|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1-521 |
0e+00 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 939.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 1 MSELAAVLTRSMQASAGDLMVLDRETSLWCRHPWPEVHGLAESVAAWLLDHDRPAAVGLVGEPTVELVAAIQGAWLAGAA 80
Cdd:PRK05851 1 MNELAAALSDAMTASGRDLVVLDRESGLWRRHPWPEVHGRAENVAARLLDRDRPGAVGLVGEPTVELVAAIQGAWLAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 81 VSILPGPVRGANDQRWADATLTRFLGIGVRTVLSQGSYLARLRSVDTaGVTIGDLSTAAHTNRSAT--PVASEGPAVLQG 158
Cdd:PRK05851 81 VSILPGPVRGADDGRWADATLTRFAGIGVRTVLSHGSHLERLRAVDS-SVTVHDLATAAHTNRSASltPPDSGGPAVLQG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTAFTASPFRWLS 238
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAFSASPFRWLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 239 WLSDSGATMTAAPNFAYNLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVLPSYGLAESTCAV 318
Cdd:PRK05851 240 WLSDSRATLTAAPNFAYNLIGKYARRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAESTCAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 319 TVPVPGIGLLADRVI--DGSGAHKHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAGYLGQQPIDPDDWFA 396
Cdd:PRK05851 320 TVPVPGIGLRVDEVTtdDGSGARRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAPIDPDDWFP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 397 TGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEANARAE 476
Cdd:PRK05851 400 TGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFRGPDEAGARSE 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 489502054 477 LIQRVASECGIVPSDVVFVSPGSLPRTSSGKLRRLAVRRSLEMAD 521
Cdd:PRK05851 480 VVQRVASECGVVPSDVVFVAPGSLPRTSSGKLRRLAVKRSLEAAD 524
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
13-518 |
7.56e-165 |
|
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: 478.27 E-value: 7.56e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 13 QASAGDLMVLDRETSLWCRHPWPEVHGLAESVAAWLLDHDRPA-AVGLVGEPTVELVAAIQGAWLAGAAVSILPGPVRGA 91
Cdd:cd05931 6 RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKPGdRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 92 NDQRWADATLTrflgIGVRTVLSQGSYLARLR-------SVDTAGVTIGDLSTAAHTNRSATP-VASEGPAVLQGTAGST 163
Cdd:cd05931 86 HAERLAAILAD----AGPRVVLTTAAALAAVRafaasrpAAGTPRLLVVDLLPDTSAADWPPPsPDPDDIAYLQYTSGST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 164 GAPRTAILSPGAVLSNLRGLNQRVGtDAATDVGCSWLPLYHDMGL-AFVLSAALAGAPLWLAPTTAFTASPFRWLSWLSD 242
Cdd:cd05931 162 GTPKGVVVTHRNLLANVRQIRRAYG-LDPGDVVVSWLPLYHDMGLiGGLLTPLYSGGPSVLMSPAAFLRRPLRWLRLISR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 243 SGATMTAAPNFAYNLIGKYARR--VSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVLPSYGLAESTCAVTV 320
Cdd:cd05931 241 YRATISAAPNFAYDLCVRRVRDedLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEATLFVSG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 321 PVPGIGLLADRV-------------IDGSGAHKHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAGYLGQQ 387
Cdd:cd05931 321 GPPGTGPVVLRVdrdalagravavaADDPAARELVSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 388 PI-----------DPDDWFATGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGV-REGAVVALGTGDRST 455
Cdd:cd05931 401 EAtaetfgalaatDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlRPGCVAAFSVPDDGE 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489502054 456 RPGLVVAAEFRGP---DEANARAELIQRVASECGIVPSDVVFVSPGSLPRTSSGKLRRLAVRRSLE 518
Cdd:cd05931 481 ERLVVVAEVERGAdpaDLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
31-515 |
7.49e-124 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 373.56 E-value: 7.49e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 31 RHPWPEVHGLAESVAAWLLDHD--RPAAVGLVGEPTVELVAAIQGAWLAGAAVSILPGPVRGANDQRWADATLTRFLGIG 108
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGvgPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGMIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 109 VRTVLSQGSYLA---RLRSVDTAGVTIGDLSTAAhtnrSATPVASE--GPAVLQGTAGSTGAPRTAILSPGAVLSNLRGL 183
Cdd:PRK07768 109 AKAVVVGEPFLAaapVLEEKGIRVLTVADLLAAD----PIDPVETGedDLALMQLTSGSTGSPKAVQITHGNLYANAEAM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 184 NQRVGTDAATDVGCSWLPLYHDMGL-AFVLSAALAGAPLWLAPTTAFTASPFRWLSWLSDSGATMTAAPNFAYNLIGKYA 262
Cdd:PRK07768 185 FVAAEFDVETDVMVSWLPLFHDMGMvGFLTVPMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 263 RRVSE---VDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVLPSYGLAESTCAVTVPVPGIGLLADRV------- 332
Cdd:PRK07768 265 RRQAKpgaFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEATLAVSFSPCGAGLVVDEVdadllaa 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 333 ------IDGSGAHKHAVLGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYL---GQQP-IDPDDWFATGDLGY 402
Cdd:PRK07768 345 lrravpATKGNTRRLATLGPPLPGLEVRV-VDEDGQVLPPRGVGVIELRGESVTPGYLtmdGFIPaQDADGWLDTGDLGY 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 403 L-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEFRG-PDEANARA---EL 477
Cdd:PRK07768 424 LtEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVAVESNAfEDPAEVRRirhQV 503
|
490 500 510
....*....|....*....|....*....|....*...
gi 489502054 478 IQRVASECGIVPSDVVFVSPGSLPRTSSGKLRRLAVRR 515
Cdd:PRK07768 504 AHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRANAAE 541
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
41-514 |
2.63e-77 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 253.77 E-value: 2.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 41 AESVAAWLLDH-----DRpaaVGLVGEPTVELVAAIQGAWLAGAAVSILPGPVRGANDQRWADaTLTRFLGIGVRTVLSQ 115
Cdd:PRK09192 59 AEAGARRLLALglkpgDR---VALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGRESYIA-QLRGMLASAQPAAIIT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 116 GSYLARLrsVDTAGVTIGDLSTAAHTNRSATPVAS--------EGPAVLQGTAGSTGAPRTAILSPGAVLSNLR-----G 182
Cdd:PRK09192 135 PDELLPW--VNEATHGNPLLHVLSHAWFKALPEADvalprptpDDIAYLQYSSGSTRFPRGVIITHRALMANLRaishdG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 183 LNQRVGtdaatDVGCSWLPLYHDMGL-AFVLSAALAGAPLWLAPTTAFTASPFRWLSWLSDSGATMTAAPNFAYNLIgky 261
Cdd:PRK09192 213 LKVRPG-----DRCVSWLPFYHDMGLvGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELC--- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 262 ARRVSEVDLGAL-----RVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVLPSYGLAESTCAVTVPVPGIGLLADRV---- 332
Cdd:PRK09192 285 ARRVNSKDLAELdlscwRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEATLAVSFSPLGSGIVVEEVdrdr 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 333 ----------IDGSGAHKHAVL-GNPIPGMEVRIScGDQAAGNASREIGEIEIRGASMMAGYLGQQP----IDPDDWFAT 397
Cdd:PRK09192 365 leyqgkavapGAETRRVRTFVNcGKALPGHEIEIR-NEAGMPLPERVVGHICVRGPSLMSGYFRDEEsqdvLAADGWLDT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 398 GDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTgDRSTRPGLVVAAEFRGPDEAnARAEL 477
Cdd:PRK09192 444 GDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAFSI-AQENGEKIVLLVQCRISDEE-RRGQL 521
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 489502054 478 IQRVAS----ECGiVPSDVVFVSPGSLPRTSSGKLRRLAVR 514
Cdd:PRK09192 522 IHALAAlvrsEFG-VEAAVELVPPHSLPRTSSGKLSRAKAK 561
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-518 |
3.90e-70 |
|
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: 231.24 E-value: 3.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 4 LAAVLTRSMQASAGDLMVLDRETSLwcrhPWPEVHGLAESVAAWLLDH-----DRpaaVGLVGEPTVELVAAIQGAWLAG 78
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRL----TYAELDARARRLAAALRALgvgpgDR---VALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 79 AAVSILpgpvrganDQRWADATLTRFLG-IGVRTVLSqgsylarlrsvdtagvtigdlstaahtnrsatpvasegpAVLQ 157
Cdd:COG0318 74 AVVVPL--------NPRLTAEELAYILEdSGARALVT---------------------------------------ALIL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 158 GTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAaTDVGCSWLPLYHDMGL-AFVLSAALAGAPLWLAPTTaftaSPFRW 236
Cdd:COG0318 107 YTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP-GDVVLVALPLFHVFGLtVGLLAPLLAGATLVLLPRF----DPERV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 237 LSWLSDSGAT-MTAAPNFAYNLIgkYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapFGFdagAVLPSYGLAEST 315
Cdd:COG0318 182 LELIERERVTvLFGVPTMLARLL--RHPEFARYDLSSLRLVVSGGAPLPPELLERFEER---FGV---RIVEGYGLTETS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 316 CAVTVPVPgiglladrviDGSGAHKHAVlGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLGQQPID----P 391
Cdd:COG0318 254 PVVTVNPE----------DPGERRPGSV-GRPLPGVEVRI-VDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATaeafR 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 392 DDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPG-LVVAAEFRGPD 469
Cdd:COG0318 322 DGWLRTGDLGRLDEDGyLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVaFVVLRPGAELD 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489502054 470 EANARAELIQRVASECgiVPSDVVFVspGSLPRTSSGKLRRLAVRRSLE 518
Cdd:COG0318 402 AEELRAFLRERLARYK--VPRRVEFV--DELPRTASGKIDRRALRERYA 446
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
41-518 |
1.42e-64 |
|
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: 219.08 E-value: 1.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 41 AESVAAWLL-DHDRPA-AVGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGANDQRWADATLTRFLGIgvRTVLSQGSY 118
Cdd:cd05906 49 ARRLAAGLRqLGLRPGdSVILQFDDNEDFIPAFWACVLAG----FVPAPLTVPPTYDEPNARLRKLRHI--WQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 119 LARLRSVD-----TAGVTIGDLSTAAHTNRSAT-------PVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQR 186
Cdd:cd05906 123 LTDAELVAefaglETLSGLPGIRVLSIEELLDTaadhdlpQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQH 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 187 VGTDAAtDVGCSWLPLYHDMGLAFV-LSAALAGAPLWLAPTTAFTASPFRWLSWLSDSGATMTAAPNFAYNLIGKYARRV 265
Cdd:cd05906 203 NGLTPQ-DVFLNWVPLDHVGGLVELhLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 266 SEV--DLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVLPSYGLAEsTCA-VTVPVPgigllaDRVIDGSGAHKHA 342
Cdd:cd05906 282 EDGtwDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTE-TCSgVIYSRS------FPTYDHSQALEFV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 343 VLGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLG-----QQPIDPDDWFATGDLGYLGAGGLVVCGRAKEV 417
Cdd:cd05906 355 SLGRPIPGVSMRI-VDDEGQLLPEGEVGRLQVRGPVVTKGYYNnpeanAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDT 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 418 ISIAGRNIFPTEVELVAAQVRGVREG--AVVALGTGDRSTRpGLVV--AAEFRGPDEANARAELIQRVAS-ECGIVPSDV 492
Cdd:cd05906 434 IIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAETE-ELAIffVPEYDLQDALSETLRAIRSVVSrEVGVSPAYL 512
|
490 500
....*....|....*....|....*.
gi 489502054 493 VFVSPGSLPRTSSGKLRRLAVRRSLE 518
Cdd:cd05906 513 IPLPKEEIPKTSLGKIQRSKLKAAFE 538
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
154-518 |
1.62e-63 |
|
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: 215.04 E-value: 1.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAaTDVGCSWLPLYHDMGL-AFVLSAALAGAPLWLAPTTAFTAS 232
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKT-KDRILSWMPLTHDMGLiAFHLAPLIAGMNQYLMPTRLFIRR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 233 PFRWLSWLSDSGATMTAAPNFAYNLIGKYAR--RVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVLPSYG 310
Cdd:cd05908 188 PILWLKKASEHKATIVSSPNFGYKYFLKTLKpeKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPVYG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 311 LAESTCAVTVPVPG-----IGLLADRVIDGSG----------AHKHAVLGNPIPGMEVRIsCGDQAAGNASREIGEIEIR 375
Cdd:cd05908 268 LAEASVGASLPKAQspfktITLGRRHVTHGEPepevdkkdseCLTFVEVGKPIDETDIRI-CDEDNKILPDGYIGHIQIR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 376 GASMMAGYLG-----QQPIDPDDWFATGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGT 450
Cdd:cd05908 347 GKNVTPGYYNnpeatAKVFTDDGWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACGV 426
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489502054 451 GDRSTRPGLVVA-AEFRgpDEANARAELIQRVASEC----GIVPSDVVFVSpgSLPRTSSGKLRRLAVRRSLE 518
Cdd:cd05908 427 NNSNTRNEEIFCfIEHR--KSEDDFYPLGKKIKKHLnkrgGWQINEVLPIR--RIPKTTSGKVKRYELAQRYQ 495
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
154-521 |
4.17e-57 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 206.17 E-value: 4.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDA-ATDVGCSWLPLYHDMGL-AFVLSAALAGAPLWLAPTTAFTA 231
Cdd:PRK05691 169 AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLnPDDVIVSWLPLYHDMGLiGGLLQPIFSGVPCVLMSPAYFLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 232 SPFRWLSWLSDSGATMTAAPNFAYNLIgkyARRVSE-----VDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVL 306
Cdd:PRK05691 249 RPLRWLEAISEYGGTISGGPDFAYRLC---SERVSEsalerLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPDSFF 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 307 PSYGLAESTCAVTVPVPGIGLLADRVIDGSGAHKHAVLGN---------PIPGMEVRISCGDQAAGNASREIGEIEIRGA 377
Cdd:PRK05691 326 ASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGTgsvlmscgrSQPGHAVLIVDPQSLEVLGDNRVGEIWASGP 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 378 SMMAGYLgQQP---------IDPDDWFATGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVE-LVAAQVRGVREGAVVA 447
Cdd:PRK05691 406 SIAHGYW-RNPeasaktfveHDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEkTVEREVEVVRKGRVAA 484
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502054 448 LGTGDRStRPGLVVAAEF-RGPDEANARAELI----QRVASECGIVPSDVVFVSPGSLPRTSSGKLRRLAVRrsLEMAD 521
Cdd:PRK05691 485 FAVNHQG-EEGIGIAAEIsRSVQKILPPQALIksirQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACR--LRLAD 560
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
153-509 |
1.83e-55 |
|
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: 189.03 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 153 PAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCsWLPLYHDMGLAFVLSAALAGAPLWLAPTTaftaS 232
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLS-TLPLFHIGGLFGLLGALLAGGTVVLLPKF----D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 233 PFRWLSWLSDSGATMTAAPNFAYNLIGKYARRvSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapFGfdaGAVLPSYGLA 312
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPES-AGYDLSSLRALVSGGAPLPPELLERFEEA---PG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 313 ESTCAVTVPVPGiglladrvidgSGAHKHAVLGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLGQ----QP 388
Cdd:cd04433 150 ETGGTVATGPPD-----------DDARKPGSVGRPVPGVEVRI-VDPDGGELPPGEIGELVVRGPSVMKGYWNNpeatAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 389 IDPDDWFATGDLGYL-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEfrg 467
Cdd:cd04433 218 VDEDGWYRTGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLR--- 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489502054 468 PDEANARAELIQRVASECG--IVPSDVVFVSPgsLPRTSSGKLR 509
Cdd:cd04433 295 PGADLDAEELRAHVRERLApyKVPRRVVFVDA--LPRTASGKID 336
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
34-512 |
1.47e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 192.85 E-value: 1.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 34 WPEVHGLAESVAAWLLDHDRPAAVGLVGEPT-VELVAAIQGAWLAGAAVSILPGPVRGANDQRwADATLTRFLGIGVRTV 112
Cdd:PRK05850 38 WSQLYRRTLNVAEELRRHGSTGDRAVILAPQgLEYIVAFLGALQAGLIAVPLSVPQGGAHDER-VSAVLRDTSPSVVLTT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 113 LSQ----GSYLARLR-SVDTAGVTIGDLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGL---- 183
Cdd:PRK05850 117 SAVvddvTEYVAPQPgQSAPPVIEVDLLDLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdy 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 184 ---NQRVGTDAATDVgcSWLPLYHDMGLAF-VLSAALAGAPLWLAPTTAFTASPFRWLSWLSDSGATMTAAPNFAYNLIg 259
Cdd:PRK05850 197 fgdTGGVPPPDTTVV--SWLPFYHDMGLVLgVCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELA- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 260 kyARRVSE-----VDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVLPSYGLAESTCAVTVPVPGIG-------- 326
Cdd:PRK05850 274 --VRKTSDddmagLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEATVYVATREPGQPpesvrfdy 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 327 --LLADRVI---DGSGAhkhAVLGNPIP-GMEVRISCGDQAAGNASREIGEIEIRGASMMAGY----------LGQQPID 390
Cdd:PRK05850 352 ekLSAGHAKrceTGGGT---PLVSYGSPrSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYwqkpeetertFGATLVD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 391 PDD------WFATGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVElvaAQVRGVREGAVVALGTGDRSTRPgLVVAAE 464
Cdd:PRK05850 429 PSPgtpegpWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIE---ATIQEITGGRVAAISVPDDGTEK-LVAIIE 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489502054 465 FR---GPDEANAR--AELIQRVASEC----GIVPSDVVFVSPGSLPRTSSGKLRRLA 512
Cdd:PRK05850 505 LKkrgDSDEEAMDrlRTVKREVTSAIskshGLSVADLVLVAPGSIPITTSGKIRRAA 561
|
|
| FadD32_Coryne |
NF040633 |
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ... |
144-518 |
1.02e-53 |
|
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: 191.40 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 144 SATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVgCSWLPLYHDMGLAFVLSAALAGAPLWL 223
Cdd:NF040633 194 PAGTDPSDDTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLRL-VSWLPLHHDMGIILAAFVTILGLEFEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 224 APTTAFTASPFRWLSWLSDSGATM---TAAPNFAYNLIGKYAR--RVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPF 298
Cdd:NF040633 273 MSPRDFIQQPKRWVDQLSRREDDVnvyTVVPNFALELAARYANpeEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 299 GFDAGAVLPSYGLAESTCAVTVP----VPGIG------LLADRVIDGSGAHKHAV----LGNPIPGMEVRIScgDQAAGN 364
Cdd:NF040633 353 GLRRTALRPSYGLAEASLLVTTPqteeRPLFTyfdreaLAEGRAVEVAEDSENAVpfasNGQVVRPQVLAIV--DPETGQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 365 --ASREIGEIEIRGASMMAGYLGQQP----------------------IDPDDWFATGDLGYLGAGGLVVCGRAKEVISI 420
Cdd:NF040633 431 elPDGTVGEIWVHGDNMAAGYLDREEetaetfrntlgerlaensraegAPEDNWMATGDLGVIVDGELYITGRLKDLIVI 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 421 AGRNIFPTEVE-LVAAQVRGVREGAVVALG-TGDRSTRpgLVVAAEfRGPD---EANARAELIQR--VASECGIVPSDVV 493
Cdd:NF040633 511 AGRNHYPQDIEaTVQEASDHIRPDSVAAFAvPGDDVEK--LVILAE-RDDEadeSGDAEAIEAIRaaVTSAHGVVPADIR 587
|
410 420
....*....|....*....|....*.
gi 489502054 494 FVSPGSLPRTSSGKL-RRLAVRRSLE 518
Cdd:NF040633 588 IVAPGEIARSSSGKIaRRVNAKAYLE 613
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
130-516 |
4.75e-51 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 184.17 E-value: 4.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 130 VTIGDLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSWLPLYHDMGLA 209
Cdd:PRK12476 172 IAIDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 210 FVLSAALAGAPLWLAPTTAFTASPFRWLSWLSD---SGATMTAAPNFAYNLIgkyARR-----VSEVDLGALrVTLNGGE 281
Cdd:PRK12476 252 MIGFPAVYGGHSTLMSPTAFVRRPQRWIKALSEgsrTGRVVTAAPNFAYEWA---AQRglpaeGDDIDLSNV-VLIIGSE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 282 PVDCDGLTRFAEAMAPFGFDAGAVLPSYGLAESTCAVTVPVPGI----------GLLADRVIDGSGAHKHAVlgnpipgm 351
Cdd:PRK12476 328 PVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAepsvvyldreQLGAGRAVRVAADAPNAV-------- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 352 eVRISCG-----------DQAAGNASR--EIGEIEIRGASMMAGYLG-------------QQPID--------PDD--WF 395
Cdd:PRK12476 400 -AHVSCGqvarsqwavivDPDTGAELPdgEVGEIWLHGDNIGRGYWGrpeetertfgaklQSRLAegshadgaADDgtWL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 396 ATGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVE-LVAAQVRGVREGAVVALgTGDRSTRPGLVVAAEfRGPDEANAR 474
Cdd:PRK12476 479 RTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEaTVAEASPMVRRGYVTAF-TVPAEDNERLVIVAE-RAAGTSRAD 556
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489502054 475 AELIQR-----VASECGIVPSDVVFVSPGSLPRTSSGKLRRLAVRRS 516
Cdd:PRK12476 557 PAPAIDairaaVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQ 603
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
154-516 |
1.01e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 175.30 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAAtDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTAFTASP 233
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEG-DRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRP 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 234 FRWLSWLS----DSGATMTAAPNFAYNLIGkyARRV-----SEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGA 304
Cdd:PRK07769 262 GRWIRELArkpgGTGGTFSAAPNFAFEHAA--ARGLpkdgePPLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPTA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 305 VLPSYGLAESTCAV-TVPV---PGIgLLADRviDGSGAHKHAVLGNPIPGMEVRISCG-------------DQAAGNASR 367
Cdd:PRK07769 340 IKPSYGMAEATLFVsTTPMdeePTV-IYVDR--DELNAGRFVEVPADAPNAVAQVSAGkvgvsewavivdpETASELPDG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 368 EIGEIEIRGASMMAGYLG-------------QQPID-------PDD--WFATGDLGYLGAGGLVVCGRAKEVISIAGRNI 425
Cdd:PRK07769 417 QIGEIWLHGNNIGTGYWGkpeetaatfqnilKSRLSeshaegaPDDalWVRTGDYGVYFDGELYITGRVKDLVIIDGRNH 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 426 FPTEVELVAAQV-RGVREGAVVALGT---------------------GDRSTRpgLVVAAEfRGP----DEANARAELIQ 479
Cdd:PRK07769 497 YPQDLEYTAQEAtKALRTGYVAAFSVpanqlpqvvfddshaglkfdpEDTSEQ--LVIVAE-RAPgahkLDPQPIADDIR 573
|
410 420 430
....*....|....*....|....*....|....*...
gi 489502054 480 R-VASECGIVPSDVVFVSPGSLPRTSSGKLRRLAVRRS 516
Cdd:PRK07769 574 AaIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAA 611
|
|
| FAAL_FadD32 |
NF038339 |
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ... |
154-514 |
6.89e-45 |
|
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: 167.20 E-value: 6.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAAtDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTAFTASP 233
Cdd:NF038339 180 AYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDEN-SRGVTWLPLFHDMGLLTVILPALGGKYITIMSPAAFVRRP 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 234 FRWLSWL---SDSGATMTAAPNFAYNLIGkyARRV----SEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVL 306
Cdd:NF038339 259 GRWIRELaavSDGAGTFAAAPNFAFEHAA--ARGLpkegEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 307 PSYGLAESTCAVTVPVP---GIGLLADRviDGSGAHKHAVLGNPIPGMEVRISCG----DQAA----GNASRE-----IG 370
Cdd:NF038339 337 PSYGMAEATLFVSSTPRedeAKVIYVDR--EELNAGRIVEVDPDAPNAVAQVSCGyvarSQWAvivdPETGTElpdgqVG 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 371 EIEIRGASMMAGYLGQ-------------QPID--------PDD--WFATGDLGYLGAGGLVVCGRAKEVISIAGRNIFP 427
Cdd:NF038339 415 EIWLHGNNIGTGYWGRpeeteetfhnklkSRLEegshaegaPEDanWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYP 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 428 TEVELVAAQV-RGVREGAVVA-------------------LGTGDRSTRPGLVVAAEfRGPDEANARAELI-----QRVA 482
Cdd:NF038339 495 QDLEYSAQEAsKALRPGFVAAfsvpanqlpaevfenshsgLKYDADDSSEQLVIVAE-RAPGAGKADPQPIadavrAAIA 573
|
410 420 430
....*....|....*....|....*....|..
gi 489502054 483 SECGIVPSDVVFVSPGSLPRTSSGKLRRLAVR 514
Cdd:NF038339 574 VRHGVTVRDVLLVPAGSIPRTSSGKIARRACK 605
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
25-418 |
2.20e-41 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 153.62 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 25 ETSLWCRHPWPEVHGLAESVAAWLLDH-----DRpaaVGLVGEPTVELVAAIQGAWLAGAAVS-ILPGPVRGANDQRWAD 98
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRALgvgkgDR---VAILLPNSPEWVVAFLACLKAGAVYVpLNPRLPAEELAYILED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 99 A------TLTRFLGIGVRTVLSQGSYLARLRSVDTAGVTIGDLSTAAHTNRSATPVASEG-----PAVLQGTAGSTGAPR 167
Cdd:pfam00501 92 SgakvliTDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPpdpddLAYIIYTSGTTGKPK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 168 TAILSPGAVLSNLRGL---NQRVGTDAATDVGCSWLPLYHDMGL-AFVLSAALAGAPLWLAPTTAFTaSPFRWLSWLSDS 243
Cdd:pfam00501 172 GVMLTHRNLVANVLSIkrvRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPAL-DPAALLELIERY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 244 GATMTAAPNFAYNLIGKyARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMapfgfdAGAVLPSYGLAESTCAVTVPVP 323
Cdd:pfam00501 251 KVTVLYGVPTLLNMLLE-AGAPKRALLSSLRLVLSGGAPLPPELARRFRELF------GGALVNGYGLTETTGVVTTPLP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 324 GIGllaDRVIDGSgahkhavLGNPIPGMEVRIscGDQAAGN--ASREIGEIEIRGASMMAGYLGqQP------IDPDDWF 395
Cdd:pfam00501 324 LDE---DLRSLGS-------VGRPLPGTEVKI--VDDETGEpvPPGEPGELCVRGPGVMKGYLN-DPeltaeaFDEDGWY 390
|
410 420
....*....|....*....|....
gi 489502054 396 ATGDLGY-LGAGGLVVCGRAKEVI 418
Cdd:pfam00501 391 RTGDLGRrDEDGYLEIVGRKKDQI 414
|
|
| FAAL_FadD21 |
NF038337 |
fatty-acid--AMP ligase FAAL21/FadD21; |
154-512 |
1.65e-40 |
|
fatty-acid--AMP ligase FAAL21/FadD21;
Pssm-ID: 439631 [Multi-domain] Cd Length: 579 Bit Score: 154.26 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTD----AATDVGC-SWLPLYHDMGLAF-VLSAALAGAPLWLAPTT 227
Cdd:NF038337 166 AYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMAAYFPDtngvAPRDTTIvSWLPFYHDMGLVLgVIAPILGGYRSELTSPV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 228 AFTASPFRWLSWLSDSGATMTAAPNFAYNLIgkyARRVSE-----VDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDA 302
Cdd:NF038337 246 AFLQRPARWIHAMANGSPVFSAAPNFAFELA---VRKTTDadlagLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFRE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 303 GAVLPSYGLAESTCAVTVPVPG-----IGLLADRVIDGSGAHKHAVLGNPIP--GME----VRISCGDQAAGNASREIGE 371
Cdd:NF038337 323 DMMQPSYGLAEATVYVASRAEGgapevVHFEPEKLSEGSAQRCEARTGSPLLsyGTPtsptVRIVDPDTCIECPAGTVGE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 372 IEIRGASMMAGY---------------LGQQPIDPD-DWFATGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVElvaA 435
Cdd:NF038337 403 IWVHGDNVAEGYwqkpeetrrtfggvlANPSPGTPEgPWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDIE---S 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 436 QVRGVREGAVVALGTG-DRSTRPGLVVAAEFRGPDEANARAEL-------IQRVASECGIVPSDVVFVSPGSLPRTSSGK 507
Cdd:NF038337 480 TVQEITGGRVAAISVPvDETEKLVTIIELKKRGDSDEEAMRKLdavknnvTAAISRSHGLNVADLVLVPPGSIPTTTSGK 559
|
....*
gi 489502054 508 LRRLA 512
Cdd:NF038337 560 IRRAA 564
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
152-515 |
5.65e-35 |
|
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: 133.61 E-value: 5.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 152 GPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAatdvGCSWL---PLYHDMGLAFVLSAALAGAPLWLAPTTA 228
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGG----GDSWLlslPLYHVGGLAILVRSLLAGAELVLLERNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 229 -----FTASPFRWLSW-------LSDSGATMTAapnfaynligkyarrvsevdLGALRVTLNGGEPVDCDGLTRFAEAMA 296
Cdd:cd17630 77 alaedLAPPGVTHVSLvptqlqrLLDSGQGPAA--------------------LKSLRAVLLGGAPIPPELLERAADRGI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 297 PfgfdagaVLPSYGLAESTCAVTVPVPGiglladrvidgsgAHKHAVLGNPIPGMEVRISCGdqaagnasreiGEIEIRG 376
Cdd:cd17630 137 P-------LYTTYGMTETASQVATKRPD-------------GFGRGGVGVLLPGRELRIVED-----------GEIWVGG 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 377 ASMMAGYLGQQPIDP---DDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGD 452
Cdd:cd17630 186 ASLAMGYLRGQLVPEfneDGWFTTKDLGELHADGrLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEE 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489502054 453 RSTRPglVVAAEFRGPdeaNARAELIQRVASECGI--VPSDVVFVSpgSLPRTSSGKLRRLAVRR 515
Cdd:cd17630 266 LGQRP--VAVIVGRGP---ADPAELRAWLKDKLARfkLPKRIYPVP--ELPRTGGGKVDRRALRA 323
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
36-514 |
5.91e-35 |
|
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: 136.54 E-value: 5.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 36 EVHGLAESVAAWLLDH-----DRpaaVGLVGEPTVELVAAIQGAWLAGAAV---SILPGPVRGANDQRWADATlTRFLGI 107
Cdd:cd05936 29 ELDALAEAFAAGLQNLgvqpgDR---VALMLPNCPQFPIAYFGALKAGAVVvplNPLYTPRELEHILNDSGAK-ALIVAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 108 GVRTVLSQGSYLARlrsvdTAGVTIGDLstaahtnrsatpvasegpAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRV 187
Cdd:cd05936 105 SFTDLLAAGAPLGE-----RVALTPEDV------------------AVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 188 GTD-AATDVGCSWLPLYHDMGL-AFVLSAALAGAPLWLAPTtaftASPFRWLSWLSDSGATMTAAPNFAYN-LIGkyARR 264
Cdd:cd05936 162 EDLlEGDDVVLAALPLFHVFGLtVALLLPLALGATIVLIPR----FRPIGVLKEIRKHRVTIFPGVPTMYIaLLN--APE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 265 VSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapFGfdaGAVLPSYGLAESTCAVTV-PVPGigllADRVidGSgahkhav 343
Cdd:cd05936 236 FKKRDFSSLRLCISGGAPLPVEVAERFEEL---TG---VPIVEGYGLTETSPVVAVnPLDG----PRKP--GS------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 344 LGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLGQQPIDP----DDWFATGDLGYLGAGG-LVVCGRAKEVI 418
Cdd:cd05936 297 IGIPLPGTEVKI-VDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAeafvDGWLRTGDIGYMDEDGyFFIVDRKKDMI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 419 SIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRP-GLVVAAEFRGPDEANARAELIQRVAsecGI-VPSDVVFVS 496
Cdd:cd05936 376 IVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVkAFVVLKEGASLTEEEIIAFCREQLA---GYkVPRQVEFRD 452
|
490
....*....|....*...
gi 489502054 497 pgSLPRTSSGKLRRLAVR 514
Cdd:cd05936 453 --ELPKSAVGKILRRELR 468
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
44-508 |
1.04e-33 |
|
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: 133.49 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 44 VAAWLLDHDRpaaVGLVGEPTVELVAAIQGAWLAGAAVSilpgpvrGANDQRwADATLTRFLGI-GVRTVLSQGSYLARL 122
Cdd:cd05911 28 RKLGLKKGDV---VGIISPNSTYYPPVFLGCLFAGGIFS-------AANPIY-TADELAHQLKIsKPKVIFTDPDGLEKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 123 RSVdTAGVTIGD----LSTAAHTNRSATPVASEG------------------PAVLQGTAGSTGAPRTAILSPGAVLSNL 180
Cdd:cd05911 97 KEA-AKELGPKDkiivLDDKPDGVLSIEDLLSPTlgeededlppplkdgkddTAAILYSSGTTGLPKGVCLSHRNLIANL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 181 R-GLNQRVGTDAATDVGCSWLPLYHDMGLAFVLSAALAGAPLWLapTTAFTASPFrwLSWLSDSGATMTAAPNFAYNLIG 259
Cdd:cd05911 176 SqVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVII--MPKFDSELF--LDLIEKYKITFLYLVPPIAAALA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 260 KYARRVSEvDLGALRVTLNGGEPVdcdgLTRFAEAMAPFgFDAGAVLPSYGLAESTCAVTVPVPGiglladrvidgsgAH 339
Cdd:cd05911 252 KSPLLDKY-DLSSLRVILSGGAPL----SKELQELLAKR-FPNATIKQGYGMTETGGILTVNPDG-------------DD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 340 KHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAGYLGQQP-----IDPDDWFATGDLGYLGAGGLV-VCGR 413
Cdd:cd05911 313 KPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEatketFDEDGWLHTGDIGYFDEDGYLyIVDR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 414 AKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPG-LVVaaefRGPDEANARAELI----QRVAS----E 484
Cdd:cd05911 393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRaYVV----RKPGEKLTEKEVKdyvaKKVASykqlR 468
|
490 500
....*....|....*....|....
gi 489502054 485 CGivpsdVVFVSpgSLPRTSSGKL 508
Cdd:cd05911 469 GG-----VVFVD--EIPKSASGKI 485
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-514 |
9.08e-32 |
|
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: 127.56 E-value: 9.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 52 DRPAAVGLVGEPTVELVAAIQGAWLAGAAVSILPGPVRGANDQRWADATLtrflgiGVRTVLSQGSYLARLRSVDTAG-- 129
Cdd:cd05922 19 ERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADA------GGRIVLADAGAADRLRDALPASpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 130 ---VTIGDLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDaATDVGCSWLPLYHDM 206
Cdd:cd05922 93 pgtVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT-ADDRALTVLPLSYDY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 207 GLAFVLSAALAGAPLWLAPTTAFtasPFRWLSWLSDSGATMTAAPNFAYNLIGKYARRVSEvdLGALRVTLNGGEPVDCD 286
Cdd:cd05922 172 GLSVLNTHLLRGATLVLTNDGVL---DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAK--LPSLRYLTQAGGRLPQE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 287 GLTRFAEAMapfgfDAGAVLPSYGLAESTCAVTVpvpgigLLADRVIDGSGAhkhavLGNPIPGMEVRIScGDQAAGNAS 366
Cdd:cd05922 247 TIARLRELL-----PGAQVYVMYGQTEATRRMTY------LPPERILEKPGS-----IGLAIPGGEFEIL-DDDGTPTPP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 367 REIGEIEIRGASMMAGYLGQQPIDPD-----DWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGV 440
Cdd:cd05922 310 GEPGEIVHRGPNVMKGYWNDPPYRRKegrggGVLHTGDLARRDEDGFLfIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489502054 441 REGAVVALgtGDRSTRpGLVVAAEfrGPDEANARAelIQRVASECG---IVPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd05922 390 IEAAAVGL--PDPLGE-KLALFVT--APDKIDPKD--VLRSLAERLppyKVPATVRVVD--ELPLTASGKVDYAALR 457
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
144-510 |
1.32e-31 |
|
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: 126.57 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 144 SATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLR--GLNQRVGTDaatDVGCSWLPLYHDMGL-AFVLSAALAGAP 220
Cdd:cd17631 91 SGAKVLFDDLALLMYTSGTTGRPKGAMLTHRNLLWNAVnaLAALDLGPD---DVLLVVAPLFHIGGLgVFTLPTLLRGGT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 221 LWLAPttAFTASPFrwLSWLSDSGATMTAAPNFAYNLIGKYARRvSEVDLGALRVTLNGGEPVDcdglTRFAEAMAPFGF 300
Cdd:cd17631 168 VVILR--KFDPETV--LDLIERHRVTSFFLVPTMIQALLQHPRF-ATTDLSSLRAVIYGGAPMP----ERLLRALQARGV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 301 DagaVLPSYGLAESTCAVTVpvpgigLLADRVIDGSGAhkhavLGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMM 380
Cdd:cd17631 239 K---FVQGYGMTETSPGVTF------LSPEDHRRKLGS-----AGRPVFFVEVRI-VDPDGREVPPGEVGEIVVRGPHVM 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 381 AGYLGQQPIDP----DDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRST 455
Cdd:cd17631 304 AGYWNRPEATAaafrDGWFHTGDLGRLDEDGYLyIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGE 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489502054 456 RP-GLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRR 510
Cdd:cd17631 384 AVvAVVVPRPGAELDEDELIAHCRERLARY--KIPKSVEFVD--ALPRNATGKILK 435
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
148-510 |
1.05e-30 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 123.61 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 148 VASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATdvgcSWL---PLYHDMGLAFVLSAALAGAPLWLA 224
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDD----NWLcalPLFHISGLSILMRSVIYGMTVYLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 225 PttAFTASPFRWLswLSDSGATM-TAAPNFAYNLIGKYARRVSEvdlgALRVTLNGGEPVDCDGLTRFAEAMAPfgfdag 303
Cdd:cd05912 150 D--KFDAEQVLHL--INSGKVTIiSVVPTMLQRLLEILGEGYPN----NLRCILLGGGPAPKPLLEQCKEKGIP------ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 304 aVLPSYGLAEsTC--AVTVPvpgIGLLADRVidGSgahkhavLGNPIPGMEVRIscgdQAAGNASREIGEIEIRGASMMA 381
Cdd:cd05912 216 -VYQSYGMTE-TCsqIVTLS---PEDALNKI--GS-------AGKPLFPVELKI----EDDGQPPYEVGEILLKGPNVTK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 382 GYLGQQPIDP----DDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTR 456
Cdd:cd05912 278 GYLNRPDATEesfeNGWFKTGDIGYLDEEGfLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQV 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489502054 457 PGLVVAAEfRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRR 510
Cdd:cd05912 358 PVAFVVSE-RPISEEELIAYCSEKLAKY--KVPKKIYFVD--ELPRTASGKLLR 406
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
137-514 |
4.39e-30 |
|
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: 123.19 E-value: 4.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 137 TAAHTNRSATPVASEG-PAVLQGTAGSTGAPRTAILSPGAVLSNLRG------LNQRvgtDAATDVgcswLPLYHDMGLA 209
Cdd:cd05926 134 LADKKNAKSEGVPLPDdLALILHTSGTTGRPKGVPLTHRNLAASATNitntykLTPD---DRTLVV----MPLFHVHGLV 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 210 FVLSAAL-AGAPLWLAPttAFTASPFrWlSWLSDSGAT-MTAAPNFAYNLIGKYARRVSEVdLGALRVTLNGGEPVDCDG 287
Cdd:cd05926 207 ASLLSTLaAGGSVVLPP--RFSASTF-W-PDVRDYNATwYTAVPTIHQILLNRPEPNPESP-PPKLRFIRSCSASLPPAV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 288 LTRFAEAmapfgFDAGaVLPSYGLAESTCAVTV-PVPGiglladrvidgsGAHKHAVLGNPIpGMEVRIsCGDQAAGNAS 366
Cdd:cd05926 282 LEALEAT-----FGAP-VLEAYGMTEAAHQMTSnPLPP------------GPRKPGSVGKPV-GVEVRI-LDEDGEILPP 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 367 REIGEIEIRGASMMAGYLG-----QQPIDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGV 440
Cdd:cd05926 342 GVVGEICLRGPNVTRGYLNnpeanAEAAFKDGWFRTGDLGYLDADGyLFLTGRIKELINRGGEKISPLEVDGVLLSHPAV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 441 REGAVVALgtgdrstrPG-----LVVAAEFRGPDEANARAELIQRVASECGI--VPSDVVFVSpgSLPRTSSGKLRRLAV 513
Cdd:cd05926 422 LEAVAFGV--------PDekygeEVAAAVVLREGASVTEEELRAFCRKHLAAfkVPKKVYFVD--ELPKTATGKIQRRKV 491
|
.
gi 489502054 514 R 514
Cdd:cd05926 492 A 492
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
34-515 |
3.99e-29 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 120.99 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 34 WPEVHGLAESVAAWLLDH-----DRpaaVGLVGEPTVELVAAIQGAWLAGAAVSILPGPVRgandqrwADATLTRFLGIG 108
Cdd:COG0365 42 YAELRREVNRFANALRALgvkkgDR---VAIYLPNIPEAVIAMLACARIGAVHSPVFPGFG-------AEALADRIEDAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 109 VRTVLSQGSYLARLRSVDTAG---------------VTIG---------------DLSTAAHTNRSATPVASEGPAVLQG 158
Cdd:COG0365 112 AKVLITADGGLRGGKVIDLKEkvdealeelpslehvIVVGrtgadvpmegdldwdELLAAASAEFEPEPTDADDPLFILY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRV----GTD---AATDVGcsWLplyhdMGLAFVLSAALA-GAPLWLAPTTAFT 230
Cdd:COG0365 192 TSGTTGKPKGVVHTHGGYLVHAATTAKYVldlkPGDvfwCTADIG--WA-----TGHSYIVYGPLLnGATVVLYEGRPDF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 231 ASPFRWLSWLSDSGAT-MTAAPNFAYNLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapFGFDagaVLPSY 309
Cdd:COG0365 265 PDPGRLWELIEKYGVTvFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEA---VGVP---IVDGW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 310 GLAESTCAVTVPVPGigllaDRVIDGSgahkhavLGNPIPGMEVRI--SCGDQAAGNasrEIGEIEIRGA--SMMAGYLG 385
Cdd:COG0365 339 GQTETGGIFISNLPG-----LPVKPGS-------MGKPVPGYDVAVvdEDGNPVPPG---EEGELVIKGPwpGMFRGYWN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 386 qqpiDPD-----------DWFATGDLGYLGA-GGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDR 453
Cdd:COG0365 404 ----DPEryretyfgrfpGWYRTGDGARRDEdGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIR 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489502054 454 STRP-GLVVAAEFRGPDEAnARAELIQRVASECGI--VPSDVVFVSpgSLPRTSSGKLRRLAVRR 515
Cdd:COG0365 480 GQVVkAFVVLKPGVEPSDE-LAKELQAHVREELGPyaYPREIEFVD--ELPKTRSGKIMRRLLRK 541
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
159-517 |
1.20e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 119.14 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQ--RVGTDaatDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPttAFTASPFrw 236
Cdd:PRK06187 175 TSGTTGHPKGVVLSHRNLFLHSLAVCAwlKLSRD---DVYLVIVPMFHVHAWGLPYLALMAGAKQVIPR--RFDPENL-- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 237 LSWLSDSGATMTAAPNFAYNLIGKYaRRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapFGFDagaVLPSYGLAESTC 316
Cdd:PRK06187 248 LDLIETERVTFFFAVPTIWQMLLKA-PRAYFVDFSSLRLVIYGGAALPPALLREFKEK---FGID---LVQGYGMTETSP 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 317 AVTVPVPGIGLLADRVIDGSgahkhavLGNPIPGMEVRISCGD-QAAGNASREIGEIEIRGASMMAGYLGQQPIDP---- 391
Cdd:PRK06187 321 VVSVLPPEDQLPGQWTKRRS-------AGRPLPGVEARIVDDDgDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAetid 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 392 DDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVValGTGDRST--RPG-LVVAAEFRG 467
Cdd:PRK06187 394 GGWLHTGDVGYIDEDGyLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI--GVPDEKWgeRPVaVVVLKPGAT 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489502054 468 PDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVRRSL 517
Cdd:PRK06187 472 LDAKELRAFLRGRLAKF--KLPKRIAFVD--ELPRTSVGKILKRVLREQY 517
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
151-510 |
1.30e-28 |
|
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: 116.21 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 151 EGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTAFT 230
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 231 ASPFRWLSWLSDSGATMTaaPNFAYNLIGKYARRVSEVDlgALRVTLNGGE-PVDCDglTRFAEAmapfgFDAGAVLPSY 309
Cdd:cd17635 81 KSLFKILTTNAVTTTCLV--PTLLSKLVSELKSANATVP--SLRLIGYGGSrAIAAD--VRFIEA-----TGLTNTAQVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 310 GLAESTCAVTVPVpgiglladrvidGSGAHKHAVLGNPIPGMEVRISCGDQAAGnASREIGEIEIRGASMMAGYLGQQPI 389
Cdd:cd17635 150 GLSETGTALCLPT------------DDDSIEINAVGRPYPGVDVYLAATDGIAG-PSASFGTIWIKSPANMLGYWNNPER 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 390 DPD----DWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGL-VVAA 463
Cdd:cd17635 217 TAEvlidGWVNTGDLGERREDGfLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLaVVAS 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 489502054 464 EFRGPDEANARAELIQRvASECGIVPSDVVFVSpgSLPRTSSGKLRR 510
Cdd:cd17635 297 AELDENAIRALKHTIRR-ELEPYARPSTIVIVT--DIPRTQSGKVKR 340
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
21-512 |
4.82e-28 |
|
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: 116.47 E-value: 4.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 21 VLDRETSLWCRhpwpEVHGLAESVAAWLLDHD--RPAAVGLVGEPTVELVAAIQGAWLAGAA-VSIlpgpvrganDQRWA 97
Cdd:cd05930 6 VVDGDQSLTYA----ELDARANRLARYLRERGvgPGDLVAVLLERSLEMVVAILAVLKAGAAyVPL---------DPSYP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 98 DATLTRFLG-IGVRTVLSQGSYLArlrsvdtagvtigdlstaahtnrsatpvasegpAVLQgTAGSTGAPRTAILSPGAV 176
Cdd:cd05930 73 AERLAYILEdSGAKLVLTDPDDLA---------------------------------YVIY-TSGSTGKPKGVMVEHRGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 177 LSNLRGLNQRVGTDAaTDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTAfTASPFRWLSWLSDSGATMTAAPNFAYN 256
Cdd:cd05930 119 VNLLLWMQEAYPLTP-GDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEV-RKDPEALADLLAEEGITVLHLTPSLLR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 257 LIGKYArrvSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapfgFDAGAVLPSYGLAESTCAVTVpvpgiglladRVIDGS 336
Cdd:cd05930 197 LLLQEL---ELAALPSLRLVLVGGEALPPDLVRRWREL-----LPGARLVNLYGPTEATVDATY----------YRVPPD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 337 GAHKHAV-LGNPIPGMEVRI---SCGDQAAGnasrEIGEIEIRGASMMAGYLGQQ----------PIDPDDW-FATGDLG 401
Cdd:cd05930 259 DEEDGRVpIGRPIPNTRVYVldeNLRPVPPG----VPGELYIGGAGLARGYLNRPeltaerfvpnPFGPGERmYRTGDLV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 402 -YLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRpgL---VVAAEFRGPDEANARAEL 477
Cdd:cd05930 335 rWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKR--LvayVVPDEGGELDEEELRAHL 412
|
490 500 510
....*....|....*....|....*....|....*
gi 489502054 478 IQRVASecGIVPSDVVFVSpgSLPRTSSGKLRRLA 512
Cdd:cd05930 413 AERLPD--YMVPSAFVVLD--ALPLTPNGKVDRKA 443
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
153-514 |
6.83e-27 |
|
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: 112.86 E-value: 6.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 153 PAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAAtDVGCSWLPLYHDMGLAF-VLSAALAGAPLWLAPTTafta 231
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG-DVFLVASPMAHQTGFVYgFTLPLLLGAPVVLQDIW---- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 232 SPFRWLSWLSDSGAT-MTAAPNFAYNLIgKYARRVSEvDLGALRVTLNGGEPVDCDGLTRFAEAMAPFgfdagaVLPSYG 310
Cdd:cd05903 170 DPDKALALMREHGVTfMMGATPFLTDLL-NAVEEAGE-PLSRLRTFVCGGATVPRSLARRAAELLGAK------VCSAYG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 311 LAESTCAVTVPVPGIGLLADRViDGsgahkhavlgNPIPGMEVRIScGDQAAGNASREIGEIEIRGASMMAGYLGQQPI- 389
Cdd:cd05903 242 STECPGAVTSITPAPEDRRLYT-DG----------RPLPGVEIKVV-DDTGATLAPGVEGELLSRGPSVFLGYLDRPDLt 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 390 ---DPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALG---TGDRSTrpGLVVA 462
Cdd:cd05903 310 adaAPEGWFRTGDLARLDEDGyLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPderLGERAC--AVVVT 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489502054 463 AEFRGPDEANARAELI-QRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd05903 388 KSGALLTFDELVAYLDrQGVAKQ--YWPERLVHVD--DLPRTPSGKVQKFRLR 436
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
56-514 |
1.58e-26 |
|
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: 112.44 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 56 AVGLVGEPTVELVAAIQGAWLAGAAVSILpgpvrganDQRWADATLTRFLG-IGVRTVLSQGSYLARLrSVDTAGVTIGD 134
Cdd:cd17651 47 LVALCARRSAELVVALLAILKAGAAYVPL--------DPAYPAERLAFMLAdAGPVLVLTHPALAGEL-AVELVAVTLLD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 135 LSTAAHTNRSATPVASEG--PAVLQGTAGSTGAPRtAILSPGAVLSNLRGLNQRVGTDAATDVGCSWLPLYHDMGLAFVL 212
Cdd:cd17651 118 QPGAAAGADAEPDPALDAddLAYVIYTSGSTGRPK-GVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 213 SAALAGAPLWLAPTTAFTaSPFRWLSWLSDSGATMTAAPNFAYNLIGKYARRVSeVDLGALRVTLNGGEPVDCDGLTRFA 292
Cdd:cd17651 197 STLCAGATLVLPPEEVRT-DPPALAAWLDEQRISRVFLPTVALRALAEHGRPLG-VRLAALRYLLTGGEQLVLTEDLREF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 293 EAMAPFGfdagAVLPSYGLAESTCAVTVPVPGiglladrviDGSGAHKHAVLGNPIPGMEVRISCGDQAAGNASREiGEI 372
Cdd:cd17651 275 CAGLPGL----RLHNHYGPTETHVVTALSLPG---------DPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVP-GEL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 373 EIRGASMMAGYLGQ-----QPIDPDDWFA------TGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGV 440
Cdd:cd17651 341 YIGGAGLARGYLNRpeltaERFVPDPFVPgarmyrTGDLArWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGV 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489502054 441 REGAVVALgtGDRSTRPGLV---VAAEFRGPDEANARAELIQRVASEcgIVPSdvVFVSPGSLPRTSSGKLRRLAVR 514
Cdd:cd17651 421 REAVVLAR--EDRPGEKRLVayvVGDPEAPVDAAELRAALATHLPEY--MVPS--AFVLLDALPLTPNGKLDRRALP 491
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
151-460 |
2.75e-26 |
|
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: 111.53 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 151 EGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAaTDVGCSWLPLYHDMGLAFVLSAAL-AGAplwlapTTAF 229
Cdd:cd05907 87 DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE-GDRHLSFLPLAHVFERRAGLYVPLlAGA------RIYF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 230 TASPFRWLSWLSDSGAT-MTAAPNFaYNLIGKYARRVSEVDL----------GALRVTLNGGEPVDCDgLTRFAEAMapf 298
Cdd:cd05907 160 ASSAETLLDDLSEVRPTvFLAVPRV-WEKVYAAIKVKAVPGLkrklfdlavgGRLRFAASGGAPLPAE-LLHFFRAL--- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 299 GFDagaVLPSYGLAESTCAVTVPVPGiglladrvidgsgAHKHAVLGNPIPGMEVRIScgdqaagnasrEIGEIEIRGAS 378
Cdd:cd05907 235 GIP---VYEGYGLTETSAVVTLNPPG-------------DNRIGTVGKPLPGVEVRIA-----------DDGEILVRGPN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 379 MMAGYLGQ-----QPIDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIA-GRNIFPTEVELVAAQVRGVREGAVValgtG 451
Cdd:cd05907 288 VMLGYYKNpeataEALDADGWLHTGDLGEIDEDGfLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVI----G 363
|
....*....
gi 489502054 452 DRstRPGLV 460
Cdd:cd05907 364 DG--RPFLV 370
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
153-507 |
4.39e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 110.46 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 153 PAVLQGTAGSTGAPRtAILSPGAVLSNLRGLNQRVGTDAATDVGCSWLPLYHDMGLAF-VLSAALAGAPLWLAPTtaFTA 231
Cdd:cd05934 83 PASILYTSGTTGPPK-GVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVsVLAALSVGATLVLLPR--FSA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 232 SpfRWLSWLSDSGATMTaapnfayNLIGK-----YARRVSEVDlGALRVTLNGGEPVDCDGLTRFAEAmapFGFdagAVL 306
Cdd:cd05934 160 S--RFWSDVRRYGATVT-------NYLGAmlsylLAQPPSPDD-RAHRLRAAYGAPNPPELHEEFEER---FGV---RLL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 307 PSYGLAESTCAVTVPVPGiglladRVIDGSgahkhavLGNPIPGMEVRIScGDQAAGNASREIGEIEIRGA---SMMAGY 383
Cdd:cd05934 224 EGYGMTETIVGVIGPRDE------PRRPGS-------IGRPAPGYEVRIV-DDDGQELPAGEPGELVIRGLrgwGFFKGY 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 384 LGqqpiDPDD--------WFATGDLGYLGA-GGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALG---TG 451
Cdd:cd05934 290 YN----MPEAtaeamrngWFHTGDLGYRDAdGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPdevGE 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489502054 452 DRStrPGLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGK 507
Cdd:cd05934 366 DEV--KAVVVLRPGETLDPEELFAFCEGQLAYF--KVPRYIRFVD--DLPKTPTEK 415
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
154-510 |
4.11e-25 |
|
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: 107.91 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLRGLnQRVGTDAATDVGCSWLPLYHDMGLAF-VLSAALAGAPLWL---APTTAF 229
Cdd:cd05914 92 ALINYTSGTTGNSKGVMLTYRNIVSNVDGV-KEVVLLGKGDKILSILPLHHIYPLTFtLLLPLLNGAHVVFldkIPSAKI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 230 TASPFRWLS--------WLSDSGATMTAAPNFA-----------------YNLIGKyarRVSEVDLGALRVTLNGGEPVD 284
Cdd:cd05914 171 IALAFAQVTptlgvpvpLVIEKIFKMDIIPKLTlkkfkfklakkinnrkiRKLAFK---KVHEAFGGNIKEFVIGGAKIN 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 285 CDGLTRFAEAMAPFgfdagavLPSYGLAESTCAVTVPVPGiglladRVIDGSGahkhavlGNPIPGMEVRISCGDQAAGN 364
Cdd:cd05914 248 PDVEEFLRTIGFPY-------TIGYGMTETAPIISYSPPN------RIRLGSA-------GKVIDGVEVRIDSPDPATGE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 365 asreiGEIEIRGASMMAGY-----LGQQPIDPDDWFATGDLGYLGAGG-LVVCGRAKEVI-SIAGRNIFPTEVE------ 431
Cdd:cd05914 308 -----GEIIVRGPNVMKGYyknpeATAEAFDKDGWFHTGDLGKIDAEGyLYIRGRKKEMIvLSSGKNIYPEEIEakinnm 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 432 -LVAAQVRGVREGAVVALGT--GDRSTRPGLVVAAEFRGPDEANaRAELIQRVASECGIvpSDVVFVsPGSLPRTSSGKL 508
Cdd:cd05914 383 pFVLESLVVVQEKKLVALAYidPDFLDVKALKQRNIIDAIKWEV-RDKVNQKVPNYKKI--SKVKIV-KEEFEKTPKGKI 458
|
..
gi 489502054 509 RR 510
Cdd:cd05914 459 KR 460
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
41-513 |
1.27e-24 |
|
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: 106.56 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 41 AESVAAWLLDHDRPA--AVGLVGEPTVELVAAIQGAWLAGAAVSilpgPVRGandqrwadatltrflgigvrtvlsqGSY 118
Cdd:cd05945 26 ADALAAALASLGLDAgdPVVVYGHKSPDAIAAFLAALKAGHAYV----PLDA-------------------------SSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 119 LARLRSV-DTAGVTigdlstaahtnrsATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQR--VGTDaatDV 195
Cdd:cd05945 77 AERIREIlDAAKPA-------------LLIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDfpLGPG---DV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 196 GCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTAfTASPFRWLSWLSDSGATM-TAAPNFAYNLIGKYARRVSEvdLGALR 274
Cdd:cd05945 141 FLNQAPFSFDLSVMDLYPALASGATLVPVPRDA-TADPKQLFRFLAEHGITVwVSTPSFAAMCLLSPTFTPES--LPSLR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 275 VTLNGGEPVDCDGLTRFAEAmapfgFDAGAVLPSYGLAESTCAVTvpvpgigllaDRVIDGSGAHKHAVL--GNPIPGME 352
Cdd:cd05945 218 HFLFCGEVLPHKTARALQQR-----FPDARIYNTYGPTEATVAVT----------YIEVTPEVLDGYDRLpiGYAKPGAK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 353 VRISCGDQAAgNASREIGEIEIRGASMMAGYLG-----QQPIDPDD---WFATGDLGYLGAGGLVV-CGRAKEVISIAGR 423
Cdd:cd05945 283 LVILDEDGRP-VPPGEKGELVISGPSVSKGYLNnpektAAAFFPDEgqrAYRTGDLVRLEADGLLFyRGRLDFQVKLNGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 424 NIFPTEVELVAAQVRGVREGAVVALGTGDrsTRPGLVVAAEFRGPDEanarAELIQRVASECG------IVPSDVVFVSp 497
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVVPKYKGE--KVTELIAFVVPKPGAE----AGLTKAIKAELAerlppyMIPRRFVYLD- 434
|
490
....*....|....*.
gi 489502054 498 gSLPRTSSGKLRRLAV 513
Cdd:cd05945 435 -ELPLNANGKIDRKAL 449
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
147-508 |
2.07e-24 |
|
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: 106.26 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 147 PVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVgtDAAT-DVGCSWLPLYHDMGLAF-VLSAALAGAPLWLA 224
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIF--DPNPeDVVFGALPFFHSFGLTGcLWLPLLSGIKVVFH 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 225 --PTTAFTASPFrwlswLSDSGAT-MTAAPNFaynlIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapFGFd 301
Cdd:cd05909 221 pnPLDYKKIPEL-----IYDKKATiLLGTPTF----LRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEK---FGI- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 302 agAVLPSYGLAESTCAVTVPVPGIglladrvidgsgAHKHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMA 381
Cdd:cd05909 288 --RILEGYGTTECSPVISVNTPQS------------PNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVML 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 382 GYLG----QQPIDPDDWFATGDLGYL-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGvREGAVVALGTGDrsTR 456
Cdd:cd05909 354 GYLNepelTSFAFGDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILP-EDNEVAVVSVPD--GR 430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 457 PG----LVVAAEFRGPDEanaraelIQRVASECGI----VPSDVVFVSpgSLPRTSSGKL 508
Cdd:cd05909 431 KGekivLLTTTTDTDPSS-------LNDILKNAGIsnlaKPSYIHQVE--EIPLLGTGKP 481
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
36-510 |
2.79e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 105.81 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 36 EVHGLAESVAAWL--LDHDRPAAVGLVGEPTVELVAAIQGAWLAGAAVSILPgpVR-GANDQRW--ADAtltrflgiGVR 110
Cdd:PRK03640 32 ELHEAVVSVAGKLaaLGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN--TRlSREELLWqlDDA--------EVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 111 TVLSQGSYLARLRSVDTagVTIGDLSTAAHtnRSATPVAS---EGPAVLQGTAGSTGAPRTAILSPG-----AVLS--NL 180
Cdd:PRK03640 102 CLITDDDFEAKLIPGIS--VKFAELMNGPK--EEAEIQEEfdlDEVATIMYTSGTTGKPKGVIQTYGnhwwsAVGSalNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 181 rGLNQRvgtdaatDvgcSWL---PLYHDMGLAFVLSAALAGAPLWLAPttAFTASPF-RWLswLSDSGATMTAAPNFAYN 256
Cdd:PRK03640 178 -GLTED-------D---CWLaavPIFHISGLSILMRSVIYGMRVVLVE--KFDAEKInKLL--QTGGVTIISVVSTMLQR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 257 LIGKY-ARRVSEvdlgALRVTLNGGEPVDCDGLTRFAEAMAPfgfdagaVLPSYGLAEsTCA--VTVPVPGIglladrvi 333
Cdd:PRK03640 243 LLERLgEGTYPS----SFRCMLLGGGPAPKPLLEQCKEKGIP-------VYQSYGMTE-TASqiVTLSPEDA-------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 334 dgsgAHKHAVLGNPIPGMEVRIScgDQAAGNASREIGEIEIRGASMMAGYLGQ-----QPIDpDDWFATGDLGYLGAGG- 407
Cdd:PRK03640 303 ----LTKLGSAGKPLFPCELKIE--KDGVVVPPFEEGEIVVKGPNVTKGYLNRedatrETFQ-DGWFKTGDIGYLDEEGf 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 408 LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVValGTGDRstRPGLVVAAEF---RGPDEANARAELIQRVASE 484
Cdd:PRK03640 376 LYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV--GVPDD--KWGQVPVAFVvksGEVTEEELRHFCEEKLAKY 451
|
490 500
....*....|....*....|....*.
gi 489502054 485 cgIVPSDVVFVSpgSLPRTSSGKLRR 510
Cdd:PRK03640 452 --KVPKRFYFVE--ELPRNASGKLLR 473
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
153-515 |
9.59e-24 |
|
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: 103.91 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 153 PAVLQGTAGSTGAPRTAILSPGAVLSNLRGLnqrvgTDA----ATDVGCSWLPLYHDMGLAFVLSAAL-AGAPLWLAPTt 227
Cdd:cd05941 91 PALILYTSGTTGRPKGVVLTHANLAANVRAL-----VDAwrwtEDDVLLHVLPLHHVHGLVNALLCPLfAGASVEFLPK- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 228 aFTASPfrWLSWLSDSGATM-TAAPNFAYNLIGKYARRVSEVD------LGALRVTLNGGEPVDCDGLTRFAEAMAPFgf 300
Cdd:cd05941 165 -FDPKE--VAISRLMPSITVfMGVPTIYTRLLQYYEAHFTDPQfaraaaAERLRLMVSGSAALPVPTLEEWEAITGHT-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 301 dagaVLPSYGLAESTCAVTVPvpgigLLADRvIDGSgahkhavLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMM 380
Cdd:cd05941 240 ----LLERYGMTEIGMALSNP-----LDGER-RPGT-------VGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVF 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 381 AGYLgQQP------IDPDDWFATGDLGYLGAGGLV-VCGRAK-EVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGD 452
Cdd:cd05941 303 KEYW-NKPeatkeeFTDDGWFKTGDLGVVDEDGYYwILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPD 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489502054 453 RSTRPGLVVA--AEFRGPDEANARAELIQRVASECgiVPSDVVFVSpgSLPRTSSGKLRRLAVRR 515
Cdd:cd05941 382 WGERVVAVVVlrAGAAALSLEELKEWAKQRLAPYK--RPRRLILVD--ELPRNAMGKVNKKELRK 442
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
135-514 |
1.56e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 103.83 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 135 LSTAAHTNRSAtPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSwLPLYHDMGLAFVLSA 214
Cdd:PRK07656 151 LAAGDPAERAP-EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAA-NPFFHVFGYKAGVNA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 215 AL-AGAPLWLAPTtaFtaSPFRWLSWLSDSGATMTAAPNFAYNLIGKYARRvSEVDLGALRVTLNGGEPVDCDGLTRFAE 293
Cdd:PRK07656 229 PLmRGATILPLPV--F--DPDEVFRLIETERITVLPGPPTMYNSLLQHPDR-SAEDLSSLRLAVTGAASMPVALLERFES 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 294 AmapFGFDAgaVLPSYGLAESTCAVTVPVPGigllADRV-IDGSgahkhavLGNPIPGMEVRIScGDQAAGNASREIGEI 372
Cdd:PRK07656 304 E---LGVDI--VLTGYGLSEASGVTTFNRLD----DDRKtVAGT-------IGTAIAGVENKIV-NELGEEVPVGEVGEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 373 EIRGASMMAGYLgQQP------IDPDDWFATGDLGYLG-AGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAV 445
Cdd:PRK07656 367 LVRGPNVMKGYY-DDPeataaaIDADGWLHTGDLGRLDeEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAV 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489502054 446 ValGTGDrsTRPGLVVAAeF--RGPDEANARAELIQ----RVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:PRK07656 446 I--GVPD--ERLGEVGKA-YvvLKPGAELTEEELIAycreHLAKY--KVPRSIEFLD--ELPKNATGKVLKRALR 511
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
40-445 |
1.77e-23 |
|
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: 102.34 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 40 LAESVAAWLLDHDRPAA---VGLVGEPTVELVAAIQGAWLAGAA-VSIlpgpvrganDQRWADATLTRFLG-IGVRTVLS 114
Cdd:TIGR01733 8 RANRLARHLRAAGGVGPgdrVAVLLERSAELVVAILAVLKAGAAyVPL---------DPAYPAERLAFILEdAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 115 QGSYLARLRSVDTAGVTIGDLSTAAHTNRSATPVASEGP-----AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGT 189
Cdd:TIGR01733 79 DSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSgpddlAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 190 DAATdvgcSWL---PLYHDMGLAFVLSAALAGAPLWLAPTTAFTASPFRWLSWLSDSGATMTAAPNFAYNLIgkyaRRVS 266
Cdd:TIGR01733 159 DPDD----RVLqfaSLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL----AAAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 267 EVDLGALRVTLNGGEPVDCDGLTRFAEAmapfgFDAGAVLPSYGLAESTCAVT---VPVPGIGLLADRVIdgsgahkhav 343
Cdd:TIGR01733 231 PPALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLYGPTETTVWSTatlVDPDDAPRESPVPI---------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 344 lGNPIPGMEVRISCGDQ---AAGnasrEIGEIEIRGASMMAGYLGQ----------QPIDPDD---WFATGDLG-YLGAG 406
Cdd:TIGR01733 296 -GRPLANTRLYVLDDDLrpvPVG----VVGELYIGGPGVARGYLNRpeltaerfvpDPFAGGDgarLYRTGDLVrYLPDG 370
|
410 420 430
....*....|....*....|....*....|....*....
gi 489502054 407 GLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAV 445
Cdd:TIGR01733 371 NLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
148-518 |
1.31e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 101.23 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 148 VASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLR-GLNQRVGTDAATDVGCSWLPLYHDMGLAFVLSAALA-GAPLWLAP 225
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqGKAWVPGLGDGPERVLAALPMFHAYGLTLCLTLAVSiGGELVLLP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 226 T-------TAFTASPFRWlswlsdsgatMTAAPNFaYNLIGKYARRvSEVDLGALRVTLNGGEPVDCDGLTRFAEAMApf 298
Cdd:PRK05605 296 ApdidlilDAMKKHPPTW----------LPGVPPL-YEKIAEAAEE-RGVDLSGVRNAFSGAMALPVSTVELWEKLTG-- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 299 gfdaGAVLPSYGLAEstcavTVPVpgigLLADRVidgSGAHKHAVLGNPIPGMEVRISCGDqaagNASR-----EIGEIE 373
Cdd:PRK05605 362 ----GLLVEGYGLTE-----TSPI----IVGNPM---SDDRRPGYVGVPFPDTEVRIVDPE----DPDEtmpdgEEGELL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 374 IRGASMMAGYLGQ----QPIDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVAL 448
Cdd:PRK05605 422 VRGPQVFKGYWNRpeetAKSFLDGWFRTGDVVVMEEDGFIrIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGL 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489502054 449 GTGDRSTRpglVVAAEFRGP----DEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVRRSLE 518
Cdd:PRK05605 502 PREDGSEE---VVAAVVLEPgaalDPEGLRAYCREHLTRY--KVPRRFYHVD--ELPRDQLGKVRRREVREELL 568
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
4-431 |
1.66e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 100.95 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 4 LAAVLTRSMQASAGDLMVLDRETSLWCRHPWPEVHGLAESVAAWLLDH-----DRpaaVGLVGEPTVELVAAIQGAWLAG 78
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALgvkpgDR---VAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 79 AA-VSIlpGPVRGANDQRW----ADATL----TRFLgigVRTVLSQGSYLARLRSV----------DTAGVTIGDL---- 135
Cdd:COG1022 90 AVtVPI--YPTSSAEEVAYilndSGAKVlfveDQEQ---LDKLLEVRDELPSLRHIvvldprglrdDPRLLSLDELlalg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 136 ----STAAHTNRSATpVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAaTDVGCSWLPLYHDMGLAFV 211
Cdd:COG1022 165 revaDPAELEARRAA-VKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP-GDRTLSFLPLAHVFERTVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 212 LSAALAGAPLWLAPT-------------TAFTASP------------------------FRWLSWLS-------DSGATM 247
Cdd:COG1022 243 YYALAAGATVAFAESpdtlaedlrevkpTFMLAVPrvwekvyagiqakaeeagglkrklFRWALAVGrryararLAGKSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 248 TAAPNFAYNLIGKY-ARRVSEVdLGA-LRVTLNGGEPVDCDgLTRFAEAMapfGFDagaVLPSYGLAESTCAVTVPVPGi 325
Cdd:COG1022 323 SLLLRLKHALADKLvFSKLREA-LGGrLRFAVSGGAALGPE-LARFFRAL---GIP---VLEGYGLTETSPVITVNRPG- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 326 glladRVIDGSgahkhavLGNPIPGMEVRIScgdqaagnasrEIGEIEIRGASMMAGYLG-----QQPIDPDDWFATGDL 400
Cdd:COG1022 394 -----DNRIGT-------VGPPLPGVEVKIA-----------EDGEILVRGPNVMKGYYKnpeatAEAFDADGWLHTGDI 450
|
490 500 510
....*....|....*....|....*....|...
gi 489502054 401 GYLGAGG-LVVCGRAKEVISIA-GRNIFPTEVE 431
Cdd:COG1022 451 GELDEDGfLRITGRKKDLIVTSgGKNVAPQPIE 483
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
108-510 |
2.49e-22 |
|
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: 100.00 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 108 GVRTVLSQGSYLARLRSVDTAGVTIGD-----------LSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAV 176
Cdd:cd05904 104 GAKLAFTTAELAEKLASLALPVVLLDSaefdslsfsdlLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 177 LSNLRGLNQRVG-TDAATDVGCSWLPLYHDMGLAFVLSAALAgaplwlapttaftaspfrwlswlsdSGATMTAAPNF-- 253
Cdd:cd05904 184 IAMVAQFVAGEGsNSDSEDVFLCVLPMFHIYGLSSFALGLLR-------------------------LGATVVVMPRFdl 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 254 --AYNLIGKY-----------------ARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapfgFDAGAVLPSYGLAES 314
Cdd:cd05904 239 eeLLAAIERYkvthlpvvppivlalvkSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAK-----FPNVDLGQGYGMTES 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 315 TCAVTVPVPGIGllaDRVIDGSgahkhavLGNPIPGMEVRIScgDQAAGNA--SREIGEIEIRGASMMAGYLG-----QQ 387
Cdd:cd05904 314 TGVVAMCFAPEK---DRAKYGS-------VGRLVPNVEAKIV--DPETGESlpPNQTGELWIRGPSIMKGYLNnpeatAA 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 388 PIDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPG-LVVaaef 465
Cdd:cd05904 382 TIDKEGWLHTGDLCYIDEDGyLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMaFVV---- 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 489502054 466 RGPDEANARAELIQRVASEcgIVP----SDVVFVSpgSLPRTSSGK-LRR 510
Cdd:cd05904 458 RKPGSSLTEDEIMDFVAKQ--VAPykkvRKVAFVD--AIPKSPSGKiLRK 503
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
159-517 |
7.93e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 98.97 E-value: 7.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVGTdAATDVGCSWLPLYHDMGLAFVLSAalagaPLWLAPTTAF--TASPFRW 236
Cdd:PRK13295 205 TSGTTGEPKGVMHTANTLMANIVPYAERLGL-GADDVILMASPMAHQTGFMYGLMM-----PVMLGATAVLqdIWDPARA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 237 LSWLSDSGATMT-AAPNFAYNLIGkyARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMapfgfdaGA-VLPSYGLAEs 314
Cdd:PRK13295 279 AELIRTEGVTFTmASTPFLTDLTR--AVKESGRPVSSLRTFLCAGAPIPGALVERARAAL-------GAkIVSAWGMTE- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 315 TCAVTVPVPGIgllADRVIDGSGahkhavlGNPIPGMEVRISCGDQAAGNASrEIGEIEIRGASMMAGYLGQQPI---DP 391
Cdd:PRK13295 349 NGAVTLTKLDD---PDERASTTD-------GCPLPGVEVRVVDADGAPLPAG-QIGRLQVRGCSNFGGYLKRPQLngtDA 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 392 DDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGT---GDR-----STRPGlvva 462
Cdd:PRK13295 418 DGWFDTGDLARIDADGYIrISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDerlGERacafvVPRPG---- 493
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489502054 463 aefRGPDEANARAEL-IQRVASEcgIVPSDVVFVspGSLPRTSSGKLRRLAVRRSL 517
Cdd:PRK13295 494 ---QSLDFEEMVEFLkAQKVAKQ--YIPERLVVR--DALPRTPSGKIQKFRLREML 542
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
334-510 |
8.11e-22 |
|
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: 96.32 E-value: 8.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 334 DGSGAHKHAVlGNPIPGMEVRIScgDQAAGnasrEIGEIEIRGASMMAGYLGQQPIDPDDWFATGDLGYLGAGG-LVVCG 412
Cdd:cd17633 156 NQESRPPNSV-GRPFPNVEIEIR--NADGG----EIGKIFVKSEMVFSGYVRGGFSNPDGWMSVGDIGYVDEEGyLYLVG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 413 RAKEVISIAGRNIFPTEVELVAAQVRGVREGAVValgtGDRSTRPGLVVAAEFRGpDEANARAELI---QRVASEcgIVP 489
Cdd:cd17633 229 RESDMIIIGGINIFPTEIESVLKAIPGIEEAIVV----GIPDARFGEIAVALYSG-DKLTYKQLKRflkQKLSRY--EIP 301
|
170 180
....*....|....*....|.
gi 489502054 490 SDVVFVSpgSLPRTSSGKLRR 510
Cdd:cd17633 302 KKIIFVD--SLPYTSSGKIAR 320
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
147-514 |
5.96e-21 |
|
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: 95.78 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 147 PVASEG-PAVLQGTAGSTGAP-------RTAIL-SPGAVLSNLRGLNQRvgtdaatDVGCSWLPLYHDM--GLAFvlSAA 215
Cdd:cd12119 158 PDFDENtAAAICYTSGTTGNPkgvvyshRSLVLhAMAALLTDGLGLSES-------DVVLPVVPMFHVNawGLPY--AAA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 216 LAGAPLWLaPTTAFTASPFRWLswLSDSGATMTAA-PNFAYNLIGKYARRvsEVDLGALRVTLNGGEPVDCDGLTRFAEA 294
Cdd:cd12119 229 MVGAKLVL-PGPYLDPASLAEL--IEREGVTFAAGvPTVWQGLLDHLEAN--GRDLSSLRRVVIGGSAVPRSLIEAFEER 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 295 MAPfgfdagaVLPSYGLAEstcavTVPVPGIGLLADRVIDGSGAHKHAVL---GNPIPGMEVRI-SCGDQAAGNASREIG 370
Cdd:cd12119 304 GVR-------VIHAWGMTE-----TSPLGTVARPPSEHSNLSEDEQLALRakqGRPVPGVELRIvDDDGRELPWDGKAVG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 371 EIEIRGASMMAGYLGQQP----IDPDDWFATGDLGYLGA-GGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAV 445
Cdd:cd12119 372 ELQVRGPWVTKSYYKNDEeseaLTEDGWLRTGDVATIDEdGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAV 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 446 VALGTGDRSTRP-GLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd12119 452 IGVPHPKWGERPlAVVVLKEGATVTAEELLEFLADKVAKW--WLPDDVVFVD--EIPKTSTGKIDKKALR 517
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
138-514 |
8.22e-21 |
|
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: 94.84 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 138 AAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSpgavLSNLRGLNQRVGTDA----ATDVGCSWLPLYHDMGLAFVLS 213
Cdd:cd05919 78 ARDCEARLVVTSADDIAYLLYSSGTTGPPKGVMHA----HRDPLLFADAMAREAlgltPGDRVFSSAKMFFGYGLGNSLW 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 214 AALA-GAPLWLAPTTAftaSPFRWLSWLSDSGAT-MTAAPNFAYNLIGKYArrVSEVDLGALRVTLNGGEPVDCDGLTRF 291
Cdd:cd05919 154 FPLAvGASAVLNPGWP---TAERVLATLARFRPTvLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERW 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 292 AEAmapFGFDagaVLPSYGLAEStcavtvpvpGIGLLADRVidgsGAHKHAVLGNPIPGMEVRISCGDQAAGNASrEIGE 371
Cdd:cd05919 229 MEH---FGGP---ILDGIGATEV---------GHIFLSNRP----GAWRLGSTGRPVPGYEIRLVDEEGHTIPPG-EEGD 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 372 IEIRGASMMAGYLG----QQPIDPDDWFATGDLGYLGAGGLVV-CGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVV 446
Cdd:cd05919 289 LLVRGPSAAVGYWNnpekSRATFNGGWYRTGDKFCRDADGWYThAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVV 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489502054 447 ALGTGDRSTRPGL-VVAAEFRGPDEANARA---ELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd05919 369 AVPESTGLSRLTAfVVLKSPAAPQESLARDihrHLLERLSAH--KVPRRIAFVD--ELPRTATGKLQRFKLR 436
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
149-517 |
2.75e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.10 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 149 ASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAaTDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTta 228
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGE-DDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPK-- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 229 FTASPFrwLSWLSDSGAT-MTAAPNFAYNLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapfgFDAGAVLP 307
Cdd:PLN02860 247 FDAKAA--LQAIKQHNVTsMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKL-----FPNAKLFS 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 308 SYGLAEsTCA----VTVPVPGIGLLA------DRVIDGSGAHKHAV-LGNPIPGMEVRISCGDqaagnaSREIGEIEIRG 376
Cdd:PLN02860 320 AYGMTE-ACSsltfMTLHDPTLESPKqtlqtvNQTKSSSVHQPQGVcVGKPAPHVELKIGLDE------SSRVGRILTRG 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 377 ASMMAGYLGQQPIDPDD-----WFATGDLGYL-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVreGAVVALGT 450
Cdd:PLN02860 393 PHVMLGYWGQNSETASVlsndgWLDTGDIGWIdKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGV--ASVVVVGV 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 451 GDrsTRPGLVVAAEFR-----------GPDEANAR---AELIQRVASECGI----VP-SDVVFVSPgsLPRTSSGKLRRL 511
Cdd:PLN02860 471 PD--SRLTEMVVACVRlrdgwiwsdneKENAKKNLtlsSETLRHHCREKNLsrfkIPkLFVQWRKP--FPLTTTGKIRRD 546
|
....*.
gi 489502054 512 AVRRSL 517
Cdd:PLN02860 547 EVRREV 552
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
337-514 |
3.21e-20 |
|
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: 93.59 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 337 GAHKHAVLGNPIPGMEVRI---SCGDQAAGnasrEIGEIEIRGASMMAGYLGQqpidPDD--------WFATGDLGYLGA 405
Cdd:cd05959 327 GRVRYGTTGKPVPGYEVELrdeDGGDVADG----EPGELYVRGPSSATMYWNN----RDKtrdtfqgeWTRTGDKYVRDD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 406 GG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEANARAELIQRVASE 484
Cdd:cd05959 399 DGfYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDR 478
|
170 180 190
....*....|....*....|....*....|..
gi 489502054 485 CGI--VPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd05959 479 LAPykYPRWIVFVD--ELPKTATGKIQRFKLR 508
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
154-513 |
3.26e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 93.94 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSN-LRGLNQRVGTDAATDVGCSWLPLYHDMGLAFVLS-AALAGAPLWLAP----TT 227
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNlSIMQGYKMVLIPkfdmKM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 228 AFTAspfrwlswLSDSGATM-TAAPNFAYNLIGkyARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMapfgfdAGAVL 306
Cdd:PRK06710 289 VFEA--------IKKHKVTLfPGAPTIYIALLN--SPLLKEYDISSIRACISGSAPLPVEVQEKFETVT------GGKLV 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 307 PSYGLAESTcavtvPVPGIGLLADRVIDGSgahkhavLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAGYLGQ 386
Cdd:PRK06710 353 EGYGLTESS-----PVTHSNFLWEKRVPGS-------IGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNK 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 387 ----QPIDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDR-STRPGLV 460
Cdd:PRK06710 421 peetAAVLQDGWLHTGDVGYMDEDGFFyVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRgETVKAFV 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489502054 461 VAAEfrgpDEANARAELIQRVASECGIVPSDVVFVSPGSLPRTSSGKLRRLAV 513
Cdd:PRK06710 501 VLKE----GTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
250-510 |
3.31e-20 |
|
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: 91.79 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 250 APNFAYNLIGKYARRvsEVDLGALRVTLNGGEPVDCDGLTRFAEAMapfGFDAgaVLPSYGLAESTCAvTVPVPGiglla 329
Cdd:cd17638 96 PPTLFQSLLDHPGRK--KFDLSSLRAAVTGAATVPVELVRRMRSEL---GFET--VLTAYGLTEAGVA-TMCRPG----- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 330 DRVIDGSgahkhAVLGNPIPGMEVRisCGDQaagnasreiGEIEIRGASMMAGYLG-----QQPIDPDDWFATGDLGYL- 403
Cdd:cd17638 163 DDAETVA-----TTCGRACPGFEVR--IADD---------GEVLVRGYNVMQGYLDdpeatAEAIDADGWLHTGDVGELd 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 404 GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALgTGDRSTRPG--LVVAAEFRGPDEANARAELIQRV 481
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGV-PDERMGEVGkaFVVARPGVTLTEEDVIAWCRERL 305
|
250 260
....*....|....*....|....*....
gi 489502054 482 ASEcgIVPSDVVFVSpgSLPRTSSGKLRR 510
Cdd:cd17638 306 ANY--KVPRFVRFLD--ELPRNASGKVMK 330
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
134-507 |
4.03e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 93.40 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 134 DLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQ--RVGTDaatDVGCSWLPLYHDMGLaFV 211
Cdd:PRK07514 139 EAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDywRFTPD---DVLIHALPIFHTHGL-FV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 212 LS--AALAGAPLWLAPTtaFTASpfRWLSWLSDSGATMtAAPNFaynligkYARRVSEVDLGA-----LRVTLNGGEPVd 284
Cdd:PRK07514 215 ATnvALLAGASMIFLPK--FDPD--AVLALMPRATVMM-GVPTF-------YTRLLQEPRLTReaaahMRLFISGSAPL- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 285 cdgltrFAEAMAPFGFDAG-AVLPSYGLAESTCAVTVPVPGigllaDRVidgSGAhkhavLGNPIPGMEVRISCGDQAAG 363
Cdd:PRK07514 282 ------LAETHREFQERTGhAILERYGMTETNMNTSNPYDG-----ERR---AGT-----VGFPLPGVSLRVTDPETGAE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 364 NASREIGEIEIRGASMMAGYLgQQP------IDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQ 436
Cdd:PRK07514 343 LPPGEIGMIEVKGPNVFKGYW-RMPektaeeFRADGFFITGDLGKIDERGYVhIVGRGKDLIISGGYNVYPKEVEGEIDE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 437 VRGVREGAVVAL-----GTGdrstrpglVVAAEFRGP----DEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGK 507
Cdd:PRK07514 422 LPGVVESAVIGVphpdfGEG--------VTAVVVPKPgaalDEAAILAALKGRLARF--KQPKRVFFVD--ELPRNTMGK 489
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
156-514 |
9.21e-20 |
|
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: 90.80 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 156 LQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGtDAATDVGCSWLPLYHDMGLAF-VLSAALAGAPLWLaPTTAFTASPF 234
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLG-LTEQDRLCIPVPLFHCFGSVLgVLACLTHGATMVF-PSPSFDPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 235 rwLSWLSDSGAT-MTAAPNFAYNLIGKyaRRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMapfgfDAGAVLPSYGLAE 313
Cdd:cd05917 85 --LEAIEKEKCTaLHGVPTMFIAELEH--PDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVM-----NMKDVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 314 ST--CAVTVPVPGIgllaDRVIdgsgahkhAVLGNPIPGMEVRIScgDQAAGNASR--EIGEIEIRGASMMAGYLG---- 385
Cdd:cd05917 156 TSpvSTQTRTDDSI----EKRV--------NTVGRIMPHTEAKIV--DPEGGIVPPvgVPGELCIRGYSVMKGYWNdpek 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 386 -QQPIDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVValgtGDRSTRPGLVVAA 463
Cdd:cd05917 222 tAEAIDGDGWLHTGDLAVMDEDGYCrIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVV----GVPDERYGEEVCA 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489502054 464 EFRG-----PDEANARAELIQRVASEcgIVPSDVVFVspGSLPRTSSGKLRRLAVR 514
Cdd:cd05917 298 WIRLkegaeLTEEDIKAYCKGKIAHY--KVPRYVFFV--DEFPLTVSGKIQKFKLR 349
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
108-515 |
1.70e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 91.46 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 108 GVRTVLSQGSYLARLRSVDTAG-----VTIGDLSTAAHTNRS-ATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNlr 181
Cdd:PRK06839 100 GTTVLFVEKTFQNMALSMQKVSyvqrvISITSLKEIEDRKIDnFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWN-- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 182 GLNQRVGTD-AATDVGCSWLPLYHDMGLA-FVLSAALAGA----PLWLAPTTAftaspfrwLSWLSDSGATMT-AAPNFA 254
Cdd:PRK06839 178 ALNNTFAIDlTMHDRSIVLLPLFHIGGIGlFAFPTLFAGGviivPRKFEPTKA--------LSMIEKHKVTVVmGVPTIH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 255 YNLIGkyARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGfdagavlPSYGLAESTcavtvpvPGIGLLADRvid 334
Cdd:PRK06839 250 QALIN--CSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFG-------QGFGMTETS-------PTVFMLSEE--- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 335 gSGAHKHAVLGNPIPGMEVRIScgDQAAGNASR-EIGEIEIRGASMMAGYLgQQPIDP-----DDWFATGDLGYLGAGGL 408
Cdd:PRK06839 311 -DARRKVGSIGKPVLFCDYELI--DENKNKVEVgEVGELLIRGPNVMKEYW-NRPDATeetiqDGWLCTGDLARVDEDGF 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 409 V-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRP-GLVVAAEFRGPDEANARAELIQRVASEcg 486
Cdd:PRK06839 387 VyIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPiAFIVKKSSSVLIEKDVIEHCRLFLAKY-- 464
|
410 420
....*....|....*....|....*....
gi 489502054 487 IVPSDVVFVSpgSLPRTSSGKLRRLAVRR 515
Cdd:PRK06839 465 KIPKEIVFLK--ELPKNATGKIQKAQLVN 491
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
144-517 |
2.59e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 90.96 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 144 SATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTdAATDVGCSWLPLYHDMG-LAFVLSAALAGAPLW 222
Cdd:PRK06087 180 TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNL-TWQDVFMMPAPLGHATGfLHGVTAPFLIGARSV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 223 L----APTTAFTASPFRWLSWlsdsgaTMTAAPnFAYNLIGkyARRVSEVDLGALRVTLNGGEPVDCDgLTRFAeamapf 298
Cdd:PRK06087 259 LldifTPDACLALLEQQRCTC------MLGATP-FIYDLLN--LLEKQPADLSALRFFLCGGTTIPKK-VAREC------ 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 299 gFDAGAVLPS-YGLAESTCAVTVPVpgigllaDRVIDGSGAHKhavlGNPIPGMEVRISCGDQ---AAGNASREIGeiei 374
Cdd:PRK06087 323 -QQRGIKLLSvYGSTESSPHAVVNL-------DDPLSRFMHTD----GYAAAGVEIKVVDEARktlPPGCEGEEAS---- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 375 RGASMMAGYLGQ-----QPIDPDDWFATGDLGYLG-AGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVAL 448
Cdd:PRK06087 387 RGPNVFMGYLDEpeltaRALDEEGWYYSGDLCRMDeAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489502054 449 GT---GDRSTrPGLVVAAEFRGPDEANARAELI-QRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVRRSL 517
Cdd:PRK06087 467 PDerlGERSC-AYVVLKAPHHSLTLEEVVAFFSrKRVAKY--KYPEHIVVID--KLPRTASGKIQKFLLRKDI 534
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
140-514 |
3.27e-19 |
|
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: 90.09 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 140 HTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTdAATDVgcSWLPlyHDMGLAFVLSAALAGA 219
Cdd:cd05972 70 AAGAKAIVTDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGL-RPDDI--HWNI--ADPGWAKGAWSSFFGP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 220 PLWLAPTTAFTASPF---RWLSWLSDSGATMTAAPNFAYNLIGKyaRRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMA 296
Cdd:cd05972 145 WLLGATVFVYEGPRFdaeRILELLERYGVTSFCGPPTAYRMLIK--QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 297 PfgfdagAVLPSYGLAESTCAVTVpVPGIGLladrvidgsgahKHAVLGNPIPGMEVRIScgdQAAGNASR--EIGEIEI 374
Cdd:cd05972 223 L------PIRDGYGQTETGLTVGN-FPDMPV------------KPGSMGRPTPGYDVAII---DDDGRELPpgEEGDIAI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 375 RGA--SMMAGYLGqqpiDP--------DDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREG 443
Cdd:cd05972 281 KLPppGLFLGYVG----DPekteasirGDYYLTGDRAYRDEDGyFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEA 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489502054 444 AVVALGTGDRSTRP-GLVVAAEFRGPDEANARaELIQRVASECG--IVPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd05972 357 AVVGSPDPVRGEVVkAFVVLTSGYEPSEELAE-ELQGHVKKVLApyKYPREIEFVE--ELPKTISGKIRRVELR 427
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
53-514 |
7.49e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 89.66 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 53 RPAAVGLVGEPTVELVAAIQGAWLAGAAVSILpGPVRGANDQRW--ADATLTRFLGIGVRTVLSQGSYLAR---LRSVDT 127
Cdd:PRK06188 61 TGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL-HPLGSLDDHAYvlEDAGISTLIVDPAPFVERALALLARvpsLKHVLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 128 AG-VTIG-DLSTAAHTNRSATPVASEGP---AVLQGTAGSTGAPRTAILSpgavlsnlrglnQRVGTDAATDVGCSW--- 199
Cdd:PRK06188 140 LGpVPDGvDLLAAAAKFGPAPLVAAALPpdiAGLAYTGGTTGKPKGVMGT------------HRSIATMAQIQLAEWewp 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 200 --------LPLYHDMGlAFVLSAALAGAPLWLapTTAFtaSPFRWLSWLSDSGATMT-AAPNFAYNLIGkyARRVSEVDL 270
Cdd:PRK06188 208 adprflmcTPLSHAGG-AFFLPTLLRGGTVIV--LAKF--DPAEVLRAIEEQRITATfLVPTMIYALLD--HPDLRTRDL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 271 GALRVTLNGGEPVDCdglTRFAEAMAPFG--FdagavLPSYGLAESTCAVTVpvpgiglLADRVIDGSGAHKHAVLGNPI 348
Cdd:PRK06188 281 SSLETVYYGASPMSP---VRLAEAIERFGpiF-----AQYYGQTEAPMVITY-------LRKRDHDPDDPKRLTSCGRPT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 349 PGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLGQQPIDP----DDWFATGDLGYLGAGGLV-VCGRAKEVISIAGR 423
Cdd:PRK06188 346 PGLRVAL-LDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAeafrDGWLHTGDVAREDEDGFYyIVDRKKDMIVTGGF 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 424 NIFPTEVELVAAQVRGVREGAVValGTGDrsTRPG-LVVAAEFRGPDEANARAELIQRVASECGIV--PSDVVFVSpgSL 500
Cdd:PRK06188 425 NVFPREVEDVLAEHPAVAQVAVI--GVPD--EKWGeAVTAVVVLRPGAAVDAAELQAHVKERKGSVhaPKQVDFVD--SL 498
|
490
....*....|....
gi 489502054 501 PRTSSGKLRRLAVR 514
Cdd:PRK06188 499 PLTALGKPDKKALR 512
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
36-513 |
8.26e-19 |
|
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: 88.90 E-value: 8.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 36 EVHGLAESVAAWLLDHD-RPAA-VGLVGEPTVELVAAIQGAWLAGAA-VSILPGPVRGANDQRWADAtltrflgiGVRTV 112
Cdd:cd17643 17 ELDARANRLARTLRAEGvGPGDrVALALPRSAELIVALLAILKAGGAyVPIDPAYPVERIAFILADS--------GPSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 113 LSQGsylarlrsvdtagvtigdlstaahtnrsatpvasEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGlNQRVGTDAA 192
Cdd:cd17643 89 LTDP----------------------------------DDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 193 TDVgcsWLpLYHDMGLAF----VLSAALAGAPLWLAPTtAFTASPFRWLSWLSDSGAT-MTAAPNFAYNLIGKYARRVSE 267
Cdd:cd17643 134 DDV---WT-LFHSYAFDFsvweIWGALLHGGRLVVVPY-EVARSPEDFARLLRDEGVTvLNQTPSAFYQLVEAADRDGRD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 268 VDlgALRVTLNGGEPVDCDGLTRFAEAmapFGFDAGAVLPSYGLAESTCAVTVpvpgiglladRVIDGSGAHKHA--VLG 345
Cdd:cd17643 209 PL--ALRYVIFGGEALEAAMLRPWAGR---FGLDRPQLVNMYGITETTVHVTF----------RPLDAADLPAAAasPIG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 346 NPIPGMEVRI---SCGDQAAGnasrEIGEIEIRGASMMAGYLGQQ-------PIDPDD-----WFATGDLG-YLGAGGLV 409
Cdd:cd17643 274 RPLPGLRVYVldaDGRPVPPG----VVGELYVSGAGVARGYLGRPeltaerfVANPFGgpgsrMYRTGDLArRLPDGELE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 410 VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTR-PGLVVAAEFRGPDEANARAELIQRVASEcgIV 488
Cdd:cd17643 350 YLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRlVAYVVADDGAAADIAELRALLKELLPDY--MV 427
|
490 500
....*....|....*....|....*
gi 489502054 489 PSdvVFVSPGSLPRTSSGKLRRLAV 513
Cdd:cd17643 428 PA--RYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
136-521 |
1.55e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 88.65 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 136 STAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSwLPLYHDMGLAFVLSAA 215
Cdd:PRK06164 166 DPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAA-LPFCGVFGFSTLLGAL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 216 LAGAPLWLAPttAFTASpfRWLSWLSDSGATMTAAPNFAYNLIGKYARRvsEVDLGALRVtlnggepvdcdgltrfaeam 295
Cdd:PRK06164 245 AGGAPLVCEP--VFDAA--RTARALRRHRVTHTFGNDEMLRRILDTAGE--RADFPSARL-------------------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 296 apFGFdaGAVLPSYG-LAESTCAVTVPVPG-------IGLLADRVIDGSGAHKHAVLGNPI-PGMEVRISCGDQAAGNAS 366
Cdd:PRK06164 299 --FGF--ASFAPALGeLAALARARGVPLTGlygssevQALVALQPATDPVSVRIEGGGRPAsPEARVRARDPQDGALLPD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 367 REIGEIEIRGASMMAGYLG-----QQPIDPDDWFATGDLGYL-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGV 440
Cdd:PRK06164 375 GESGEIEIRAPSLMRGYLDnpdatARALTDDGYFRTGDLGYTrGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 441 REGAVVALgTGDRSTRP-GLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSG---KLRRLAVRrs 516
Cdd:PRK06164 455 AAAQVVGA-TRDGKTVPvAFVIPTDGASPDEAGLMAACREALAGF--KVPARVQVVE--AFPVTESAngaKIQKHRLR-- 527
|
....*
gi 489502054 517 lEMAD 521
Cdd:PRK06164 528 -EMAQ 531
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
36-512 |
2.39e-18 |
|
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: 88.76 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 36 EVHGLAESVAAWLLDHD-RP-AAVGLVGEPTVELVAAIQGAWLAGAA-VSILPG-PvrganDQRWA----DAtltrflgi 107
Cdd:COG1020 506 ELNARANRLAHHLRALGvGPgDLVGVCLERSLEMVVALLAVLKAGAAyVPLDPAyP-----AERLAymleDA-------- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 108 GVRTVLSQGSYLARLRSVDTAGVTIGDLSTAAH-TNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQR 186
Cdd:COG1020 573 GARLVLTQSALAARLPELGVPVLALDALALAAEpATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRR 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 187 VGTDAAtDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTAfTASPFRWLSWLSDSGATMTAAPNFAYNLIGKYARRvs 266
Cdd:COG1020 653 YGLGPG-DRVLQFASLSFDASVWEIFGALLSGATLVLAPPEA-RRDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-- 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 267 evDLGALRVTLNGGEPVDCDGLTRFAEAmapfgFDAGAVLPSYGLAESTCAVTVpvpgiglladRVIDGSGAHKHAV-LG 345
Cdd:COG1020 729 --ALPSLRLVLVGGEALPPELVRRWRAR-----LPGARLVNLYGPTETTVDSTY----------YEVTPPDADGGSVpIG 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 346 NPIPGMEVRI---SCGDQAAGnasrEIGEIEIRGASMMAGYLGQQ----------PIDPDD--WFATGDLG-YLGAGGLV 409
Cdd:COG1020 792 RPIANTRVYVldaHLQPVPVG----VPGELYIGGAGLARGYLNRPeltaerfvadPFGFPGarLYRTGDLArWLPDGNLE 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 410 VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEANARAELIQRVASEcgiVP 489
Cdd:COG1020 868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPP---YM 944
|
490 500
....*....|....*....|...
gi 489502054 490 SDVVFVSPGSLPRTSSGKLRRLA 512
Cdd:COG1020 945 VPAAVVLLLPLPLTGNGKLDRLA 967
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
131-517 |
4.08e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 87.37 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 131 TIGDLSTAAHTNRSATPVASEG-----PAVLQGTAGSTGAPRtAILSPG----AVLSNLRGLNQRVGTDAATDVGCSWLP 201
Cdd:PRK05857 144 IAAVTRESEHSLDAASLAGNADqgsedPLAMIFTSGTTGEPK-AVLLANrtffAVPDILQKEGLNWVTWVVGETTYSPLP 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 202 LYHDMGLAFVLSAALAGAplwLAPTTAFTASPFRWLsWLSDSGATMTAAPNFAYNLIgkYARRVSEVDLGALRVTLNGGE 281
Cdd:PRK05857 223 ATHIGGLWWILTCLMHGG---LCVTGGENTTSLLEI-LTTNAVATTCLVPTLLSKLV--SELKSANATVPSLRLVGYGGS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 282 PVDCDGLtRFAEAMapfGFDAGAVlpsYGLAESTC-AVTVPVPgiglladrviDGSGAHKHA-VLGNPIPGMEVRISCGD 359
Cdd:PRK05857 297 RAIAADV-RFIEAT---GVRTAQV---YGLSETGCtALCLPTD----------DGSIVKIEAgAVGRPYPGVDVYLAATD 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 360 QAAGNA-----SREIGEIEIRGASMMAGYLGQ----QPIDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTE 429
Cdd:PRK05857 360 GIGPTApgagpSASFGTLWIKSPANMLGYWNNpertAEVLIDGWVNTGDLLERREDGFFyIKGRSSEMIICGGVNIAPDE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 430 VELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEFRgPDEANARaELIQRVA------SECGIVPSDVVFVSpgSLPRT 503
Cdd:PRK05857 440 VDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAE-LDESAAR-ALKHTIAarfrreSEPMARPSTIVIVT--DIPRT 515
|
410
....*....|....
gi 489502054 504 SSGKLRRLAVRRSL 517
Cdd:PRK05857 516 QSGKVMRASLAAAA 529
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
154-511 |
6.54e-18 |
|
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: 85.99 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLrgLNQRVGTD-AATDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTtaftas 232
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANA--LQSAVWTGlTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMA------ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 233 pfRW-----LSWLSDSGATM-TAAPNFAYNLIGkyARRVSEVDLGALRVTLNGGEPVdcdgltrfAEAMAP-----FGFD 301
Cdd:cd05935 159 --RWdretaLELIEKYKVTFwTNIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPM--------PPAVAEkllklTGLR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 302 agaVLPSYGLAESTCAVTVPVPGiglladrvidgsgAHKHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMA 381
Cdd:cd05935 227 ---FVEGYGLTETMSQTHTNPPL-------------RPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 382 GYLgQQP---------IDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTG 451
Cdd:cd05935 291 GYW-NRPeeteesfieIKGRRFFRTGDLGYMDEEGyFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDE 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489502054 452 DRSTRPG--LVVAAEFRGP-DEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGK-LRRL 511
Cdd:cd05935 370 RVGEEVKafIVLRPEYRGKvTEEDIIEWAREQMAAY--KYPREVEFVD--ELPRSASGKiLWRL 429
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
148-514 |
7.43e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 86.47 E-value: 7.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 148 VASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGC----SWLPLYHDM-----GLAFVLSAA--- 215
Cdd:PRK08751 205 IEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCevviTALPLYHIFaltanGLVFMKIGGcnh 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 216 LAGAP---------LWLAPTTAFTASPFRWLSWLSdsgatmtaAPNFAynligkyarrvsEVDLGALRVTLNGGEPVDCD 286
Cdd:PRK08751 285 LISNPrdmpgfvkeLKKTRFTAFTGVNTLFNGLLN--------TPGFD------------QIDFSSLKMTLGGGMAVQRS 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 287 GLTRFAEAMAPfgfdagAVLPSYGLAEstcavTVPVPGIGLLADRVIDGSgahkhavLGNPIPGMEVRIScGDQAAGNAS 366
Cdd:PRK08751 345 VAERWKQVTGL------TLVEAYGLTE-----TSPAACINPLTLKEYNGS-------IGLPIPSTDACIK-DDAGTVLAI 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 367 REIGEIEIRGASMMAGYLgQQP------IDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRG 439
Cdd:PRK08751 406 GEIGELCIKGPQVMKGYW-KRPeetakvMDADGWLHTGDIARMDEQGFVyIVDRKKDMILVSGFNVYPNEIEDVIAMMPG 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 440 VREgaVVALGTGDRSTrpGLVVAAEFRGPD--------EANARAELIQRVAsecgivPSDVVFVSpgSLPRTSSGKLRRL 511
Cdd:PRK08751 485 VLE--VAAVGVPDEKS--GEIVKVVIVKKDpaltaedvKAHARANLTGYKQ------PRIIEFRK--ELPKTNVGKILRR 552
|
...
gi 489502054 512 AVR 514
Cdd:PRK08751 553 ELR 555
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
129-518 |
7.47e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 86.37 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 129 GVTIGDLSTAAHTNRSATPVAsegpavLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTdAATDVGCSWLPLYHDMGL 208
Cdd:PRK12583 185 TVSREALAERQASLDRDDPIN------IQYTSGTTGFPKGATLSHHNILNNGYFVAESLGL-TEHDRLCVPVPLYHCFGM 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 209 AFVLSAALAGAPLWLAPTTAFtaspfrwlswlsDSGATMTA-APNFAYNLIGKYARRVSEV--------DLGALRVTLNG 279
Cdd:PRK12583 258 VLANLGCMTVGACLVYPNEAF------------DPLATLQAvEEERCTALYGVPTMFIAELdhpqrgnfDLSSLRTGIMA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 280 GEPVDCDGLTRFAEAMapfgfDAGAVLPSYGLAESTcavtvPVPGIGLLAD----RVidgsgahkhAVLGNPIPGMEVRI 355
Cdd:PRK12583 326 GAPCPIEVMRRVMDEM-----HMAEVQIAYGMTETS-----PVSLQTTAADdlerRV---------ETVGRTQPHLEVKV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 356 ScgdQAAGN--ASREIGEIEIRGASMMAGYLGQ-----QPIDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFP 427
Cdd:PRK12583 387 V---DPDGAtvPRGEIGELCTRGYSVMKGYWNNpeataESIDEDGWMHTGDLATMDEQGYVrIVGRSKDMIIRGGENIYP 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 428 TEVELVAAQVRGVREGAVValgtGDRSTRPGLVVAAEFR-GPDEANARAELiqRVASECGI----VPSDVVFVSpgSLPR 502
Cdd:PRK12583 464 REIEEFLFTHPAVADVQVF----GVPDEKYGEEIVAWVRlHPGHAASEEEL--REFCKARIahfkVPRYFRFVD--EFPM 535
|
410
....*....|....*..
gi 489502054 503 TSSGKLRRLAVR-RSLE 518
Cdd:PRK12583 536 TVTGKVQKFRMReISIE 552
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
45-513 |
8.74e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 86.09 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 45 AAWLLDHDRpaaVGLVGEPTVELVAAIQGAWLAGAAVSILpGPVRGANDQR------WADATLTRFLGIGVRTVLSQGSY 118
Cdd:PRK05852 62 RSGLLPGDR---VALRMGSNAEFVVALLAASRADLVVVPL-DPALPIAEQRvrsqaaGARVVLIDADGPHDRAEPTTRWW 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 119 LARLRSVDTAGVTIGDLS-----TAAHTNRSATPVA-SEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGL--NQRVGTD 190
Cdd:PRK05852 138 PLTVNVGGDSGPSGGTLSvhldaATEPTPATSTPEGlRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIitGYRLSPR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 191 AATdvgCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTA-FTASPFrwlsW--LSDSGAT-MTAAPNFAYNLIGKYARRVS 266
Cdd:PRK05852 218 DAT---VAVMPLYHGHGLIAALLATLASGGAVLLPARGrFSAHTF----WddIKAVGATwYTAVPTIHQILLERAATEPS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 267 EVDLGALRVTLNGGEPVDCdgltrfAEAMAPFGFDAGAVLPSYGLAESTCAVTVpvpgiglladRVIDGSGAHKHAVLGN 346
Cdd:PRK05852 291 GRKPAALRFIRSCSAPLTA------ETAQALQTEFAAPVVCAFGMTEATHQVTT----------TQIEGIGQTENPVVST 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 347 PI----PGMEVRISCGDQAAGNASrEIGEIEIRGASMMAGYLGQQPIDP----DDWFATGDLGYLGAGG-LVVCGRAKEV 417
Cdd:PRK05852 355 GLvgrsTGAQIRIVGSDGLPLPAG-AVGEVWLRGTTVVRGYLGDPTITAanftDGWLRTGDLGSLSAAGdLSIRGRIKEL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 418 ISIAGRNIFPTEVELVAAQVRGVREGAVValgtGDRSTRPGLVVAAEFRGPDEANARAELIQRVASEcGIVPSDV--VFV 495
Cdd:PRK05852 434 INRGGEKISPERVEGVLASHPNVMEAAVF----GVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRE-RLAAFEIpaSFQ 508
|
490
....*....|....*...
gi 489502054 496 SPGSLPRTSSGKLRRLAV 513
Cdd:PRK05852 509 EASGLPHTAKGSLDRRAV 526
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
159-514 |
1.08e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.43 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGL-----NQRVGtdaatdvGCSWLPLYHDMGLAFVLSAALAGAPLWLAPttaftasp 233
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASVQGFqryfqLQQVN-------SFCVLPLYHVSGLMQFMRSFLTGGKLVILP-------- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 234 frwLSWLSDSGATMTAAPNFAYNLIGKYARRVSEVD---LGALRVTLNGGEPVDCDGLTRFAEAMAPFGfdagavlPSYG 310
Cdd:PRK07445 193 ---YKRLKSGQELPPNPSDFFLSLVPTQLQRLLQLRpqwLAQFRTILLGGAPAWPSLLEQARQLQLRLA-------PTYG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 311 LAESTCAVTVpvpgigLLADRVIDGSGAhkhavLGNPIPGMEVRISCGDqaagnasreIGEIEIRGASMMAGYLgQQPID 390
Cdd:PRK07445 263 MTETASQIAT------LKPDDFLAGNNS-----SGQVLPHAQITIPANQ---------TGNITIQAQSLALGYY-PQILD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 391 PDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREgaVVALGTGDRstRPGLVVAAEFRGPD 469
Cdd:PRK07445 322 SQGIFETDDLGYLDAQGyLHILGRNSQKIITGGENVYPAEVEAAILATGLVQD--VCVLGLPDP--HWGEVVTAIYVPKD 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 489502054 470 EANARAELIQRVASECGIV--PSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:PRK07445 398 PSISLEELKTAIKDQLSPFkqPKHWIPVP--QLPRNPQGKINRQQLQ 442
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
148-510 |
3.40e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 84.34 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 148 VASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQ------RVGTDAATDVgcswLPLYHDMGLAF--VLSAALAGA 219
Cdd:PRK08974 203 LVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAaygpllHPGKELVVTA----LPLYHIFALTVncLLFIELGGQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 220 PLWLA---------------PTTAFTASPFRWLSWLSDsgatmtaaPNFAynligkyarrvsEVDLGALRVTLNGGEPVD 284
Cdd:PRK08974 279 NLLITnprdipgfvkelkkyPFTAITGVNTLFNALLNN--------EEFQ------------ELDFSSLKLSVGGGMAVQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 285 CDGLTRFAEAMAPFgfdagaVLPSYGLAESTCAVTV-PVpgiglladRVIDGSGAhkhavLGNPIPGMEVRISCGDqaaG 363
Cdd:PRK08974 339 QAVAERWVKLTGQY------LLEGYGLTECSPLVSVnPY--------DLDYYSGS-----IGLPVPSTEIKLVDDD---G 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 364 N--ASREIGEIEIRGASMMAGYLgQQP-----IDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAA 435
Cdd:PRK08974 397 NevPPGEPGELWVKGPQVMLGYW-QRPeatdeVIKDGWLATGDIAVMDEEGfLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489502054 436 QVRGVREgaVVALGTGDRSTrpGLVVAAEFRGPDEANARAELIQ--RVASECGIVPSDVVFVSpgSLPRTSSGK-LRR 510
Cdd:PRK08974 476 LHPKVLE--VAAVGVPSEVS--GEAVKIFVVKKDPSLTEEELIThcRRHLTGYKVPKLVEFRD--ELPKSNVGKiLRR 547
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
34-515 |
3.56e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 83.89 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 34 WPEVHGLAESVAAWLLDHDRpaaVGLVGEPTVELVAAIQGAWLAGAAVSILPgPVRGANDQR--WADATLTRFLGIgvrt 111
Cdd:PRK07787 28 RSDLAGAATAVAERVAGARR---VAVLATPTLATVLAVVGALIAGVPVVPVP-PDSGVAERRhiLADSGAQAWLGP---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 112 vlsqgsylarlRSVDTAGVTIGDLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDA 191
Cdd:PRK07787 100 -----------APDDPAGLPHVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 192 AtDVGCSWLPLYHDMGLAF-VLSAALAGAPLwlAPTTAFTasPFRWLSWLSDSGATMTAAPNFaynligkYARRVSEVD- 269
Cdd:PRK07787 169 D-DVLVHGLPLFHVHGLVLgVLGPLRIGNRF--VHTGRPT--PEAYAQALSEGGTLYFGVPTV-------WSRIAADPEa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 270 ---LGALRVTLNGGEPVDCDGLTRFAEAmapfgfdAG-AVLPSYGLAESTCAVTVpvpgiglLADrvidgsGAHKHAVLG 345
Cdd:PRK07787 237 araLRGARLLVSGSAALPVPVFDRLAAL-------TGhRPVERYGMTETLITLST-------RAD------GERRPGWVG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 346 NPIPGMEVRISCGDQAAGNASRE-IGEIEIRGASMMAGYLGQ-----QPIDPDDWFATGDLGYLGAGGLV--VCGRAKEV 417
Cdd:PRK07787 297 LPLAGVETRLVDEDGGPVPHDGEtVGELQVRGPTLFDGYLNRpdataAAFTADGWFRTGDVAVVDPDGMHriVGRESTDL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 418 ISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRpglVVAaeFRGPDEANARAELIQRVASECGI--VPSDVVFV 495
Cdd:PRK07787 377 IKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQR---IVA--YVVGADDVAADELIDFVAQQLSVhkRPREVRFV 451
|
490 500
....*....|....*....|
gi 489502054 496 SpgSLPRTSSGKLRRLAVRR 515
Cdd:PRK07787 452 D--ALPRNAMGKVLKKQLLS 469
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
144-520 |
3.91e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 84.62 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 144 SATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSwLPLYHDMGL-AFVLSAALAGAPLW 222
Cdd:PRK07529 206 SGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCG-LPLFHVNALlVTGLAPLARGAHVV 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 223 LApttafTASPFRwlswlsDSGA--------------TMTAAPNfAYNliGKYARRVSEVDLGALRVTLNGGEPVDCDGL 288
Cdd:PRK07529 285 LA-----TPQGYR------GPGVianfwkiveryrinFLSGVPT-VYA--ALLQVPVDGHDISSLRYALCGAAPLPVEVF 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 289 TRFAEAMAPfgfdagAVLPSYGLAESTCAVTVPVPGiglladrvidgsGAHKHAVLGNPIPGMEVRISCGDqAAGNASR- 367
Cdd:PRK07529 351 RRFEAATGV------RIVEGYGLTEATCVSSVNPPD------------GERRIGSVGLRLPYQRVRVVILD-DAGRYLRd 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 368 ----EIGEIEIRGASMMAGYL-GQQPIDP---DDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVR 438
Cdd:PRK07529 412 cavdEVGVLCIAGPNVFSGYLeAAHNKGLwleDGWLNTGDLGRIDADGYFwLTGRAKDLIIRGGHNIDPAAIEEALLRHP 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 439 GVREGAVVA--------LGTGDRSTRPGLVV-AAEFRgpdeANARAELIQRVAsecgiVPSDVVFVSPgsLPRTSSGK-- 507
Cdd:PRK07529 492 AVALAAAVGrpdahageLPVAYVQLKPGASAtEAELL----AFARDHIAERAA-----VPKHVRILDA--LPKTAVGKif 560
|
410
....*....|....*.
gi 489502054 508 ---LRRLAVRRSLEMA 520
Cdd:PRK07529 561 kpaLRRDAIRRVLRAA 576
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
138-510 |
7.55e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 83.27 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 138 AAHTNRSATPvASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGT--DAATDVGCSWLPLYHDMGLAF-VLSA 214
Cdd:PRK05677 195 AGQPVTEANP-QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSnlNEGCEILIAPLPLYHIYAFTFhCMAM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 215 ALAGAPLWLAPTTAFTASPFRWLSWLSDSG----ATMTAApnfaynLIGKYARRvsEVDLGALRVTLNGGEPVDCDGLTR 290
Cdd:PRK05677 274 MLIGNHNILISNPRDLPAMVKELGKWKFSGfvglNTLFVA------LCNNEAFR--KLDFSALKLTLSGGMALQLATAER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 291 FAEAMApfgfdaGAVLPSYGLAESTCAVTV-PVPGIGLladrvidgsgahkhAVLGNPIPGMEVRIsCGDQAAGNASREI 369
Cdd:PRK05677 346 WKEVTG------CAICEGYGMTETSPVVSVnPSQAIQV--------------GTIGIPVPSTLCKV-IDDDGNELPLGEV 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 370 GEIEIRGASMMAGYLgQQP------IDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVRE 442
Cdd:PRK05677 405 GELCVKGPQVMKGYW-QRPeatdeiLDSDGWLKTGDIALIQEDGYMrIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489502054 443 GAvvALGTGDRSTRPGLVVAAEFRgPDEANARAELIQRVASECGI--VPSDVVFVSpgSLPRTSSGK-LRR 510
Cdd:PRK05677 484 CA--AIGVPDEKSGEAIKVFVVVK-PGETLTKEQVMEHMRANLTGykVPKAVEFRD--ELPTTNVGKiLRR 549
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
36-515 |
1.36e-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: 341277 [Multi-domain] Cd Length: 437 Bit Score: 82.18 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 36 EVHGLAESVAAWLLDHD-RPAAV--GLVGEpTVELVAAIQGAWLAGAAVSILP---GPvrgandqrwaDATLTRFLGIGV 109
Cdd:cd05973 5 ELRALSARFANALQELGvGPGDVvaGLLPR-TPELVVTILGIWRLGAVYQPLFtafGP----------KAIEHRLRTSGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 110 RTVLSQGSYLARLrsvdtagvtigdlstaahtnrsatpvaSEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGT 189
Cdd:cd05973 74 RLVVTDAANRHKL---------------------------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 190 DAATDVGCSwlplyHDMGLAFVLSAALAGaPLWLAPTTAFTASPFRW-LSW--LSDSGATMTAAPNFAYNLIGKYARRVS 266
Cdd:cd05973 127 RPEDSFWNA-----ADPGWAYGLYYAITG-PLALGHPTILLEGGFSVeSTWrvIERLGVTNLAGSPTAYRLLMAAGAEVP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 267 EVDLGALRVTLNGGEPVDCDGLTRFAEAMAPfgfdagAVLPSYGLAEstcaVTVPVPGIGLLADRVIDGSgahkhavLGN 346
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGV------PIHDHYGQTE----LGMVLANHHALEHPVHAGS-------AGR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 347 PIPGMEVRIsCGDQAAGNASREIG--EIEIRGASMM--AGYLGQQPIDPD-DWFATGDLGYLGAGGLV-VCGRAKEVISI 420
Cdd:cd05973 264 AMPGWRVAV-LDDDGDELGPGEPGrlAIDIANSPLMwfRGYQLPDTPAIDgGYYLTGDTVEFDPDGSFsFIGRADDVITM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 421 AGRNIFPTEVELVAAQVRGVREGAVVALGTGDRS--TRPGLVVAAEFRG-PDEANARAELI-QRVASECgiVPSDVVFVS 496
Cdd:cd05973 343 SGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTevVKAFVVLRGGHEGtPALADELQLHVkKRLSAHA--YPRTIHFVD 420
|
490
....*....|....*....
gi 489502054 497 pgSLPRTSSGKLRRLAVRR 515
Cdd:cd05973 421 --ELPKTPSGKIQRFLLRR 437
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
154-510 |
1.36e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 82.76 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNL--------RGLNQRVGTDAATDVgCSwLPLYHDMGLA--FVLSAALAGAPLwL 223
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEKKPRPDQLNFV-CA-LPLYHIFALTvcGLLGMRTGGRNI-L 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 224 APT----TAFTASpfrwlswLSDSGATMTAAPNFAYNLIgKYARRVSEVDLGALRVTLNGG----EPVdcdgltrfaeAM 295
Cdd:PRK07059 284 IPNprdiPGFIKE-------LKKYQVHIFPAVNTLYNAL-LNNPDFDKLDFSKLIVANGGGmavqRPV----------AE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 296 APFGFDAGAVLPSYGLAEstcavTVPVpgigLLADRV--IDGSGAhkhavLGNPIPGMEVRISCGDqaaGN--ASREIGE 371
Cdd:PRK07059 346 RWLEMTGCPITEGYGLSE-----TSPV----ATCNPVdaTEFSGT-----IGLPLPSTEVSIRDDD---GNdlPLGEPGE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 372 IEIRGASMMAGYLgQQP------IDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGA 444
Cdd:PRK07059 409 ICIRGPQVMAGYW-NRPdetakvMTADGFFRTGDVGVMDERGYTkIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVA 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502054 445 VValGTGDrsTRPGLVVAAEFRGPDEANARAELIQRVASECG--IVPSDVVFVSpgSLPRTSSGK-LRR 510
Cdd:PRK07059 488 AV--GVPD--EHSGEAVKLFVVKKDPALTEEDVKAFCKERLTnyKRPKFVEFRT--ELPKTNVGKiLRR 550
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
154-515 |
1.60e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 80.86 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAatdvgcSWL---PLYHDMGLAFVLSAALAGA-PLWLAPTTAF 229
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG------QWLlalPAHHIAGLQVLVRSVIAGSePVELDVSAGF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 230 TASPFrwlswlSDSGATMTAAPNF----AYNLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPfgfdagaV 305
Cdd:PRK07824 112 DPTAL------PRAVAELGGGRRYtslvPMQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAAAGIN-------V 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 306 LPSYGLAEsTCAvtvpvpgiGLLADrvidgsgahkhavlGNPIPGMEVRIscgdqaagnasrEIGEIEIRGASMMAGYLG 385
Cdd:PRK07824 179 VRTYGMSE-TSG--------GCVYD--------------GVPLDGVRVRV------------EDGRIALGGPTLAKGYRN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 386 qqPIDPDD-----WFATGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVValGTGDRstRPG-L 459
Cdd:PRK07824 224 --PVDPDPfaepgWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF--GLPDD--RLGqR 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489502054 460 VVAAEFRGPDEANARAELIQRVASECGI--VPSDVVFVspGSLPRTSSGKLRRLAVRR 515
Cdd:PRK07824 298 VVAAVVGDGGPAPTLEALRAHVARTLDRtaAPRELHVV--DELPRRGIGKVDRRALVR 353
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
153-510 |
2.47e-16 |
|
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: 80.01 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 153 PAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAaTDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPttAFtaS 232
Cdd:cd17637 2 PFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTE-ADVYLNMLPLFHIAGLNLALATFHAGGANVVME--KF--D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 233 PFRWLSWLSDSGAT-MTAAPNFAYNLIGKYARrvSEVDLGALRVTLNGGEPvdcDGLTRFaEAMAPFGFDAGavlpsYGL 311
Cdd:cd17637 77 PAEALELIEEEKVTlMGSFPPILSNLLDAAEK--SGVDLSSLRHVLGLDAP---ETIQRF-EETTGATFWSL-----YGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 312 AESTCAVTvpvpgIGLLADRviDGSGahkhavlGNPIPGMEVRI---SCGDQAAGnasrEIGEIEIRGASMMAGYLGQQP 388
Cdd:cd17637 146 TETSGLVT-----LSPYRER--PGSA-------GRPGPLVRVRIvddNDRPVPAG----ETGEIVVRGPLVFQGYWNLPE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 389 IDP----DDWFATGDLGYLGAGG-LVVCGR--AKEVISIAGRNIFPTEVELVAAQVRGVREgaVVALGTGDRSTRPGlVV 461
Cdd:cd17637 208 LTAytfrNGWHHTGDLGRFDEDGyLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAE--VCVIGVPDPKWGEG-IK 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489502054 462 AAEFRGPDEANARAELIQRVASEcgIV----PSDVVFVSpgSLPRTSSGKLRR 510
Cdd:cd17637 285 AVCVLKPGATLTADELIEFVGSR--IArykkPRYVVFVE--ALPKTADGSIDR 333
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
159-515 |
5.78e-16 |
|
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: 79.45 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNqRVGTDAATDVGCSWLPLYHDMGLAFVLSAALA--GAPLWLAPTTAFTASPFR- 235
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEVYNAWMLA-LNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLAsgAHVVLAGPAGYRNPGLFDn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 236 -WLSWLSDSGATMTAAPNfaynLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPfgfdagAVLPSYGLAES 314
Cdd:cd05944 89 fWKLVERYRITSLSTVPT----VYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGL------PVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 315 TCAVTVPVPGiglladrvidgsGAHKHAVLGNPIPGMEVRISCGDqAAGNASR-----EIGEIEIRGASMMAGYL---GQ 386
Cdd:cd05944 159 TCLVAVNPPD------------GPKRPGSVGLRLPYARVRIKVLD-GVGRLLRdcapdEVGEICVAGPGVFGGYLyteGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 387 QPIDPDD-WFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVElvAAQVRGVREGAVVALGTGDR----------S 454
Cdd:cd05944 226 KNAFVADgWLNTGDLGRLDADGYLfITGRAKDLIIRGGHNIDPALIE--EALLRHPAVAFAGAVGQPDAhagelpvayvQ 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489502054 455 TRPGLVVAAEfrgPDEANARAELIQRVAsecgiVPSDVVFVSPgsLPRTSSGK-----LRRLAVRR 515
Cdd:cd05944 304 LKPGAVVEEE---ELLAWARDHVPERAA-----VPKHIEVLEE--LPVTAVGKvfkpaLRADAIHR 359
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
147-481 |
7.56e-16 |
|
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: 79.81 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 147 PVASEgPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTdAATDVGCSWLPLYHDMGLAFVLSAALAGaplwLAPT 226
Cdd:cd05910 82 PKADE-PAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI-RPGEVDLATFPLFALFGPALGLTSVIPD----MDPT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 227 TAFTASPFRWLSWLSDSGATMTAAPNFAYNLIGKYARRvSEVDLGALRVTLNGGEPVDCDGLTRFAEAMApfgfDAGAVL 306
Cdd:cd05910 156 RPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ-HGITLPSLRRVLSAGAPVPIALAARLRKMLS----DEAEIL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 307 PSYGLAEStcavtVPVPGIG---LLADRVIDGSGaHKHAVLGNPIPGMEVRI---------SCGDQAAGNASrEIGEIEI 374
Cdd:cd05910 231 TPYGATEA-----LPVSSIGsreLLATTTAATSG-GAGTCVGRPIPGVRVRIieiddepiaEWDDTLELPRG-EIGEITV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 375 RGASMMAGYLGQQPI-------DPDD--WFATGDLGYL-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGA 444
Cdd:cd05910 304 TGPTVTPTYVNRPVAtalakidDNSEgfWHRMGDLGYLdDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSA 383
|
330 340 350
....*....|....*....|....*....|....*..
gi 489502054 445 VVALGTGDRStRPGLVVAAEfrgPDEANARAELIQRV 481
Cdd:cd05910 384 LVGVGKPGCQ-LPVLCVEPL---PGTITPRARLEQEL 416
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
40-512 |
9.05e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 79.64 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 40 LAESVAAWLLDHDRP--AAVGLVGEPTVELVAAIQGAWLAGAA-VSILPGPVRGANDQRWADAtltrflgiGVRTVLSQG 116
Cdd:cd12116 21 RANRLAARLRARGVGpgDRVAVYLPRSARLVAAMLAVLKAGAAyVPLDPDYPADRLRYILEDA--------EPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 117 SYLARLRSVDTAGVTIGDLSTAAHTNRSaTPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAatdvG 196
Cdd:cd12116 93 ALPDRLPAGLPVLLLALAAAAAAPAAPR-TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGP----G 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 197 CSWLPLY---HDMGLAFVLSAALAGAPLWLAPTTAfTASPFRWLSWLSDSGAT-MTAAPNFAYNLIGkyarrVSEVDLGA 272
Cdd:cd12116 168 DRLLAVTtyaFDISLLELLLPLLAGARVVIAPRET-QRDPEALARLIEAHSITvMQATPATWRMLLD-----AGWQGRAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 273 LRVtLNGGEPVDCDGLTRFAEAmapfgfdAGAVLPSYGLAESTcavtvpvpgIGLLADRVIDGSGahkHAVLGNPIPGME 352
Cdd:cd12116 242 LTA-LCGGEALPPDLAARLLSR-------VGSLWNLYGPTETT---------IWSTAARVTAAAG---PIPIGRPLANTQ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 353 VRIScgdQAAGN--ASREIGEIEIRGASMMAGYLGQ----------QPIDPDD--WFATGDLG-YLGAGGLVVCGRAKEV 417
Cdd:cd12116 302 VYVL---DAALRpvPPGVPGELYIGGDGVAQGYLGRpaltaerfvpDPFAGPGsrLYRTGDLVrRRADGRLEYLGRADGQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 418 ISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSp 497
Cdd:cd12116 379 VKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAY--MVPSAFVRLD- 455
|
490
....*....|....*
gi 489502054 498 gSLPRTSSGKLRRLA 512
Cdd:cd12116 456 -ALPLTANGKLDRKA 469
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
154-514 |
1.09e-15 |
|
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: 79.88 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQ-RVGTDAATDVGC-SWLPLYHDMGLAFVLSAALAGAPLWLAPTtaFTA 231
Cdd:cd17642 187 ALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpIFGNQIIPDTAIlTVIPFHHGFGMFTTLGYLICGFRVVLMYK--FEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 232 SPFrwLSWLSDSGATMT--AAPNFAY----NLIGKYarrvsevDLGALRVTLNGGEPvdcdgLTRFAEAMAPFGFDAGAV 305
Cdd:cd17642 265 ELF--LRSLQDYKVQSAllVPTLFAFfaksTLVDKY-------DLSNLHEIASGGAP-----LSKEVGEAVAKRFKLPGI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 306 LPSYGLAESTCAVtvpvpgiglladrVIDGSGAHKHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAGYLG 385
Cdd:cd17642 331 RQGYGLTETTSAI-------------LITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVN 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 386 -----QQPIDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGL 459
Cdd:cd17642 398 npeatKALIDKDGWLHSGDIAYYDEDGhFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAA 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 460 VVAAEfrgPDEANARAELIQRVASEcgIVPSD-----VVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd17642 478 VVVLE---AGKTMTEKEVMDYVASQ--VSTAKrlrggVKFVD--EVPKGLTGKIDRRKIR 530
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
153-512 |
1.47e-15 |
|
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: 78.91 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 153 PAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSwLPLYHDMGLAF--VLSAALAGAPLWLAPTtaft 230
Cdd:cd05920 141 VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAV-LPAAHNFPLACpgVLGTLLAGGRVVLAPD---- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 231 ASPFRWLSWLSDSGATMTAA-PNFAYNLIGKYARRVSevDLGALRVTLNGGepvdcdglTRFAEAMAPfgfDAGAVLPS- 308
Cdd:cd05920 216 PSPDAAFPLIEREGVTVTALvPALVSLWLDAAASRRA--DLSSLRLLQVGG--------ARLSPALAR---RVPPVLGCt 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 309 ----YGLAEstcavtvpvpgiGLLADRVIDGSGAHKHAVLGNPI-PGMEVRIScgdQAAGN--ASREIGEIEIRGASMMA 381
Cdd:cd05920 283 lqqvFGMAE------------GLLNYTRLDDPDEVIIHTQGRPMsPDDEIRVV---DEEGNpvPPGEEGELLTRGPYTIR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 382 GYL-----GQQPIDPDDWFATGDLGYL-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRST 455
Cdd:cd05920 348 GYYrapehNARAFTPDGFYRTGDLVRRtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGE 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489502054 456 RPGLVVAaefrgPDEANARAELIQRVASECGI----VPSDVVFVSpgSLPRTSSGKLRRLA 512
Cdd:cd05920 428 RSCAFVV-----LRDPPPSAAQLRRFLRERGLaaykLPDRIEFVD--SLPLTAVGKIDKKA 481
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
41-512 |
1.97e-15 |
|
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: 78.78 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 41 AESVAAWLLDHD-RP-AAVGLVGEPTVELVAAIQGAWLAGAA-VSIlpgpvrganDQRWADATLTRFLG-IGVRTVLSQG 116
Cdd:cd12117 32 ANRLARRLRAAGvGPgDVVGVLAERSPELVVALLAVLKAGAAyVPL---------DPELPAERLAFMLAdAGAKVLLTDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 117 SYLARLRSVDTAGVTIGDLSTAAHTNrSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLrgLNQRVGTDAATDVG 196
Cdd:cd12117 103 SLAGRAGGLEVAVVIDEALDAGPAGN-PAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLV--KNTNYVTLGPDDRV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 197 CSWLPLYHDMGLAFVLSAALAGAPLWLAPT-TAFTASPFRWLswLSDSGAT---MTAApnfaynLIGKYARRVSEVdLGA 272
Cdd:cd12117 180 LQTSPLAFDASTFEIWGALLNGARLVLAPKgTLLDPDALGAL--IAEEGVTvlwLTAA------LFNQLADEDPEC-FAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 273 LRVTLNGGEPVDCDGLTRFAEAMAPfgfdaGAVLPSYGLAEST-CAVTVPVPGIGLLADRVidgsgahkhaVLGNPIPGM 351
Cdd:cd12117 251 LRELLTGGEVVSPPHVRRVLAACPG-----LRLVNGYGPTENTtFTTSHVVTELDEVAGSI----------PIGRPIANT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 352 EVRISCGD---QAAGnasrEIGEIEIRGASMMAGYLGQQ----------PIDPDD-WFATGDL-GYLGAGGLVVCGRAKE 416
Cdd:cd12117 316 RVYVLDEDgrpVPPG----VPGELYVGGDGLALGYLNRPaltaerfvadPFGPGErLYRTGDLaRWLPDGRLEFLGRIDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 417 VISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTR-PGLVVAAEFRGPDEanARAELIQRVASecGIVPSDVVFV 495
Cdd:cd12117 392 QVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRlVAYVVAEGALDAAE--LRAFLRERLPA--YMVPAAFVVL 467
|
490
....*....|....*..
gi 489502054 496 spGSLPRTSSGKLRRLA 512
Cdd:cd12117 468 --DELPLTANGKVDRRA 482
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
151-511 |
2.36e-15 |
|
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: 78.31 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 151 EGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSWLPLYHDMGLAFVLSAALAGAPLwLAPTTAFt 230
Cdd:cd05969 89 EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTN-VVYEGRF- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 231 aSPFRWLSWLSDSGAT-MTAAPNFAYNLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLtrfAEAMAPFGFdagAVLPSY 309
Cdd:cd05969 167 -DAESWYGIIERVKVTvWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAI---RWGMEVFGV---PIHDTW 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 310 GLAESTCAVTVPVPGIGLladrvidgsgahKHAVLGNPIPGMEVRISCGDqaaGNASR--EIGEIEIRGA--SMMAGYLG 385
Cdd:cd05969 240 WQTETGSIMIANYPCMPI------------KPGSMGKPLPGVKAAVVDEN---GNELPpgTKGILALKPGwpSMFRGIWN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 386 QQP----IDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRP-GL 459
Cdd:cd05969 305 DEEryknSFIDGWYLTGDLAYRDEDGYFwFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIkAF 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489502054 460 VVAAEFRGPDEAnARAELIQRVASECG--IVPSDVVFVSpgSLPRTSSGK-LRRL 511
Cdd:cd05969 385 ISLKEGFEPSDE-LKEEIINFVRQKLGahVAPREIEFVD--NLPKTRSGKiMRRV 436
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
159-431 |
2.39e-15 |
|
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: 78.17 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAaTDVGCSWLPLYHDMGLAFVLSAALAGAP------------LWLAPT 226
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQP-GDRFLSILPIWHSYERSAEYFIFACGCSqaytsirtlkddLKRVKP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 227 TAFTASPFRWLSWLSDSGATMTAAPNFAYNLIGKYarrvseVDLGALRVTLNGGEPVdCDGLTRFAEAMapfGFDagaVL 306
Cdd:cd17640 175 HYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF------LSGGIFKFGISGGGAL-PPHVDTFFEAI---GIE---VL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 307 PSYGLAEstcavTVPVPGIGLLaDRVIDGSgahkhavLGNPIPGMEVRIScgDQAAGNASR--EIGEIEIRGASMMAGYL 384
Cdd:cd17640 242 NGYGLTE-----TSPVVSARRL-KCNVRGS-------VGRPLPGTEIKIV--DPEGNVVLPpgEKGIVWVRGPQVMKGYY 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489502054 385 GQ-----QPIDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIA-GRNIFPTEVE 431
Cdd:cd17640 307 KNpeatsKVLDSDGWFNTGDLGWLTCGGeLVLTGRAKDTIVLSnGENVEPQPIE 360
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
57-512 |
2.53e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.43 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 57 VGLVGEPTVELVAAIQGAWLAGAAVSILpgpvrganDQRWADATLTRFLG-IGVRTVLSQGSYLARLRSVDTAGVTIGDL 135
Cdd:PRK12467 565 VGIAVERSIEMVVGLLAVLKAGGAYVPL--------DPEYPQDRLAYMLDdSGVRLLLTQSHLLAQLPVPAGLRSLCLDE 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 136 STAAHTNRSA----TPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTdAATDVGCSWLPLYHDMGLAFV 211
Cdd:PRK12467 637 PADLLCGYSGhnpeVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQL-AADDSMLMVSTFAFDLGVTEL 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 212 LSAALAGAPLWLAP-TTAFTASPFrwLSWLSDSGATMTAAPNFAYNLIGKYARrvSEVDLGALRVTLnGGEPVDCDGLTR 290
Cdd:PRK12467 716 FGALASGATLHLLPpDCARDAEAF--AALMADQGVTVLKIVPSHLQALLQASR--VALPRPQRALVC-GGEALQVDLLAR 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 291 FAEAMapfgfDAGAVLPSYGLAESTCAVTVPVPGiglLADRVIDGSgahkhaVLGNPIPGMEVRI--SCGDQAAGNAsre 368
Cdd:PRK12467 791 VRALG-----PGARLINHYGPTETTVGVSTYELS---DEERDFGNV------PIGQPLANLGLYIldHYLNPVPVGV--- 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 369 IGEIEIRGASMMAGYLGQ----------QPIDPDD--WFATGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAA 435
Cdd:PRK12467 854 VGELYIGGAGLARGYHRRpaltaerfvpDPFGADGgrLYRTGDLArYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLL 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 436 QVRGVREGAVVAL-GTGDRSTRPGLVVAAEFRGPDEANARAEL---IQRVASECgIVPSDVVFVSpgSLPRTSSGKLRRL 511
Cdd:PRK12467 934 AQPGVREAVVLAQpGDAGLQLVAYLVPAAVADGAEHQATRDELkaqLRQVLPDY-MVPAHLLLLD--SLPLTPNGKLDRK 1010
|
.
gi 489502054 512 A 512
Cdd:PRK12467 1011 A 1011
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
36-512 |
3.84e-15 |
|
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: 77.70 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 36 EVHGLAESVAAWLLDH----DRPAAVGLvgEPTVELVAAIQGAWLAGAA-VSILPGPVRGANDQRWADAtltrflgiGVR 110
Cdd:cd17646 28 ELDERANRLAHLLRARgvgpEDRVAVLL--PRSADLVVALLAVLKAGAAyLPLDPGYPADRLAYMLADA--------GPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 111 TVLSQGSYLARLRSVDTAGVTIGDLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTD 190
Cdd:cd17646 98 VVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 191 AATDVGCSwLPLYHDMGLAFVLSAALAGAPLWLAPTTAFTaSPFRWLSWLSDSGATMTaapNFAYNLIGKYARRVSEVDL 270
Cdd:cd17646 178 PGDRVLQK-TPLSFDVSVWELFWPLVAGARLVVARPGGHR-DPAYLAALIREHGVTTC---HFVPSMLRVFLAEPAAGSC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 271 GALRVTLNGGEPVDCDGLTRFAEAMapfgfdaGAVL-PSYGLAESTCAVTvpvpgigllADRVIDGSGAHKHAVlGNPIP 349
Cdd:cd17646 253 ASLRRVFCSGEALPPELAARFLALP-------GAELhNLYGPTEAAIDVT---------HWPVRGPAETPSVPI-GRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 350 GMEVRISCGD---QAAGnasrEIGEIEIRGASMMAGYLGQQPIDPD----DWFA-------TGDLGYLGAGGLV-VCGRA 414
Cdd:cd17646 316 NTRLYVLDDAlrpVPVG----VPGELYLGGVQLARGYLGRPALTAErfvpDPFGpgsrmyrTGDLARWRPDGALeFLGRS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 415 KEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTR--PGLVVAAEFRGPDEANARAELIQRVASEcgIVPSDV 492
Cdd:cd17646 392 DDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARlvGYVVPAAGAAGPDTAALRAHLAERLPEY--MVPAAF 469
|
490 500
....*....|....*....|
gi 489502054 493 VFVSpgSLPRTSSGKLRRLA 512
Cdd:cd17646 470 VVLD--ALPLTANGKLDRAA 487
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
148-514 |
5.02e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 77.51 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 148 VASEGPAVLQGTAGSTGAPRTAILS----PGAVLSNLRGLnqrvGTDAATDVGCSWLPLYHDMGLAFVLSAALAGAPLWL 223
Cdd:PRK07786 171 IPNDSPALIMYTSGTTGRPKGAVLThanlTGQAMTCLRTN----GADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 224 APTTAFtaSPFRWLSWLSDSGATMTAAPNFAYNLIGKyARRVSEVDLgALRVTLNGGEPVDCDGLTRFAEAmapfgFDAG 303
Cdd:PRK07786 247 YPLGAF--DPGQLLDVLEAEKVTGIFLVPAQWQAVCA-EQQARPRDL-ALRVLSWGAAPASDTLLRQMAAT-----FPEA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 304 AVLPSYGLAES---TCavtvpvpgiglladrVIDGSGA-HKHAVLGNPIPGMEVRI---SCGDQAAGnasrEIGEIEIRG 376
Cdd:PRK07786 318 QILAAFGQTEMspvTC---------------MLLGEDAiRKLGSVGKVIPTVAARVvdeNMNDVPVG----EVGEIVYRA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 377 ASMMAGYLgQQPIDPDD-----WFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVValGT 450
Cdd:PRK07786 379 PTLMSGYW-NNPEATAEafaggWFHSGDLVRQDEEGYVwVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVI--GR 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489502054 451 GDRSTRPGLVVAAEFRGPDEANARAELIQ----RVASECGivPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:PRK07786 456 ADEKWGEVPVAVAAVRNDDAALTLEDLAEfltdRLARYKH--PKALEIVD--ALPRNPAGKVLKTELR 519
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
149-515 |
7.35e-15 |
|
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: 76.70 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 149 ASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLnQRVGTDAATDVGCSWLPLyhDM----GLAFVLSAALagapLWLA 224
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGV-QFPFNLFPRDGDLYWTPA--DWawigGLLDVLLPSL----YFGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 225 PTTAFTASPF---RWLSWLSDSGATMTAAPNFAYNLIGKYARRVSEVDLgALRVTLNGGEPVdcdGLTRFAEAMAPFGFD 301
Cdd:cd05971 159 PVLAHRMTKFdpkAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQV-KLRAIATGGESL---GEELLGWAREQFGVE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 302 AGAVlpsYGLAE-----STCAVTVPVpgiglladrvidgsgahKHAVLGNPIPGMEVRIsCGDQAAGNASREIGEIEIR- 375
Cdd:cd05971 235 VNEF---YGQTEcnlviGNCSALFPI-----------------KPGSMGKPIPGHRVAI-VDDNGTPLPPGEVGEIAVEl 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 376 -GASMMAGYLGQQPIDPD----DWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALG 449
Cdd:cd05971 294 pDPVAFLGYWNNPSATEKkmagDWLLTGDLGRKDSDGYFwYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIP 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489502054 450 TGDRSTR-PGLVVAAEFRGPDEANARaELIQRVASECGIVPSDVVFVSPGSLPRTSSGKLRRLAVRR 515
Cdd:cd05971 374 DPIRGEIvKAFVVLNPGETPSDALAR-EIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
341-518 |
1.06e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 76.36 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 341 HAVlGNPIPGMEVRISCGDQAAGNASrEIGEIEIRGASMMAGYLG----QQPIDPDDWFATGDLGYLGAGGLV-VCGRAK 415
Cdd:PRK07638 307 NSV-GRPFHNVQVRICNEAGEEVQKG-EIGTVYVKSPQFFMGYIIggvlARELNADGWMTVRDVGYEDEEGFIyIVGREK 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 416 EVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEfrgPDEANARAELIQRVASEcgIVPSDVVFV 495
Cdd:PRK07638 385 NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGS---ATKQQLKSFCLQRLSSF--KIPKEWHFV 459
|
170 180
....*....|....*....|...
gi 489502054 496 SpgSLPRTSSGKLRRLAVRRSLE 518
Cdd:PRK07638 460 D--EIPYTNSGKIARMEAKSWIE 480
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
131-446 |
1.21e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 76.06 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 131 TIGDLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVgtdaATDVGCSWL---PLYHDMG 207
Cdd:PRK09029 115 ALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLM----PFTAQDSWLlslPLFHVSG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 208 LAFVlsaalagaplWlapttaftaspfRWLSwlsdSGATMT--AAPNFAYNLIGkyarrVSEVDL--------------- 270
Cdd:PRK09029 191 QGIV----------W------------RWLY----AGATLVvrDKQPLEQALAG-----CTHASLvptqlwrlldnrsep 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 271 GALRVTLNGGE--PVDcdgLTRFAEAMapfGFD--AGavlpsYGLAE--ST-CAVtvpvpgiglladrVIDGsgahkHAV 343
Cdd:PRK09029 240 LSLKAVLLGGAaiPVE---LTEQAEQQ---GIRcwCG-----YGLTEmaSTvCAK-------------RADG-----LAG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 344 LGNPIPGMEVRISCGdqaagnasreigEIEIRGASMMAGYLGQQPIDP----DDWFATGDLGYLGAGGLVVCGRAKEV-I 418
Cdd:PRK09029 291 VGSPLPGREVKLVDG------------EIWLRGASLALGYWRQGQLVPlvndEGWFATRDRGEWQNGELTILGRLDNLfF 358
|
330 340
....*....|....*....|....*...
gi 489502054 419 SiAGRNIFPTEVELVAAQVRGVREGAVV 446
Cdd:PRK09029 359 S-GGEGIQPEEIERVINQHPLVQQVFVV 385
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
159-516 |
2.04e-14 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 76.50 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAaTDVGCSWLPLYHdmglAFVLSAALAGaPLWLAPTTAFTASPfrwls 238
Cdd:PRK08633 790 SSGSEGEPKGVMLSHHNILSNIEQISDVFNLRN-DDVILSSLPFFH----SFGLTVTLWL-PLLEGIKVVYHPDP----- 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 239 wlSDS----------GAT-MTAAPNFaynlIGKYAR--RVSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapFGFDagaV 305
Cdd:PRK08633 859 --TDAlgiaklvakhRATiLLGTPTF----LRLYLRnkKLHPLMFASLRLVVAGAEKLKPEVADAFEEK---FGIR---I 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 306 LPSYGLAESTCAVTVPVPgigllaDRVIDGSG---AHKHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAG 382
Cdd:PRK08633 927 LEGYGATETSPVASVNLP------DVLAADFKrqtGSKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKG 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 383 YLGQ--------QPIDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDR 453
Cdd:PRK08633 1001 YLGDpektaeviKDIDGIGWYVTGDKGHLDEDGfLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVPDE 1080
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489502054 454 STRPGLVVAAEfrgpdEANARAELIQRVASECGI----VPSDVVFVSpgSLPRTSSGKL-----RRLAVRRS 516
Cdd:PRK08633 1081 KKGEKLVVLHT-----CGAEDVEELKRAIKESGLpnlwKPSRYFKVE--ALPLLGSGKLdlkglKELALALL 1145
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
34-447 |
2.35e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 75.45 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 34 WPEVHGLAESVAAWLL---DHDRPAAVGLVGEPTVELVAAIQGAWLAGAAVSilpgpvrGANDQRWADATLTRFLGIGVR 110
Cdd:PRK13388 29 WREVLAEAAARAAALIalaDPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLV-------GLNTTRRGAALAADIRRADCQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 111 TVLSQGSYLARLRSVDTAGVTIGDLSTAAHTNRSA--------TPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRG 182
Cdd:PRK13388 102 LLVTDAEHRPLLDGLDLPGVRVLDVDTPAYAELVAaagaltphREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 183 LNQRVGTDAAtDVGCSWLPLYHDMGLAFVLSAALA-GAPLWLAPTtaFTASPFrwlswLSD---SGATMtaapnfaYNLI 258
Cdd:PRK13388 182 LTERFGLTRD-DVCYVSMPLFHSNAVMAGWAPAVAsGAAVALPAK--FSASGF-----LDDvrrYGATY-------FNYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 259 GKyarrvsevdlgALRVTLNGGE-PVDCDGLTRFA---EA----MAPFGFDAGA-VLPSYGLAESTCAVTvPVPGI--GL 327
Cdd:PRK13388 247 GK-----------PLAYILATPErPDDADNPLRVAfgnEAsprdIAEFSRRFGCqVEDGYGSSEGAVIVV-REPGTppGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 328 LadrvidGSGAHKHAVLgNPIPGMEVRISCGDQ--AAGNASREIGEI-EIRGASMMAGYLGQQPIDPD----DWFATGDL 400
Cdd:PRK13388 315 I------GRGAPGVAIY-NPETLTECAVARFDAhgALLNADEAIGELvNTAGAGFFEGYYNNPEATAErmrhGMYWSGDL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489502054 401 GYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVA 447
Cdd:PRK13388 388 AYRDADGwIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYA 435
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
303-518 |
2.50e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 75.46 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 303 GAVLPSY-GLAESTCAVTVpVPGIGLLADrviDGSGAhKHAVLGNPIPGMEVRIScgdQAAGN--ASREIGEIEIRGASM 379
Cdd:PRK07470 305 GKVLVQYfGLGEVTGNITV-LPPALHDAE---DGPDA-RIGTCGFERTGMEVQIQ---DDEGRelPPGETGEICVIGPAV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 380 MAGYLGQQPIDP----DDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVvaLGTGDR- 453
Cdd:PRK07470 377 FAGYYNNPEANAkafrDGWFRTGDLGHLDARGFLyITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAV--LGVPDPv 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489502054 454 --STRPGLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVRRSLE 518
Cdd:PRK07470 455 wgEVGVAVCVARDGAPVDEAELLAWLDGKVARY--KLPKRFFFWD--ALPKSGYGKITKKMVREELE 517
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
159-514 |
3.12e-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: 74.71 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAAtDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTAFtASPFRWLS 238
Cdd:cd17649 102 TSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPG-DRELQFASFNFDGAHEQLLPPLICGACVVLRPDELW-ASADELAE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 239 WLSDSGATMTAAPNFAYNLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAmapfgfdAGAVLPSYGLAESTCAV 318
Cdd:cd17649 180 MVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKA-------PVRLFNAYGPTEATVTP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 319 TVPVPGIGLLAdrvidgsgAHKHAVLGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLGQQPI-------DP 391
Cdd:cd17649 253 LVWKCEAGAAR--------AGASMPIGRPLGGRSAYI-LDADLNPVPVGVTGELYIGGEGLARGYLGRPELtaerfvpDP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 392 DD-----WFATGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVV--AA 463
Cdd:cd17649 324 FGapgsrLYRTGDLArWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVlrAA 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489502054 464 EFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd17649 404 AAQPELRAQLRTALRASLPDY--MVPAHLVFLA--RLPLTPNGKLDRKALP 450
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
150-415 |
4.50e-14 |
|
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: 74.56 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 150 SEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTD-AATDVGCSWLPLYHDMGLAFVLSAALAGA------PLW 222
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELlGPDDRYLAYLPLAHIFELAAENVCLYRGGtigygsPRT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 223 LAPT--------------TAFTASPFRW-------LSWLSDSGATMTAAPNFAYNLIGKYAR--------------RVSE 267
Cdd:cd17639 167 LTDKskrgckgdltefkpTLMVGVPAIWdtirkgvLAKLNPMGGLKRTLFWTAYQSKLKALKegpgtplldelvfkKVRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 268 VDLGALRVTLNGGEPVDCDglT-RFaeaMAPFGfdaGAVLPSYGLAESTCAVTVPVPGiGLLADRVidgsgahkhavlGN 346
Cdd:cd17639 247 ALGGRLRYMLSGGAPLSAD--TqEF---LNIVL---CPVIQGYGLTETCAGGTVQDPG-DLETGRV------------GP 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502054 347 PIPGMEVRIScgDQAAGN----ASREIGEIEIRGASMMAGYLGQ-----QPIDPDDWFATGDLGYLGAGG-LVVCGRAK 415
Cdd:cd17639 306 PLPCCEIKLV--DWEEGGystdKPPPRGEILIRGPNVFKGYYKNpektkEAFDGDGWFHTGDIGEFHPDGtLKIIDRKK 382
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
138-514 |
8.85e-14 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 73.89 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 138 AAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPG--AV-----LSNLRGLNQRVGTDAATDVGcsWLplyhdMGLAF 210
Cdd:cd05967 217 AKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGghAValnwsMRNIYGIKPGDVWWAASDVG--WV-----VGHSY 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 211 VLSaalagAPLWLAPTTAF-------TASPFRWLSWLSDSGAT-MTAAPNfAYNLIGKY---ARRVSEVDLGALRVTLNG 279
Cdd:cd05967 290 IVY-----GPLLHGATTVLyegkpvgTPDPGAFWRVIEKYQVNaLFTAPT-AIRAIRKEdpdGKYIKKYDLSSLRTLFLA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 280 GEPVDCDGLTrFAEAMAPFgfdagAVLPSYGLAESTCAVTVPVPGIGLLADrvidgsgahKHAVLGNPIPGMEVRIScgd 359
Cdd:cd05967 364 GERLDPPTLE-WAENTLGV-----PVIDHWWQTETGWPITANPVGLEPLPI---------KAGSPGKPVPGYQVQVL--- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 360 QAAGN--ASREIGEIEIRG--------------ASMMAGYLGQQPidpdDWFATGDLGYLGAGG-LVVCGRAKEVISIAG 422
Cdd:cd05967 426 DEDGEpvGPNELGNIVIKLplppgclltlwkndERFKKLYLSKFP----GYYDTGDAGYKDEDGyLFIMGRTDDVINVAG 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 423 RNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRP-GLVVAAEFRGPDEANARAELIQRVASECGIV--PSDVVFVSpgS 499
Cdd:cd05967 502 HRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPlGLVVLKEGVKITAEELEKELVALVREQIGPVaaFRLVIFVK--R 579
|
410
....*....|....*
gi 489502054 500 LPRTSSGKLRRLAVR 514
Cdd:cd05967 580 LPKTRSGKILRRTLR 594
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
95-480 |
9.45e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 73.78 E-value: 9.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 95 RWADATLTRFLGIGvRTVLSQGSYLARLRSVDTAGVTIGdlstaahtnrsaTPVASEGPAVLQGTAGSTGAPRTAILSPG 174
Cdd:PRK09274 131 GWGKPSVRRLVTVG-GRLLWGGTTLATLLRDGAAAPFPM------------ADLAPDDMAAILFTSGSTGTPKGVVYTHG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 175 ---AVLSNLRGL--NQRVGTDAATdvgcswLPLyhdmglaFVL-SAALAGAPLW--LAPTTAFTASPFRWLSWLSDSGAT 246
Cdd:PRK09274 198 mfeAQIEALREDygIEPGEIDLPT------FPL-------FALfGPALGMTSVIpdMDPTRPATVDPAKLFAAIERYGVT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 247 -MTAAPnfAY-NLIGKYARRvSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPfgfdaGA-VLPSYGLAEStcavtVPVP 323
Cdd:PRK09274 265 nLFGSP--ALlERLGRYGEA-NGIKLPSLRRVISAGAPVPIAVIERFRAMLPP-----DAeILTPYGATEA-----LPIS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 324 GIG---LLADRViDGSGAHKHAVLGNPIPGMEVR--------ISCGDQAAGNASREIGEIEIRGASMMAGYLgQQP---- 388
Cdd:PRK09274 332 SIEsreILFATR-AATDNGAGICVGRPVDGVEVRiiaisdapIPEWDDALRLATGEIGEIVVAGPMVTRSYY-NRPeatr 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 389 ----IDPDD--WFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRsTRPGLVV 461
Cdd:PRK09274 410 lakiPDGQGdvWHRMGDLGYLDAQGrLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGA-QRPVLCV 488
|
410
....*....|....*....
gi 489502054 462 AAEfrgPDEANARAELIQR 480
Cdd:PRK09274 489 ELE---PGVACSKSALYQE 504
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
134-508 |
1.02e-13 |
|
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: 73.77 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 134 DLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRV-----------GTDAATDVGCSWLpL 202
Cdd:cd17634 215 DLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVfdygpgdiywcTADVGWVTGHSYL-L 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 203 YHDMgLAFVLSAALAGAPLWLAPTtaftaspfRWLSWLSDSGAT-MTAAPNFAYNLIGKYARRVSEVDLGALRVTLNGGE 281
Cdd:cd17634 294 YGPL-ACGATTLLYEGVPNWPTPA--------RMWQVVDKHGVNiLYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 282 PVDCDGLTRFAEAMapfGFDAGAVLPSYGLAESTCAVTVPVPGIGLL----ADRVIDGSGAHKHAVLGNPIP-GMEVRIS 356
Cdd:cd17634 365 PINPEAYEWYWKKI---GKEKCPVVDTWWQTETGGFMITPLPGAIELkagsATRPVFGVQPAVVDNEGHPQPgGTEGNLV 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 357 CGDQAAGNASREIGEIEIRGASMMAGYlgqqpidpDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAA 435
Cdd:cd17634 442 ITDPWPGQTRTLFGDHERFEQTYFSTF--------KGMYFSGDGARRDEDGYYwITGRSDDVINVAGHRLGTAEIESVLV 513
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489502054 436 QVRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEANARAELIQRVASECG--IVPSDVVFVspGSLPRTSSGKL 508
Cdd:cd17634 514 AHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGplATPDVVHWV--DSLPKTRSGKI 586
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
121-431 |
1.03e-13 |
|
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: 73.61 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 121 RLRSVDTAgVTIGDLSTAAHTNRSATPVASEGP---AVLQGTAGSTGAPRTAILSPGAVLSNLRGLnQRVGTDAATDVGC 197
Cdd:cd17641 126 RLISFEDV-VALGRALDRRDPGLYEREVAAGKGedvAVLCTTSGTTGKPKLAMLSHGNFLGHCAAY-LAADPLGPGDEYV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 198 SWLPLYHDMGLAFVLsaalaGAPLWL--------APTTA-----------FTASPFRWLSWLSDSGATMTAAPNF----- 253
Cdd:cd17641 204 SVLPLPWIGEQMYSV-----GQALVCgfivnfpeEPETMmedlreigptfVLLPPRVWEGIAADVRARMMDATPFkrfmf 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 254 -----AYNLIGKYARRVSEVDLG-----------------------ALRVTLNGGEPVDCDgLTRFAEAMapfGFDAGAV 305
Cdd:cd17641 279 elgmkLGLRALDRGKRGRPVSLWlrlaswladallfrplrdrlgfsRLRSAATGGAALGPD-TFRFFHAI---GVPLKQL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 306 lpsYGLAESTCAVTVpvpgiglladrviDGSGAHKHAVLGNPIPGMEVRIScgdqaagnasrEIGEIEIRGASMMAGYLG 385
Cdd:cd17641 355 ---YGQTELAGAYTV-------------HRDGDVDPDTVGVPFPGTEVRID-----------EVGEILVRSPGVFVGYYK 407
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489502054 386 QQP-----IDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIA-GRNIFPTEVE 431
Cdd:cd17641 408 NPEataedFDEDGWLHTGDAGYFKENGhLVVIDRAKDVGTTSdGTRFSPQFIE 460
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
265-511 |
1.08e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 73.47 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 265 VSEVDLGAL--RVTLNGGEPVDCDGLTRFAEAmapfgFDAGAVLPSYGLAESTCavtvpvpgIGLLADRVIDGSGAHKHA 342
Cdd:PLN02330 295 VEEFDLSKLklQAIMTAAAPLAPELLTAFEAK-----FPGVQVQEAYGLTEHSC--------ITLTHGDPEKGHGIAKKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 343 VLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAGYLGQQ-----PIDPDDWFATGDLGYL-GAGGLVVCGRAKE 416
Cdd:PLN02330 362 SVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKeetdrTIDEDGWLHTGDIGYIdDDGDIFIVDRIKE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 417 VISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEfrgPDEANARAELIQRVASECGIVPSDVVFVS 496
Cdd:PLN02330 442 LIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVIN---PKAKESEEDILNFVAANVAHYKKVRVVQF 518
|
250
....*....|....*.
gi 489502054 497 PGSLPRTSSGK-LRRL 511
Cdd:PLN02330 519 VDSIPKSLSGKiMRRL 534
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
137-508 |
1.75e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 72.69 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 137 TAAHTNRSATPVASEGP---AVLQGTAGSTGAPRTAILSPGAVLSNLRGlNQRVGTDAATDVGCSWLPLYHDMGLAFVLS 213
Cdd:PRK08314 173 KEALAAGLAPPPHTAGPddlAVLPYTSGTTGVPKGCMHTHRTVMANAVG-SVLWSNSTPESVVLAVLPLFHVTGMVHSMN 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 214 AAL-AGA-----PLWLAPTTAFTASPFRWLSWLSDSgaTMT----AAPNFAynligkyarrvsEVDLGALRVTLNGGEPV 283
Cdd:PRK08314 252 APIyAGAtvvlmPRWDREAAARLIERYRVTHWTNIP--TMVvdflASPGLA------------ERDLSSLRYIGGGGAAM 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 284 dcdgltrfAEAMAP-----FGFDagaVLPSYGLAEsTCAVTVPVPgigllADRvidgsgaHKHAVLGNPIPGMEVRISCG 358
Cdd:PRK08314 318 --------PEAVAErlkelTGLD---YVEGYGLTE-TMAQTHSNP-----PDR-------PKLQCLGIPTFGVDARVIDP 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 359 DQAAGNASREIGEIEIRGASMMAGYLGQQ--------PIDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTE 429
Cdd:PRK08314 374 ETLEELPPGEVGEIVVHGPQVFKGYWNRPeataeafiEIDGKRFFRTGDLGRMDEEGyFFITDRLKRMINASGFKVWPAE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 430 VELVAAQVRGVREGAVVALgtgdRSTRPG------LVVAAEFRGPDEANaraELI----QRVASEcgIVPSDVVFVSpgS 499
Cdd:PRK08314 454 VENLLYKHPAIQEACVIAT----PDPRRGetvkavVVLRPEARGKTTEE---EIIawarEHMAAY--KYPRIVEFVD--S 522
|
....*....
gi 489502054 500 LPRTSSGKL 508
Cdd:PRK08314 523 LPKSGSGKI 531
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
159-514 |
3.30e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 72.09 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGA-VLSNLRGLNQRVGTDAATDVGCSWLPLYH--DMGLAFvlSAALAGAPLWLAPTTAFTASPFR 235
Cdd:PRK06018 185 TSGTTGDPKGVLYSHRSnVLHALMANNGDALGTSAADTMLPVVPLFHanSWGIAF--SAPSMGTKLVMPGAKLDGASVYE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 236 WLSwlsDSGATMTAAPNFAYNLIGKYARRvSEVDLGALRVTLNGGEPVDCDGLTRFAEamapfgFDAGaVLPSYGLAEst 315
Cdd:PRK06018 263 LLD---TEKVTFTAGVPTVWLMLLQYMEK-EGLKLPHLKMVVCGGSAMPRSMIKAFED------MGVE-VRHAWGMTE-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 316 cavTVPVPGIGLLADRVIDGSGAHKHAVL---GNPIPGMEVRISCGDQAA----GNASreiGEIEIRGASMMAGYL--GQ 386
Cdd:PRK06018 330 ---MSPLGTLAALKPPFSKLPGDARLDVLqkqGYPPFGVEMKITDDAGKElpwdGKTF---GRLKVRGPAVAAAYYrvDG 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 387 QPIDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEf 465
Cdd:PRK06018 404 EILDDDGFFDTGDVATIDAYGYMrITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLK- 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489502054 466 rgPDEANARAELIQRVASECG--IVPSDVVFVspGSLPRTSSGKLRRLAVR 514
Cdd:PRK06018 483 --PGETATREEILKYMDGKIAkwWMPDDVAFV--DAIPHTATGKILKTALR 529
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
41-513 |
4.15e-13 |
|
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: 71.53 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 41 AESVAAWLLDH-DRPA-AVGLVGEPTVELVAAIQGAWLAGAA-VSIlpgpvrganDQRWADATLTRFLG-IGVRTVLSQG 116
Cdd:cd12114 22 ARRVAGALKAAgVRPGdLVAVTLPKGPEQVVAVLGILAAGAAyVPV---------DIDQPAARREAILAdAGARLVLTDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 117 SYLARLRSVDTAGVTIGDLSTAAHTNrSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAAtDVG 196
Cdd:cd12114 93 PDAQLDVAVFDVLILDLDALAAPAPP-PPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPD-DRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 197 CSWLPLYHDMGLAFVLSAALAGAPLWLaPTTAFTASPFRWLSWLSDSGATM-TAAPNFAYNLIGKYARrvSEVDLGALRV 275
Cdd:cd12114 171 LALSSLSFDLSVYDIFGALSAGATLVL-PDEARRRDPAHWAELIERHGVTLwNSVPALLEMLLDVLEA--AQALLPSLRL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 276 TLNGGEPVDCDGLTRFAEAMApfgfdaGAVLPSYGLAEST------CAVTVPVPgigllADRVIDgsgahkhavLGNPIP 349
Cdd:cd12114 248 VLLSGDWIPLDLPARLRALAP------DARLISLGGATEAsiwsiyHPIDEVPP-----DWRSIP---------YGRPLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 350 GMEVRI------SCGDQAAGnasreigEIEIRGASMMAGYLGQQ-------PIDPDD--WFATGDLG-YLGAGGLVVCGR 413
Cdd:cd12114 308 NQRYRVldprgrDCPDWVPG-------ELWIGGRGVALGYLGDPeltaarfVTHPDGerLYRTGDLGrYRPDGTLEFLGR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 414 AKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVA-AEFRGPDEANARAELIQRVASecGIVPSDV 492
Cdd:cd12114 381 RDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPdNDGTPIAPDALRAFLAQTLPA--YMIPSRV 458
|
490 500
....*....|....*....|.
gi 489502054 493 VFVSpgSLPRTSSGKLRRLAV 513
Cdd:cd12114 459 IALE--ALPLTANGKVDRAAL 477
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
147-514 |
4.65e-13 |
|
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: 71.18 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 147 PVASE-GPAVLQGTAGSTGAPRtailspGAVLSNlRG--LNQrVGTDAATDVGCS----W-LPLYHDMGLAFVLS-AALA 217
Cdd:cd12118 128 PPADEwDPIALNYTSGTTGRPK------GVVYHH-RGayLNA-LANILEWEMKQHpvylWtLPMFHCNGWCFPWTvAAVG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 218 GAPLWLAPTTAftasPFRWlSWLSDSGAT-MTAAPNfAYNLIGKYARRVSEVDLGALRVTLNGGEPVdcdglTRFAEAMA 296
Cdd:cd12118 200 GTNVCLRKVDA----KAIY-DLIEKHKVThFCGAPT-VLNMLANAPPSDARPLPHRVHVMTAGAPPP-----AAVLAKME 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 297 PFGFDagaVLPSYGLAESTCAVTV----------P------------VPGIGLLADRVIDgsgahkhAVLGNPIPGmevr 354
Cdd:cd12118 269 ELGFD---VTHVYGLTETYGPATVcawkpewdelPteerarlkarqgVRYVGLEEVDVLD-------PETMKPVPR---- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 355 iscgdqaagnASREIGEIEIRGASMMAGYLGqqpiDP--------DDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNI 425
Cdd:cd12118 335 ----------DGKTIGEIVFRGNIVMKGYLK----NPeataeafrGGWFHSGDLAVIHPDGYIeIKDRSKDIIISGGENI 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 426 FPTEVELVAAQVRGVREGAVVAlgtgdrstRP----GLVVAA--EFRGPDEANArAELIQ--RVASECGIVPSDVVFvsp 497
Cdd:cd12118 401 SSVEVEGVLYKHPAVLEAAVVA--------RPdekwGEVPCAfvELKEGAKVTE-EEIIAfcREHLAGFMVPKTVVF--- 468
|
410
....*....|....*..
gi 489502054 498 GSLPRTSSGKLRRLAVR 514
Cdd:cd12118 469 GELPKTSTGKIQKFVLR 485
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
138-515 |
5.41e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 71.92 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 138 AAHTNRSAtpvasEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSwLPLYHDMGL-AFVLSAAL 216
Cdd:PRK06814 785 VYFCNRDP-----DDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNA-LPVFHSFGLtGGLVLPLL 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 217 AGAPLWLAPttaftaSP--FRWLSWL-SDSGAT-MTAAPNFaynLIGkYARRVSEVDLGALRVTLNGGEPVDCDglTR-- 290
Cdd:PRK06814 859 SGVKVFLYP------SPlhYRIIPELiYDTNATiLFGTDTF---LNG-YARYAHPYDFRSLRYVFAGAEKVKEE--TRqt 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 291 FAEAmapFGFdagAVLPSYGLAESTCAVTVPVPgiglLADRVidGSgahkhavLGNPIPGMEVRIscgDQAAGnaSREIG 370
Cdd:PRK06814 927 WMEK---FGI---RILEGYGVTETAPVIALNTP----MHNKA--GT-------VGRLLPGIEYRL---EPVPG--IDEGG 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 371 EIEIRGASMMAGYLGQ------QPIdPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREG 443
Cdd:PRK06814 983 RLFVRGPNVMLGYLRAenpgvlEPP-ADGWYDTGDIVTIDEEGFItIKGRAKRFAKIAGEMISLAAVEELAAELWPDALH 1061
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489502054 444 AVVALGTGDRSTRPGLVVaaefrgpDEANARAELIQRVASECGI----VPSDVVFVSpgSLPRTSSGKLRRLAVRR 515
Cdd:PRK06814 1062 AAVSIPDARKGERIILLT-------TASDATRAAFLAHAKAAGAselmVPAEIITID--EIPLLGTGKIDYVAVTK 1128
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
145-477 |
5.63e-13 |
|
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: 70.96 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 145 ATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAaTDVGCSWLPLYH--------------DMGLAF 210
Cdd:cd05932 131 RPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEE-NDRMLSYLPLAHvtervfveggslygGVLVAF 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 211 VLSAALAGAPLWLAPTTAFTASPFRWLSWLSDSGATMTAA--------PnfaynLIGKYARRVSEVDLG--ALRVTLNGG 280
Cdd:cd05932 210 AESLDTFVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQQklnlllkiP-----VVNSLVKRKVLKGLGldQCRLAGCGS 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 281 EPVDCDGLTRFAEamapFGFDagaVLPSYGLAESTCAVTVPVPGiglladrvidgsgAHKHAVLGNPIPGMEVRIScgdq 360
Cdd:cd05932 285 APVPPALLEWYRS----LGLN---ILEAYGMTENFAYSHLNYPG-------------RDKIGTVGNAGPGVEVRIS---- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 361 aagnasrEIGEIEIRGASMMAGYLGQ-----QPIDPDDWFATGDLGYLGA-GGLVVCGRAKEVISIA-GRNIFPTEVELV 433
Cdd:cd05932 341 -------EDGEILVRSPALMMGYYKDpeataEAFTADGFLRTGDKGELDAdGNLTITGRVKDIFKTSkGKYVAPAPIENK 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489502054 434 AAQVRGVRegAVVALGTGdrSTRP-GLVVAAEF-RGPDEANARAEL 477
Cdd:cd05932 414 LAEHDRVE--MVCVIGSG--LPAPlALVVLSEEaRLRADAFARAEL 455
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
345-511 |
5.96e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 70.88 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 345 GNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASM-MAGYLGQ----QPIDPDDWFATGDLGYLGAGGLV-VCGRAKEVI 418
Cdd:PRK12406 327 GKAAPGAELRF-VDEDGRPLPQGEIGEIYSRIAGNpDFTYHNKpekrAEIDRGGFITSGDVGYLDADGYLfLCDRKRDMV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 419 SIAGRNIFPTEVELVAAQVRGVREGAVvaLGTGDRSTRPGLVVAAEF---RGPDEANARAELIQRVASEcgIVPSDVVFV 495
Cdd:PRK12406 406 ISGGVNIYPAEIEAVLHAVPGVHDCAV--FGIPDAEFGEALMAVVEPqpgATLDEADIRAQLKARLAGY--KVPKHIEIM 481
|
170
....*....|....*...
gi 489502054 496 SpgSLPRTSSGKL--RRL 511
Cdd:PRK12406 482 A--ELPREDSGKIfkRRL 497
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
120-517 |
6.32e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 70.99 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 120 ARLRSVDTAGVTIgdlSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPgavlSNLRGLNQRVGTDAATDVGCSW 199
Cdd:PRK09088 107 GRTDVEDLAAFIA---SADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSE----RNLQQTAHNFGVLGRVDAHSSF 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 200 L---PLYHDMGLAFVLSAALA-GAPLWLAPttAFtaSPFRWLSWLSDSGATMT---AAPNFAYNLigkyaRRVSEVDLGA 272
Cdd:PRK09088 180 LcdaPMFHIIGLITSVRPVLAvGGSILVSN--GF--EPKRTLGRLGDPALGIThyfCVPQMAQAF-----RAQPGFDAAA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 273 LR---VTLNGGEPVDCDGLTRFAEAMAPfgfdagaVLPSYGLAESTCavtvpVPGIGLLADRVIDGSGAhkhavLGNPIP 349
Cdd:PRK09088 251 LRhltALFTGGAPHAAEDILGWLDDGIP-------MVDGFGMSEAGT-----VFGMSVDCDVIRAKAGA-----AGIPTP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 350 GMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYL-----GQQPIDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGR 423
Cdd:PRK09088 314 TVQTRV-VDDQGNDCPAGVPGELLLRGPNLSPGYWrrpqaTARAFTGDGWFRTGDIARRDADGFFwVVDRKKDMFISGGE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 424 NIFPTEVELVAAQVRGVREGAVVALGtgdrSTRPG-----LVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpg 498
Cdd:PRK09088 393 NVYPAEIEAVLADHPGIRECAVVGMA----DAQWGevgylAIVPADGAPLDLERIRSHLSTRLAKY--KVPKHLRLVD-- 464
|
410
....*....|....*....
gi 489502054 499 SLPRTSSGKLRRLAVRRSL 517
Cdd:PRK09088 465 ALPRTASGKLQKARLRDAL 483
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
26-515 |
7.37e-13 |
|
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: 70.42 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 26 TSLWCRHPWPEVHGLAESVAAWLLDH--DRPAAVGLVGEPTVELVAAIQGAWLAGAAVsiLPgpvrgandqrwadatltr 103
Cdd:cd17653 17 ESLGGSLTYGELDAASNALANRLLQLgvVPGDVVPLLSDRSLEMLVAILAILKAGAAY--VP------------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 104 flgigvrtvLSQGSYLARLRSV-DTAGVTIGDLSTAAHTnrsatpvasegPAVLQGTAGSTGAPRTAILSPGAVLSNLRG 182
Cdd:cd17653 77 ---------LDAKLPSARIQAIlRTSGATLLLTTDSPDD-----------LAYIIFTSGSTGIPKGVMVPHRGVLNYVSQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 183 LNQRVGTDAATDVGcswlplyHDMGLAF------VLSAALAGAPLWLA-PTTAFTAspfrwlswLSDSGATMTAAPNFay 255
Cdd:cd17653 137 PPARLDVGPGSRVA-------QVLSIAFdacigeIFSTLCNGGTLVLAdPSDPFAH--------VARTVDALMSTPSI-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 256 nlIGKYARRvsevDLGALRVTLNGGEPVDCDGLTRFAEAMApfgfdagaVLPSYGLAESTCAVTVPvpgiGLLADRVIdg 335
Cdd:cd17653 200 --LSTLSPQ----DFPNLKTIFLGGEAVPPSLLDRWSPGRR--------LYNAYGPTECTISSTMT----ELLPGQPV-- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 336 sgahkhaVLGNPIPGMEVRI-SCGDQAAgnASREIGEIEIRGASMMAGYLGQQPID-----PDDW------FATGDLGYL 403
Cdd:cd17653 260 -------TIGKPIPNSTCYIlDADLQPV--PEGVVGEICISGVQVARGYLGNPALTaskfvPDPFwpgsrmYRTGDYGRW 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 404 GA-GGLVVCGRAKEVISIAGRNI-FPTEVELVAAQVRGVREGAVVALGtgdrstrpGLVVAaeFRGP---DEANARAELI 478
Cdd:cd17653 331 TEdGGLEFLGREDNQVKVRGFRInLEEIEEVVLQSQPEVTQAAAIVVN--------GRLVA--FVTPetvDVDGLRSELA 400
|
490 500 510
....*....|....*....|....*....|....*..
gi 489502054 479 QRVASECgiVPSdvVFVSPGSLPRTSSGKLRRLAVRR 515
Cdd:cd17653 401 KHLPSYA--VPD--RIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
36-510 |
1.05e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 70.41 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 36 EVHGLAESVAAWL-LDHDRPA-AVGLVGEPTVELVAAIQGAWLAGAAVSILPGPVRgandqrwADATLTRFLGIGVRTVL 113
Cdd:PRK13383 65 ELQRATESLARRLtRDGVAPGrAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFR-------SDALAAALRAHHISTVV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 114 SQGSYLARLRSVDTAgVTIGDLSTAAHTNRSATP-VASEGPAVLQgTAGSTGAPRTAILSP------GAVLSNLRGLNQR 186
Cdd:PRK13383 138 ADNEFAERIAGADDA-VAVIDPATAGAEESGGRPaVAAPGRIVLL-TSGTTGKPKGVPRAPqlrsavGVWVTILDRTRLR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 187 VGTDAATDvgcswLPLYHDMGLA-FVLSAALAGAPL----WLAPTTAFTASPFRwlswlsdsGATMTAAPNFAYNLIGKY 261
Cdd:PRK13383 216 TGSRISVA-----MPMFHGLGLGmLMLTIALGGTVLthrhFDAEAALAQASLHR--------ADAFTAVPVVLARILELP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 262 ARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAgavlpsYGLAEStcavtvpvpGIGLLAdrvIDGSGAHKH 341
Cdd:PRK13383 283 PRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNG------YGSTEV---------GIGALA---TPADLRDAP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 342 AVLGNPIPGMEVRI-SCGDQAAGnaSREIGEIEIRGASMMAGYL-GQQPIDPDDWFATGDLGYL-GAGGLVVCGRAKEVI 418
Cdd:PRK13383 345 ETVGKPVAGCPVRIlDRNNRPVG--PRVTGRIFVGGELAGTRYTdGGGKAVVDGMTSTGDMGYLdNAGRLFIVGREDDMI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 419 SIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTR-PGLVVAAEFRGPDEANARAELIQRVASecGIVPSDVVFVSp 497
Cdd:PRK13383 423 ISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRlAAFVVLHPGSGVDAAQLRDYLKDRVSR--FEQPRDINIVS- 499
|
490
....*....|...
gi 489502054 498 gSLPRTSSGKLRR 510
Cdd:PRK13383 500 -SIPRNPTGKVLR 511
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
112-514 |
1.50e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 70.06 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 112 VLSQGSYLARLRS---VDTAGVtigdLSTAAHTNRSA-TPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRV 187
Cdd:PRK06060 106 VVTSDALRDRFQPsrvAEAAEL----MSEAARVAPGGyEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 188 GTDAATDVGCSWLPLYHDMGLafvlsaalaGAPLWLAPTTAFTA--SPfrwLSWLSDSGATMTA--APNFAYNLIGKYAR 263
Cdd:PRK06060 182 LRLTPEDTGLCSARMYFAYGL---------GNSVWFPLATGGSAviNS---APVTPEAAAILSArfGPSVLYGVPNFFAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 264 RV---SEVDLGALRVTLNGGEPVDcdglTRFAEAMAPFgFDAGAVLPSYGLAEStcavtvpvpGIGLLADRVIDgsgaHK 340
Cdd:PRK06060 250 VIdscSPDSFRSLRCVVSAGEALE----LGLAERLMEF-FGGIPILDGIGSTEV---------GQTFVSNRVDE----WR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 341 HAVLGNPIPGMEVRISCGDQAAGNASREiGEIEIRGASMMAGYLG--QQPIDPDDWFATGDLGYLGAGGLVVCG-RAKEV 417
Cdd:PRK06060 312 LGTLGRVLPPYEIRVVAPDGTTAGPGVE-GDLWVRGPAIAKGYWNrpDSPVANEGWLDTRDRVCIDSDGWVTYRcRADDT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 418 ISIAGRNIFPTEVELVAAQVRGVREGAVVAL--GTGdRSTRPGLVVAAEFRGPDEANARaELIQRVASECGIVPSDVVFV 495
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAVreSTG-ASTLQAFLVATSGATIDGSVMR-DLHRGLLNRLSAFKVPHRFA 468
|
410
....*....|....*....
gi 489502054 496 SPGSLPRTSSGKLRRLAVR 514
Cdd:PRK06060 469 VVDRLPRTPNGKLVRGALR 487
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
159-517 |
1.59e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 69.74 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSP--------GAVLSNLRGLNQRvgtDAATDVgcswLPLYHDMGLAFVLSAALAGAPLWLaPTTAFT 230
Cdd:PRK07008 184 TSGTTGNPKGALYSHrstvlhayGAALPDAMGLSAR---DAVLPV----VPMFHVNAWGLPYSAPLTGAKLVL-PGPDLD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 231 ASPFRWLswLSDSGATMTAA-PNFAYNLIGkYARRVSeVDLGALRVTLNGGEPVDCDGLTRFAEAmapFGFDagaVLPSY 309
Cdd:PRK07008 256 GKSLYEL--IEAERVTFSAGvPTVWLGLLN-HMREAG-LRFSTLRRTVIGGSACPPAMIRTFEDE---YGVE---VIHAW 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 310 GLAESTcavtvPVPGIGLLADRVIDGSGAHKHAVL---GNPIPGMEVRISCGDQAA----GNASreiGEIEIRGASMMAG 382
Cdd:PRK07008 326 GMTEMS-----PLGTLCKLKWKHSQLPLDEQRKLLekqGRVIYGVDMKIVGDDGRElpwdGKAF---GDLQVRGPWVIDR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 383 YLGQQPiDP--DDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGL 459
Cdd:PRK07008 398 YFRGDA-SPlvDGWFPTGDVATIDADGfMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLL 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489502054 460 VVAaefRGPDEANARAELIQ----RVASecGIVPSDVVFVSpgSLPRTSSGKLRRLAVRRSL 517
Cdd:PRK07008 477 VVV---KRPGAEVTREELLAfyegKVAK--WWIPDDVVFVD--AIPHTATGKLQKLKLREQF 531
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
13-515 |
2.00e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.37 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 13 QASAGDLMVLDRET-----SLWCRHP--WPEVHGLAESVAAwlLDHDRPAAVGLVGEPTVELVAAI--QGAWLAGAAVSI 83
Cdd:PRK12316 1971 QAALGELALLDAGErqrilADWDRTPeaYPRGPGVHQRIAE--QAARAPEAIAVVFGDQHLSYAELdsRANRLAHRLRAR 2048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 84 LPGP-VRGANDQRWADATLTRFLGI--------------------------GVRTVLSQGSYLARLRSvdTAGVTIGDLS 136
Cdd:PRK12316 2049 GVGPeVRVAIAAERSFELVVALLAVlkaggayvpldpnypaerlaymledsGAALLLTQRHLLERLPL--PAGVARLPLD 2126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 137 TAAH-----TNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAAtDVGCSWLPLYHDMGLAFV 211
Cdd:PRK12316 2127 RDAEwadypDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPA-DCELQFMSFSFDGAHEQW 2205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 212 LSAALAGAPLWLAPTTAFTasPFRWLSWLSDSGATMTAAPNFAYNLIGKYARRvsEVDLGALRVTLNGGEPVDCDGLTRF 291
Cdd:PRK12316 2206 FHPLLNGARVLIRDDELWD--PEQLYDEMERHGVTILDFPPVYLQQLAEHAER--DGRPPAVRVYCFGGEAVPAASLRLA 2281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 292 AEAMAPfgfdaGAVLPSYGLAEstcAVTVPVpgigLLADRVIDGSGAhKHAVLGNPIPGmevRISCGDQAAGN--ASREI 369
Cdd:PRK12316 2282 WEALRP-----VYLFNGYGPTE---AVVTPL----LWKCRPQDPCGA-AYVPIGRALGN---RRAYILDADLNllAPGMA 2345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 370 GEIEIRGASMMAGYLGQQPI-------DPDD-----WFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQ 436
Cdd:PRK12316 2346 GELYLGGEGLARGYLNRPGLtaerfvpDPFSasgerLYRTGDLARYRADGVVeYLGRIDHQVKIRGFRIELGEIEARLQA 2425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502054 437 VRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVRR 515
Cdd:PRK12316 2426 HPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAY--MVPAHWVVLE--RLPLNPNGKLDRKALPK 2500
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
150-425 |
2.11e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 69.46 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 150 SEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLnQRVGTDAATDVGCSWLPLYHDMGL-AFVLSAALAGAPLwlapttA 228
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRAC-LKFFSPKEDDVMMSFLPPFHAYGFnSCTLFPLLSGVPV------V 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 229 FTASPF---RWLSWLSDSGATMTAAPNFAYNLIGKYARRvSEVDLGALRVTLNGGEPVDcDGLTRFAEAMAPfgfdagAV 305
Cdd:PRK06334 255 FAYNPLypkKIVEMIDEAKVTFLGSTPVFFDYILKTAKK-QESCLPSLRFVVIGGDAFK-DSLYQEALKTFP------HI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 306 LPSYGLAESTCAvtvPVPGIGlladrviDGSGAHKHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAGYLG 385
Cdd:PRK06334 327 QLRQGYGTTECS---PVITIN-------TVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLG 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489502054 386 QQP------IDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNI 425
Cdd:PRK06334 397 EDFgqgfveLGGETWYVTGDLGYVDRHGeLFLKGRLSRFVKIGAEMV 443
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
269-518 |
2.42e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 69.14 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 269 DLGALRVTLNGGEPVDCDGLTRFAEAmapfgFDAGAVLPSYGLAESTCAVTVpvpgigLLADRVIDGSGAhkhavLGNPI 348
Cdd:PRK06145 262 DLDSLAWCIGGGEKTPESRIRDFTRV-----FTRARYIDAYGLTETCSGDTL------MEAGREIEKIGS-----TGRAL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 349 PGMEVRISCGDQAAGNASREiGEIEIRGASMMAGYLGqqpiDP--------DDWFATGDLGYLGAGG-LVVCGRAKEVIS 419
Cdd:PRK06145 326 AHVEIRIADGAGRWLPPNMK-GEICMRGPKVTKGYWK----DPektaeafyGDWFRSGDVGYLDEEGfLYLTDRKKDMII 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 420 IAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRP-GLVVAAEFRGPDEANARAELIQRVASecGIVPSDVVFVSpg 498
Cdd:PRK06145 401 SGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERItAVVVLNPGATLTLEALDRHCRQRLAS--FKVPRQLKVRD-- 476
|
250 260
....*....|....*....|
gi 489502054 499 SLPRTSSGKLRRLAVRRSLE 518
Cdd:PRK06145 477 ELPRNPSGKVLKRVLRDELN 496
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
145-514 |
2.67e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 69.08 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 145 ATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNL---RGLNQRVGTDA------ATDVGCSWLPLYHDMGL-AFVLSA 214
Cdd:PRK12492 201 PVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMlqvRACLSQLGPDGqplmkeGQEVMIAPLPLYHIYAFtANCMCM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 215 ALAGAP--LWLAP--TTAFTASPFRW----LSWLSDSGATMTAAPNFaynligkyarrvSEVDLGALRVTLNGGepvdcd 286
Cdd:PRK12492 281 MVSGNHnvLITNPrdIPGFIKELGKWrfsaLLGLNTLFVALMDHPGF------------KDLDFSALKLTNSGG------ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 287 glTRFAEAMAPF--GFDAGAVLPSYGLAE-STCAVTVPVpgiGLLAdrvidgsgahKHAVLGNPIPGMEVRIsCGDQAAG 363
Cdd:PRK12492 343 --TALVKATAERweQLTGCTIVEGYGLTEtSPVASTNPY---GELA----------RLGTVGIPVPGTALKV-IDDDGNE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 364 NASREIGEIEIRGASMMAGYLgQQP------IDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQ 436
Cdd:PRK12492 407 LPLGERGELCIKGPQVMKGYW-QQPeataeaLDAEGWFKTGDIAVIDPDGFVrIVDRKKDLIIVSGFNVYPNEIEDVVMA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 437 VRGVREGAVVALgtgdrstrpglvvaaefrgPDEANARAELIQRVASECGI-----------------VPSDVVFVSpgS 499
Cdd:PRK12492 486 HPKVANCAAIGV-------------------PDERSGEAVKLFVVARDPGLsveelkayckenftgykVPKHIVLRD--S 544
|
410
....*....|....*
gi 489502054 500 LPRTSSGKLRRLAVR 514
Cdd:PRK12492 545 LPMTPVGKILRRELR 559
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
342-511 |
2.78e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 69.19 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 342 AVLGNPIPGMEVRIScgDQAAGNASR-EIGEIEIRGASMMAGYLG---QQPIDpdDWFATGDLGYLGAGGLV-VCGRAKE 416
Cdd:PRK07788 376 GTVGRPPKGVTVKIL--DENGNEVPRgVVGRIFVGNGFPFEGYTDgrdKQIID--GLLSSGDVGYFDEDGLLfVDGRDDD 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 417 VISIAGRNIFPTEVELVAAQVRGVREGAVValGTGDRSTRPGL---VVAAEFRGPDEANARAELIQRVASECgiVPSDVV 493
Cdd:PRK07788 452 MIVSGGENVFPAEVEDLLAGHPDVVEAAVI--GVDDEEFGQRLrafVVKAPGAALDEDAIKDYVRDNLARYK--VPRDVV 527
|
170
....*....|....*....
gi 489502054 494 FVSpgSLPRTSSGK-LRRL 511
Cdd:PRK07788 528 FLD--ELPRNPTGKvLKRE 544
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
149-514 |
4.17e-12 |
|
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: 68.27 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 149 ASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSWLPLYHDMGLAFVLSAAL-AGAPLWLAPTt 227
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFgVGASGVLLEE- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 228 aftASPFRWLSWLSDSGAT-MTAAPNFAYNLIGKyaRRVSEVDLGALRVTLNGGEpvdcdgltrfaeamapfgfdagaVL 306
Cdd:cd05958 174 ---ATPDLLLSAIARYKPTvLFTAPTAYRAMLAH--PDAAGPDLSSLRKCVSAGE-----------------------AL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 307 PSYGLAESTCAVTVP-VPGIGLLADRVIDGSGAHKHA---VLGNPIPGMEVRIScgdQAAGNA--SREIGEIEIRGASmm 380
Cdd:cd05958 226 PAALHRAWKEATGIPiIDGIGSTEMFHIFISARPGDArpgATGKPVPGYEAKVV---DDEGNPvpDGTIGRLAVRGPT-- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 381 aGYLG-----QQPIDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRS 454
Cdd:cd05958 301 -GCRYladkrQRTYVQGGWNITGDTYSRDPDGYFrHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRG 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489502054 455 TRP-GLVVAAEFRGPDEANARA--ELIQRVASECGiVPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd05958 380 VVVkAFVVLRPGVIPGPVLARElqDHAKAHIAPYK-YPRAIEFVT--ELPRTATGKLQRFALR 439
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
147-520 |
7.44e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 67.37 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 147 PVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATD--VGCswlPLYHDMGL-AFVLSAALAGA-PLW 222
Cdd:PRK08308 97 NYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETpiVAC---PVTHSYGLiCGVLAALTRGSkPVI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 223 LApttaftaspfrwlswlsdsgatmTAAPNFAYNLIGKYARRV---SEVDLGALRVTLNGGEpvdcdgltRFAEAMApfg 299
Cdd:PRK08308 174 IT-----------------------NKNPKFALNILRNTPQHIlyaVPLMLHILGRLLPGTF--------QFHAVMT--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 300 fdAGAVLPS----------------YGLAESTC-AVTVPVpgiglladrvidgsgaHKHAVLGNPIPgmEVRIScgdqaA 362
Cdd:PRK08308 220 --SGTPLPEawfyklrerttymmqqYGCSEAGCvSICPDM----------------KSHLDLGNPLP--HVSVS-----A 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 363 GNASREIGEIEIRgasmmagyLGQQPIdpddwfATGDLGYL-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVR 441
Cdd:PRK08308 275 GSDENAPEEIVVK--------MGDKEI------FTKDLGYKsERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 442 EgAVVALGTGDRStrpGLVVAAEF---RGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRrlavRRSLE 518
Cdd:PRK08308 341 E-AVVYRGKDPVA---GERVKAKVishEEIDPVQLREWCIQHLAPY--QVPHEIESVT--EIPKNANGKVS----RKLLE 408
|
..
gi 489502054 519 MA 520
Cdd:PRK08308 409 LG 410
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
108-517 |
7.61e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 67.50 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 108 GVRTVLSQG-SYLARLRSVDTAGVTIGDLStAAHTNRSAT---PVASE-GPAVLQGTAGSTGAPRTAILSPGAVLsnLRG 182
Cdd:PRK05620 134 CVRAVVFIGpSDADSAAAHMPEGIKVYSYE-ALLDGRSTVydwPELDEtTAAAICYSTGTTGAPKGVVYSHRSLY--LQS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 183 LNQRVGTDAATDVGCSWL---PLYHDMGLAFVLSAALAGAPLWLaptTAFTASPFRWLSWLSDSGA-TMTAAPNFAYNLI 258
Cdd:PRK05620 211 LSLRTTDSLAVTHGESFLccvPIYHVLSWGVPLAAFMSGTPLVF---PGPDLSAPTLAKIIATAMPrVAHGVPTLWIQLM 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 259 GKYARRVSEvdLGALRVTLNGGEPVDCDGLTRFAEAmapFGFDagaVLPSYGLAESTCAVTVPVPGIGLladrviDGSGA 338
Cdd:PRK05620 288 VHYLKNPPE--RMSLQEIYVGGSAVPPILIKAWEER---YGVD---VVHVWGMTETSPVGTVARPPSGV------SGEAR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 339 HKHAVLGNPIP-GMEVRISCGDQAAGNASREIGEIEIRGASMMAGYL---------------------GQQPIDPDDWFA 396
Cdd:PRK05620 354 WAYRVSQGRFPaSLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYhspteegggaastfrgedvedANDRFTADGWLR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 397 TGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVE--LVAAQVrgVREGAVVALGTGDRSTRP-GLVVAAEFRGPDEAN 472
Cdd:PRK05620 434 TGDVGSVTRDGfLTIHDRARDVIRSGGEWIYSAQLEnyIMAAPE--VVECAVIGYPDDKWGERPlAVTVLAPGIEPTRET 511
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489502054 473 A---RAELIQRVASecGIVPSDVVFVSpgSLPRTSSGKLRRLAVRRSL 517
Cdd:PRK05620 512 AerlRDQLRDRLPN--WMLPEYWTFVD--EIDKTSVGKFDKKDLRQHL 555
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
260-517 |
7.78e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 67.56 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 260 KYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGavlpsYGLAESTCAVTvpvpgiglladRVIDGSGAH 339
Cdd:PLN02574 308 KKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQG-----YGMTESTAVGT-----------RGFNTEKLS 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 340 KHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAGYLG-----QQPIDPDDWFATGDLGYLGAGG-LVVCGR 413
Cdd:PLN02574 372 KYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNnpkatQSTIDKDGWLRTGDIAYFDEDGyLYIVDR 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 414 AKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPglvVAAEFRGPDEANARAELIQRVASEcgIVP---- 489
Cdd:PLN02574 452 LKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIP---VAFVVRRQGSTLSQEAVINYVAKQ--VAPykkv 526
|
250 260
....*....|....*....|....*...
gi 489502054 490 SDVVFVSpgSLPRTSSGKLRRLAVRRSL 517
Cdd:PLN02574 527 RKVVFVQ--SIPKSPAGKILRRELKRSL 552
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
34-516 |
8.32e-12 |
|
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: 67.37 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 34 WPEVHGLAESVAAWLLDH------DRpaaVGLVGEPTVELVAAIQGAWLAGaavsILPGPVR---------------GAN 92
Cdd:cd05905 17 WGKLLSRAEKIAAVLQKKvglkpgDR---VALMYPDPLDFVAAFYGCLYAG----VVPIPIEppdisqqlgfllgtcKVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 93 DQRWADATLTRFLgIGVRTVLSQGSYLARL---RSVDTAGVTIgdlSTAAHTNRSAT--PVASEGPAVLQGTAGSTGAPR 167
Cdd:cd05905 90 VALTVEACLKGLP-KKLLKSKTAAEIAKKKgwpKILDFVKIPK---SKRSKLKKWGPhpPTRDGDTAYIEYSFSSDGSLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 168 TAILSPGAVLSNLRGLNQRVGTDAA-TDVGCswLPLYHDMGLAF-VLSAALAGAPLWLAPTTAFTASPFRWLSWLSDSGA 245
Cdd:cd05905 166 GVAVSHSSLLAHCRALKEACELYESrPLVTV--LDFKSGLGLWHgCLLSVYSGHHTILIPPELMKTNPLLWLQTLSQYKV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 246 TMTAAP----NFAYNLIGKY--ARRVSEVDLGALRVTLnggepVDCDG------LTRFAEAMAPFGFDAGAVLPSYGlae 313
Cdd:cd05905 244 RDAYVKlrtlHWCLKDLSSTlaSLKNRDVNLSSLRMCM-----VPCENrprissCDSFLKLFQTLGLSPRAVSTEFG--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 314 stcavTVPVPGIGLLAD--------------------RVIDGSGAHKHAVLGNP--IPGMEVRIS-------CGDQaagn 364
Cdd:cd05905 316 -----TRVNPFICWQGTsgpepsrvyldmralrhgvvRLDERDKPNSLPLQDSGkvLPGAQVAIVnpetkglCKDG---- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 365 asrEIGEIEIRGASMMAGYLG-----------------QQPIDPDDWFATGDLGYLGAG----------GLV-VCGRAKE 416
Cdd:cd05905 387 ---EIGEIWVNSPANASGYFLldgetndtfkvfpstrlSTGITNNSYARTGLLGFLRPTkctdlnveehDLLfVVGSIDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 417 VISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDrstrpgLVVAAEFRGPDEANArAELIQRVASEC----GIVPSDV 492
Cdd:cd05905 464 TLEVRGLRHHPSDIEATVMRVHPYRGRCAVFSITGL------VVVVAEQPPGSEEEA-LDLVPLVLNAIleehQVIVDCV 536
|
570 580
....*....|....*....|....
gi 489502054 493 VFVSPGSLPRTSSGKLRRLAVRRS 516
Cdd:cd05905 537 ALVPPGSLPKNPLGEKQRMEIRQA 560
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-513 |
1.66e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.29 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 108 GVRTVLSQGSYLARLRSVDTAGVTIGDlSTAAHTNRSAT----PVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGL 183
Cdd:PRK12316 4648 GAALLLTQSHLLQRLPIPDGLASLALD-RDEDWEGFPAHdpavRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT 4726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 184 NQRVGTDAATDVgcswlplYHDMGLAFVLSAA------LAGAPLWLAPTTAFtaSPFRWLSWLSDSGATMTAAPNFAYNL 257
Cdd:PRK12316 4727 GERYELTPDDRV-------LQFMSFSFDGSHEglyhplINGASVVIRDDSLW--DPERLYAEIHEHRVTVLVFPPVYLQQ 4797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 258 IGKYARRVSEVdlGALRVTLNGGEPVDCDGLTRFAEAMAPFGfdagaVLPSYGLAESTCAVTvpvpgigLLADRVIDGSG 337
Cdd:PRK12316 4798 LAEHAERDGEP--PSLRVYCFGGEAVAQASYDLAWRALKPVY-----LFNGYGPTETTVTVL-------LWKARDGDACG 4863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 338 AhKHAVLGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLGQQPI-------DPDD-----WFATGDLGYLGA 405
Cdd:PRK12316 4864 A-AYMPIGTPLGNRSGYV-LDGQLNPLPVGVAGELYLGGEGVARGYLERPALtaerfvpDPFGapggrLYRTGDLARYRA 4941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 406 GGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEANARAELIQRVASE 484
Cdd:PRK12316 4942 DGVIdYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAA 5021
|
410 420 430
....*....|....*....|....*....|....*
gi 489502054 485 CG------IVPSDVVFVSpgSLPRTSSGKLRRLAV 513
Cdd:PRK12316 5022 LRerlpeyMVPAHLVFLA--RMPLTPNGKLDRKAL 5054
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
106-508 |
1.78e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 66.49 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 106 GIGVRTVLSQGSYLARLRSVDtagvtigDLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSnlrglnQ 185
Cdd:PRK08316 133 TLILSLVLGGREAPGGWLDFA-------DWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIA------E 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 186 RVGTDAATDVGCS-----WLPLYHDMGL-AFVLSAALAGAPLWLAPT---------------TAFTASPFRWLSWLSdsg 244
Cdd:PRK08316 200 YVSCIVAGDMSADdiplhALPLYHCAQLdVFLGPYLYVGATNVILDApdpelilrtieaeriTSFFAPPTVWISLLR--- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 245 atmtaAPNFAynligkyarrvsEVDLGALRVTLNGGEPVDCDGLTRFAE---AMAPFGFdagavlpsYGLAEstcavtvp 321
Cdd:PRK08316 277 -----HPDFD------------TRDLSSLRKGYYGASIMPVEVLKELRErlpGLRFYNC--------YGQTE-------- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 322 vpgIGLLADRVIDGSGAHKHAVLGNPIPGMEVRI---SCGDQAAGnasrEIGEIEIRGASMMAGYLGqqpiDP------- 391
Cdd:PRK08316 324 ---IAPLATVLGPEEHLRRPGSAGRPVLNVETRVvddDGNDVAPG----EVGEIVHRSPQLMLGYWD----DPektaeaf 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 392 -DDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALgtgdrstrPG-----LVVAAE 464
Cdd:PRK08316 393 rGGWFHSGDLGVMDEEGyITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL--------PDpkwieAVTAVV 464
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489502054 465 FRGPDEANARAELI----QRVASEcgIVPSDVVFVSpgSLPRTSSGKL 508
Cdd:PRK08316 465 VPKAGATVTEDELIahcrARLAGF--KVPKRVIFVD--ELPRNPSGKI 508
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
34-521 |
1.82e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 66.24 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 34 WPEVHGLAESVAAWL---LDHDRPAAVGLVGEPTVELVAAIQGAWLAGAAVSILPGPVRGANDQRWADATLTRFlgigvr 110
Cdd:PRK07867 31 WREHIRGSAARAAALrarLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQL------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 111 tVLSQGSYLARLRSVDTaGVTIGDLSTAAHTNRSATP---------VASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLR 181
Cdd:PRK07867 105 -VLTESAHAELLDGLDP-GVRVINVDSPAWADELAAHrdaeppfrvADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 182 GLNQRVGTDAATDVGCSwLPLYHDMGLAFVLSAALA-GAPLWLAPTtaFTASPFrwlswLSDS---GATMtaapnfaYNL 257
Cdd:PRK07867 183 MLAQRFGLGPDDVCYVS-MPLFHSNAVMAGWAVALAaGASIALRRK--FSASGF-----LPDVrryGATY-------ANY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 258 IGK---YARRVSEVDLGA---LRVTL-NGGEPVDcdgLTRFAEAmapFGFdagAVLPSYGLAESTCAVT----VPVPGIG 326
Cdd:PRK07867 248 VGKplsYVLATPERPDDAdnpLRIVYgNEGAPGD---IARFARR---FGC---VVVDGFGSTEGGVAITrtpdTPPGALG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 327 LLADRVidgsgAHKHAVLGNPIPGMEVriscGDQAAGNASREIGE-IEIRGASMMAGYLGQQPIDP----DDWFATGDLG 401
Cdd:PRK07867 319 PLPPGV-----AIVDPDTGTECPPAED----ADGRLLNADEAIGElVNTAGPGGFEGYYNDPEADAermrGGVYWSGDLA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 402 YLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVAL---GTGDRstrpglVVAAEFRGPD---EANAR 474
Cdd:PRK07867 390 YRDADGYAyFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVpdpVVGDQ------VMAALVLAPGakfDPDAF 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 489502054 475 AELIqRVASECG--IVPSDVVFVSpgSLPRTSSGK-LRRLAVRRSLEMAD 521
Cdd:PRK07867 464 AEFL-AAQPDLGpkQWPSYVRVCA--ELPRTATFKvLKRQLSAEGVDCAD 510
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
148-518 |
1.97e-11 |
|
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: 66.32 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 148 VASEGPAVLQGTAGSTGA----PRTAilspGAVLSNLRGLNQRVGTDAATDVGCSwLPLYHDMGLAF--VLSAALAGAPL 221
Cdd:COG1021 181 PDPDDVAFFQLSGGTTGLpkliPRTH----DDYLYSVRASAEICGLDADTVYLAA-LPAAHNFPLSSpgVLGVLYAGGTV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 222 WLAPTTaftaSPFRWLSWLSDSGATMTAAPNFAYNLIGKYARRvSEVDLGALRVTLNGGepvdcdglTRFAEAmapfgfD 301
Cdd:COG1021 256 VLAPDP----SPDTAFPLIERERVTVTALVPPLALLWLDAAER-SRYDLSSLRVLQVGG--------AKLSPE------L 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 302 AGAVLP--------SYGLAESTCAVTvpvpgiglladRvIDGSGAHKHAVLGNPI-PGMEVRIScgDqAAGN--ASREIG 370
Cdd:COG1021 317 ARRVRPalgctlqqVFGMAEGLVNYT-----------R-LDDPEEVILTTQGRPIsPDDEVRIV--D-EDGNpvPPGEVG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 371 EIEIRGASMMAGYLG-----QQPIDPDDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGA 444
Cdd:COG1021 382 ELLTRGPYTIRGYYRapehnARAFTPDGFYRTGDLVRRTPDGyLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 445 VVA-----LGtgdrsTRPGLVVAaefrgPDEANARAELIQRVASECGI----VPSDVVFVSpgSLPRTSSGKLRRLAVRR 515
Cdd:COG1021 462 VVAmpdeyLG-----ERSCAFVV-----PRGEPLTLAELRRFLRERGLaafkLPDRLEFVD--ALPLTAVGKIDKKALRA 529
|
...
gi 489502054 516 SLE 518
Cdd:COG1021 530 ALA 532
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
147-511 |
2.80e-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: 65.61 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 147 PVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTD-AATDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAP 225
Cdd:cd05923 146 PREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVV 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 226 TtAFtaSPFRWLSWLSDSGAT-MTAAPNFAYNLIGKYA---RRVSEVDlgalRVTLNGGEPVDcdGLTRFAEAMAPfgfd 301
Cdd:cd05923 226 E-EF--DPADALKLIEQERVTsLFATPTHLDALAAAAEfagLKLSSLR----HVTFAGATMPD--AVLERVNQHLP---- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 302 aGAVLPSYGLAESTCAVTV--PVPGIGLLAdrvidgsGAHKHAVLgnpipgmeVRISCGDQAAGNASREiGEIEIRGASM 379
Cdd:cd05923 293 -GEKVNIYGTTEAMNSLYMrdARTGTEMRP-------GFFSEVRI--------VRIGGSPDEALANGEE-GELIVAAAAD 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 380 MA--GYLGQQPIDP----DDWFATGDLGYL-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALgtgd 452
Cdd:cd05923 356 AAftGYLNQPEATAkklqDGWYRTGDVGYVdPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV---- 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489502054 453 RSTRPGLVVAAeFRGPDEANARAELIQRVASECGIV----PSDVVFVSpgSLPRTSSGK-LRRL 511
Cdd:cd05923 432 ADERWGQSVTA-CVVPREGTLSADELDQFCRASELAdfkrPRRYFFLD--ELPKNAMNKvLRRQ 492
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
154-431 |
3.55e-11 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 65.46 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 154 AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATD---VGCSWLPLYH------DMGLA--------FVLSAAL 216
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqeSVVSYLPLSHiaaqilDIWLPikvggqvyFAQPDAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 217 AGAplwLAPT------TAFTASPFRWlSWLSDSGATMTAAPNFAYNLIGKYARRVS-EVDLgalrvTLNGGE--PVDCDG 287
Cdd:cd05933 233 KGT---LVKTlrevrpTAFMGVPRVW-EKIQEKMKAVGAKSGTLKRKIASWAKGVGlETNL-----KLMGGEspSPLFYR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 288 LTR---FAEAMAPFGFD-------AGAVLPS----------------YGLAESTCAVTVPVPGiglladrvidgsgAHKH 341
Cdd:cd05933 304 LAKklvFKKVRKALGLDrcqkfftGAAPISRetlefflslnipimelYGMSETSGPHTISNPQ-------------AYRL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 342 AVLGNPIPGMEVRISCGDqAAGnasreIGEIEIRGASMMAGYLG-----QQPIDPDDWFATGDLGYLGAGG-LVVCGRAK 415
Cdd:cd05933 371 LSCGKALPGCKTKIHNPD-ADG-----IGEICFWGRHVFMGYLNmedktEEAIDEDGWLHSGDLGKLDEDGfLYITGRIK 444
|
330
....*....|....*..
gi 489502054 416 EVISIA-GRNIFPTEVE 431
Cdd:cd05933 445 ELIITAgGENVPPVPIE 461
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
118-512 |
4.65e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 65.50 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 118 YLARLRsvDTagVTIGD-LSTAAH---TNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLnQRVGTDAAT 193
Cdd:PRK08043 332 YLEDLK--DD--VTTADkLWIFAHllmPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQI-KTIADFTPN 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 194 DVGCSWLPLYHDMGLAF-VLSAALAGAPLWLAPttaftaSPFRWlswlsdsgatmTAAPNFAYN-----------LIGKY 261
Cdd:PRK08043 407 DRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYP------SPLHY-----------RIVPELVYDrnctvlfgtstFLGNY 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 262 ARRVSEVDLGALRVTLNGGEpvdcdgltRFAEAMAPFGFDAGA--VLPSYGLAESTCAVTVPVPGiglladrvidgsgAH 339
Cdd:PRK08043 470 ARFANPYDFARLRYVVAGAE--------KLQESTKQLWQDKFGlrILEGYGVTECAPVVSINVPM-------------AA 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 340 KHAVLGNPIPGMEVR-ISCGDQAAGnasreiGEIEIRGASMMAGYL--------------GQQPIDPDDWFATGDLGYLG 404
Cdd:PRK08043 529 KPGTVGRILPGMDARlLSVPGIEQG------GRLQLKGPNIMNGYLrvekpgvlevptaeNARGEMERGWYDTGDIVRFD 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 405 AGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVAlgTGDRSTRPGLVVAAEfrgpDEANARaELIQRVAS 483
Cdd:PRK08043 603 EQGFVqIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAI--KSDASKGEALVLFTT----DSELTR-EKLQQYAR 675
|
410 420 430
....*....|....*....|....*....|....*...
gi 489502054 484 ECGI----VPSDVVFVSpgSLPRTSSGK-----LRRLA 512
Cdd:PRK08043 676 EHGVpelaVPRDIRYLK--QLPLLGSGKpdfvtLKSMV 711
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
345-515 |
8.15e-11 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 64.39 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 345 GNPIPGMEVRISCGD---QAAGnasrEIGEIEIRGASMMAGYLGQQPIDPDDWF-ATGDLGYL-GAGGLVVCGRAKEVIS 419
Cdd:PRK13382 368 GRPAEGTEIRILDQDfreVPTG----EVGTIFVRNDTQFDGYTSGSTKDFHDGFmASGDVGYLdENGRLFVVGRDDEMIV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 420 IAGRNIFPTEVELVAAQVRGVREGAVvaLGTGDRSTRPGL---VVAAefrgPDEANARAELIQRVASECG--IVPSDVVF 494
Cdd:PRK13382 444 SGGENVYPIEVEKTLATHPDVAEAAV--IGVDDEQYGQRLaafVVLK----PGASATPETLKQHVRDNLAnyKVPRDIVV 517
|
170 180
....*....|....*....|.
gi 489502054 495 VspGSLPRTSSGKLRRLAVRR 515
Cdd:PRK13382 518 L--DELPRGATGKILRRELQA 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
57-513 |
8.98e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.98 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 57 VGLVGEPTVELVAAIQGAWLAGAA-VSILPGPVRGANDQRWADAtltrflgiGVRTVLSQgSYLARLRSVDtAGVTIGDL 135
Cdd:PRK12316 564 VGVAMERSIEMVVALLAILKAGGAyVPLDPEYPAERLAYMLEDS--------GVQLLLSQ-SHLGRKLPLA-AGVQVLDL 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 136 STAA------HTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSwLPLYHDMGLA 209
Cdd:PRK12316 634 DRPAawlegySEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQK-TPFSFDVSVW 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 210 FVLSAALAGAPLWLAPTTAFTaSPFRWLSWLSDSGATMTaapNFAYNLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLT 289
Cdd:PRK12316 713 EFFWPLMSGARLVVAAPGDHR-DPAKLVELINREGVDTL---HFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQE 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 290 RFaEAMAPfgfdAGAVLPSYGLAESTCAVT-----------VPV--PgIGLLADRVIDGSgahkhavlGNPIPgmeVRIS 356
Cdd:PRK12316 789 QV-FAKLP----QAGLYNLYGPTEAAIDVThwtcveeggdsVPIgrP-IANLACYILDAN--------LEPVP---VGVL 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 357 cgdqaagnasreiGEIEIRGASMMAGYLGQQPI-----------DPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRN 424
Cdd:PRK12316 852 -------------GELYLAGRGLARGYHGRPGLtaerfvpspfvAGERMYRTGDLARYRADGVIeYAGRIDHQVKLRGLR 918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 425 IFPTEVELVAAQVRGVREGAVVALgtgDRSTRPGLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTS 504
Cdd:PRK12316 919 IELGEIEARLLEHPWVREAAVLAV---DGKQLVGYVVLESEGGDWREALKAHLAASLPEY--MVPAQWLALE--RLPLTP 991
|
....*....
gi 489502054 505 SGKLRRLAV 513
Cdd:PRK12316 992 NGKLDRKAL 1000
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
159-431 |
1.02e-10 |
|
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: 64.16 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLN---QRVGTDAATDVGCSWLPLYHDMGLAFVLSAALAGAPL--W----------- 222
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFkilEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIgfYsgdirlllddi 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 223 --LAPTtAFTASPfRWLSWLSDS-GATMTAAP-------NFAYNL-IGKYARRVSEVD---------------LGALRVT 276
Cdd:cd05927 202 kaLKPT-VFPGVP-RVLNRIYDKiFNKVQAKGplkrklfNFALNYkLAELRSGVVRASpfwdklvfnkikqalGGNVRLM 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 277 LNGGEPVDCDGLTRFAEAMApfgfdaGAVLPSYGLAESTCAVTVPVPGiglladrviDGSGAHkhavLGNPIPGMEVRI- 355
Cdd:cd05927 280 LTGSAPLSPEVLEFLRVALG------CPVLEGYGQTECTAGATLTLPG---------DTSVGH----VGGPLPCAEVKLv 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 356 ---SCGDQAAGNASReiGEIEIRGASMMAGYLgQQP------IDPDDWFATGDLG-YLGAGGLVVCGRAKEVISIA-GRN 424
Cdd:cd05927 341 dvpEMNYDAKDPNPR--GEVCIRGPNVFSGYY-KDPektaeaLDEDGWLHTGDIGeWLPNGTLKIIDRKKNIFKLSqGEY 417
|
....*..
gi 489502054 425 IFPTEVE 431
Cdd:cd05927 418 VAPEKIE 424
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
134-510 |
1.42e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 63.52 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 134 DLSTAAHTNRSATP---VASEGPAVLQGTAGSTGAPRTAILSpgavlsnlrglnQR--VGTDAAT----------DVGCS 198
Cdd:PRK06178 189 DLLPALRACTAPVPlppPALDALAALNYTGGTTGMPKGCEHT------------QRdmVYTAAAAyavavvggedSVFLS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 199 WLPLY----HDMGLAFVLsaaLAGAPLWLAPttaftaspfRWlswlsDSGATMTAAPNFAYN----LIGKYAR-----RV 265
Cdd:PRK06178 257 FLPEFwiagENFGLLFPL---FSGATLVLLA---------RW-----DAVAFMAAVERYRVTrtvmLVDNAVElmdhpRF 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 266 SEVDLGALRVT--------LNGgepvdcDGLTRFAEAmapfgfdAGAVL--PSYGLAESTCAVTVPVpgiGLLADrviDG 335
Cdd:PRK06178 320 AEYDLSSLRQVrvvsfvkkLNP------DYRQRWRAL-------TGSVLaeAAWGMTETHTCDTFTA---GFQDD---DF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 336 SGAHKHAVLGNPIPGMEVRISCGDQAAGNASREIGEIEIRGASMMAGYLGQQPIDP----DDWFATGDLG-YLGAGGLVV 410
Cdd:PRK06178 381 DLLSQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAealrDGWLHTGDIGkIDEQGFLHY 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 411 CGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRP-GLVVAAEFRGPDEANARAELIQRVASEcgIVP 489
Cdd:PRK06178 461 LGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPvAFVQLKPGADLTAAALQAWCRENMAVY--KVP 538
|
410 420
....*....|....*....|.
gi 489502054 490 sDVVFVSpgSLPRTSSGKLRR 510
Cdd:PRK06178 539 -EIRIVD--ALPMTATGKVRK 556
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
150-514 |
1.93e-10 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 63.28 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 150 SEGPAVLQGTAGSTGAPRTAILSPG-----AVLSNLRGLNQRVGTDAA--TDVGcsWLplyhdMGLAFVLSAALAGAPLW 222
Cdd:cd05968 235 SEDPLMIIYTSGTTGKPKGTVHVHAgfplkAAQDMYFQFDLKPGDLLTwfTDLG--WM-----MGPWLIFGGLILGATMV 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 223 LAPTTAFTASPFRWLSWLSDSGAT-MTAAPNFAYNLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMapfGFD 301
Cdd:cd05968 308 LYDGAPDHPKADRLWRMVEDHEIThLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETV---GKG 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 302 AGAVLPSYGLAEstcavtvpVPGiGLLADRVIDgsgAHKHAVLGNPIPGMEVRIScgDQAAGNASREIGEIEIRGA--SM 379
Cdd:cd05968 385 RNPIINYSGGTE--------ISG-GILGNVLIK---PIKPSSFNGPVPGMKADVL--DESGKPARPEVGELVLLAPwpGM 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 380 MAGYLGqqpiDPDDWFAT-----------GDLGYLGAGGL-VVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVA 447
Cdd:cd05968 451 TRGFWR----DEDRYLETywsrfdnvwvhGDFAYYDEEGYfYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 448 LGTGDRSTRPGL-VVAAEFRGPDEANARaELIQRVASECG--IVPSDVVFVspGSLPRTSSGKLRRLAVR 514
Cdd:cd05968 527 VPHPVKGEAIVCfVVLKPGVTPTEALAE-ELMERVADELGkpLSPERILFV--KDLPKTRNAKVMRRVIR 593
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
369-515 |
5.53e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 61.89 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 369 IGEIEIRGASMMAGYLGqqpiDP--------DDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRG 439
Cdd:PRK08162 388 IGEIMFRGNIVMKGYLK----NPkateeafaGGWFHTGDLAVLHPDGYIkIKDRSKDIIISGGENISSIEVEDVLYRHPA 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 440 VREGAVVAlgtgdrstRP----GLVVAA--EFRgpDEANAR-AELIQRVASECG--IVPSDVVFvspGSLPRTSSGKLRR 510
Cdd:PRK08162 464 VLVAAVVA--------KPdpkwGEVPCAfvELK--DGASATeEEIIAHCREHLAgfKVPKAVVF---GELPKTSTGKIQK 530
|
....*
gi 489502054 511 LAVRR 515
Cdd:PRK08162 531 FVLRE 535
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
309-512 |
5.98e-10 |
|
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: 61.18 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 309 YGLAESTCAVTV-PVPgiglladrvidgSGAHKHAVLGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLGQ- 386
Cdd:cd12115 246 YGPSEDTTYSTVaPVP------------PGASGEVSIGRPLANTQAYV-LDRALQPVPLGVPGELYIGGAGVARGYLGRp 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 387 ---------QPIDPDDW-FATGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRST 455
Cdd:cd12115 313 gltaerflpDPFGPGARlYRTGDLVrWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGER 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489502054 456 R-PGLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLA 512
Cdd:cd12115 393 RlVAYIVAEPGAAGLVEDLRRHLGTRLPAY--MVPSRFVRLD--ALPLTPNGKIDRSA 446
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
153-514 |
7.48e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 61.19 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 153 PAVLQGTAGSTGAPRTAILS-PGAVLSNLRGLnqrVGTDAATDVGCSW-LPLYHDMGLAFVLS-AALAGAPLWLAPTTAf 229
Cdd:PLN03102 188 PISLNYTSGTTADPKGVVIShRGAYLSTLSAI---IGWEMGTCPVYLWtLPMFHCNGWTFTWGtAARGGTSVCMRHVTA- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 230 tasPFRWLSWLSDSGATMTAAPNfAYNLIGKYARRVSEVDLGALRVtLNGGEPVDCdGLTRFAEAMapfGFDagaVLPSY 309
Cdd:PLN03102 264 ---PEIYKNIEMHNVTHMCCVPT-VFNILLKGNSLDLSPRSGPVHV-LTGGSPPPA-ALVKKVQRL---GFQ---VMHAY 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 310 GLAESTCAVtvpvpgigLLAD------RVIDGSGAHKHAVLGNPIPGM---EVRISCGDQAAGNASREIGEIEIRGASMM 380
Cdd:PLN03102 332 GLTEATGPV--------LFCEwqdewnRLPENQQMELKARQGVSILGLadvDVKNKETQESVPRDGKTMGEIVIKGSSIM 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 381 AGYLGQQPIDPD----DWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRST 455
Cdd:PLN03102 404 KGYLKNPKATSEafkhGWLNTGDVGVIHPDGHVeIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGE 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489502054 456 RPGLVVAAEfrgPDEANARAELIQRVASECGIV------------PSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:PLN03102 484 TPCAFVVLE---KGETTKEDRVDKLVTRERDLIeycrenlphfmcPRKVVFLQ--ELPKNGNGKILKPKLR 549
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
345-506 |
1.28e-09 |
|
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: 59.62 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 345 GNPIPGMEVRIscGDqAAGN--ASREIGEIEIRGASMMAGYLGQQPIDP----DDWFATGDLGY-LGAGGLVVCGRAKEV 417
Cdd:cd17636 166 GRPSPLVQVRI--LD-EDGRevPDGEVGEIVARGPTVMAGYWNRPEVNArrtrGGWHHTNDLGRrEPDGSLSFVGPKTRM 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 418 ISIAGRNIFPTEVELVAAQVRGVREGAVvaLGTGDrSTRPGLVVAAEFRGPDEANARAELI----QRVASECGivPSDVV 493
Cdd:cd17636 243 IKSGAENIYPAEVERCLRQHPAVADAAV--IGVPD-PRWAQSVKAIVVLKPGASVTEAELIehcrARIASYKK--PKSVE 317
|
170
....*....|...
gi 489502054 494 FVSpgSLPRTSSG 506
Cdd:cd17636 318 FAD--ALPRTAGG 328
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
369-519 |
3.56e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 59.09 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 369 IGEIEIRGASMMAGYLGQQPIDPD----DWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREG 443
Cdd:PLN02479 402 MGEIVMRGNMVMKGYLKNPKANEEafanGWFHSGDLGVKHPDGYIeIKDRSKDIIISGGENISSLEVENVVYTHPAVLEA 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 444 AVVALGTGDRSTRPGLVVA--AEFRGPDEANARAELIQRVASECG--IVPSDVVFvspGSLPRTSSGKLRRLAVR-RSLE 518
Cdd:PLN02479 482 SVVARPDERWGESPCAFVTlkPGVDKSDEAALAEDIMKFCRERLPayWVPKSVVF---GPLPKTATGKIQKHVLRaKAKE 558
|
.
gi 489502054 519 M 519
Cdd:PLN02479 559 M 559
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
395-511 |
3.68e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 58.62 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 395 FATGDLGYLgAGGLVVC-----------GRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAA 463
Cdd:COG1541 297 YRTGDLTRL-LPEPCPCgrthprigrilGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVEL 375
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489502054 464 EfRGPDEANARAELIQRVASECGIVPsDVVFVSPGSLPRtSSGKLRRL 511
Cdd:COG1541 376 A-PGASLEALAEAIAAALKAVLGLRA-EVELVEPGSLPR-SEGKAKRV 420
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
159-440 |
4.35e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 58.96 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVGTdAATDVGCSWLPLYHDMGLAFVLSAALAGAPLW---------------L 223
Cdd:PLN02736 229 TSGTTGTPKGVVLTHGNLIANVAGSSLSTKF-YPSDVHISYLPLAHIYERVNQIVMLHYGVAVGfyqgdnlklmddlaaL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 224 APTTaFTASPFRW-------LSWLSDSGATMTAAPNFAYN------LIGKYA---------RRVSEVDLGALRVTLNGGE 281
Cdd:PLN02736 308 RPTI-FCSVPRLYnriydgiTNAVKESGGLKERLFNAAYNakkqalENGKNPspmwdrlvfNKIKAKLGGRVRFMSSGAS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 282 PVDCDGLT--RFAeamapFGfdaGAVLPSYGLAESTCAVTVPVPGiglladrviDGSGAHkhavLGNPIPGMEVRIScgD 359
Cdd:PLN02736 387 PLSPDVMEflRIC-----FG---GRVLEGYGMTETSCVISGMDEG---------DNLSGH----VGSPNPACEVKLV--D 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 360 QAAGNASRE-----IGEIEIRGASMMAGYLGQQP-----IDPDDWFATGDLG-YLGAGGLVVCGRAKEVISIA-GRNIFP 427
Cdd:PLN02736 444 VPEMNYTSEdqpypRGEICVRGPIIFKGYYKDEVqtrevIDEDGWLHTGDIGlWLPGGRLKIIDRKKNIFKLAqGEYIAP 523
|
330
....*....|...
gi 489502054 428 TEVELVAAQVRGV 440
Cdd:PLN02736 524 EKIENVYAKCKFV 536
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
4-514 |
4.76e-09 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 58.62 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 4 LAAVLTRSMQASAGDLMVLDRETslwcRHPWPEVHGLAESVAAWLLDH-----DRpaaVGLVGEPTVELVAAIQG-AWLA 77
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVFGGT----RWTYAEAARAAAAAAHALAAAgvkrgDR---VALMCGNRIEFLDVFLGcAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 78 GAAVSIlPGPVRGAndqrwadaTLTRFLG-IGVRTVLSQGSYLARLRSVD-----TAGVTIGDLSTAAHTNRS------- 144
Cdd:PRK06155 96 AIAVPI-NTALRGP--------QLEHILRnSGARLLVVEAALLAALEAADpgdlpLPAVWLLDAPASVSVPAGwstaplp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 145 -------ATPVASEGPAVLQGTAGSTGaPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSWLPLYHDMGLAFVLSAALA 217
Cdd:PRK06155 167 pldapapAAAVQPGDTAAILYTSGTTG-PSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 218 GAPLWLAPTtaFTASPFrWLSwLSDSGATMTAapnfaynLIGKY-----ARRVSEVDLG-ALRVTLNGGEPVDCdgltrF 291
Cdd:PRK06155 246 GATYVLEPR--FSASGF-WPA-VRRHGATVTY-------LLGAMvsillSQPARESDRAhRVRVALGPGVPAAL-----H 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 292 AEAMAPFGFDAgavLPSYGLAESTCAVTVPVPgiglladrvidgsgAHKHAVLGNPIPGMEVRISC-GDQA--AGnasrE 368
Cdd:PRK06155 310 AAFRERFGVDL---LDGYGSTETNFVIAVTHG--------------SQRPGSMGRLAPGFEARVVDeHDQElpDG----E 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 369 IGEIEIRGA---SMMAGYLGqqpiDP--------DDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQ 436
Cdd:PRK06155 369 PGELLLRADepfAFATGYFG----MPektveawrNLWFHTGDRVVRDADGwFRFVDRIKDAIRRRGENISSFEVEQVLLS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 437 VRGVREGAVVALG---TGDRstrpglVVAAEFRGPDEANARAELIQRVASECG--IVPSDVVFVSpgSLPRTSSGKLRRL 511
Cdd:PRK06155 445 HPAVAAAAVFPVPselGEDE------VMAAVVLRDGTALEPVALVRHCEPRLAyfAVPRYVEFVA--ALPKTENGKVQKF 516
|
...
gi 489502054 512 AVR 514
Cdd:PRK06155 517 VLR 519
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
57-515 |
1.09e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.43 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 57 VGLVGEPTVELVAAIQGAWLAGAAVSILpgpvrganDQRWADATLTRFLG-IGVRTVLSQgsylARLRSVDTAGVTIGDL 135
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPL--------DPEYPEERLAYMLEdSGAQLLLSQ----SHLRLPLAQGVQVLDL 3177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 136 STAAHTNRSATP---VASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTdAATDVGCSWLPLYHDMGLAFVL 212
Cdd:PRK12316 3178 DRGDENYAEANPairTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGL-GVGDRVLQFTTFSFDVFVEELF 3256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 213 SAALAGAPLWLAPTTafTASPFRWLSWLSDSGATMTaaPNFAYNLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFa 292
Cdd:PRK12316 3257 WPLMSGARVVLAGPE--DWRDPALLVELINSEGVDV--LHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV- 3331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 293 eamapfgFDAGAVLPSYGLAESTCAVTVpvpgiglladrvIDGSGAHKHAV-LGNPIPGMEVRIsCGDQAAGNASREIGE 371
Cdd:PRK12316 3332 -------FAGLPLYNLYGPTEATITVTH------------WQCVEEGKDAVpIGRPIANRACYI-LDGSLEPVPVGALGE 3391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 372 IEIRGASMMAGY-----LGQQPIDPDDW------FATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRG 439
Cdd:PRK12316 3392 LYLGGEGLARGYhnrpgLTAERFVPDPFvpgerlYRTGDLARYRADGVIeYIGRVDHQVKIRGFRIELGEIEARLLEHPW 3471
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489502054 440 VREGAVVALgtgDRSTRPGLVVAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLAVRR 515
Cdd:PRK12316 3472 VREAVVLAV---DGRQLVAYVVPEDEAGDLREALKAHLKASLPEY--MVPAHLLFLE--RMPLTPNGKLDRKALPR 3540
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
151-513 |
1.47e-08 |
|
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: 57.09 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 151 EGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGCSWLPLYHDMGLAFVLSAALAGAPLWLAPTTAfT 230
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEV-K 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 231 ASPFRWLSWLSDSGAT-MTAAPNFAYNLIGKYARRvsEVDLGALRVTLNGGEPVDCDGltrFAEAMAPFGfdAGAVL-PS 308
Cdd:cd17650 172 LDPAALYDLILKSRITlMESTPALIRPVMAYVYRN--GLDLSAMRLLIVGSDGCKAQD---FKTLAARFG--QGMRIiNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 309 YGLAESTCAVTVpvpgIGLLADRVIDGSgahkHAVLGNPIPGMEVRI---SCGDQAAGNAsreiGEIEIRGASMMAGYLG 385
Cdd:cd17650 245 YGVTEATIDSTY----YEEGRDPLGDSA----NVPIGRPLPNTAMYVldeRLQPQPVGVA----GELYIGGAGVARGYLN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 386 -----QQPIDPDDW------FATGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVAlgTGDR 453
Cdd:cd17650 313 rpeltAERFVENPFapgermYRTGDLArWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAV--REDK 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489502054 454 STRPGL---VVAAEfrGPDEANARAELIQRVASEcgIVPSdvVFVSPGSLPRTSSGKLRRLAV 513
Cdd:cd17650 391 GGEARLcayVVAAA--TLNTAELRAFLAKELPSY--MIPS--YYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
344-511 |
1.61e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 57.21 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 344 LGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGA--SMMAGYLGqqpiDP--------DDWFATGDLGYLGAGG---LVv 410
Cdd:PRK04319 378 MGKPLPGIEAAI-VDDQGNELPPNRMGNLAIKKGwpSMMRGIWN----NPekyesyfaGDWYVSGDSAYMDEDGyfwFQ- 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 411 cGRAKEVISIAGRNIFPTEVE-------LVAA--------QVRGVREGAVVALgtgdrstRPGLvvaaefrGPDEAnARA 475
Cdd:PRK04319 452 -GRVDDVIKTSGERVGPFEVEsklmehpAVAEagvigkpdPVRGEIIKAFVAL-------RPGY-------EPSEE-LKE 515
|
170 180 190
....*....|....*....|....*....|....*....
gi 489502054 476 ELIQRVASECG--IVPSDVVFVSpgSLPRTSSGK-LRRL 511
Cdd:PRK04319 516 EIRGFVKKGLGahAAPREIEFKD--KLPKTRSGKiMRRV 552
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
345-440 |
1.77e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 57.13 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 345 GNPIPGMEVRIScgDQAAGN--ASREIGEIEIRGASMMAGYLG-----QQPIDPDDWFATGDLGYLGAGGLV-VCGRAKE 416
Cdd:PRK08315 374 GRALPHLEVKIV--DPETGEtvPRGEQGELCTRGYSVMKGYWNdpektAEAIDADGWMHTGDLAVMDEEGYVnIVGRIKD 451
|
90 100 110
....*....|....*....|....*....|..
gi 489502054 417 VISIAGRNIFPTEVE--------LVAAQVRGV 440
Cdd:PRK08315 452 MIIRGGENIYPREIEeflythpkIQDVQVVGV 483
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
338-514 |
2.14e-08 |
|
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: 56.62 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 338 AHKHAVlGNPIPGmEVRIsCGDQAAGNASREIGEIEIRGASMMA---GYLGQQP-IDPDDWFATGDLGYLGAGG-LVVCG 412
Cdd:cd05929 294 THPGSV-GRAVLG-KVHI-LDEDGNEVPPGEIGEVYFANGPGFEytnDPEKTAAaRNEGGWSTLGDVGYLDEDGyLYLTD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 413 RAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEANARAELI----QRVASEcgIV 488
Cdd:cd05929 371 RRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIaflrDRLSRY--KC 448
|
170 180
....*....|....*....|....*.
gi 489502054 489 PSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd05929 449 PRSIEFVA--ELPRDDTGKLYRRLLR 472
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
216-514 |
2.79e-08 |
|
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: 56.35 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 216 LAGAPLWLAPTTAFTasPFRWLSWLSDSGATMTAAPNFAYNLIGKyaRRVSEVDLGALRVTLNGGEPVDCDGLTRFAEam 295
Cdd:cd05970 250 IAGAAVFVYDYDKFD--PKALLEKLSKYGVTTFCAPPTIYRFLIR--EDLSRYDLSSLRYCTTAGEALNPEVFNTFKE-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 296 apfgFDAGAVLPSYGLAEST-CAVTVPVPGIglladrvidgsgahKHAVLGNPIPGMEVRISCGDQAAGNASREiGEIEI 374
Cdd:cd05970 324 ----KTGIKLMEGFGQTETTlTIATFPWMEP--------------KPGSMGKPAPGYEIDLIDREGRSCEAGEE-GEIVI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 375 RGAS-----MMAGYLGqqpiDP--------DDWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGV 440
Cdd:cd05970 385 RTSKgkpvgLFGGYYK----DAektaevwhDGYYHTGDAAWMDEDGyLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAV 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 441 REGAVvalgTGDRSTRPGLVVAAEFRGPDEANARAELIQRVASECGIV------PSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:cd05970 461 LECAV----TGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVtapykyPRIVEFVD--ELPKTISGKIRRVEIR 534
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
159-512 |
8.42e-08 |
|
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: 54.75 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGcswlplyHDMGLAFVLSAA------LAGAPLWLAPT------ 226
Cdd:cd17644 114 TSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVL-------QFASIAFDVAAEeiyvtlLSGATLVLRPEemrssl 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 227 ------------TAFTASPFRWLSWLSDSGATMTAAPNfaynligkyarrvsevdlgALRVTLNGGEPVDCDGLTRFAEA 294
Cdd:cd17644 187 edfvqyiqqwqlTVLSLPPAYWHLLVLELLLSTIDLPS-------------------SLRLVIVGGEAVQPELVRQWQKN 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 295 MAPFGfdagAVLPSYGLAESTCAVTVpvpgigllADRVIDGSGAHKHAVLGNPIPGMEVRIScgDQAAGNASREI-GEIE 373
Cdd:cd17644 248 VGNFI----QLINVYGPTEATIAATV--------CRLTQLTERNITSVPIGRPIANTQVYIL--DENLQPVPVGVpGELH 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 374 IRGASMMAGYLG----------QQPID---PDDWFATGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRG 439
Cdd:cd17644 314 IGGVGLARGYLNrpeltaekfiSHPFNsseSERLYKTGDLArYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHND 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502054 440 VREGAVVAlgtgdRSTRPG------LVVAAEFRGPDEANARAELIQRVASEcgIVPSdvVFVSPGSLPRTSSGKLRRLA 512
Cdd:cd17644 394 VKTAVVIV-----REDQPGnkrlvaYIVPHYEESPSTVELRQFLKAKLPDY--MIPS--AFVVLEELPLTPNGKIDRRA 463
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
159-512 |
2.95e-07 |
|
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: 52.64 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRtailspGAVL--SNLRGLNQRVGTDAATDVGCSWLPLYH---DMGLAFVLSAALAGAPLWLAPTTAFTA-S 232
Cdd:cd17652 101 TSGSTGRPK------GVVVthRGLANLAAAQIAAFDVGPGSRVLQFASpsfDASVWELLMALLAGATLVLAPAEELLPgE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 233 PFRWLswLSDSGATMTAAPNFAYNLigkyarrVSEVDLGALRVTLNGGEPVDCDGLTRFAeamapfgfDAGAVLPSYGLA 312
Cdd:cd17652 175 PLADL--LREHRITHVTLPPAALAA-------LPPDDLPDLRTLVVAGEACPAELVDRWA--------PGRRMINAYGPT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 313 ESTCAVTV--PVPGIGLLAdrvidgsgahkhavLGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLGQQPID 390
Cdd:cd17652 238 ETTVCATMagPLPGGGVPP--------------IGRPVPGTRVYV-LDARLRPVPPGVPGELYIAGAGLARGYLNRPGLT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 391 PDDWFA------------TGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVAlgTGDRSTRP 457
Cdd:cd17652 303 AERFVAdpfgapgsrmyrTGDLARWRADGqLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVV--RDDRPGDK 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489502054 458 GLV---VAAEFRGPDEANARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRLA 512
Cdd:cd17652 381 RLVayvVPAPGAAPTAAELRAHLAERLPGY--MVPAAFVVLD--ALPLTPNGKLDRRA 434
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
134-514 |
3.28e-07 |
|
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: 52.85 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 134 DLSTAAHTNRSATPVASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRgLNQRVGTD-AATDVgcSWLplYHDMGlaFVL 212
Cdd:cd05928 157 ELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLK-VNGRYWLDlTASDI--MWN--TSDTG--WIK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 213 SAALAGAPLWLAPTTAFTAS-----PFRWLSWLSDSGATMTAAPNFAYNLIgkYARRVSEVDLGALRVTLNGGEPVDCDG 287
Cdd:cd05928 230 SAWSSLFEPWIQGACVFVHHlprfdPLVILKTLSSYPITTFCGAPTVYRML--VQQDLSSYKFPSLQHCVTGGEPLNPEV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 288 LTRFAEAMapfGFDagaVLPSYGLAES--TCAVTvpvPGIGLladrvidgsgahKHAVLGNPIPGMEVRIsCGDQAAGNA 365
Cdd:cd05928 308 LEKWKAQT---GLD---IYEGYGQTETglICANF---KGMKI------------KPGSMGKASPPYDVQI-IDDNGNVLP 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 366 SREIGEIEI-----RGASMMAGYLGqqpiDPD--------DWFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVE 431
Cdd:cd05928 366 PGTEGDIGIrvkpiRPFGLFSGYVD----NPEktaatirgDFYLTGDRGIMDEDGyFWFMGRADDVINSSGYRIGPFEVE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 432 LVAAQVRGVREGAVVALGTGDRS--TRPGLVVAAEFRGPDEANARAELIQRVASECG--IVPSDVVFVSpgSLPRTSSGK 507
Cdd:cd05928 442 SALIEHPAVVESAVVSSPDPIRGevVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTApyKYPRKVEFVQ--ELPKTVTGK 519
|
....*..
gi 489502054 508 LRRLAVR 514
Cdd:cd05928 520 IQRNELR 526
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
369-513 |
3.66e-07 |
|
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: 52.48 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 369 IGEIEIRGASMMAGYLGQQ----------PIDPDD-WFATGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQ 436
Cdd:cd17656 327 VGELYISGASVARGYLNRQeltaekffpdPFDPNErMYRTGDLArYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLN 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502054 437 VRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEanaraELIQRVASECG--IVPSdvVFVSPGSLPRTSSGKLRRLAV 513
Cdd:cd17656 407 HPGVSEAVVLDKADDKGEKYLCAYFVMEQELNIS-----QLREYLAKQLPeyMIPS--FFVPLDQLPLTPNGKVDRKAL 478
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
306-508 |
4.83e-07 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 52.38 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 306 LPSYGLAESTcavtvpvpgIGLLADRvidGSGAHKHAVLGNPIPGMEVRI--SCGDQAAGNasrEIGEIEIRGA---SMM 380
Cdd:PRK08008 316 LTSYGMTETI---------VGIIGDR---PGDKRRWPSIGRPGFCYEAEIrdDHNRPLPAG---EIGEICIKGVpgkTIF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 381 AGYLgQQP------IDPDDWFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVValGTGDr 453
Cdd:PRK08008 381 KEYY-LDPkatakvLEADGWLHTGDTGYVDEEGFFyFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV--GIKD- 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489502054 454 STRPGLVVAAEFRGPDEANARAELIQRVASECGI--VPSDVVFVSpgSLPRTSSGKL 508
Cdd:PRK08008 457 SIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKfkVPSYLEIRK--DLPRNCSGKI 511
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
159-440 |
6.31e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 51.95 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAAT----DVGCSWLPLYH--DMGLAFVLSAALAGAPLW---------- 222
Cdd:PLN02614 231 TSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAAltvkDVYLSYLPLAHifDRVIEECFIQHGAAIGFWrgdvkllied 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 223 ---LAPTTaFTASPfRWLSW--------LSDSG----ATMTAAPNFAYNLIGKYARRVSEVDL--------------GAL 273
Cdd:PLN02614 311 lgeLKPTI-FCAVP-RVLDRvysglqkkLSDGGflkkFVFDSAFSYKFGNMKKGQSHVEASPLcdklvfnkvkqglgGNV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 274 RVTLNGGEPVdCDGLTRFAEAMApfgfdAGAVLPSYGLAESTCAVTVPVPG-IGLLAdrvidgsgahkhaVLGNPIPGME 352
Cdd:PLN02614 389 RIILSGAAPL-ASHVESFLRVVA-----CCHVLQGYGLTESCAGTFVSLPDeLDMLG-------------TVGPPVPNVD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 353 VRISCGDQ----AAGNASReiGEIEIRGASMMAGYLGQQPIDP----DDWFATGDLG-YLGAGGLVVCGRAKEVISIA-G 422
Cdd:PLN02614 450 IRLESVPEmeydALASTPR--GEICIRGKTLFSGYYKREDLTKevliDGWLHTGDVGeWQPNGSMKIIDRKKNIFKLSqG 527
|
330
....*....|....*...
gi 489502054 423 RNIFPTEVELVAAQVRGV 440
Cdd:PLN02614 528 EYVAVENIENIYGEVQAV 545
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
347-511 |
1.14e-06 |
|
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: 51.41 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 347 PIPGMEVRI--SCGDQAAGNASreiGEIEIRGA--SMMAGYLGqqpiDPD-----------DWFATGDlgylGA-----G 406
Cdd:cd05966 415 PFFGIEPAIldEEGNEVEGEVE---GYLVIKRPwpGMARTIYG----DHEryedtyfskfpGYYFTGD----GArrdedG 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 407 GLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVValGTGDRSTRPGLVVAAEFRGPDEANA--RAELIQRVASE 484
Cdd:cd05966 484 YYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVV--GRPHDIKGEAIYAFVTLKDGEEPSDelRKELRKHVRKE 561
|
170 180 190
....*....|....*....|....*....|
gi 489502054 485 CG--IVPSDVVFVSpgSLPRTSSGK-LRRL 511
Cdd:cd05966 562 IGpiATPDKIQFVP--GLPKTRSGKiMRRI 589
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
338-511 |
1.14e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 51.06 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 338 AHKHAVlGNPIPGmEVRIsCGDQAAGNASREIGEIEIRgasMMAG---YLGqqpiDPD---------DWFATGDLGYLGA 405
Cdd:PRK08276 312 AHPGSV-GKAVLG-EVRI-LDEDGNELPPGEIGTVYFE---MDGYpfeYHN----DPEktaaarnphGWVTVGDVGYLDE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 406 GG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRpglVVA----AEFRGPDEANArAELI-- 478
Cdd:PRK08276 382 DGyLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGER---VKAvvqpADGADAGDALA-AELIaw 457
|
170 180 190
....*....|....*....|....*....|....*...
gi 489502054 479 --QRVAsecGI-VPSDVVFVSpgSLPRTSSGKL--RRL 511
Cdd:PRK08276 458 lrGRLA---HYkCPRSIDFED--ELPRTPTGKLykRRL 490
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
422-510 |
1.87e-06 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 434024 [Multi-domain] Cd Length: 96 Bit Score: 46.31 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 422 GRNIFPTEVELVAAQVRGVREGAVVALgtgdrsTRPG----LVVAAEFRGP--DEANARAELIQRVA----SECGIVPsD 491
Cdd:pfam14535 1 GVNVFPSQIEEVLLEIPGVGPEYQIIV------TREGgldeLEVKVEVAEGfsDEIKDLEALEKRIAkelkSVLGVSV-K 73
|
90
....*....|....*....
gi 489502054 492 VVFVSPGSLPRtSSGKLRR 510
Cdd:pfam14535 74 VELVEPGTLPR-SEGKAKR 91
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
217-515 |
1.96e-06 |
|
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: 50.26 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 217 AGAPLWLAPTTAFTASpfRWLSWLSDSGATMTAAPNFAYnligkyaRRVSEVDLGALRVTLN----GGEPVDCDGLTRFA 292
Cdd:cd05974 151 AGATVFLFNYARFDAK--RVLAALVRYGVTTLCAPPTVW-------RMLIQQDLASFDVKLRevvgAGEPLNPEVIEQVR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 293 EAMAPfgfdagAVLPSYGLAESTCAVTvPVPGigllaDRVIDGSgahkhavLGNPIPGMEVRIScgdQAAGNASREiGEI 372
Cdd:cd05974 222 RAWGL------TIRDGYGQTETTALVG-NSPG-----QPVKAGS-------MGRPLPGYRVALL---DPDGAPATE-GEV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 373 EI-----RGASMMAGYLGqqpiDPDD--------WFATGDLGYLGAGG-LVVCGRAKEVISIAGRNIFPTEVELVAAQVR 438
Cdd:cd05974 279 ALdlgdtRPVGLMKGYAG----DPDKtahamrggYYRTGDIAMRDEDGyLTYVGRADDVFKSSDYRISPFELESVLIEHP 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489502054 439 GVREGAVVALGTGDRSTRPGLVVAAEfRGPDEANARAELIQRVASECGIVPSDVVFVSPGSLPRTSSGKLRRLAVRR 515
Cdd:cd05974 355 AVAEAAVVPSPDPVRLSVPKAFIVLR-AGYEPSPETALEIFRFSRERLAPYKRIRRLEFAELPKTISGKIRRVELRR 430
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
21-511 |
2.10e-06 |
|
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: 50.09 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 21 VLDRETSLWCRhpwpEVHGLAESVAAWLLDHDRPAA---VGLVGEPTVELVAAIQGAWLAGAA-VSILPG-PvrganDQR 95
Cdd:cd17648 6 VVYGDKRLTYR----ELNERANRLAHYLLSVAEIRPddlVGLVLDKSELMIIAILAVWKAGAAyVPIDPSyP-----DER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 96 wadatltrflgigVRTVLSQGSylarLRSVDTagvTIGDLSTAAHTnrsatpvasegpavlqgtAGSTGAPRTAILSPGA 175
Cdd:cd17648 77 -------------IQFILEDTG----ARVVIT---NSTDLAYAIYT------------------SGTTGKPKGVLVEHGS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 176 VLSNLRGLNQRVGTDAATDVGCSWLPLY-HDMGLAFVLSAALAGAPLwLAPTTAFTASPFRWLSWLSDSGAT-MTAAPNF 253
Cdd:cd17648 119 VVNLRTSLSERYFGRDNGDEAVLFFSNYvFDFFVEQMTLALLNGQKL-VVPPDEMRFDPDRFYAYINREKVTyLSGTPSV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 254 aynligkyarrVSEVDLGAL----RVTLNGgepvdcdgltrfaEAMAPFGFD------AGAVLPSYGLAESTC-AVTVPV 322
Cdd:cd17648 198 -----------LQQYDLARLphlkRVDAAG-------------EEFTAPVFEklrsrfAGLIINAYGPTETTVtNHKRFF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 323 PGigllaDRVIDGSgahkhavLGNPIPGMEVRIsCGDQAAGNASREIGEIEIRGASMMAGYLGQQPIDPDDW-------- 394
Cdd:cd17648 254 PG-----DQRFDKS-------LGRPVRNTKCYV-LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqte 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 395 -----------FATGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVA-------LGTGDR-- 453
Cdd:cd17648 321 qerargrnarlYKTGDLVrWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkedasqaQSRIQKyl 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489502054 454 ----STRPGLVVAAEFRgpdeANARAELIQRvasecgIVPSDVVFVSpgSLPRTSSGKL--RRL 511
Cdd:cd17648 401 vgyyLPEPGHVPESDLL----SFLRAKLPRY------MVPARLVRLE--GIPVTINGKLdvRAL 452
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
370-518 |
2.90e-06 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 49.98 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 370 GEIEIRGASMMAGYLG-----QQPIDPDDWFATGDLGYL-GAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREG 443
Cdd:PLN02246 384 GEICIRGPQIMKGYLNdpeatANTIDKDGWLHTGDIGYIdDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADA 463
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502054 444 AVVALGTGDRSTRPglvVAAEFRGPDEANARAELIQRVASEcgIV----PSDVVFVSpgSLPRTSSGKLRRLAVRRSLE 518
Cdd:PLN02246 464 AVVPMKDEVAGEVP---VAFVVRSNGSEITEDEIKQFVAKQ--VVfykrIHKVFFVD--SIPKAPSGKILRKDLRAKLA 535
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
273-513 |
4.72e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.78 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 273 LRVTLNGGEPVDCDGLTRFAEAMAPFGFdagavLPSYGLAEstcavTVPVPGIGLLADRVIDGSGAhkhaVLGNPIPGME 352
Cdd:PRK05691 2450 VRMCITGGEALTGEHLQRIRQAFAPQLF-----FNAYGPTE-----TVVMPLACLAPEQLEEGAAS----VPIGRVVGAR 2515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 353 VRISCGDQAAGNASREIGEIEIRGASMMAGYLGQ----------QPIDPDD--WFATGDLGYLGAGGLV-VCGRAKEVIS 419
Cdd:PRK05691 2516 VAYILDADLALVPQGATGELYVGGAGLAQGYHDRpgltaerfvaDPFAADGgrLYRTGDLVRLRADGLVeYVGRIDHQVK 2595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 420 IAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEFRGPDEanARAELIQRVASECG------IVPSDVV 493
Cdd:PRK05691 2596 IRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDE--AQAALREALKAHLKqqlpdyMVPAHLI 2673
|
250 260
....*....|....*....|
gi 489502054 494 FVspGSLPRTSSGKLRRLAV 513
Cdd:PRK05691 2674 LL--DSLPLTANGKLDRRAL 2691
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
131-236 |
6.32e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 48.72 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 131 TIGDLSTAAHTNRSATPVASEG-----PAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNqrVGTDA-ATDVGCSWLPLYH 204
Cdd:PRK08279 174 GYEDLAAAAAGAPTTNPASRSGvtakdTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFG--GLLRLtPDDVLYCCLPLYH 251
|
90 100 110
....*....|....*....|....*....|...
gi 489502054 205 DMGLAFVLSAALA-GAPLWLAPTtaFTASPFrW 236
Cdd:PRK08279 252 NTGGTVAWSSVLAaGATLALRRK--FSASRF-W 281
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
159-518 |
1.01e-05 |
|
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: 47.92 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVgcswlpL----YH-DMGLAFVLSAALAGAplwlaptTAFTASP 233
Cdd:cd05918 114 TSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRV------LqfasYTfDVSILEIFTTLAAGG-------CLCIPSE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 234 FRWLSWLSDSGATMtaAPNFAYnLIGKYARRVSEVDLGALRVTLNGGEPVDCDGLTRFAEAMApfgfdagaVLPSYGLAE 313
Cdd:cd05918 181 EDRLNDLAGFINRL--RVTWAF-LTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVR--------LINAYGPAE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 314 STCAVTVPVPG-------IGLLAD---RVIDGSGAHKHAVLGnpipgmevriscgdqaagnasrEIGEIEIRGASMMAGY 383
Cdd:cd05918 250 CTIAATVSPVVpstdprnIGRPLGatcWVVDPDNHDRLVPIG----------------------AVGELLIEGPILARGY 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 384 LGQQ-------PIDPDDWFA-----------TGDLGYLGA-GGLVVCGRAKEVISIAGRNIFPTEVE-LVAAQVRGVREG 443
Cdd:cd05918 308 LNDPektaaafIEDPAWLKQegsgrgrrlyrTGDLVRYNPdGSLEYVGRKDTQVKIRGQRVELGEIEhHLRQSLPGAKEV 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 444 AVVALGTGDRSTRPGLVVAAEFRGPDEANAR------------AELIQRVASECG------IVPSDVVFVSpgSLPRTSS 505
Cdd:cd05918 388 VVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDgdslflepsdefRALVAELRSKLRqrlpsyMVPSVFLPLS--HLPLTAS 465
|
410
....*....|...
gi 489502054 506 GKLRRLAVRRSLE 518
Cdd:cd05918 466 GKIDRRALRELAE 478
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
56-512 |
1.35e-05 |
|
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: 47.71 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 56 AVGLVGEPTVELVAAIQGAWLAGAA-VSILPgpvrgandqrwaDATLTRFLGI----GVRTVLSQGSYLARLRSVDTAGV 130
Cdd:cd17655 49 IVGIMAERSLEMIVGILGILKAGGAyLPIDP------------DYPEERIQYIledsGADILLTQSHLQPPIAFIGLIDL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 131 TigDLSTAAHTNRSATPVASEGP--AVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVGTDAATDVGcSWLPLYHDMGL 208
Cdd:cd17655 117 L--DEDTIYHEESENLEPVSKSDdlAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVA-LFASISFDASV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 209 AFVLSAALAGAPLWLAP-TTAFTASPFrwLSWLSDSGATMTAAPNFAYNLIgKYARRVSEVDLgalRVTLNGGEPVDCDG 287
Cdd:cd17655 194 TEIFASLLSGNTLYIVRkETVLDGQAL--TQYIRQNRITIIDLTPAHLKLL-DAADDSEGLSL---KHLIVGGEALSTEL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 288 LTRFAEAmapFGfDAGAVLPSYGLAEST-CAVTVPvpgiglladrvIDGSGAHKHAV-LGNPIPGMEVRIScgD-----Q 360
Cdd:cd17655 268 AKKIIEL---FG-TNPTITNAYGPTETTvDASIYQ-----------YEPETDQQVSVpIGKPLGNTRIYIL--DqygrpQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 361 AAGNAsreiGEIEIRGASMMAGYLG----------QQPIDPDD-WFATGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPT 428
Cdd:cd17655 331 PVGVA----GELYIGGEGVARGYLNrpeltaekfvDDPFVPGErMYRTGDLArWLPDGNIEFLGRIDHQVKIRGYRIELG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 429 EVELVAAQVRGVREGAVVALGTGDRStrpgLVVAAEFRGPDEANArAELIQRVASECG--IVPSdvVFVSPGSLPRTSSG 506
Cdd:cd17655 407 EIEARLLQHPDIKEAVVIARKDEQGQ----NYLCAYIVSEKELPV-AQLREFLARELPdyMIPS--YFIKLDEIPLTPNG 479
|
....*.
gi 489502054 507 KLRRLA 512
Cdd:cd17655 480 KVDRKA 485
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
144-514 |
1.76e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 144 SATPVASEGP--AVLQGTAGSTGAPR--------TAILSPG----AVLSNLRGLNQrvgtdaaTDVGCSWLPLYHdmgla 209
Cdd:PRK13390 139 GAGPRLTEQPcgAVMLYSSGTTGFPKgiqpdlpgRDVDAPGdpivAIARAFYDISE-------SDIYYSSAPIYH----- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 210 fvlsaalagaplwlapttaftASPFRWLSWLSDSGATMTAAPNFAYNLIGKYARRV-----------------------S 266
Cdd:PRK13390 207 ---------------------AAPLRWCSMVHALGGTVVLAKRFDAQATLGHVERYritvtqmvptmfvrllkldadvrT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 267 EVDLGALRVTLNGGEPVDCDGLTRFAEAMAPFGFDAGAVLPSYGLAestcavtvpvpgiglladrVIDGSG--AHKHAVl 344
Cdd:PRK13390 266 RYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMT-------------------FIDSPDwlAHPGSV- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 345 GNPIPGmEVRIsCGDQAAGNASREIGEIEIRGASMMAGYL--------GQQPIDPDdWFATGDLGYLGAGG-LVVCGRAK 415
Cdd:PRK13390 326 GRSVLG-DLHI-CDDDGNELPAGRIGTVYFERDRLPFRYLndpektaaAQHPAHPF-WTTVGDLGSVDEDGyLYLADRKS 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 416 EVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVV--AAEFRGPDEAnARaELIQRVASECG--IVPSD 491
Cdd:PRK13390 403 FMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIqlVEGIRGSDEL-AR-ELIDYTRSRIAhyKAPRS 480
|
410 420
....*....|....*....|...
gi 489502054 492 VVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:PRK13390 481 VEFVD--ELPRTPTGKLVKGLLR 501
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
370-512 |
3.48e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 46.58 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 370 GEIEIRGASMMAGYLGQqpidPD--------DWFA-------TGDLG-YLGAGGLVVCGRAKEVISIAGRNIFPTEVELV 433
Cdd:PRK10252 803 GDLYLTGIQLAQGYLGR----PDltasrfiaDPFApgermyrTGDVArWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRA 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 434 AAQVRGVREGAVVAL------GTGDRSTR-PGLVVAAEFRGPDEANARAELIQRVASEcgIVPsdVVFVSPGSLPRTSSG 506
Cdd:PRK10252 879 MQALPDVEQAVTHACvinqaaATGGDARQlVGYLVSQSGLPLDTSALQAQLRERLPPH--MVP--VVLLQLDQLPLSANG 954
|
....*.
gi 489502054 507 KLRRLA 512
Cdd:PRK10252 955 KLDRKA 960
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
368-488 |
7.05e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 45.59 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 368 EIGEIEIRGASMMAGYLGQQPI-----------DPDDW----------------------FATGDLG-YLGAGGLVVCGR 413
Cdd:cd17647 314 EVGEIYVRAGGLAEGYRGLPELnkekfvnnwfvEPDHWnyldkdnnepwrqfwlgprdrlYRTGDLGrYLPNGDCECCGR 393
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489502054 414 AKEVISIAGRNIFPTEVELVAAQVRGVREGavVALGTGDRSTRPGLV--VAAEFRGPDEANARAELIQRVASECGIV 488
Cdd:cd17647 394 ADDQVKIRGFRIELGEIDTHISQHPLVREN--ITLVRRDKDEEPTLVsyIVPRFDKPDDESFAQEDVPKEVSTDPIV 468
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
429-507 |
8.51e-05 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 40.99 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 429 EVELVAAQVRGVREGAVValgtGDRSTRPGLVVAAeF--RGPDEANARAELIQRVASECG--IVPSDVVFVSpgSLPRTS 504
Cdd:pfam13193 1 EVESALVSHPAVAEAAVV----GVPDELKGEAPVA-FvvLKPGVELLEEELVAHVREELGpyAVPKEVVFVD--ELPKTR 73
|
...
gi 489502054 505 SGK 507
Cdd:pfam13193 74 SGK 76
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
367-515 |
1.11e-04 |
|
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: 44.73 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 367 REIGEIEIRGASMMAGYLGQQPIDPDD-----WFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGV 440
Cdd:cd05915 358 KALGEVQLKGPWITGGYYGNEEATRSAltpdgFFRTGDIAVWDEEGYVeIKDRLKDLIKSGGEWISSVDLENALMGHPKV 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502054 441 REGAVValGTGDRSTRPGLVVAAEFRgpdEANARAELI----QRVASECGIVPSDVVFvsPGSLPRTSSGKLRRLAVRR 515
Cdd:cd05915 438 KEAAVV--AIPHPKWQERPLAVVVPR---GEKPTPEELnehlLKAGFAKWQLPDAYVF--AEEIPRTSAGKFLKRALRE 509
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
412-515 |
1.55e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 44.15 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 412 GRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRPGLVVAAEfRGPDEANARAELIQRVASECGI---V 488
Cdd:cd05913 320 GRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVR-PEADDDEKLEALKQRLERHIKSvlgV 398
|
90 100
....*....|....*....|....*..
gi 489502054 489 PSDVVFVSPGSLPRtSSGKLRRLAVRR 515
Cdd:cd05913 399 TVEVELVEPGSLPR-SEGKAKRVIDKR 424
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
34-236 |
1.78e-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: 43.88 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 34 WPEVHGLAESVAAWLLDH--DRPAAVGLVGEPTVELVAAIQGAWLAGAAVSILPGPVRGANdqrwadatltrflgigvrt 111
Cdd:cd05940 6 YAELDAMANRYARWLKSLglKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGES------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 112 vlsqgsyLARLRSVDTAGVTIGDlstaahtnrsatpvasegPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLnQRVGTDA 191
Cdd:cd05940 67 -------LAHCLNVSSAKHLVVD------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFF-AGSGGAL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489502054 192 ATDVGCSWLPLYHDMGLAFVLSAAL-AGAPLWLAptTAFTASPFrW 236
Cdd:cd05940 121 PSDVLYTCLPLYHSTALIVGWSACLaSGATLVIR--KKFSASNF-W 163
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
412-511 |
3.04e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 43.59 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 412 GRAKEVISIAGRNIFPTEVE--LVAAQvrGVREGAVValGTGDRSTRPGL---VVAAEFRGPDEAnARAELIQRVASECG 486
Cdd:PRK00174 503 GRVDDVLNVSGHRLGTAEIEsaLVAHP--KVAEAAVV--GRPDDIKGQGIyafVTLKGGEEPSDE-LRKELRNWVRKEIG 577
|
90 100
....*....|....*....|....*..
gi 489502054 487 -IVPSDVVFVSPGsLPRTSSGK-LRRL 511
Cdd:PRK00174 578 pIAKPDVIQFAPG-LPKTRSGKiMRRI 603
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
412-514 |
5.70e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 42.63 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 412 GRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTRP-GLVVAAEFRGPDEANAR----AELIQRVASECG 486
Cdd:PRK10524 493 GRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAvAFVVPKDSDSLADREARlaleKEIMALVDSQLG 572
|
90 100 110
....*....|....*....|....*....|
gi 489502054 487 IV--PSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:PRK10524 573 AVarPARVWFVS--ALPKTRSGKLLRRAIQ 600
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
159-437 |
7.15e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 42.14 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRVG-TD---AATDVGCSWLPLYH----DMGLAFVLSAALAGapLW-------- 222
Cdd:PLN02861 228 TSGTTGEPKGVILTNRAIIAEVLSTDHLLKvTDrvaTEEDSYFSYLPLAHvydqVIETYCISKGASIG--FWqgdirylm 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 223 -----LAPTTaFTASPFRW-------LSWLSDSGATMTAAPNFAYNLIGKYARR------------------VSEVDLGA 272
Cdd:PLN02861 306 edvqaLKPTI-FCGVPRVYdriytgiMQKISSGGMLRKKLFDFAYNYKLGNLRKglkqeeasprldrlvfdkIKEGLGGR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 273 LRVTLNGGEPvdcdgLTRFAEAMAPFgFDAGAVLPSYGLAESTCAVTVPVPGIGLLADRVidgsgahkhavlGNPIPGME 352
Cdd:PLN02861 385 VRLLLSGAAP-----LPRHVEEFLRV-TSCSVLSQGYGLTESCGGCFTSIANVFSMVGTV------------GVPMTTIE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 353 VRISC----GDQAAGNASReiGEIEIRGASMMAGYLGQQPIDP----DDWFATGDLGYLGAGGlvvcgrAKEVISiAGRN 424
Cdd:PLN02861 447 ARLESvpemGYDALSDVPR--GEICLRGNTLFSGYHKRQDLTEevliDGWFHTGDIGEWQPNG------AMKIID-RKKN 517
|
330
....*....|....
gi 489502054 425 IFP-TEVELVAAQV 437
Cdd:PLN02861 518 IFKlSQGEYVAVEN 531
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
159-415 |
7.42e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 42.27 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 159 TAGSTGAPRTAILSPGAVLSNLRGLNQRV----GTDAATDVGCSWLPLYHDMGLA----FVLSAALA--GAPLWLAPTTA 228
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLTAGILALEDRLndliGPPEEDETYCSYLPLAHIMEFGvtniFLARGALIgfGSPRTLTDTFA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 229 ------FTASPFrwlswlsdsgatMTAAPNFAYNLIGK--------------------YARR------------------ 264
Cdd:PTZ00216 352 rphgdlTEFRPV------------FLIGVPRIFDTIKKaveaklppvgslkrrvfdhaYQSRlralkegkdtpywnekvf 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 265 --VSEVDLGALRVTLNGGEPVdcdgltrfAEAMAPF---GFdaGAVLPSYGLAESTCavtvpVPGIGLLADRvidgsgah 339
Cdd:PTZ00216 420 saPRAVLGGRVRAMLSGGGPL--------SAATQEFvnvVF--GMVIQGWGLTETVC-----CGGIQRTGDL-------- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 340 KHAVLGNPIPGMEVRISCGDQAAGNASREI-GEIEIRGASMMAGYLGQ-----QPIDPDDWFATGDLGYLGAGG-LVVCG 412
Cdd:PTZ00216 477 EPNAVGQLLKGVEMKLLDTEEYKHTDTPEPrGEILLRGPFLFKGYYKQeeltrEVLDEDGWFHTGDVGSIAANGtLRIIG 556
|
...
gi 489502054 413 RAK 415
Cdd:PTZ00216 557 RVK 559
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
338-514 |
1.50e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 41.22 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 338 AHKHAVlGNPIPGmEVRIsCGDQAAGNASREIGEIEIRGASMMAgYLG-----QQPIDPD-DWFATGDLGYLGAGG-LVV 410
Cdd:PRK13391 325 AHPGTV-GRAMFG-DLHI-LDDDGAELPPGEPGTIWFEGGRPFE-YLNdpaktAEARHPDgTWSTVGDIGYVDEDGyLYL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 411 CGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVALGTGDRSTR-PGLVVAAEFRGPDEANArAELI----QRVASEc 485
Cdd:PRK13391 401 TDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEvKAVVQPVDGVDPGPALA-AELIafcrQRLSRQ- 478
|
170 180
....*....|....*....|....*....
gi 489502054 486 gIVPSDVVFVSpgSLPRTSSGKLRRLAVR 514
Cdd:PRK13391 479 -KCPRSIDFED--ELPRLPTGKLYKRLLR 504
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
273-508 |
2.49e-03 |
|
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: 40.53 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 273 LRVTLNGGEPvdCDGLTRFAEAMAPFgfDAGAVLPSYGLAESTC-AVTVPVPgiglladrvIDGSGAHkhavLGNPIPG- 350
Cdd:cd17654 240 LRVLALGGEP--FPSLVILSSWRGKG--NRTRIFNIYGITEVSCwALAYKVP---------EEDSPVQ----LGSPLLGt 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 351 -MEVRISCGDQAAGNASreIGEIEIRGasMMAGYLGQQPidpDDWFATGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTE 429
Cdd:cd17654 303 vIEVRDQNGSEGTGQVF--LGGLNRVC--ILDDEVTVPK---GTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDL 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502054 430 VELVAAQVRGVrEGAVVALGTGDRstrpglvVAAEFRGPDEANARAELIQRVASECGIVPSDVVFVSpgSLPRTSSGKL 508
Cdd:cd17654 376 IQQVIESCLGV-ESCAVTLSDQQR-------LIAFIVGESSSSRIHKELQLTLLSSHAIPDTFVQID--KLPLTSHGKV 444
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
394-507 |
3.40e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 39.67 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 394 WFATGDLGYLGAGGLV-VCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVValgtGDRSTRPGLVVAA--EFRGPDE 470
Cdd:cd05924 246 YAVPGDRATVEADGTVtLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV----GRPDERWGQEVVAvvQLREGAG 321
|
90 100 110
....*....|....*....|....*....|....*....
gi 489502054 471 ANaRAELIQRVASECG--IVPSDVVFVspGSLPRTSSGK 507
Cdd:cd05924 322 VD-LEELREHCRTRIAryKLPKQVVFV--DEIERSPAGK 357
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
288-513 |
4.49e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 39.49 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 288 LTRFAEAMapfgfdagaVLPSYGLAESTCAVT-VPVpgigllADRVIDgsgAHKHAVLGNPIPGMEVRIscgDQAAGN-- 364
Cdd:PRK04813 281 LERFPSAT---------IYNTYGPTEATVAVTsIEI------TDEMLD---QYKRLPIGYAKPDSPLLI---IDEEGTkl 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 365 ASREIGEIEIRGASMMAGYLGQQ--------PIDPDDWFATGDLGYLGAGGLVVCGRAKEVISIAGRNIFPTEVELVAAQ 436
Cdd:PRK04813 340 PDGEQGEIVISGPSVSKGYLNNPektaeaffTFDGQPAYHTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 437 VRGVREGAVVALGTGDRSTR-PGLVVAAEFRGPDEA----NARAELIQRVASEcgIVPSDVVFVSpgSLPRTSSGKLRRL 511
Cdd:PRK04813 420 SSYVESAVVVPYNKDHKVQYlIAYVVPKEEDFEREFeltkAIKKELKERLMEY--MIPRKFIYRD--SLPLTPNGKIDRK 495
|
..
gi 489502054 512 AV 513
Cdd:PRK04813 496 AL 497
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
36-513 |
7.05e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 39.38 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 36 EVHGLAESVAAWLLDHD--RPAAVGLVGEPTVELVAAIQGAWLAGAAVSILpgpvrganDQRWADATLTRFLG-IGVRTV 112
Cdd:PRK05691 1161 ELHAQANRLAHYLRDKGvgPDVCVAIAAERSPQLLVGLLAILKAGGAYVPL--------DPDYPAERLAYMLAdSGVELL 1232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 113 LSQGSYLARLRSVDtaGVTIGDLSTAAHTNRSATP----VASEGPAVLQGTAGSTGAPRTAILSPGAVLSNLRGLNQRVG 188
Cdd:PRK05691 1233 LTQSHLLERLPQAE--GVSAIALDSLHLDSWPSQApglhLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYA 1310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 189 TDAaTDVGCSWLPLYHDMGLAFVLSAALAGAPLWLApTTAFTASPFRWLSWLSDSGATMTaapNFAYNLIGKYARRVSEV 268
Cdd:PRK05691 1311 LDD-SDVLMQKAPISFDVSVWECFWPLITGCRLVLA-GPGEHRDPQRIAELVQQYGVTTL---HFVPPLLQLFIDEPLAA 1385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 269 DLGALRVTLNGGEPVDCDGLTRFAEamapfgfdagaVLPS------YGLAESTCAVTvpvpgigLLADRVIDGsgahKHA 342
Cdd:PRK05691 1386 ACTSLRRLFSGGEALPAELRNRVLQ-----------RLPQvqlhnrYGPTETAINVT-------HWQCQAEDG----ERS 1443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 343 VLGNPIPGMEVRISCGD---QAAGNAsreiGEIEIRGASMMAGYLGQQPI-------DPDD-----WFATGDLGYLGA-G 406
Cdd:PRK05691 1444 PIGRPLGNVLCRVLDAElnlLPPGVA----GELCIGGAGLARGYLGRPALtaerfvpDPLGedgarLYRTGDRARWNAdG 1519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502054 407 GLVVCGRAKEVISIAGRNIFPTEVELVAAQVRGVREGAVVAlgtgdRSTRPGLVVAAEFRGPDEANARAELIQRVASEcg 486
Cdd:PRK05691 1520 ALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLV-----REGAAGAQLVGYYTGEAGQEAEAERLKAALAA-- 1592
|
490 500 510
....*....|....*....|....*....|
gi 489502054 487 IVPSDVV---FVSPGSLPRTSSGKLRRLAV 513
Cdd:PRK05691 1593 ELPEYMVpaqLIRLDQMPLGPSGKLDRRAL 1622
|
|
| |
