAKLV-------LPGPYLDPaslaELIEREGVTFAAGvPTVWQGL----LDHLEANG-RDLSSLRRVVIG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 311 AEPIDETAVQTFVDAGARfkmpaecVFPAYGMAEATlavsfaPLFTGLTLDVVEADALEAENRAVpvpegdpRRGTdgvr 390
Cdd:cd12119 289 GSAVPRSLIEAFEERGVR-------VIHAWGMTETS------PLGTVARPPSEHSNLSEDEQLAL-------RAKQ---- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 391 sfallGRPLDGLEAEIVDDAGKRV--DEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGR 467
Cdd:cd12119 345 -----GRPVPGVELRIVDDDGRELpwDGKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIdEDGYLTITDR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 468 RKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLEsklAGDAEAEKNLMKQVSARVrdAVDMRP 547
Cdd:cd12119 420 SKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLK---EGATVTAEELLEFLADKV--AKWWLP 494
|
570 580
....*....|....*....|...
gi 300790052 548 YAVVVLPAgsLPKTPSGKV-KRA 569
Cdd:cd12119 495 DDVVFVDE--IPKTSTGKIdKKA 515
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
33-472 |
1.60e-29 |
|
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: 122.34 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDTVRVLGMIGSD 112
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 qdalggpggLAPRPGSGAGPrnvTVLLGE-PFDQLAPVLEQKgigfqlitelAAAEPLPDVVVTDEGDTALLQLTSGSTA 191
Cdd:cd05904 114 ---------LAEKLASLALP---VVLLDSaEFDSLSFSDLLF----------EADEAEPPVVVIKQDDVAALLYSSGTTG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 192 DPKAVRITYGNLYSNVKAMVERAEFDFDV-DVMVSWLPTFHDMGMVGFLTVPMTFGVELVkITPVEFLSGPLiwpELITK 270
Cdd:cd05904 172 RSKGVMLTHRNLIAMVAQFVAGEGSNSDSeDVFLCVLPMFHIYGLSSFALGLLRLGATVV-VMPRFDLEELL---AAIER 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 271 YHGT-TTAAPNFAYAIVGRRMArvdedDAYDLSKLRIALNGAEPIDETAVQTFvdagaRFKMPAECVFPAYGMAEATLAV 349
Cdd:cd05904 248 YKVThLPVVPPIVLALVKSPIV-----DKYDLSSLRQIMSGAAPLGKELIEAF-----RAKFPNVDLGQGYGMTESTGVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 350 SfaplftgltldvveadaleaenrAVPVPEGDPRRGTDgvrsfalLGRPLDGLEAEIVD-DAGKRVDEREVGEIRLRGEA 428
Cdd:cd05904 318 A-----------------------MCFAPEKDRAKYGS-------VGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPS 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 300790052 429 VTPGYLtmDGPLATQ---DEDGWLNTGDLGYL-VDGQIVICGRRKDVI 472
Cdd:cd05904 368 IMKGYL--NNPEATAatiDKEGWLHTGDLCYIdEDGYLFIVDRLKELI 413
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
30-485 |
4.55e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 121.42 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 30 VRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLA-----------------AAPVLIAPTVQAVWLAggsvTMLHQPTPR 92
Cdd:PRK12583 44 LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWApncaewlltqfatarigAILVNINPAYRASELE----YALGQSGVR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 93 TDLAEWAEDTVRVLGMIGS--DQDALGGPGGLAPR--PGSgagpRNVTVLLGEP------FDQLAPvlEQKGIGFQLITE 162
Cdd:PRK12583 120 WVICADAFKTSDYHAMLQEllPGLAEGQPGALACErlPEL----RGVVSLAPAPppgflaWHELQA--RGETVSREALAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 163 LAAAeplpdvvvTDEGDTALLQLTSGSTADPKAVRITYGNLYSNvKAMVERAEFDFDVDVMVSWLPTFHDMGMVGFLTVP 242
Cdd:PRK12583 194 RQAS--------LDRDDPINIQYTSGTTGFPKGATLSHHNILNN-GYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGC 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 243 MTFGVELvkITPVEFLSgPLIWPELITKYHGTTTaapnfaYAIVGRRMARVD--EDDAYDLSKLRIALNGAEPIDETAVQ 320
Cdd:PRK12583 265 MTVGACL--VYPNEAFD-PLATLQAVEEERCTAL------YGVPTMFIAELDhpQRGNFDLSSLRTGIMAGAPCPIEVMR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 321 TFVDagarfKMPAECVFPAYGMAEATlavsfaPLftglTLDVVEADALEaenravpvpegdprrgtdgvRSFALLGRPLD 400
Cdd:PRK12583 336 RVMD-----EMHMAEVQIAYGMTETS------PV----SLQTTAADDLE--------------------RRVETVGRTQP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 401 GLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQ-DEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRN 478
Cdd:PRK12583 381 HLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESiDEDGWMHTGDLATMdEQGYVRIVGRSKDMIIRGGEN 460
|
....*..
gi 300790052 479 LYPTDIE 485
Cdd:PRK12583 461 IYPREIE 467
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
143-583 |
4.73e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 121.39 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 143 FDQLAPVLEQkgigFQLITELAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDV 222
Cdd:PRK06087 156 VDKLAPATSS----LSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQ-DV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 223 MVSWLPTFHDMGMVGFLTVPMTFG---VELVKITPVEFLSgpLIWPELITKYHGTTTaapnFAYAIVgrrmaRVDEDDAY 299
Cdd:PRK06087 231 FMMPAPLGHATGFLHGVTAPFLIGarsVLLDIFTPDACLA--LLEQQRCTCMLGATP----FIYDLL-----NLLEKQPA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 300 DLSKLRIALNGAEPIDETAVQtfvDAGARFKMPAECvfpaYGMAEATLAVsFAPLftgltldvveADALEaenravpvpe 379
Cdd:PRK06087 300 DLSALRFFLCGGTTIPKKVAR---ECQQRGIKLLSV----YGSTESSPHA-VVNL----------DDPLS---------- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 380 gdprrgtdgvRSFALLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGDLGY 456
Cdd:PRK06087 352 ----------RFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYL--DEPELTAralDEEGWYYSGDLCR 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 457 L-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAV---RLdaGSRRERFAVVLESKLAGDAEAEKNLM 532
Cdd:PRK06087 420 MdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMpdeRL--GERSCAYVVLKAPHHSLTLEEVVAFF 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 300790052 533 kqvsARVRDAVDMRPYAVVVLPAgsLPKTPSGKVKRAATAQQFADRIKKNA 583
Cdd:PRK06087 498 ----SRKRVAKYKYPEHIVVIDK--LPRTASGKIQKFLLRKDIMRRLTQDV 542
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
33-501 |
9.22e-29 |
|
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: 118.52 E-value: 9.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVA-GGFERGTAVGVLAA--APVLIAptVQAVWLAGGSVTML--HQPTPRtdLAEWAEDT-VRVL 106
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLErsAELVVA--ILAVLKAGAAYVPLdpAYPAER--LAFILEDAgARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 107 gmigsdqdaLGGPGGLAPRPGSGAGPRNVTVLLGEPFDQLAPvleqkgigfqliTELAAAEPLPDvvvtdegDTALLQLT 186
Cdd:TIGR01733 77 ---------LTDSALASRLAGLVLPVILLDPLELAALDDAPA------------PPPPDAPSGPD-------DLAYVIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 187 SGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTvPMTFGVELVKITPVEFLSGPLIWPE 266
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD-DRVLQFASLSFDASVEEIFG-ALLAGATLVVPPEDEERDDAALLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 267 LITkyHGTTTAApnfayAIVGRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFvdagaRFKMPAECVFPAYGMAEAT 346
Cdd:TIGR01733 207 LIA--EHPVTVL-----NLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRW-----RARGPGARLINLYGPTETT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 347 LAVSFAPLftgltldvveadALEAENRAVPVPegdprrgtdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRG 426
Cdd:TIGR01733 275 VWSTATLV------------DPDDAPRESPVP----------------IGRPLANTRLYVLDDDLRPVPVGVVGELYIGG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 427 EAVTPGYLTMDG---------PLATQDEDGWLNTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRa 496
Cdd:TIGR01733 327 PGVARGYLNRPEltaerfvpdPFAGGDGARLYRTGDLVrYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVR- 405
|
....*
gi 300790052 497 gNAVA 501
Cdd:TIGR01733 406 -EAVV 409
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
33-569 |
9.58e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 118.93 E-value: 9.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAApvliAPTVQAVWLAggsvtmlhqptprtdlaewaedtvrvLGMIGSD 112
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDN----CPEFLFAWFA--------------------------LAKLGAV 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 qdalggpgglaprpgsgAGPRNvTVLLGepfDQLAPVLEQKGigfqlitelaaaeplPDVVVTDegdTALLQLTSGSTAD 192
Cdd:cd05934 55 -----------------LVPIN-TALRG---DELAYIIDHSG---------------AQLVVVD---PASILYTSGTTGP 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 193 PKAVRITYGNLYSNVKAMVERAEFDfDVDVMVSWLPTFH----DMGMVGFLTVPMTFgVELVKITPVEFlsgpliWPElI 268
Cdd:cd05934 96 PKGVVITHANLTFAGYYSARRFGLG-EDDVYLTVLPLFHinaqAVSVLAALSVGATL-VLLPRFSASRF------WSD-V 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 269 TKYHGTTTAAPNFAYAIVGRRMARVDEDDAydlsKLRIALNGAEPIDETAvqtfvDAGARFKMPaecVFPAYGMAEATLA 348
Cdd:cd05934 167 RRYGATVTNYLGAMLSYLLAQPPSPDDRAH----RLRAAYGAPNPPELHE-----EFEERFGVR---LLEGYGMTETIVG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 349 VsfaplftgltldvveadaleaenrAVPVPEgdprrgTDGVRSFallGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGE- 427
Cdd:cd05934 235 V------------------------IGPRDE------PRRPGSI---GRPAPGYEVRIVDDDGQELPAGEPGELVIRGLr 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 428 --AVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRL 504
Cdd:cd05934 282 gwGFFKGYYNMPEATAEAMRNGWFHTGDLGYRdADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPD 361
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300790052 505 DAGSRRERFAVVLEsklAGDAEAEKNLMKQVSARVrdAVDMRPYAVVVLPagSLPKTPSGKVKRA 569
Cdd:cd05934 362 EVGEDEVKAVVVLR---PGETLDPEELFAFCEGQL--AYFKVPRYIRFVD--DLPKTPTEKVAKA 419
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
162-568 |
7.15e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 118.18 E-value: 7.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 162 ELAAAEPLPDVVVTDE-----GDTALLQLTSGSTADPKAVRITYGNLYSN-------VKAMVERAEfdfdvdVMVSWLPT 229
Cdd:PRK05605 198 TLVDAAIGGDGSDVSHprptpDDVALILYTSGTTGKPKGAQLTHRNLFANaaqgkawVPGLGDGPE------RVLAALPM 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 230 FHDMGMVGFLTVPMTFGVELVKITPVEFlsgPLIWPelITKYHgTTTAAPnfAYAIVGRRMARVDEDDAYDLSKLRIALN 309
Cdd:PRK05605 272 FHAYGLTLCLTLAVSIGGELVLLPAPDI---DLILD--AMKKH-PPTWLP--GVPPLYEKIAEAAEERGVDLSGVRNAFS 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 310 GAEPIDETAVQTFVDA-GARfkmpaecVFPAYGMAEAtlavsfAPLFTGltldvveadaleaeNravpvPEGDPRR-GTD 387
Cdd:PRK05605 344 GAMALPVSTVELWEKLtGGL-------LVEGYGLTET------SPIIVG--------------N-----PMSDDRRpGYV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 388 GVrsfallgrPLDGLEAEIVD--DAGKRVDEREVGEIRLRGEAVTPGYLTMdgPLATQD--EDGWLNTGDLGYL-VDGQI 462
Cdd:PRK05605 392 GV--------PFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNR--PEETAKsfLDGWFRTGDVVVMeEDGFI 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 463 VICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVRda 542
Cdd:PRK05605 462 RIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYK-- 539
|
410 420
....*....|....*....|....*.
gi 300790052 543 VDMRPYAVVVLPAGSLpktpsGKVKR 568
Cdd:PRK05605 540 VPRRFYHVDELPRDQL-----GKVRR 560
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
178-570 |
1.01e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 114.50 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 178 GDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFGVELVKITPVEF 257
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPD-DVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 258 LSGPL---IWpELITKYHGTTTAAPNFAYAIVGRRmarvdEDDAyDLSKLRIALNGAEPIDETAVQTFVDAgarFKMPae 334
Cdd:cd05944 81 RNPGLfdnFW-KLVERYRITSLSTVPTVYAALLQV-----PVNA-DISSLRFAMSGAAPLPVELRARFEDA---TGLP-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 335 cVFPAYGMAEATLAVSFAPlftgltldvveadaleaenravpvPEGDPRRGTDGVR--SFALLGRPLDGLEAEIVDDAGK 412
Cdd:cd05944 149 -VVEGYGLTEATCLVAVNP------------------------PDGPKRPGSVGLRlpYARVRIKVLDGVGRLLRDCAPD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 413 rvderEVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSV 491
Cdd:cd05944 204 -----EVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRH 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 492 EGVRAGNAVAvRLDAGSRRERFAVVlesKLAGDAEAEK-NLMKQVSARV--RDAVdmrPYAVVVLPagSLPKTPSGKVKR 568
Cdd:cd05944 279 PAVAFAGAVG-QPDAHAGELPVAYV---QLKPGAVVEEeELLAWARDHVpeRAAV---PKHIEVLE--ELPVTAVGKVFK 349
|
..
gi 300790052 569 AA 570
Cdd:cd05944 350 PA 351
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
163-568 |
1.68e-27 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 116.69 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 163 LAAAEPLPDvvvtdegDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVP 242
Cdd:PRK13295 189 LARLRPGPD-------DVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGAD-DVILMASPMAHQTGFMYGLMMP 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 243 MTFGVELVKI---TPVEFLSgpLIWPELITkyhgTTTAAPNFAYaivgrRMARVDEDDAYDLSKLRIALNGAEPIDETAV 319
Cdd:PRK13295 261 VMLGATAVLQdiwDPARAAE--LIRTEGVT----FTMASTPFLT-----DLTRAVKESGRPVSSLRTFLCAGAPIPGALV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 320 QTfvdagARFKMPAECVfPAYGMAEATLAvsfaplfTGLTLDvveaDALEaenravpvpegdprrgtdgvRSFALLGRPL 399
Cdd:PRK13295 330 ER-----ARAALGAKIV-SAWGMTENGAV-------TLTKLD----DPDE--------------------RASTTDGCPL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 400 DGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATqDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRN 478
Cdd:PRK13295 373 PGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT-DADGWFDTGDLARIdADGYIRISGRSKDVIIRGGEN 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 479 LYPTDIERAATSVEGVRAGNAVAV---RLdaGSRRERFaVVLESKLAGDAEAEKNLMKqvSARVrdAVDMRPYAVVVLPA 555
Cdd:PRK13295 452 IPVVEIEALLYRHPAIAQVAIVAYpdeRL--GERACAF-VVPRPGQSLDFEEMVEFLK--AQKV--AKQYIPERLVVRDA 524
|
410
....*....|...
gi 300790052 556 gsLPKTPSGKVKR 568
Cdd:PRK13295 525 --LPRTPSGKIQK 535
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
135-578 |
1.79e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.11 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 135 VTVLLGEPFDQLAPVLEQKGIGFQ---LITELAAAE--PLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLY----S 205
Cdd:PRK06839 101 TTVLFVEKTFQNMALSMQKVSYVQrviSITSLKEIEdrKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFwnalN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 206 NVKAMVERAEfdfdvDVMVSWLPTFHdMGMVGFLTVPMTF--GVELV--KITPVEFLSgpLIWPELITKYHGTTTaapnf 281
Cdd:PRK06839 181 NTFAIDLTMH-----DRSIVLLPLFH-IGGIGLFAFPTLFagGVIIVprKFEPTKALS--MIEKHKVTVVMGVPT----- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 282 ayaiVGRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGARFKMpaecvfpAYGMAEATLAVSFaplftgltld 361
Cdd:PRK06839 248 ----IHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQ-------GFGMTETSPTVFM---------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 362 vveadaleaenravpVPEGDPRRGTDGVrsfallGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLA 441
Cdd:PRK06839 307 ---------------LSEEDARRKVGSI------GKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 442 TQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESk 520
Cdd:PRK06839 366 ETIQDGWLCTGDLARVdEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS- 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 300790052 521 laGDAEAEKNLMKQVSARVrdAVDMRPYAVVVLPagSLPKTPSGKVKRAATAQQFADR 578
Cdd:PRK06839 445 --SSVLIEKDVIEHCRLFL--AKYKIPKEIVFLK--ELPKNATGKIQKAQLVNQLKSR 496
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
33-582 |
1.93e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 115.83 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDtvrvlgmigsd 112
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDD----------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 qdalggpgglaprpgSGAgprnVTVLLGEPFDQlapvlEQKGIGFQLITELAAaEPLPDVVVT---DEGDTALLQLTSGS 189
Cdd:PRK03640 98 ---------------AEV----KCLITDDDFEA-----KLIPGISVKFAELMN-GPKEEAEIQeefDLDEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 190 TADPKAVRITYGN-LYSNVKAMVERAEFDFDvdvmvSWL---PTFHDMG---MVGFLTVPMTfgVELVKITPVEFLSgpl 262
Cdd:PRK03640 153 TGKPKGVIQTYGNhWWSAVGSALNLGLTEDD-----CWLaavPIFHISGlsiLMRSVIYGMR--VVLVEKFDAEKIN--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 263 iwpELITKYHGTTTAApnfAYAIVGRRMARVdEDDAYDlSKLRIALNGAEPIDETAVQTFVDAGarfkMPaecVFPAYGM 342
Cdd:PRK03640 223 ---KLLQTGGVTIISV---VSTMLQRLLERL-GEGTYP-SSFRCMLLGGGPAPKPLLEQCKEKG----IP---VYQSYGM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 343 AE-ATLAVSFAPlftgltldvveADALEAENRAvpvpegdprrgtdgvrsfallGRPLDGLEAEIVDDaGKRVDEREVGE 421
Cdd:PRK03640 288 TEtASQIVTLSP-----------EDALTKLGSA---------------------GKPLFPCELKIEKD-GVVVPPFEEGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 422 IRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVragNAV 500
Cdd:PRK03640 335 IVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGV---AEA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 501 AVrldAGSRRERFAVVLESKLAGDAEAEKNLMKQVsARVRDAVDMRPYAVVVlpAGSLPKTPSGKVKRaataQQFADRIK 580
Cdd:PRK03640 412 GV---VGVPDDKWGQVPVAFVVKSGEVTEEELRHF-CEEKLAKYKVPKRFYF--VEELPRNASGKLLR----HELKQLVE 481
|
..
gi 300790052 581 KN 582
Cdd:PRK03640 482 EM 483
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
170-570 |
3.76e-27 |
|
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: 114.55 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 170 PDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTvPMTFGVEL 249
Cdd:cd05930 85 AKLVLTDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPG-DRVLQFTSFSFDVSVWEIFG-ALLAGATL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 250 VKITPVEFLSGPLIWPEL----ITKYHGTTTAAPNFayaivgrrmarVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDA 325
Cdd:cd05930 163 VVLPEEVRKDPEALADLLaeegITVLHLTPSLLRLL-----------LQELELAALPSLRLVLVGGEALPPDLVRRWREL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 326 GarfkmPAECVFPAYGMAEATLAVSFAplftgltldvvEADALEAENRAVPVpegdprrgtdgvrsfallGRPLDGLEAE 405
Cdd:cd05930 232 L-----PGARLVNLYGPTEATVDATYY-----------RVPPDDEEDGRVPI------------------GRPIPNTRVY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 406 IVDDAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQ--------DEDGWL-NTGDLG-YLVDGQIVICGRRKD-VIIM 474
Cdd:cd05930 278 VLDENLRPVPPGVPGELYIGGAGLARGYL--NRPELTAerfvpnpfGPGERMyRTGDLVrWLPDGNLEFLGRIDDqVKIR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 475 GGRnLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQvsarvRDAVDMRPYAVVVLP 554
Cdd:cd05930 356 GYR-IELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAE-----RLPDYMVPSAFVVLD 429
|
410
....*....|....*.
gi 300790052 555 AgsLPKTPSGKVKRAA 570
Cdd:cd05930 430 A--LPLTPNGKVDRKA 443
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-568 |
3.99e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 112.76 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 183 LQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFGVELVKITPVEFLSGPL 262
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQ-DRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 263 --IWPELITKYHGTttaaPNFAYAIVGRrmarvDEDDAYDLSKLRIALNGAEPIDETAVQTFVDagarfKMPAECVFPAY 340
Cdd:cd05917 86 eaIEKEKCTALHGV----PTMFIAELEH-----PDFDKFDLSSLRTGIMAGAPCPPELMKRVIE-----VMNMKDVTIAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 341 GMAEATlavsfaPLFTGLTLDVveadalEAENRAVPVpegdprrgtdgvrsfallGRPLDGLEAEIVDDAGKRVDER-EV 419
Cdd:cd05917 152 GMTETS------PVSTQTRTDD------SIEKRVNTV------------------GRIMPHTEAKIVDPEGGIVPPVgVP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 420 GEIRLRGEAVTPGYLTMdgPLATQ---DEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIER--------A 487
Cdd:cd05917 202 GELCIRGYSVMKGYWND--PEKTAeaiDGDGWLHTGDLAVMdEDGYCRIVGRIKDMIIRGGENIYPREIEEflhthpkvS 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 488 ATSVEGV---RAGNAVA--VRLDAGSRRerfavvlesklagDAEAEKNLMKQVSARvrdavdmrpYAV--VVLPAGSLPK 560
Cdd:cd05917 280 DVQVVGVpdeRYGEEVCawIRLKEGAEL-------------TEEDIKAYCKGKIAH---------YKVprYVFFVDEFPL 337
|
....*...
gi 300790052 561 TPSGKVKR 568
Cdd:cd05917 338 TVSGKIQK 345
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
172-517 |
4.98e-27 |
|
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: 114.74 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 172 VVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFGVELVk 251
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPE-DVVFGALPFFHSFGLTGCLWLPLLSGIKVV- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 252 itpveFLSGPL---IWPELITKYHGTTT-AAPNFAYAIVGRRmarvdedDAYDLSKLRIALNGAEPIDETAVQTFVDaga 327
Cdd:cd05909 219 -----FHPNPLdykKIPELIYDKKATILlGTPTFLRGYARAA-------HPEDFSSLRLVVAGAEKLKDTLRQEFQE--- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 328 RFKMPaecVFPAYGMAEAtlavsfAPLFtgltldvveadaleaenrAVPVPEGDPRRGTdgvrsfalLGRPLDGLEAEIV 407
Cdd:cd05909 284 KFGIR---ILEGYGTTEC------SPVI------------------SVNTPQSPNKEGT--------VGRPLPGMEVKIV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 408 DDAGK-RVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIE 485
Cdd:cd05909 329 SVETHeEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIE 408
|
330 340 350
....*....|....*....|....*....|..
gi 300790052 486 RAATSVEGVRAGNAVAVRLDaGSRRERFAVVL 517
Cdd:cd05909 409 DILSEILPEDNEVAVVSVPD-GRKGEKIVLLT 439
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
163-489 |
9.14e-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: 113.61 E-value: 9.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 163 LAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDM--------- 233
Cdd:cd17640 73 LNHSESVALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG-DRFLSILPIWHSYersaeyfif 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 234 --GMVGFLTVPMTFGVELVKITPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGRrmarvdeddAYDLSKLRIALNGA 311
Cdd:cd17640 152 acGCSQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLF---------FLSGGIFKFGISGG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 312 EPIdETAVQTFVDA-GARfkmpaecVFPAYGMAEATLAVSFAPLftgltldvveadaleaenravpvpeGDPRRGTdgvr 390
Cdd:cd17640 223 GAL-PPHVDTFFEAiGIE-------VLNGYGLTETSPVVSARRL-------------------------KCNVRGS---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 391 sfalLGRPLDGLEAEIVDDAGKRVDER-EVGEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGDLGYLV-DGQIVIC 465
Cdd:cd17640 266 ----VGRPLPGTEIKIVDPEGNVVLPPgEKGIVWVRGPQVMKGYY--KNPEATSkvlDSDGWFNTGDLGWLTcGGELVLT 339
|
330 340
....*....|....*....|....*
gi 300790052 466 GRRKDVIIM-GGRNLYPTDIERAAT 489
Cdd:cd17640 340 GRAKDTIVLsNGENVEPQPIEEALM 364
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
162-570 |
1.39e-26 |
|
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: 112.56 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 162 ELAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSWLPTFHDMGMVGFLTV 241
Cdd:cd05919 75 AYIARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 242 PMTFGV-----------ELVKITPVEFlsGPLIWpelitkyhgttTAAPNFaYAivgrRMARVDEDDAYDLSKLRIALNG 310
Cdd:cd05919 155 PLAVGAsavlnpgwptaERVLATLARF--RPTVL-----------YGVPTF-YA----NLLDSCAGSPDALRSLRLCVSA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 311 AEPIDEtavqtfvdagarfkmpaecvfpayGMAEATLAVSFAPLFTGLtlDVVEADALEAENRAvpvpeGDPRRGTdgvr 390
Cdd:cd05919 217 GEALPR------------------------GLGERWMEHFGGPILDGI--GATEVGHIFLSNRP-----GAWRLGS---- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 391 sfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTM-DGPLATQdEDGWLNTGDL-GYLVDGQIVICGRR 468
Cdd:cd05919 262 ----TGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNpEKSRATF-NGGWYRTGDKfCRDADGWYTHAGRA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 469 KDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVrdAVDMRPY 548
Cdd:cd05919 337 DDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERL--SAHKVPR 414
|
410 420
....*....|....*....|..
gi 300790052 549 AVVVLPAgsLPKTPSGKVKRAA 570
Cdd:cd05919 415 RIAFVDE--LPRTATGKLQRFK 434
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
179-568 |
7.84e-26 |
|
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: 110.46 E-value: 7.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFGVElvkitpVEFL 258
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTED-DVLLHVLPLHHVHGLVNALLCPLFAGAS------VEFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 259 SGPLIWPELITKYHGTTT---AAPNFaYAivgRRMARVDEDD-------AYDLSKLRIALNGAEPIDETAVQTFVDAGAR 328
Cdd:cd05941 163 PKFDPKEVAISRLMPSITvfmGVPTI-YT---RLLQYYEAHFtdpqfarAAAAERLRLMVSGSAALPVPTLEEWEAITGH 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 329 FkmpaecVFPAYGMAEATLAVSfAPLftgltldvveadaleaenravpvpEGDPRRGTdgvrsfalLGRPLDGLEAEIVD 408
Cdd:cd05941 239 T------LLERYGMTEIGMALS-NPL------------------------DGERRPGT--------VGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 409 D-AGKRVDEREVGEIRLRGEAVTPGYLTMdgPLATQDE---DGWLNTGDLG-YLVDGQIVICGRRKDVII-MGGRNLYPT 482
Cdd:cd05941 280 EeTGEPLPRGEVGEIQVRGPSVFKEYWNK--PEATKEEftdDGWFKTGDLGvVDEDGYYWILGRSSVDIIkSGGYKVSAL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 483 DIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLES-KLAGDAEAEKNLMKQVSARVRdavdmRPYAVVVLPAgsLPKT 561
Cdd:cd05941 358 EIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAgAAALSLEELKEWAKQRLAPYK-----RPRRLILVDE--LPRN 430
|
....*..
gi 300790052 562 PSGKVKR 568
Cdd:cd05941 431 AMGKVNK 437
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
164-570 |
1.37e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 109.84 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 164 AAAEPLPDVVVTDEgDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMvGFLTVPM 243
Cdd:cd05922 104 AARASAPAHEVSHE-DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD-DRALTVLPLSYDYGL-SVLNTHL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 244 TFGVELVkITPvEFLSGPLIWpELITKYHGTTTAAPNFAYAIvgrrMARVDEDDAyDLSKLRIALNGAEPIDETAVQTFv 323
Cdd:cd05922 181 LRGATLV-LTN-DGVLDDAFW-EDLREHGATGLAGVPSTYAM----LTRLGFDPA-KLPSLRYLTQAGGRLPQETIARL- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 324 dagaRFKMPAECVFPAYGMAEATLAVSFAPlftgltldvveadaleaenravpvPEGDPRRGTDgvrsfalLGRPLDGLE 403
Cdd:cd05922 252 ----RELLPGAQVYVMYGQTEATRRMTYLP------------------------PERILEKPGS-------IGLAIPGGE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 404 AEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDE-DGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYP 481
Cdd:cd05922 297 FEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRgGGVLHTGDLARRdEDGFLFIVGRRDRMIKLFGNRISP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 482 TDIERAATSVEGVRAGNAVAVRLDAGsrrERFAVVLESKLAGDAEAeknLMKQVSARVRDAvdMRPYAVVVLpaGSLPKT 561
Cdd:cd05922 377 TEIEAAARSIGLIIEAAAVGLPDPLG---EKLALFVTAPDKIDPKD---VLRSLAERLPPY--KVPATVRVV--DELPLT 446
|
....*....
gi 300790052 562 PSGKVKRAA 570
Cdd:cd05922 447 ASGKVDYAA 455
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
24-568 |
6.62e-25 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 109.05 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 24 GEPKEPVRRTWAEVHEEARRIAGGLVAGGFERG------------TAVGVLAAApvliapTVQAVWlaggSV--TMLhqp 89
Cdd:COG0365 32 GEDGEERTLTYAELRREVNRFANALRALGVKKGdrvaiylpnipeAVIAMLACA------RIGAVH----SPvfPGF--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 90 TPRtDLAEWAEDT-VRVLgmIGSDQDALGG-PGGLAPR----PGSGAGPRNVTVllgepFDQLAPVLEQKGIgFQLITEL 163
Cdd:COG0365 99 GAE-ALADRIEDAeAKVL--ITADGGLRGGkVIDLKEKvdeaLEELPSLEHVIV-----VGRTGADVPMEGD-LDWDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 164 AAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMverAEFDFDV---DVM-----VSWLptfhdMGM 235
Cdd:COG0365 170 AAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATT---AKYVLDLkpgDVFwctadIGWA-----TGH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 236 VGFLTVPMTFGVELVkitpveFLSGPLIWP------ELITKYHGTTT-AAPNfAYaivgRRMARVDED--DAYDLSKLRI 306
Cdd:COG0365 242 SYIVYGPLLNGATVV------LYEGRPDFPdpgrlwELIEKYGVTVFfTAPT-AI----RALMKAGDEplKKYDLSSLRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 307 ALNGAEPIDETAVQTFVDAgarFKMPaecVFPAYGMAEATLAVsfaplftgltldvveadaleaenrAVPVPEGDPRRGT 386
Cdd:COG0365 311 LGSAGEPLNPEVWEWWYEA---VGVP---IVDGWGQTETGGIF------------------------ISNLPGLPVKPGS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 387 dgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGE--AVTPGYLtmDGPLATQDE-----DGWLNTGDLGYL-V 458
Cdd:COG0365 361 --------MGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYW--NDPERYRETyfgrfPGWYRTGDGARRdE 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 459 DGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRagNAVAV-RLDAGsRRER---FaVVLESKLAGDAEAEKNLMKQ 534
Cdd:COG0365 431 DGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVA--EAAVVgVPDEI-RGQVvkaF-VVLKPGVEPSDELAKELQAH 506
|
570 580 590
....*....|....*....|....*....|....
gi 300790052 535 VSARVrdAVDMRPYAVVVLPAgsLPKTPSGKVKR 568
Cdd:COG0365 507 VREEL--GPYAYPREIEFVDE--LPKTRSGKIMR 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
170-570 |
1.65e-24 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 106.62 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 170 PDVVVTDEGDTALLQLTSGSTADPKAVRITYGNlysnVKAMVERAEFDFDVDVMVSWLpTFHDMGM---VGFLTVPMTFG 246
Cdd:cd17643 85 PSLLLTDPDDLAYVIYTSGSTGRPKGVVVSHAN----VLALFAATQRWFGFNEDDVWT-LFHSYAFdfsVWEIWGALLHG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 247 VELVKI------TPVEFLSgpLIWPELITKYHGTTTAapnFayaivgRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQ 320
Cdd:cd17643 160 GRLVVVpyevarSPEDFAR--LLRDEGVTVLNQTPSA---F------YQLVEAADRDGRDPLALRYVIFGGEALEAAMLR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 321 TFVdagARFKMPAECVFPAYGMAEATLAVSFAPLftgltldvVEADALEAENravpvpegdprrgtdgvrsfALLGRPLD 400
Cdd:cd17643 229 PWA---GRFGLDRPQLVNMYGITETTVHVTFRPL--------DAADLPAAAA--------------------SPIGRPLP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 401 GLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQ---DEDG-----WLNTGDLG-YLVDGQIVICGRRKDV 471
Cdd:cd17643 278 GLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERfvaNPFGgpgsrMYRTGDLArRLPDGELEYLGRADEQ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 472 IIMGGRNLYPTDIERAATSVEGVRAGnAVAVRLDA-GSRRERFAVVLESKLAGDAEAEKNLMKqvsARVRDAvdMRPYAV 550
Cdd:cd17643 358 VKIRGFRIELGEIEAALATHPSVRDA-AVIVREDEpGDTRLVAYVVADDGAAADIAELRALLK---ELLPDY--MVPARY 431
|
410 420
....*....|....*....|
gi 300790052 551 VVLPAgsLPKTPSGKVKRAA 570
Cdd:cd17643 432 VPLDA--LPLTVNGKLDRAA 449
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
31-568 |
6.11e-23 |
|
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: 102.45 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 31 RRTWAEVHEEARRIAGGLVAGGFERGTAVG-VLAAAPVLIAPTVQAVwLAGGSVTMLHQPTPRTDLAEWAEDtvrvlgmi 109
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLlIMLDTVDFPTAFLGAI-RAGIVPVPVNTLLTPDDYAYYLED-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 gSDQDALGGPGGLAPRPGS---GAGPRNVTVLLGEPFDQLAPVLeqkgigfQLITELAAAEPLPDVVVTDEGDTALLQLT 186
Cdd:cd05959 100 -SRARVVVVSGELAPVLAAaltKSEHTLVVLIVSGGAGPEAGAL-------LLAELVAAEAEQLKPAATHADDPAFWLYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 187 SGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSWLPTFHDMGMVGFLTVPMTFGVELV----KITPVEFLsgpl 262
Cdd:cd05959 172 SGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVlmpeRPTPAAVF---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 263 iwpELITKYHGTTT-AAPNFaYAivgrRMARVDEDDAYDLSKLRIALNGAEPIDEtavqtfvDAGARFKMpaecvfpayg 341
Cdd:cd05959 248 ---KRIRRYRPTVFfGVPTL-YA----AMLAAPNLPSRDLSSLRLCVSAGEALPA-------EVGERWKA---------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 342 maeatlavsfaplFTGLT-LDVV---EADALEAENRAvpvpeGDPRRGTDGvrsfallgRPLDGLEAEIVDDAGKRVDER 417
Cdd:cd05959 303 -------------RFGLDiLDGIgstEMLHIFLSNRP-----GRVRYGTTG--------KPVPGYEVELRDEDGGDVADG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 418 EVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDlGYLV--DGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVR 495
Cdd:cd05959 357 EPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGD-KYVRddDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVL 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300790052 496 AGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVrdAVDMRPYAVVVLpaGSLPKTPSGKVKR 568
Cdd:cd05959 436 EAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRL--APYKYPRWIVFV--DELPKTATGKIQR 504
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
179-575 |
7.63e-23 |
|
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: 99.71 E-value: 7.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSwLPTFHDMGMvGFLTVPMTFGVELVKITPVefl 258
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLS-LPLYHVGGL-AILVRSLLAGAELVLLERN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 259 sgpliWPELITKYHGTTTAApnfayAIVGRRMARVDEDDAY--DLSKLRIALNGAEPIDETAVQTFVDAGARfkmpaecV 336
Cdd:cd17630 76 -----QALAEDLAPPGVTHV-----SLVPTQLQRLLDSGQGpaALKSLRAVLLGGAPIPPELLERAADRGIP-------L 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 337 FPAYGMAEatlavsFAPLFTGLTLDvveadaleaenravpvpegDPRRGTDgvrsfallGRPLDGLEAEIVDDagkrvde 416
Cdd:cd17630 139 YTTYGMTE------TASQVATKRPD-------------------GFGRGGV--------GVLLPGRELRIVED------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 417 revGEIRLRGEAVTPGYLTMDGPLATqDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVR 495
Cdd:cd17630 179 ---GEIWVGGASLAMGYLRGQLVPEF-NEDGWFTTKDLGELhADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 496 AGNAVAVrldaGSRR--ERFAVVLESklagdaeAEKNLMKQVSARVRDAVD--MRPYAVVVLPAgsLPKTPSGKVKRAAT 571
Cdd:cd17630 255 DAFVVGV----PDEElgQRPVAVIVG-------RGPADPAELRAWLKDKLArfKLPKRIYPVPE--LPRTGGGKVDRRAL 321
|
....
gi 300790052 572 AQQF 575
Cdd:cd17630 322 RAWL 325
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
30-568 |
1.21e-22 |
|
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: 101.22 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 30 VRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGsvtmlhqptprtdlaewaedtvrVLGMI 109
Cdd:cd12118 28 RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGA-----------------------VLNAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 GSDQDAlggpgglaprpgsgagpRNVTVLLGEPFDQLAPVLEQkgigFQLITELAAAEPLPD-VVVTDEGDTALLQLTSG 188
Cdd:cd12118 85 NTRLDA-----------------EEIAFILRHSEAKVLFVDRE----FEYEDLLAEGDPDFEwIPPADEWDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 189 STADPKAVRITYGNLYSNvkAMVERAEFDFDVDVMVSW-LPTFHDMGMVGFLTVPMTFG--VELVKITPveflsgPLIWp 265
Cdd:cd12118 144 TTGRPKGVVYHHRGAYLN--ALANILEWEMKQHPVYLWtLPMFHCNGWCFPWTVAAVGGtnVCLRKVDA------KAIY- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 266 ELITKYHGT-TTAAPnfayaIVGRRMARVDEDDAYDLS-KLRIALNGAEPidetavqtfvDAGARFKMPAE--CVFPAYG 341
Cdd:cd12118 215 DLIEKHKVThFCGAP-----TVLNMLANAPPSDARPLPhRVHVMTAGAPP----------PAAVLAKMEELgfDVTHVYG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 342 MAEATLAVSFAPLFTgltldvvEADALEAENRAVpvpegdpRRGTDGVRSFALLgrPLDGLEAEIVDDAGKrvDEREVGE 421
Cdd:cd12118 280 LTETYGPATVCAWKP-------EWDELPTEERAR-------LKARQGVRYVGLE--EVDVLDPETMKPVPR--DGKTIGE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 422 IRLRGEAVTPGYLtmDGPLATQD--EDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGn 498
Cdd:cd12118 342 IVFRGNIVMKGYL--KNPEATAEafRGGWFHSGDLAVIhPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEA- 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300790052 499 AVAVRLDagsrrERFAVVLES--KLAGDAEA-EKNLMKQvsARVRDAVDMRPYAVVVLPagsLPKTPSGKVKR 568
Cdd:cd12118 419 AVVARPD-----EKWGEVPCAfvELKEGAKVtEEEIIAF--CREHLAGFMVPKTVVFGE---LPKTSTGKIQK 481
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
171-584 |
2.56e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 100.88 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 171 DVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSN----VKAMVERAEFDfdvDVMVSWLPTFHDMGMVGFLTVPMTFG 246
Cdd:PRK06710 199 EVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNtlmgVQWLYNCKEGE---EVVLGVLPFFHVYGMTAVMNLSIMQG 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 247 VELVKITPVEFlsgPLIWpELITKYHGTT-TAAPNFAYAIVGRRMARvdeddAYDLSKLRIALNGAEPIDETAVQTF--V 323
Cdd:PRK06710 276 YKMVLIPKFDM---KMVF-EAIKKHKVTLfPGAPTIYIALLNSPLLK-----EYDISSIRACISGSAPLPVEVQEKFetV 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 324 DAGArfkmpaecVFPAYGMAEATlavsfaplftgltlDVVEADALeAENRavpVPegdprrGTDGVrsfallgrPLDGLE 403
Cdd:PRK06710 347 TGGK--------LVEGYGLTESS--------------PVTHSNFL-WEKR---VP------GSIGV--------PWPDTE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 404 AEIVD-DAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYP 481
Cdd:PRK06710 387 AMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMdEDGFFYVKDRKKDMIVASGFNVYP 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 482 TDIERAATSVEGVRagNAVAVRLDAGSRRER---FAVVLESKLAGDAEAEKNLMKQVSA-RVRDAVDMRpyavvvlpaGS 557
Cdd:PRK06710 467 REVEEVLYEHEKVQ--EVVTIGVPDPYRGETvkaFVVLKEGTECSEEELNQFARKYLAAyKVPKVYEFR---------DE 535
|
410 420
....*....|....*....|....*..
gi 300790052 558 LPKTPSGKVKRAATAQQfadRIKKNAD 584
Cdd:PRK06710 536 LPKTTVGKILRRVLIEE---EKRKNED 559
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
172-570 |
3.50e-22 |
|
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: 99.33 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 172 VVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMvsWlpTFHDMGMVGFL----TVPMTFGV 247
Cdd:cd05972 75 AIVTDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPD-DIH--W--NIADPGWAKGAwssfFGPWLLGA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 248 ELVKITPVEFlsGPLIWPELITKYHGTTTAAPNFAYaivgRRMARVDEDdAYDLSKLRIALNGAEPIDETAVQTFVDAga 327
Cdd:cd05972 150 TVFVYEGPRF--DAERILELLERYGVTSFCGPPTAY----RMLIKQDLS-SYKFSHLRLVVSAGEPLNPEVIEWWRAA-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 328 rFKMPaecVFPAYGMAEatlavsfaplfTGLTLDVVeadaleaenRAVPVPEGDprrgtdgvrsfalLGRPLDGLEAEIV 407
Cdd:cd05972 221 -TGLP---IRDGYGQTE-----------TGLTVGNF---------PDMPVKPGS-------------MGRPTPGYDVAII 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 408 DDAGKRVDEREVGEIRLRGEAVTP--GYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDI 484
Cdd:cd05972 264 DDDGRELPPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGDYYLTGDRAYRdEDGYFWFVGRADDIIKSSGYRIGPFEV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 485 ERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESklagDAEAEKNLMKQVSARVRDAVDMRPYAVVVLPAGSLPKTPSG 564
Cdd:cd05972 344 ESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTS----GYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISG 419
|
....*.
gi 300790052 565 KVKRAA 570
Cdd:cd05972 420 KIRRVE 425
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
179-568 |
3.02e-21 |
|
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: 94.88 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFGVELVkitPVEFL 258
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTED-DRYLIINPFFHTFGYKAGIVACLLTGATVV---PVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 259 SGPLIWPELITKYHGTTTAAPNFAYAIVGrrmarVDEDDAYDLSKLRIALNGAEPIDETAVQTFvdagaRFKMPAECVFP 338
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLD-----HPGRKKFDLSSLRAAVTGAATVPVELVRRM-----RSELGFETVLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 339 AYGMAEATLAVSFAPlftgltldvveadaleaenravpvpegdprrGTDGVRSFALLGRPLDGLEAEIVDDagkrvdere 418
Cdd:cd17638 147 AYGLTEAGVATMCRP-------------------------------GDDAETVATTCGRACPGFEVRIADD--------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 419 vGEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGDLGYLVD-GQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGV 494
Cdd:cd17638 187 -GEVLVRGYNVMQGYL--DDPEATAeaiDADGWLHTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGV 263
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300790052 495 RAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAeknlmkqVSARVRDavDMRPYAV--VVLPAGSLPKTPSGKVKR 568
Cdd:cd17638 264 AQVAVIGVPDERMGEVGKAFVVARPGVTLTEED-------VIAWCRE--RLANYKVprFVRFLDELPRNASGKVMK 330
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
172-568 |
3.52e-21 |
|
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: 96.39 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 172 VVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFGVELVK 251
Cdd:cd05935 78 VVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS-DVILACLPLFHVTGFVGSLNTAVYVGGTYVL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 252 ITpveflsgplIW-----PELITKYHGT-TTAAPnfayAIVGRRMARVdEDDAYDLSKLRIALNGAEPIDETAVQTFVD- 324
Cdd:cd05935 157 MA---------RWdretaLELIEKYKVTfWTNIP----TMLVDLLATP-EFKTRDLSSLKVLTGGGAPMPPAVAEKLLKl 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 325 AGARFkmpaecvFPAYGMAEAtlavsFAPLFTGltldvveadaleaenravpvPEGDPRRGTdgvrsfalLGRPLDGLEA 404
Cdd:cd05935 223 TGLRF-------VEGYGLTET-----MSQTHTN--------------------PPLRPKLQC--------LGIP*FGVDA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 405 EIVD-DAGKRVDEREVGEIRLRGEAVTPGYltMDGPLATQD---EDG---WLNTGDLGYL-VDGQIVICGRRKDVIIMGG 476
Cdd:cd05935 263 RVIDiETGRELPPNEVGEIVVRGPQIFKGY--WNRPEETEEsfiEIKgrrFFRTGDLGYMdEEGYFFFVDRVKRMINVSG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 477 RNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEkNLMKQvsARVRDAVDMRPYAVVVLPag 556
Cdd:cd05935 341 FKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE-DIIEW--AREQMAAYKYPREVEFVD-- 415
|
410
....*....|..
gi 300790052 557 SLPKTPSGKVKR 568
Cdd:cd05935 416 ELPRSASGKILW 427
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
33-582 |
5.22e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 96.59 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEdTVRVLGMIGSD 112
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAE-AAGAKLIVTND 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 QD-----ALGGPgglaprpgsgagprnvTVLLGEpfDQLAPVLEQKGIgfqliteLAAAEPLPDVVVTDE---GDTALLQ 184
Cdd:PLN02330 136 TNygkvkGLGLP----------------VIVLGE--EKIEGAVNWKEL-------LEAADRAGDTSDNEEilqTDLCALP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 185 LTSGSTADPKAVRITYGNLYSNVKAMV--ERAEFDFDVdVMVSWLPTFHDMGMVGFLTVPMTFGVELVKITPVE---FLS 259
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVANLCSSLfsVGPEMIGQV-VTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFElrtFLN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 260 GpliwpeLITKYHGTTTAAPNFAYAIVGRRMarVDEddaYDLSKLRI--ALNGAEPIDETAVQTFVDagarfKMPAECVF 337
Cdd:PLN02330 270 A------LITQEVSFAPIVPPIILNLVKNPI--VEE---FDLSKLKLqaIMTAAAPLAPELLTAFEA-----KFPGVQVQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 338 PAYGMAEatlavsfaplftgltldvveadaleaeNRAVPVPEGDPRRGtDGVRSFALLGRPLDGLEAEIVD-DAGKRVDE 416
Cdd:PLN02330 334 EAYGLTE---------------------------HSCITLTHGDPEKG-HGIAKKNSVGFILPNLEVKFIDpDTGRSLPK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 417 REVGEIRLRGEAVTPGYLTMDGPLA-TQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIER---AATSV 491
Cdd:PLN02330 386 NTPGELCVRSQCVMQGYYNNKEETDrTIDEDGWLHTGDIGYIdDDGDIFIVDRIKELIKYKGFQVAPAELEAillTHPSV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 492 EGVragnAVAVRLDAGSRRERFAVVLESKLAgdAEAEKNLMKQVSARVRDAVDMRpyavVVLPAGSLPKTPSGKVKRAAT 571
Cdd:PLN02330 466 EDA----AVVPLPDEEAGEIPAACVVINPKA--KESEEDILNFVAANVAHYKKVR----VVQFVDSIPKSLSGKIMRRLL 535
|
570
....*....|.
gi 300790052 572 AQQFADRIKKN 582
Cdd:PLN02330 536 KEKMLSINKAN 546
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
2-578 |
5.89e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.49 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 2 SRFVDTLVATATKRGQQRGMVTGEPKEPVrrTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGG 81
Cdd:PRK05852 16 PRIADLVEVAATRLPEAPALVVTADRIAI--SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 82 SVTMLHQPTPRTDLAewaeDTVRVLGMIGSDQDALGgPGGLAPrPGSGAGPRNVTVllgepfdqlAPVLEQKGiGFQLIT 161
Cdd:PRK05852 94 VVVPLDPALPIAEQR----VRSQAAGARVVLIDADG-PHDRAE-PTTRWWPLTVNV---------GGDSGPSG-GTLSVH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 162 ELAAAEPLPdVVVTDEG---DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDfDVDVMVSWLPTFHDMGMVGF 238
Cdd:PRK05852 158 LDAATEPTP-ATSTPEGlrpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLS-PRDATVAVMPLYHGHGLIAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 239 LTVPMTFGVELVKITPVEFlSGPLIWPELITKYHGTTTAAPNFaYAIVGRRMArvDEDDAYDLSKLRIALNGAEPIDETA 318
Cdd:PRK05852 236 LLATLASGGAVLLPARGRF-SAHTFWDDIKAVGATWYTAVPTI-HQILLERAA--TEPSGRKPAALRFIRSCSAPLTAET 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 319 VQTFVDagaRFKMPAECvfpAYGMAEATLAVSfaplftglTLDVVEADaleaenravpvpegdprRGTDGVRSFALLGRP 398
Cdd:PRK05852 312 AQALQT---EFAAPVVC---AFGMTEATHQVT--------TTQIEGIG-----------------QTENPVVSTGLVGRS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 399 lDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGR 477
Cdd:PRK05852 361 -TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLsAAGDLSIRGRIKELINRGGE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 478 NLYPTDIERAATSVEGVRAgNAVAVRLDAGSRRERFAVVLESKLAGDAEAEknlmkqVSARVRDAVDMRPYAVVVLPAGS 557
Cdd:PRK05852 440 KISPERVEGVLASHPNVME-AAVFGVPDQLYGEAVAAVIVPRESAPPTAEE------LVQFCRERLAAFEIPASFQEASG 512
|
570 580
....*....|....*....|.
gi 300790052 558 LPKTPSGKVKRAATAQQFADR 578
Cdd:PRK05852 513 LPHTAKGSLDRRAVAEQFGHS 533
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
160-568 |
7.37e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 96.20 E-value: 7.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 160 ITELAAA--EPLPDVVVTDEgDTALLQLTSGSTADPKAVRITYGNLYSNVKAMV--ERAEFDFDV-DVMVSWLPTFHDMG 234
Cdd:PLN02246 160 FSELTQAdeNELPEVEISPD-DVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVdgENPNLYFHSdDVILCVLPMFHIYS 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 235 MVGFLTVPMTFGVELVkITPvEFLSGPLIwpELITKYHgtTTAAPnFAYAIVgRRMARVDEDDAYDLSKLRIALNGAEPI 314
Cdd:PLN02246 239 LNSVLLCGLRVGAAIL-IMP-KFEIGALL--ELIQRHK--VTIAP-FVPPIV-LAIAKSPVVEKYDLSSIRMVLSGAAPL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 315 DETAVQTFvdagaRFKMPAECVFPAYGMAEATLAVSFAPLFtgltldvveadALEaenravPVPegdprrgtdgVRSFAl 394
Cdd:PLN02246 311 GKELEDAF-----RAKLPNAVLGQGYGMTEAGPVLAMCLAF-----------AKE------PFP----------VKSGS- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 LGRPLDGLEAEIVD-DAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGDLGYL-VDGQIVICGRRK 469
Cdd:PLN02246 358 CGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYL--NDPEATAntiDKDGWLHTGDIGYIdDDDELFIVDRLK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 470 DVIIMGGRNLYPTDIERAATSVEGVrAGNAVAVRLD--AGSRRERFAVVLE-SKLAGDaEAEKNLMKQV--SARVRDavd 544
Cdd:PLN02246 436 ELIKYKGFQVAPAELEALLISHPSI-ADAAVVPMKDevAGEVPVAFVVRSNgSEITED-EIKQFVAKQVvfYKRIHK--- 510
|
410 420
....*....|....*....|....
gi 300790052 545 mrpyavvVLPAGSLPKTPSGKVKR 568
Cdd:PLN02246 511 -------VFFVDSIPKAPSGKILR 527
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
170-568 |
7.99e-21 |
|
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: 96.06 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 170 PDVVVTDEgDTALLQLTSGSTADPKAVRITYGNL---YSNVKAMVERAEFDFDVDVMvSWLPTFHDMGMVGFLTVpMTFG 246
Cdd:cd17642 177 PPSFDRDE-QVALIMNSSGSTGLPKGVQLTHKNIvarFSHARDPIFGNQIIPDTAIL-TVIPFHHGFGMFTTLGY-LICG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 247 VELVKITPVE---FLSGpliwpelITKYHGTTT--AAPNFAYaivgrrMARVDEDDAYDLSKLRIALNGAEPID-ETAVQ 320
Cdd:cd17642 254 FRVVLMYKFEeelFLRS-------LQDYKVQSAllVPTLFAF------FAKSTLVDKYDLSNLHEIASGGAPLSkEVGEA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 321 TfvdaGARFKMPAecVFPAYGMAEATLAVsfapLFTgltldvveadaleaenravpvPEGDPRRGTdgvrsfalLGRPLD 400
Cdd:cd17642 321 V----AKRFKLPG--IRQGYGLTETTSAI----LIT---------------------PEGDDKPGA--------VGKVVP 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 401 GLEAEIVD-DAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMG 475
Cdd:cd17642 362 FFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYV--NNPEATKaliDKDGWLHSGDIAYYdEDGHFFIVDRLKSLIKYK 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 476 GRNLYPTDIERAATSVEGVR-AGNAVAVRLDAGSRRERFaVVLEsklAGDAEAEKNLMKQVSARVRDAVDMRPYAVVVlp 554
Cdd:cd17642 440 GYQVPPAELESILLQHPKIFdAGVAGIPDEDAGELPAAV-VVLE---AGKTMTEKEVMDYVASQVSTAKRLRGGVKFV-- 513
|
410
....*....|....
gi 300790052 555 aGSLPKTPSGKVKR 568
Cdd:cd17642 514 -DEVPKGLTGKIDR 526
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
33-568 |
3.06e-20 |
|
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: 94.07 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGG-SVTMLHQPTPRT--DLAEWAEDTVRVLGMI 109
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHiSVPLYPTLNPDTirYVLEHSESKALFVGKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 GSDQD-ALGGPGGLAPRPGSGAGPRNVTvllgEPFDQLapvleqkgigfqliteLAAAEPLPDVVVTDEGDTALLQLTSG 188
Cdd:cd05932 88 DDWKAmAPGVPEGLISISLPPPSAANCQ----YQWDDL----------------IAQHPPLEERPTRFPEQLATLIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 189 STADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFH-------DMG------MVGFLTVPMTFGVELVKITPV 255
Cdd:cd05932 148 TTGQPKGVMLTFGSFAWAAQAGIEHIGTEEN-DRMLSYLPLAHvtervfvEGGslyggvLVAFAESLDTFVEDVQRARPT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 256 EFLSGPLIWpeliTKY-HGTTTAAPN----------FAYAIVGRRMArvdedDAYDLSKLRIALNGAEPIDETAVQTFVD 324
Cdd:cd05932 227 LFFSVPRLW----TKFqQGVQDKIPQqklnlllkipVVNSLVKRKVL-----KGLGLDQCRLAGCGSAPVPPALLEWYRS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 325 AGARfkmpaecVFPAYGMAEaTLAVSFaplftgltldvveadaleaenraVPVPeGDPRRGTdgvrsfalLGRPLDGLEA 404
Cdd:cd05932 298 LGLN-------ILEAYGMTE-NFAYSH-----------------------LNYP-GRDKIGT--------VGNAGPGVEV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 405 EIVDDagkrvderevGEIRLRGEAVTPGYLTmdGPLATQ---DEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMG-GRNL 479
Cdd:cd05932 338 RISED----------GEILVRSPALMMGYYK--DPEATAeafTADGFLRTGDKGELdADGNLTITGRVKDIFKTSkGKYV 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 480 YPTDIERAATSVEGVRAgnavAVRLDAGSRRERFAVVL--ESKLAGDAEAEKNL---MKQVSARVRDAVDMRP---YAVV 551
Cdd:cd05932 406 APAPIENKLAEHDRVEM----VCVIGSGLPAPLALVVLseEARLRADAFARAELeasLRAHLARVNSTLDSHEqlaGIVV 481
|
570 580
....*....|....*....|
gi 300790052 552 VLPAGSLPK---TPSGKVKR 568
Cdd:cd05932 482 VKDPWSIDNgilTPTLKIKR 501
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
153-568 |
3.36e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 94.44 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 153 KGIGFQLITELAAAEPLPDVVVtDEGDTALLQLTSGSTADPKAVRITYGNLYSN---VKAMVErAEFDFDVDVMVSWLP- 228
Cdd:PRK05677 183 QAVKFNDALAKGAGQPVTEANP-QADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMG-SNLNEGCEILIAPLPl 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 229 ------TFHDMGMvgfltvpMTFGVELVKItpveflSGPLIWPELI-----TKYHGTTTAAPNFAyAIVGRRMARvdedd 297
Cdd:PRK05677 261 yhiyafTFHCMAM-------MLIGNHNILI------SNPRDLPAMVkelgkWKFSGFVGLNTLFV-ALCNNEAFR----- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 298 AYDLSKLRIALNGAepideTAVQTfvDAGARFKMPAEC-VFPAYGMAEATLAVSFAPLftgltldvveadaleaenravp 376
Cdd:PRK05677 322 KLDFSALKLTLSGG-----MALQL--ATAERWKEVTGCaICEGYGMTETSPVVSVNPS---------------------- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 377 vpeGDPRRGTdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMdgPLATQ---DEDGWLNTGD 453
Cdd:PRK05677 373 ---QAIQVGT--------IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQR--PEATDeilDSDGWLKTGD 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 454 LGYLV-DGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLM 532
Cdd:PRK05677 440 IALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHM 519
|
410 420 430
....*....|....*....|....*....|....*...
gi 300790052 533 K-QVSA-RVRDAVDMRpyavvvlpaGSLPKTPSGKVKR 568
Cdd:PRK05677 520 RaNLTGyKVPKAVEFR---------DELPTTNVGKILR 548
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
130-577 |
5.14e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 93.40 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 130 AGPRnVTVLLGEPFDQLAPVLEQKGIG--FQL-------ITELAAAEPLP-DVVVTDEGDTALLQLTSGSTADPKAVRIT 199
Cdd:PRK07514 99 AEPA-LVVCDPANFAWLSKIAAAAGAPhvETLdadgtgsLLEAAAAAPDDfETVPRGADDLAAILYTSGTTGRSKGAMLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 200 YGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMvgfltvpmtfgveLVKITPVEFLSGPLIW-----PELITKYHGT 274
Cdd:PRK07514 178 HGNLLSNALTLVDYWRFTPD-DVLIHALPIFHTHGL-------------FVATNVALLAGASMIFlpkfdPDAVLALMPR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 275 TTA---APNFaYAivgrRM---ARVDEDDAydlSKLRIALNGAEPIdetAVQTFVDAGARfkmPAECVFPAYGMAEATLA 348
Cdd:PRK07514 244 ATVmmgVPTF-YT----RLlqePRLTREAA---AHMRLFISGSAPL---LAETHREFQER---TGHAILERYGMTETNMN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 349 VSfAPLftgltldvveadaleaenravpvpEGDPRRGTdgvrsfalLGRPLDGLEAEIVD-DAGKRVDEREVGEIRLRGE 427
Cdd:PRK07514 310 TS-NPY------------------------DGERRAGT--------VGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGP 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 428 AVTPGYLTMdgPLATQDE---DGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVR-------- 495
Cdd:PRK07514 357 NVFKGYWRM--PEKTAEEfraDGFFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVesavigvp 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 496 ------AGNAVAVRLDAGSRRERfAVV--LESKLAGdaeaeknlMKQvsarvrdavdmrPYAVVVLPAgsLPKTPSGKVK 567
Cdd:PRK07514 435 hpdfgeGVTAVVVPKPGAALDEA-AILaaLKGRLAR--------FKQ------------PKRVFFVDE--LPRNTMGKVQ 491
|
490
....*....|
gi 300790052 568 RAATAQQFAD 577
Cdd:PRK07514 492 KNLLREQYAD 501
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
179-568 |
8.52e-20 |
|
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: 90.78 E-value: 8.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSWLPTFHDMGMVGFLTVPMTFGVelvKITPVEFL 258
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGL---CVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 259 SGPLIWPELITKYHGTTTAAPNFAYAIVGRRMARVDEddaydLSKLRIALNGAEPIDETAVQTFVdagarfKMPAECVFP 338
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANAT-----VPSLRLIGYGGSRAIAADVRFIE------ATGLTNTAQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 339 AYGMAEATLAvsfapLFTGLTLDVVEADALeaenravpvpegdprrgtdgvrsfallGRPLDGLEAEIVDDAGKRVDERE 418
Cdd:cd17635 148 VYGLSETGTA-----LCLPTDDDSIEINAV---------------------------GRPYPGVDVYLAATDGIAGPSAS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 419 VGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYLV-DGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAG 497
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERReDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQEC 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300790052 498 nAVAVRLDagsrrERFAVVLESKLAGDAEAEKNLMKQVSARVRDAVD--MRPYAVVVLPagSLPKTPSGKVKR 568
Cdd:cd17635 276 -ACYEISD-----EEFGELVGLAVVASAELDENAIRALKHTIRRELEpyARPSTIVIVT--DIPRTQSGKVKR 340
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
33-566 |
4.08e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 90.72 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDTVRVLGMIGSD 112
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 QDALggPGGLAPRPGSGAGPRNVTVLLGEPfdqlapvleqkgigfqlitelaaAEPLPDVVVTDEGDTALLQLTSGSTAD 192
Cdd:PRK06145 109 FDAI--VALETPKIVIDAAAQADSRRLAQG-----------------------GLEIPPQAAVAPTDLVRLMYTSGTTDR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 193 PKAVRITYGNLY----SNVKAMVERAEFDFDV-----DVMVSWLPTFHDMGMVGFLTVPMTFGVELV-KITPVEFLSGPL 262
Cdd:PRK06145 164 PKGVMHSYGNLHwksiDHVIALGLTASERLLVvgplyHVGAFDLPGIAVLWVGGTLRIHREFDPEAVlAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 263 IWPELITkyhgtttaapnfayaivgrRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTF--VDAGARFkmpaecvFPAY 340
Cdd:PRK06145 244 MAPVMLS-------------------RVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFtrVFTRARY-------IDAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 341 GMAEAtlavsfaplftgltldvVEADALEAENRAVpvpegdprrgtDGVRSfalLGRPLDGLEAEIVDDAGKRVDEREVG 420
Cdd:PRK06145 298 GLTET-----------------CSGDTLMEAGREI-----------EKIGS---TGRALAHVEIRIADGAGRWLPPNMKG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 421 EIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYLVD-GQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNA 499
Cdd:PRK06145 347 EICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEeGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAV 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300790052 500 VAVRLDAGSRRERFAVVLEsklAGDAEAEKNLMKQVSARVRDAVDMRPYAVVvlpaGSLPKTPSGKV 566
Cdd:PRK06145 427 IGVHDDRWGERITAVVVLN---PGATLTLEALDRHCRQRLASFKVPRQLKVR----DELPRNPSGKV 486
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
30-568 |
4.15e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 90.76 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 30 VRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLA---AAPVLiaptvqaVWLAGGSVTMLHQPTprtDLAEWAEDTVRVL 106
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGhnsDAYAL-------LWLACARAGAVHVPV---NFMLTGEELAYIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 107 GMIGSDqdALGGPGGLAPRPGSGAGPRNVTVLLGEPFDQLAPVleqkGIGFQLITELAAAEP--LPDVVVTDEgDTALLQ 184
Cdd:PRK08316 105 DHSGAR--AFLVDPALAPTAEAALALLPVDTLILSLVLGGREA----PGGWLDFADWAEAGSvaEPDVELADD-DLAQIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 185 LTSGSTADPKAVRITYGNLYSN-VKAMVErAEFDFDvDVMVSWLPTFHDMGMVGFLtvpMTF------GVELVKITPVEF 257
Cdd:PRK08316 178 YTSGTESLPKGAMLTHRALIAEyVSCIVA-GDMSAD-DIPLHALPLYHCAQLDVFL---GPYlyvgatNVILDAPDPELI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 258 LsgPLIWPELITKYhgtttaapnFAYAIVGRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFvdagaRFKMPAECVF 337
Cdd:PRK08316 253 L--RTIEAERITSF---------FAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKEL-----RERLPGLRFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 338 PAYGMAEatlavsFAPLFTGLTldvveadaleaenravpvPEGDPRRGTDGvrsfallGRPLDGLEAEIVDDAGKRVDER 417
Cdd:PRK08316 317 NCYGQTE------IAPLATVLG------------------PEEHLRRPGSA-------GRPVLNVETRVVDDDGNDVAPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 418 EVGEIRLRGEAVTPGYLtmDGPLATQD--EDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGV 494
Cdd:PRK08316 366 EVGEIVHRSPQLMLGYW--DDPEKTAEafRGGWFHSGDLGVMdEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 495 ragNAVAVrldAGSRRERF------AVVLEsklAGDAEAEKNLMKQVSARVrdAVDMRPYAVVVLPagSLPKTPSGKV-K 567
Cdd:PRK08316 444 ---AEVAV---IGLPDPKWieavtaVVVPK---AGATVTEDELIAHCRARL--AGFKVPKRVIFVD--ELPRNPSGKIlK 510
|
.
gi 300790052 568 R 568
Cdd:PRK08316 511 R 511
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
163-585 |
4.86e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 91.57 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 163 LAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVP 242
Cdd:PRK06814 778 LAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPE-DKVFNALPVFHSFGLTGGLVLP 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 243 MTFGVelvkitPVEFLSGPL---IWPELI-----TKYHGTTTAAPNFAyaivgrRMArvdedDAYDLSKLRIALNGAEPI 314
Cdd:PRK06814 857 LLSGV------KVFLYPSPLhyrIIPELIydtnaTILFGTDTFLNGYA------RYA-----HPYDFRSLRYVFAGAEKV 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 315 DETAVQTFVDA-GARfkmpaecVFPAYGMAEAT--LAVSfAPLFtgltldvveadaleaeNRAvpvpegdprrGTdgvrs 391
Cdd:PRK06814 920 KEETRQTWMEKfGIR-------ILEGYGVTETApvIALN-TPMH----------------NKA----------GT----- 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 392 falLGRPLDGLEAEIVDDAGkrVDERevGEIRLRGEAVTPGYLTMDGPLATQD-EDGWLNTGDlgyLV----DGQIVICG 466
Cdd:PRK06814 961 ---VGRLLPGIEYRLEPVPG--IDEG--GRLFVRGPNVMLGYLRAENPGVLEPpADGWYDTGD---IVtideEGFITIKG 1030
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 467 RRKDVIIMGGRNLYPTDIERAATSVEgVRAGNAVAVRLDAgSRRERFAVVLESKlagDAEAEkNLMKQVSArvRDAVD-M 545
Cdd:PRK06814 1031 RAKRFAKIAGEMISLAAVEELAAELW-PDALHAAVSIPDA-RKGERIILLTTAS---DATRA-AFLAHAKA--AGASElM 1102
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 300790052 546 RPYAVVVLPAgsLPKTPSGKVKRAATAQQFADRIKKNADA 585
Cdd:PRK06814 1103 VPAEIITIDE--IPLLGTGKIDYVAVTKLAEEAAAKPEAA 1140
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
148-541 |
4.92e-19 |
|
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: 90.21 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 148 PVLEQKGIGFQ-LITELAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEF-DFDVDvmvs 225
Cdd:cd05910 54 PVLIDPGMGRKnLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIrPGEVD---- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 226 wLPTFHDMGMVGFLtvpmtFGVELVkITPVEFL----SGPLIWPELITKYHGTTTaapnFAYAIVGRRMARVDEDDAYDL 301
Cdd:cd05910 130 -LATFPLFALFGPA-----LGLTSV-IPDMDPTrparADPQKLVGAIRQYGVSIV----FGSPALLERVARYCAQHGITL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 302 SKLRIALNGAEPIDETAVQTFvdagARFKMPAECVFPAYGMAEAtlavsfaplftgLTLDVVEADALEAENRAVPvpegD 381
Cdd:cd05910 199 PSLRRVLSAGAPVPIALAARL----RKMLSDEAEILTPYGATEA------------LPVSSIGSRELLATTTAAT----S 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 382 PRRGTdgvrsfaLLGRPLDGLEAEIV--DDAG-------KRVDEREVGEIRLRGEAVTPGYLTMdgPLAT-----QDEDG 447
Cdd:cd05910 259 GGAGT-------CVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTPTYVNR--PVATalakiDDNSE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 448 --WLNTGDLGYLVD-GQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVrldaGSRRERFAVVLESKLAGD 524
Cdd:cd05910 330 gfWHRMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV----GKPGCQLPVLCVEPLPGT 405
|
410
....*....|....*..
gi 300790052 525 AEAEKNLMKQVSARVRD 541
Cdd:cd05910 406 ITPRARLEQELRALAKD 422
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
7-575 |
7.90e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 89.66 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 7 TLVATATKRGQQR-GMVTGEpkepVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAA--APVLIAptVQAVWLAGGSV 83
Cdd:PRK06188 16 HLLVSALKRYPDRpALVLGD----TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLnrPEVLMA--IGAAQLAGLRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 84 TMLHQPTPRTDLAEWAEDT-VRVLgmigsdqdaLGGPGGLAPRPGS-GAGPRNVTVLLGepfdqLAPVleqkGIGFQLIT 161
Cdd:PRK06188 90 TALHPLGSLDDHAYVLEDAgISTL---------IVDPAPFVERALAlLARVPSLKHVLT-----LGPV----PDGVDLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 162 ELAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVerAEFDFDVDVMvswlptfhdmgmvgFLTV 241
Cdd:PRK06188 152 AAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQL--AEWEWPADPR--------------FLMC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 242 pmtfgvelvkiTPVEFLSGPLIWPELITKyhGTTTAAPNFAYAIVGRRMAR----------------VDEDD--AYDLSK 303
Cdd:PRK06188 216 -----------TPLSHAGGAFFLPTLLRG--GTVIVLAKFDPAEVLRAIEEqritatflvptmiyalLDHPDlrTRDLSS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 304 LRIALNGAEPIDETAVQtfvDAGARFkmpAECVFPAYGMAEATLAVSfaplftglTLDVVEADAleaenravpvpeGDPR 383
Cdd:PRK06188 283 LETVYYGASPMSPVRLA---EAIERF---GPIFAQYYGQTEAPMVIT--------YLRKRDHDP------------DDPK 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 384 RgtdgvrsFALLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMdgPLATQD--EDGWLNTGDLGYL-VDG 460
Cdd:PRK06188 337 R-------LTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNR--PEETAEafRDGWLHTGDVAREdEDG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 461 QIVICGRRKDVIIMGGRNLYPTDIER--------AATSVEGV---RAGNAV-AVrldagsrrerfaVVLESKLAGDAEAE 528
Cdd:PRK06188 408 FYYIVDRKKDMIVTGGFNVFPREVEDvlaehpavAQVAVIGVpdeKWGEAVtAV------------VVLRPGAAVDAAEL 475
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 300790052 529 KNLMKQvsarvRDAVDMRPYAVVVlpAGSLPKTPSGKVKRAATAQQF 575
Cdd:PRK06188 476 QAHVKE-----RKGSVHAPKQVDF--VDSLPLTALGKPDKKALRARY 515
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
32-568 |
1.03e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 89.60 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 32 RTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAE-DTVRVLGMig 110
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAArEGVKALVY-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 111 sDQDALGGPGGLAPR-PGSGAGPRNVTVllGEPFDQLAPVLEQkgigfqlITELAAAEPLPdvVVTDEGdtALLQLTSGS 189
Cdd:PRK07788 153 -DDEFTDLLSALPPDlGRLRAWGGNPDD--DEPSGSTDETLDD-------LIAGSSTAPLP--KPPKPG--GIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 190 TADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGmVGFLTVPMTFGVELV---KITPVEFLsgpliwpE 266
Cdd:PRK07788 219 TGTPKGAPRPEPSPLAPLAGLLSRVPFRAG-ETTLLPAPMFHATG-WAHLTLAMALGSTVVlrrRFDPEATL-------E 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 267 LITKYHGTT-TAAPNFAyaivgRRMARVDED--DAYDLSKLRIALNGAEPIDETAVQTFVDAgarFkmpAECVFPAYGMA 343
Cdd:PRK07788 290 DIAKHKATAlVVVPVML-----SRILDLGPEvlAKYDTSSLKIIFVSGSALSPELATRALEA---F---GPVLYNLYGST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 344 EatlaVSFAplftgltldvveadaleaenrAVPVPEgdprrgtDGVRSFALLGRPLDGLEAEIVDDAGKRVDEREVGEIR 423
Cdd:PRK07788 359 E----VAFA---------------------TIATPE-------DLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 424 LRGEAVTPGYLtmdGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAV 502
Cdd:PRK07788 407 VGNGFPFEGYT---DGRDKQIIDGLLSSGDVGYFdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300790052 503 RLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARV---RDavdmrpyaVVVLPAgsLPKTPSGKVKR 568
Cdd:PRK07788 484 DDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYkvpRD--------VVFLDE--LPRNPTGKVLK 542
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
28-570 |
1.06e-18 |
|
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: 89.33 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 28 EPVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDT--VRV 105
Cdd:cd17651 17 EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAgpVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 106 LgmigsdqdalggpggLAPRPGSGAGPRNVTVLLGEPFdqlapvleqkgigfqlitELAAAEPLPDVVVTDEGDTALLQL 185
Cdd:cd17651 97 L---------------THPALAGELAVELVAVTLLDQP------------------GAAAGADAEPDPALDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 186 TSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTvPMTFGVELVKITPVEFLSGPLIWP 265
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVAWQARASSLGPG-ARTLQFAGLGFDVSVQEIFS-TLCAGATLVLPPEEVRTDPPALAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 266 ELITkyHGTTTAapnFAYAIVGRRMARVDEDDAYDLSKLRIALNGAEPIDET-AVQTFVDAgarfkMPAECVFPAYGMAE 344
Cdd:cd17651 222 WLDE--QRISRV---FLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTeDLREFCAG-----LPGLRLHNHYGPTE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 345 ATLAvsfaplfTGLTLDVVEADALEAenravpvpegdprrgtdgvrsfALLGRPLDGLEAEIVDDAGKRVDEREVGEIRL 424
Cdd:cd17651 292 THVV-------TALSLPGDPAAWPAP----------------------PPIGRPIDNTRVYVLDAALRPVPPGVPGELYI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 425 RGEAVTPGYLTMDGpLATQD--EDGWLN------TGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVR 495
Cdd:cd17651 343 GGAGLARGYLNRPE-LTAERfvPDPFVPgarmyrTGDLArWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVR 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300790052 496 AGNAVAVRLDAGSRRERFAVVLESKLAGDAEAeknLMKQVSARVRDAvdMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:cd17651 422 EAVVLAREDRPGEKRLVAYVVGDPEAPVDAAE---LRAALATHLPEY--MVPSAFVLLDA--LPLTPNGKLDRRA 489
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
33-485 |
7.17e-18 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 87.09 E-value: 7.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAA-APVLIAPTVQAVWLAGGSVTMLHQPTPrtdlaewaEDTVRVL----- 106
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDnRPEWVWAELAAQAIGALSLGIYQDSMA--------EEVAYLLnytga 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 107 -GMIGSDQDALGGPGGLAPRPgsgagPRNVTVLLGEP-----FDQlaPVLEQKGIGFQLITELAAAEP---LPDVVVTDE 177
Cdd:cd17641 85 rVVIAEDEEQVDKLLEIADRI-----PSVRYVIYCDPrgmrkYDD--PRLISFEDVVALGRALDRRDPglyEREVAAGKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 178 GDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVeRAEFDFDVDVMVSWLPTFHDM--------GMVGFLTV-----PMT 244
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYL-AADPLGPGDEYVSVLPLPWIGeqmysvgqALVCGFIVnfpeePET 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 245 FGVELVKITPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGRRMarvdeddaydlsklRIALNGAepidetavqtfvD 324
Cdd:cd17641 237 MMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGM--------------KLGLRAL------------D 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 325 AGARFKMPAECVFPAYGMAEATLavsFAPL-----FTGLTLDVVEADALEAEN----RAVPVP----------------- 378
Cdd:cd17641 291 RGKRGRPVSLWLRLASWLADALL---FRPLrdrlgFSRLRSAATGGAALGPDTfrffHAIGVPlkqlygqtelagaytvh 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 379 -EGDPRRGTDGVrsfallgrPLDGLEAEIVddagkrvderEVGEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGDL 454
Cdd:cd17641 368 rDGDVDPDTVGV--------PFPGTEVRID----------EVGEILVRSPGVFVGYY--KNPEATAedfDEDGWLHTGDA 427
|
490 500 510
....*....|....*....|....*....|...
gi 300790052 455 GYL-VDGQIVICGRRKDVIIMG-GRNLYPTDIE 485
Cdd:cd17641 428 GYFkENGHLVVIDRAKDVGTTSdGTRFSPQFIE 460
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
31-577 |
7.95e-18 |
|
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: 86.74 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 31 RRTWAEVHEEARRIAGGLVAGGFERGTAVGV-----------------LAAAPVLIAPTvqavwlaggsvtmlHQptpRT 93
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVqlpnvaefvivffalfrAGAIPVFALPA--------------HR---RA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 94 DLAEWAEDTVRVlGMIGSDQDALGGPGGLAPR-PGSGAGPRNVtVLLGEPFDQLApvleqkgigfqlITELAAAEPLPDV 172
Cdd:COG1021 113 EISHFAEQSEAV-AYIIPDRHRGFDYRALARElQAEVPSLRHV-LVVGDAGEFTS------------LDALLAAPADLSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 173 VVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMV--GFLTVPMTFGveLV 250
Cdd:COG1021 179 PRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDAD-TVYLAALPAAHNFPLSspGVLGVLYAGG--TV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 251 KITPVeflSGPLIWPELITKYHGTTTAA-PnfayAIVGRRMARVDEDDaYDLSKLRIALNGAEPIDETAVQTFVDA-GAR 328
Cdd:COG1021 256 VLAPD---PSPDTAFPLIERERVTVTALvP----PLALLWLDAAERSR-YDLSSLRVLQVGGAKLSPELARRVRPAlGCT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 329 FKMpaecVFpayGMAEATLavsfapLFTGLtldvveadaleaenravpvpeGDPRRgtdgvRSFALLGRPL-DGLEAEIV 407
Cdd:COG1021 328 LQQ----VF---GMAEGLV------NYTRL---------------------DDPEE-----VILTTQGRPIsPDDEVRIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 408 DDAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGDLGYLV-DGQIVICGRRKDVIIMGGRNLYPTD 483
Cdd:COG1021 369 DEDGNPVPPGEVGELLTRGPYTIRGYY--RAPEHNArafTPDGFYRTGDLVRRTpDGYLVVEGRAKDQINRGGEKIAAEE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 484 IERAATSVEGVRAGNAVAV---RLdaGSRRERFAVVLESKLAgdaeaeknlMKQVSARVRD---AVDMRPYAVVVLPAgs 557
Cdd:COG1021 447 VENLLLAHPAVHDAAVVAMpdeYL--GERSCAFVVPRGEPLT---------LAELRRFLRErglAAFKLPDRLEFVDA-- 513
|
570 580
....*....|....*....|
gi 300790052 558 LPKTPSGKVKRAATAQQFAD 577
Cdd:COG1021 514 LPLTAVGKIDKKALRAALAA 533
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
31-495 |
1.21e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 85.91 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 31 RRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDT-VRVLgmI 109
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSgARVL--I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 GSDqDALggpgglapRPGSGAGPRNVTVLLGEPFDQ------LAPVLEQKGIGFQLITELAAAEPLPDVVVTdEGDTALL 183
Cdd:PRK12406 89 AHA-DLL--------HGLASALPAGVTVLSVPTPPEiaaayrISPALLTPPAGAIDWEGWLAQQEPYDGPPV-PQPQSMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 184 qLTSGSTADPKAVRITygnlysnvKAMVERAEFDFDVDVMVSWLPTfhdmGMVGFLTVPM-------------TFGVELV 250
Cdd:PRK12406 159 -YTSGTTGHPKGVRRA--------APTPEQAAAAEQMRALIYGLKP----GIRALLTGPLyhsapnayglragRLGGVLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 251 ---KITPVEFLSgpLIWPELITKYHGTTTaapnfayaIVGRRMARVDEDDA-YDLSKLRIALNGAEPIDETAVQTFVDag 326
Cdd:PRK12406 226 lqpRFDPEELLQ--LIERHRITHMHMVPT--------MFIRLLKLPEEVRAkYDVSSLRHVIHAAAPCPADVKRAMIE-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 327 arFKMPAECVFpaYGMAEaTLAVSFAplftgltldvVEADALEaenravpvpegdpRRGTdgvrsfalLGRPLDGLEAEI 406
Cdd:PRK12406 294 --WWGPVIYEY--YGSTE-SGAVTFA----------TSEDALS-------------HPGT--------VGKAAPGAELRF 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 407 VDDAGKRVDEREVGEIRLRGEAVTP-GYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDI 484
Cdd:PRK12406 338 VDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLdADGYLFLCDRKRDMVISGGVNIYPAEI 417
|
490
....*....|.
gi 300790052 485 ERAATSVEGVR 495
Cdd:PRK12406 418 EAVLHAVPGVH 428
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
176-585 |
2.42e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 85.19 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 176 DEGDTALLQLTSGSTADPKAVRITY-GNLYSNVKAMVERAEFDFDVDVMVSWLPTFHDMGMVGFLTVPMTfGVELVkiTP 254
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHrSNVLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSM-GTKLV--MP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 255 VEFLSGPLIWpELITKYHGTTTAAPNFAYAIVGRRMarvdEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGARfkmpae 334
Cdd:PRK06018 252 GAKLDGASVY-ELLDTEKVTFTAGVPTVWLMLLQYM----EKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVE------ 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 335 cVFPAYGMAE----ATLAvSFAPLFTGLTLDVvEADALEAEnravpvpegdprrgtdgvrsfallGRPLDGLEAEIVDDA 410
Cdd:PRK06018 321 -VRHAWGMTEmsplGTLA-ALKPPFSKLPGDA-RLDVLQKQ------------------------GYPPFGVEMKITDDA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 411 GKRV--DEREVGEIRLRGEAVTPGYLTMDGPLAtqDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERA 487
Cdd:PRK06018 374 GKELpwDGKTFGRLKVRGPAVAAAYYRVDGEIL--DDDGFFDTGDVATIdAYGYMRITDRSKDVIKSGGEWISSIDLENL 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 488 ATSVEGVRAGNAVAVRLDAGSRRERFAVVLEsklAGDAEAEKNLMKQVSARVrdAVDMRPYAVVVLpaGSLPKTPSGKVK 567
Cdd:PRK06018 452 AVGHPKVAEAAVIGVYHPKWDERPLLIVQLK---PGETATREEILKYMDGKI--AKWWMPDDVAFV--DAIPHTATGKIL 524
|
410
....*....|....*...
gi 300790052 568 RAATAQQFADRIKKNADA 585
Cdd:PRK06018 525 KTALREQFKDYKLPTAAA 542
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
8-485 |
2.50e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 85.24 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 8 LVATATKRGQQRGMVTGEPkepvRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLH 87
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNR----RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 88 QptpRTDLAEwAEDTVRVLG--MIGSDQDALGGPgglaPRPGSGAGPR-NVTVLLGEPFDQLAPVLEQKgIGFQLITELA 164
Cdd:PLN02860 89 Y---RWSFEE-AKSAMLLVRpvMLVTDETCSSWY----EELQNDRLPSlMWQVFLESPSSSVFIFLNSF-LTTEMLKQRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 165 AAEPLPDVVVTDEgDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMT 244
Cdd:PLN02860 160 LGTTELDYAWAPD-DAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGED-DVYLHTAPLCHIGGLSSALAMLMV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 245 FGVELvkITPvEFLSGPLIwpELITKYHGTT-TAAPNFAYAIVgrRMARVDEDDAYDLSKLRIaLNGAEPID----ETAV 319
Cdd:PLN02860 238 GACHV--LLP-KFDAKAAL--QAIKQHNVTSmITVPAMMADLI--SLTRKSMTWKVFPSVRKI-LNGGGSLSsrllPDAK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 320 QTFvdagarfkmPAECVFPAYGMAEATLAVSFAPLF--TGLTLDVVEADALEAENRAVPVPEGdprrgtdgvrsfALLGR 397
Cdd:PLN02860 310 KLF---------PNAKLFSAYGMTEACSSLTFMTLHdpTLESPKQTLQTVNQTKSSSVHQPQG------------VCVGK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 398 PLDGLEAEIVDDAGKRVderevGEIRLRGEAVTPGYltMDGPLATQDE---DGWLNTGDLGYLVD-GQIVICGRRKDVII 473
Cdd:PLN02860 369 PAPHVELKIGLDESSRV-----GRILTRGPHVMLGY--WGQNSETASVlsnDGWLDTGDIGWIDKaGNLWLIGRSNDRIK 441
|
490
....*....|..
gi 300790052 474 MGGRNLYPTDIE 485
Cdd:PLN02860 442 TGGENVYPEEVE 453
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
396-580 |
4.14e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 84.45 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIM 474
Cdd:PRK07638 310 GRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEdEEGFIYIVGREKNMILF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 475 GGRNLYPTDIERAATSVEGVRagNAVAVrldaGSRRERFAVVLESKLAGDAEAeknlmKQVSARVRD--AVDMRPYAVVV 552
Cdd:PRK07638 390 GGINIFPEEIESVLHEHPAVD--EIVVI----GVPDSYWGEKPVAIIKGSATK-----QQLKSFCLQrlSSFKIPKEWHF 458
|
170 180
....*....|....*....|....*...
gi 300790052 553 lpAGSLPKTPSGKVKRAATAQQFADRIK 580
Cdd:PRK07638 459 --VDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
33-570 |
7.39e-17 |
|
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: 83.40 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAA-APVLIAPTVqAVWLAGGSVTMLHQPTPRTDLAEWAEDtvrvlgmigs 111
Cdd:cd12117 24 TYAELNERANRLARRLRAAGVGPGDVVGVLAErSPELVVALL-AVLKAGAAYVPLDPELPAERLAFMLAD---------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 112 dqdalggpgglaprpgsgAGPRnvTVLLGEPFDQLAPVLEQKGIGFQlitELAAAEPLPDVVVTDEGDTALLQLTSGSTA 191
Cdd:cd12117 93 ------------------AGAK--VLLTDRSLAGRAGGLEVAVVIDE---ALDAGPAGNPAVPVSPDDLAYVMYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 192 DPKAVRITYGN---LYSNVKAMVERAEfdfDVDVMVSWLP----TFHdmgmvgfLTVPMTFGVELVkITPVEFLSGPLIW 264
Cdd:cd12117 150 RPKGVAVTHRGvvrLVKNTNYVTLGPD---DRVLQTSPLAfdasTFE-------IWGALLNGARLV-LAPKGTLLDPDAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 265 PELITKyHGTTTAapnFAYAIVGRRMARVDEDDaydLSKLRIALNGAEPIDETAVQTFVDAGARFKmpaecVFPAYGMAE 344
Cdd:cd12117 219 GALIAE-EGVTVL---WLTAALFNQLADEDPEC---FAGLRELLTGGEVVSPPHVRRVLAACPGLR-----LVNGYGPTE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 345 ATLavsfaplFTglTLDVVEADALEAEnravPVPegdprrgtdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRL 424
Cdd:cd12117 287 NTT-------FT--TSHVVTELDEVAG----SIP----------------IGRPIANTRVYVLDEDGRPVPPGVPGELYV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 425 RGEAVTPGYLtmDGPLATQD---EDGWLN------TGDL-GYLVDGQIVICGRRKD-VIIMGGRnLYPTDIERAATSVEG 493
Cdd:cd12117 338 GGDGLALGYL--NRPALTAErfvADPFGPgerlyrTGDLaRWLPDGRLEFLGRIDDqVKIRGFR-IELGEIEAALRAHPG 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300790052 494 VRAgNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARvrdavdMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:cd12117 415 VRE-AVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAY------MVPAAFVVLDE--LPLTANGKVDRRA 482
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
170-485 |
9.92e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 83.56 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 170 PDVVVTDegdTALLQLTSGSTADPKAVRITYGNLYSNVK--------AMVERAEFdfdvdvMVSWLPTFHdmgmVGFLTV 241
Cdd:PRK08974 201 PELVPED---LAFLQYTGGTTGVAKGAMLTHRNMLANLEqakaaygpLLHPGKEL------VVTALPLYH----IFALTV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 242 PMTFGVEL----VKIT-PVEFlsgPLIWPELiTKYHGTTTAAPNFAY-AIVGRrmarvDEDDAYDLSKLRIALNGAEPId 315
Cdd:PRK08974 268 NCLLFIELggqnLLITnPRDI---PGFVKEL-KKYPFTAITGVNTLFnALLNN-----EEFQELDFSSLKLSVGGGMAV- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 316 ETAVQTfvdagaRFKMPAEC-VFPAYGMAEAtlavsfAPLFTGLTLDVVEADAleaeNRAVPVPEGDPRrgtdgvrsfal 394
Cdd:PRK08974 338 QQAVAE------RWVKLTGQyLLEGYGLTEC------SPLVSVNPYDLDYYSG----SIGLPVPSTEIK----------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 lgrpldgleaeIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMdgPLATQD--EDGWLNTGDLGYLVD-GQIVICGRRKDV 471
Cdd:PRK08974 391 -----------LVDDDGNEVPPGEPGELWVKGPQVMLGYWQR--PEATDEviKDGWLATGDIAVMDEeGFLRIVDRKKDM 457
|
330
....*....|....
gi 300790052 472 IIMGGRNLYPTDIE 485
Cdd:PRK08974 458 ILVSGFNVYPNEIE 471
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
8-570 |
1.70e-16 |
|
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: 82.32 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 8 LVATATKRGQQRGMVTGEPkepVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLH 87
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEG---RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 88 QPTPRTDLAEWAEDTVRVLGMIGSDQDALGGPGGLAPRPGSgagprnvtvllgepfdqlapvleqkgigfqliTELAAAE 167
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGD--------------------------------EALAAPP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 168 PLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSWLPTFhDMGMVGFLtVPMTFGV 247
Cdd:cd17646 128 ATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSF-DVSVWELF-WPLVAGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 248 ELVkITPVEFLSGPLIWPELITKyHGTTTAapNFAYAIVGrrmARVDEDDAYDLSKLRIALNGAEPIDetavqtfVDAGA 327
Cdd:cd17646 206 RLV-VARPGGHRDPAYLAALIRE-HGVTTC--HFVPSMLR---VFLAEPAAGSCASLRRVFCSGEALP-------PELAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 328 RF-KMPAECVFPAYGMAEATLAVSfaplftgltldvveADALEAENRAVPVPegdprrgtdgvrsfalLGRPLDGLEAEI 406
Cdd:cd17646 272 RFlALPGAELHNLYGPTEAAIDVT--------------HWPVRGPAETPSVP----------------IGRPVPNTRLYV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 407 VDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLN-------TGDLG-YLVDGQIVICGRRKDVIIMGGRN 478
Cdd:cd17646 322 LDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGpgsrmyrTGDLArWRPDGALEFLGRSDDQVKIRGFR 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 479 LYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEknLMKQVSARVRDAvdMRPYAVVVLPAgsL 558
Cdd:cd17646 402 VEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAA--LRAHLAERLPEY--MVPAAFVVLDA--L 475
|
570
....*....|..
gi 300790052 559 PKTPSGKVKRAA 570
Cdd:cd17646 476 PLTANGKLDRAA 487
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
186-573 |
1.96e-16 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 82.25 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 186 TSGSTADPKAVRITYGNLYSNVKAMVE------------RAEFDFDVDVMvSWLPTFHDMGMVGFLTVPMT--FGV--EL 249
Cdd:PRK04813 151 TSGTTGKPKGVQISHDNLVSFTNWMLEdfalpegpqflnQAPYSFDLSVM-DLYPTLASGGTLVALPKDMTanFKQlfET 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 250 VKITPVEflsgplIWpelitkyhgttTAAPNFAyaivgrRMARVDED-DAYDLSKLRIAL-NGAEPIDETAvQTFVDaga 327
Cdd:PRK04813 230 LPQLPIN------VW-----------VSTPSFA------DMCLLDPSfNEEHLPNLTHFLfCGEELPHKTA-KKLLE--- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 328 RFkmPAECVFPAYGMAEATLAVsfaplfTGLTldvVEADALEAENRaVPVpegdprrgtdgvrsfallGRPLDGLEAEIV 407
Cdd:PRK04813 283 RF--PSATIYNTYGPTEATVAV------TSIE---ITDEMLDQYKR-LPI------------------GYAKPDSPLLII 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 408 DDAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQ----DEDGW--LNTGDLGYLVDGQIVICGRRKDVIIMGGRNLYP 481
Cdd:PRK04813 333 DEEGTKLPDGEQGEIVISGPSVSKGYL--NNPEKTAeaffTFDGQpaYHTGDAGYLEDGLLFYQGRIDFQIKLNGYRIEL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 482 TDIERAATSVEGVRagNAVAVRLDAGSRRERFAVVLESKlAGDAEAEKNLMKQVSARVRDavDMRPYavvVLPA-----G 556
Cdd:PRK04813 411 EEIEQNLRQSSYVE--SAVVVPYNKDHKVQYLIAYVVPK-EEDFEREFELTKAIKKELKE--RLMEY---MIPRkfiyrD 482
|
410
....*....|....*..
gi 300790052 557 SLPKTPSGKVKRAATAQ 573
Cdd:PRK04813 483 SLPLTPNGKIDRKALIE 499
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
171-570 |
2.28e-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: 81.74 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 171 DVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFD-----------FDVDVmvswlptfhdmgMVGFL 239
Cdd:cd17650 86 KLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDsfpvrllqmasFSFDV------------FAGDF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 240 TVPMTFGVELVkITPVEFLSGPLIWPELITKYHGTT-TAAPNFAYAIvgrrMARVDEDDaYDLSKLRIALNGAepiDETA 318
Cdd:cd17650 154 ARSLLNGGTLV-ICPDEVKLDPAALYDLILKSRITLmESTPALIRPV----MAYVYRNG-LDLSAMRLLIVGS---DGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 319 VQTFVDAGARFKMPAECVfPAYGMAEATLAVSFAPlftgltldvvEADALEAENRAVPVpegdprrgtdgvrsfallGRP 398
Cdd:cd17650 225 AQDFKTLAARFGQGMRII-NSYGVTEATIDSTYYE----------EGRDPLGDSANVPI------------------GRP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 399 LDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLT---------MDGPLATQDEdgWLNTGDLG-YLVDGQIVICGRR 468
Cdd:cd17650 276 LPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNrpeltaerfVENPFAPGER--MYRTGDLArWRADGNVELLGRV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 469 KDVIIMGGRNLYPTDIERAATSVEGVRAGnAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARvrdavdMRPY 548
Cdd:cd17650 354 DHQVKIRGFRIELGEIESQLARHPAIDEA-VVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSY------MIPS 426
|
410 420
....*....|....*....|..
gi 300790052 549 AVVVLPAgsLPKTPSGKVKRAA 570
Cdd:cd17650 427 YYVQLDA--LPLTPNGKVDRRA 446
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
396-568 |
2.68e-16 |
|
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: 80.14 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGkrvdeREVGEIRLRGEAVTPGYLTMDGplatQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIM 474
Cdd:cd17633 166 GRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGF----SNPDGWMSVGDIGYVdEEGYLYLVGRESDMIII 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 475 GGRNLYPTDIERAATSVEGVRagNAVAVRLdAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVRdavdmRPYAVVVLp 554
Cdd:cd17633 237 GGINIFPTEIESVLKAIPGIE--EAIVVGI-PDARFGEIAVALYSGDKLTYKQLKRFLKQKLSRYE-----IPKKIIFV- 307
|
170
....*....|....
gi 300790052 555 aGSLPKTPSGKVKR 568
Cdd:cd17633 308 -DSLPYTSSGKIAR 320
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
31-569 |
2.79e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 82.11 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 31 RRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAA-APVLIAPTVQAVWLAGGSV---TMLHQPTPRTDLAEwaedtvrvl 106
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGnRIEFLDVFLGCAWLGAIAVpinTALRGPQLEHILRN--------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 107 gmigSDQDALGGPGGLAPRPGS---GAGPRNVTVLLGEPFDQLAPVleqkgiGFQLITELAAAEPLPDVVVTDeGDTALL 183
Cdd:PRK06155 117 ----SGARLLVVEAALLAALEAadpGDLPLPAVWLLDAPASVSVPA------GWSTAPLPPLDAPAPAAAVQP-GDTAAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 184 QLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVpMTFGVELVkITPVEFLSGplI 263
Cdd:PRK06155 186 LYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGAD-DVLYTTLPLFHTNALNAFFQA-LLAGATYV-LEPRFSASG--F 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 264 WPELitKYHGTTtaapnFAY---AIVGRRMARVDEDDAYDlSKLRIALNGAEPidetaVQTFVDAGARFKMPAecvFPAY 340
Cdd:PRK06155 261 WPAV--RRHGAT-----VTYllgAMVSILLSQPARESDRA-HRVRVALGPGVP-----AALHAAFRERFGVDL---LDGY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 341 GMAEAtlavsfaplftgltldvveadaleaeNRAVPVPEGDPRRGTdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVG 420
Cdd:PRK06155 325 GSTET--------------------------NFVIAVTHGSQRPGS--------MGRLAPGFEARVVDEHDQELPDGEPG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 421 EIRLRGE---AVTPGYLTMdgPLATQD--EDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGV 494
Cdd:PRK06155 371 ELLLRADepfAFATGYFGM--PEKTVEawRNLWFHTGDRVVRdADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAV 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300790052 495 RAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAeknLMKQVSARVrdavdmrPYAVV---VLPAGSLPKTPSGKVKRA 569
Cdd:PRK06155 449 AAAAVFPVPSELGEDEVMAAVVLRDGTALEPVA---LVRHCEPRL-------AYFAVpryVEFVAALPKTENGKVQKF 516
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
158-569 |
3.12e-16 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 81.73 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 158 QLITELAAAEPLPdvvVTDEGDTALLqlTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSwLPTFHDMgmvG 237
Cdd:PRK13382 181 VLIAAHAGQRPEP---TGRKGRVILL--TSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIV-APMFHAW---G 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 238 FLTVPMTFGVELVKITPVEFlsGPLIWPELITKYHGTTTAapnfAYAIVGRRMARVDED--DAYDLSKLRIALNGAEPID 315
Cdd:PRK13382 252 FSQLVLAASLACTIVTRRRF--DPEATLDLIDRHRATGLA----VVPVMFDRIMDLPAEvrNRYSGRSLRFAAASGSRMR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 316 ETAVQTFVDagaRFkmpAECVFPAYGMAEATLAVSFAPlftgltldvveADALEAENRAvpvpegdprrgtdgvrsfall 395
Cdd:PRK13382 326 PDVVIAFMD---QF---GDVIYNNYNATEAGMIATATP-----------ADLRAAPDTA--------------------- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLtmdgPLATQD-EDGWLNTGDLGYLVD-GQIVICGRRKDVII 473
Cdd:PRK13382 368 GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYT----SGSTKDfHDGFMASGDVGYLDEnGRLFVVGRDDEMIV 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 474 MGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKnlmkqvsARVRD--AVDMRPYAVV 551
Cdd:PRK13382 444 SGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLK-------QHVRDnlANYKVPRDIV 516
|
410
....*....|....*...
gi 300790052 552 VLPagSLPKTPSGKVKRA 569
Cdd:PRK13382 517 VLD--ELPRGATGKILRR 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-570 |
3.88e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 82.70 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 31 RRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDT-VRVLgmi 109
Cdd:PRK12316 3082 RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSgAQLL--- 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 gsdqdalggpggLAPRPGSGAGPRNVTVLLGEPFDQlapvleqkgigfqlitelAAAEPLPDVVVTDEgDTALLQLTSGS 189
Cdd:PRK12316 3159 ------------LSQSHLRLPLAQGVQVLDLDRGDE------------------NYAEANPAIRTMPE-NLAYVIYTSGS 3207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 190 TADPKAVRITYGNLYSNVKAMVEraEFDFDVDVMVSWLPTFHDMGMVGFLTVPMTFGVELVkitpvefLSGPLIWPELIT 269
Cdd:PRK12316 3208 TGKPKGVGIRHSALSNHLCWMQQ--AYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVV-------LAGPEDWRDPAL 3278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 270 KYHGTTTAAPNFAYAIVGRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGArfkmpaecVFPAYGMAEATLav 349
Cdd:PRK12316 3279 LVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP--------LYNLYGPTEATI-- 3348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 350 sfaplfTGLTLDVVEADaleaenravpvpegdprrgtdgvRSFALLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAV 429
Cdd:PRK12316 3349 ------TVTHWQCVEEG-----------------------KDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGL 3399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 430 TPGYLTMDG-------PLATQDEDGWLNTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAgnavA 501
Cdd:PRK12316 3400 ARGYHNRPGltaerfvPDPFVPGERLYRTGDLArYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVRE----A 3475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300790052 502 VRLDAGSRRERFAVVLESKlagDAEAEKNLMKQVSARVRDAvdMRPYAVVVLPagSLPKTPSGKVKRAA 570
Cdd:PRK12316 3476 VVLAVDGRQLVAYVVPEDE---AGDLREALKAHLKASLPEY--MVPAHLLFLE--RMPLTPNGKLDRKA 3537
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
33-568 |
4.25e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 81.43 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLV-AGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDTVRVLGMIGS 111
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 112 DQ----DALGGPGGLAPRPGSgagprnvtvllgepFDQLAPvleQKGIGFQLITElaAAEPLPDVVVTDEgDTALLQLTS 187
Cdd:PLN02574 148 ENveklSPLGVPVIGVPENYD--------------FDSKRI---EFPKFYELIKE--DFDFVPKPVIKQD-DVAAIMYSS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 188 GSTADPKAVRITYGNLYSNVKAMV--ERAEFDFDV--DVMVSWLPTFHDMGMVGFLTVPMTFGVELVKITpvEFLSGPLI 263
Cdd:PLN02574 208 GTTGASKGVVLTHRNLIAMVELFVrfEASQYEYPGsdNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMR--RFDASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 264 wpELITKYHGTT-TAAPNFAYAIVgrRMARvdEDDAYDLSKLRIALNGAEPIDETAVQTFVDAgarfkMPAECVFPAYGM 342
Cdd:PLN02574 286 --KVIDRFKVTHfPVVPPILMALT--KKAK--GVCGEVLKSLKQVSCGAAPLSGKFIQDFVQT-----LPHVDFIQGYGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 343 AEATlAVSfaplftgltldvveadaleaenravpvpegdpRRG--TDGVRSFALLGRPLDGLEAEIVD-DAGKRVDEREV 419
Cdd:PLN02574 355 TEST-AVG--------------------------------TRGfnTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 420 GEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATS-VEGV 494
Cdd:PLN02574 402 GELWIQGPGVMKGYL--NNPKATQstiDKDGWLRTGDIAYFdEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLIShPEII 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300790052 495 RAGNAVAVRLDAGSRRERFAVvlesKLAGDAEAEKNLMKQVSARVrdavdmRPYAVV--VLPAGSLPKTPSGKVKR 568
Cdd:PLN02574 480 DAAVTAVPDKECGEIPVAFVV----RRQGSTLSQEAVINYVAKQV------APYKKVrkVVFVQSIPKSPAGKILR 545
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-568 |
8.70e-16 |
|
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: 79.78 E-value: 8.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 29 PVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAapvliaptvqavwlaggsvtmlhqPTPRTDLAEWAedtVRVLGM 108
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLS------------------------QGPECAIAHIA---ILRSGA 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 109 IGSDQDALGGPGGLAPR-PGSGAgprnvtvllgepfdqlapvleqkgigfqlitelaaaeplpDVVVTDEG-DTALLQLT 186
Cdd:cd05971 57 IAVPLFALFGPEALEYRlSNSGA----------------------------------------SALVTDGSdDPALIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 187 SGSTADPKAV----RITYGNLysnvkAMVERAEFDFDVDVMVSWLPTfhDMGMVGFL---TVP-MTFGVELVKITPVEFL 258
Cdd:cd05971 97 SGTTGPPKGAlhahRVLLGHL-----PGVQFPFNLFPRDGDLYWTPA--DWAWIGGLldvLLPsLYFGVPVLAHRMTKFD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 259 SGPLIwpELITKyHGTTTAapnFAYAIVGRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDAgarFKMPaecVFP 338
Cdd:cd05971 170 PKAAL--DLMSR-YGVTTA---FLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQ---FGVE---VNE 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 339 AYGMAEATLAVSFAPLFtgltldvveadaleaenravpvpeGDPRRGTdgvrsfalLGRPLDGLEAEIVDDAGKRVDERE 418
Cdd:cd05971 238 FYGQTECNLVIGNCSAL------------------------FPIKPGS--------MGKPIPGHRVAIVDDNGTPLPPGE 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 419 VGEIRLRgeavTPGYLTM----DGPLATQDE--DGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSV 491
Cdd:cd05971 286 VGEIAVE----LPDPVAFlgywNNPSATEKKmaGDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKH 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 492 EGVRagNAVAVRLDAGSRRE---RFAVVLESKLAGDAeaeknLMKQVSARVRDAVDMRPYAVVVLPAGSLPKTPSGKVKR 568
Cdd:cd05971 362 PAVL--MAAVVGIPDPIRGEivkAFVVLNPGETPSDA-----LAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRR 434
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
179-566 |
9.25e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 81.12 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKA--MVERAEFDfdvDVMVSWLPTFHDMGMVGFLTVPMTFGVelvkitPVE 256
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQisDVFNLRND---DVILSSLPFFHSFGLTVTLWLPLLEGI------KVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 257 FLSGPL----IwPELITKYHGTTT-AAPNF--AYAivgrRMARVDEDdayDLSKLRIALNGAEPIDETAVQTFVDagaRF 329
Cdd:PRK08633 854 YHPDPTdalgI-AKLVAKHRATILlGTPTFlrLYL----RNKKLHPL---MFASLRLVVAGAEKLKPEVADAFEE---KF 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 330 KMPaecVFPAYGMAEATlavsfaPLFTGLTLDVVEADALEaenravpvpEGDPRRGTdgvrsfalLGRPLDGLEAEIVD- 408
Cdd:PRK08633 923 GIR---ILEGYGATETS------PVASVNLPDVLAADFKR---------QTGSKEGS--------VGMPLPGVAVRIVDp 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 409 DAGKRVDEREVGEIRLRGEAVTPGYLtmDGP------LATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGG----- 476
Cdd:PRK08633 977 ETFEELPPGEDGLILIGGPQVMKGYL--GDPektaevIKDIDGIGWYVTGDKGHLdEDGFLTITDRYSRFAKIGGemvpl 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 477 --------RNLYPTDIERAATSVEGVRAGNAVavrldagsrrerfaVVLESKLAGDAEAEKNLMKQVSarvrDAVDMRPY 548
Cdd:PRK08633 1055 gaveeelaKALGGEEVVFAVTAVPDEKKGEKL--------------VVLHTCGAEDVEELKRAIKESG----LPNLWKPS 1116
|
410
....*....|....*...
gi 300790052 549 AVVVLPAgsLPKTPSGKV 566
Cdd:PRK08633 1117 RYFKVEA--LPLLGSGKL 1132
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
33-578 |
9.70e-16 |
|
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: 81.06 E-value: 9.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTML--HQPTPRtdLAEWAEDtvrvlgmig 110
Cdd:COG1020 503 TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLdpAYPAER--LAYMLED--------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 111 sdqdalggpgglaprpgsgAGPRnvtVLLGEPfdQLAPVLEQKGIGFQLI--TELAAAEPLPDVVVTDEGDTALLQLTSG 188
Cdd:COG1020 572 -------------------AGAR---LVLTQS--ALAARLPELGVPVLALdaLALAAEPATNPPVPVTPDDLAYVIYTSG 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 189 STADPKAVRITYGNLYSNVKAMVERAEFDfDVDVMVSWLPTFHDMGMVGFLtVPMTFGVELVkITPVEFLSGPLIWPELI 268
Cdd:COG1020 628 STGRPKGVMVEHRALVNLLAWMQRRYGLG-PGDRVLQFASLSFDASVWEIF-GALLSGATLV-LAPPEARRDPAALAELL 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 269 TKYHGTT-TAAPNFAYAIVgrrmarvdEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGARFKmpaecVFPAYGMAEATL 347
Cdd:COG1020 705 ARHRVTVlNLTPSLLRALL--------DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGAR-----LVNLYGPTETTV 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 348 AVSFAPLftgltldvveaDALEAENRAVPVpegdprrgtdgvrsfallGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGE 427
Cdd:COG1020 772 DSTYYEV-----------TPPDADGGSVPI------------------GRPIANTRVYVLDAHLQPVPVGVPGELYIGGA 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 428 AVTPGYLTMDGPLATQ------DEDG--WLNTGDLG-YLVDGQIVICGRRKD-VIIMGGRnLYPTDIERAATSVEGVRAG 497
Cdd:COG1020 823 GLARGYLNRPELTAERfvadpfGFPGarLYRTGDLArWLPDGNLEFLGRADDqVKIRGFR-IELGEIEAALLQHPGVREA 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 498 nAVAVRLDAGSRRERFAVVLESKLAGDAEAEknlmkqVSARVRDAVDMRPYAVVVLPAGSLPKTPSGKVKRAATAQQFAD 577
Cdd:COG1020 902 -VVVAREDAPGDKRLVAYVVPEAGAAAAAAL------LRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAA 974
|
.
gi 300790052 578 R 578
Cdd:COG1020 975 A 975
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
31-570 |
9.74e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.54 E-value: 9.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 31 RRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDT-VRVLGMI 109
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSgVQLLLSQ 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 GSDQDALGGPGGlaprpgsgagprnVTVLLgepFDQLAPVLEqkgigfqlitelAAAEPLPDVVVTDEgDTALLQLTSGS 189
Cdd:PRK12316 616 SHLGRKLPLAAG-------------VQVLD---LDRPAAWLE------------GYSEENPGTELNPE-NLAYVIYTSGS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 190 TADPKAVRITYGNLYSNVKAMVERAEFDfDVDVMVSWLPTFHDMGMVGFLtVPMTFGVELVkITPVEFLSGPLIWPELIT 269
Cdd:PRK12316 667 TGKPKGAGNRHRALSNRLCWMQQAYGLG-VGDTVLQKTPFSFDVSVWEFF-WPLMSGARLV-VAAPGDHRDPAKLVELIN 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 270 KyHGTTT--AAPNFAYAIVGrrmarvDEDDAYDLSKLRIALNGaEPIDETAVQTFVDagarfKMPAECVFPAYGMAEATL 347
Cdd:PRK12316 744 R-EGVDTlhFVPSMLQAFLQ------DEDVASCTSLRRIVCSG-EALPADAQEQVFA-----KLPQAGLYNLYGPTEAAI 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 348 avsfaplftgltlDVVEADALEAENRAVPVpegdprrgtdgvrsfallGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGE 427
Cdd:PRK12316 811 -------------DVTHWTCVEEGGDSVPI------------------GRPIANLACYILDANLEPVPVGVLGELYLAGR 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 428 AVTPGY-----LTMDGPLATQDEDG--WLNTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAgna 499
Cdd:PRK12316 860 GLARGYhgrpgLTAERFVPSPFVAGerMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE--- 936
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300790052 500 vAVRLDAGSRRERFAVVLESKLAGDAEAeknLMKQVSARVRDAvdMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:PRK12316 937 -AAVLAVDGKQLVGYVVLESEGGDWREA---LKAHLAASLPEY--MVPAQWLALER--LPLTPNGKLDRKA 999
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
167-566 |
1.12e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.06 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 167 EPLPDVV-----VTDEGDTALLQLTSGSTADPKAVRITYGNLY-SNVKAMVERAEFDFDVDVmvsW-LPTFHDMGMVgfl 239
Cdd:PLN03102 170 EPTPSLVarmfrIQDEHDPISLNYTSGTTADPKGVVISHRGAYlSTLSAIIGWEMGTCPVYL---WtLPMFHCNGWT--- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 240 tvpMTFGVELVKITPV--EFLSGPLIWPELitKYHGTT--TAAPN-FAYAIVGRRMarvdeDDAYDLSKLRIaLNGAEPI 314
Cdd:PLN03102 244 ---FTWGTAARGGTSVcmRHVTAPEIYKNI--EMHNVThmCCVPTvFNILLKGNSL-----DLSPRSGPVHV-LTGGSPP 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 315 DETAVQTFVDAGARfkmpaecVFPAYGMAEATLAVSFAplftgltldvveadalEAENRAVPVPEGDPR--RGTDGVRSF 392
Cdd:PLN03102 313 PAALVKKVQRLGFQ-------VMHAYGLTEATGPVLFC----------------EWQDEWNRLPENQQMelKARQGVSIL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 393 ALlgRPLDGLEAEIVDDAGKrvDEREVGEIRLRGEAVTPGYLTmdGPLATQD--EDGWLNTGDLGYL-VDGQIVICGRRK 469
Cdd:PLN03102 370 GL--ADVDVKNKETQESVPR--DGKTMGEIVIKGSSIMKGYLK--NPKATSEafKHGWLNTGDVGVIhPDGHVEIKDRSK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 470 DVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMkqvsARVRDAVD----- 544
Cdd:PLN03102 444 DIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLV----TRERDLIEycren 519
|
410 420
....*....|....*....|....*.
gi 300790052 545 ----MRPYAVVVLPagSLPKTPSGKV 566
Cdd:PLN03102 520 lphfMCPRKVVFLQ--ELPKNGNGKI 543
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
8-578 |
1.57e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 79.70 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 8 LVATATKRGQQRGMVTGEpkepVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGS-VTML 86
Cdd:PRK07470 13 LRQAARRFPDRIALVWGD----RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVwVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 87 HQPTPrTDLAEWAEdTVRVLGMIGSDqdalGGPGGLAPRPGSGAGPRNVTVLLGEPFdqlapvleqkGIGFQLITELAAA 166
Cdd:PRK07470 89 FRQTP-DEVAYLAE-ASGARAMICHA----DFPEHAAAVRAASPDLTHVVAIGGARA----------GLDYEALVARHLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 167 EPLPDVVVtDEGDTALLQLTSGSTADPKAVRITYGNL---YSNVKAMVERAEFDFDVDVMVSwlPTFHDMGMVGFLTVPM 243
Cdd:PRK07470 153 ARVANAAV-DHDDPCWFFFTSGTTGRPKAAVLTHGQMafvITNHLADLMPGTTEQDASLVVA--PLSHGAGIHQLCQVAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 244 tfGVELVkITPVEFLSGPLIWpELITKYHGTTTaapnFAYAIVGRRMARVDEDDAYDLSKLRIALNGAEPIDETAVQTfv 323
Cdd:PRK07470 230 --GAATV-LLPSERFDPAEVW-ALVERHRVTNL----FTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKR-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 324 dagARFKMPAECVfPAYGMAEATLAVSFAPlftgltldvveadalEAENRAVPVPegDPRRGTdgvrsfalLGRPLDGLE 403
Cdd:PRK07470 300 ---ALAKLGKVLV-QYFGLGEVTGNITVLP---------------PALHDAEDGP--DARIGT--------CGFERTGME 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 404 AEIVDDAGKRVDEREVGEIRLRGEAVTPGYLtmDGPLATQD--EDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLY 480
Cdd:PRK07470 351 VQIQDDEGRELPPGETGEICVIGPAVFAGYY--NNPEANAKafRDGWFRTGDLGHLdARGFLYITGRASDMYISGGSNVY 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 481 PTDIER--------AATSVEGV------RAGNAVAVRLDAGS-RRERFAVVLESKLagdaeaeknlmkqvsARVRdavdm 545
Cdd:PRK07470 429 PREIEEkllthpavSEVAVLGVpdpvwgEVGVAVCVARDGAPvDEAELLAWLDGKV---------------ARYK----- 488
|
570 580 590
....*....|....*....|....*....|...
gi 300790052 546 RPYAVVVLPAgsLPKTPSGKVKRAATAQQFADR 578
Cdd:PRK07470 489 LPKRFFFWDA--LPKSGYGKITKKMVREELEER 519
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
33-570 |
1.70e-15 |
|
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: 79.26 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDTVRVLgmigsd 112
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 qdALGGPGGLAPRPGSGAGPRNVTVLLGEPFDQLAPvleqkgigfqlitelaaaEPLPDvvvtdegDTALLQLTSGSTAD 192
Cdd:cd12116 88 --VLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRT------------------PVSPD-------DLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 193 PKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTvPMTFGVELVkITPVEFLSGPLIWPELITKyH 272
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMRERLGLGPG-DRLLAVTTYAFDISLLELLL-PLLAGARVV-IAPRETQRDPEALARLIEA-H 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 273 GTTT--AAPnfayaiVGRRMARVDEDDAydLSKLRiALNGAEPIDETAVQTFVDAGArfkmpaeCVFPAYGMAEATLAVS 350
Cdd:cd12116 217 SITVmqATP------ATWRMLLDAGWQG--RAGLT-ALCGGEALPPDLAARLLSRVG-------SLWNLYGPTETTIWST 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 351 faplftgltldvveADALEAENRAVPvpegdprrgtdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVT 430
Cdd:cd12116 281 --------------AARVTAAAGPIP------------------IGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVA 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 431 PGY-----LT----MDGPLATQDEDgWLNTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGnAV 500
Cdd:cd12116 329 QGYlgrpaLTaerfVPDPFAGPGSR-LYRTGDLVrRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQA-AV 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 501 AVRLDAGSRRERFAVVLESKLAGDAEAeknLMKQVSARVRDAvdMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:cd12116 407 VVREDGGDRRLVAYVVLKAGAAPDAAA---LRAHLRATLPAY--MVPSAFVRLDA--LPLTANGKLDRKA 469
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
396-485 |
2.73e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 78.70 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVD-DAGKRVDEREVGEIRLRGEAVTPGYLTMdgPLATQ---DEDGWLNTGDLGYL-VDGQIVICGRRKD 470
Cdd:PRK08315 374 GRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWND--PEKTAeaiDADGWMHTGDLAVMdEEGYVNIVGRIKD 451
|
90
....*....|....*
gi 300790052 471 VIIMGGRNLYPTDIE 485
Cdd:PRK08315 452 MIIRGGENIYPREIE 466
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
125-485 |
2.78e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 78.57 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 125 RPGSGAGPRNVtVLLGEPFDQLAPVleqkgIGFQLITELAAAEpLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNL- 203
Cdd:PRK08008 127 QQEDATPLRHI-CLTRVALPADDGV-----SSFTQLKAQQPAT-LCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLr 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 204 ----YSNVKAMVeRAEfdfdvDVMVSWLPTFHdmgmVGF-LTVPM---TFGVELVKitpVEFLSGPLIWPElITKYHGTT 275
Cdd:PRK08008 200 fagyYSAWQCAL-RDD-----DVYLTVMPAFH----IDCqCTAAMaafSAGATFVL---LEKYSARAFWGQ-VCKYRATI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 276 T-AAPnfayAIVGRRMAR--VDEDDAYDLSKLRIALNgaepIDETAVQTFVdagARFKMPaecVFPAYGMAEaTLAvsfa 352
Cdd:PRK08008 266 TeCIP----MMIRTLMVQppSANDRQHCLREVMFYLN----LSDQEKDAFE---ERFGVR---LLTSYGMTE-TIV---- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 353 plftGLTLDvveadaleaenravpvPEGDPRRgtdgvrsFALLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEavtPG 432
Cdd:PRK08008 327 ----GIIGD----------------RPGDKRR-------WPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGV---PG 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300790052 433 YLTMDG----PLATQ---DEDGWLNTGDLGYlVD--GQIVICGRRKDVIIMGGRNLYPTDIE 485
Cdd:PRK08008 377 KTIFKEyyldPKATAkvlEADGWLHTGDTGY-VDeeGFFYFVDRRCNMIKRGGENVSCVELE 437
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
174-570 |
3.36e-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: 77.90 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 174 VTDEGDTALLQLTSGSTADPKAVRitygNLYSNVKAMVE-------RAEFDfdvDVMVSWLPTFHDMGMVGFLTVPMTFG 246
Cdd:cd05958 93 LTASDDICILAFTSGTTGAPKATM----HFHRDPLASADryavnvlRLRED---DRFVGSPPLAFTFGLGGVLLFPFGVG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 247 ---VELVKITPVEFLSgpliwpeLITKYHGTTTAAPNFAYaivgRRMARVDEDDAYDLSKLRIALNGAEpidetavqtfv 323
Cdd:cd05958 166 asgVLLEEATPDLLLS-------AIARYKPTVLFTAPTAY----RAMLAHPDAAGPDLSSLRKCVSAGE----------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 324 dagarfKMPAEcvfpaygMAEATLAVSFAPLFTGLtldvveaDALEAENRAVPVPEGDPRRGTdgvrsfalLGRPLDGLE 403
Cdd:cd05958 224 ------ALPAA-------LHRAWKEATGIPIIDGI-------GSTEMFHIFISARPGDARPGA--------TGKPVPGYE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 404 AEIVDDAGKRVDEREVGEIRLRGEAvtpGYLTMDGPLA-TQDEDGWLNTGDLgYLV--DGQIVICGRRKDVIIMGGRNLY 480
Cdd:cd05958 276 AKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQrTYVQGGWNITGDT-YSRdpDGYFRHQGRSDDMIVSGGYNIA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 481 PTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVrdAVDMRPYAVVVLPagSLPK 560
Cdd:cd05958 352 PPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHI--APYKYPRAIEFVT--ELPR 427
|
410
....*....|
gi 300790052 561 TPSGKVKRAA 570
Cdd:cd05958 428 TATGKLQRFA 437
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
172-570 |
1.01e-14 |
|
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: 76.64 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 172 VVVTDEGDT-ALLQLTSGSTADPKAVRITYGNLYSNVKAMVER------------AEFDFDVDVMvSWLPtfhdmgmvgf 238
Cdd:cd17649 87 LLLTHHPRQlAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERygltpgdrelqfASFNFDGAHE-QLLP---------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 239 ltvPMTFGVELVkITPVEFLSGPLIWPELITKyHGTTTAAPNFAYaivGRRMARVDEDDAYDLSK-LRIALNGAEPIDet 317
Cdd:cd17649 156 ---PLICGACVV-LRPDELWASADELAEMVRE-LGVTVLDLPPAY---LQQLAEEADRTGDGRPPsLRLYIFGGEALS-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 318 avqtfVDAGARFKMPAECVFPAYGMAEATLAVsfaplftglTLDVVEADALEAENrAVPvpegdprrgtdgvrsfalLGR 397
Cdd:cd17649 226 -----PELLRRWLKAPVRLFNAYGPTEATVTP---------LVWKCEAGAARAGA-SMP------------------IGR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 398 PLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQ---DEDG-----WLNTGDLG-YLVDGQIVICGRR 468
Cdd:cd17649 273 PLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERfvpDPFGapgsrLYRTGDLArWRDDGVIEYLGRV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 469 KDVIIMGGRNLYPTDIERAATSVEGVRAGnAVAVRLDAGSRRERFAVVLESKLAGDAEAEKnLMKQVSARVRDAvdMRPY 548
Cdd:cd17649 353 DHQVKIRGFRIELGEIEAALLEHPGVREA-AVVALDGAGGKQLVAYVVLRAAAAQPELRAQ-LRTALRASLPDY--MVPA 428
|
410 420
....*....|....*....|..
gi 300790052 549 AVVVLPagSLPKTPSGKVKRAA 570
Cdd:cd17649 429 HLVFLA--RLPLTPNGKLDRKA 448
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
28-487 |
2.03e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.14 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 28 EPVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAApvlIAPTVQA---VWLAGGsvtMLHQPTPRTDLA-------- 96
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPN---IPAMVEAhfgVPMAGA---VLNTLNTRLDAAsiafmlrh 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 97 ----------EWAEDTVRVLGMIGSDQ----DALGGPGGLAPRPGSgagprnvtvLLGEPFdqlapvleqkgigfqlite 162
Cdd:PRK08162 114 geakvlivdtEFAEVAREALALLPGPKplviDVDDPEYPGGRFIGA---------LDYEAF------------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 163 LAAAEP-----LPDvvvtDEGDTALLQLTSGSTADPKAV----RITYGNLYSNVKA--MVERAefdfdvdVMVSWLPTFH 231
Cdd:PRK08162 166 LASGDPdfawtLPA----DEWDAIALNYTSGTTGNPKGVvyhhRGAYLNALSNILAwgMPKHP-------VYLWTLPMFH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 232 DMGMVGFLTVPMTFGVE--LVKITPVeflsgpLIWpELITKyHGTT--TAAPnfayaIVGRRMARVDEDDAydlsklria 307
Cdd:PRK08162 235 CNGWCFPWTVAARAGTNvcLRKVDPK------LIF-DLIRE-HGVThyCGAP-----IVLSALINAPAEWR--------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 308 lngaEPIDETaVQTFVdAGArfkMPAECVFPayGMAEATLAVSFAplfTGLTlDV---VEADALEAENRAVPVPEGDPRR 384
Cdd:PRK08162 293 ----AGIDHP-VHAMV-AGA---APPAAVIA--KMEEIGFDLTHV---YGLT-ETygpATVCAWQPEWDALPLDERAQLK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 385 GTDGVRSFALLGrpldgleAEIVD-DAGKRV--DEREVGEIRLRGEAVTPGYLTmdGPLATQD--EDGWLNTGDLGYL-V 458
Cdd:PRK08162 358 ARQGVRYPLQEG-------VTVLDpDTMQPVpaDGETIGEIMFRGNIVMKGYLK--NPKATEEafAGGWFHTGDLAVLhP 428
|
490 500
....*....|....*....|....*....
gi 300790052 459 DGQIVICGRRKDVIIMGGRNLYPTDIERA 487
Cdd:PRK08162 429 DGYIKIKDRSKDIIISGGENISSIEVEDV 457
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
33-570 |
2.03e-14 |
|
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: 75.82 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDtvrvlgmigsd 112
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILED----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 qdalggpgglaprpgsgAGPRnvtvllgepfdqlapvleqkgigfqlitelaaaeplpdVVVTDEGDTALLQLTSGSTAD 192
Cdd:cd12115 95 -----------------AQAR--------------------------------------LVLTDPDDLAYVIYTSGSTGR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 193 PKAVRITYGNlysnVKAMVERAEFDFDVDVMVSWL---PTFHDMGmVGFLTVPMTFGVELVkitpveFLSGPLIWPELit 269
Cdd:cd12115 120 PKGVAIEHRN----AAAFLQWAAAAFSAEELAGVLastSICFDLS-VFELFGPLATGGKVV------LADNVLALPDL-- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 270 kyhgtttAAPNFAYAI--VGRRMARVDEDDAYDLSKLRIALNGaEPIDETAVQTFVDagarfKMPAECVFPAYGMAEATL 347
Cdd:cd12115 187 -------PAAAEVTLIntVPSAAAELLRHDALPASVRVVNLAG-EPLPRDLVQRLYA-----RLQVERVVNLYGPSEDTT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 348 AVSFAPLftgltldvveadaleaenravpvpegdpRRGTDGVRSfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGE 427
Cdd:cd12115 254 YSTVAPV----------------------------PPGASGEVS---IGRPLANTQAYVLDRALQPVPLGVPGELYIGGA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 428 AVTPGYLtmDGPLATQDE---DGWL------NTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAG 497
Cdd:cd12115 303 GVARGYL--GRPGLTAERflpDPFGpgarlyRTGDLVrWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300790052 498 NAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQvsarvRDAVDMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:cd12115 381 VVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGT-----RLPAYMVPSRFVRLDA--LPLTPNGKIDRSA 446
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
173-570 |
2.24e-14 |
|
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: 75.83 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 173 VVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHdmgmvGF-LTVPMTFGVELVK 251
Cdd:cd05920 134 LAESIPEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQD-TVYLAVLPAAH-----NFpLACPGVLGTLLAG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 252 ITPVefLSG--------PLIWPELITkyhgTTTAAPnfayAIVGRRMARVDEDDAyDLSKLRIALNGAEPIDETAVQtfv 323
Cdd:cd05920 208 GRVV--LAPdpspdaafPLIEREGVT----VTALVP----ALVSLWLDAAASRRA-DLSSLRLLQVGGARLSPALAR--- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 324 DAGARFKMPAECVFpayGMAEATLAvsfaplFTGLtldvveadaleaenravpvpeGDPrrgtdGVRSFALLGRPLDGL- 402
Cdd:cd05920 274 RVPPVLGCTLQQVF---GMAEGLLN------YTRL---------------------DDP-----DEVIIHTQGRPMSPDd 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 403 EAEIVDDAGKRVDEREVGEIRLRGEAVTPGYltMDGPLATQ---DEDGWLNTGDLGYLV-DGQIVICGRRKDVIIMGGRN 478
Cdd:cd05920 319 EIRVVDEEGNPVPPGEEGELLTRGPYTIRGY--YRAPEHNArafTPDGFYRTGDLVRRTpDGYLVVEGRIKDQINRGGEK 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 479 LYPTDIERAATSVEGVRAGNAVAV-RLDAGSRRERFAVVLESKLaGDAEAEKNLMKQVSARVRdavdmRPYAVVVLPagS 557
Cdd:cd05920 397 IAAEEVENLLLRHPAVHDAAVVAMpDELLGERSCAFVVLRDPPP-SAAQLRRFLRERGLAAYK-----LPDRIEFVD--S 468
|
410
....*....|...
gi 300790052 558 LPKTPSGKVKRAA 570
Cdd:cd05920 469 LPLTAVGKIDKKA 481
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
176-573 |
3.16e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 75.03 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 176 DEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFG---VELVKI 252
Cdd:PRK07787 126 DPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTAD-DVLVHGLPLFHVHGLVLGVLGPLRIGnrfVHTGRP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 253 TPVEFLSGpliwpeliTKYHGTTTaapnFAYAIVGRRMARvDEDDAYDLSKLRIALNGAEPIDETAVQTFVDAGARfkMP 332
Cdd:PRK07787 205 TPEAYAQA--------LSEGGTLY----FGVPTVWSRIAA-DPEAARALRGARLLVSGSAALPVPVFDRLAALTGH--RP 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 333 AEcvfpAYGMAEATLAVSfaplftgltldvVEADaleaenravpvpeGDPRRGTdgvrsfalLGRPLDGLEAEIVDDAGK 412
Cdd:PRK07787 270 VE----RYGMTETLITLS------------TRAD-------------GERRPGW--------VGLPLAGVETRLVDEDGG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 413 RV--DEREVGEIRLRGEAVTPGYLTM-DGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRK-DVIIMGGRNLYPTDIERA 487
Cdd:PRK07787 313 PVphDGETVGELQVRGPTLFDGYLNRpDATAAAFTADGWFRTGDVAVVdPDGMHRIVGREStDLIKSGGYRIGAGEIETA 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 488 ATSVEGVRAGNAVAV-RLDAGSRRERFAVvlesklAGDAEAEKNLMKQVSARVrdAVDMRPYAVVVLPAgsLPKTPSGKV 566
Cdd:PRK07787 393 LLGHPGVREAAVVGVpDDDLGQRIVAYVV------GADDVAADELIDFVAQQL--SVHKRPREVRFVDA--LPRNAMGKV 462
|
....*..
gi 300790052 567 KRAATAQ 573
Cdd:PRK07787 463 LKKQLLS 469
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
33-570 |
4.29e-14 |
|
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: 74.61 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPV--LIAptVQAVWLAGGSVTML--HQPTPRTD--LAEWAEDTVRVL 106
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPeqVVA--VLGILAAGAAYVPVdiDQPAARREaiLADAGARLVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 107 GMIgsdqdalggpgglaprpgsgagprnvTVLLGEPFDQLAPVLEqkgigfqliteLAAAEPLPDVVVTDEGDTALLQLT 186
Cdd:cd12114 92 GPD--------------------------AQLDVAVFDVLILDLD-----------ALAAPAPPPPVDVAPDDLAYVIFT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 187 SGSTADPKAVRITYGNLYSNVKAMVER------------AEFDFDvdvmvswLPTFHDMGmvgfltvPMTFGVELVKITP 254
Cdd:cd12114 135 SGSTGTPKGVMISHRAALNTILDINRRfavgpddrvlalSSLSFD-------LSVYDIFG-------ALSAGATLVLPDE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 255 VEfLSGPLIWPELITKyHGTTtaAPNFAYAIVGRRMArVDEDDAYDLSKLRIALNGAEPIDetavqtfVDAGARFK--MP 332
Cdd:cd12114 201 AR-RRDPAHWAELIER-HGVT--LWNSVPALLEMLLD-VLEAAQALLPSLRLVLLSGDWIP-------LDLPARLRalAP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 333 AECVFPAYGMAEATLAVSFAPLftgltldvveaDALEAENRAVPvpegdprrgtdgvrsfalLGRPLDGLEAEIVDDAGK 412
Cdd:cd12114 269 DARLISLGGATEASIWSIYHPI-----------DEVPPDWRSIP------------------YGRPLANQRYRVLDPRGR 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 413 RVDEREVGEIRLRGEAVTPGYLtmDGPLATQ-----DEDG--WLNTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDI 484
Cdd:cd12114 320 DCPDWVPGELWIGGRGVALGYL--GDPELTAarfvtHPDGerLYRTGDLGrYRPDGTLEFLGRRDGQVKVRGYRIELGEI 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 485 ERAATSVEGVRAGNAVAVRlDAGSRRERFAVVLESKLAGDAEAEknLMKQVSARVRDAvdMRPYAVVVLPAgsLPKTPSG 564
Cdd:cd12114 398 EAALQAHPGVARAVVVVLG-DPGGKRLAAFVVPDNDGTPIAPDA--LRAFLAQTLPAY--MIPSRVIALEA--LPLTANG 470
|
....*.
gi 300790052 565 KVKRAA 570
Cdd:cd12114 471 KVDRAA 476
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
175-575 |
4.45e-14 |
|
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: 75.08 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 175 TDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMV-GFLTVPMTfGVELVKIT 253
Cdd:cd05905 146 TRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYES-RPLVTVLDFKSGLGLWhGCLLSVYS-GHHTILIP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 254 PVEFLSGPLIWPELITKYHGTTTAAP-NFAYAIVGRRMARVDEDDAYD--LSKLRIALNGAE-PIDETAVQTFVDAGARF 329
Cdd:cd05905 224 PELMKTNPLLWLQTLSQYKVRDAYVKlRTLHWCLKDLSSTLASLKNRDvnLSSLRMCMVPCEnRPRISSCDSFLKLFQTL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 330 KMPAECVFPAYGmaeaTLAVSF----APLFTGLTLDVVEADALEaENRAVPVPEGDPRRGT--DGvrsfallGRPLDGLE 403
Cdd:cd05905 304 GLSPRAVSTEFG----TRVNPFicwqGTSGPEPSRVYLDMRALR-HGVVRLDERDKPNSLPlqDS-------GKVLPGAQ 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 404 AEIVDDAGK---RVDEreVGEIRLRGEAVTPGYLTMDGPLATQDED-------------GWLNTGDLGYLVDGQIV---- 463
Cdd:cd05905 372 VAIVNPETKglcKDGE--IGEIWVNSPANASGYFLLDGETNDTFKVfpstrlstgitnnSYARTGLLGFLRPTKCTdlnv 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 464 -------ICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAvrldagSRRERFAVVLESKLAGDAEAeKNLMKQVS 536
Cdd:cd05905 450 eehdllfVVGSIDETLEVRGLRHHPSDIEATVMRVHPYRGRCAVF------SITGLVVVVAEQPPGSEEEA-LDLVPLVL 522
|
410 420 430
....*....|....*....|....*....|....*....
gi 300790052 537 ARVRDAVDMRPYAVVVLPAGSLPKTPSGKVKRAATAQQF 575
Cdd:cd05905 523 NAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAF 561
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
395-568 |
4.65e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 75.03 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 LGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATqdeDGWLNTGDLGYLVD-GQIVICGRRKDVII 473
Cdd:PRK13383 347 VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKAVV---DGMTSTGDMGYLDNaGRLFIVGREDDMII 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 474 MGGRNLYPTDIERAATSVEGVrAGNAVAVRLDA--GSRRERFaVVLESKLAGDAEAEKNLMKQVSARVRDAVDMRPYAvv 551
Cdd:PRK13383 424 SGGENVYPRAVENALAAHPAV-ADNAVIGVPDErfGHRLAAF-VVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVS-- 499
|
170
....*....|....*..
gi 300790052 552 vlpagSLPKTPSGKVKR 568
Cdd:PRK13383 500 -----SIPRNPTGKVLR 511
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
33-487 |
5.31e-14 |
|
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: 74.70 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLA--AAPVLIApTVQAVwLAGGSVTMLHqPTPRTD----LAEWAE------ 100
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGfnSPEWFIA-AVGAI-FAGGIAVGIY-TTNSPEacqyVAETSEanilvv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 101 DTVRVLGMIGSDQDALggpgglaprpgsgagPR-NVTVLLGEPFDQLAPVLeqkgIGFQLITELAAAEP---LPDVVVTD 176
Cdd:cd05933 87 ENQKQLQKILQIQDKL---------------PHlKAIIQYKEPLKEKEPNL----YSWDEFMELGRSIPdeqLDAIISSQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 177 E-GDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVD---VMVSWLPTFHDMGMVGFLTVPMTFG------ 246
Cdd:cd05933 148 KpNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqeSVVSYLPLSHIAAQILDIWLPIKVGgqvyfa 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 247 ---------VE-LVKITPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGRRMARVDEDDAYD---------------- 300
Cdd:cd05933 228 qpdalkgtlVKtLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLmggespsplfyrlakk 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 301 --LSKLRIAL---------NGAEPIDETAVQTFVDAGARfkmpaecVFPAYGMAEATlavsfAPLFtgltldvveadale 369
Cdd:cd05933 308 lvFKKVRKALgldrcqkffTGAAPISRETLEFFLSLNIP-------IMELYGMSETS-----GPHT-------------- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 370 aenraVPVPEgdprrgtdgvrSFALL--GRPLDGLEAEIVDDagkrvDEREVGEIRLRGEAVTPGYLTM-DGPLATQDED 446
Cdd:cd05933 362 -----ISNPQ-----------AYRLLscGKALPGCKTKIHNP-----DADGIGEICFWGRHVFMGYLNMeDKTEEAIDED 420
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 300790052 447 GWLNTGDLGYL-VDGQIVICGRRKDVIIM-GGRNLYPTDIERA 487
Cdd:cd05933 421 GWLHSGDLGKLdEDGFLYITGRIKELIITaGGENVPPVPIEDA 463
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
155-568 |
5.58e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 74.91 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 155 IGFQLITELAAAEPLPDVVVTDEgDTALLQLTSGSTADPKAVRITYGNLYSNVKA----MVERAEFDFDVDVMVSWLPTF 230
Cdd:PRK08751 186 IRFREALALGRKHSMPTLQIEPD-DIAFLQYTGGTTGVAKGAMLTHRNLVANMQQahqwLAGTGKLEEGCEVVITALPLY 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 231 HDMGMVGFLTVPMTFGvelvkiTPVEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGRrMARVDEDDAYDLSKLRIALNG 310
Cdd:PRK08751 265 HIFALTANGLVFMKIG------GCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNG-LLNTPGFDQIDFSSLKMTLGG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 311 AepideTAVQTFVdAGARFKMPAECVFPAYGMAEATLAVSFAPLftgltldvveadALEAENRAVpvpegdprrgtdgvr 390
Cdd:PRK08751 338 G-----MAVQRSV-AERWKQVTGLTLVEAYGLTETSPAACINPL------------TLKEYNGSI--------------- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 391 sfallGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLAT-QDEDGWLNTGDLGYL-VDGQIVICGRR 468
Cdd:PRK08751 385 -----GLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKvMDADGWLHTGDIARMdEQGFVYIVDRK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 469 KDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRlDAGSRRERFAVVLESKLAGDAEaeknlmkQVSARVRDAVDMRPY 548
Cdd:PRK08751 460 KDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVP-DEKSGEIVKVVIVKKDPALTAE-------DVKAHARANLTGYKQ 531
|
410 420
....*....|....*....|
gi 300790052 549 AVVVLPAGSLPKTPSGKVKR 568
Cdd:PRK08751 532 PRIIEFRKELPKTNVGKILR 551
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
179-471 |
6.92e-14 |
|
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: 74.56 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKAM---VERAEFDFDVDVMVSWLP------------TFHDMGMVGFLTVPM 243
Cdd:cd05927 115 DLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkiLEILNKINPTDVYISYLPlahifervvealFLYHGAKIGFYSGDI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 244 TFGVELVKI-TPVEFLSGPLIWPELITKYHGTTTAAP-------NFAYAIVGRRMARVDED-----DAYDLSK------- 303
Cdd:cd05927 195 RLLLDDIKAlKPTVFPGVPRVLNRIYDKIFNKVQAKGplkrklfNFALNYKLAELRSGVVRaspfwDKLVFNKikqalgg 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 304 -LRIALNGAEPIDETaVQTFVDAgarfkMPAECVFPAYGMAEaTLAVSFaplftgLTLdvveadaleaenravpvpEGDP 382
Cdd:cd05927 275 nVRLMLTGSAPLSPE-VLEFLRV-----ALGCPVLEGYGQTE-CTAGAT------LTL------------------PGDT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 383 RRGTdgvrsfalLGRPLDGLEAEIVD------DAGKRVDErevGEIRLRGEAVTPGYLtmDGPLATQ---DEDGWLNTGD 453
Cdd:cd05927 324 SVGH--------VGGPLPCAEVKLVDvpemnyDAKDPNPR---GEVCIRGPNVFSGYY--KDPEKTAealDEDGWLHTGD 390
|
330
....*....|....*....
gi 300790052 454 LG-YLVDGQIVICGRRKDV 471
Cdd:cd05927 391 IGeWLPNGTLKIIDRKKNI 409
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
178-502 |
7.10e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 74.29 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 178 GDTALLQLTSGSTADPKAVRITYGNLYSNVKAM------VERAEFDFDVDVMVSWLPTFHDMGM-VGFLTVPMTFGVELV 250
Cdd:PRK07059 204 DDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMeawlqpAFEKKPRPDQLNFVCALPLYHIFALtVCGLLGMRTGGRNIL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 251 KITP------VEFLSG--PLIWPELITKYHGTTTAaPNFayaivgrrmarvdedDAYDLSKLRIALNGAepideTAVQTF 322
Cdd:PRK07059 284 IPNPrdipgfIKELKKyqVHIFPAVNTLYNALLNN-PDF---------------DKLDFSKLIVANGGG-----MAVQRP 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 323 VdAGARFKMPAECVFPAYGMAEAtlavsfAPLFTGLTLDVVEADaleaenravpvpegdprrGTdgvrsfalLGRPLDGL 402
Cdd:PRK07059 343 V-AERWLEMTGCPITEGYGLSET------SPVATCNPVDATEFS------------------GT--------IGLPLPST 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 403 EAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLA-TQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLY 480
Cdd:PRK07059 390 EVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAkVMTADGFFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVY 469
|
330 340
....*....|....*....|..
gi 300790052 481 PTDIERAATSVEGVRAGNAVAV 502
Cdd:PRK07059 470 PNEIEEVVASHPGVLEVAAVGV 491
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
170-570 |
9.15e-14 |
|
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: 73.44 E-value: 9.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 170 PDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERaefdFDVDVMVSWLpTFHDMGM-VGFLTVPMTF--G 246
Cdd:cd17652 85 PALLLTTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA----FDVGPGSRVL-QFASPSFdASVWELLMALlaG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 247 VELVKITPVEFLSG-PLIwpELITKYHGTTTAAPNFAYAIVgrrmarvdedDAYDLSKLRIALNGAEPIDETAVQTFVda 325
Cdd:cd17652 160 ATLVLAPAEELLPGePLA--DLLREHRITHVTLPPAALAAL----------PPDDLPDLRTLVVAGEACPAELVDRWA-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 326 garfkmPAECVFPAYGMAEATLAVSFAPLFTGltldvveadaleaeNRAVPVpegdprrgtdgvrsfallGRPLDGLEAE 405
Cdd:cd17652 226 ------PGRRMINAYGPTETTVCATMAGPLPG--------------GGVPPI------------------GRPVPGTRVY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 406 IVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQ--------DEDGWLNTGDLG-YLVDGQIVICGRRKDVIIMGG 476
Cdd:cd17652 268 VLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERfvadpfgaPGSRMYRTGDLArWRADGQLEFLGRADDQVKIRG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 477 RNLYPTDIERAATSVEGVRAGnAVAVRLDAGSRRERFAVVLESklAGDAEAEKNLMKQVSARVRDAvdMRPYAVVVLPAg 556
Cdd:cd17652 348 FRIELGEVEAALTEHPGVAEA-VVVVRDDRPGDKRLVAYVVPA--PGAAPTAAELRAHLAERLPGY--MVPAAFVVLDA- 421
|
410
....*....|....
gi 300790052 557 sLPKTPSGKVKRAA 570
Cdd:cd17652 422 -LPLTPNGKLDRRA 434
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
164-568 |
9.59e-14 |
|
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: 73.57 E-value: 9.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 164 AAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERA---EFDFDvDVMVSWLPTFHDMGMVGFLT 240
Cdd:cd05929 111 AAEGGSPETPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAAlgfGPGAD-SVYLSPAPLYHAAPFRWSMT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 241 VPMTFG--VELVKITPVEFLsgpliwpELITKYHGTTTaapNFAYAIVgRRMARVDED--DAYDLSKLRIALNGAEPIDE 316
Cdd:cd05929 190 ALFMGGtlVLMEKFDPEEFL-------RLIERYRVTFA---QFVPTMF-VRLLKLPEAvrNAYDLSSLKRVIHAAAPCPP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 317 TAVQTFVDAGArfkmpaECVFPAYGMAEATlavsfaplftGLTLdvveadaleaenravpvpegdpRRGTDGVRSFALLG 396
Cdd:cd05929 259 WVKEQWIDWGG------PIIWEYYGGTEGQ----------GLTI----------------------INGEEWLTHPGSVG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 397 RPLDGlEAEIVDDAGKRVDEREVGEIRLRGeavTPGYLTMDGPLATQ---DEDGWLNTGDLGYL-VDGQIVICGRRKDVI 472
Cdd:cd05929 301 RAVLG-KVHILDEDGNEVPPGEIGEVYFAN---GPGFEYTNDPEKTAaarNEGGWSTLGDVGYLdEDGYLYLTDRRSDMI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 473 IMGGRNLYPTDIERAATSVEGVRAGNAVAVRlDAGSRRERFAVV--LESKLAGDAEAE-------KNLMKQVSARVRDAV 543
Cdd:cd05929 377 ISGGVNIYPQEIENALIAHPKVLDAAVVGVP-DEELGQRVHAVVqpAPGADAGTALAEeliaflrDRLSRYKCPRSIEFV 455
|
410 420
....*....|....*....|....*
gi 300790052 544 DmrpyavvvlpagSLPKTPSGKVKR 568
Cdd:cd05929 456 A------------ELPRDDTGKLYR 468
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
176-476 |
1.35e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 73.31 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 176 DEGDTALLQLTSGSTADPKAVRITYGNLYSNvkamvERAEFDF----DVDVMVSWLPTFHDMGMVGFLTVPMTFGVelvk 251
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLAN-----QRACLKFfspkEDDVMMSFLPPFHAYGFNSCTLFPLLSGV---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 252 itPVEFLSGPLiWP----ELITKYHGT-TTAAPNFAYAIVgrRMARVDEDdayDLSKLRIALNGAEPIDETAVQtfvdaG 326
Cdd:PRK06334 252 --PVVFAYNPL-YPkkivEMIDEAKVTfLGSTPVFFDYIL--KTAKKQES---CLPSLRFVVIGGDAFKDSLYQ-----E 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 327 ARFKMPAECVFPAYGMAEATlavsfaPLFTGLTldvveadaleaenravpvpEGDPRRGTdgvrsfaLLGRPLDGLEAEI 406
Cdd:PRK06334 319 ALKTFPHIQLRQGYGTTECS------PVITINT-------------------VNSPKHES-------CVGMPIRGMDVLI 366
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300790052 407 VDDAGK-RVDEREVGEIRLRGEAVTPGYLTMD--GPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGG 476
Cdd:PRK06334 367 VSEETKvPVSSGETGLVLTRGTSLFSGYLGEDfgQGFVELGGETWYVTGDLGYVdRHGELFLKGRLSRFVKIGA 440
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
33-566 |
1.65e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 73.07 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLV-AGGFERGTAVGVLAA-APVLIApTVQAVWLAGGSVTMLHqPTPRTD-LAEWAEDTVRVLGMI 109
Cdd:PRK08314 37 SYRELLEEAERLAGYLQqECGVRKGDRVLLYMQnSPQFVI-AYYAILRANAVVVPVN-PMNREEeLAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 GSDQ----DALGGPGGLAP---RPGSGAGPRNVTVLLGEPFDQLAPVLEQKGIGFQLITE-LAAAEPLPDVVVTDEgDTA 181
Cdd:PRK08314 115 GSELapkvAPAVGNLRLRHvivAQYSDYLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKEaLAAGLAPPPHTAGPD-DLA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 182 LLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTFGVELVKITpveflsgp 261
Cdd:PRK08314 194 VLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPE-SVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP-------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 262 lIW-----PELITKYHGTT-----------TAAPNFAyaivgrrmarvdeddAYDLSKLR-IALNGAEPIDETAVQTFVD 324
Cdd:PRK08314 265 -RWdreaaARLIERYRVTHwtniptmvvdfLASPGLA---------------ERDLSSLRyIGGGGAAMPEAVAERLKEL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 325 AGARFkmpaecvFPAYGMAEaTLAVSFAplftgltldvveadaleaeNravpvPEGDPRRGTdgvrsfalLGRPLDGLEA 404
Cdd:PRK08314 329 TGLDY-------VEGYGLTE-TMAQTHS-------------------N-----PPDRPKLQC--------LGIPTFGVDA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 405 EIVD-DAGKRVDEREVGEIRLRGEAVTPGYltMDGPLATQDE----DG--WLNTGDLGYL-VDGQIVICGRRKDVIIMGG 476
Cdd:PRK08314 369 RVIDpETLEELPPGEVGEIVVHGPQVFKGY--WNRPEATAEAfieiDGkrFFRTGDLGRMdEEGYFFITDRLKRMINASG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 477 RNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEknlmkQVSARVRDavDMRPYAV--VVLP 554
Cdd:PRK08314 447 FKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEE-----EIIAWARE--HMAAYKYprIVEF 519
|
570
....*....|..
gi 300790052 555 AGSLPKTPSGKV 566
Cdd:PRK08314 520 VDSLPKSGSGKI 531
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-585 |
2.19e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 73.66 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 31 RRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDT-VRVLgmi 109
Cdd:PRK12467 537 VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSgVRLL--- 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 gsdqdaLGGPGGLAPRPGsgagPRNVTVLlgePFDQLAPVLEQKgigfqlitelaaAEPLPDVVVtDEGDTALLQLTSGS 189
Cdd:PRK12467 614 ------LTQSHLLAQLPV----PAGLRSL---CLDEPADLLCGY------------SGHNPEVAL-DPDNLAYVIYTSGS 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 190 TADPKAVRITYGNLYSNVKAMVERaeFDFDVDVMVSWLPTFHDMGMVGFLTVPMTFGVELVKITPVEFLSGPLIWPELIT 269
Cdd:PRK12467 668 TGQPKGVAISHGALANYVCVIAER--LQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMAD 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 270 kyHGTTTAAPNFAYAIVGRRMARVDEDdaydlSKLRIALNGAEPIDETAVQTFVDAGarfkmPAECVFPAYGMAEATLAV 349
Cdd:PRK12467 746 --QGVTVLKIVPSHLQALLQASRVALP-----RPQRALVCGGEALQVDLLARVRALG-----PGARLINHYGPTETTVGV 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 350 SFAPLftgltldvveaDALEAENRAVPvpegdprrgtdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAV 429
Cdd:PRK12467 814 STYEL-----------SDEERDFGNVP------------------IGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGL 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 430 TPGYLTMDG---------PLATQDEDGWlNTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRagNA 499
Cdd:PRK12467 865 ARGYHRRPAltaerfvpdPFGADGGRLY-RTGDLArYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVR--EA 941
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 500 VAVRLDAGSRRERFAVVLESKLAGDAE-AEKNLMKQVSARVRDAVDMRPYAVVVLpaGSLPKTPSGKVKRAATAQQFADR 578
Cdd:PRK12467 942 VVLAQPGDAGLQLVAYLVPAAVADGAEhQATRDELKAQLRQVLPDYMVPAHLLLL--DSLPLTPNGKLDRKALPKPDASA 1019
|
....*..
gi 300790052 579 IKKNADA 585
Cdd:PRK12467 1020 VQATFVA 1026
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
385-576 |
2.24e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 72.89 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 385 GTDGVRSFALLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYltMDGPLATQD--EDGWLNTGDLGYL-VDGQ 461
Cdd:PRK07786 337 GEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGY--WNNPEATAEafAGGWFHSGDLVRQdEEGY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 462 IVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRagnAVAVrldAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVRD 541
Cdd:PRK07786 415 VWVVDRKKDMIISGGENIYCAEVENVLASHPDIV---EVAV---IGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTD 488
|
170 180 190
....*....|....*....|....*....|....*..
gi 300790052 542 --AVDMRPYAVVVLPAgsLPKTPSGKVKRAATAQQFA 576
Cdd:PRK07786 489 rlARYKHPKALEIVDA--LPRNPAGKVLKTELRERYG 523
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
396-569 |
2.59e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 72.53 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYltMDGPLATQ---DEDGWLNTGDLGYL-VDGQIVICGRRKDV 471
Cdd:PRK09088 309 GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGY--WRRPQATArafTGDGWFRTGDIARRdADGFFWVVDRKKDM 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 472 IIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEaekNLMKQVSARVrdAVDMRPYAVV 551
Cdd:PRK09088 387 FISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE---RIRSHLSTRL--AKYKVPKHLR 461
|
170
....*....|....*...
gi 300790052 552 VLPAgsLPKTPSGKVKRA 569
Cdd:PRK09088 462 LVDA--LPRTASGKLQKA 477
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
173-472 |
5.11e-13 |
|
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: 71.48 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 173 VVTDEG--DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVER-AEFDFDVDVMVSWLPTFHDM------------GMVG 237
Cdd:cd17639 81 IFTDGKpdDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRvPELLGPDDRYLAYLPLAHIFelaaenvclyrgGTIG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 238 F-----LTVPMTFGV--ELVKITPVEFLSGPLIWpELITKYHGTTTAAPNF--------AYAivgRRMARVDEddAYDL- 301
Cdd:cd17639 161 YgsprtLTDKSKRGCkgDLTEFKPTLMVGVPAIW-DTIRKGVLAKLNPMGGlkrtlfwtAYQ---SKLKALKE--GPGTp 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 302 ---------------SKLRIALNGAEPIDEtAVQTFVdagarfKMPAECVFPAYGMAEaTLAvsfaplftgltldvvead 366
Cdd:cd17639 235 lldelvfkkvraalgGRLRYMLSGGAPLSA-DTQEFL------NIVLCPVIQGYGLTE-TCA------------------ 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 367 aleaeNRAVPVPeGDPRRGTdgvrsfalLGRPLDGLEAEIVD--DAGKRVDEREV-GEIRLRGEAVTPGYLtmDGPLATQ 443
Cdd:cd17639 289 -----GGTVQDP-GDLETGR--------VGPPLPCCEIKLVDweEGGYSTDKPPPrGEILIRGPNVFKGYY--KNPEKTK 352
|
330 340 350
....*....|....*....|....*....|...
gi 300790052 444 ---DEDGWLNTGDLGYLV-DGQIVICGRRKDVI 472
Cdd:cd17639 353 eafDGDGWFHTGDIGEFHpDGTLKIIDRKKDLV 385
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
28-568 |
5.92e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 71.41 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 28 EPVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVlaaapvlIAPTVQAVWLAGGSVTM-----------LHQPTPRTDLA 96
Cdd:PLN02479 42 GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAV-------IAPNIPAMYEAHFGVPMagavvncvnirLNAPTIAFLLE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 97 EWAEDTVRVlgmigsDQD----ALGGPGGLAPRPGSGAGPRNVTVLLGEPFD--QLAPVLEQKGIGFQ--LIT---ELAA 165
Cdd:PLN02479 115 HSKSEVVMV------DQEfftlAEEALKILAEKKKSSFKPPLLIVIGDPTCDpkSLQYALGKGAIEYEkfLETgdpEFAW 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 166 AEPlpdvvvTDEGDTALLQLTSGSTADPKAVRITYGNLYsnVKAMVERAEFDFDVDVMVSW-LPTFHDMGMVGFLTVPMT 244
Cdd:PLN02479 189 KPP------ADEWQSIALGYTSGTTASPKGVVLHHRGAY--LMALSNALIWGMNEGAVYLWtLPMFHCNGWCFTWTLAAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 245 FG--VELVKITPVEFLSGpliwpelITKYhGTT--TAAPNFAYAIVGRRMarvdEDDAYDLSKL-RIALNGAEPiDETAV 319
Cdd:PLN02479 261 CGtnICLRQVTAKAIYSA-------IANY-GVThfCAAPVVLNTIVNAPK----SETILPLPRVvHVMTAGAAP-PPSVL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 320 QTFVDAGARfkmpaecVFPAYGMAEA---TLAVSFAPlftgltldvvEADALEAENRAvpvpegdPRRGTDGVRSFALLG 396
Cdd:PLN02479 328 FAMSEKGFR-------VTHTYGLSETygpSTVCAWKP----------EWDSLPPEEQA-------RLNARQGVRYIGLEG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 397 rpLDgleaeIVD-DAGKRV--DEREVGEIRLRGEAVTPGYLtmDGPLATQD--EDGWLNTGDLGYL-VDGQIVICGRRKD 470
Cdd:PLN02479 384 --LD-----VVDtKTMKPVpaDGKTMGEIVMRGNMVMKGYL--KNPKANEEafANGWFHSGDLGVKhPDGYIEIKDRSKD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 471 VIIMGGRNLYPTDIERAATSVEGVRAGNAVAvRLDagsrrERFA------VVLESKLAGDAEA--EKNLMKqvSARVRDA 542
Cdd:PLN02479 455 IIISGGENISSLEVENVVYTHPAVLEASVVA-RPD-----ERWGespcafVTLKPGVDKSDEAalAEDIMK--FCRERLP 526
|
570 580
....*....|....*....|....*.
gi 300790052 543 VDMRPYAVVVlpaGSLPKTPSGKVKR 568
Cdd:PLN02479 527 AYWVPKSVVF---GPLPKTATGKIQK 549
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
221-568 |
7.19e-13 |
|
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: 69.99 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 221 DVMVSWLPTFHDMGMVGFLTVPMTFGVELV--KITPVEFLsgpliwpELITKYHGTTTAApnFAyAIVGRRMARVDEDDa 298
Cdd:cd17637 42 DVYLNMLPLFHIAGLNLALATFHAGGANVVmeKFDPAEAL-------ELIEEEKVTLMGS--FP-PILSNLLDAAEKSG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 299 YDLSKLRI--ALNGAEPIDETAVQTfvdaGARFkmpaecvFPAYGMAEATLAVSFAPLFTgltldvveadaleaenravp 376
Cdd:cd17637 111 VDLSSLRHvlGLDAPETIQRFEETT----GATF-------WSLYGQTETSGLVTLSPYRE-------------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 377 vpegdpRRGTdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGY 456
Cdd:cd17637 160 ------RPGS--------AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 457 L-VDGQIVICGRR--KDVIIMGGRNLYPTDIERA--------ATSVEGV---RAGNAV-AVrldagsrrerfaVVLEskl 521
Cdd:cd17637 226 FdEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVilehpaiaEVCVIGVpdpKWGEGIkAV------------CVLK--- 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 300790052 522 AGDAEAEKNLMKQVSARVrdAVDMRPYAVVVlpAGSLPKTPSGKVKR 568
Cdd:cd17637 291 PGATLTADELIEFVGSRI--ARYKKPRYVVF--VEALPKTADGSIDR 333
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
156-509 |
1.22e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 70.31 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 156 GFQLITELAAAEPLP-DVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMveRAEFDF---DVDvmvswLPTFh 231
Cdd:PRK09274 151 GTTLATLLRDGAAAPfPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL--REDYGIepgEID-----LPTF- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 232 dmgmvgfltvpmtfgvelvkitPVEFLSGPL-----IWPEL----------------ITKYHGTTTaapnFAYAIVGRRM 290
Cdd:PRK09274 223 ----------------------PLFALFGPAlgmtsVIPDMdptrpatvdpaklfaaIERYGVTNL----FGSPALLERL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 291 ARVDEDDAYDLSKLRIALNGAEPIDETAVQTF---VDAGARfkmpaecVFPAYGMAEAtLAVSfaplftgltldVVEADA 367
Cdd:PRK09274 277 GRYGEANGIKLPSLRRVISAGAPVPIAVIERFramLPPDAE-------ILTPYGATEA-LPIS-----------SIESRE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 368 LEAENRAVPvpegDPRRGTdgvrsfaLLGRPLDGLEAEIVD---------DAGKRVDEREVGEIRLRGEAVTPGYLtmDG 438
Cdd:PRK09274 338 ILFATRAAT----DNGAGI-------CVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRSYY--NR 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300790052 439 PLATQ-----DEDG--WLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSR 509
Cdd:PRK09274 405 PEATRlakipDGQGdvWHRMGDLGYLdAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGAQR 483
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
32-568 |
1.27e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 70.32 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 32 RTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDtvrvlgmigS 111
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD---------S 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 112 DQDALGGPGGLAP--RPGSGAGPRNVTVLL--GEPFDqlapvleqkgiGFQLITELAAAEPlpDVVVTDEGDTALLQLTS 187
Cdd:PRK08276 83 GAKVLIVSAALADtaAELAAELPAGVPLLLvvAGPVP-----------GFRSYEEALAAQP--DTPIADETAGADMLYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 188 GSTADPKAVR--ITYGNLYSNVKAMVERAEFDFDVD---VMVSWLPTFHDMGMVGFLTVpMTFGVELV---KITPVEFLs 259
Cdd:PRK08276 150 GTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGpdsVYLSPAPLYHTAPLRFGMSA-LALGGTVVvmeKFDAEEAL- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 260 gpliwpELITKYHGTTTA-APnfayaIVGRRMARVDED--DAYDLSKLRIALNGAEPIDETAVQTFVD-AGArfkmpaeC 335
Cdd:PRK08276 228 ------ALIERYRVTHSQlVP-----TMFVRMLKLPEEvrARYDVSSLRVAIHAAAPCPVEVKRAMIDwWGP-------I 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 336 VFPAYGMAEATlavsfaplftGLTLdVVEADALEaenravpvpegdpRRGTdgvrsfalLGRPLDGlEAEIVDDAGKRVD 415
Cdd:PRK08276 290 IHEYYASSEGG----------GVTV-ITSEDWLA-------------HPGS--------VGKAVLG-EVRILDEDGNELP 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 416 EREVGEIRLRGEAVTPGYLtmDGPLAT---QDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSV 491
Cdd:PRK08276 337 PGEIGTVYFEMDGYPFEYH--NDPEKTaaaRNPHGWVTVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTH 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 492 EGVrAGNAVAVRLDAGSRRERFAVV--LESKLAGDAEAEKNLmkqVSARVRDAVDMRPYAVVVLPAgsLPKTPSGK-VKR 568
Cdd:PRK08276 415 PKV-ADVAVFGVPDEEMGERVKAVVqpADGADAGDALAAELI---AWLRGRLAHYKCPRSIDFEDE--LPRTPTGKlYKR 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-570 |
1.64e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.14 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDTVRVLGMIGSD 112
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH 2109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 113 -QDALGGPGGLAprpgsgagprnvtVLLGEPFDQLApvleqkgigfqlitELAAAEPLPDvvvTDEGDTALLQLTSGSTA 191
Cdd:PRK12316 2110 lLERLPLPAGVA-------------RLPLDRDAEWA--------------DYPDTAPAVQ---LAGENLAYVIYTSGSTG 2159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 192 DPKAVRITYGNLYSNVKAMVERAEFDfDVDVMVSWLPTFHDmGMVGFLTVPMTFGVELVkitpvefLSGPLIW-PELI-- 268
Cdd:PRK12316 2160 LPKGVAVSHGALVAHCQAAGERYELS-PADCELQFMSFSFD-GAHEQWFHPLLNGARVL-------IRDDELWdPEQLyd 2230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 269 -TKYHGTTTAAPNFAYAivgRRMARVDEDDAYDLsKLRIALNGAEPIDetavQTFVDAGARfKMPAECVFPAYGMAEATL 347
Cdd:PRK12316 2231 eMERHGVTILDFPPVYL---QQLAEHAERDGRPP-AVRVYCFGGEAVP----AASLRLAWE-ALRPVYLFNGYGPTEAVV 2301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 348 AVSfaplftgltldVVEADALEAENRAvpvpegdprrgtdgvrsFALLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGE 427
Cdd:PRK12316 2302 TPL-----------LWKCRPQDPCGAA-----------------YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGE 2353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 428 AVTPGYLTMDGPLATQ------DEDGWL--NTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRagN 498
Cdd:PRK12316 2354 GLARGYLNRPGLTAERfvpdpfSASGERlyRTGDLArYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVR--E 2431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300790052 499 AVAVRLDAGSRRERFAVVLESKLAGDAEAEknLMKQVSARVRDAvdMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:PRK12316 2432 AVVVAQDGASGKQLVAYVVPDDAAEDLLAE--LRAWLAARLPAY--MVPAHWVVLER--LPLNPNGKLDRKA 2497
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
8-459 |
2.57e-12 |
|
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: 69.38 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 8 LVATATKRGQQRGMVTGEPKEPVRR-TWAEVHEEARRIAGGLVAGGFERGTAVGVLAA--------------APVLIAPT 72
Cdd:cd05921 1 LAHWARQAPDRTWLAEREGNGGWRRvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGnsiehalmalaamyAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 73 VQAVWLAGGSVTMLH----QPTPRTDLAEWAEDTVRVLGMIGSDQDALGGPGGLAPrpgsgagprnvtvllGEPFDQLAP 148
Cdd:cd05921 81 SPAYSLMSQDLAKLKhlfeLLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVA---------------GRGAISFAE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 149 VLEQkgigfqliTELAAAEPLPDVVVTDegDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVE-RAEFDFDVDVMVSWL 227
Cdd:cd05921 146 LAAT--------PPTAAVDAAFAAVGPD--TVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQtYPFFGEEPPVLVDWL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 228 P---TF---HDMGMV----GFLTV----PMTFGVE-----LVKITPVEFLSGPLIWPELITKYHGTTTAAPNF------- 281
Cdd:cd05921 216 PwnhTFggnHNFNLVlyngGTLYIddgkPMPGGFEetlrnLREISPTVYFNVPAGWEMLVAALEKDEALRRRFfkrlklm 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 282 AYAivGRRMArvdeDDAYDlsklrialngaePIDETAVQTfvdAGARFKMPAecvfpAYGMAEAtlavsfAPLFTGLTLD 361
Cdd:cd05921 296 FYA--GAGLS----QDVWD------------RLQALAVAT---VGERIPMMA-----GLGATET------APTATFTHWP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 362 VVEAdaleaenravpvpegdprrgtdgvrsfALLGRPLDGLEAEIVDDAGKRvderevgEIRLRGEAVTPGYLtmDGPLA 441
Cdd:cd05921 344 TERS---------------------------GLIGLPAPGTELKLVPSGGKY-------EVRVKGPNVTPGYW--RQPEL 387
|
490 500
....*....|....*....|.
gi 300790052 442 TQ---DEDGWLNTGDLGYLVD 459
Cdd:cd05921 388 TAqafDEEGFYCLGDAAKLAD 408
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
266-570 |
3.37e-12 |
|
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: 69.06 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 266 ELITKYHGTTTAAPNFAYaivgRRMARVDEDDaYDLSKLRIALNGAEPIDETAVQTFVDAGARFKMPAecvfpaYGMAEA 345
Cdd:cd05970 270 EKLSKYGVTTFCAPPTIY----RFLIREDLSR-YDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEG------FGQTET 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 346 TLAVSFAPLFtgltldvveadaleaenravpvpegDPRRGTdgvrsfalLGRPLDGLEAEIVDDAGKRVDEREVGEIRLR 425
Cdd:cd05970 339 TLTIATFPWM-------------------------EPKPGS--------MGKPAPGYEIDLIDREGRSCEAGEEGEIVIR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 426 GEAVTP-----GYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATS----VEGVR 495
Cdd:cd05970 386 TSKGKPvglfgGYYKDAEKTAEVWHDGYYHTGDAAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQhpavLECAV 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300790052 496 AGNAVAVRldaGSRRERFAVvleskLAGDAEAEKNLMKQVSARVRDAVDMRPYAVVVLPAGSLPKTPSGKVKRAA 570
Cdd:cd05970 466 TGVPDPIR---GQVVKATIV-----LAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVE 532
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
395-572 |
4.05e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 68.88 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 LGRPLDGLEAEIVDDAG------KRVDEREVGEIRLRGEAVTPGYltMDGPLATQD--EDGWLNTGDL-GYLVDGQIVIC 465
Cdd:PRK05857 344 VGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGY--WNNPERTAEvlIDGWVNTGDLlERREDGFFYIK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 466 GRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLagDAEAEKNLMKQVSARVRDAVD- 544
Cdd:PRK05857 422 GRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEL--DESAARALKHTIAARFRRESEp 499
|
170 180
....*....|....*....|....*....
gi 300790052 545 -MRPYAVVVLpaGSLPKTPSGKVKRAATA 572
Cdd:PRK05857 500 mARPSTIVIV--TDIPRTQSGKVMRASLA 526
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
15-566 |
4.57e-12 |
|
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: 68.76 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 15 RGQQRGMVTGEPKEPVRRTW--AEVHEEARRIAGGLVAGGFERGTAVGVLAaaPVLiaPTVQAVWLAGGSVTMLHQP--- 89
Cdd:cd17634 66 NGDRTAIIYEGDDTSQSRTIsyRELHREVCRFAGTLLDLGVKKGDRVAIYM--PMI--PEAAVAMLACARIGAVHSVifg 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 90 --TPRTDLAEWAEDTVRVLgmIGSDqdalggpGGLapRPG---------------SGAGPRNVTVLLGEPfdqlAPVLEQ 152
Cdd:cd17634 142 gfAPEAVAGRIIDSSSRLL--ITAD-------GGV--RAGrsvplkknvddalnpNVTSVEHVIVLKRTG----SDIDWQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 153 KGIGFQLITELAAAEPLPDVVVTDEGDTALLQLTSGSTADPK-AVRITYGNLYSNVKAMveRAEFDFDVDVMVSWlptFH 231
Cdd:cd17634 207 EGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKgVLHTTGGYLVYAATTM--KYVFDYGPGDIYWC---TA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 232 DMG-MVGFLTvpMTFGVELVKITPVEFLSGPlIWP------ELITKyHGTTT--AAPNfayAIVGRRMARVDEDDAYDLS 302
Cdd:cd17634 282 DVGwVTGHSY--LLYGPLACGATTLLYEGVP-NWPtparmwQVVDK-HGVNIlyTAPT---AIRALMAAGDDAIEGTDRS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 303 KLRIALNGAEPIDETAVQTFVDAGARFKMPaecVFPAYGMAEATLAVsfAPLFTGltldvveADALEAENRAVPVPegdp 382
Cdd:cd17634 355 SLRILGSVGEPINPEAYEWYWKKIGKEKCP---VVDTWWQTETGGFM--ITPLPG-------AIELKAGSATRPVF---- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 383 rrgtdgvrsfallgrpldGLEAEIVDDAGKRVDEREVGEIRLrGEAVTPGYLTMDGPLATQDE------DGWLNTGDLGY 456
Cdd:cd17634 419 ------------------GVQPAVVDNEGHPQPGGTEGNLVI-TDPWPGQTRTLFGDHERFEQtyfstfKGMYFSGDGAR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 457 L-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLagdaEAEKNLMKQV 535
Cdd:cd17634 480 RdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGV----EPSPELYAEL 555
|
570 580 590
....*....|....*....|....*....|...
gi 300790052 536 SARVRDavDMRPYAV--VVLPAGSLPKTPSGKV 566
Cdd:cd17634 556 RNWVRK--EIGPLATpdVVHWVDSLPKTRSGKI 586
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
153-568 |
5.23e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 68.31 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 153 KGIGFQLITELAAAEPLPDVVVTDEgDTALLQLTSGSTADPKAVRITYGNLYSN---VKAMVER------AEFDFDVDVM 223
Cdd:PRK12492 183 QAVPFKQALRQGRGLSLKPVPVGLD-DIAVLQYTGGTTGLAKGAMLTHGNLVANmlqVRACLSQlgpdgqPLMKEGQEVM 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 224 VSWLPTFHDMGMVGFLTVPMTFGVELVKITPVEFLSGpliWPELITKYHGTTTAAPNFAYaivgrrMARVDEDD--AYDL 301
Cdd:PRK12492 262 IAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPG---FIKELGKWRFSALLGLNTLF------VALMDHPGfkDLDF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 302 SKLRIALNGAepideTAVqtfVDAGA-RFKMPAEC-VFPAYGMAEATLAVSFAPLftgltldvveadaleaENRAvpvpe 379
Cdd:PRK12492 333 SALKLTNSGG-----TAL---VKATAeRWEQLTGCtIVEGYGLTETSPVASTNPY----------------GELA----- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 380 gdpRRGTDGVrsfallgrPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMdgPLATQ---DEDGWLNTGDLGY 456
Cdd:PRK12492 384 ---RLGTVGI--------PVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQ--PEATAealDAEGWFKTGDIAV 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 457 L-VDGQIVICGRRKDVIIMGGRNLYPTDIER-----------AATSVEGVRAGNAV---AVRLDAGSRRERFAVVLESKL 521
Cdd:PRK12492 451 IdPDGFVRIVDRKKDLIIVSGFNVYPNEIEDvvmahpkvancAAIGVPDERSGEAVklfVVARDPGLSVEELKAYCKENF 530
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 300790052 522 AGdaeaeKNLMKQVSARvrdavdmrpyavvvlpaGSLPKTPSGKVKR 568
Cdd:PRK12492 531 TG-----YKVPKHIVLR-----------------DSLPMTPVGKILR 555
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
179-517 |
1.02e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 67.81 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGM-VGFLTVPMTfGVELvkitpveF 257
Cdd:PRK08043 366 DAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPN-DRFMSALPLFHSFGLtVGLFTPLLT-GAEV-------F 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 258 L-SGPL---IWPELI-----TKYHGTTTAAPNFAyaivgrRMArvdedDAYDLSKLRIALNGAEPIDETAVQTFVDA-GA 327
Cdd:PRK08043 437 LyPSPLhyrIVPELVydrncTVLFGTSTFLGNYA------RFA-----NPYDFARLRYVVAGAEKLQESTKQLWQDKfGL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 328 RfkmpaecVFPAYGMAEAtlavsfAPlftgltldVVeadaleaenrAVPVPEGdPRRGTdgvrsfalLGRPLDGLEAEIV 407
Cdd:PRK08043 506 R-------ILEGYGVTEC------AP--------VV----------SINVPMA-AKPGT--------VGRILPGMDARLL 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 408 DDAGKrvdeREVGEIRLRGEAVTPGYLTMDGP----------LATQDEDGWLNTGDLGYLVD-GQIVICGRRKDVIIMGG 476
Cdd:PRK08043 546 SVPGI----EQGGRLQLKGPNIMNGYLRVEKPgvlevptaenARGEMERGWYDTGDIVRFDEqGFVQIQGRAKRFAKIAG 621
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 300790052 477 RNLYPTDIERAATSVEGvRAGNAVAVRLDAgSRRErfAVVL 517
Cdd:PRK08043 622 EMVSLEMVEQLALGVSP-DKQHATAIKSDA-SKGE--ALVL 658
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
175-568 |
1.06e-11 |
|
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: 67.14 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 175 TDEGDTALLQLTSGSTADPKAVRITYGNLYSnvKAMVERAEFDFDVDVMV------SWLptfhdMGMVGFLTVPMTFGVE 248
Cdd:cd05969 86 TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIF--YYFTGKYVLDLHPDDIYwctadpGWV-----TGTVYGIWAPWLNGVT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 249 LVkITPVEFlsGPLIWPELITKYHGTT--TAAPNFayaivgRRMARVDED--DAYDLSKLRIALNGAEPIDETAVQTFVD 324
Cdd:cd05969 159 NV-VYEGRF--DAESWYGIIERVKVTVwyTAPTAI------RMLMKEGDElaRKYDLSSLRFIHSVGEPLNPEAIRWGME 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 325 AgarFKMPaecVFPAYGMAE-ATLAVSFAPlftgltldvveadaleaenrAVPVPEGDprrgtdgvrsfalLGRPLDGLE 403
Cdd:cd05969 230 V---FGVP---IHDTWWQTEtGSIMIANYP--------------------CMPIKPGS-------------MGKPLPGVK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 404 AEIVDDAGKRVDEREVGEIRLRGE--AVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLY 480
Cdd:cd05969 271 AAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRdEDGYFWFVGRADDIIKTSGHRVG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 481 PTDIERAATSVEGVrAGNAVAVRLDAgSRRERFA--VVLESKLAGDAEAEKNLMKQVSARVRDAVDMRPYAVVvlpaGSL 558
Cdd:cd05969 351 PFEVESALMEHPAV-AEAGVIGKPDP-LRGEIIKafISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFV----DNL 424
|
410
....*....|
gi 300790052 559 PKTPSGKVKR 568
Cdd:cd05969 425 PKTRSGKIMR 434
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-570 |
1.17e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 68.26 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 30 VRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDtvrvlgmi 109
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIED-------- 3190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 110 gsdqdalggpgglaprpgSGagprnVTVLLGEpfdqlAPVLEQKGI---GFQLITELAAAEPLPD---VVVTDEGDTALL 183
Cdd:PRK12467 3191 ------------------SG-----VKLLLTQ-----AHLLEQLPApagDTALTLDRLDLNGYSEnnpSTRVMGENLAYV 3242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 184 QLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLTVPMTfGVELVkITPVEFLSGPLI 263
Cdd:PRK12467 3243 IYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAN-DRVLLFMSFSFDGAQERFLWTLIC-GGCLV-VRDNDLWDPEEL 3319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 264 WPELitKYHGTTTAapNFAYAIVgrrMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFvdagaRFKMPAECVFPAYGMA 343
Cdd:PRK12467 3320 WQAI--HAHRISIA--CFPPAYL---QQFAEDAGGADCASLDIYVFGGEAVPPAAFEQV-----KRKLKPRGLTNGYGPT 3387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 344 EATLAVsfaplftglTLDVVEADAlEAENRAVPVpegdprrgtdgvrsfallGRPLDGLEAEIVDDAGKRVDEREVGEIR 423
Cdd:PRK12467 3388 EAVVTV---------TLWKCGGDA-VCEAPYAPI------------------GRPVAGRSIYVLDGQLNPVPVGVAGELY 3439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 424 LRGEAVTPGY-----LTMDGPLAT--QDEDGWL-NTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGV 494
Cdd:PRK12467 3440 IGGVGLARGYhqrpsLTAERFVADpfSGSGGRLyRTGDLArYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV 3519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300790052 495 RagNAVAVRLDAGSRRERFAVVLESKLAGDAEAEknLMKQVSARVRDAvdMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:PRK12467 3520 R--EAVVLARDGAGGKQLVAYVVPADPQGDWRET--LRDHLAASLPDY--MVPAQLLVLAA--MPLGPNGKVDRKA 3587
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
396-568 |
1.99e-11 |
|
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: 66.39 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVT----PGYLTMDGPLAtqdEDGWLNTGDLGYL-VDGQIVICGRRKD 470
Cdd:cd05973 262 GRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPAI---DGGYYLTGDTVEFdPDGSFSFIGRADD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 471 VIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVrdAVDMRPYAV 550
Cdd:cd05973 339 VITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRL--SAHAYPRTI 416
|
170
....*....|....*...
gi 300790052 551 VVLPAgsLPKTPSGKVKR 568
Cdd:cd05973 417 HFVDE--LPKTPSGKIQR 432
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
117-485 |
4.47e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 65.51 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 117 GGPGGLAPRPGSGAGPRNVTvllgepFDQLapvlEQKGIgfqlITELAAAEPLPDvvvtdegDTALLQLTSGSTADPKAV 196
Cdd:PLN02736 181 GGADEPLPSLPSGTGVEIVT------YSKL----LAQGR----SSPQPFRPPKPE-------DVATICYTSGTTGTPKGV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 197 RITYGNLYSNVKAMVERAEFdFDVDVMVSWLPTFHDMGMVGFLtVPMTFGV--------------ELVKITPVEFLSGPL 262
Cdd:PLN02736 240 VLTHGNLIANVAGSSLSTKF-YPSDVHISYLPLAHIYERVNQI-VMLHYGVavgfyqgdnlklmdDLAALRPTIFCSVPR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 263 IWPELITKYHGTTTAAPN-----FAYAIVGRRMARVDED------DAYDLSKL--------RIALNGAEPIDETaVQTF- 322
Cdd:PLN02736 318 LYNRIYDGITNAVKESGGlkerlFNAAYNAKKQALENGKnpspmwDRLVFNKIkaklggrvRFMSSGASPLSPD-VMEFl 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 323 -VDAGARfkmpaecVFPAYGMAEATLAVSfaplftglTLDvveadaleaenravpvpEGDprrgtdgvRSFALLGRPLDG 401
Cdd:PLN02736 397 rICFGGR-------VLEGYGMTETSCVIS--------GMD-----------------EGD--------NLSGHVGSPNPA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 402 LEAEIVDdagkrVDEREV---------GEIRLRGEAVTPGYLTMDgpLATQ---DEDGWLNTGDLG-YLVDGQIVICGRR 468
Cdd:PLN02736 437 CEVKLVD-----VPEMNYtsedqpyprGEICVRGPIIFKGYYKDE--VQTReviDEDGWLHTGDIGlWLPGGRLKIIDRK 509
|
410
....*....|....*...
gi 300790052 469 KDVIIMG-GRNLYPTDIE 485
Cdd:PLN02736 510 KNIFKLAqGEYIAPEKIE 527
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
139-576 |
4.95e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 65.45 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 139 LGEPFDQLAPVLEQKGIgFQLITELAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLY----SNVKAMVERA 214
Cdd:PRK06178 171 LPLPDSLRAPRLAAAGA-IDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVytaaAAYAVAVVGG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 215 EfdfdVDVMVSWLPTF----HDMGMVgfltVPMTFGVELVKIT---PVEFLsgpliwpELITKYHGTTTAAP--NFAYAI 285
Cdd:PRK06178 250 E----DSVFLSFLPEFwiagENFGLL----FPLFSGATLVLLArwdAVAFM-------AAVERYRVTRTVMLvdNAVELM 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 286 VGRRMARvdeddaYDLSKLRialngaepidETAVQTFV-----DAGARFKMPAECVF--PAYGMAEATLAVSFAPLFTGL 358
Cdd:PRK06178 315 DHPRFAE------YDLSSLR----------QVRVVSFVkklnpDYRQRWRALTGSVLaeAAWGMTETHTCDTFTAGFQDD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 359 TLDVveadaleaenRAVPVpegdprrgtdgvrsfaLLGRPLDGLEAEIVD-DAGKRVDEREVGEIRLRGEAVTPGYltMD 437
Cdd:PRK06178 379 DFDL----------LSQPV----------------FVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGY--WN 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 438 GPLATQD--EDGWLNTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVrAGNAVAVRLDAGSRRERFA 514
Cdd:PRK06178 431 KPEATAEalRDGWLHTGDIGkIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAV-LGSAVVGRPDPDKGQVPVA 509
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300790052 515 -VVLESKLAGDAEAeknlmkqVSARVRDAvdMRPYAV---VVLPAgsLPKTPSGKVKRAATAQQFA 576
Cdd:PRK06178 510 fVQLKPGADLTAAA-------LQAWCREN--MAVYKVpeiRIVDA--LPMTATGKVRKQDLQALAE 564
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
396-495 |
6.00e-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: 63.86 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLG-YLVDGQIVICGRRKDVIIM 474
Cdd:cd17636 166 GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGrREPDGSLSFVGPKTRMIKS 245
|
90 100
....*....|....*....|.
gi 300790052 475 GGRNLYPTDIERAATSVEGVR 495
Cdd:cd17636 246 GAENIYPAEVERCLRQHPAVA 266
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-573 |
7.49e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.75 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDT-VRVLGMIGS 111
Cdd:PRK12316 4578 TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSgAALLLTQSH 4657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 112 DQDALGGPGGLAprpgsgagprnvtvllgepfdqlAPVLEQKGI--GFqlitelAAAEPLpdvVVTDEGDTALLQLTSGS 189
Cdd:PRK12316 4658 LLQRLPIPDGLA-----------------------SLALDRDEDweGF------PAHDPA---VRLHPDNLAYVIYTSGS 4705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 190 TADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVswLPTFHDMGMVGFLTVPMTFGVELVkitpvefLSGPLIW-PE-- 266
Cdd:PRK12316 4706 TGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQ--FMSFSFDGSHEGLYHPLINGASVV-------IRDDSLWdPErl 4776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 267 --LITKYHGTTTAAPNFAYaivgRRMARVDEDDAyDLSKLRIALNGAEpidetAVQTFVDAGARFKMPAECVFPAYGMAE 344
Cdd:PRK12316 4777 yaEIHEHRVTVLVFPPVYL----QQLAEHAERDG-EPPSLRVYCFGGE-----AVAQASYDLAWRALKPVYLFNGYGPTE 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 345 ATLAVsfaplftgLTLDVveadaleaenravpvpegdpRRGTDGVRSFALLGRPLDGLEAEIVDDAGKRVDEREVGEIRL 424
Cdd:PRK12316 4847 TTVTV--------LLWKA--------------------RDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYL 4898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 425 RGEAVTPGYLTMDGPLATQ------DEDG--WLNTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVR 495
Cdd:PRK12316 4899 GGEGVARGYLERPALTAERfvpdpfGAPGgrLYRTGDLArYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVR 4978
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 496 AGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVRDAVD--MRPYAVVVLpaGSLPKTPSGKVKRAATAQ 573
Cdd:PRK12316 4979 EAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPeyMVPAHLVFL--ARMPLTPNGKLDRKALPQ 5056
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
3-568 |
8.16e-11 |
|
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: 64.45 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 3 RFVDTLVATATKRGQQRGMVTgEPKEPVRRTWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGS 82
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIA-DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 83 VTMLH---QPTPRTDLAEWAEDTVRVLGMIGSDQDALGGPGG----LAPRPGSGagprnvtvllgepfdqlapvleqkgi 155
Cdd:cd05923 80 PALINprlKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVrvlaLSDLVGLG-------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 156 gfqlitELAAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDF-DVDVMVSWLPTFHDMG 234
Cdd:cd05923 134 ------EPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHgRHNVVLGLMPLYHVIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 235 MVGFLTVPMTFGVELVKIT---PVEFLSgpLIWPELITKYHGTTTAAPNFAYAIvgrrmarvdEDDAYDLSKLR-IALNG 310
Cdd:cd05923 208 FFAVLVAALALDGTYVVVEefdPADALK--LIEQERVTSLFATPTHLDALAAAA---------EFAGLKLSSLRhVTFAG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 311 AepideTAVQTFVDAGARFKmPAECVfPAYGMAEAtLAVSFAPlftgltldvveadaleaenravpvpegDPRRGTDG-- 388
Cdd:cd05923 277 A-----TMPDAVLERVNQHL-PGEKV-NIYGTTEA-MNSLYMR---------------------------DARTGTEMrp 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 389 -----VRSFALLGRPL----DGLEAEIVDDAGkrvderevgeirlrGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-V 458
Cdd:cd05923 322 gffseVRIVRIGGSPDealaNGEEGELIVAAA--------------ADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVdP 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 459 DGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRagnAVAVrldAGSRRERFA-VVLESKLAGDAEAEKNLMKQVSA 537
Cdd:cd05923 388 SGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVT---EVVV---IGVADERWGqSVTACVVPREGTLSADELDQFCR 461
|
570 580 590
....*....|....*....|....*....|.
gi 300790052 538 RVRDAVDMRPYAVVVLPAgsLPKTPSGKVKR 568
Cdd:cd05923 462 ASELADFKRPRRYFFLDE--LPKNAMNKVLR 490
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
162-459 |
1.00e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 64.51 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 162 ELAAAEPLPDVV----VTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMveRAEFDFDVD---VMVSWLP---TF- 230
Cdd:PRK08180 189 ALLATPPTAAVDaahaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQML--AQTFPFLAEeppVLVDWLPwnhTFg 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 231 --HDMGMV----GFLTV----PMTFGVE-----LVKITPVEFLSGPLIWPELITkyhgtttaapnfayaivgrrMARVDE 295
Cdd:PRK08180 267 gnHNLGIVlyngGTLYIddgkPTPGGFDetlrnLREISPTVYFNVPKGWEMLVP--------------------ALERDA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 296 DDAYDL-SKLRIALNGA--------EPIDETAVQTfvdAGARFKMPAecvfpAYGMAEAtlavsfAPLFTGLTldvvead 366
Cdd:PRK08180 327 ALRRRFfSRLKLLFYAGaalsqdvwDRLDRVAEAT---CGERIRMMT-----GLGMTET------APSATFTT------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 367 alEAENRAvpvpegdprrgtdgvrsfALLGRPLDGLEAEIVDDAGKRvderevgEIRLRGEAVTPGYLtmDGPLATQ--- 443
Cdd:PRK08180 386 --GPLSRA------------------GNIGLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPGYW--RAPELTAeaf 436
|
330
....*....|....*.
gi 300790052 444 DEDGWLNTGDLGYLVD 459
Cdd:PRK08180 437 DEEGYYRSGDAVRFVD 452
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
179-573 |
1.27e-10 |
|
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: 63.87 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYSNVKAMVER------------AEFDFDVDVmvswlptfhdmGMVgFLTvpMTFG 246
Cdd:cd17653 106 DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARldvgpgsrvaqvLSIAFDACI-----------GEI-FST--LCNG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 247 VELVKITPveflSGPliWPELITKYHgTTTAAPNFayaivgrrMARVDEDDaydLSKLRIALNGAEPIDetavQTFVDAG 326
Cdd:cd17653 172 GTLVLADP----SDP--FAHVARTVD-ALMSTPSI--------LSTLSPQD---FPNLKTIFLGGEAVP----PSLLDRW 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 327 ArfkmPAECVFPAYGMAEATLAVSFAplftgltldvveadALEAENRAVpvpegdprrgtdgvrsfalLGRPLDGLEAEI 406
Cdd:cd17653 230 S----PGRRLYNAYGPTECTISSTMT--------------ELLPGQPVT-------------------IGKPIPNSTCYI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 407 VDDAGKRVDEREVGEIRLRGEAVTPGYL-----TMDGPLATQDEDGWL--NTGDLGYLV-DGQIVICGRRKDVI-IMGGR 477
Cdd:cd17653 273 LDADLQPVPEGVVGEICISGVQVARGYLgnpalTASKFVPDPFWPGSRmyRTGDYGRWTeDGGLEFLGREDNQVkVRGFR 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 478 -NLYpTDIERAATSVEGVRAGNAVAV--RLDAgsrrerFAVVLESKLAGDAEAEKNLMKQVsarvrdavdMRPYAVVVLP 554
Cdd:cd17653 353 iNLE-EIEEVVLQSQPEVTQAAAIVVngRLVA------FVTPETVDVDGLRSELAKHLPSY---------AVPDRIIALD 416
|
410
....*....|....*....
gi 300790052 555 agSLPKTPSGKVKRAATAQ 573
Cdd:cd17653 417 --SFPLTANGKVDRKALRE 433
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
404-568 |
2.59e-10 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 62.47 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 404 AEIVD-DAGKRVDEREVGEIrlrgeAVTPgyLTMDG-PLatqdedgwL--NTGDLGYLVDGQ---------IV-ICGRRK 469
Cdd:COG1541 263 VEIIDpETGEPVPEGEEGEL-----VVTT--LTKEAmPL--------IryRTGDLTRLLPEPcpcgrthprIGrILGRAD 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 470 DVIIMGGRNLYPTDIERAATSVEGVrAGNAVAVrLDAGSRRERFAVVLEskLAGDAEAEKnLMKQVSARVRDAVDMRPyA 549
Cdd:COG1541 328 DMLIIRGVNVFPSQIEEVLLRIPEV-GPEYQIV-VDREGGLDELTVRVE--LAPGASLEA-LAEAIAAALKAVLGLRA-E 401
|
170
....*....|....*....
gi 300790052 550 VVVLPAGSLPKTPsGKVKR 568
Cdd:COG1541 402 VELVEPGSLPRSE-GKAKR 419
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
142-487 |
4.87e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 61.81 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 142 PFDQLAPVLEQKGIGFQLITELAAAEPLPDVVVTDEGDT-----------ALLQLTSGSTADPKAVRITYGNLYSNVKAM 210
Cdd:PRK09029 88 PQPLLEELLPSLTLDFALVLEGENTFSALTSLHLQLVEGahavawqpqrlATMTLTSGSTGLPKAAVHTAQAHLASAEGV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 211 VEraEFDFDVDVmvSWL---PTFHDMGMvGFLTVPMTFGVELVKITPVEFLSGpliwpelitkYHGTTTAApnfayaIVG 287
Cdd:PRK09029 168 LS--LMPFTAQD--SWLlslPLFHVSGQ-GIVWRWLYAGATLVVRDKQPLEQA----------LAGCTHAS------LVP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 288 RRMARVDEDDAYDLSKLRIALNGAEPIDETAVQtfvdagARfKMPAECvFPAYGMAEAtlavsfaplftGLTLDVVEADa 367
Cdd:PRK09029 227 TQLWRLLDNRSEPLSLKAVLLGGAAIPVELTEQ------AE-QQGIRC-WCGYGLTEM-----------ASTVCAKRAD- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 368 leaenravpvpegdprrGTDGVrsfallGRPLDGLEAEIVDDagkrvderevgEIRLRGEAVTPGYLtMDG---PLAtqD 444
Cdd:PRK09029 287 -----------------GLAGV------GSPLPGREVKLVDG-----------EIWLRGASLALGYW-RQGqlvPLV--N 329
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 300790052 445 EDGWLNTGDLGYLVDGQIVICGRRKDVIIMGGRNLYPTDIERA 487
Cdd:PRK09029 330 DEGWFATRDRGEWQNGELTILGRLDNLFFSGGEGIQPEEIERV 372
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
15-577 |
7.82e-10 |
|
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: 61.56 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 15 RGQQRGMVTGEPKEPVRR--TWAEVHEEARRIAGGLVAGGFERG------------TAVGVLAAAPVliaPTVQAVWLAG 80
Cdd:cd05967 64 RGDQIALIYDSPVTGTERtyTYAELLDEVSRLAGVLRKLGVVKGdrviiympmipeAAIAMLACARI---GAIHSVVFGG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 81 GSVTMLHQptpRTDLAEwaedTVRVLGmigsdqdALGG--PGGLAP-RP-------GSGAGPRNVTVLlgePFDQLAPVL 150
Cdd:cd05967 141 FAAKELAS---RIDDAK----PKLIVT-------ASCGiePGKVVPyKPlldkaleLSGHKPHHVLVL---NRPQVPADL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 151 EQKGIGFQLITELAAAEPLPDVVVtDEGDTALLQLTSGSTADPKAV-RITYGNLysnvkamveraefdfdvdVMVSW-LP 228
Cdd:cd05967 204 TKPGRDLDWSELLAKAEPVDCVPV-AATDPLYILYTSGTTGKPKGVvRDNGGHA------------------VALNWsMR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 229 TFHDM--GMVGFLTVPM---------TFGVELVKITPVEFLSGPLIWPE------LITKyHGTTT--AAPNfayAIvgRR 289
Cdd:cd05967 265 NIYGIkpGDVWWAASDVgwvvghsyiVYGPLLHGATTVLYEGKPVGTPDpgafwrVIEK-YQVNAlfTAPT---AI--RA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 290 MARVDEDDA----YDLSKLRIALNGAEPIDetaVQTFVDAGARFKMPaecVFPAYGMAEATLAVSFAPLftGLTLdvvea 365
Cdd:cd05967 339 IRKEDPDGKyikkYDLSSLRTLFLAGERLD---PPTLEWAENTLGVP---VIDHWWQTETGWPITANPV--GLEP----- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 366 daleaenraVPVPEGDPrrgtdgvrsfallGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGeAVTPGYLTMdgpLATQDE 445
Cdd:cd05967 406 ---------LPIKAGSP-------------GKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLT---LWKNDE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 446 ----------DGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFA 514
Cdd:cd05967 460 rfkklylskfPGYYDTGDAGYKdEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGL 539
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300790052 515 VVLEsklAGDAEAEKNLMKQVSARVRDAVD--MRPYAVVVLpaGSLPKTPSGKVKRaATAQQFAD 577
Cdd:cd05967 540 VVLK---EGVKITAEELEKELVALVREQIGpvAAFRLVIFV--KRLPKTRSGKILR-RTLRKIAD 598
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
418-539 |
1.37e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 60.91 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 418 EVGEIRLRGEAVTPGYLtmDGPLATQD---EDGWLNTGDLGYLV-DGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEG 493
Cdd:PRK06164 376 ESGEIEIRAPSLMRGYL--DNPDATARaltDDGYFRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPG 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 300790052 494 VRAGNAVAVRLDAGSRRERFaVVLESKLAGDAEAEKNLMKQ------VSARV 539
Cdd:PRK06164 454 VAAAQVVGATRDGKTVPVAF-VIPTDGASPDEAGLMAACREalagfkVPARV 504
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
172-570 |
1.95e-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: 60.14 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 172 VVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVER------------AEFDFDV---DVMVSWLPtfhdmgmv 236
Cdd:cd17644 100 VLLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEygitssdrvlqfASIAFDVaaeEIYVTLLS-------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 237 gfltvpmtfGVELVKITPVEFLSGPLIWP----ELITKYHGTTTAAPNFAYAIVgrrmarvdEDDAYDLSKLRIALNGAE 312
Cdd:cd17644 172 ---------GATLVLRPEEMRSSLEDFVQyiqqWQLTVLSLPPAYWHLLVLELL--------LSTIDLPSSLRLVIVGGE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 313 PIDETAVQTFVDAGARFkmpAECvFPAYGMAEATLAVSFAplftgltldvveadaleaenravpvpegDPRRGTDGVRSF 392
Cdd:cd17644 235 AVQPELVRQWQKNVGNF---IQL-INVYGPTEATIAATVC----------------------------RLTQLTERNITS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 393 ALLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMD---------GPLATQDEDGWLNTGDLG-YLVDGQI 462
Cdd:cd17644 283 VPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPeltaekfisHPFNSSESERLYKTGDLArYLPDGNI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 463 VICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAgNAVAVRLD-AGSRRERFAVVLESKLAGDAEAEKNLMKQvsarvRD 541
Cdd:cd17644 363 EYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT-AVVIVREDqPGNKRLVAYIVPHYEESPSTVELRQFLKA-----KL 436
|
410 420
....*....|....*....|....*....
gi 300790052 542 AVDMRPYAVVVLPagSLPKTPSGKVKRAA 570
Cdd:cd17644 437 PDYMIPSAFVVLE--ELPLTPNGKIDRRA 463
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
172-577 |
2.94e-09 |
|
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: 59.48 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 172 VVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFD------------FDVDVMVSWLpTFHDMGMV--- 236
Cdd:cd05918 100 VLTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTsesrvlqfasytFDVSILEIFT-TLAAGGCLcip 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 237 ----------GFLTvpmTFGVELVKITPveflsgpliwpelitkyhgtttaapnfayaivgrRMARVDEDDayDLSKLRI 306
Cdd:cd05918 179 seedrlndlaGFIN---RLRVTWAFLTP----------------------------------SVARLLDPE--DVPSLRT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 307 ALNGAEPIDETAVQTFVDaGARfkmpaecVFPAYGMAEATLAVSFAPlftgltldvveadaleaenravPVPEGDPRrgt 386
Cdd:cd05918 220 LVLGGEALTQSDVDTWAD-RVR-------LINAYGPAECTIAATVSP----------------------VVPSTDPR--- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 387 dgvrsfaLLGRPLDGLeAEIVD--DAGKRVDEREVGEIRLRGEAVTPGYL---------TMDGPLATQDEDGWLN----- 450
Cdd:cd05918 267 -------NIGRPLGAT-CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLndpektaaaFIEDPAWLKQEGSGRGrrlyr 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 451 TGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERA-ATSVEGVRAGNAVAVRLDAGSRRERFAVVL----------- 517
Cdd:cd05918 339 TGDLVrYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHlRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVvldgsssgsgd 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300790052 518 -ESKLAGDAEAEKNLMKQVSARVRDAV--DMRPYAVVVLPagSLPKTPSGKVKRAATAQQFAD 577
Cdd:cd05918 419 gDSLFLEPSDEFRALVAELRSKLRQRLpsYMVPSVFLPLS--HLPLTASGKIDRRALRELAES 479
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
172-566 |
6.18e-09 |
|
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: 58.57 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 172 VVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVER----AEFDFDVDVMVSWLPTFHdmgmVGFLTVPMTFGV 247
Cdd:cd17648 88 VVITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERyfgrDNGDEAVLFFSNYVFDFF----VEQMTLALLNGQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 248 ELVkITPVEFLSGPLIWPELI-----TKYHGTTTAAPNFAYAIVG--RRMARVDED-DAYDLSKLRialngaepidetav 319
Cdd:cd17648 164 KLV-VPPDEMRFDPDRFYAYInrekvTYLSGTPSVLQQYDLARLPhlKRVDAAGEEfTAPVFEKLR-------------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 320 qtfvdagARFKMPaecVFPAYGMAEATLAvsfaplftgltldvveadaleaeNRAVPVPEGDPRRGTdgvrsfalLGRPL 399
Cdd:cd17648 229 -------SRFAGL---IINAYGPTETTVT-----------------------NHKRFFPGDQRFDKS--------LGRPV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 400 DGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMD---------GPLATQDE--DG----WLNTGDLG-YLVDGQIV 463
Cdd:cd17648 268 RNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPeltaerflpNPFQTEQEraRGrnarLYKTGDLVrWLPSGELE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 464 ICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGnAVAVRLDAGSRRERFAVVLESKLAGDAEA--EKNLMKQVSARVRD 541
Cdd:cd17648 348 YLGRNDFQVKIRGQRIEPGEVEAALASYPGVREC-AVVAKEDASQAQSRIQKYLVGYYLPEPGHvpESDLLSFLRAKLPR 426
|
410 420
....*....|....*....|....*
gi 300790052 542 AvdMRPYAVVVLPagSLPKTPSGKV 566
Cdd:cd17648 427 Y--MVPARLVRLE--GIPVTINGKL 447
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
396-577 |
7.70e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 58.18 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGKRV--DEREVGEIRLRGEAVTPGYLTMDG-PLAtqdeDGWLNTGDLGYL-VDGQIVICGRRKDV 471
Cdd:PRK07008 359 GRVIYGVDMKIVGDDGRELpwDGKAFGDLQVRGPWVIDRYFRGDAsPLV----DGWFPTGDVATIdADGFMQITDRSKDV 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 472 IIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVlesKLAGDAEAEKNLMKQVSARVrdAVDMRPYAVV 551
Cdd:PRK07008 435 IKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVV---KRPGAEVTREELLAFYEGKV--AKWWIPDDVV 509
|
170 180
....*....|....*....|....*.
gi 300790052 552 VLPAgsLPKTPSGKVKRAATAQQFAD 577
Cdd:PRK07008 510 FVDA--IPHTATGKLQKLKLREQFRD 533
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
175-469 |
9.74e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 58.06 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 175 TDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVER-----AEFDFDvDVMVSWLPTFHDM------------GMVG 237
Cdd:PTZ00216 261 ENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRlndliGPPEED-ETYCSYLPLAHIMefgvtniflargALIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 238 FLTvPMTF--------GvELVKITPVEFLSGPLIWpELITKYHGTTTAAPN------FAYAIVGRRMARVDEDDA----- 298
Cdd:PTZ00216 340 FGS-PRTLtdtfarphG-DLTEFRPVFLIGVPRIF-DTIKKAVEAKLPPVGslkrrvFDHAYQSRLRALKEGKDTpywne 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 299 --YDL------SKLRIALNGAEPIDEtAVQTFVDAgaRFKMpaecVFPAYGMAEaTLAVSFAPLFTGLTLDVVeadalea 370
Cdd:PTZ00216 417 kvFSApravlgGRVRAMLSGGGPLSA-ATQEFVNV--VFGM----VIQGWGLTE-TVCCGGIQRTGDLEPNAV------- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 371 enravpvpegdprrgtdgvrsfallGRPLDGLEAEIVD-DAGKRVDEREV-GEIRLRGEAVTPGYLTMdgPLATQ---DE 445
Cdd:PTZ00216 482 -------------------------GQLLKGVEMKLLDtEEYKHTDTPEPrGEILLRGPFLFKGYYKQ--EELTRevlDE 534
|
330 340
....*....|....*....|....*
gi 300790052 446 DGWLNTGDLGYL-VDGQIVICGRRK 469
Cdd:PTZ00216 535 DGWFHTGDVGSIaANGTLRIIGRVK 559
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
164-485 |
1.07e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 57.78 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 164 AAAEPLPDVVVTDEGDTALLQLTSGSTADPKAVritYGNLYSnvkamveraefdfdvdvmvswLPTFHDMGMVGFLTVPM 243
Cdd:PRK13391 140 EAVAGLPATPIADESLGTDMLYSSGTTGRPKGI---KRPLPE---------------------QPPDTPLPLTAFLQRLW 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 244 TFGVELVKITPVE-FLSGPLIWPELITKYHGTTTAAPNF----AYAIVGR--------------RMARVDED--DAYDLS 302
Cdd:PRK13391 196 GFRSDMVYLSPAPlYHSAPQRAVMLVIRLGGTVIVMEHFdaeqYLALIEEygvthtqlvptmfsRMLKLPEEvrDKYDLS 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 303 KLRIALNGAEPIDETAVQTFVDagarFKMPAecVFPAYGMAEATLavsfaplFTGLTldvvEADALEaenravpvpegdp 382
Cdd:PRK13391 276 SLEVAIHAAAPCPPQVKEQMID----WWGPI--IHEYYAATEGLG-------FTACD----SEEWLA------------- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 383 RRGTdgvrsfalLGRPLDGlEAEIVDDAGKRVDEREVGEIRLRGEavTP-GYLTMDGPLA-TQDEDG-WLNTGDLGYL-V 458
Cdd:PRK13391 326 HPGT--------VGRAMFG-DLHILDDDGAELPPGEPGTIWFEGG--RPfEYLNDPAKTAeARHPDGtWSTVGDIGYVdE 394
|
330 340
....*....|....*....|....*..
gi 300790052 459 DGQIVICGRRKDVIIMGGRNLYPTDIE 485
Cdd:PRK13391 395 DGYLYLTDRAAFMIISGGVNIYPQEAE 421
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
163-566 |
3.87e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 163 LAAAEPlpdvVVTDEGDTALLQLTSGSTADPKAVRitygnlysnvKAMVERaEFDFDVDVMVSWLPTFHDMGM--VGFLT 240
Cdd:PRK13390 137 LAGAGP----RLTEQPCGAVMLYSSGTTGFPKGIQ----------PDLPGR-DVDAPGDPIVAIARAFYDISEsdIYYSS 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 241 VPMtfgvelvkitpveFLSGPLIWPELITKYHGTTTAAPNF-AYAIVGR-----------------RMARVDED--DAYD 300
Cdd:PRK13390 202 API-------------YHAAPLRWCSMVHALGGTVVLAKRFdAQATLGHveryritvtqmvptmfvRLLKLDADvrTRYD 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 301 LSKLRIALNGAEPIDETAVQTFVDagarfkMPAECVFPAYGMAEATlavsfaplftGLTLdvveadaleaenraVPVPEG 380
Cdd:PRK13390 269 VSSLRAVIHAAAPCPVDVKHAMID------WLGPIVYEYYSSTEAH----------GMTF--------------IDSPDW 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 381 DPRRGTdgvrsfalLGRPLDGlEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDG---WLNTGDLGYL 457
Cdd:PRK13390 319 LAHPGS--------VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 458 -VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVS 536
Cdd:PRK13390 390 dEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTR 469
|
410 420 430
....*....|....*....|....*....|
gi 300790052 537 ARVRDAVDMRPYAVVvlpaGSLPKTPSGKV 566
Cdd:PRK13390 470 SRIAHYKAPRSVEFV----DELPRTPTGKL 495
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
396-578 |
1.06e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 54.28 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDdagkrvderevGEIRLRGEAVTPGY--LTMDGPLAtqdEDGWLNTGDLGYLVDGQIVICGRRKDVII 473
Cdd:PRK07824 195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYrnPVDPDPFA---EPGWFRTDDLGALDDGVLTVLGRADDAIS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 474 MGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLEsklAGDAEAEKNLMKQVSARVRDAVDMRPYAVVvl 553
Cdd:PRK07824 261 TGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGD---GGPAPTLEALRAHVARTLDRTAAPRELHVV-- 335
|
170 180
....*....|....*....|....*
gi 300790052 554 paGSLPKTPSGKVKRAATAQQFADR 578
Cdd:PRK07824 336 --DELPRRGIGKVDRRALVRRFAGE 358
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
158-502 |
1.19e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 54.65 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 158 QLITELAAAEPLPDVvvtDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVG 237
Cdd:PRK13388 133 ELVAAAGALTPHREV---DAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRD-DVCYVSMPLFHSNAVMA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 238 FLTVPMTFGVELV---KITPVEFLSGpliwpelITKYHGTTtaapnFAYaiVGRRMA-------RVDEDDaydlSKLRIA 307
Cdd:PRK13388 209 GWAPAVASGAAVAlpaKFSASGFLDD-------VRRYGATY-----FNY--VGKPLAyilatpeRPDDAD----NPLRVA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 308 L-NGAEPIDETA-VQTFvdaGARfkmpaecVFPAYGMAEATLAVSFAPLFtgltldvveadaleaenravpvPEGDPRRG 385
Cdd:PRK13388 271 FgNEASPRDIAEfSRRF---GCQ-------VEDGYGSSEGAVIVVREPGT----------------------PPGSIGRG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 386 TDGVR-------------SFALLGRPLDGLEA--EIVDDAGKRVDErevgeirlrgeavtpGYLTMDGPLATQDEDGWLN 450
Cdd:PRK13388 319 APGVAiynpetltecavaRFDAHGALLNADEAigELVNTAGAGFFE---------------GYYNNPEATAERMRHGMYW 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 300790052 451 TGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVragNAVAV 502
Cdd:PRK13388 384 SGDLAYRdADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI---NRVAV 433
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
396-494 |
1.52e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 54.40 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAgkRVDE---REVGEIRLRGEAVTPGYL-----TMDGPLATQD------------EDGWLNTGDLG 455
Cdd:PRK05620 361 GRFPASLEYRIVNDG--QVMEstdRNEGEIQVRGNWVTASYYhspteEGGGAASTFRgedvedandrftADGWLRTGDVG 438
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 300790052 456 YLV-DGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGV 494
Cdd:PRK05620 439 SVTrDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEV 478
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
186-496 |
2.98e-07 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 53.24 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 186 TSGSTADPKAVRITYGNLYSNVKAMveRAEFDFDVDVMVswlptfhdmgmvgFLTVPMTFGVELVK------------IT 253
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCILPNIQHF--RSLFNITSEDIL-------------FLTSPLTFDPSVVEiflslssgatllIV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 254 PVEFLSGPLIWPELITKYHGTTTAapnFAYAIVGRRMARVDEDDAY--DLSKLRIALNGAEPIdetaVQTFVDAGARFKM 331
Cdd:cd17654 191 PTSVKVLPSKLADILFKRHRITVL---QATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPF----PSLVILSSWRGKG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 332 PAECVFPAYGMAEATlavSFAplftgLTLDVVEADAleaenravPVPegdprrgtdgvrsfalLGRPLDGLEAEIVDDAG 411
Cdd:cd17654 264 NRTRIFNIYGITEVS---CWA-----LAYKVPEEDS--------PVQ----------------LGSPLLGTVIEVRDQNG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 412 KRVD-EREVGEIRLRGeaVTPGYltMDGPLATqdedgWLNTGDLGYLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATS 490
Cdd:cd17654 312 SEGTgQVFLGGLNRVC--ILDDE--VTVPKGT-----MRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIES 382
|
....*.
gi 300790052 491 VEGVRA 496
Cdd:cd17654 383 CLGVES 388
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
158-574 |
4.17e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 53.11 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 158 QLITELAAAEPLPDVVVTdeGDT-ALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVSWLPTFHDMGMV 236
Cdd:PRK06060 126 ELMSEAARVAPGGYEPMG--GDAlAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 237 GFLTVPMTFGVELVkITPVEFlsGPLIWPELITKYHGTTT-AAPNFayaivgrrMARVdeddaydlsklrialngaepID 315
Cdd:PRK06060 204 NSVWFPLATGGSAV-INSAPV--TPEAAAILSARFGPSVLyGVPNF--------FARV--------------------ID 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 316 ETAVQTFvdagarfkMPAECVFPAYGMAEATLAVSFAPLFTGL-TLDVVEADalEAENRAVPVPEGDPRRGTdgvrsfal 394
Cdd:PRK06060 253 SCSPDSF--------RSLRCVVSAGEALELGLAERLMEFFGGIpILDGIGST--EVGQTFVSNRVDEWRLGT-------- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 LGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDGPLATqdEDGWLNTGDLGYLV-DGQIVICGRRKDVII 473
Cdd:PRK06060 315 LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVA--NEGWLDTRDRVCIDsDGWVTYRCRADDTEV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 474 MGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARVRDAVDMRPYAVVvl 553
Cdd:PRK06060 393 IGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVV-- 470
|
410 420
....*....|....*....|.
gi 300790052 554 paGSLPKTPSGKVKRAATAQQ 574
Cdd:PRK06060 471 --DRLPRTPNGKLVRGALRKQ 489
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
162-575 |
6.14e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 52.38 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 162 ELAA-AEPLPDVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLT 240
Cdd:PRK07867 135 ELAAhRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPD-DVCYVSMPLFHSNAVMAGWA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 241 VPMTFGVELV---KITPVEFLSGpliwpelITKYHGTttaapnfaYA-IVGRRMARV-----DEDDAYdlSKLRIAL-NG 310
Cdd:PRK07867 214 VALAAGASIAlrrKFSASGFLPD-------VRRYGAT--------YAnYVGKPLSYVlatpeRPDDAD--NPLRIVYgNE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 311 AEPIDetaVQTFvdaGARFkmpaEC-VFPAYGMAEatLAVSFAplftgltldvveadaleaenRAVPVPEGDPRRGTDGV 389
Cdd:PRK07867 277 GAPGD---IARF---ARRF----GCvVVDGFGSTE--GGVAIT--------------------RTPDTPPGALGPLPPGV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 390 rsfALLGrPLDGLE---AEIvDDAGKRVDEREVGE-IRLRGEAVTPGYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVI 464
Cdd:PRK07867 325 ---AIVD-PDTGTEcppAED-ADGRLLNADEAIGElVNTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRdADGYAYF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 465 CGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDAGSRRERFAVVLESKLAGDAEAeknLMKQVSARVRDAVD 544
Cdd:PRK07867 400 AGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDA---FAEFLAAQPDLGPK 476
|
410 420 430
....*....|....*....|....*....|..
gi 300790052 545 MRPYAVVVlpAGSLPKTPSGKV-KRAATAQQF 575
Cdd:PRK07867 477 QWPSYVRV--CAELPRTATFKVlKRQLSAEGV 506
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
395-580 |
8.78e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 51.53 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 LGRPLDGLEAEIVDDAgkrvdereVGEIRLRGEAVTPGYLtmdgPlATQDEDGWLNTGDLGYLV-DGQIVICGRRKDVII 473
Cdd:PRK07445 285 SGQVLPHAQITIPANQ--------TGNITIQAQSLALGYY----P-QILDSQGIFETDDLGYLDaQGYLHILGRNSQKII 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 474 MGGRNLYPTDIE---RAATSVEGV--------RAGNAVAvrldagsrrerfAVVLESKLAGDAEAEKNLMKQVSARVRda 542
Cdd:PRK07445 352 TGGENVYPAEVEaaiLATGLVQDVcvlglpdpHWGEVVT------------AIYVPKDPSISLEELKTAIKDQLSPFK-- 417
|
170 180 190
....*....|....*....|....*....|....*...
gi 300790052 543 vdmRPYAVVVLPAgsLPKTPSGKVKRAATAQQFADRIK 580
Cdd:PRK07445 418 ---QPKHWIPVPQ--LPRNPQGKINRQQLQQIAVQRLG 450
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
161-570 |
2.13e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.81 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 161 TELAAAEPLPdVVVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDvDVMVSWLPTFHDMGMVGFLt 240
Cdd:PRK10252 582 APLAPQGAAP-LQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTAD-DVVLQKTPCSFDVSVWEFF- 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 241 VPMTFGVELVkITPVEFLSGPLIWPELITKYHGTTTA-APNFAYAIVGrrmARVDEDDAYDLSKLRIALNGAEPIDETAV 319
Cdd:PRK10252 659 WPFIAGAKLV-MAEPEAHRDPLAMQQFFAEYGVTTTHfVPSMLAAFVA---SLTPEGARQSCASLRQVFCSGEALPADLC 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 320 QTFvdaGARFKMPaecVFPAYGMAEATLAVSFAPLFtgltldvveADALeAENRAVPVPEGDPRRGTdgvrsfallgrpl 399
Cdd:PRK10252 735 REW---QQLTGAP---LHNLYGPTEAAVDVSWYPAF---------GEEL-AAVRGSSVPIGYPVWNT------------- 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 400 dGLEaeIVDDAGKRVDEREVGEIRLRGEAVTPGYLT---------MDGPLAtQDEDGWLnTGDLG-YLVDGQIVICGRRK 469
Cdd:PRK10252 786 -GLR--ILDARMRPVPPGVAGDLYLTGIQLAQGYLGrpdltasrfIADPFA-PGERMYR-TGDVArWLDDGAVEYLGRSD 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 470 DVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRLDA------GSRRERFAVVLESKLAGDAEAeknLMKQVSARVRDAv 543
Cdd:PRK10252 861 DQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQaaatggDARQLVGYLVSQSGLPLDTSA---LQAQLRERLPPH- 936
|
410 420
....*....|....*....|....*..
gi 300790052 544 dMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:PRK10252 937 -MVPVVLLQLDQ--LPLSANGKLDRKA 960
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
171-527 |
2.20e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 50.79 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 171 DVVVTDEGDTALLQLTSGSTADPKAVRITYGN---LYSNVKAMVERAEFDFDV-DVMVSWLPTFHDM------------G 234
Cdd:PLN02614 216 DLPIKKKSDICTIMYTSGTTGDPKGVMISNESivtLIAGVIRLLKSANAALTVkDVYLSYLPLAHIFdrvieecfiqhgA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 235 MVGFLTVPMTFGVE-LVKITPVEFLSGPLIWPELITKYHGTTT-----------AAPNFAYAIVGRRMARVDEDDAYD-- 300
Cdd:PLN02614 296 AIGFWRGDVKLLIEdLGELKPTIFCAVPRVLDRVYSGLQKKLSdggflkkfvfdSAFSYKFGNMKKGQSHVEASPLCDkl 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 301 -LSKL--------RIALNGAEPIdETAVQTFVdagarfKMPAEC-VFPAYGMAEATlAVSFAPLFTGL-TLDVVeadale 369
Cdd:PLN02614 376 vFNKVkqglggnvRIILSGAAPL-ASHVESFL------RVVACChVLQGYGLTESC-AGTFVSLPDELdMLGTV------ 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 370 aenrAVPVPEGDPRrgtdgvrsfallgrpldgLEA--EIVDDAgkrVDEREVGEIRLRGEAVTPGYLTMDGPLATQDEDG 447
Cdd:PLN02614 442 ----GPPVPNVDIR------------------LESvpEMEYDA---LASTPRGEICIRGKTLFSGYYKREDLTKEVLIDG 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 448 WLNTGDLG-YLVDGQIVICGRRKDVIIMG-GRNLYPTDIERAATSVEGVRA----GNA-----VAVRLDAGSRRERFAVv 516
Cdd:PLN02614 497 WLHTGDVGeWQPNGSMKIIDRKKNIFKLSqGEYVAVENIENIYGEVQAVDSvwvyGNSfesflVAIANPNQQILERWAA- 575
|
410
....*....|.
gi 300790052 517 lESKLAGDAEA 527
Cdd:PLN02614 576 -ENGVSGDYNA 585
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
176-568 |
3.15e-06 |
|
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: 50.12 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 176 DEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFD-VDVMVSWLPTFHDMGMVGFLTVpMTFGVELVKITp 254
Cdd:cd05915 151 PERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSeKDVVLPVVPMFHVNAWCLPYAA-TLVGAKQVLPG- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 255 vEFLSGPLIWPELITKYHGTTTAAPNFAYAIVGrrmARVDEDDAYDLSkLRIALNGAEPIDetaVQTFVDAGARFK-MPA 333
Cdd:cd05915 229 -PRLDPASLVELFDGEGVTFTAGVPTVWLALAD---YLESTGHRLKTL-RRLVVGGSAAPR---SLIARFERMGVEvRQG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 334 ECVFPAYGMAEATLAVSfaplftgltldvveadaleaENRAVPVPEGDPRRGTDGVRSFALLGRPLDGLEAEIVDDAgkr 413
Cdd:cd05915 301 YGLTETSPVVVQNFVKS--------------------HLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDG--- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 414 vdeREVGEIRLRGEAVTPGYLT-MDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRRKDVIIMGGRNLYPTDIERAATSV 491
Cdd:cd05915 358 ---KALGEVQLKGPWITGGYYGnEEATRSALTPDGFFRTGDIAVWdEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGH 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300790052 492 EGVRAGNAVAvRLDAGSRRERFAVVlesKLAgDAEAEKNLMKQVSARVRDAVDMRPYAVVVlpAGSLPKTPSGKVKR 568
Cdd:cd05915 435 PKVKEAAVVA-IPHPKWQERPLAVV---VPR-GEKPTPEELNEHLLKAGFAKWQLPDAYVF--AEEIPRTSAGKFLK 504
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
137-568 |
3.35e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 49.65 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 137 VLLGEPFDQLAPV--LEQKGIGFQLI---TELAAAEPLPDVV-----VTDEGDTA-------------LLQLTSGSTADP 193
Cdd:PRK08308 37 VCLKDPFDIITLVffLKEKGASVLPIhpdTPKEAAIRMAKRAgchglLYGESDFTkleavnylaeepsLLQYSSGTTGEP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 194 KAVRITYGNLYSNVKAMVERAEFDFDVDVMVSwLPTFHDMGMVGFLTVPMTFGVElvkitpveflsgpliwPELITkyhg 273
Cdd:PRK08308 117 KLIRRSWTEIDREIEAYNEALNCEQDETPIVA-CPVTHSYGLICGVLAALTRGSK----------------PVIIT---- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 274 ttTAAPNFAYAIVgrrmARVDEDDAYDLSKLRIALNGAEPIDET--AVQTfvdAGARfkMPAEC----------VFPAYG 341
Cdd:PRK08308 176 --NKNPKFALNIL----RNTPQHILYAVPLMLHILGRLLPGTFQfhAVMT---SGTP--LPEAWfyklrerttyMMQQYG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 342 MAEATlAVSFAPlftgltlDVVEADALeaenrAVPVPEGDPRRGTDgvrsfalLGRPldgleAEIVDDAGKRvderevgE 421
Cdd:PRK08308 245 CSEAG-CVSICP-------DMKSHLDL-----GNPLPHVSVSAGSD-------ENAP-----EEIVVKMGDK-------E 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 422 IRlrgeavtpgyltmdgplatqdedgwlnTGDLGYLV-DGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRagNAV 500
Cdd:PRK08308 293 IF---------------------------TKDLGYKSeRGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQ--EAV 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300790052 501 AVRLDAGSRRERFAVvlesklagdaeaeknlmkQVSAR-VRDAVDMRPYAVVVLPA----------GSLPKTPSGKVKR 568
Cdd:PRK08308 344 VYRGKDPVAGERVKA------------------KVISHeEIDPVQLREWCIQHLAPyqvpheiesvTEIPKNANGKVSR 404
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
395-569 |
3.64e-06 |
|
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: 49.77 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 LGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTM---DGP---LATQDEDGWLnTGDLGYL-VDGQIVICGR 467
Cdd:cd05928 345 MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSgyvDNPektAATIRGDFYL-TGDRGIMdEDGYFWFMGR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 468 RKDVIIMGGRNLYPTDIERAATSVEGVrAGNAVAVRLDA--GSRRERFAVVLESKLAGDAEAeknLMKQVSARVRDAVDM 545
Cdd:cd05928 424 ADDVINSSGYRIGPFEVESALIEHPAV-VESAVVSSPDPirGEVVKAFVVLAPQFLSHDPEQ---LTKELQQHVKSVTAP 499
|
170 180
....*....|....*....|....
gi 300790052 546 RPYAVVVLPAGSLPKTPSGKVKRA 569
Cdd:cd05928 500 YKYPRKVEFVQELPKTVTGKIQRN 523
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
186-485 |
6.04e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 49.35 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 186 TSGSTADPKA-VRITYGNL----YSNVKAMVERAEFDFDVDVMVSWLpTFHdMGMVGFLTVPMTFgvelvkitpVEFLSG 260
Cdd:PTZ00237 262 TSGTTGNSKAvVRSNGPHLvglkYYWRSIIEKDIPTVVFSHSSIGWV-SFH-GFLYGSLSLGNTF---------VMFEGG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 261 PL--------IWpELITKYHGTTTaapnFAYAIVGRRMARVDED-----DAYDLSKLRIALNGAEPIDETaVQTFVDAga 327
Cdd:PTZ00237 331 IIknkhieddLW-NTIEKHKVTHT----LTLPKTIRYLIKTDPEatiirSKYDLSNLKEIWCGGEVIEES-IPEYIEN-- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 328 rfKMPAECVfPAYGMAEatlavsfaplfTGLTLdVVEADALEAENRAVpvpegdprrgtdgvrsfallGRPLDGLEAEIV 407
Cdd:PTZ00237 403 --KLKIKSS-RGYGQTE-----------IGITY-LYCYGHINIPYNAT--------------------GVPSIFIKPSIL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 408 DDAGKRVDEREVGEIRLRgeavtpgyLTMDGPLAT----QDED---------GWLNTGDLGYL-VDGQIVICGRRKDVII 473
Cdd:PTZ00237 448 SEDGKELNVNEIGEVAFK--------LPMPPSFATtfykNDEKfkqlfskfpGYYNSGDLGFKdENGYYTIVSRSDDQIK 519
|
330
....*....|..
gi 300790052 474 MGGRNLYPTDIE 485
Cdd:PTZ00237 520 ISGNKVQLNTIE 531
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
459-570 |
1.22e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 48.02 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 459 DGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRlDA--GSRRERFAVVLESKLAGDAEA----EKNLM 532
Cdd:PRK10524 486 DGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVK-DAlkGQVAVAFVVPKDSDSLADREArlalEKEIM 564
|
90 100 110
....*....|....*....|....*....|....*...
gi 300790052 533 KQVSARVrDAVdMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:PRK10524 565 ALVDSQL-GAV-ARPARVWFVSA--LPKTRSGKLLRRA 598
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
395-570 |
1.38e-05 |
|
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: 47.85 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 LGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVTPGYLTMDgPLATQ-------DEDGWL-NTGDLG-YLVDGQIVIC 465
Cdd:cd17656 303 IGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQ-ELTAEkffpdpfDPNERMyRTGDLArYLPDGNIEFL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 466 GRRKDVIIMGGRNLYPTDIERAATSVEGVRAGnAVAVRLDAGSRRERFAVVLESKLAGDAEAEKNLMKQVSARvrdavdM 545
Cdd:cd17656 382 GRADHQVKIRGYRIELGEIEAQLLNHPGVSEA-VVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEY------M 454
|
170 180
....*....|....*....|....*
gi 300790052 546 RPYAVVvlPAGSLPKTPSGKVKRAA 570
Cdd:cd17656 455 IPSFFV--PLDQLPLTPNGKVDRKA 477
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
395-568 |
3.15e-05 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 46.79 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 LGRPLDGLEAEIVDDAGKRVDErevGEIRLRGEAVTP-----GYLTMDGPLATQDEDGWLNTGDLGYL-VDGQIVICGRR 468
Cdd:cd05974 254 MGRPLPGYRVALLDPDGAPATE---GEVALDLGDTRPvglmkGYAGDPDKTAHAMRGGYYRTGDIAMRdEDGYLTYVGRA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 469 KDVIIMGGRNLYPTDIERAATSVEGVrAGNAVAVRLDAgsrrERFAV----VLeskLAGDAEAEKNLMKQVSARVRDAvd 544
Cdd:cd05974 331 DDVFKSSDYRISPFELESVLIEHPAV-AEAAVVPSPDP----VRLSVpkafIV---LRAGYEPSPETALEIFRFSRER-- 400
|
170 180
....*....|....*....|....*
gi 300790052 545 MRPYAVVV-LPAGSLPKTPSGKVKR 568
Cdd:cd05974 401 LAPYKRIRrLEFAELPKTISGKIRR 425
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
396-568 |
4.12e-05 |
|
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: 46.40 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 396 GRPLDGLEAEIVDDAGKRVDEREVGEIRLR----GEAVT----------------PG-YLTMDGplATQDEDGWlntgdl 454
Cdd:cd05966 413 TRPFFGIEPAILDEEGNEVEGEVEGYLVIKrpwpGMARTiygdheryedtyfskfPGyYFTGDG--ARRDEDGY------ 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 455 gylvdgqIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVrAGNAVAVRLDAGSRRERFA-VVLESKLAGDAEAEKNLMK 533
Cdd:cd05966 485 -------YWITGRVDDVINVSGHRLGTAEVESALVAHPAV-AEAAVVGRPHDIKGEAIYAfVTLKDGEEPSDELRKELRK 556
|
170 180 190
....*....|....*....|....*....|....*..
gi 300790052 534 QVSARVRdavdmrPYAV--VVLPAGSLPKTPSGKVKR 568
Cdd:cd05966 557 HVRKEIG------PIATpdKIQFVPGLPKTRSGKIMR 587
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-570 |
8.18e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.93 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 33 TWAEVHEEARRIAGGLVAGGFERGTAVGVLAAAPVLIAPTVQAVWLAGGSVTMLHQPTPRTDLAEWAEDT-VRVLGMIGS 111
Cdd:PRK05691 1158 DYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSgVELLLTQSH 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 112 DQDALGGPGGLAPRPgsgagprnvtvllgepFDQLapvleqkgigfqlitELAAAEPLPDVVVTDEGDTALLQLTSGSTA 191
Cdd:PRK05691 1238 LLERLPQAEGVSAIA----------------LDSL---------------HLDSWPSQAPGLHLHGDNLAYVIYTSGSTG 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 192 DPKAVRITYGNLYSNVKAMveRAEFDFDV-DVMVSWLPTFHDMGmVGFLTVPMTFGVELVKITPVEFlSGPLIWPELITK 270
Cdd:PRK05691 1287 QPKGVGNTHAALAERLQWM--QATYALDDsDVLMQKAPISFDVS-VWECFWPLITGCRLVLAGPGEH-RDPQRIAELVQQ 1362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 271 YHGTTTaapNFAYAIVgrrMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFVDagarfKMPAECVFPAYGMAEATLAVS 350
Cdd:PRK05691 1363 YGVTTL---HFVPPLL---QLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQ-----RLPQVQLHNRYGPTETAINVT 1431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 351 FAPLftgltldvveadaleaenravpvpegdprRGTDGVRSfaLLGRPLDGLEAEIVDDAGKRVDEREVGEIRLRGEAVT 430
Cdd:PRK05691 1432 HWQC-----------------------------QAEDGERS--PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLA 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 431 PGYLTMDGPLATQ---DEDG-----WLNTGDLG-YLVDGQIVICGRRKDVIIMGGRNLYPTDIERAATSVEGVRAGnAVA 501
Cdd:PRK05691 1481 RGYLGRPALTAERfvpDPLGedgarLYRTGDRArWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQA-AVL 1559
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300790052 502 VRLDAGSRRerfAVVLESKLAGDAEAEKNLMKQVSARVRDAvdMRPYAVVVLPAgsLPKTPSGKVKRAA 570
Cdd:PRK05691 1560 VREGAAGAQ---LVGYYTGEAGQEAEAERLKAALAAELPEY--MVPAQLIRLDQ--MPLGPSGKLDRRA 1621
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
395-568 |
8.78e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 45.27 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 395 LGRPLDGLEAEIVDDAGKRVDEREVGEIRLRgeavtPGYLTMDGPLATQDE-------DGWLNTGDLGYL-VDGQIVICG 466
Cdd:PRK04319 378 MGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-----KGWPSMMRGIWNNPEkyesyfaGDWYVSGDSAYMdEDGYFWFQG 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 467 RRKDVIIMGGRNLYPTDIERA-----ATSVEGVrAGNAVAVRldaGSRRERFaVVLESKLAGDAEAEKNLMKQVSARVRD 541
Cdd:PRK04319 453 RVDDVIKTSGERVGPFEVESKlmehpAVAEAGV-IGKPDPVR---GEIIKAF-VALRPGYEPSEELKEEIRGFVKKGLGA 527
|
170 180
....*....|....*....|....*..
gi 300790052 542 AVDMRPYAVvvlpAGSLPKTPSGKVKR 568
Cdd:PRK04319 528 HAAPREIEF----KDKLPKTRSGKIMR 550
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
179-504 |
1.27e-04 |
|
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: 44.65 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 179 DTALLQLTSGSTADPKAVRITYGNLYsNVKAMVERAEFDFDVDVMVSWLPTFHDMG-MVGFLTVPMTfGVELV---KITP 254
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAW-RGGAFFAGSGGALPSDVLYTCLPLYHSTAlIVGWSACLAS-GATLVirkKFSA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 255 VEFlsgpliWPELItKYHGTTtaapnFAYaiVG---RRMARVDEDDAYDLSKLRIAL-NGAEPidetavQTFVDAGARFK 330
Cdd:cd05940 160 SNF------WDDIR-KYQATI-----FQY--IGelcRYLLNQPPKPTERKHKVRMIFgNGLRP------DIWEEFKERFG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 331 MPAECVFpaYGMAEATL----------AVSFAP--LFTGLTLDVVEADaleaenravpVPEGDPRRGTDGVrsfallgrp 398
Cdd:cd05940 220 VPRIAEF--YAATEGNSgfinffgkpgAIGRNPslLRKVAPLALVKYD----------LESGEPIRDAEGR--------- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 399 ldgleaeivddaGKRVDEREVGEIRLRGEAVTP--GYLtmdGPLATQ---------DEDGWLNTGDLGYLVD-GQIVICG 466
Cdd:cd05940 279 ------------CIKVPRGEPGLLISRINPLEPfdGYT---DPAATEkkilrdvfkKGDAWFNTGDLMRLDGeGFWYFVD 343
|
330 340 350
....*....|....*....|....*....|....*...
gi 300790052 467 RRKDVIIMGGRNLYPTDIERAATSVEGVRAGNAVAVRL 504
Cdd:cd05940 344 RLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQV 381
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
173-570 |
1.96e-04 |
|
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: 44.24 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 173 VVTDEGDTALLQLTSGSTADPKAVRITYGNLYSNVKAMVERAEFDFDVDVMVswLPTFHDMGMVGFLTVPMTFGVELVKI 252
Cdd:cd17655 132 PVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVAL--FASISFDASVTEIFASLLSGNTLYIV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 253 TPVEFLSGPLIWPELITKYHGTTTAAPNFayaivgrrMARVDEDDAYDLSKLRIALNGAEPIDETAVQTFvdaGARFKMP 332
Cdd:cd17655 210 RKETVLDGQALTQYIRQNRITIIDLTPAH--------LKLLDAADDSEGLSLKHLIVGGEALSTELAKKI---IELFGTN 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 333 AEcVFPAYGMAEATLavsfaplftGLTLDVVEadalEAENRAVPVPegdprrgtdgvrsfalLGRPLDGLEAEIVDDAGK 412
Cdd:cd17655 279 PT-ITNAYGPTETTV---------DASIYQYE----PETDQQVSVP----------------IGKPLGNTRIYILDQYGR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 413 RVDEREVGEIRLRGEAVTPGYLT---------MDGPLA-------TQDEDGWLNTGDLGYL--VDGQIVICGRRkdvIIM 474
Cdd:cd17655 329 PQPVGVAGELYIGGEGVARGYLNrpeltaekfVDDPFVpgermyrTGDLARWLPDGNIEFLgrIDHQVKIRGYR---IEL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 475 GgrnlyptDIERAATSVEGVRAGnAVAVRLDagsrrERFAVVLESKLAGDAEAEKNLMKQVSARvrdavDMRPYAVvvlP 554
Cdd:cd17655 406 G-------EIEARLLQHPDIKEA-VVIARKD-----EQGQNYLCAYIVSEKELPVAQLREFLAR-----ELPDYMI---P 464
|
410 420
....*....|....*....|.
gi 300790052 555 A-----GSLPKTPSGKVKRAA 570
Cdd:cd17655 465 SyfiklDEIPLTPNGKVDRKA 485
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
132-459 |
2.64e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 43.88 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 132 PRNVTVLLGEPFDQLAPVLEQKGIgfQLITELAAAE-----PLPDVV---VTDEGDTALLQL----------TSGSTADP 193
Cdd:PRK12582 158 PRVVFAQSGAPFARALAALDLLDV--TVVHVTGPGEgiasiAFADLAatpPTAAVAAAIAAItpdtvakylfTSGSTGMP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 194 KAVRITYGNLYSNVKAM--VERAEFDFDVDVMVSWLPTFHDM-GMVGFLTV-------------PMTFGVE-----LVKI 252
Cdd:PRK12582 236 KAVINTQRMMCANIAMQeqLRPREPDPPPPVSLDWMPWNHTMgGNANFNGLlwgggtlyiddgkPLPGMFEetirnLREI 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 253 TPVEFLSGPLiwpelitkyhgtttaapnfAYAIVGRRMARVDEDDAYDLSKLR-IALNGA-------EPIDETAVQTfvd 324
Cdd:PRK12582 316 SPTVYGNVPA-------------------GYAMLAEAMEKDDALRRSFFKNLRlMAYGGAtlsddlyERMQALAVRT--- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300790052 325 AGARFKmpaecVFPAYGMAEAtlavsfAPLFTGLTLDvveadaleaenravpvpegdprrgTDGVrsfALLGRPLDGLEA 404
Cdd:PRK12582 374 TGHRIP-----FYTGYGATET------APTTTGTHWD------------------------TERV---GLIGLPLPGVEL 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 300790052 405 EIVDDAGKRvderevgEIRLRGEAVTPGYLTM-DGPLATQDEDGWLNTGDLGYLVD 459
Cdd:PRK12582 416 KLAPVGDKY-------EVRVKGPNVTPGYHKDpELTAAAFDEEGFYRLGDAARFVD 464
|
|
|