|
Name |
Accession |
Description |
Interval |
E-value |
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
12-539 |
0e+00 |
|
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: 829.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 12 PPLTPIGFLERAATVYGDCTSIVYGSnTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAI 91
Cdd:cd12118 2 VPLTPLSFLERAAAVYPDRTSIVYGD-RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 92 LNNINTRLDARTVSVLLRHCGSKLLFVDVfsvdlaveaismmttdppilvfiadkeeeggdadvadrtkfSYTYDDLIHR 171
Cdd:cd12118 81 LNALNTRLDAEEIAFILRHSEAKVLFVDR-----------------------------------------EFEYEDLLAE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 172 GDLDFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVG 251
Cdd:cd12118 120 GDPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 252 GTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEF--QPLNRPVNILTAGAPPPAAVLLRAESIGFVISHGYG 329
Cdd:cd12118 200 GTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSdaRPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 330 LTETAGLNVSCAWKPQWNRLPASDRARLKARQGVRTVGFTEIDVVDPESGRSVERNGETVGEIVMRGSSIMLGYLKDPVG 409
Cdd:cd12118 280 LTETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLKNPEA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 410 TEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLK 489
Cdd:cd12118 360 TAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELK 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 9759119 490 SGltQRPTEVEMIEYCRKKMPKYMVPKTVSFvDELPKTSTGKVMKFVLRE 539
Cdd:cd12118 440 EG--AKVTEEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
6-542 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 753.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 6 PCAANSPPLTPIGFLERAATVYGDCTSIVYGSnTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAV 85
Cdd:PRK08162 10 RNAANYVPLTPLSFLERAAEVYPDRPAVIHGD-RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 86 PMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTTDPPILVFIADKEEEGGDAdVADRTkfsytY 165
Cdd:PRK08162 89 PMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRF-IGALD-----Y 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 166 DDLIHRGDLDFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPW 245
Cdd:PRK08162 163 EAFLASGDPDFAWTLPADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNGWCFPW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 246 GIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNML-SATNEFQ-PLNRPVNILTAGAPPPAAVLLRAESIGFV 323
Cdd:PRK08162 243 TVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALiNAPAEWRaGIDHPVHAMVAGAAPPAAVIAKMEEIGFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 324 ISHGYGLTETAGLNVSCAWKPQWNRLPASDRARLKARQGVRTVGFTEIDVVDPESGRSVERNGETVGEIVMRGSSIMLGY 403
Cdd:PRK08162 323 LTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIMFRGNIVMKGY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 404 LKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPC 483
Cdd:PRK08162 403 LKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPC 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 9759119 484 AFVSLKSGLTQrpTEVEMIEYCRKKMPKYMVPKTVSFvDELPKTSTGKVMKFVLREIAK 542
Cdd:PRK08162 483 AFVELKDGASA--TEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAK 538
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
8-552 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 660.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 8 AANSPPLTPIGFLERAATVYGDCTSIVYGSnTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPM 87
Cdd:PLN02479 14 AANYTALTPLWFLERAAVVHPTRKSVVHGS-VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 88 SGAILNNINTRLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTT------DPPILVFIADKEEEGGDADVADRtKF 161
Cdd:PLN02479 93 AGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEkkkssfKPPLLIVIGDPTCDPKSLQYALG-KG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 162 SYTYDDLIHRGDLDFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGW 241
Cdd:PLN02479 172 AIEYEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGW 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 242 SYPWGIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNML---SATNEFQPLNRPVNILTAGAPPPAAVLLRAE 318
Cdd:PLN02479 252 CFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIvnaPKSETILPLPRVVHVMTAGAAPPPSVLFAMS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 319 SIGFVISHGYGLTETAGLNVSCAWKPQWNRLPASDRARLKARQGVRTVGFTEIDVVDPESGRSVERNGETVGEIVMRGSS 398
Cdd:PLN02479 332 EKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPADGKTMGEIVMRGNM 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 399 IMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFW 478
Cdd:PLN02479 412 VMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERW 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9759119 479 GETPCAFVSLKSGLT---QRPTEVEMIEYCRKKMPKYMVPKTVSFvDELPKTSTGKVMKFVLREIAKKMGTTRLSRM 552
Cdd:PLN02479 492 GESPCAFVTLKPGVDksdEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKAKEMGPVKKSRL 567
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1-544 |
0e+00 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 631.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 1 MEQMKPCAANSPPLTPIGFLERAATVYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYE 80
Cdd:PLN03102 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYG-KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 81 LQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTTD-----PPIlVFIadkeeegGDADV 155
Cdd:PLN03102 80 MHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEdsnlnLPV-IFI-------HEIDF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 156 ADRTKFS-YTYDDLIHRGD----LDFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYL 230
Cdd:PLN03102 152 PKRPSSEeLDYECLIQRGEptpsLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 231 WTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATN--EFQPLNRPVNILTAGAP 308
Cdd:PLN03102 232 WTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNslDLSPRSGPVHVLTGGSP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 309 PPAAVLLRAESIGFVISHGYGLTETAGLNVSCAWKPQWNRLPASDRARLKARQGVRTVGFTEIDVVDPESGRSVERNGET 388
Cdd:PLN03102 312 PPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPRDGKT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 389 VGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEV 468
Cdd:PLN03102 392 MGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLET 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 469 AVVARPDVFWGETPCAFVSLKSGLTQRP--------TEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREI 540
Cdd:PLN03102 472 AVVAMPHPTWGETPCAFVVLEKGETTKEdrvdklvtRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
....
gi 9759119 541 AKKM 544
Cdd:PLN03102 552 AKGL 555
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
19-543 |
9.70e-149 |
|
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: 435.01 E-value: 9.70e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATVYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTR 98
Cdd:COG0318 4 LLRRAAARHPDRPALVFG-GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 99 LDARTVSVLLRHCGSKLLFVdvfsvdlaveaismmttdppilvfiadkeeeggdadvadrtkfsytyddlihrgdldfkw 178
Cdd:COG0318 83 LTAEELAYILEDSGARALVT------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 179 irpesewdpVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIA-AVGGTNVCL 257
Cdd:COG0318 103 ---------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPlLAGATLVLL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 RKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRP--VNILTAGAPPPAAVLLRAES-IGFVISHGYGLTETA 334
Cdd:COG0318 174 PRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSslRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTETS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 335 GLnVSCAWKPQWNRLPASdrarlkarQGvRTVGFTEIDVVDPEsGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEKAL 414
Cdd:COG0318 254 PV-VTVNPEDPGERRPGS--------VG-RPLPGVEVRIVDED-GRELPPG--EVGEIVVRGPNVMKGYWNDPEATAEAF 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 415 KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQ 494
Cdd:COG0318 321 RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG--A 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 9759119 495 RPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKK 543
Cdd:COG0318 399 ELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAA 447
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-539 |
3.91e-147 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 433.46 E-value: 3.91e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 9 ANSPPLTPIGFLERAATVYGDCTsIVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMS 88
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKE-AVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 89 GAILNNINTRLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTTDPPILVfiadkeeeGGDADVADRTKFSYTYDDL 168
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIV--------EGDGPAAPLAPEVGEYEEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 169 IHRGDLDFKWIRPEsEWDPVVLNYTSGTTSAPKGVVHCHRGIF--VMSIDSLIDWTvpKNPVYLWTLPIFHANGWSypWG 246
Cdd:PRK06187 152 LAAASDTFDFPDID-ENDAAAMLYTSGTTGHPKGVVLSHRNLFlhSLAVCAWLKLS--RDDVYLVIVPMFHVHAWG--LP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 247 IAAV--GGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNE--FQPLNRPVNILTAGAPPPAAVLLRAES--- 319
Cdd:PRK06187 227 YLALmaGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRayFVDFSSLRLVIYGGAALPPALLREFKEkfg 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 320 IGFVisHGYGLTETAGLnVSCAwkpqwnRLPASDRARLKARqgvRTVG----FTEIDVVDPEsGRSVERNGETVGEIVMR 395
Cdd:PRK06187 307 IDLV--QGYGMTETSPV-VSVL------PPEDQLPGQWTKR---RSAGrplpGVEARIVDDD-GDELPPDGGEVGEIIVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 396 GSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPD 475
Cdd:PRK06187 374 GPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPD 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9759119 476 VFWGETPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK06187 454 EKWGERPVAVVVLKPG--ATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
13-539 |
3.14e-137 |
|
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: 407.59 E-value: 3.14e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 13 PLTPIGFLERAATVYGDCTsivYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAIL 92
Cdd:cd05915 1 LERAAALFGRKEVVSRLHT---GE-VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 93 NNINTRLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMT--TDPPilvfiadkeeeggdadvADRTKFSyTYDDLIH 170
Cdd:cd05915 77 HTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKtvQHFV-----------------VMDEKAP-EGYLAYE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 171 RGDLDFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFV--MSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIA 248
Cdd:cd05915 139 EALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLhsLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAAT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 249 AVGGTNVCLRK-FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRP--VNILTAGAPPPAaVLLRAESIG-FVI 324
Cdd:cd05915 219 LVGAKQVLPGPrLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKtlRRLVVGGSAAPR-SLIARFERMgVEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 325 SHGYGLTETAGLNVSCAWKPQWNRLPASDRARLKARQGVRTvgFTE-IDVVDPESgRSVERNGETVGEIVMRGSSIMLGY 403
Cdd:cd05915 298 RQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPI--PLVrLRVADEEG-RPVPKDGKALGEVQLKGPWITGGY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 404 LKDPVGTE-KALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETP 482
Cdd:cd05915 375 YGNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERP 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 483 CAFVSLKSGLTQrptEVEMIEYCRKKMPKY-MVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05915 455 LAVVVPRGEKPT---PEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
20-534 |
5.56e-136 |
|
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: 401.60 E-value: 5.56e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:cd17631 1 LRRRARRHPDRTALVFG-GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLLFvdvfsvdlaveaismmttdppilvfiadkeeeggdadvadrtkfsytyddlihrgdlDfkwi 179
Cdd:cd17631 80 TPPEVAYILADSGAKVLF---------------------------------------------------------D---- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 180 rpesewDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPW-GIAAVGGTNVCLR 258
Cdd:cd17631 99 ------DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTlPTLLRGGTVVILR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 259 KFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQP--LNRPVNILTAGAPPPAAVLLRAESIGFVISHGYGLTETAGl 336
Cdd:cd17631 173 KFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATtdLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSP- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 337 NVSCawkpqwnrLPASDrARLKARQGVRTVGFTEIDVVDPEsGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEKALKN 416
Cdd:cd17631 252 GVTF--------LSPED-HRRKLGSAGRPVFFVEVRIVDPD-GREVPPG--EVGEIVVRGPHVMAGYWNRPEATAAAFRD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 417 GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRP 496
Cdd:cd17631 320 GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG--AEL 397
|
490 500 510
....*....|....*....|....*....|....*...
gi 9759119 497 TEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMK 534
Cdd:cd17631 398 DEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
19-539 |
5.83e-126 |
|
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: 378.90 E-value: 5.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATVYGDcTSIVY----GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNN 94
Cdd:cd12119 1 LLEHAARLHGD-REIVSrtheGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 95 INTRLDARTVSVLLRHCGSKLLFVDVFSVDLaVEAIsmMTTDPPILVFIADKEEEGGDADVADRTkfsYTYDDLIHRGDL 174
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPL-LEAI--APRLPTVEHVVVMTDDAAMPEPAGVGV---LAYEELLAAESP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 175 DFKWirPE-SEWDPVVLNYTSGTTSAPKGVVHCHRGIFV--MSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWgIAAVG 251
Cdd:cd12119 154 EYDW--PDfDENTAAAICYTSGTTGNPKGVVYSHRSLVLhaMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPY-AAAMV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 252 GTNVCL--RKFDAPLIYRLIRDHGVTHMCGAPVVLNML-----SATNEFQPLNRpvnILTAGAPPPAAVLLRAESIGFVI 324
Cdd:cd12119 231 GAKLVLpgPYLDPASLAELIEREGVTFAAGVPTVWQGLldhleANGRDLSSLRR---VVIGGSAVPRSLIEAFEERGVRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 325 SHGYGLTETAGLNVSCAWKPQWNRLPASDRARLKARQGvRTVGFTEIDVVDPEsGRSVERNGETVGEIVMRGSSIMLGYL 404
Cdd:cd12119 308 IHAWGMTETSPLGTVARPPSEHSNLSEDEQLALRAKQG-RPVPGVELRIVDDD-GRELPWDGKAVGELQVRGPWVTKSYY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 405 KDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCA 484
Cdd:cd12119 386 KNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 485 FVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd12119 466 VVVLKEG--ATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
20-538 |
3.89e-105 |
|
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: 323.75 E-value: 3.89e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:cd05936 5 LEEAARRFPDKTALIFM-GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLLFVDVfsvdlaveaismmttdppilvfiadkeeeggdadvadrtkfsyTYDDLIHRGDLDFKWI 179
Cdd:cd05936 84 TPRELEHILNDSGAKALIVAV-------------------------------------------SFTDLLAAGAPLGERV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 180 RPESEwDPVVLNYTSGTTSAPKGVVHCHRGIF--VMSIDSLIDWTVPKNPVYLWTLPIFHANGWS----YPWgiaAVGGT 253
Cdd:cd05936 121 ALTPE-DVAVLQYTSGTTGVPKGAMLTHRNLVanALQIKAWLEDLLEGDDVVLAALPLFHVFGLTvallLPL---ALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 254 NVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPV--NILTAGAPPPAAVLLRAESI-GFVISHGYGL 330
Cdd:cd05936 197 IVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSlrLCISGGAPLPVEVAERFEELtGVPIVEGYGL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 331 TETAglNVSCAwkpqwNRLPASDRARlkarqgvrTVGF----TEIDVVDPEsGRSVERnGEtVGEIVMRGSSIMLGYLKD 406
Cdd:cd05936 277 TETS--PVVAV-----NPLDGPRKPG--------SIGIplpgTEVKIVDDD-GEELPP-GE-VGELWVRGPQVMKGYWNR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 407 PVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFV 486
Cdd:cd05936 339 PEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFV 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 9759119 487 SLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05936 419 VLKEG--ASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
20-446 |
1.71e-103 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 317.72 E-value: 1.71e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLLFVDVFSVDLAVEAismmttdppilvfIADKEEEGGDADVADRTKFSyTYDDLIHRGDLDFKWI 179
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLE-------------ALGKLEVVKLVLVLDRDPVL-KEEPLPEEAKPADVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 180 RPE---SEWDPVVLNYTSGTTSAPKGVVHCHRGI----FVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSY-PWGIAAVG 251
Cdd:pfam00501 147 PPPpppDPDDLAYIIYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 252 GTNVCLRKF---DAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRP--VNILTAGAPPPAAVLLRAESI-GFVIS 325
Cdd:pfam00501 227 ATVVLPPGFpalDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSslRLVLSGGAPLPPELARRFRELfGGALV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 326 HGYGLTETAGlnVSCawkpqwNRLPASDRARLKARQGvRTVGFTEIDVVDPESGRSVERNgeTVGEIVMRGSSIMLGYLK 405
Cdd:pfam00501 307 NGYGLTETTG--VVT------TPLPLDEDLRSLGSVG-RPLPGTEVKIVDDETGEPVPPG--EPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 9759119 406 DPVGTEKALKN-GWFYTGDVGVIHSDGYLEIKDRSKDIIITG 446
Cdd:pfam00501 376 DPELTAEAFDEdGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
186-533 |
1.26e-102 |
|
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: 312.68 E-value: 1.26e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLI 265
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 266 YRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRP--VNILTAGAPPPAAVLLRAESI-GFVISHGYGLTETAGLnVSCAW 342
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSslRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGT-VATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 343 KPQWNRLPASdrarlkarQGvRTVGFTEIDVVDPESGrsvERNGETVGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTG 422
Cdd:cd04433 160 PDDDARKPGS--------VG-RPVPGVEVRIVDPDGG---ELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 423 DVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEVEMI 502
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG--ADLDAEELR 305
|
330 340 350
....*....|....*....|....*....|.
gi 9759119 503 EYCRKKMPKYMVPKTVSFVDELPKTSTGKVM 533
Cdd:cd04433 306 AHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
18-546 |
3.06e-99 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 310.33 E-value: 3.06e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 18 GFLERAATVYGDCTSIVYGSnTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINT 97
Cdd:PRK08316 15 DILRRSARRYPDKTALVFGD-RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 98 RLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTTDPPILVFIADKEE-EGGDADVadrtkfsytyDDLIHRGDLDF 176
Cdd:PRK08316 94 MLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREaPGGWLDF----------ADWAEAGSVAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 177 KWIRPESEwDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANG---WSYPWgiAAVGGT 253
Cdd:PRK08316 164 PDVELADD-DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQldvFLGPY--LYVGAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 254 NVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPlnRPVNILTAG----APPPAAVL--LRAESIGFVISHG 327
Cdd:PRK08316 241 NVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDT--RDLSSLRKGyygaSIMPVEVLkeLRERLPGLRFYNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 328 YGLTETAGLnvSCAWKPQwnrlpasDRARLKARQGvRTVGFTEIDVVDpESGRSVERnGEtVGEIVMRGSSIMLGYLKDP 407
Cdd:PRK08316 319 YGQTEIAPL--ATVLGPE-------EHLRRPGSAG-RPVLNVETRVVD-DDGNDVAP-GE-VGEIVHRSPQLMLGYWDDP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 408 VGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVS 487
Cdd:PRK08316 386 EKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 9759119 488 LKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKKMGT 546
Cdd:PRK08316 466 PKAG--ATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGAFT 522
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
10-539 |
4.59e-97 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 304.13 E-value: 4.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 10 NSPPLTPIGFLERAATVYGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSG 89
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRL-TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 90 AILNNINTRLDARTVSVLLRHCGSKLLFVdvfsVDLAVEAISMMTTDPPILVFIADKEEEGGDADVADRTkfsyTYDDLI 169
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFV----LGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMK----TFTDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 170 HRGDLDFKW--IRPEsewDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWgI 247
Cdd:PRK07656 152 AAGDPAERApeVDPD---DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGV-N 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 248 AAV--GGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNML-----SATNEFQPLNRPVnilTAGAPPPAAVLLRAES- 319
Cdd:PRK07656 228 APLmrGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLlqhpdRSAEDLSSLRLAV---TGAASMPVALLERFESe 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 320 IGF-VISHGYGLTETAGLNVSCawkpqwnrlPASDRARLKARQGVRTVGFTEIDVVDpESGRSVERnGEtVGEIVMRGSS 398
Cdd:PRK07656 305 LGVdIVLTGYGLSEASGVTTFN---------RLDDDRKTVAGTIGTAIAGVENKIVN-ELGEEVPV-GE-VGELLVRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 399 IMLGYLKDPVGTEKALKN-GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVF 477
Cdd:PRK07656 373 VMKGYYDDPEATAAAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9759119 478 WGETPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK07656 453 LGEVGKAYVVLKPG--AELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
41-538 |
6.03e-84 |
|
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: 267.24 E-value: 6.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDv 120
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 fsvdlaveaismmttdppilvfiadkeeeggdadvadrtkfsytyddlihrgdldfkwirpesewdPVVLNYTSGTTSAP 200
Cdd:cd05934 83 ------------------------------------------------------------------PASILYTSGTTGPP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 201 KGVVHCHRgIFVMSIDSLIDWT-VPKNPVYLWTLPIFHANGWSYPWGIA-AVGGTNVCLRKFDAPLIYRLIRDHGVTHMC 278
Cdd:cd05934 97 KGVVITHA-NLTFAGYYSARRFgLGEDDVYLTVLPLFHINAQAVSVLAAlSVGATLVLLPRFSASRFWSDVRRYGATVTN 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 279 GAPVVLNMLSATNEF-QPLNRPVNiLTAGAPPPAAVLLRAES-IGFVISHGYGLTETAGlnVSCAWKPQWNRLPASDRAR 356
Cdd:cd05934 176 YLGAMLSYLLAQPPSpDDRAHRLR-AAYGAPNPPELHEEFEErFGVRLLEGYGMTETIV--GVIGPRDEPRRPGSIGRPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 357 lkarQGVrtvgftEIDVVDPEsGRSVERNgeTVGEIVMR---GSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYL 433
Cdd:cd05934 253 ----PGY------EVRIVDDD-GQELPAG--EPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 434 EIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYM 513
Cdd:cd05934 320 YFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG--ETLDPEELFAFCEGQLAYFK 397
|
490 500
....*....|....*....|....*
gi 9759119 514 VPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05934 398 VPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
11-542 |
8.07e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 262.72 E-value: 8.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 11 SPPLTPIGFLERAATVYGDcTSIVygSNTV------YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFA 84
Cdd:PRK07008 7 DMPLLISSLIAHAARHAGD-TEIV--SRRVegdihrYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 85 VPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDVFSVDLaVEAISMMTtdPPILVFIAdkeeeGGDAD--VADRTKFS 162
Cdd:PRK07008 84 VSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTFLPL-VDALAPQC--PNVKGWVA-----MTDAAhlPAGSTPLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 163 yTYDDLIHRGDLDFKWIRPEsEWDPVVLNYTSGTTSAPKGVVHCHRGIF----------VMSIdSLIDWTVPknpvylwT 232
Cdd:PRK07008 156 -CYETLVGAQDGDYDWPRFD-ENQASSLCYTSGTTGNPKGALYSHRSTVlhaygaalpdAMGL-SARDAVLP-------V 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 233 LPIFHANGWSYPWGIAAVGGTNVCL-RKFDAPLIYRLIRDHGVTHMCGAPVVLNML-----SATNEFQPLNRPVniLTAG 306
Cdd:PRK07008 226 VPMFHVNAWGLPYSAPLTGAKLVLPgPDLDGKSLYELIEAERVTFSAGVPTVWLGLlnhmrEAGLRFSTLRRTV--IGGS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 307 APPPAAVLLRAESIGFVISHGYGLTETAGLNVSCAWKPQWNRLPASDRARLKARQGvRTVGFTEIDVVDPEsGRSVERNG 386
Cdd:PRK07008 304 ACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQLPLDEQRKLLEKQG-RVIYGVDMKIVGDD-GRELPWDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 387 ETVGEIVMRGSSIMLGYLKdpvGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVN 466
Cdd:PRK07008 382 KAFGDLQVRGPWVIDRYFR---GDASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVA 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 467 EVAVVARPDVFWGETPCAFVSLKSGLtqRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAK 542
Cdd:PRK07008 459 EAACIACAHPKWDERPLLVVVKRPGA--EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR 532
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
37-533 |
8.74e-81 |
|
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: 260.99 E-value: 8.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 37 SNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLL 116
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 117 FVDVFSVDLAVEAISMMTTDPPILVFiADKEEEGGDADVADRTKFSYTYDDLihrgdldfKWIRPESEWDPVVLNYTSGT 196
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPKDKIIVL-DDKPDGVLSIEDLLSPTLGEEDEDL--------PPPLKDGKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 197 TSAPKGVVHCHRGIF--VMSIDSLIDWTVPKNPVYLWTLPIFHANGwsYPWGIAAV--GGTNVCLRKFDAPLIYRLIRDH 272
Cdd:cd05911 158 TGLPKGVCLSHRNLIanLSQVQTFLYGNDGSNDVILGFLPLYHIYG--LFTTLASLlnGATVIIMPKFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 273 GVTHMCGAPVVLNMLSATNEFQP--LNRPVNILTAGAPPPAAV--LLRAESIGFVISHGYGLTETAGLnvsCAWKPQWNR 348
Cdd:cd05911 236 KITFLYLVPPIAAALAKSPLLDKydLSSLRVILSGGAPLSKELqeLLAKRFPNATIKQGYGMTETGGI---LTVNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 349 LPASdrarlkarqgvrtVG----FTEIDVVDPESGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFYTGD 423
Cdd:cd05911 313 KPGS-------------VGrllpNVEAKIVDDDGKDSLGPN--EPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 424 VGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEVEMIE 503
Cdd:cd05911 378 IGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG--EKLTEKEVKD 455
|
490 500 510
....*....|....*....|....*....|....
gi 9759119 504 YCRKKMPKYmvpK----TVSFVDELPKTSTGKVM 533
Cdd:cd05911 456 YVAKKVASY---KqlrgGVVFVDEIPKSASGKIL 486
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
40-539 |
4.98e-80 |
|
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: 257.69 E-value: 4.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 40 VYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFV- 118
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 119 DVFSvdlaveaismmTTDPpilvfiadkEEEGGDadvadrtkfsytyddlihrgdldfkwirpesewdPVVLNYTSGTTS 198
Cdd:cd05903 81 ERFR-----------QFDP---------AAMPDA----------------------------------VALLLFTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 199 APKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCL-RKFDAPLIYRLIRDHGVTHM 277
Cdd:cd05903 107 EPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLqDIWDPDKALALMREHGVTFM 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 278 CGAPVVLNMLSATNEFQ--PLNRPVNILTAGAPPPAAVLLRA-ESIGFVISHGYGLTETAGLNVSCAWKPQWNRLPASDR 354
Cdd:cd05903 187 MGATPFLTDLLNAVEEAgePLSRLRTFVCGGATVPRSLARRAaELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 355 ARLkarqGVrtvgftEIDVVDpESGRSVERNGEtvGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLE 434
Cdd:cd05903 267 PLP----GV------EIKVVD-DTGATLAPGVE--GELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLR 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 435 IKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEVEMIEYC-RKKMPKYM 513
Cdd:cd05903 334 ITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG--ALLTFDELVAYLdRQGVAKQY 411
|
490 500
....*....|....*....|....*.
gi 9759119 514 VPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05903 412 WPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
13-539 |
6.34e-80 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 260.45 E-value: 6.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 13 PLTPIGFLERAATVYGD---CTSIVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSG 89
Cdd:PRK06018 9 PLLCHRIIDHAARIHGNrevVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 90 AILNNINTRLDARTVSVLLRHCGSKLLFVDvfsvdlaveaismmTTDPPILVFIADKEEEG------GDADVADRTKF-- 161
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIINHAEDRVVITD--------------LTFVPILEKIADKLPSVeryvvlTDAAHMPQTTLkn 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 162 SYTYDDLIHRGDLDFKWiRPESEWDPVVLNYTSGTTSAPKGVVHCHRG-----IFVMSIDSLidWTVPKNPVyLWTLPIF 236
Cdd:PRK06018 155 AVAYEEWIAEADGDFAW-KTFDENTAAGMCYTSGTTGDPKGVLYSHRSnvlhaLMANNGDAL--GTSAADTM-LPVVPLF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 237 HANGWsypwGIAAVG---GTNVCL--RKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPV--NILTAGAPP 309
Cdd:PRK06018 231 HANSW----GIAFSApsmGTKLVMpgAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHlkMVVCGGSAM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 310 PAAVLLRAESIGFVISHGYGLTETAGLNVSCAWKPQWNRLPASDRARLKARQGVRTVGfTEIDVVDPEsGRSVERNGETV 389
Cdd:PRK06018 307 PRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAALKPPFSKLPGDARLDVLQKQGYPPFG-VEMKITDDA-GKELPWDGKTF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 390 GEIVMRGSSIMLGYLKdpVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVA 469
Cdd:PRK06018 385 GRLKVRGPAVAAAYYR--VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAA 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 470 VVARPDVFWGETPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK06018 463 VIGVYHPKWDERPLLIVQLKPG--ETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
19-550 |
7.82e-79 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 258.12 E-value: 7.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATVYGDCTSIVY----GSNTVYTWREtnLRCL--RVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAIL 92
Cdd:COG0365 14 CLDRHAEGRGDKVALIWegedGEERTLTYAE--LRREvnRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 93 NNINTRLDARTVSVLLRHCGSKLLFVD---------VFSVDLAVEAISMMTTDPPILVFiadkEEEGGDADVADrtkfSY 163
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITAdgglrggkvIDLKEKVDEALEELPSLEHVIVV----GRTGADVPMEG----DL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 164 TYDDLIHR--GDLDFKWIRPEsewDPVVLNYTSGTTSAPKGVVHCHRGIFV---MSIDSLIDWTvpKNPVYLWTLPIFHA 238
Cdd:COG0365 164 DWDELLAAasAEFEPEPTDAD---DPLFILYTSGTTGKPKGVVHTHGGYLVhaaTTAKYVLDLK--PGDVFWCTADIGWA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 239 NGWSY----PWgiaAVGGTNVCLRK----FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVN----ILTAG 306
Cdd:COG0365 239 TGHSYivygPL---LNGATVVLYEGrpdfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSslrlLGSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 307 APPPAAVLLRA-ESIGFVISHGYGLTETAGLNVSCAWK-PQWnrlPASdrarlkarQGVRTVGFtEIDVVDPEsGRSVER 384
Cdd:COG0365 316 EPLNPEVWEWWyEAVGVPIVDGWGQTETGGIFISNLPGlPVK---PGS--------MGKPVPGY-DVAVVDED-GNPVPP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 385 NgeTVGEIVMRGS--SIMLGYLKDPVGTEKALKN---GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVL 459
Cdd:COG0365 383 G--EEGELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESAL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 460 YTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTqrPTEV---EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFV 536
Cdd:COG0365 461 VSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVE--PSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRL 538
|
570
....*....|....
gi 9759119 537 LREIAKKMGTTRLS 550
Cdd:COG0365 539 LRKIAEGRPLGDTS 552
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
9-544 |
2.68e-76 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 251.27 E-value: 2.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 9 ANSPPLT--PIG-FLERAATVYGDCTSIVY-GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFA 84
Cdd:PRK08315 8 PTDVPLLeqTIGqLLDRTAARYPDREALVYrDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 85 VPMSGAILNNINTRLDARTVSVLLRHCGSKLLF-VDVFS----VDLAVEAISMMTTDPP------------ILVFIADKE 147
Cdd:PRK08315 88 TAKIGAILVTINPAYRLSELEYALNQSGCKALIaADGFKdsdyVAMLYELAPELATCEPgqlqsarlpelrRVIFLGDEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 148 EEGGD--ADVADRTKfSYTYDDLIHRGD-LDFkwirpeseWDPVVLNYTSGTTSAPKGVVHCHRGI-----FV-MSI--- 215
Cdd:PRK08315 168 HPGMLnfDELLALGR-AVDDAELAARQAtLDP--------DDPINIQYTSGTTGFPKGATLTHRNIlnngyFIgEAMklt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 216 --DSL-IdwtvpknPVylwtlPIFH------ANgwsypwgIAAV--GGTNVC-LRKFDAPLIYRLIRDHGVTHMCGAPvv 283
Cdd:PRK08315 239 eeDRLcI-------PV-----PLYHcfgmvlGN-------LACVthGATMVYpGEGFDPLATLAAVEEERCTALYGVP-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 284 lNMLSATnefqpLNRP-----------VNILtAGAPPPAAVLLRaesigfVIS--H------GYGLTETAglnvscawkp 344
Cdd:PRK08315 298 -TMFIAE-----LDHPdfarfdlsslrTGIM-AGSPCPIEVMKR------VIDkmHmsevtiAYGMTETS---------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 345 qwnrlPASDRAR----LKARqgVRTVG----FTEIDVVDPESGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEKAL-K 415
Cdd:PRK08315 355 -----PVSTQTRtddpLEKR--VTTVGralpHLEVKIVDPETGETVPRG--EQGELCTRGYSVMKGYWNDPEKTAEAIdA 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 416 NGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQR 495
Cdd:PRK08315 426 DGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPG--AT 503
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 9759119 496 PTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKKM 544
Cdd:PRK08315 504 LTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
19-544 |
1.20e-75 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 247.85 E-value: 1.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATVYGDCTSIVyGSNTVYTWRETNLRCLRVASSL-SSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINT 97
Cdd:PRK06839 7 WIEKRAYLHPDRIAII-TEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 98 RLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTTDPPILVfiadkeeeGGDADVADRTkfsytyddlihRGDLDfk 177
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISI--------TSLKEIEDRK-----------IDNFV-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 178 wirPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSL--IDWTVPKNPVYLwtLPIFHANG---WSYPWGIAavGG 252
Cdd:PRK06839 145 ---EKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTfaIDLTMHDRSIVL--LPLFHIGGiglFAFPTLFA--GG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 253 TNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLN-RPVNIL-TAGAPPPAAVLLRAESIGFVISHGYGL 330
Cdd:PRK06839 218 VIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNlQSVRWFyNGGAPCPEELMREFIDRGFLFGQGFGM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 331 TETAglnvscawkPQWNRLpASDRARLKARQGVRTVGFTEIDVVDPESGRsVERNGetVGEIVMRGSSIMLGYLKDPVGT 410
Cdd:PRK06839 298 TETS---------PTVFML-SEEDARRKVGSIGKPVLFCDYELIDENKNK-VEVGE--VGELLIRGPNVMKEYWNRPDAT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 411 EKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKS 490
Cdd:PRK06839 365 EETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 9759119 491 GLTQrpTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKKM 544
Cdd:PRK06839 445 SSVL--IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKSR 496
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
41-539 |
4.90e-75 |
|
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: 243.79 E-value: 4.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRhcgskllfvdv 120
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 fsvdlaveaismmttdppilvfiadkeeeggDADVAdrtkfsytYDDLihrgdldfkwirpesewdpVVLNYTSGTTSAP 200
Cdd:cd05912 71 -------------------------------DSDVK--------LDDI-------------------ATIMYTSGTTGKP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 201 KGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGA 280
Cdd:cd05912 93 KGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 281 PVVLN-MLSATNEFQPLN-RpvNILTAGAPPPAAVLLRAESIGFVISHGYGLTETAGLNVSCAWKPQWNRLPASDRARLK 358
Cdd:cd05912 173 PTMLQrLLEILGEGYPNNlR--CILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 359 ArqgvrtvgftEIDVVDPESgrsverNGETVGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDR 438
Cdd:cd05912 251 V----------ELKIEDDGQ------PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDR 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 439 SKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRptevEMIEYCRKKMPKYMVPKTV 518
Cdd:cd05912 315 RSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEE----ELIAYCSEKLAKYKVPKKI 390
|
490 500
....*....|....*....|.
gi 9759119 519 SFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05912 391 YFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
21-539 |
9.32e-74 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 243.25 E-value: 9.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 21 ERAATVYGDcTSIVYGsntvytwrETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLD 100
Cdd:PRK06145 17 DRAALVYRD-QEISYA--------EFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 101 ARTVSVLLRHCGSKLLFVDV-FSVDLAVEAismmttdpPILVFiadkeeegGDADVADRTKFSytyddlihRGDLDFKWI 179
Cdd:PRK06145 88 ADEVAYILGDAGAKLLLVDEeFDAIVALET--------PKIVI--------DAAAQADSRRLA--------QGGLEIPPQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 180 RPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPwGIA--AVGGTNVCL 257
Cdd:PRK06145 144 AAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLP-GIAvlWVGGTLRIH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 RKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEfqPLNRPVNILT---AGAPPPAAVLLRAESIGFVISH---GYGLT 331
Cdd:PRK06145 223 REFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPD--RDRFDLDSLAwciGGGEKTPESRIRDFTRVFTRARyidAYGLT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 332 ETAGlnvscawkpqWNRLPASDRARLKARQGVRTVGFTEIDVVDpESGRSVERNGEtvGEIVMRGSSIMLGYLKDPVGTE 411
Cdd:PRK06145 301 ETCS----------GDTLMEAGREIEKIGSTGRALAHVEIRIAD-GAGRWLPPNMK--GEICMRGPKVTKGYWKDPEKTA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 412 KALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSG 491
Cdd:PRK06145 368 EAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 9759119 492 LTQrpTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK06145 448 ATL--TLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
14-544 |
1.66e-73 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 241.79 E-value: 1.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 14 LTPigflERAATVYGDCTsivygsntvYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILN 93
Cdd:PRK03640 14 LTP----DRTAIEFEEKK---------VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 94 NINTRLDARTVSVLLRHCGSKLLFvdvfsvdlaveaismmtTDPPIlvfiADKEEEGGdadvadrtkfSYTYDDLIhrgD 173
Cdd:PRK03640 81 LLNTRLSREELLWQLDDAEVKCLI-----------------TDDDF----EAKLIPGI----------SVKFAELM---N 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 174 LDFKWIRPESEWDpvvLN------YTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWS----- 242
Cdd:PRK03640 127 GPKEEAEIQEEFD---LDevatimYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSilmrs 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 243 --YpwgiaavGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSAtnEFQPLNRPVN---ILTAGAPPPAAVLLRA 317
Cdd:PRK03640 204 viY-------GMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLE--RLGEGTYPSSfrcMLLGGGPAPKPLLEQC 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 318 ESIGFVISHGYGLTETAGLNVScawkpqwnrLPASDrarlkARQGVRTVG---F-TEIDVVDPEsgrsVERNGETVGEIV 393
Cdd:PRK03640 275 KEKGIPVYQSYGMTETASQIVT---------LSPED-----ALTKLGSAGkplFpCELKIEKDG----VVVPPFEEGEIV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 394 MRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVAR 473
Cdd:PRK03640 337 VKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGV 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9759119 474 PDVFWGETPCAFVSLKSGLtqrpTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKKM 544
Cdd:PRK03640 417 PDDKWGQVPVAFVVKSGEV----TEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
10-534 |
5.92e-73 |
|
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: 240.98 E-value: 5.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 10 NSPPLTPIGFLerAATVYGDCTSIVYGSN-TVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMS 88
Cdd:cd05904 3 TDLPLDSVSFL--FASAHPSRPALIDAATgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 89 GAILNNINTRLDARTVSVLLRHCGSKLlfvdVFSVDLAVEAISmmTTDPPILVFiaDKEEEGGDADVADrtkfsytyDDL 168
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKL----AFTTAELAEKLA--SLALPVVLL--DSAEFDSLSFSDL--------LFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 169 IHRGDLDFKWIRPEsewDPVVLNYTSGTTSAPKGVVHCHRGIFVM--SIDSLIDWTVPKNPVYLWTLPIFHANGWS-YPW 245
Cdd:cd05904 145 ADEAEPPVVVIKQD---DVAALLYSSGTTGRSKGVMLTHRNLIAMvaQFVAGEGSNSDSEDVFLCVLPMFHIYGLSsFAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 246 GIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHM-CGAPVVLNMLSATNEFQ-PLNRPVNILTAGAPPPAAVLLR-AESIGF 322
Cdd:cd05904 222 GLLRLGATVVVMPRFDLEELLAAIERYKVTHLpVVPPIVLALVKSPIVDKyDLSSLRQIMSGAAPLGKELIEAfRAKFPN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 323 V-ISHGYGLTETAGLNVSCAwkpqwnrLPASDRARLKarqgvrTVGF----TEIDVVDPESGRSVERNgeTVGEIVMRGS 397
Cdd:cd05904 302 VdLGQGYGMTESTGVVAMCF-------APEKDRAKYG------SVGRlvpnVEAKIVDPETGESLPPN--QTGELWIRGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 398 SIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDV 476
Cdd:cd05904 367 SIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDE 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 477 FWGETPCAFVSLKSGLTQrpTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMK 534
Cdd:cd05904 447 EAGEVPMAFVVRKPGSSL--TEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILR 502
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
33-539 |
1.24e-72 |
|
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: 239.91 E-value: 1.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 33 IVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCG 112
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 113 SKLLFVDVFSVDLAVEAISMMTtdppilVFIADKEEEGGDADVADRTKfSYTYDDLIHRGDLDFKWIRPEsewDPVVLNY 192
Cdd:cd05926 87 SKLVLTPKGELGPASRAASKLG------LAILELALDVGVLIRAPSAE-SLSNLLADKKNAKSEGVPLPD---DLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 193 TSGTTSAPKGVVHCHRGIfVMSIDSLIdwTV----PKNPVYLwTLPIFHANGWsypwgIAAV------GGTNVCLRKFDA 262
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNL-AASATNIT--NTykltPDDRTLV-VMPLFHVHGL-----VASLlstlaaGGSVVLPPRFSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 263 PLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVN---ILTAGAPPPAAVLLRAE-SIGFVISHGYGLTETAGLNV 338
Cdd:cd05926 228 STFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKlrfIRSCSASLPPAVLEALEaTFGAPVLEAYGMTEAAHQMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 339 ScawkpqwNRLPASDRarlkaRQGvrTVGF---TEIDVVDpESGRSVErNGEtVGEIVMRGSSIMLGYLKDPVGT-EKAL 414
Cdd:cd05926 308 S-------NPLPPGPR-----KPG--SVGKpvgVEVRILD-EDGEILP-PGV-VGEICLRGPNVTRGYLNNPEANaEAAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 415 KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQ 494
Cdd:cd05926 371 KDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREG--A 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 9759119 495 RPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05926 449 SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
36-543 |
4.96e-72 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 239.96 E-value: 4.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 36 GSNTVYTWREtnLRCL--RVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGS 113
Cdd:PRK13295 51 GAPRRFTYRE--LAALvdRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 114 KLLFV-DVF-SVDLAveaiSMMTTDPPIL-----VFIADKEEEGGDADVADRTKFSYTYDDLI----HRGDLDfkwirpe 182
Cdd:PRK13295 129 KVLVVpKTFrGFDHA----AMARRLRPELpalrhVVVVGGDGADSFEALLITPAWEQEPDAPAilarLRPGPD------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 183 sewDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYpwGIA---AVGGTNVCLRK 259
Cdd:PRK13295 198 ---DVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMY--GLMmpvMLGATAVLQDI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 260 FDAPLIYRLIRDHGVTH-MCGAPVVLNMLSATNEfqpLNRPVNILT----AGAPPPAAVLLRA-ESIGFVISHGYGLTET 333
Cdd:PRK13295 273 WDPARAAELIRTEGVTFtMASTPFLTDLTRAVKE---SGRPVSSLRtflcAGAPIPGALVERArAALGAKIVSAWGMTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 334 AGLNVSCawkpqwnrlPASDRARLKARQGVRTVGfTEIDVVDPEsGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEKA 413
Cdd:PRK13295 350 GAVTLTK---------LDDPDERASTTDGCPLPG-VEVRVVDAD-GAPLPAG--QIGRLQVRGCSNFGGYLKRPQLNGTD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 414 lKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGlt 493
Cdd:PRK13295 417 -ADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-- 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 494 QRPTEVEMIEYCR-KKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKK 543
Cdd:PRK13295 494 QSLDFEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
18-540 |
1.21e-70 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 236.19 E-value: 1.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 18 GFLERAATVYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINT 97
Cdd:PRK06155 25 AMLARQAERYPDRPLLVFG-GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 98 RLDARTVSVLLRHCGSKLLFVDVFSVDlAVEAISMMTTDPPILVFIadkeeeggDADVADRTKFSYTYDDLIHRGD-LDF 176
Cdd:PRK06155 104 ALRGPQLEHILRNSGARLLVVEAALLA-ALEAADPGDLPLPAVWLL--------DAPASVSVPAGWSTAPLPPLDApAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 177 KWIRPEsewDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVC 256
Cdd:PRK06155 175 AAVQPG---DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 257 LRKFDAPLIYRLIRDHG--VTHMCGApvVLNMLSATNEfQPLNR--PVNILTAGAPPPAAVLLRAESIGFVISHGYGLTE 332
Cdd:PRK06155 252 EPRFSASGFWPAVRRHGatVTYLLGA--MVSILLSQPA-RESDRahRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 TaglNVSCAWKPQWNRLPASDRARlkarqgvrtVGFtEIDVVDpESGRSVErNGEtVGEIVMRGS---SIMLGYLKDPVG 409
Cdd:PRK06155 329 T---NFVIAVTHGSQRPGSMGRLA---------PGF-EARVVD-EHDQELP-DGE-PGELLLRADepfAFATGYFGMPEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 410 TEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLK 489
Cdd:PRK06155 393 TVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLR 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 490 SGLTQRPteVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREI 540
Cdd:PRK06155 473 DGTALEP--VALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
11-539 |
6.58e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 234.08 E-value: 6.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 11 SPPLTPIGF-LERAATVYGDCTSIV-YGsnTVYTWRETNLRCLRVASSLSS-IGIGRSDVVSVLSPNTPAMYELQFAVPM 87
Cdd:PRK08314 6 TLPETSLFHnLEVSARRYPDKTAIVfYG--RAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 88 SGAILNNINTRLDARTVSVLLRHCGSKLLFVdvfSVDLAVE------------AISMMTTD----------PPILVFIAD 145
Cdd:PRK08314 84 ANAVVVPVNPMNREEELAHYVTDSGARVAIV---GSELAPKvapavgnlrlrhVIVAQYSDylpaepeiavPAWLRAEPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 146 KEEEGGDADVADRTKFSYTYDDLIHRGDLDfkwirpesewDPVVLNYTSGTTSAPKGVVHCHRGIFVmSIDSLIDW-TVP 224
Cdd:PRK08314 161 LQALAPGGVVAWKEALAAGLAPPPHTAGPD----------DLAVLPYTSGTTGVPKGCMHTHRTVMA-NAVGSVLWsNST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 225 KNPVYLWTLPIFHANGWSYpwGIAA---VGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQP--LNRP 299
Cdd:PRK08314 230 PESVVLAVLPLFHVTGMVH--SMNApiyAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAErdLSSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 300 VNILTAGAPPPAAV---LLRAESIGFVisHGYGLTETAGLNVScawkpqwNrlPAsDRARLKArQGVRTVGfTEIDVVDP 376
Cdd:PRK08314 308 RYIGGGGAAMPEAVaerLKELTGLDYV--EGYGLTETMAQTHS-------N--PP-DRPKLQC-LGIPTFG-VDARVIDP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 377 ESGRSVERNGetVGEIVMRGSSIMLGYLKDPVGTEKAL--KNG--WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSS 452
Cdd:PRK08314 374 ETLEELPPGE--VGEIVVHGPQVFKGYWNRPEATAEAFieIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 453 VEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK08314 452 AEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
....*..
gi 9759119 533 MKFVLRE 539
Cdd:PRK08314 532 LWRQLQE 538
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
42-534 |
2.53e-69 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 229.64 E-value: 2.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFvdvf 121
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 122 svdlaveaismmtTDPPIlvfiadkEEEGGDADVADRTKFSYTYD-DLIHRGDLDfkwirpesewDPVVLNYTSGTTSAP 200
Cdd:TIGR01923 77 -------------TDSLL-------EEKDFQADSLDRIEAAGRYEtSLSASFNMD----------QIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 201 KGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAplIYRLIRDHGVTHMCGA 280
Cdd:TIGR01923 127 KAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 281 PVVLN-MLSATNEFQPLNRpvnILTAGAPPPAAVLLRAESIGFVISHGYGLTETAglNVSCAWKPQWnrlpasdrarLKA 359
Cdd:TIGR01923 205 PTQLNrLLDEGGHNENLRK---ILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETC--SQVTTATPEM----------LHA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 360 RqgvrtvgfteIDVVDPESGRSVE---RNGETVGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIK 436
Cdd:TIGR01923 270 R----------PDVGRPLAGREIKikvDNKEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 437 DRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQrpteVEMIEYCRKKMPKYMVPK 516
Cdd:TIGR01923 340 GRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQ----AKLIAYLTEKLAKYKVPI 415
|
490
....*....|....*...
gi 9759119 517 TVSFVDELPKTSTGKVMK 534
Cdd:TIGR01923 416 AFEKLDELPYNASGKILR 433
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
41-541 |
7.62e-68 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 228.89 E-value: 7.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLF-VD 119
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIcAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 120 VFS----VDLAVEAI-SMMTTDPPIL----------VFIADKEEEGGdadvadrtkfSYTYDDLIHRGDLdfkwIRPE-- 182
Cdd:PRK12583 126 AFKtsdyHAMLQELLpGLAEGQPGALacerlpelrgVVSLAPAPPPG----------FLAWHELQARGET----VSREal 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 183 -------SEWDPVVLNYTSGTTSAPKGVVHCHRGI-----FVMSIDSLIDWTVPKNPVylwtlPIFHANGWSYP-WGIAA 249
Cdd:PRK12583 192 aerqaslDRDDPINIQYTSGTTGFPKGATLSHHNIlnngyFVAESLGLTEHDRLCVPV-----PLYHCFGMVLAnLGCMT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 250 VGGTNVC-LRKFDAPLIYRLIRDHGVTHMCGAPVvlnMLSAT------NEFQPLNRPVNILtAGAPPPAAVLLR--AESI 320
Cdd:PRK12583 267 VGACLVYpNEAFDPLATLQAVEEERCTALYGVPT---MFIAEldhpqrGNFDLSSLRTGIM-AGAPCPIEVMRRvmDEMH 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 321 GFVISHGYGLTETAGLNVSCAwkpqwnrlPASDrarLKARqgVRTVGFT----EIDVVDPEsGRSVERnGEtVGEIVMRG 396
Cdd:PRK12583 343 MAEVQIAYGMTETSPVSLQTT--------AADD---LERR--VETVGRTqphlEVKVVDPD-GATVPR-GE-IGELCTRG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 397 SSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPD 475
Cdd:PRK12583 407 YSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPD 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 476 VFWGETPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIA 541
Cdd:PRK12583 487 EKYGEEIVAWVRLHPG--HAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
22-539 |
1.50e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 222.17 E-value: 1.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 22 RAATVYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAI---LNNINTR 98
Cdd:PRK06188 20 SALKRYPDRPALVLG-DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRrtaLHPLGSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 99 LDARTVsvlLRHCGSKLLFVD-VFSVDLAVEAISMMTTDPPILVFiadkeeegGDADVADrtkfsytydDLIHRGD-LDF 176
Cdd:PRK06188 99 DDHAYV---LEDAGISTLIVDpAPFVERALALLARVPSLKHVLTL--------GPVPDGV---------DLLAAAAkFGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 177 KWIRPESEW-DPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANG-WSYPwgIAAVGGTN 254
Cdd:PRK06188 159 APLVAAALPpDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGaFFLP--TLLRGGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 255 VCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNML-----SATNEFQPLNrpvnILTAGAPPPAAVLLRA--ESIGFVISHG 327
Cdd:PRK06188 237 IVLAKFDPAEVLRAIEEQRITATFLVPTMIYALldhpdLRTRDLSSLE----TVYYGASPMSPVRLAEaiERFGPIFAQY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 328 YGLTEtAGLNVSCAWKPQWNRlpasDRARLKARQGvRTVGFTEIDVVDPEsGRSVERnGEtVGEIVMRGSSIMLGYLKDP 407
Cdd:PRK06188 313 YGQTE-APMVITYLRKRDHDP----DDPKRLTSCG-RPTPGLRVALLDED-GREVAQ-GE-VGEICVRGPLVMDGYWNRP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 408 VGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVS 487
Cdd:PRK06188 384 EETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 9759119 488 LKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK06188 464 LRPG--AAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
186-539 |
9.18e-65 |
|
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: 217.54 E-value: 9.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIFVMsIDSLID-WTVPKNPVYLWTLPIFHANGWSYpwGIAA---VGGTNVCLRKFD 261
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAAN-VRALVDaWRWTEDDVLLHVLPLHHVHGLVN--ALLCplfAGASVEFLPKFD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 262 APLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLN---------RPVNILTAG-APPPAAVLLRAESI-GFVISHGYGL 330
Cdd:cd05941 167 PKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDpqfaraaaaERLRLMVSGsAALPVPTLEEWEAItGHTLLERYGM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 331 TETaGLNVSCawkpqwnrlpasdraRLKARQGVRTVGF----TEIDVVDPESGRSVerNGETVGEIVMRGSSIMLGYLKD 406
Cdd:cd05941 247 TEI-GMALSN---------------PLDGERRPGTVGMplpgVQARIVDEETGEPL--PRGEVGEIQVRGPSVFKEYWNK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 407 PVGTEKALK-NGWFYTGDVGVIHSDGYLEIKDRSK-DIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCA 484
Cdd:cd05941 309 PEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVA 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 485 FVSLKSGLTQrPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05941 389 VVVLRAGAAA-LSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
2-541 |
1.62e-64 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 221.75 E-value: 1.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 2 EQMkPCAANSPPLTPIGFLERAATVYGDCTSIVYGSNT-------VYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPN 74
Cdd:PRK07529 14 EAV-PLAARDLPASTYELLSRAAARHPDAPALSFLLDAdpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 75 TPamyELQFAV--PMSGAILNNINTRLDARTVSVLLRHCGSKLL-----FVDVFSVDLAVEAISMMTTDPPILV------ 141
Cdd:PRK07529 93 LP---ETHFALwgGEAAGIANPINPLLEPEQIAELLRAAGAKVLvtlgpFPGTDIWQKVAEVLAALPELRTVVEvdlary 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 142 ------FIADKEEEGGDADVADrtkfsytYDDLIHRGD---LDFKwiRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFV 212
Cdd:PRK07529 170 lpgpkrLAVPLIRRKAHARILD-------FDAELARQPgdrLFSG--RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 213 M--SIDSLIDWTVPKnpVYLWTLPIFHANGwSYPWGIAAV--GGTNVclrkFDAPLIYR----------LIRDHGVTHMC 278
Cdd:PRK07529 241 NawLGALLLGLGPGD--TVFCGLPLFHVNA-LLVTGLAPLarGAHVV----LATPQGYRgpgvianfwkIVERYRINFLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 279 GAPVVLNMLsatnefqpLNRPVN---------ILTAGAPPPAAVLLRAES-IGFVISHGYGLTETAGLnVSCAWkPQWNR 348
Cdd:PRK07529 314 GVPTVYAAL--------LQVPVDghdisslryALCGAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCV-SSVNP-PDGER 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 349 LPASDRARLkARQGVRTVgfteidVVDPESGRSVERNGETVGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIH 428
Cdd:PRK07529 384 RIGSVGLRL-PYQRVRVV------ILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRID 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 429 SDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQrpTEVEMIEYCRKK 508
Cdd:PRK07529 457 ADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASA--TEAELLAFARDH 534
|
570 580 590
....*....|....*....|....*....|....
gi 9759119 509 MP-KYMVPKTVSFVDELPKTSTGKVMKFVLREIA 541
Cdd:PRK07529 535 IAeRAAVPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
5-540 |
8.43e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 218.72 E-value: 8.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 5 KPCAANSPPLTP----------IGFLERAATVYGDCTSI-VYGSNTvyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSP 73
Cdd:PRK05605 13 KPWLQSYAPWTPhdldygdttlVDLYDNAVARFGDRPALdFFGATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 74 NTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFV------------------DVFSVDL--AVEAISMM 133
Cdd:PRK05605 91 NCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVwdkvaptverlrrttpleTIVSVNMiaAMPLLQRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 134 TTDPPILVFIADKEEEGGDADVAdrtkfsYTYDDLIHRGDLDFKWI----RPESEwDPVVLNYTSGTTSAPKGVVHCHRG 209
Cdd:PRK05605 171 ALRLPIPALRKARAALTGPAPGT------VPWETLVDAAIGGDGSDvshpRPTPD-DVALILYTSGTTGKPKGAQLTHRN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 210 IFVMSIDSL--IDWTVPKNPVYLWTLPIFHANGWSYPWGIA-AVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNM 286
Cdd:PRK05605 244 LFANAAQGKawVPGLGDGPERVLAALPMFHAYGLTLCLTLAvSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 287 LSATNEFQ--PLNRPVNILT-AGAPPPAAVLLRAESIGFVISHGYGLTETAGLNVScawkpqwNrlPASDrARlkaRQGV 363
Cdd:PRK05605 324 IAEAAEERgvDLSGVRNAFSgAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVG-------N--PMSD-DR---RPGY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 364 RTVGF--TEIDVVDPESGRSVERNGETvGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKD 441
Cdd:PRK05605 391 VGVPFpdTEVRIVDPEDPDETMPDGEE-GELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 442 IIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPTEVEmiEYCRKKMPKYMVPKTVSFV 521
Cdd:PRK05605 470 LIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLR--AYCREHLTRYKVPRRFYHV 547
|
570
....*....|....*....
gi 9759119 522 DELPKTSTGKVMKfvlREI 540
Cdd:PRK05605 548 DELPRDQLGKVRR---REV 563
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
49-537 |
4.60e-63 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 212.72 E-value: 4.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 49 RCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDVFSVDLAVe 128
Cdd:cd05935 10 VVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSELDDLAL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 129 aismmttdppilvfiadkeeeggdadvadrtkfsytyddlihrgdldfkwirpesewdpvvLNYTSGTTSAPKGVVHCHR 208
Cdd:cd05935 89 -------------------------------------------------------------IPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 209 GIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIA-AVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNML 287
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAvYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 288 SATNEFQP--LNRPVNILTAGAPPPAAV---LLRAESIGFVisHGYGLTETAglnvscawkPQWNRLPAsdrARLKAR-Q 361
Cdd:cd05935 188 LATPEFKTrdLSSLKVLTGGGAPMPPAVaekLLKLTGLRFV--EGYGLTETM---------SQTHTNPP---LRPKLQcL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 362 GVRTVGfTEIDVVDPESGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEKAL--KNG--WFYTGDVGVIHSDGYLEIKD 437
Cdd:cd05935 254 GIP*FG-VDARVIDIETGRELPPN--EVGEIVVRGPQIFKGYWNRPEETEESFieIKGrrFFRTGDLGYMDEEGYFFFVD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 438 RSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPTEVEMIEYCRKKMPKYMVPKT 517
Cdd:cd05935 331 RVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPRE 410
|
490 500
....*....|....*....|
gi 9759119 518 VSFVDELPKTSTGKVMKFVL 537
Cdd:cd05935 411 VEFVDELPRSASGKILWRLL 430
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
186-538 |
2.76e-62 |
|
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: 208.29 E-value: 2.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIF--VMSIDSLIDWTvpKNPVYLWTLPIFHANGwsypwgiaAVGGTNVCLRK---- 259
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGERLGLT--EQDRLCIPVPLFHCFG--------SVLGVLACLTHgatm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 260 ------FDAPLIYRLIRDHGVTHMCGAPvvlNMLSATNEfQPLNRPVNI------LTAGAPPPAAVLLRA-ESIGFV-IS 325
Cdd:cd05917 73 vfpspsFDPLAVLEAIEKEKCTALHGVP---TMFIAELE-HPDFDKFDLsslrtgIMAGAPCPPELMKRViEVMNMKdVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 326 HGYGLTETAglnvscawkpqwnrlPASDRARLKARQGVR--TVG----FTEIDVVDPESGRSVERNgeTVGEIVMRGSSI 399
Cdd:cd05917 149 IAYGMTETS---------------PVSTQTRTDDSIEKRvnTVGrimpHTEAKIVDPEGGIVPPVG--VPGELCIRGYSV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 400 MLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFW 478
Cdd:cd05917 212 MKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERY 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 479 GETPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05917 292 GEEVCAWIRLKEG--AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
20-539 |
6.06e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 212.72 E-value: 6.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTT-TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTTDPPILVFiadkeeeGGDADVAdrtkfSYTYDDLIHRGDLDFKWI 179
Cdd:PRK07786 102 TPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVA-------GGSSDDS-----VLGYEDLLAEAGPAHAPV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 180 R-PESEwdPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKN-PVYLWTLPIFHANGWSYPWGIAAVGGTNVC- 256
Cdd:PRK07786 170 DiPNDS--PALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINsDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIy 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 257 -LRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGAPPPAAVLLRAESIGF---VISHGYGLTE 332
Cdd:PRK07786 248 pLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpeaQILAAFGQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 TAglNVSCAwkpqwnrlpasdrarLKARQGVRTVGFTEiDVVDPESGRSVERN------GEtVGEIVMRGSSIMLGYLKD 406
Cdd:PRK07786 328 MS--PVTCM---------------LLGEDAIRKLGSVG-KVIPTVAARVVDENmndvpvGE-VGEIVYRAPTLMSGYWNN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 407 PVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFV 486
Cdd:PRK07786 389 PEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 9759119 487 SLKSGLTQRPTEvEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK07786 469 AVRNDDAALTLE-DLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
19-539 |
1.17e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 211.82 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATVYGDCTSIVYGSNTvYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTR 98
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 99 LDARTVSVLLRHCGSKLLfvdVFSVDLAVEAISMMTTDPPILVFIADKEEEGGDAdvadrtkfsytYDDLI--HRGDlDF 176
Cdd:PRK07470 91 QTPDEVAYLAEASGARAM---ICHADFPEHAAAVRAASPDLTHVVAIGGARAGLD-----------YEALVarHLGA-RV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 177 KWIRPESEwDPVVLNYTSGTTSAPKGVVHCHRGI-FVMSiDSLIDWT--VPKNPVYLWTLPIFHANGWSYPWGIAAvGGT 253
Cdd:PRK07470 156 ANAAVDHD-DPCWFFFTSGTTGRPKAAVLTHGQMaFVIT-NHLADLMpgTTEQDASLVVAPLSHGAGIHQLCQVAR-GAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 254 NVCL--RKFDAPLIYRLIRDHGVTHMCGAPVVLNML---SATNEFQ--PLNrpvNILTAGAPPPAAVLLRA-ESIGFVIS 325
Cdd:PRK07470 233 TVLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLvehPAVDRYDhsSLR---YVIYAGAPMYRADQKRAlAKLGKVLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 326 HGYGLTETAGlNVSCawkpqwnrLPASDRARLKARQ-GVRTVGF----TEIDVVDPEsGRSVErNGETvGEIVMRGSSIM 400
Cdd:PRK07470 310 QYFGLGEVTG-NITV--------LPPALHDAEDGPDaRIGTCGFertgMEVQIQDDE-GRELP-PGET-GEICVIGPAVF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 401 LGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGE 480
Cdd:PRK07470 378 AGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGE 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 9759119 481 TPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK07470 458 VGVAVCVARDG--APVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
41-538 |
3.70e-61 |
|
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: 207.57 E-value: 3.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAIlnnintrldartvsvllrhcgskllfvdv 120
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAV----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 fsvdlAVEAISMMTTDppilvfiadkeeeggdaDVADRTKfsytyddlihrgDLDFKWIRPESEwDPVVLNYTSGTTSAP 200
Cdd:cd05972 52 -----YVPLTTLLGPK-----------------DIEYRLE------------AAGAKAIVTDAE-DPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 201 KGVVHCHRgIFVMSIDSLIDWTVPKNPVYLWTLPifhANGWSY--------PWgiaAVGGTNVC--LRKFDAPLIYRLIR 270
Cdd:cd05972 97 KGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIA---DPGWAKgawssffgPW---LLGATVFVyeGPRFDAERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 271 DHGVTHMCGAPVVLNMLSA--TNEFQPLnRPVNILTAGAP-PPAAVLLRAESIGFVISHGYGLTETAGLNVSCAWkpqwn 347
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIKqdLSSYKFS-HLRLVVSAGEPlNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPD----- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 348 rlpasdrarLKARQGvrTVGFT----EIDVVDpESGRSVERNgeTVGEIVMRGS--SIMLGYLKDPVGTEKALKNGWFYT 421
Cdd:cd05972 244 ---------MPVKPG--SMGRPtpgyDVAIID-DDGRELPPG--EEGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 422 GDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTqrPTEV-- 499
Cdd:cd05972 310 GDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEEla 387
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 9759119 500 -EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05972 388 eELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-539 |
5.66e-61 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 210.22 E-value: 5.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 9 ANSPPLTPIGFlERAATVYGDCTSIVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMS 88
Cdd:PLN02246 20 PNHLPLHDYCF-ERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 89 GAILNNINTRLDARTVSVLLRHCGSKLL-----FVDVFSVDLAVEAISMMTTDPPI---LVFIADKEEEGGDADVADrtk 160
Cdd:PLN02246 99 GAVTTTANPFYTPAEIAKQAKASGAKLIitqscYVDKLKGLAEDDGVTVVTIDDPPegcLHFSELTQADENELPEVE--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 161 fsytyddlihrgdldfkwIRPEsewDPVVLNYTSGTTSAPKGVVHCHRGIfVMSIDSLIDWTVP-----KNPVYLWTLPI 235
Cdd:PLN02246 176 ------------------ISPD---DVVALPYSSGTTGLPKGVMLTHKGL-VTSVAQQVDGENPnlyfhSDDVILCVLPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 236 FHangwsypwgIAA----------VGGTNVCLRKFDAPLIYRLIRDHGVTHmcgAPVVLNMLSATNEFQPLNR----PVN 301
Cdd:PLN02246 234 FH---------IYSlnsvllcglrVGAAILIMPKFEIGALLELIQRHKVTI---APFVPPIVLAIAKSPVVEKydlsSIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 302 ILTAGAPPPAAVL---LRAESIGFVISHGYGLTEtAG--LNVSCAWKPQwnrlPasdrarLKARQG-----VRTvgfTEI 371
Cdd:PLN02246 302 MVLSGAAPLGKELedaFRAKLPNAVLGQGYGMTE-AGpvLAMCLAFAKE----P------FPVKSGscgtvVRN---AEL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 372 DVVDPESGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENV 450
Cdd:PLN02246 368 KIVDPETGASLPRN--QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 451 SSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLtqRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTG 530
Cdd:PLN02246 446 APAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGS--EITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSG 523
|
....*....
gi 9759119 531 KVMKFVLRE 539
Cdd:PLN02246 524 KILRKDLRA 532
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
19-543 |
1.81e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 209.50 E-value: 1.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATVYGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTR 98
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDI-TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 99 LDARTVSVLLRHCGSK------LLFVDVFSVDLAVEAISMMTTD-------PPILVFIADKEEEGGDADVADRTKFSYTY 165
Cdd:PRK06710 108 YTERELEYQLHDSGAKvilcldLVFPRVTNVQSATKIEHVIVTRiadflpfPKNLLYPFVQKKQSNLVVKVSESETIHLW 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 166 DDLIHRGDLDFKwIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIF---VMSIDSLIDwTVPKNPVYLWTLPIFHANGWS 242
Cdd:PRK06710 188 NSVEKEVNTGVE-VPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVsntLMGVQWLYN-CKEGEEVVLGVLPFFHVYGMT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 243 YPWGIAAVGGTN-VCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATnefqPLNRPVNI------LTAGAPPPAAVLL 315
Cdd:PRK06710 266 AVMNLSIMQGYKmVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNS----PLLKEYDIssiracISGSAPLPVEVQE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 316 RAESI-GFVISHGYGLTETAGLNVS-CAWKpqwNRLPASdrarlkarqgvrtVGF----TEIDVVDPESGRSVeRNGEtV 389
Cdd:PRK06710 342 KFETVtGGKLVEGYGLTESSPVTHSnFLWE---KRVPGS-------------IGVpwpdTEAMIMSLETGEAL-PPGE-I 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 390 GEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVA 469
Cdd:PRK06710 404 GEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9759119 470 VVARPDVFWGETPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKK 543
Cdd:PRK06710 484 TIGVPDPYRGETVKAFVVLKEG--TECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKR 555
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
22-545 |
3.71e-59 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 205.37 E-value: 3.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 22 RAATVYGDCTSIVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDA 101
Cdd:PRK06087 31 QTARAMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 102 RTVSVLLRHCGSKLLFVDVF-----SVDLAVEAISMMTTDPPILVFiaDKEEEGGDADVADR---TKFSYTYDDLIHRGD 173
Cdd:PRK06087 111 AELVWVLNKCQAKMFFAPTLfkqtrPVDLILPLQNQLPQLQQIVGV--DKLAPATSSLSLSQiiaDYEPLTTAITTHGDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 174 LdfkwirpesewdPVVLnYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYpwGIAA---V 250
Cdd:PRK06087 189 L------------AAVL-FTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLH--GVTApflI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 251 GGTNVCLRKFDAPLIYRLIRDHGVTHMCGA-PVVLNMLSATNEfQPLNRPV--NILTAGAPPPAAVLLRAESIGFVISHG 327
Cdd:PRK06087 254 GARSVLLDIFTPDACLALLEQQRCTCMLGAtPFIYDLLNLLEK-QPADLSAlrFFLCGGTTIPKKVARECQQRGIKLLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 328 YGLTEtaglnvSCawkPQWNRLPASDRARLKARQGVRTVGfTEIDVVDpESGRSVERNGEtvGEIVMRGSSIMLGYLKDP 407
Cdd:PRK06087 333 YGSTE------SS---PHAVVNLDDPLSRFMHTDGYAAAG-VEIKVVD-EARKTLPPGCE--GEEASRGPNVFMGYLDEP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 408 VGTEKALKN-GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFV 486
Cdd:PRK06087 400 ELTARALDEeGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYV 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9759119 487 SLKsGLTQRPTEVEMIEY-CRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR-EIAKKMG 545
Cdd:PRK06087 480 VLK-APHHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRkDIMRRLT 539
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
31-539 |
8.03e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 203.60 E-value: 8.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 31 TSIVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRH 110
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 111 CGSKLLFVDVFSVDLAVEAISMMTTDPPilVFIADKEEEGGDADVADRTKFSYTYDdlihrgdldfkwirPESEWDPVVL 190
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVP--LLLVVAGPVPGFRSYEEALAAQPDTP--------------IADETAGADM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 191 NYTSGTTSAPKGV------VHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPL 264
Cdd:PRK08276 146 LYSSGTTGRPKGIkrplpgLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 265 IYRLIRDHGVTHMCGAPVVL-NMLSATNEFQ------PLNRPVNiltAGAPPPAAVLlRA--ESIGFVISHGYGLTETAG 335
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFvRMLKLPEEVRarydvsSLRVAIH---AAAPCPVEVK-RAmiDWWGPIIHEYYASSEGGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 336 LNVSCAwkPQWNRLPASdrarlkarqgvrtVG---FTEIDVVDpESGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEK 412
Cdd:PRK08276 302 VTVITS--EDWLAHPGS-------------VGkavLGEVRILD-EDGNELPPG--EIGTVYFEMDGYPFEYHNDPEKTAA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 413 A-LKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSG 491
Cdd:PRK08276 364 ArNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 9759119 492 LTQRP-TEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK08276 444 ADAGDaLAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
192-534 |
4.14e-58 |
|
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: 196.57 E-value: 4.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRgifvMSIDSLIDWT----VPKNPVYLWTLPIFHANGWSYPWgIAAV--GGTNVCLRKFDAPLI 265
Cdd:cd17638 7 FTSGTTGRSKGVMCAHR----QTLRAAAAWAdcadLTEDDRYLIINPFFHTFGYKAGI-VACLltGATVVPVAVFDVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 266 YRLIRDHGVTHMCGAPVV-LNMLS--ATNEFQPLNRPVNILTAGAPPPAAVLLRAESIGF-VISHGYGLTEtAGLNVSCa 341
Cdd:cd17638 82 LEAIERERITVLPGPPTLfQSLLDhpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFeTVLTAYGLTE-AGVATMC- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 342 wKPqwnrlpaSDRARLKARQGVRTVGFTEIDVVDPesgrsverngetvGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFY 420
Cdd:cd17638 160 -RP-------GDDAETVATTCGRACPGFEVRIADD-------------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 421 TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQrpTEVE 500
Cdd:cd17638 219 TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTL--TEED 296
|
330 340 350
....*....|....*....|....*....|....
gi 9759119 501 MIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMK 534
Cdd:cd17638 297 VIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
13-539 |
5.75e-58 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 203.09 E-value: 5.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 13 PLTPIGFLERAATVYGDCTSIVYGSNT--VYTWRETNLRCLRVASSL-SSIGIGRSDVVSVLSPNTPAMYELQFAVPMSG 89
Cdd:PRK05620 9 PLSLTRILEYGSTVHGDTTVTTWGGAEqeQTTFAAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 90 AILNNINTRLDARTVSVLLRHCGSKLLFVDVfsvDLAVEAISMMTTDPPI--LVFIADKEEEggDADVADRTKFS-YTYD 166
Cdd:PRK05620 89 AVFNPLNKQLMNDQIVHIINHAEDEVIVADP---RLAEQLGEILKECPCVraVVFIGPSDAD--SAAAHMPEGIKvYSYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 167 DLIHRGDLDFKWirPE-SEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSI-----DSLidwTVPKNPVYLWTLPIFHANG 240
Cdd:PRK05620 164 ALLDGRSTVYDW--PElDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLslrttDSL---AVTHGESFLCCVPIYHVLS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 241 WSYPwgIAA-VGGTNVCL--RKFDAPLIYRLIRDH--GVTHmcGAPVVLNMLSATNEFQPLNRPV--NILTAGAP-PPAA 312
Cdd:PRK05620 239 WGVP--LAAfMSGTPLVFpgPDLSAPTLAKIIATAmpRVAH--GVPTLWIQLMVHYLKNPPERMSlqEIYVGGSAvPPIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 313 VLLRAESIGFVISHGYGLTETAGL-NVScawkpqwnRLPA--SDRARLKAR--QGVRTVGFtEIDVVDpeSGRSVERNGE 387
Cdd:PRK05620 315 IKAWEERYGVDVVHVWGMTETSPVgTVA--------RPPSgvSGEARWAYRvsQGRFPASL-EYRIVN--DGQVMESTDR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 388 TVGEIVMRGSSIMLGYLKDPVGT-----------------EKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENV 450
Cdd:PRK05620 384 NEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedanDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 451 SSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLT-QRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTST 529
Cdd:PRK05620 464 YSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEpTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSV 543
|
570
....*....|
gi 9759119 530 GKVMKFVLRE 539
Cdd:PRK05620 544 GKFDKKDLRQ 553
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
186-532 |
3.00e-57 |
|
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: 194.41 E-value: 3.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLI 265
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 266 YRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAG--APPPAAVLLRAESIGFVIshGYGLTETAGLnVSCAwk 343
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGldAPETIQRFEETTGATFWS--LYGQTETSGL-VTLS-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 344 pqwnrlPASDRARLKARQGVrtvgFTEIDVVDpESGRSVERnGETvGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGD 423
Cdd:cd17637 156 ------PYRERPGSAGRPGP----LVRVRIVD-DNDRPVPA-GET-GEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 424 VGVIHSDGYLEIKDRS--KDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEVEM 501
Cdd:cd17637 223 LGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG--ATLTADEL 300
|
330 340 350
....*....|....*....|....*....|.
gi 9759119 502 IEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17637 301 IEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
41-539 |
7.99e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 197.72 E-value: 7.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCgskllfvdv 120
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDA--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 fsvdlaveaismmttDPPILVfiadkeeegGDADVADRTKFSYTYDDLIHRGDLDFKWIRPESEWD-PVVLNYTSGTTSA 199
Cdd:PRK09088 94 ---------------EPRLLL---------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPErVSLILFTSGTSGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 200 PKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGW-SYPWGIAAVGGTNVCLRKFDAPLIYRLIRDH--GVTH 276
Cdd:PRK09088 150 PKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLiTSVRPVLAVGGSILVSNGFEPKRTLGRLGDPalGITH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 277 MCGAPVVLNMLSATNEFQP--LNRPVNILTAGAPPPAAVLLRAESIGFVISHGYGLTETA---GLNVSCAwkpqwnrlpa 351
Cdd:PRK09088 230 YFCVPQMAQAFRAQPGFDAaaLRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGtvfGMSVDCD---------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 352 SDRARLKArQGVRTVGfTEIDVVDpESGRSVeRNGETvGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSD 430
Cdd:PRK09088 300 VIRAKAGA-AGIPTPT-VQTRVVD-DQGNDC-PAGVP-GELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 431 GYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPTEVemIEYCRKKMP 510
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERI--RSHLSTRLA 452
|
490 500
....*....|....*....|....*....
gi 9759119 511 KYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK09088 453 KYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
33-539 |
5.13e-56 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 196.07 E-value: 5.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 33 IVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCG 112
Cdd:PRK13391 17 IMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 113 SKLLFVDVFSVDLAVEAISMMTTDPPILVFIADKEEEGGDaDVADRTKfsytyddlihrgDLDFKWIRPESEWDPvvLNY 192
Cdd:PRK13391 97 ARALITSAAKLDVARALLKQCPGVRHRLVLDGDGELEGFV-GYAEAVA------------GLPATPIADESLGTD--MLY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 193 TSGTTSAPKGVVhchRGIFVMSIDSLIDWTVPKNP--------VYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPL 264
Cdd:PRK13391 162 SSGTTGRPKGIK---RPLPEQPPDTPLPLTAFLQRlwgfrsdmVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 265 IYRLIRDHGVTHMCGAPVVLN-MLSATNE------FQPLNRPVNiltAGAPPPAAVllRAESI---GFVISHGYGLTETA 334
Cdd:PRK13391 239 YLALIEEYGVTHTQLVPTMFSrMLKLPEEvrdkydLSSLEVAIH---AAAPCPPQV--KEQMIdwwGPIIHEYYAATEGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 335 GLNVSCAwkPQWnrlpasdrarlKARQGvrTVG---FTEIDVVDpESGRSVErNGEtVGEIVMRGSSiMLGYLKDPVGTE 411
Cdd:PRK13391 314 GFTACDS--EEW-----------LAHPG--TVGramFGDLHILD-DDGAELP-PGE-PGTIWFEGGR-PFEYLNDPAKTA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 412 KAL--KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLK 489
Cdd:PRK13391 375 EARhpDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPV 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 490 SGLTQRPT-EVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK13391 455 DGVDPGPAlAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
24-538 |
1.18e-55 |
|
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: 195.28 E-value: 1.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 24 ATVYGDCTSIVYGSNTvYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDART 103
Cdd:cd05959 14 NEGRGDKTAFIDDAGS-LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 104 VSVLLRHCGSKLLFVdvfSVDLAVEAISMMTTDPPILVFIADKEEEGGDADVADRTKFSYTyddliHRGDLDFKWIRPEs 183
Cdd:cd05959 93 YAYYLEDSRARVVVV---SGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAA-----EAEQLKPAATHAD- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 184 ewDPVVLNYTSGTTSAPKGVVHCHRGIFVMSI----DSLidwTVPKNPVYLWTLPIFHA----NGWSYPWGiaaVGGTNV 255
Cdd:cd05959 164 --DPAFWLYSSGSTGRPKGVVHLHADIYWTAElyarNVL---GIREDDVCFSAAKLFFAyglgNSLTFPLS---VGATTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 256 CLRKFDAP-LIYRLIRDHGVTHMCGAPVVLN-MLSATNEFQPLNRPVNI-LTAGAPPPAAVLLRAES-IGFVISHGYGLT 331
Cdd:cd05959 236 LMPERPTPaAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLcVSAGEALPAEVGERWKArFGLDILDGIGST 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 332 ETagLNVSCAWKPQWNRLPASdrarlkarqGVRTVGFtEIDVVDpESGRSVErNGEtVGEIVMRGSSIMLGYLKDPVGTE 411
Cdd:cd05959 316 EM--LHIFLSNRPGRVRYGTT---------GKPVPGY-EVELRD-EDGGDVA-DGE-PGELYVRGPSSATMYWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 412 KALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSG 491
Cdd:cd05959 381 DTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPG 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 9759119 492 LT-QRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05959 461 YEdSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
20-537 |
3.44e-54 |
|
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: 190.80 E-value: 3.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVY-GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTR 98
Cdd:cd05923 7 LRRAASRAPDACAIADpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 99 LDARTVSVLLRhcgskllFVDVFSVDLAVEAISMMTtdppilVFIADKEEEGGDADVADRTKFSYTydDLIhrgdlDFKW 178
Cdd:cd05923 87 LKAAELAELIE-------RGEMTAAVIAVDAQVMDA------IFQSGVRVLALSDLVGLGEPESAG--PLI-----EDPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 179 IRPEsewDPVVLNYTSGTTSAPKGVVHCHRGI--FVMSIDSLIDWTVPKNPVYLWTLPIFHANG-WSYPWGIAAVGGTNV 255
Cdd:cd05923 147 REPE---QPAFVFYTSGTTGLPKGAVIPQRAAesRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGfFAVLVAALALDGTYV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 256 CLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLN-RPVNILT-AGAPPPAAVLLRAESI--GFVISHgYGLT 331
Cdd:cd05923 224 VVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTfAGATMPDAVLERVNQHlpGEKVNI-YGTT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 332 ETaglnvscawkpqWNRLPASDrarlkARQG--VRTVGFTEIDVVdPESGRSVE--RNGETvGEIVMR--GSSIMLGYLK 405
Cdd:cd05923 303 EA------------MNSLYMRD-----ARTGteMRPGFFSEVRIV-RIGGSPDEalANGEE-GELIVAaaADAAFTGYLN 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 406 DPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAF 485
Cdd:cd05923 364 QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTAC 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 9759119 486 VSLKSGltqRPTEVEMIEYCR-KKMPKYMVPKTVSFVDELPKTSTGKVMKFVL 537
Cdd:cd05923 444 VVPREG---TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
24-538 |
9.95e-53 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 187.58 E-value: 9.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 24 ATVYGDCTSIVY----GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:PRK08008 17 ADVYGHKTALIFessgGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLL-----FVDVFsvdlavEAISMMTTDPPILVFIADkEEEGGDADVADrtkfsytYDDLIHRGDL 174
Cdd:PRK08008 97 LREESAWILQNSQASLLvtsaqFYPMY------RQIQQEDATPLRHICLTR-VALPADDGVSS-------FTQLKAQQPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 175 DFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSliDWTVP--KNPVYLWTLPIFHANgWSYPWGIAA--V 250
Cdd:PRK08008 163 TLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYS--AWQCAlrDDDVYLTVMPAFHID-CQCTAAMAAfsA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 251 GGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNML----SATNEFQPLNRPVNILTAgapppaavLLRAESIGFVISH 326
Cdd:PRK08008 240 GATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLmvqpPSANDRQHCLREVMFYLN--------LSDQEKDAFEERF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 327 G------YGLTETAG--LNVSCAWKPQWnrlPASDRArlkarqgvrtvGFT-EIDVVDpESGRSVERNgeTVGEIVMRG- 396
Cdd:PRK08008 312 GvrlltsYGMTETIVgiIGDRPGDKRRW---PSIGRP-----------GFCyEAEIRD-DHNRPLPAG--EIGEICIKGv 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 397 --SSIMLGYLKDPVGTEKALK-NGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVAR 473
Cdd:PRK08008 375 pgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 474 PDVFWGETPCAFVSLKSGLTQrpTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:PRK08008 455 KDSIRDEAIKAFVVLNEGETL--SEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
19-542 |
2.60e-52 |
|
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: 186.50 E-value: 2.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATVYGDCTSIVYGSNTvYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAI------- 91
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERR-LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvfalpa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 92 -----LNNINTRLDARTVSVLLRHCGskllfvdvFS-VDLAVEAISMMTTDPPILVFiadkeeegGDADVAdrtkfsYTY 165
Cdd:COG1021 109 hrraeISHFAEQSEAVAYIIPDRHRG--------FDyRALARELQAEVPSLRHVLVV--------GDAGEF------TSL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 166 DDLIhRGDLDFKWIRPESeWDPVVLNYTSGTTSAPKgvvhchrgifvmsidsLIDWT----------------VPKNPVY 229
Cdd:COG1021 167 DALL-AAPADLSEPRPDP-DDVAFFQLSGGTTGLPK----------------LIPRThddylysvrasaeicgLDADTVY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 230 LWTLPIFHANGWSYPwGIAAV---GGTNVCLRKFDAPLIYRLIRDHGVTHMC-GAPVVLNMLSAtnefqPLNRPVN---- 301
Cdd:COG1021 229 LAALPAAHNFPLSSP-GVLGVlyaGGTVVLAPDPSPDTAFPLIERERVTVTAlVPPLALLWLDA-----AERSRYDlssl 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 302 --ILTAGA--PPPAAVLLRAEsIGFVISHGYGLTEtaGLnVSCawkpqwNRLPASDRARlkarqgVRTVG-----FTEID 372
Cdd:COG1021 303 rvLQVGGAklSPELARRVRPA-LGCTLQQVFGMAE--GL-VNY------TRLDDPEEVI------LTTQGrpispDDEVR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 373 VVDPEsGRSVERnGEtVGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVS 451
Cdd:COG1021 367 IVDED-GNPVPP-GE-VGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 452 SVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSgltQRPTEVEMIEYCR-KKMPKYMVPKTVSFVDELPKTSTG 530
Cdd:COG1021 444 AEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRG---EPLTLAELRRFLReRGLAAFKLPDRLEFVDALPLTAVG 520
|
570
....*....|..
gi 9759119 531 KVMKFVLREIAK 542
Cdd:COG1021 521 KIDKKALRAALA 532
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
23-540 |
5.46e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 186.29 E-value: 5.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 23 AATVYGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDA- 101
Cdd:PRK07788 58 AARRAPDRAALIDERGTL-TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGp 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 102 RTVSVLLRHcGSKLLFVDvfsvDLAVEAISMMTTD-PPILVFIADKEEEGGDADVADrtkfsyTYDDLIHRGDlDFKWIR 180
Cdd:PRK07788 137 QLAEVAARE-GVKALVYD----DEFTDLLSALPPDlGRLRAWGGNPDDDEPSGSTDE------TLDDLIAGSS-TAPLPK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 181 PESEWDPVVLnyTSGTTSAPKGVVHCHRGIFVmSIDSLIDWtVP--KNPVYLWTLPIFHANGWSYpWGIA-AVGGTNVCL 257
Cdd:PRK07788 205 PPKPGGIVIL--TSGTTGTPKGAPRPEPSPLA-PLAGLLSR-VPfrAGETTLLPAPMFHATGWAH-LTLAmALGSTVVLR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 RKFDAPLIYRLIRDHGVTHMCGAPVVLN-MLSATNEFQP---LNRPVNILTAGAPPPAAVLLRA-ESIGFVISHGYGLTE 332
Cdd:PRK07788 280 RRFDPEATLEDIAKHKATALVVVPVMLSrILDLGPEVLAkydTSSLKIIFVSGSALSPELATRAlEAFGPVLYNLYGSTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 TAGLNVScawKPQ-WNRLPAsdrarlkarqgvrTVG----FTEIDVVDpESGRSVERNgeTVGEIVMRGSSIMLGYLKdp 407
Cdd:PRK07788 360 VAFATIA---TPEdLAEAPG-------------TVGrppkGVTVKILD-ENGNEVPRG--VVGRIFVGNGFPFEGYTD-- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 408 vGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVS 487
Cdd:PRK07788 419 -GRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVV 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 9759119 488 LKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREI 540
Cdd:PRK07788 498 KAPG--AALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
20-538 |
6.20e-52 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 186.16 E-value: 6.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTR- 98
Cdd:PLN02860 13 LTRLATLRGNAVVTISG-NRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 99 ------------------LDARTVSVLLRHCGSKL------LFVDVFSVDLAVEAISMMTTDPPILVFIADKEeeggdad 154
Cdd:PLN02860 92 sfeeaksamllvrpvmlvTDETCSSWYEELQNDRLpslmwqVFLESPSSSVFIFLNSFLTTEMLKQRALGTTE------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 155 vadrtkfsytyddlihrgdLDFKWIrPEsewDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLP 234
Cdd:PLN02860 165 -------------------LDYAWA-PD---DAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 235 IFHANGWSYPWGIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNML---SATNEFQPLNRPVNILTAGAPPPA 311
Cdd:PLN02860 222 LCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLislTRKSMTWKVFPSVRKILNGGGSLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 312 AVLLRAESIGF---VISHGYGLTETAG------LNV----SCAWKPQWNRLPASDRARLKarQGVrTVG----FTEIDVV 374
Cdd:PLN02860 302 SRLLPDAKKLFpnaKLFSAYGMTEACSsltfmtLHDptleSPKQTLQTVNQTKSSSVHQP--QGV-CVGkpapHVELKIG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 375 DPESGRsverngetVGEIVMRGSSIMLGYLKDPVGTEKALKN-GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSV 453
Cdd:PLN02860 379 LDESSR--------VGRILTRGPHVMLGYWGQNSETASVLSNdGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 454 EVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPTEVEMIE------------YCR-KKMPKYMVPKtvSF 520
Cdd:PLN02860 451 EVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKENAKknltlssetlrhHCReKNLSRFKIPK--LF 528
|
570 580
....*....|....*....|.
gi 9759119 521 V---DELPKTSTGKVMKFVLR 538
Cdd:PLN02860 529 VqwrKPFPLTTTGKIRRDEVR 549
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
34-538 |
3.15e-51 |
|
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: 181.51 E-value: 3.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 34 VYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGS 113
Cdd:cd05919 4 FYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 114 KLLFVDvfsvdlaveaismmttdppilvfiadkeeeggDADVAdrtkfsytyddlihrgdldfkwirpesewdpvVLNYT 193
Cdd:cd05919 84 RLVVTS--------------------------------ADDIA--------------------------------YLLYS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 194 SGTTSAPKGVVHCHRG--IFVMSIDSLIDWTVPKNPVYlwTLP-IFHA----NGWSYPWgiaAVGGTNVCLRKF-DAPLI 265
Cdd:cd05919 100 SGTTGPPKGVMHAHRDplLFADAMAREALGLTPGDRVF--SSAkMFFGyglgNSLWFPL---AVGASAVLNPGWpTAERV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 266 YRLIRDHGVTHMCGAPVVL-NMLSATNEFQPLNRPVNILT-AGAPPPAAVLLR-AESIGFVISHGYGLTETAGLNVScaw 342
Cdd:cd05919 175 LATLARFRPTVLYGVPTFYaNLLDSCAGSPDALRSLRLCVsAGEALPRGLGERwMEHFGGPILDGIGATEVGHIFLS--- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 343 kpqwNRlpaSDRARLKArQGVRTVGFtEIDVVDPEsGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTG 422
Cdd:cd05919 252 ----NR---PGAWRLGS-TGRPVPGY-EIRLVDEE-GHTIPPG--EEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 423 DVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPTEVEMI 502
Cdd:cd05919 320 DKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDI 399
|
490 500 510
....*....|....*....|....*....|....*..
gi 9759119 503 -EYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05919 400 hRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
41-541 |
1.61e-50 |
|
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: 179.62 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLfvdv 120
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 fsvdlaveaismMTTDppilvfiadkeeeggdaDVADRTKfsytyddlihrgdldfkwirPEsewDPVVLNYTSGTTSAP 200
Cdd:cd05969 77 ------------ITTE-----------------ELYERTD--------------------PE---DPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 201 KGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYP-WGIAAVGGTNVCLR-KFDAPLIYRLIRDHGVTHMC 278
Cdd:cd05969 105 KGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGiWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWY 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 279 GAPVVLNML----SATNEFQPLNRPVNILTAGAP-PPAAVLLRAESIGFVISHGYGLTETAGL---NVSCawkpqwnrLP 350
Cdd:cd05969 185 TAPTAIRMLmkegDELARKYDLSSLRFIHSVGEPlNPEAIRWGMEVFGVPIHDTWWQTETGSImiaNYPC--------MP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 351 ASDRARLKARQGVrtvgftEIDVVDpESGRSVERNgeTVGEIVMRGS--SIMLGYLKDPVGTEKALKNGWFYTGDVGVIH 428
Cdd:cd05969 257 IKPGSMGKPLPGV------KAAVVD-ENGNELPPG--TKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 429 SDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLtqRPTE---VEMIEYC 505
Cdd:cd05969 328 EDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF--EPSDelkEEIINFV 405
|
490 500 510
....*....|....*....|....*....|....*.
gi 9759119 506 RKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIA 541
Cdd:cd05969 406 RQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
36-538 |
2.15e-50 |
|
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: 179.17 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 36 GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKL 115
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 116 LFVDvfsvdlaveaismmttdppilvfiadkeeeGGDadvadrtkfsytyddlihrgdldfkwirpesewDPVVLNYTSG 195
Cdd:cd05971 82 LVTD------------------------------GSD---------------------------------DPALIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 196 TTSAPKGVVHCHRgiFVMSidslidwtvpKNPVYLWTLPIFHANGWSYpWGIAA---VGGTNVCL--------------- 257
Cdd:cd05971 99 TTGPPKGALHAHR--VLLG----------HLPGVQFPFNLFPRDGDLY-WTPADwawIGGLLDVLlpslyfgvpvlahrm 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 RKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEfqPLNRPVNILTA---GAPPPAAVLLR--AESIGFVISHGYGLTE 332
Cdd:cd05971 166 TKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGE--QLKHAQVKLRAiatGGESLGEELLGwaREQFGVEVNEFYGQTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 TAGLNVSCAwkpqwNRLPASDRARLKARQGVRtvgfteIDVVDpESGRSVERNgeTVGEIVMR--GSSIMLGYLKDPVGT 410
Cdd:cd05971 244 CNLVIGNCS-----ALFPIKPGSMGKPIPGHR------VAIVD-DNGTPLPPG--EVGEIAVElpDPVAFLGYWNNPSAT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 411 EKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKS 490
Cdd:cd05971 310 EKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNP 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 491 GLTqrPTEV---EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05971 390 GET--PSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
4-474 |
6.20e-50 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 181.45 E-value: 6.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 4 MKPCAANSPPLTPIGFLERAATVYGDCTSIVY---GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYE 80
Cdd:COG1022 1 MSEFSDVPPADTLPDLLRRRAARFPDRVALREkedGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 81 LQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFV-DVFSVDLAVEAISMMTTDPPILVFiaDKEEEGGDADVadrt 159
Cdd:COG1022 81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRHIVVL--DPRGLRDDPRL---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 160 kfsYTYDDLIHRGD-------LDFKW--IRPEsewDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYL 230
Cdd:COG1022 155 ---LSLDELLALGRevadpaeLEARRaaVKPD---DLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 231 WTLPIFH--ANGWSYpwGIAAVGGTNVCLRkfDAPLIYRLIRDHGVTHMCGAP---------VVLNMLSAT--------- 290
Cdd:COG1022 229 SFLPLAHvfERTVSY--YALAAGATVAFAE--SPDTLAEDLREVKPTFMLAVPrvwekvyagIQAKAEEAGglkrklfrw 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 291 --------NEFQPLNRPVNIL----------------------------TAGAPPPAAVLLRAESIGFVISHGYGLTETA 334
Cdd:COG1022 305 alavgrryARARLAGKSPSLLlrlkhaladklvfsklrealggrlrfavSGGAALGPELARFFRALGIPVLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 335 GlnVSCAWKPQWNRLpasdrarlkarqgvRTVG----FTEIdvvdpesgrsveRNGETvGEIVMRGSSIMLGYLKDPVGT 410
Cdd:COG1022 385 P--VITVNRPGDNRI--------------GTVGpplpGVEV------------KIAED-GEILVRGPNVMKGYYKNPEAT 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 411 EKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIIT-GGENVSSVEVETVLYTNPAVNEVAVVA--RP 474
Cdd:COG1022 436 AEAFdADGWLHTGDIGELDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVVGdgRP 503
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-541 |
5.60e-49 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 173.44 E-value: 5.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRGI----FVMSIDSLIDwtvpKNPVYLWTLPIFHANGwSYPWGIAAV--GGTNVclrkFDAPLI 265
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEvynaWMLALNSLFD----PDDVLLCGLPLFHVNG-SVVTLLTPLasGAHVV----LAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 266 YR----------LIRDHGVTHMCGAPVVLNMLSATnefqPLNRPVNIL----TAGAPPPAAVLLRAE-SIGFVISHGYGL 330
Cdd:cd05944 80 YRnpglfdnfwkLVERYRITSLSTVPTVYAALLQV----PVNADISSLrfamSGAAPLPVELRARFEdATGLPVVEGYGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 331 TETAGLnVSCAWkPQWNRLPASDRARLKARQgvrtvgfTEIDVVDPESGRSVERNGETVGEIVMRGSSIMLGYLKDPVGT 410
Cdd:cd05944 156 TEATCL-VAVNP-PDGPKRPGSVGLRLPYAR-------VRIKVLDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 411 EKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKS 490
Cdd:cd05944 227 NAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKP 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 9759119 491 GLTQRPTEVEmiEYCRKKMP-KYMVPKTVSFVDELPKTSTGKVMKFVLREIA 541
Cdd:cd05944 307 GAVVEEEELL--AWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
36-544 |
8.68e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 177.24 E-value: 8.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 36 GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKL 115
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 116 LFV-------DVFSVdLAVEAISMMTTDPPILVFIADKEEEGGDADVADRTKFsytydDLIHRGDLDFKWIRPESEWDPV 188
Cdd:PRK06164 111 LVVwpgfkgiDFAAI-LAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLF-----ALPDPAPPAAAGERAADPDAGA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 189 VLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLIYRL 268
Cdd:PRK06164 185 LLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 269 IRDHGVTHMCGAPVVLN-MLSATNEFQPLNRpVNILTAGAPPPAA--VLLRAESIGFVISHGYGLTETAGLnVSCAwkpq 345
Cdd:PRK06164 265 LRRHRVTHTFGNDEMLRrILDTAGERADFPS-ARLFGFASFAPALgeLAALARARGVPLTGLYGSSEVQAL-VALQ---- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 346 wnrlPASDRARLKARQGVRTV-GFTEIDVVDPESGRSVErNGETvGEIVMRGSSIMLGYLKDPVGTEKALK-NGWFYTGD 423
Cdd:PRK06164 339 ----PATDPVSVRIEGGGRPAsPEARVRARDPQDGALLP-DGES-GEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 424 VGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARpdVFWGET-PCAFVSLKSGltQRPTEVEMI 502
Cdd:PRK06164 413 LGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTvPVAFVIPTDG--ASPDEAGLM 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 9759119 503 EYCRKKMPKYMVPKTVSFVDELPKTSTG---KVMKFVLREIAKKM 544
Cdd:PRK06164 489 AACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQAR 533
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
41-472 |
1.52e-48 |
|
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: 174.71 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDv 120
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 fsvdlaveaismmttDPpilvfiadkeeeggdADVAdrtkfsytyddlihrgdldfkwirpesewdpvVLNYTSGTTSAP 200
Cdd:cd05907 85 ---------------DP---------------DDLA--------------------------------TIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 201 KGVVHCHRGIfvMS-IDSLID-WTVPKNPVYLWTLP---IFHANGWSYpwGIAAVGGTNVClrkfdAPLIYRLIRDHGV- 274
Cdd:cd05907 103 KGVMLSHRNI--LSnALALAErLPATEGDRHLSFLPlahVFERRAGLY--VPLLAGARIYF-----ASSAETLLDDLSEv 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 275 --THMCGAPVVLNMLS------ATNEFQ-------PLNRPVNILTAGAPPPAAVLLRAESIGFVISHGYGLTETAGlnVS 339
Cdd:cd05907 174 rpTVFLAVPRVWEKVYaaikvkAVPGLKrklfdlaVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSA--VV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 340 CAWKPQWNRLpasdrarlkarqgvRTVGfteiDVVDPESGRSVERngetvGEIVMRGSSIMLGYLKDPVGT-EKALKNGW 418
Cdd:cd05907 252 TLNPPGDNRI--------------GTVG----KPLPGVEVRIADD-----GEILVRGPNVMLGYYKNPEATaEALDADGW 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 419 FYTGDVGVIHSDGYLEIKDRSKDIIIT-GGENVSSVEVETVLYTNPAVNEVAVVA 472
Cdd:cd05907 309 LHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
21-534 |
3.59e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 176.00 E-value: 3.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 21 ERAATVYgdctsivYGSNTVYTwrETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLD 100
Cdd:PRK06178 48 QRPAIIF-------YGHVITYA--ELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 101 ARTVSVLLRHCGSKLLFV-DVFS-------VDLAVEAI-----SMMTTDPPILV----FIADKEEEGGDADV--ADRTKf 161
Cdd:PRK06178 119 EHELSYELNDAGAEVLLAlDQLApvveqvrAETSLRHVivtslADVLPAEPTLPlpdsLRAPRLAAAGAIDLlpALRAC- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 162 syTYDDLIHRGDLDfkwirpesewDPVVLNYTSGTTSAPKGVVHCHRG-IFVMSIDSLIDWTVPKNPVYLWTLPIFHANG 240
Cdd:PRK06178 198 --TAPVPLPPPALD----------ALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 241 WS----YPwgiAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGapVVLNML-------SATNEFQPLNRP-----VNILT 304
Cdd:PRK06178 266 ENfgllFP---LFSGATLVLLARWDAVAFMAAVERYRVTRTVM--LVDNAVelmdhprFAEYDLSSLRQVrvvsfVKKLN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 305 agappPAAVLLRAESIGFVISHG-YGLTET-------AGLNVscawkpqwnrlpasDRARLKARQ---GVRTVGfTEIDV 373
Cdd:PRK06178 341 -----PDYRQRWRALTGSVLAEAaWGMTEThtcdtftAGFQD--------------DDFDLLSQPvfvGLPVPG-TEFKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 374 VDPESGRSVERNGEtvGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSV 453
Cdd:PRK06178 401 CDFETGELLPLGAE--GEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 454 EVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQrpTEVEMIEYCRKKMPKYMVPkTVSFVDELPKTSTGKVM 533
Cdd:PRK06178 479 EVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADL--TAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVR 555
|
.
gi 9759119 534 K 534
Cdd:PRK06178 556 K 556
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
186-541 |
1.66e-46 |
|
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: 165.58 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIfVMSIDSLIDWtVPKNP--VYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAP 263
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANL-LASAAGLHSR-LGFGGgdSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 264 LIYRLirDHGVTHMCGAPVVL-NMLSATNEFQPLNRPVNILTAGAPPPAAVLLRAESIGFVISHGYGLTETAGlnVSCAW 342
Cdd:cd17630 79 AEDLA--PPGVTHVSLVPTQLqRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETAS--QVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 343 kpqwnRLPASDRARLKARQGVRtvgftEIDVVDPesgrsverngetvGEIVMRGSSIMLGYLKdPVGTEKALKNGWFYTG 422
Cdd:cd17630 155 -----RPDGFGRGGVGVLLPGR-----ELRIVED-------------GEIWVGGASLAMGYLR-GQLVPEFNEDGWFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 423 DVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltqrPTEVEMI 502
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP----ADPAELR 286
|
330 340 350
....*....|....*....|....*....|....*....
gi 9759119 503 EYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIA 541
Cdd:cd17630 287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
12-540 |
7.74e-46 |
|
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: 168.86 E-value: 7.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 12 PPLTPIG----------FLERAATVyGDCTSIVYGSNTV-YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTpamye 80
Cdd:cd17642 6 GPFYPLEdgtageqlhkAMKRYASV-PGTIAFTDAHTGVnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENS----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 81 LQFAVPMS-----GAILNNINTRLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTTDPPILVFIADKEEEGGDADv 155
Cdd:cd17642 80 LQFFLPVIaglfiGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 156 adrTKFSYTYDDlIHRGDLDFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIfVMSIDSLIDWTVPKNPV----YLW 231
Cdd:cd17642 159 ---YTFITQNLP-PGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNI-VARFSHARDPIFGNQIIpdtaILT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 232 TLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNML--SATNEFQPLNRPVNILTAGAPP 309
Cdd:cd17642 234 VIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFakSTLVDKYDLSNLHEIASGGAPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 310 PAAV-LLRAESIGF-VISHGYGLTETAglnVSCAWKPQWNRLPASdrarlkarQGVRTVGFtEIDVVDPESGRSVERNGE 387
Cdd:cd17642 314 SKEVgEAVAKRFKLpGIRQGYGLTETT---SAILITPEGDDKPGA--------VGKVVPFF-YAKVVDLDTGKTLGPNER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 388 tvGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVN 466
Cdd:cd17642 382 --GELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIF 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 467 EVAVVARPDVFWGETPCAFVSLKSGLTQrpTEVEMIEYCRKKM-PKYMVPKTVSFVDELPKTSTGKVMKFVLREI 540
Cdd:cd17642 460 DAGVAGIPDEDAGELPAAVVVLEAGKTM--TEKEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
177-543 |
2.60e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 167.92 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 177 KWIRPESEWDPVV-LNYTSGTTSAPKGVVHCHRGIfvmsIDSLI--DWTV-----PKNPVYLWTLPIFHangwsypwgIA 248
Cdd:PRK08974 197 QYVKPELVPEDLAfLQYTGGTTGVAKGAMLTHRNM----LANLEqaKAAYgpllhPGKELVVTALPLYH---------IF 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 249 AV----------GGTNVCL---RkfDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAG--APPPAAV 313
Cdd:PRK08974 264 ALtvncllfielGGQNLLItnpR--DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGggMAVQQAV 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 314 LLRAESI-GFVISHGYGLTETAGLnVSCawkpqwnrlpasDRARLKARQGvrTVGF----TEIDVVDpESGRSVErNGET 388
Cdd:PRK08974 342 AERWVKLtGQYLLEGYGLTECSPL-VSV------------NPYDLDYYSG--SIGLpvpsTEIKLVD-DDGNEVP-PGEP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 389 vGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEV 468
Cdd:PRK08974 405 -GELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEV 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 469 AVVARPDVFWGETPCAFVSLK-SGLTQRptevEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKK 543
Cdd:PRK08974 484 AAVGVPSEVSGEAVKIFVVKKdPSLTEE----ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 555
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
20-534 |
2.86e-45 |
|
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: 166.35 E-value: 2.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVyGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVpmsgailnninTRL 99
Cdd:cd05920 21 LARSAARHPDRIAVV-DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFAL-----------LRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLLFVdvfsvdlaVEAISmmttdpPILVFIADkeeeggdadvadrtkfsyTYDDLIHRGDldFKWI 179
Cdd:cd05920 89 GAVPVLALPSHRRSELSAF--------CAHAE------AVAYIVPD------------------RHAGFDHRAL--AREL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 180 RpESEWDPVVLNYTSGTTSAPKGVVHCHRGiFVMSIDSLIDWT-VPKNPVYLWTLPIFHANGWSYP--WGIAAVGGTNVC 256
Cdd:cd05920 135 A-ESIPEVALFLLSGGTTGTPKLIPRTHND-YAYNVRASAEVCgLDQDTVYLAVLPAAHNFPLACPgvLGTLLAGGRVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 257 LRKFDAPLIYRLIRDHGVTHMCGAPVVLNM-LSATNEFQPLNRPVNILTAGA---PPPAAVLLRAEsIGFVISHGYGLTE 332
Cdd:cd05920 213 APDPSPDAAFPLIEREGVTVTALVPALVSLwLDAAASRRADLSSLRLLQVGGarlSPALARRVPPV-LGCTLQQVFGMAE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 taGLnvscawkPQWNRLPASDrARLKARQGVRTVGFTEIDVVDpESGRSVErNGETvGEIVMRGSSIMLGYLKDPVGTEK 412
Cdd:cd05920 292 --GL-------LNYTRLDDPD-EVIIHTQGRPMSPDDEIRVVD-EEGNPVP-PGEE-GELLTRGPYTIRGYYRAPEHNAR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 413 AL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSg 491
Cdd:cd05920 359 AFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD- 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 9759119 492 ltQRPTEVEMIEYCRKK-MPKYMVPKTVSFVDELPKTSTGKVMK 534
Cdd:cd05920 438 --PPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
48-539 |
1.70e-44 |
|
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: 164.09 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 48 LRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLR--HCGSKLLFVdvfSVDL 125
Cdd:cd05929 3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKcgACPAYKSSR---APRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 126 AVEAISMMTTDPPILVFIADKEEEGGDADVADRTKFSYTyddlihrgdldfkwIRPESEWDPVVLNYTSGTTSAPKGVVH 205
Cdd:cd05929 80 EACAIIEIKAAALVCGLFTGGGALDGLEDYEAAEGGSPE--------------TPIEDEAAGWKMLYSGGTTGRPKGIKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 206 CHRGIFVmSIDSLIDWTVPKNP----VYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAP 281
Cdd:cd05929 146 GLPGGPP-DNDTLMAAALGFGPgadsVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 282 VVLNMLSATNEFQPLNRPVNILT----AGAPPPAAVllRAESI---GFVISHGYGLTETAGLnvSCAWKPQWnrlpasdr 354
Cdd:cd05929 225 TMFVRLLKLPEAVRNAYDLSSLKrvihAAAPCPPWV--KEQWIdwgGPIIWEYYGGTEGQGL--TIINGEEW-------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 355 arLKARQGVRTVGFTEIDVVDpESGRSVERNgeTVGEIVMRGSSIMLgYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYL 433
Cdd:cd05929 293 --LTHPGSVGRAVLGKVHILD-EDGNEVPPG--EIGEVYFANGPGFE-YTNDPEKTAAARnEGGWSTLGDVGYLDEDGYL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 434 EIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFV-SLKSGLTQRPTEVEMIEYCRKKMPKY 512
Cdd:cd05929 367 YLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqPAPGADAGTALAEELIAFLRDRLSRY 446
|
490 500
....*....|....*....|....*..
gi 9759119 513 MVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05929 447 KCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
41-538 |
2.06e-44 |
|
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: 163.07 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDV 120
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 fsvdlaveaismmttdppilvfiadkeeeggdadvADRTKFsytyDDlihrgdldfkwirpesewDPVVLNYTSGTTSAP 200
Cdd:cd05973 81 -----------------------------------ANRHKL----DS------------------DPFVMMFTSGTTGLP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 201 KGVVHCHRGIfvMSIDSLIDWTVPKNP--VYlWTL--PifhanGWSYPWGIAAVG----GTNVCLRK--FDAPLIYRLIR 270
Cdd:cd05973 104 KGVPVPLRAL--AAFGAYLRDAVDLRPedSF-WNAadP-----GWAYGLYYAITGplalGHPTILLEggFSVESTWRVIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 271 DHGVTHMCGAPVVLNML---SATNEFQPLNRPVNILTAGAP-PPAAVLLRAESIGFVISHGYGLTETaGLNVSCAWKPQW 346
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLmaaGAEVPARPKGRLRRVSSAGEPlTPEVIRWFDAALGVPIHDHYGQTEL-GMVLANHHALEH 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 347 nrlPASDRARLKARQGVRTVgfteidVVDpESGRSVERNGETVGEIVMRGSSIML--GYLKDPvgtEKALKNGWFYTGDV 424
Cdd:cd05973 255 ---PVHAGSAGRAMPGWRVA------VLD-DDGDELGPGEPGRLAIDIANSPLMWfrGYQLPD---TPAIDGGYYLTGDT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 425 GVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPT-EVEMIE 503
Cdd:cd05973 322 VEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAlADELQL 401
|
490 500 510
....*....|....*....|....*....|....*
gi 9759119 504 YCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05973 402 HVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
52-532 |
3.22e-44 |
|
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: 162.99 E-value: 3.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 52 RVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRH----CGSKLLFVDVFSVDLAV 127
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYlvadAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 128 EAIsmmtTDPPILVFIADKEEEGGDADVADRtkfsytyddlihrgdldfkwiRPESEWDPVVLNYTSGTTSAPKGVVHCH 207
Cdd:cd05922 85 DAL----PASPDPGTVLDADGIRAARASAPA---------------------HEVSHEDLALLLYTSGSTGSPKLVRLSH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 208 RGIF--VMSIDSLIDWTvpKNPVYLWTLPIfhangwSYPWGIA------AVGGTNVCLRKFDAPL-IYRLIRDHGVTHMC 278
Cdd:cd05922 140 QNLLanARSIAEYLGIT--ADDRALTVLPL------SYDYGLSvlnthlLRGATLVLTNDGVLDDaFWEDLREHGATGLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 279 GAPVVLNMLsATNEFQPLNRP-VNILT-AGAPPPAAVL--LRAESIGFVISHGYGLTETaglnvscawKPQWNRLPASdr 354
Cdd:cd05922 212 GVPSTYAML-TRLGFDPAKLPsLRYLTqAGGRLPQETIarLRELLPGAQVYVMYGQTEA---------TRRMTYLPPE-- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 355 aRLKARQGV--RTVGFTEIDVVDPESGRsvERNGEtVGEIVMRGSSIMLGYLKDPVG-TEKALKNGWFYTGDVGVIHSDG 431
Cdd:cd05922 280 -RILEKPGSigLAIPGGEFEILDDDGTP--TPPGE-PGEIVHRGPNVMKGYWNDPPYrRKEGRGGGVLHTGDLARRDEDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 432 YLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFwGETPCAFVSLKSGLTQRPteveMIEYCRKKMPK 511
Cdd:cd05922 356 FLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD----VLRSLAERLPP 430
|
490 500
....*....|....*....|.
gi 9759119 512 YMVPKTVSFVDELPKTSTGKV 532
Cdd:cd05922 431 YKVPATVRVVDELPLTASGKV 451
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
186-532 |
3.44e-44 |
|
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: 159.39 E-value: 3.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLI 265
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 266 YRLIRDHGVTH-MCGAPVVLNMLSATNEFQP-LNRPVNilTAGAPPPAAVLLRAESIGFVISHGYGLTETAGLNVscawk 343
Cdd:cd17636 81 LELIEAERCTHaFLLPPTIDQIVELNADGLYdLSSLRS--SPAAPEWNDMATVDTSPWGRKPGGYGQTEVMGLAT----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 344 pqWNRLpasdrarlkARQGVRTVG----FTEIDVVDPEsGRSVERnGETvGEIVMRGSSIMLGYLKDPVGTEKALKNGWF 419
Cdd:cd17636 154 --FAAL---------GGGAIGGAGrpspLVQVRILDED-GREVPD-GEV-GEIVARGPTVMAGYWNRPEVNARRTRGGWH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 420 YTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEV 499
Cdd:cd17636 220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG--ASVTEA 297
|
330 340 350
....*....|....*....|....*....|...
gi 9759119 500 EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17636 298 ELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
42-539 |
3.47e-44 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 164.55 E-value: 3.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDVF 121
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 122 SVDLAVEAISmmttDPPILVFIADKEEEGGDAdvadrtkfsyTYDDLI--HRGDLdfkwIRPESEWDPVVLnYTSGTTSA 199
Cdd:PRK13382 150 FSATVDRALA----DCPQATRIVAWTDEDHDL----------TVEVLIaaHAGQR----PEPTGRKGRVIL-LTSGTTGT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 200 PKGVVHCHRGIF--VMSIDSLIDWTVpKNPVYLwTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHM 277
Cdd:PRK13382 211 PKGARRSGPGGIgtLKAILDRTPWRA-EEPTVI-VAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDLIDRHRATGL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 278 CGAPVVLN-MLSATNEFqpLNRPVN-----ILTAGAP-PPAAVLLRAESIGFVISHGYGLTEtAGLnVSCAwkpqwnrLP 350
Cdd:PRK13382 289 AVVPVMFDrIMDLPAEV--RNRYSGrslrfAAASGSRmRPDVVIAFMDQFGDVIYNNYNATE-AGM-IATA-------TP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 351 ASDRARL----KARQGvrtvgfTEIDVVDPEsGRSVErNGEtVGEIVMRGSSIMLGYLKdpvGTEKALKNGWFYTGDVGV 426
Cdd:PRK13382 358 ADLRAAPdtagRPAEG------TEIRILDQD-FREVP-TGE-VGTIFVRNDTQFDGYTS---GSTKDFHDGFMASGDVGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 427 IHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPTEVEmiEYCR 506
Cdd:PRK13382 426 LDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLK--QHVR 503
|
490 500 510
....*....|....*....|....*....|...
gi 9759119 507 KKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK13382 504 DNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
19-547 |
4.49e-44 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 164.38 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATVYGDCTSIVYG-SNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINT 97
Cdd:PLN02330 33 FVLQDAELYADKVAFVEAvTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 98 RLDARTVSVLLRHCGSKLLFVDvfsvDLAVEAISMMTTdpPILVFIADKEEEGGD----ADVADRTKFSYTYDDlIHRGD 173
Cdd:PLN02330 113 TALESEIKKQAEAAGAKLIVTN----DTNYGKVKGLGL--PVIVLGEEKIEGAVNwkelLEAADRAGDTSDNEE-ILQTD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 174 LdfkwirpesewdpVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSL--IDWTVPKNPVYLWTLPIFHANGWSypwGIAAV- 250
Cdd:PLN02330 186 L-------------CALPFSSGTTGISKGVMLTHRNLVANLCSSLfsVGPEMIGQVVTLGLIPFFHIYGIT---GICCAt 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 251 ---GGTNVCLRKFDAPLIYRLIRDHGVTHM-CGAPVVLNMLS--ATNEFQPLNRPVN-ILTAGAP--PPAAVLLRAESIG 321
Cdd:PLN02330 250 lrnKGKVVVMSRFELRTFLNALITQEVSFApIVPPIILNLVKnpIVEEFDLSKLKLQaIMTAAAPlaPELLTAFEAKFPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 322 FVISHGYGLTETaglnvSCAwkpqwnRLPASDRARLKARQGVRTVGFT----EIDVVDPESGRSVERNgeTVGEIVMRGS 397
Cdd:PLN02330 330 VQVQEAYGLTEH-----SCI------TLTHGDPEKGHGIAKKNSVGFIlpnlEVKFIDPDTGRSLPKN--TPGELCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 398 SIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDV 476
Cdd:PLN02330 397 CVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9759119 477 FWGETPCAFVSLKSGLTQrpTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREiakKMGTT 547
Cdd:PLN02330 477 EAGEIPAACVVINPKAKE--SEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE---KMLSI 542
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
21-538 |
4.43e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 160.56 E-value: 4.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 21 ERAATVYGDCTSIVygsntvyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLD 100
Cdd:PRK13390 12 DRPAVIVAETGEQV-------SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 101 ARTVSVLLRHCGSKLLFVDVFSVDLAVEAismmttdppilvfiadkeeeGGDADVadRTKFSYTYDDLihrGDLD--FKW 178
Cdd:PRK13390 85 APEADYIVGDSGARVLVASAALDGLAAKV--------------------GADLPL--RLSFGGEIDGF---GSFEaaLAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 179 IRPESEWDP--VVLNYTSGTTSAPKG----------------VVHCHRGIFVMSidslidwtvpKNPVYLWTLPIFHANG 240
Cdd:PRK13390 140 AGPRLTEQPcgAVMLYSSGTTGFPKGiqpdlpgrdvdapgdpIVAIARAFYDIS----------ESDIYYSSAPIYHAAP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 241 WSYPWGIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVV-LNMLSATNEFQP---LNRPVNILTAGAPPPAAVL-L 315
Cdd:PRK13390 210 LRWCSMVHALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMfVRLLKLDADVRTrydVSSLRAVIHAAAPCPVDVKhA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 316 RAESIGFVISHGYGLTETAGLNVSCAwkPQWNRLPASdrarlKARQGVRTVGFTEIDVVDPESGRsverngetVGEIVMR 395
Cdd:PRK13390 290 MIDWLGPIVYEYYSSTEAHGMTFIDS--PDWLAHPGS-----VGRSVLGDLHICDDDGNELPAGR--------IGTVYFE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 396 GSSIMLGYLKDPVGTEKALKNG---WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVA 472
Cdd:PRK13390 355 RDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIG 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9759119 473 RPDVFWGETPCAFVSLKSGLtqRPTEV---EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:PRK13390 435 VPDPEMGEQVKAVIQLVEGI--RGSDElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
21-533 |
5.51e-43 |
|
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: 161.98 E-value: 5.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 21 ERAATVY-GDCTSIVygsnTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:cd17634 68 DRTAIIYeGDDTSQS----RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLLFV-DVF-----SVDL---AVEAISMMTTdPPILVFIADKEEeggdADVADRTKFSYTYDDLIH 170
Cdd:cd17634 144 APEAVAGRIIDSSSRLLITaDGGvragrSVPLkknVDDALNPNVT-SVEHVIVLKRTG----SDIDWQEGRDLWWRDLIA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 171 RGDLDFKWIRPESEwDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLID-WTVPKNPVYLWTLPIfhanGW--SYPW-- 245
Cdd:cd17634 219 KASPEHQPEAMNAE-DPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYvFDYGPGDIYWCTADV----GWvtGHSYll 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 246 -GIAAVGGTNVCLRKF----DAPLIYRLIRDHGVTHMCGAPVVLNMLSA--TNEFQPLNRP-VNILTAGAPP--PAAVLL 315
Cdd:cd17634 294 yGPLACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAagDDAIEGTDRSsLRILGSVGEPinPEAYEW 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 316 RAESIGF----VISHGYGlTETAGLNVScawkpqwnrlPASDRARLKARQGVRTVGFTEIDVVDPEsGRSVErnGETVGE 391
Cdd:cd17634 374 YWKKIGKekcpVVDTWWQ-TETGGFMIT----------PLPGAIELKAGSATRPVFGVQPAVVDNE-GHPQP--GGTEGN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 392 IVMRGS--SIMLGYLKDP---VGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVN 466
Cdd:cd17634 440 LVITDPwpGQTRTLFGDHerfEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVA 519
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 467 EVAVVARPDVFWGETPCAFVSLKSGLTQRPT-EVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVM 533
Cdd:cd17634 520 EAAVVGIPHAIKGQAPYAYVVLNHGVEPSPElYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
45-539 |
6.13e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 160.25 E-value: 6.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 45 ETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLfvdVFSVD 124
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL---IAHAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 125 LAVEAISMMTTDPPILVFIADKEeeggdadVADRTKFSytyDDLI--HRGDLDFK-WIRPESEWD------PVVLNYTSG 195
Cdd:PRK12406 93 LLHGLASALPAGVTVLSVPTPPE-------IAAAYRIS---PALLtpPAGAIDWEgWLAQQEPYDgppvpqPQSMIYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 196 TTSAPKGVvhcHRGIFV-------MSIDSLIdWTVPKNPVYLWTLPIFHANGWSYpwGIAA--VGGTNVCLRKFDAPLIY 266
Cdd:PRK12406 163 TTGHPKGV---RRAAPTpeqaaaaEQMRALI-YGLKPGIRALLTGPLYHSAPNAY--GLRAgrLGGVLVLQPRFDPEELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 267 RLIRDHGVTHMCGAPV----VLNMLSATNEFQPLNRPVNILTAGAPPPAAVLlRA--ESIGFVISHGYGLTETAGlnVSC 340
Cdd:PRK12406 237 QLIERHRITHMHMVPTmfirLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVK-RAmiEWWGPVIYEYYGSTESGA--VTF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 341 AWKPQWNRLPASDRarlKARQGVrtvgftEIDVVDpESGRSVErNGEtVGEIVMRGSSIML-GYLKDPVGTEKALKNGWF 419
Cdd:PRK12406 314 ATSEDALSHPGTVG---KAAPGA------ELRFVD-EDGRPLP-QGE-IGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 420 YTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTqrPTEV 499
Cdd:PRK12406 382 TSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGAT--LDEA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 9759119 500 EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK12406 460 DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
192-539 |
8.05e-43 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 160.04 E-value: 8.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRGIFVMSIdSLID-WTVPKNPVYLWTLPIFHANGWSYPWGIA-AVGGTNVCLRKFDAPLIYRLI 269
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNAL-TLVDyWRFTPDDVLIHALPIFHTHGLFVATNVAlLAGASMIFLPKFDPDAVLALM 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 270 RDhgVTHMCGAPVVLNMLSATNEFQP-LNRPVNILTAGAPPPAAVLLRA--ESIGFVISHGYGLTETaGLNVScawkpqw 346
Cdd:PRK07514 242 PR--ATVMMGVPTFYTRLLQEPRLTReAAAHMRLFISGSAPLLAETHREfqERTGHAILERYGMTET-NMNTS------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 347 NRLpASDRarlkaRQGvrTVGF----TEIDVVDPESGRSVERnGEtVGEIVMRGSSIMLGYLKDPVGTEKALK-NGWFYT 421
Cdd:PRK07514 312 NPY-DGER-----RAG--TVGFplpgVSLRVTDPETGAELPP-GE-IGMIEVKGPNVFKGYWRMPEKTAEEFRaDGFFIT 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 422 GDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEVEM 501
Cdd:PRK07514 382 GDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG--AALDEAAI 459
|
330 340 350
....*....|....*....|....*....|....*...
gi 9759119 502 IEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK07514 460 LAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
53-552 |
8.97e-43 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 160.78 E-value: 8.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 53 VASSLS-SIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLlfvdVFSVDLAVEAIS 131
Cdd:PLN02574 79 MAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGL----AFTSPENVEKLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 132 MMTTdPPILVfiadkeEEGGDADvaDRTKFSYTYDDLIhRGDLDFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRG-- 209
Cdd:PLN02574 155 PLGV-PVIGV------PENYDFD--SKRIEFPKFYELI-KEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNli 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 210 ----IFVMSIDSLIDWTVPKNpVYLWTLPIFHANGWS-YPWGIAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMcgaPVVL 284
Cdd:PLN02574 225 amveLFVRFEASQYEYPGSDN-VYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHF---PVVP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 285 NMLSA---------TNEFQPLNRpvniLTAGAPPPAAVLLraESIGFVISH-----GYGLTE-----TAGLNVscawkpq 345
Cdd:PLN02574 301 PILMAltkkakgvcGEVLKSLKQ----VSCGAAPLSGKFI--QDFVQTLPHvdfiqGYGMTEstavgTRGFNT------- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 346 wnrlpasdrarlKARQGVRTVGF----TEIDVVDPESGRSVERNGetVGEIVMRGSSIMLGYLKDPVGTE-KALKNGWFY 420
Cdd:PLN02574 368 ------------EKLSKYSSVGLlapnMQAKVVDWSTGCLLPPGN--CGELWIQGPGVMKGYLNNPKATQsTIDKDGWLR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 421 TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQrpTEVE 500
Cdd:PLN02574 434 TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTL--SQEA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 9759119 501 MIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKfvlREIAKKMGTTRLSRM 552
Cdd:PLN02574 512 VINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILR---RELKRSLTNSVSSRL 560
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
167-534 |
1.08e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 159.00 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 167 DLIHRGDLDFKWIRPESewdPVVLNYTSGTTSAPKGVVHCHRGIfVMSIDSLID---WTvpKNPVYLWTLPIFHANGWSY 243
Cdd:PRK07787 113 RLHARSWHRYPEPDPDA---PALIVYTSGTTGPPKGVVLSRRAI-AADLDALAEawqWT--ADDVLVHGLPLFHVHGLVL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 244 pwGIAA---VGGTNVCLRKFdAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAG-APPPAAVLLR-AE 318
Cdd:PRK07787 187 --GVLGplrIGNRFVHTGRP-TPEAYAQALSEGGTLYFGVPTVWSRIAADPEAARALRGARLLVSGsAALPVPVFDRlAA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 319 SIGFVISHGYGLTETAgLNVSCawkpqwnrlpasdRARLKARQGvrTVGF----TEIDVVDpESGRSVERNGETVGEIVM 394
Cdd:PRK07787 264 LTGHRPVERYGMTETL-ITLST-------------RADGERRPG--WVGLplagVETRLVD-EDGGPVPHDGETVGELQV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 395 RGSSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDR-SKDIIITGGENVSSVEVETVLYTNPAVNEVAVVA 472
Cdd:PRK07787 327 RGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVG 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9759119 473 RPDVFWGETPCAFVSLKSGltqrPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMK 534
Cdd:PRK07787 407 VPDDDLGQRIVAYVVGADD----VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLK 464
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
18-531 |
2.35e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 159.28 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 18 GFLERAATVYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINT 97
Cdd:PRK07798 7 DLFEAVADAVPDRVALVCG-DRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 98 RLDARTVSVLLRHCGSKLLfvdVFSVDLA--VEAISMMTTDPPILVFIADkeeeGGDADVADrtkFSYTYDDLIHRGD-- 173
Cdd:PRK07798 86 RYVEDELRYLLDDSDAVAL---VYEREFAprVAEVLPRLPKLRTLVVVED----GSGNDLLP---GAVDYEDALAAGSpe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 174 LDFkwirPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVP---------------KNPVYLWTLPIFHA 238
Cdd:PRK07798 156 RDF----GERSPDDLYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEpiedeeelakraaagPGMRRFPAPPLMHG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 239 NGWSYPWGIAAVGGTNVCLR--KFDAPLIYRLIRDHGVTHMC------GAPvvlnMLSATNEFQP--LNRPVNILTAGAP 308
Cdd:PRK07798 232 AGQWAAFAALFSGQTVVLLPdvRFDADEVWRTIEREKVNVITivgdamARP----LLDALEARGPydLSSLFAIASGGAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 309 --PPAAVLLRAESIGFVISHGYGLTETaGLNVSCAWKPqwnRLPASDRARLKArqGVRTVgfteidVVDpESGRSVERNG 386
Cdd:PRK07798 308 fsPSVKEALLELLPNVVLTDSIGSSET-GFGGSGTVAK---GAVHTGGPRFTI--GPRTV------VLD-EDGNPVEPGS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 387 ETVGEIVMRGSsIMLGYLKDPVGTEKALK--NG--WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTN 462
Cdd:PRK07798 375 GEIGWIARRGH-IPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAH 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9759119 463 PAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGK 531
Cdd:PRK07798 454 PDVADALVVGVPDERWGQEVVAVVQLREG--ARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
186-538 |
9.88e-42 |
|
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: 155.71 E-value: 9.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIfvmsIDSLIDWTV------PKNpVYLWTLPIFHANGWS----YPWGiaaVGGTNV 255
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDP----LASADRYAVnvlrlrEDD-RFVGSPPLAFTFGLGgvllFPFG---VGASGV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 256 CLRKFDAPLIYRLIRDHGVTHMCGAPVVLN-MLSATNEFQPLNRPVNILT-AGAPPPAAVLLR-AESIGFVISHGYGLTE 332
Cdd:cd05958 170 LLEEATPDLLLSAIARYKPTVLFTAPTAYRaMLAHPDAAGPDLSSLRKCVsAGEALPAALHRAwKEATGIPIIDGIGSTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 TAGLNVSCAwkpqwnrlpaSDRARlKARQGVRTVGFtEIDVVDpESGRSVERNgeTVGEIVMRGSSIMLgYLKDPvGTEK 412
Cdd:cd05958 250 MFHIFISAR----------PGDAR-PGATGKPVPGY-EAKVVD-DEGNPVPDG--TIGRLAVRGPTGCR-YLADK-RQRT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 413 ALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGL 492
Cdd:cd05958 313 YVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGV 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 9759119 493 TQRPTEVEMI-EYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05958 393 IPGPVLARELqDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
41-538 |
9.27e-41 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 155.44 E-value: 9.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAIL---------NNINTRL---DAR---TVS 105
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVgplfeafmeEAVRDRLedsEAKvliTTP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 106 VLLRHCGSKLLfvdvfsvdlaveaismmttdpPIL--VFIADKEEEGGDADVADRTKFSYTYDDLihrgdlDFKWIRPEs 183
Cdd:PRK04319 154 ALLERKPADDL---------------------PSLkhVLLVGEDVEEGPGTLDFNALMEQASDEF------DIEWTDRE- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 184 ewDPVVLNYTSGTTSAPKGVVHCHRGIfvmsidsLIDWTVPKnpvylWTLPiFHAN---------GW----SYpwGIAA- 249
Cdd:PRK04319 206 --DGAILHYTSGSTGKPKGVLHVHNAM-------LQHYQTGK-----YVLD-LHEDdvywctadpGWvtgtSY--GIFAp 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 250 --VGGTNVCLR-KFDAPLIYRLIRDHGVTHMCGAPVVLNML-SATNE------FQPLNrpvNILTAGAP-PPAAVLLRAE 318
Cdd:PRK04319 269 wlNGATNVIDGgRFSPERWYRILEDYKVTVWYTAPTAIRMLmGAGDDlvkkydLSSLR---HILSVGEPlNPEVVRWGMK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 319 SIGFVISHGYGLTETAGLNVScawkpqwnRLPASDrarLKARQGVRTVGFTEIDVVDPESGrsvERNGETVGEIVMRGS- 397
Cdd:PRK04319 346 VFGLPIHDNWWMTETGGIMIA--------NYPAMD---IKPGSMGKPLPGIEAAIVDDQGN---ELPPNRMGNLAIKKGw 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 398 -SIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDV 476
Cdd:PRK04319 412 pSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDP 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 477 FWGETPCAFVSLKSGLTqrPTE---VEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:PRK04319 492 VRGEIIKAFVALRPGYE--PSEelkEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
31-532 |
2.93e-39 |
|
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: 148.83 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 31 TSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL-DARtVSVLLR 109
Cdd:cd05930 4 VAVVDGDQSL-TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYpAER-LAYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 110 HCGSKLLFvdvfsvdlaveaismmtTDPpilvfiadkeeeggdadvadrtkfsytyDDLIHrgdldfkwirpesewdpvV 189
Cdd:cd05930 82 DSGAKLVL-----------------TDP----------------------------DDLAY------------------V 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 190 LnYTSGTTSAPKGVVHCHRGIfvmsiDSLIDW---TVPKNP---VYLWTLPIFHANGWSYPWGIAAvGGTNVCLRK---F 260
Cdd:cd05930 99 I-YTSGSTGKPKGVMVEHRGL-----VNLLLWmqeAYPLTPgdrVLQFTSFSFDVSVWEIFGALLA-GATLVVLPEevrK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 261 DAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGAPPPAAVLLRAESIGF--VISHGYGLTETAGlnV 338
Cdd:cd05930 172 DPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLPgaRLVNLYGPTEATV--D 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 339 SCAWkpqwnRLPASDRARlkarqGVRTVGF----TEIDVVDPEsGRSVErNGEtVGEIVMRGSSIMLGYLKDPVGTEKAL 414
Cdd:cd05930 250 ATYY-----RVPPDDEED-----GRVPIGRpipnTRVYVLDEN-LRPVP-PGV-PGELYIGGAGLARGYLNRPELTAERF 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 415 ------KNGWFY-TGDVGVIHSDGYLEIKDRSKDII-ITG-----GEnvssveVETVLYTNPAVNEVAVVARPDVFWGET 481
Cdd:cd05930 317 vpnpfgPGERMYrTGDLVRWLPDGNLEFLGRIDDQVkIRGyrielGE------IEAALLAHPGVREAAVVAREDGDGEKR 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 482 PCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd05930 391 LVAYVVPDEG--GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
190-542 |
8.38e-39 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 149.40 E-value: 8.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 190 LNYTSGTTSAPKGVVHCHRGIF--VMSID-----SLIDWTVPKNPVYLWTLPIFH--ANGWSYPWGIAAvGGTNVCL--- 257
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRNIVanVLQMEawlqpAFEKKPRPDQLNFVCALPLYHifALTVCGLLGMRT-GGRNILIpnp 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 RkfDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGA-----PPPAAVLLraESIGFVISHGYGLTE 332
Cdd:PRK07059 288 R--DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGgmavqRPVAERWL--EMTGCPITEGYGLSE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 TAglNVSCAwkpqwNRLPASDRARlkarqgvrTVGF----TEIDVVDpESGRSVErNGEtVGEIVMRGSSIMLGYLKDPV 408
Cdd:PRK07059 364 TS--PVATC-----NPVDATEFSG--------TIGLplpsTEVSIRD-DDGNDLP-LGE-PGEICIRGPQVMAGYWNRPD 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 409 GTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVS 487
Cdd:PRK07059 426 ETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 488 LKSgltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAK 542
Cdd:PRK07059 506 KKD---PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA 557
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
176-545 |
1.20e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 149.14 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 176 FKWIRPESEwDPVVLNYTSGTTSAPKGVVHCHRGIF--VMSIDSLIDWTVPKNPVYLWT-LPIFHANGWSYPWGIAAV-G 251
Cdd:PRK05677 199 VTEANPQAD-DVAVLQYTGGTTGVAKGAMLTHRNLVanMLQCRALMGSNLNEGCEILIApLPLYHIYAFTFHCMAMMLiG 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 252 GTNVCLRK-FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAG---APPPAAVLLRAESIGFVISHG 327
Cdd:PRK05677 278 NHNILISNpRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSggmALQLATAERWKEVTGCAICEG 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 328 YGLTETaglnvscawkpqwnrlpaSDRARLKARQGVR--TVGF----TEIDVVDPEsGRSVERnGEtVGEIVMRGSSIML 401
Cdd:PRK05677 358 YGMTET------------------SPVVSVNPSQAIQvgTIGIpvpsTLCKVIDDD-GNELPL-GE-VGELCVKGPQVMK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 402 GYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGE 480
Cdd:PRK05677 417 GYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGE 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 481 TPCAFVSLKSGLTQrpTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR-EIAKKMG 545
Cdd:PRK05677 497 AIKVFVVVKPGETL--TKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRdEELKKAG 560
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
68-532 |
4.93e-38 |
|
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: 146.32 E-value: 4.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 68 VSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFV-DVFSVDLAVEAISMMTTDPPIlVFIADK 146
Cdd:cd05909 34 VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTsKQFIEKLKLHHLFDVEYDARI-VYLEDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 147 EEEGGDAD---VADRTKFSYTYDDLIhrgdldfKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIF--VMSIDSLIDW 221
Cdd:cd05909 113 RAKISKADkckAFLAGKFPPKWLLRI-------FGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAIFDP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 222 TvpKNPVYLWTLPIFHANGWS----YP--WGIAAVGGTNvclrkfdaPLIYR----LIRDHGVTHMCGAPVVLNML--SA 289
Cdd:cd05909 186 N--PEDVVFGALPFFHSFGLTgclwLPllSGIKVVFHPN--------PLDYKkipeLIYDKKATILLGTPTFLRGYarAA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 290 TNE-FQPLNRPVniltAGAP--PPAAVLLRAESIGFVISHGYGLTETAGLnVSCawkpqwNRlPASDRarlkaRQGvrTV 366
Cdd:cd05909 256 HPEdFSSLRLVV----AGAEklKDTLRQEFQEKFGIRILEGYGTTECSPV-ISV------NT-PQSPN-----KEG--TV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 367 GFT----EIDVVDPESGRSVErNGETvGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDI 442
Cdd:cd05909 317 GRPlpgmEVKIVSVETHEEVP-IGEG-GLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 443 IITGGENVSSVEVETVLYTN-PAVNEVAVVARPDVFWGETPCAFVSLKSgltqrPTEVEMIEYCRK-KMPKYMVPKTVSF 520
Cdd:cd05909 395 AKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTD-----TDPSSLNDILKNaGISNLAKPSYIHQ 469
|
490
....*....|..
gi 9759119 521 VDELPKTSTGKV 532
Cdd:cd05909 470 VEEIPLLGTGKP 481
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
36-540 |
1.00e-37 |
|
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: 147.25 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 36 GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKL 115
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 116 LFV-DVFS-----VDL---AVEAISMMTTDPPILVfiadkEEEGGDADVADRTKFSYtYDDLIHRGDLDFKWIRPEsewD 186
Cdd:cd05968 167 LITaDGFTrrgreVNLkeeADKACAQCPTVEKVVV-----VRHLGNDFTPAKGRDLS-YDEEKETAGDGAERTESE---D 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 187 PVVLNYTSGTTSAPKGVVHCHRGIFV-MSIDSLIDWTVPKNPVYLWtlpiFHANGWSY-PW---GIAAVGGTNVCLR--- 258
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVHAGFPLkAAQDMYFQFDLKPGDLLTW----FTDLGWMMgPWlifGGLILGATMVLYDgap 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 259 KFDAPL-IYRLIRDHGVTHMCGAPVVLNMLSATNEfQPLNR--------------PVNiltagaPPPAAVLLRAESIGFV 323
Cdd:cd05968 314 DHPKADrLWRMVEDHEITHLGLSPTLIRALKPRGD-APVNAhdlsslrvlgstgePWN------PEPWNWLFETVGKGRN 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 324 ISHGY-GLTETAGLNVSCAW-KPqwnrlpasdrarLKARQGVRTVGFTEIDVVDpESGRSVErngETVGEIVMRGSSIML 401
Cdd:cd05968 387 PIINYsGGTEISGGILGNVLiKP------------IKPSSFNGPVPGMKADVLD-ESGKPAR---PEVGELVLLAPWPGM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 402 --GYLKDPVGTEKA----LKNGWFYtGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPD 475
Cdd:cd05968 451 trGFWRDEDRYLETywsrFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPH 529
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 476 VFWGETPCAFVSLKSGLTQRPT-EVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREI 540
Cdd:cd05968 530 PVKGEAIVCFVVLKPGVTPTEAlAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAA 595
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
22-539 |
2.70e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 144.78 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 22 RAATVYGDCTsivygsntvYTWRETnlrcLRVASSLSSIGIGRSDV-----VSVLSPNTPAMYELQFAVPMSGAILNNIN 96
Cdd:PRK13388 17 TIAVRYGDRT---------WTWREV----LAEAAARAAALIALADPdrplhVGVLLGNTPEMLFWLAAAALGGYVLVGLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 97 TrldARTVSVLLRhcgskllfvDVFSVDLAVeaismMTTDPPILVFIADKEEEGGDADVADrtkfSYTYDDLIHRgDLDF 176
Cdd:PRK13388 84 T---TRRGAALAA---------DIRRADCQL-----LVTDAEHRPLLDGLDLPGVRVLDVD----TPAYAELVAA-AGAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 177 KWIRPESEWDPVVLNYTSGTTSAPKGVVhCHRGIFVMSIDSLID-WTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNV 255
Cdd:PRK13388 142 TPHREVDAMDPFMLIFTSGTTGAPKAVR-CSHGRLAFAGRALTErFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 256 CLR-KFDAPLIYRLIRDHGVTHM--CGAPvvLNMLSATNEfQPLNRPvNILTAGAPPPAAVLLRAE---SIGFVISHGYG 329
Cdd:PRK13388 221 ALPaKFSASGFLDDVRRYGATYFnyVGKP--LAYILATPE-RPDDAD-NPLRVAFGNEASPRDIAEfsrRFGCQVEDGYG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 330 LTETAGLNVscawkpqwnRLPAsdrarlkARQGVRTVGFTEIDVVDPESGRSVER----------NG-ETVGEIV-MRGS 397
Cdd:PRK13388 297 SSEGAVIVV---------REPG-------TPPGSIGRGAPGVAIYNPETLTECAVarfdahgallNAdEAIGELVnTAGA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 398 SIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVF 477
Cdd:PRK13388 361 GFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDER 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9759119 478 WGETPCAFVSLKSGLTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK13388 441 VGDQVMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
34-539 |
3.85e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 144.44 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 34 VYGSNTVYTWRETNLRCLRVASSLSS-IGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINT--RLDARTVSVLLRH 110
Cdd:PRK07867 22 LYFEDSFTSWREHIRGSAARAAALRArLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPtrRGAALARDIAHAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 111 CgsKLLFVDVFSVDLAVEAismmttDPPILVFIADKEEeggdadvadrtkfsytYDDLI--HRGDL-DFKWIRPEsewDP 187
Cdd:PRK07867 102 C--QLVLTESAHAELLDGL------DPGVRVINVDSPA----------------WADELaaHRDAEpPFRVADPD---DL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 188 VVLNYTSGTTSAPKGVVHCHRGIFVMSIdSLID--WTVPKNPVYLwTLPIFHANGWSYPWGIAAVGGTNVCLR-KFDAPL 264
Cdd:PRK07867 155 FMLIFTSGTSGDPKAVRCTHRKVASAGV-MLAQrfGLGPDDVCYV-SMPLFHSNAVMAGWAVALAAGASIALRrKFSASG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 265 IYRLIRDHGVTHM--CGAPvvLNMLSATNEfQPLNR--PVNIL--TAGAPPPAAVLlrAESIGFVISHGYGLTETAglnV 338
Cdd:PRK07867 233 FLPDVRRYGATYAnyVGKP--LSYVLATPE-RPDDAdnPLRIVygNEGAPGDIARF--ARRFGCVVVDGFGSTEGG---V 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 339 SCAWKPQwnrlpasdrarlkARQGVRTVGFTEIDVVDPESGRSVER---------NG-ETVGEIV-MRGSSIMLGYLKDP 407
Cdd:PRK07867 305 AITRTPD-------------TPPGALGPLPPGVAIVDPDTGTECPPaedadgrllNAdEAIGELVnTAGPGGFEGYYNDP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 408 VGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVS 487
Cdd:PRK07867 372 EADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 9759119 488 LKSGLTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK07867 452 LAPGAKFDPDAFAEFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
20-539 |
5.42e-37 |
|
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: 144.18 E-value: 5.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIV----YGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLspnTPAMYELQFAVP---MSGAIL 92
Cdd:cd05970 23 VDAMAKEYPDKLALVwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLT---LKRRYEFWYSLLalhKLGAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 93 NNINTRLDARTVSVLLRHCGSKLLFVDV-FSVDLAVEAISMMTTDPPILVFIADKEEEGGDadvadrtkfsyTYDDLIHR 171
Cdd:cd05970 100 IPATHQLTAKDIVYRIESADIKMIVAIAeDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWI-----------DFRKLIKN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 172 GDLDFKwiRPESEW-----DPVVLNYTSGTTSAPKGVVHchrgifvmsidsliDWTVPKNpvYLWTLPIFH---ANGWSY 243
Cdd:cd05970 169 ASPDFE--RPTANSypcgeDILLVYFSSGTTGMPKMVEH--------------DFTYPLG--HIVTAKYWQnvrEGGLHL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 244 P-----WGIAAVG--------GTNVCL---RKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATN----EFQPLNRPVnil 303
Cdd:cd05970 231 TvadtgWGKAVWGkiygqwiaGAAVFVydyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDlsryDLSSLRYCT--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 304 TAGAPPPAAVLLR-AESIGFVISHGYGLTETAglnVSCAWKPQWNRLPASdrarlkarQGVRTVGFtEIDVVDPEsGRSV 382
Cdd:cd05970 308 TAGEALNPEVFNTfKEKTGIKLMEGFGQTETT---LTIATFPWMEPKPGS--------MGKPAPGY-EIDLIDRE-GRSC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 383 ErNGETvGEIVMRGSS-----IMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVET 457
Cdd:cd05970 375 E-AGEE-GEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVES 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 458 VLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTqrPTEV---EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMK 534
Cdd:cd05970 453 ALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYE--PSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
....*
gi 9759119 535 FVLRE 539
Cdd:cd05970 531 VEIRE 535
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
20-532 |
1.34e-36 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 142.61 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTL-TYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMmTTDPPILVFIADKEEEGGDADVADrtkfSYTYDDLIHRGDLDFKWI 179
Cdd:TIGR03098 85 KAEQVAHILADCNVRLLVTSSERLDLLHPALPG-CHDLRTLIIVGDPAHASEGHPGEE----PASWPKLLALGDADPPHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 180 RPESewDPVVLNYTSGTTSAPKGVVHCHRGIF--VMSIDSLIDWTvPKNPVyLWTLPIFHANGWSYPWGIAAVGGTNVCL 257
Cdd:TIGR03098 160 VIDS--DMAAILYTSGSTGRPKGVVLSHRNLVagAQSVATYLENR-PDDRL-LAVLPLSFDYGFNQLTTAFYVGATVVLH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 RKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSA----TNEFQPLNRPVNilTAGAPPPAAVL-LRAESIGFVISHGYGLTE 332
Cdd:TIGR03098 236 DYLLPRDVLKALEKHGITGLAAVPPLWAQLAQldwpESAAPSLRYLTN--SGGAMPRATLSrLRSFLPNARLFLMYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 taglnvscAWKPQWnrLPASDRARLKARQGvRTVGFTEIDVVDPESGRSVErnGETvGEIVMRGSSIMLGYLKDPVGT-- 410
Cdd:TIGR03098 314 --------AFRSTY--LPPEEVDRRPDSIG-KAIPNAEVLVLREDGSECAP--GEE-GELVHRGALVAMGYWNDPEKTae 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 411 ----------EKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGE 480
Cdd:TIGR03098 380 rfrplppfpgELHLPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQ 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 9759119 481 TPCAFVSLKSGLTQRPTevEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:TIGR03098 460 AIVLVVTPPGGEELDRA--ALLAECRARLPNYMVPALIHVRQALPRNANGKI 509
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
36-539 |
5.49e-36 |
|
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: 141.06 E-value: 5.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 36 GSNTVYTWRETNLRCLRVASSLS-SIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSK 114
Cdd:cd05928 37 GDEVKWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 115 LLfVDVFSVDLAVEAISMMTTDPPILVFIADKEEEGGdadvadrtkfsYTYDDLIHRGDLDFKWIRPESEwDPVVLNYTS 194
Cdd:cd05928 117 CI-VTSDELAPEVDSVASECPSLKTKLLVSEKSRDGW-----------LNFKELLNEASTEHHCVETGSQ-EPMAIYFTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 195 GTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPifhANGW--SYPWGIAAVGGTNVC-----LRKFDAPLIYR 267
Cdd:cd05928 184 GTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTS---DTGWikSAWSSLFEPWIQGACvfvhhLPRFDPLVILK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 268 LIRDHGVTHMCGAPVVLNMLSATN----EFQPLNrpvNILTAGAPPPAAVLLR-AESIGFVISHGYGLTETAglnVSCAW 342
Cdd:cd05928 261 TLSSYPITTFCGAPTVYRMLVQQDlssyKFPSLQ---HCVTGGEPLNPEVLEKwKAQTGLDIYEGYGQTETG---LICAN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 343 KPQWNRLPASdrarlkarQGVRTVGFtEIDVVDpESGRSVERNGEtvGEIVMRGS-----SIMLGYLKDPVGTEKALKNG 417
Cdd:cd05928 335 FKGMKIKPGS--------MGKASPPY-DVQIID-DNGNVLPPGTE--GDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 418 WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPT 497
Cdd:cd05928 403 FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDP 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 9759119 498 E---VEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05928 483 EqltKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
41-539 |
1.88e-35 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 139.20 E-value: 1.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTpamyeLQFAVPMSGAILNNI-----NTRLDARTVSVLLRHCGSKL 115
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDG-----VDFPIAFLGAIRAGIvpvalNTLLTADDYAYMLEDSRARV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 116 LFVdvfSVDLaVEAISMMTTDPPIL--VFIADKEEEGGD------ADVADRTKFSYTYDDlihrgdldfkwirpesewDP 187
Cdd:TIGR02262 106 VFV---SGAL-LPVIKAALGKSPHLehRVVVGRPEAGEVqlaellATESEQFKPAATQAD------------------DP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 188 VVLNYTSGTTSAPKGVVHCHRGIFVMS-IDSLIDWTVPKNPVYLWTLPIFHA----NGWSYPWGiaaVGGTNVCLRKFDA 262
Cdd:TIGR02262 164 AFWLYSSGSTGMPKGVVHTHSNPYWTAeLYARNTLGIREDDVCFSAAKLFFAyglgNALTFPMS---VGATTVLMGERPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 263 P-LIYRLIRDHGVTHMCGAPVVL-NMLSATNefQPLNRPVNI---LTAGAPPPAAVLLRAES-IGFVISHGYGLTETAGL 336
Cdd:TIGR02262 241 PdAVFDRLRRHQPTIFYGVPTLYaAMLADPN--LPSEDQVRLrlcTSAGEALPAEVGQRWQArFGVDIVDGIGSTEMLHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 337 NVScawkpqwnRLPasDRARLkARQGVRTVGFtEIDVVDpESGRSVErNGEtVGEIVMRGSSIMLGYLKDPVGTEKALKN 416
Cdd:TIGR02262 319 FLS--------NLP--GDVRY-GTSGKPVPGY-RLRLVG-DGGQDVA-DGE-PGELLISGPSSATMYWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 417 GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRP 496
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPG--QTA 461
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 9759119 497 TEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:TIGR02262 462 LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
35-537 |
3.81e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 137.57 E-value: 3.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 35 YGSNTvYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSK 114
Cdd:cd05914 3 YGGEP-LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 115 LLFVdvfsvdlaveaismmttdppilvfiADKEeeggdaDVAdrtkfsytyddlihrgdldfkwirpesewdpvVLNYTS 194
Cdd:cd05914 82 AIFV-------------------------SDED------DVA--------------------------------LINYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 195 GTTSAPKGVVHCHRGIfVMSIDSLIDWT-VPKNPVYLWTLPIFHANGWSYPWGIA-AVGGTNVCLRKFDAPLIyRLIRDH 272
Cdd:cd05914 99 GTTGNSKGVMLTYRNI-VSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPlLNGAHVVFLDKIPSAKI-IALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 273 GVTHMCGAPVVLNMLS-ATNEFQP----------LNRPVN----------------------ILTAGAPPPAAVLLRAES 319
Cdd:cd05914 177 QVTPTLGVPVPLVIEKiFKMDIIPkltlkkfkfkLAKKINnrkirklafkkvheafggnikeFVIGGAKINPDVEEFLRT 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 320 IGFVISHGYGLTETAGLnVSCAwkpQWNRLPASDRARLKARQGVRtvgfteIDVVDPESGRsverngetvGEIVMRGSSI 399
Cdd:cd05914 257 IGFPYTIGYGMTETAPI-ISYS---PPNRIRLGSAGKVIDGVEVR------IDSPDPATGE---------GEIIVRGPNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 400 MLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITG-GENVSSVEVETVLYTNPAVNEVAVVARPD-- 475
Cdd:cd05914 318 MKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVVQEKkl 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 476 VFWGETPCAFVSLKSGLTQRPTEV---EMIEYCRKKMPKY-MVPKTVSFVDELPKTSTGKVMKFVL 537
Cdd:cd05914 398 VALAYIDPDFLDVKALKQRNIIDAikwEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
41-541 |
4.58e-35 |
|
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: 136.93 E-value: 4.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILnnintrldartvsvllrhcgskllfvdv 120
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVV---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 fsvdlaVEAISMMTTDPpilvfIADKEEEGGDADVAdrtkfsytYDDLIHRGDldfkwirpesewdPVVLNYTSGTTSAP 200
Cdd:cd05974 53 ------IPATTLLTPDD-----LRDRVDRGGAVYAA--------VDENTHADD-------------PMLLYFTSGTTSKP 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 201 KGVVHCHRGIFVMSIDSLIdWTVPKNPVYLWTL--PIFHANGWS---YPWGI-AAVGGTNVClrKFDAPLIYRLIRDHGV 274
Cdd:cd05974 101 KLVEHTHRSYPVGHLSTMY-WIGLKPGDVHWNIssPGWAKHAWScffAPWNAgATVFLFNYA--RFDAKRVLAALVRYGV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 275 THMCGAPVVLNMLSATNEFQPLNRPVNILTAGAPPPAAVLLRAESI-GFVISHGYGLTETAGLNVSCAWKPqwnrlpasd 353
Cdd:cd05974 178 TTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAwGLTIRDGYGQTETTALVGNSPGQP--------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 354 rarLKARQGVRTVGFTEIDVVDPESGRSVErngetvGEIVM-----RGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIH 428
Cdd:cd05974 249 ---VKAGSMGRPLPGYRVALLDPDGAPATE------GEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 429 SDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRP-TEVEMIEYCRK 507
Cdd:cd05974 320 EDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPeTALEIFRFSRE 399
|
490 500 510
....*....|....*....|....*....|....
gi 9759119 508 KMPKYMVPKTVSFVdELPKTSTGKVMKFVLREIA 541
Cdd:cd05974 400 RLAPYKRIRRLEFA-ELPKTISGKIRRVELRRRE 432
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
186-534 |
6.80e-35 |
|
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: 134.31 E-value: 6.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLI---DWTVpkNPVYLWTLPIFHANG--WS----YPWGIAAVGGTNVC 256
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKeglNWVV--GDVTYLPLPATHIGGlwWIltclIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 257 LRKFdapliYRLIRDHGVTHMCGAPVVLNMLsaTNEFQPLNRPVN----ILTAGAPPPAAVLLRAESIGFV-ISHGYGLT 331
Cdd:cd17635 80 YKSL-----FKILTTNAVTTTCLVPTLLSKL--VSELKSANATVPslrlIGYGGSRAIAADVRFIEATGLTnTAQVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 332 ETAglNVSCawkpqwnrLPASDRARLKARQGVRTVGfTEIDVVDPEsGRSVERNGEtvGEIVMRGSSIMLGYLKDPVGTE 411
Cdd:cd17635 153 ETG--TALC--------LPTDDDSIEINAVGRPYPG-VDVYLAATD-GIAGPSASF--GTIWIKSPANMLGYWNNPERTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 412 KALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVsLKSG 491
Cdd:cd17635 219 EVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAV-VASA 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 9759119 492 LTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMK 534
Cdd:cd17635 298 ELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
19-532 |
3.67e-34 |
|
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: 135.02 E-value: 3.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATvYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTR 98
Cdd:cd12117 3 FEEQAAR-TPDAVAVVYG-DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 99 LDARTVSVLLRHCGSKLLFVDVFSVDLAVEAIsmmttdPPILVFIADKEEEGGDADVAdrtkfsytyddlihrgdldfkw 178
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLE------VAVVIDEALDAGPAGNPAVP---------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 179 IRPEsewDPVVLNYTSGTTSAPKGVVHCHRGI--FVMSIDSLidwTVPKNPVYLWTLPI-FHANGWSYpWGIAAVGGTNV 255
Cdd:cd12117 133 VSPD---DLAYVMYTSGSTGRPKGVAVTHRGVvrLVKNTNYV---TLGPDDRVLQTSPLaFDASTFEI-WGALLNGARLV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 256 CLRK---FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNE--FQPLNRpvnILTAG--APPPAAVLLRAESIGFVISHGY 328
Cdd:cd12117 206 LAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQLADEDPecFAGLRE---LLTGGevVSPPHVRRVLAACPGLRLVNGY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 329 GLTETAGlnVSCAWkpqwnRLPASDRARLKARQGvRTVGFTEIDVVDpESGRSVErNGEtVGEIVMRGSSIMLGYLKDPV 408
Cdd:cd12117 283 GPTENTT--FTTSH-----VVTELDEVAGSIPIG-RPIANTRVYVLD-EDGRPVP-PGV-PGELYVGGDGLALGYLNRPA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 409 GTEK------ALKNGWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGET 481
Cdd:cd12117 352 LTAErfvadpFGPGERLYrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKR 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 482 PCAFVSLksglTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd12117 432 LVAYVVA----EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
21-541 |
1.24e-33 |
|
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: 135.14 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 21 ERAATVYgdcTSIVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTP-AMYELqFAVPMSGAILNNINTRL 99
Cdd:cd05967 66 DQIALIY---DSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPeAAIAM-LACARIGAIHSVVFGGF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLLFVDVFSV---------DLAVEAISMMTTdPPILVFIADKEEEGGDADVADRtkfSYTYDDLIH 170
Cdd:cd05967 142 AAKELASRIDDAKPKLIVTASCGIepgkvvpykPLLDKALELSGH-KPHHVLVLNRPQVPADLTKPGR---DLDWSELLA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 171 -RGDLDFKWIrpESEwDPVVLNYTSGTTSAPKGVVHCHRGIFVM---SIDSLIDwtVPKNPVYLWTLPIfhanGW----S 242
Cdd:cd05967 218 kAEPVDCVPV--AAT-DPLYILYTSGTTGKPKGVVRDNGGHAVAlnwSMRNIYG--IKPGDVWWAASDV----GWvvghS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 243 Y-PWGIAAVGGTNVC-----LRKFDAPLIYRLIRDHGVTHMCGAPVVLNmlsATNEFQP---------LNRPVNILTAGA 307
Cdd:cd05967 289 YiVYGPLLHGATTVLyegkpVGTPDPGAFWRVIEKYQVNALFTAPTAIR---AIRKEDPdgkyikkydLSSLRTLFLAGE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 308 P--PPAAVLLRAESIGFVISHgYGLTETaGLNVSCAWKPQWNRLPasdrarlKARQGVRTVGFTEIDVVDPEsGRSVERN 385
Cdd:cd05967 366 RldPPTLEWAENTLGVPVIDH-WWQTET-GWPITANPVGLEPLPI-------KAGSPGKPVPGYQVQVLDED-GEPVGPN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 386 geTVGEIVMRGS---SIMLGYLKDPVGTEKALKN---GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVL 459
Cdd:cd05967 436 --ELGNIVIKLPlppGCLLTLWKNDERFKKLYLSkfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 460 YTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRPTEV--EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVL 537
Cdd:cd05967 514 LSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
....
gi 9759119 538 REIA 541
Cdd:cd05967 594 RKIA 597
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
20-530 |
3.36e-33 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 133.09 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVYGSN-TVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTR 98
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADrIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 99 LDARTVSVLLRHCGSKLLFVDvfSVDLAVEAISMMTTDPPILVFIADKEEEGGDADVADRTKFSYTYDDLIHRGdldfkw 178
Cdd:PRK05852 102 LPIAEQRVRSQAAGARVVLID--ADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEG------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 179 IRPesewDPVVLNYTSGTTSAPKGVVHCHRGIfVMSIDSLI--------DWTVPknpvylwTLPIFHANGWsypwgIAA- 249
Cdd:PRK05852 174 LRP----DDAMIMFTGGTTGLPKMVPWTHANI-ASSVRAIItgyrlsprDATVA-------VMPLYHGHGL-----IAAl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 250 ----VGGTNVCLR---KFDAPLIYRLIRDHGVTHMCGAPVVLNML--SATNEFQPLNRPV--NILTAGAP--PPAAVLLR 316
Cdd:PRK05852 237 latlASGGAVLLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILleRAATEPSGRKPAAlrFIRSCSAPltAETAQALQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 317 AESIGFVIShGYGLTETAGLNVScawkpqwNRLPASDRARlKARQGVRTVGFT---EIDVVDPESGrsvERNGETVGEIV 393
Cdd:PRK05852 317 TEFAAPVVC-AFGMTEATHQVTT-------TQIEGIGQTE-NPVVSTGLVGRStgaQIRIVGSDGL---PLPAGAVGEVW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 394 MRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVAR 473
Cdd:PRK05852 385 LRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 9759119 474 PDVFWGETPCAFVSLKSglTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTG 530
Cdd:PRK05852 465 PDQLYGEAVAAVIVPRE--SAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKG 519
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
192-532 |
3.67e-33 |
|
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: 131.60 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRgifvmSIDSLIDWTVPKNPV-----------YLWTLPIFhangwsYPWGIAAVGGTNVCLRK- 259
Cdd:cd05945 104 FTSGSTGRPKGVQISHD-----NLVSFTNWMLSDFPLgpgdvflnqapFSFDLSVM------DLYPALASGATLVPVPRd 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 260 --FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRP--VNILTAGAPPPAAVL--LRAESIGFVISHGYGLTET 333
Cdd:cd05945 173 atADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPslRHFLFCGEVLPHKTAraLQQRFPDARIYNTYGPTEA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 334 aglNVSCAWKpQWNRLPASDRARLkarqgvrTVGF----TEIDVVDpESGRSVErNGETvGEIVMRGSSIMLGYLKDPVG 409
Cdd:cd05945 253 ---TVAVTYI-EVTPEVLDGYDRL-------PIGYakpgAKLVILD-EDGRPVP-PGEK-GELVISGPSVSKGYLNNPEK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 410 TEKAL----KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAF 485
Cdd:cd05945 319 TAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAF 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 9759119 486 VSLKSGLTQRPTeVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd05945 399 VVPKPGAEAGLT-KAIKAELAERLPPYMIPRRFVYLDELPLNANGKI 444
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-531 |
7.83e-33 |
|
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: 129.04 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRGIFVMSI---------DSLIDWTVP---KNP--VYLWTLPIFHANGWsYPWGIAAVGGTNVCL 257
Cdd:cd05924 10 YTGGTTGMPKGVMWRQEDIFRMLMggadfgtgeFTPSEDAHKaaaAAAgtVMFPAPPLMHGTGS-WTAFGGLLGGQTVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 --RKFDAPLIYRLIRDHGVTHMcgaPVV--------LNMLSATNEFqPLNRPVNILTAGAPPPAAV---LLRAESiGFVI 324
Cdd:cd05924 89 pdDRFDPEEVWRTIEKHKVTSM---TIVgdamarplIDALRDAGPY-DLSSLFAISSGGALLSPEVkqgLLELVP-NITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 325 SHGYGLTETAGLNVSCAwkpqwnrLPASDRARLKARQGVRTVgfteidVVDPeSGRSVERNGETVGEIVMRGSsIMLGYL 404
Cdd:cd05924 164 VDAFGSSETGFTGSGHS-------AGSGPETGPFTRANPDTV------VLDD-DGRVVPPGSGGVGWIARRGH-IPLGYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 405 KDPVGTEKALK--NG--WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGE 480
Cdd:cd05924 229 GDEAKTAETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 481 TPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGK 531
Cdd:cd05924 309 EVVAVVQLREG--AGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
192-544 |
4.40e-32 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 131.97 E-value: 4.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRGIfvMS-IDSLID-WTVPKNPVYLWTLPIFHANGWS----YPW--GIAAVGGTNvclrKFDAP 263
Cdd:PRK08633 789 FSSGSEGEPKGVMLSHHNI--LSnIEQISDvFNLRNDDVILSSLPFFHSFGLTvtlwLPLleGIKVVYHPD----PTDAL 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 264 LIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLN-RPVNILTAGA---PPPAAVLLRaESIGFVISHGYGLTET---AGL 336
Cdd:PRK08633 863 GIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMfASLRLVVAGAeklKPEVADAFE-EKFGIRILEGYGATETspvASV 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 337 NVSCAWKPQWNRLPASdrarlkaRQGvrTVGF----TEIDVVDPESGRSVERNGEtvGEIVMRGSSIMLGYLKDPVGTEK 412
Cdd:PRK08633 942 NLPDVLAADFKRQTGS-------KEG--SVGMplpgVAVRIVDPETFEELPPGED--GLILIGGPQVMKGYLGDPEKTAE 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 413 ALKN----GWFYTGDVGVIHSDGYLEIKDR----SKdiiiTGGENVSSVEVE----TVLYTNPAVneVAVVARPDVFWGE 480
Cdd:PRK08633 1011 VIKDidgiGWYVTGDKGHLDEDGFLTITDRysrfAK----IGGEMVPLGAVEeelaKALGGEEVV--FAVTAVPDEKKGE 1084
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 481 tpcAFVSLksgLTQRPTEVEMIEYCRKK--MPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKKM 544
Cdd:PRK08633 1085 ---KLVVL---HTCGAEDVEELKRAIKEsgLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALAL 1144
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
186-541 |
7.08e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 129.56 E-value: 7.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHrGIFVMSIDSLIDWTVPKNP-----------VYLWTLPIFHANGWSYPWGIAAVGGT- 253
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTH-GNLVANMLQVRACLSQLGPdgqplmkegqeVMIAPLPLYHIYAFTANCMCMMVSGNh 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 254 NVCLRK-FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILT--AGAPPPAAVLLRAESI-GFVISHGYG 329
Cdd:PRK12492 287 NVLITNpRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTnsGGTALVKATAERWEQLtGCTIVEGYG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 330 LTETAglNVSCAwkpqwNrlPASDRARLKarqgvrTVGF----TEIDVVDPESgrsVERNGETVGEIVMRGSSIMLGYLK 405
Cdd:PRK12492 367 LTETS--PVAST-----N--PYGELARLG------TVGIpvpgTALKVIDDDG---NELPLGERGELCIKGPQVMKGYWQ 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 406 DPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCA 484
Cdd:PRK12492 429 QPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKL 508
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 485 FVSLKS-GLTQRptevEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIA 541
Cdd:PRK12492 509 FVVARDpGLSVE----ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
18-532 |
1.30e-31 |
|
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: 127.78 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 18 GFLERAATVYGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINT 97
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTL-TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 98 RLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAismmtTDPPILVFIADKEEEGGDADVAdrtkfsytyddlihrgdldfk 177
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAG-----GDVALLGDEALAAPPATPPLVP--------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 178 wIRPEsewDPVVLNYTSGTTSAPKGVVHCHRGIFvmsidSLIDW------TVPKNPVYLWTLPIFHANGWSYPWGIAAvG 251
Cdd:cd17646 135 -PRPD---NLAYVIYTSGSTGRPKGVMVTHAGIV-----NRLLWmqdeypLGPGDRVLQKTPLSFDVSVWELFWPLVA-G 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 252 GTNVCLR---KFDAPLIYRLIRDHGVTHMCGAPVVLNML---SATNEFQPLNRpvnILTAGA--PPPAAVLLRAESiGFV 323
Cdd:cd17646 205 ARLVVARpggHRDPAYLAALIREHGVTTCHFVPSMLRVFlaePAAGSCASLRR---VFCSGEalPPELAARFLALP-GAE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 324 ISHGYGLTETAgLNVScAWkpqwnrlPASDRARlkaRQGV---RTVGFTEIDVVDpESGRSVERNgeTVGEIVMRGSSIM 400
Cdd:cd17646 281 LHNLYGPTEAA-IDVT-HW-------PVRGPAE---TPSVpigRPVPNTRLYVLD-DALRPVPVG--VPGELYLGGVQLA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 401 LGYLKDPVGTEKALKNGWF------Y-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVAR 473
Cdd:cd17646 346 RGYLGRPALTAERFVPDPFgpgsrmYrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVAR 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 9759119 474 PDVFWGETPCAFVSLKSGLTQRPTEvEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17646 426 AAPAGAARLVGYVVPAAGAAGPDTA-ALRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
183-544 |
1.79e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 127.59 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 183 SEWDPVVLNYTSGTTSAPKGVVHCHRGiFVMSIDSLI-DWTVPKNPVYLWTLPIFHANgwsYPWG-IAA--VGGTNVCLR 258
Cdd:PRK07638 141 VQNAPFYMGFTSGSTGKPKAFLRAQQS-WLHSFDCNVhDFHMKREDSVLIAGTLVHSL---FLYGaISTlyVGQTVHLMR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 259 KFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFqpLNRPVNILTAGAPPPAAVLLRAESIgFVISHGYGLTETAGLN- 337
Cdd:PRK07638 217 KFIPNQVLDKLETENISVMYTVPTMLESLYKENRV--IENKMKIISSGAKWEAEAKEKIKNI-FPYAKLYEFYGASELSf 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 338 VSCAWKPQWNRLPASdrarlkarqgvrtVG--FTEIDV-VDPESGRSVERnGETvGEIVMRGSSIMLGYLKDPVGTEKAL 414
Cdd:PRK07638 294 VTALVDEESERRPNS-------------VGrpFHNVQVrICNEAGEEVQK-GEI-GTVYVKSPQFFMGYIIGGVLARELN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 415 KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSlksgltQ 494
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIK------G 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 9759119 495 RPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKKM 544
Cdd:PRK07638 433 SATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQ 482
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
20-543 |
6.23e-31 |
|
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: 127.29 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVY-----GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMyelqfAVPMS-----G 89
Cdd:cd05966 59 LDRHLKERGDKVAIIWegdepDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPEL-----VIAMLacariG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 90 AILNNINTRLDARTVSVLLRHCGSKLLF-VDVFS-----------VDLAVEAISMMTTdppILVFiadkEEEGGDAD-VA 156
Cdd:cd05966 134 AVHSVVFAGFSAESLADRINDAQCKLVItADGGYrggkviplkeiVDEALEKCPSVEK---VLVV----KRTGGEVPmTE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 157 DRTKFsytYDDLI--HRGDLDFKWIRPEsewDPVVLNYTSGTTSAPKGVVHCHRGIFV---MSIDSLIDwtVPKNPVYLW 231
Cdd:cd05966 207 GRDLW---WHDLMakQSPECEPEWMDSE---DPLFILYTSGSTGKPKGVVHTTGGYLLyaaTTFKYVFD--YHPDDIYWC 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 232 TLPIfhanGW----SY-PWGIAAVGGTNVClrkFD-APL------IYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRP 299
Cdd:cd05966 279 TADI----GWitghSYiVYGPLANGATTVM---FEgTPTypdpgrYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 300 VNIL----TAGAP-PPAAVLLRAESIG---FVISHGYGLTETAGLNVSCawkpqwnrLPASdrARLKArqGVRTVGF--T 369
Cdd:cd05966 352 LSSLrvlgSVGEPiNPEAWMWYYEVIGkerCPIVDTWWQTETGGIMITP--------LPGA--TPLKP--GSATRPFfgI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 370 EIDVVDPESGrsvERNGETVGEIVMRGS--SIMLGYLKDPvgtEKALK------NGWFYTGDVGVIHSDGYLEIKDRSKD 441
Cdd:cd05966 420 EPAILDEEGN---EVEGEVEGYLVIKRPwpGMARTIYGDH---ERYEDtyfskfPGYYFTGDGARRDEDGYYWITGRVDD 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 442 IIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLT-QRPTEVEMIEYCRKKMPKYMVPKTVSF 520
Cdd:cd05966 494 VINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEpSDELRKELRKHVRKEIGPIATPDKIQF 573
|
570 580
....*....|....*....|...
gi 9759119 521 VDELPKTSTGKVMKFVLREIAKK 543
Cdd:cd05966 574 VPGLPKTRSGKIMRRILRKIAAG 596
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
41-471 |
1.83e-30 |
|
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: 124.39 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAIlnNI--NTRLDARTVSVLLRHCGSKLLFV 118
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV--DVvrGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 119 DVFSVDLAVeaismmttdppilvfiadkeeeggdadvadrtkfsytyddlihrgdldfkwirpesewdpvvLNYTSGTTS 198
Cdd:cd17640 84 ENDSDDLAT--------------------------------------------------------------IIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 199 APKGVVHCHRGiFVMSIDSLIDWTVPK-NPVYLWTLPIFHANGWSYPWGIAAVGGTNVC--LRKFDA------------- 262
Cdd:cd17640 102 NPKGVMLTHAN-LLHQIRSLSDIVPPQpGDRFLSILPIWHSYERSAEYFIFACGCSQAYtsIRTLKDdlkrvkphyivsv 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 263 PLIYRLIRDHGVTHMCGAPVVLNMLSAT----NEFQplnrpVNILTAGAPPPAAVLLrAESIGFVISHGYGLTETAGLnV 338
Cdd:cd17640 181 PRLWESLYSGIQKQVSKSSPIKQFLFLFflsgGIFK-----FGISGGGALPPHVDTF-FEAIGIEVLNGYGLTETSPV-V 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 339 SCawkpqwNRLPASDRArlkarqgvrTVGF----TEIDVVDPESGRSVERNGEtvGEIVMRGSSIMLGYLKDPVGTEKAL 414
Cdd:cd17640 254 SA------RRLKCNVRG---------SVGRplpgTEIKIVDPEGNVVLPPGEK--GIVWVRGPQVMKGYYKNPEATSKVL 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 9759119 415 -KNGWFYTGDVGVIHSDGYLEIKDRSKD-IIITGGENVSSVEVETVLYTNPAVNEVAVV 471
Cdd:cd17640 317 dSDGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
20-539 |
2.40e-30 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 125.37 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVYGsNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:PRK08279 43 FEEAAARHPDRPALLFE-DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 dartVSVLLRHC----GSKLLFVDVFSVDLAVEAISMMTTDPPILVFIADKEEEGGDADVADRTKFSYTYDDLIHRGDLD 175
Cdd:PRK08279 122 ----RGAVLAHSlnlvDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 176 FKwirpesewDPVVLNYTSGTTSAPKGVVHCHR------GIFVMSIDSlidwtVPKNPVYLwTLPIFHANGWSYPWGIA- 248
Cdd:PRK08279 198 AK--------DTAFYIYTSGTTGLPKAAVMSHMrwlkamGGFGGLLRL-----TPDDVLYC-CLPLYHNTGGTVAWSSVl 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 249 AVGGTNVCLRKF------------DAPLI--------YRL-------IRDHGVTHMCGapvvlNMLSAT--NEFQplNRp 299
Cdd:PRK08279 264 AAGATLALRRKFsasrfwddvrryRATAFqyigelcrYLLnqppkptDRDHRLRLMIG-----NGLRPDiwDEFQ--QR- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 300 vniltagapppaavllraesigFVISH---GYGLTE--TAGLNV-----SCAWKPQWNRLPAsdrarlkarqgvRTVGFt 369
Cdd:PRK08279 336 ----------------------FGIPRileFYAASEgnVGFINVfnfdgTVGRVPLWLAHPY------------AIVKY- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 370 eidvvDPESGRSVeRN-------------GETVGEIVMRGSsiMLGYLkDPVGTEKAL-----KNG--WFYTGDVGVIHS 429
Cdd:PRK08279 381 -----DVDTGEPV-RDadgrcikvkpgevGLLIGRITDRGP--FDGYT-DPEASEKKIlrdvfKKGdaWFNTGDLMRDDG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 430 DGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAV--VARPDVFwGETPCAFVSLKSGLTQRPTevEMIEYCRK 507
Cdd:PRK08279 452 FGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVPGTD-GRAGMAAIVLADGAEFDLA--ALAAHLYE 528
|
570 580 590
....*....|....*....|....*....|..
gi 9759119 508 KMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:PRK08279 529 RLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
52-537 |
4.57e-29 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 120.88 E-value: 4.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 52 RVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCgskllfvDVFSVDLAVEAIS 131
Cdd:PRK05857 53 GLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQIT-------DPAAALVAPGSKM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 132 MMTTDPPILVFIADKEEEGGdadvADRTKFSytyddliHRGDLDFKWIRPESEWD-PVVLNYTSGTTSAPKGVVHCHRGI 210
Cdd:PRK05857 126 ASSAVPEALHSIPVIAVDIA----AVTRESE-------HSLDAASLAGNADQGSEdPLAMIFTSGTTGEPKAVLLANRTF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 211 FVMSiDSL-------IDWTVpkNPVYLWTLPIFHANG-WsypWGIAAVGGTNVCLRKFDAPL-IYRLIRDHGVTHMCGAP 281
Cdd:PRK05857 195 FAVP-DILqkeglnwVTWVV--GETTYSPLPATHIGGlW---WILTCLMHGGLCVTGGENTTsLLEILTTNAVATTCLVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 282 VVLNMLSATNEFQPLNRPVNILTA--GAPPPAAVLLRAESIGFVISHGYGLTETaGLNVSCawkpqwnrLPASDRARLKA 359
Cdd:PRK05857 269 TLLSKLVSELKSANATVPSLRLVGygGSRAIAADVRFIEATGVRTAQVYGLSET-GCTALC--------LPTDDGSIVKI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 360 RQGV--RTVGFTEIDVVDPE-SGRSVERNGETV--GEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLE 434
Cdd:PRK05857 340 EAGAvgRPYPGVDVYLAATDgIGPTAPGAGPSAsfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 435 IKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGetpcAFVSLK-------SGLTQRPTEVEMIEYCRK 507
Cdd:PRK05857 420 IKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG----ALVGLAvvasaelDESAARALKHTIAARFRR 495
|
490 500 510
....*....|....*....|....*....|
gi 9759119 508 KMPKYMVPKTVSFVDELPKTSTGKVMKFVL 537
Cdd:PRK05857 496 ESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
42-532 |
6.04e-29 |
|
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: 120.81 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSLSSIGiGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNI----NTRLDARTVSVLLRhCGSKLLF 117
Cdd:cd05931 26 TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppptPGRHAERLAAILAD-AGPRVVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 118 VDVFSVDLAVEAISMMTTDPPILVFIADKEEEGGDADVADRTkfsytyddlihrgdldfkwIRPEsewDPVVLNYTSGTT 197
Cdd:cd05931 104 TTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPS-------------------PDPD---DIAYLQYTSGST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 198 SAPKGVVHCHRGIF--VMSIDSLIDWTvPKNPVYLWtLPIFHANGWSYPWGIAA-VGGTNVCLRKFD---APLIY-RLIR 270
Cdd:cd05931 162 GTPKGVVVTHRNLLanVRQIRRAYGLD-PGDVVVSW-LPLYHDMGLIGGLLTPLySGGPSVLMSPAAflrRPLRWlRLIS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 271 DHGVTHMcGAPvvlNM---LsATNEFQPLNRP------VNILTAGAPPPAAVLLRA-----ESIGF---VISHGYGLTEt 333
Cdd:cd05931 240 RYRATIS-AAP---NFaydL-CVRRVRDEDLEgldlssWRVALNGAEPVRPATLRRfaeafAPFGFrpeAFRPSYGLAE- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 334 AGLNVSCAWKPQWNRLPASDRARLKAR---------QGVRTVG------FTEIDVVDPESGRSVERNgeTVGEIVMRGSS 398
Cdd:cd05931 314 ATLFVSGGPPGTGPVVLRVDRDALAGRavavaaddpAARELVScgrplpDQEVRIVDPETGRELPDG--EVGEIWVRGPS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 399 IMLGYLKDPVGTEKALK-------NGWFYTGDVGVIHsDGYLEIKDRSKDIIITGGENVSSVEVE-TVLYTNPAVNE--V 468
Cdd:cd05931 392 VASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPgcV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 469 AVVARPD-----------VFWGETPCAFVSLKSGLTQR-PTEVEmieycrkkmpkyMVPKTVSFV--DELPKTSTGKV 532
Cdd:cd05931 471 AAFSVPDdgeerlvvvaeVERGADPADLAAIAAAIRAAvAREHG------------VAPADVVLVrpGSIPRTSSGKI 536
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
186-542 |
6.15e-29 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 120.75 E-value: 6.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIfVMSIDSLIDWTV------PKNPVYLWTLPIFH-----ANGWSYpwgiAAVGGTN 254
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHRNL-VANMQQAHQWLAgtgkleEGCEVVITALPLYHifaltANGLVF----MKIGGCN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 255 VCLRK-FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGApppAAVLLRA------ESIGFVISHG 327
Cdd:PRK08751 284 HLISNpRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGG---GMAVQRSvaerwkQVTGLTLVEA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 328 YGLTETAglnvscawkpqwnrlPAS--DRARLKARQGVRTVGFTEIDVVDPESGRSVERNGEtVGEIVMRGSSIMLGYLK 405
Cdd:PRK08751 361 YGLTETS---------------PAAciNPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGE-IGELCIKGPQVMKGYWK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 406 DPVGTEKALK-NGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCA 484
Cdd:PRK08751 425 RPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKV 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 485 FVSLKSgltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAK 542
Cdd:PRK08751 505 VIVKKD---PALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
186-532 |
6.32e-29 |
|
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: 117.12 E-value: 6.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPK----------GVVHCHRGIFVMSIDSLIdwTVPKNPVYlwTLPIFHAngwsypwgIAA--VGGT 253
Cdd:cd17633 1 NPFYIGFTSGTTGLPKayyrserswiESFVCNEDLFNISGEDAI--LAPGPLSH--SLFLYGA--------ISAlyLGGT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 254 NVCLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEfqPLNRPVNILTAGA--PPPAAVLLRAESIGFVISHGYGLT 331
Cdd:cd17633 69 FIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLE--PESKIKSIFSSGQklFESTKKKLKNIFPKANLIEFYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 332 ETAGLNVSCawkPQWNRLPASdrarlkarqgvrtVG--FTEIDVvdpesgRSVERNGETVGEIVMRGSSIMLGYLKDPVG 409
Cdd:cd17633 147 ELSFITYNF---NQESRPPNS-------------VGrpFPNVEI------EIRNADGGEIGKIFVKSEMVFSGYVRGGFS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 410 TekalKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLK 489
Cdd:cd17633 205 N----PDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD 280
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 9759119 490 sGLTQRptevEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17633 281 -KLTYK----QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
41-471 |
9.22e-29 |
|
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: 119.88 E-value: 9.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDV 120
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 FS--------VDLAVEAISMMTTDPPilvfiadkeeeggdadvadrtKFSYTYDDLIHRGDLDFKWIRPESEwDPVVLNY 192
Cdd:cd05932 87 LDdwkamapgVPEGLISISLPPPSAA---------------------NCQYQWDDLIAQHPPLEERPTRFPE-QLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 193 TSGTTSAPKGVVHCHrGIFVMSIDSLI-DWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLRK------------ 259
Cdd:cd05932 145 TSGTTGQPKGVMLTF-GSFAWAAQAGIeHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAEsldtfvedvqra 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 260 -----FDAPLIYRLIRdHGVTHMCGA---------PVVlNMLSATNEFQPLN-RPVNILTAG-APPPAAVLLRAESIGFV 323
Cdd:cd05932 224 rptlfFSVPRLWTKFQ-QGVQDKIPQqklnlllkiPVV-NSLVKRKVLKGLGlDQCRLAGCGsAPVPPALLEWYRSLGLN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 324 ISHGYGLTETAGLNVSCawKPqwnrlpasdrarlkARQGVRTVGfteidvvdpESGRSVE-RNGETvGEIVMRGSSIMLG 402
Cdd:cd05932 302 ILEAYGMTENFAYSHLN--YP--------------GRDKIGTVG---------NAGPGVEvRISED-GEILVRSPALMMG 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9759119 403 YLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITG-GENVSSVEVETVLYTNPAVNEVAVV 471
Cdd:cd05932 356 YYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
42-470 |
9.51e-29 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 118.14 E-value: 9.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSL-SSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDv 120
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 121 fsvdlAVEAISMMTTDPPILVFIADKEEEGGDADVADRTKFSYTYDDLIHrgdldfkwirpesewdpvVLnYTSGTTSAP 200
Cdd:TIGR01733 80 -----SALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAY------------------VI-YTSGSTGRP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 201 KGVVHCHRGIFvmsidSLIDWTVPKNP-----VYLWTLPI-FHANGWSYpWGIAAVGGTNVCL----RKFDAPLIYRLIR 270
Cdd:TIGR01733 136 KGVVVTHRSLV-----NLLAWLARRYGldpddRVLQFASLsFDASVEEI-FGALLAGATLVVPpedeERDDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 271 DHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGAPPPAAV-LLRAESIGFVISHGYGLTETAglnVSCAWKPqwnrl 349
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPPALASLRLVILGGEALTPALVdRWRARGPGARLINLYGPTETT---VWSTATL----- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 350 PASDRARLKARQGV-RTVGFTEIDVVDPEsGRSVERNGetVGEIVMRGSSIMLGYLKDPVGTEKALKNGWFY-------- 420
Cdd:TIGR01733 282 VDPDDAPRESPVPIgRPLANTRLYVLDDD-LRPVPVGV--VGELYIGGPGVARGYLNRPELTAERFVPDPFAggdgarly 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 421 -TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAV 470
Cdd:TIGR01733 359 rTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
182-542 |
3.19e-28 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 118.89 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 182 ESEwDPVVLNYTSGTTSAPKGVVHCHRGIFV---MSIDSLIDwtVPKNPVYLWTLPIfhanGW----SY-PWGIAAVGGT 253
Cdd:TIGR02188 235 DSE-DPLFILYTSGSTGKPKGVLHTTGGYLLyaaMTMKYVFD--IKDGDIFWCTADV----GWitghSYiVYGPLANGAT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 254 NVClrkF-------DAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNIL----TAGAP--PPAAVLLR---- 316
Cdd:TIGR02188 308 TVM---FegvptypDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLrllgSVGEPinPEAWMWYYkvvg 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 317 ------------AESIGFVISHGYGLTETaglnvscawKPQWNRLPASdrarlkarqGVrtvgftEIDVVDpESGRSVER 384
Cdd:TIGR02188 385 kercpivdtwwqTETGGIMITPLPGATPT---------KPGSATLPFF---------GI------EPAVVD-EEGNPVEG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 385 NGETvGEIVMRGS--SIMLGYLKDP---VGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVL 459
Cdd:TIGR02188 440 PGEG-GYLVIKQPwpGMLRTIYGDHerfVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESAL 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 460 YTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRP-TEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:TIGR02188 519 VSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDeLRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLR 598
|
....
gi 9759119 539 EIAK 542
Cdd:TIGR02188 599 KIAA 602
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
186-545 |
7.12e-28 |
|
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: 116.93 E-value: 7.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHR----GIFVMSiDSLIDWTVPKNpVYLWTLPIFHangwsypwgIAAVGGTNVCLRK-- 259
Cdd:cd17639 89 DLACIMYTSGSTGNPKGVMLTHGnlvaGIAGLG-DRVPELLGPDD-RYLAYLPLAH---------IFELAAENVCLYRgg 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 260 ---FDAPL-----IYRliRDHG------VTHMCGAPV--------VLNMLSATNEFQP---------------------- 295
Cdd:cd17639 158 tigYGSPRtltdkSKR--GCKGdltefkPTLMVGVPAiwdtirkgVLAKLNPMGGLKRtlfwtayqsklkalkegpgtpl 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 296 LNRPV-------------NILTAGAPppaavlLRAESIGFV------ISHGYGLTETaglnVSCAWKPQWNRLpasdrar 356
Cdd:cd17639 236 LDELVfkkvraalggrlrYMLSGGAP------LSADTQEFLnivlcpVIQGYGLTET----CAGGTVQDPGDL------- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 357 LKARQGvRTVGFTEIDVVDPESGRSVERNGETVGEIVMRGSSIMLGYLKDPVGTEKALK-NGWFYTGDVGVIHSDGYLEI 435
Cdd:cd17639 299 ETGRVG-PPLPCCEIKLVDWEEGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKI 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 436 KDRSKDIIIT-GGENVSSVEVETVLYTNPAVNEVAVVARPD-VFwgetPCAFVSlksgltqrPTEVEMIEYCRKKMPKYm 513
Cdd:cd17639 378 IDRKKDLVKLqNGEYIALEKLESIYRSNPLVNNICVYADPDkSY----PVAIVV--------PNEKHLTKLAEKHGVIN- 444
|
410 420 430
....*....|....*....|....*....|....*.
gi 9759119 514 vpktvsfvDELPKT-STGKVMKFV---LREIAKKMG 545
Cdd:cd17639 445 --------SEWEELcEDKKLQKAVlksLAETARAAG 472
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
20-532 |
1.05e-27 |
|
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: 116.29 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 20 LERAATVYGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRL-TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 -DARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTTDPPILVFIADkeeeggdadvadrtkfsytyDDLIHRGDLDfkw 178
Cdd:cd17651 80 pAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGAD--------------------AEPDPALDAD--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 179 irpesewDPVVLNYTSGTTSAPKGVVHCHRgifvmSIDSLIDW------TVPKNPVYLWTLPIFHANGWSYpWGIAAVGG 252
Cdd:cd17651 137 -------DLAYVIYTSGSTGRPKGVVMPHR-----SLANLVAWqarassLGPGARTLQFAGLGFDVSVQEI-FSTLCAGA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 253 TnVCLR----KFDAPLIYRLIRDHGVTHMCGAPVVLNMLSAtnEFQPLNRPV----NILTAGAPPPAAVLLR---AESIG 321
Cdd:cd17651 204 T-LVLPpeevRTDPPALAAWLDEQRISRVFLPTVALRALAE--HGRPLGVRLaalrYLLTGGEQLVLTEDLRefcAGLPG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 322 FVISHGYGLTETAglNVSCAWKPQwnrlpASDRARLKARQGvRTVGFTEIDVVDpESGRSVERnGEtVGEIVMRGSSIML 401
Cdd:cd17651 281 LRLHNHYGPTETH--VVTALSLPG-----DPAAWPAPPPIG-RPIDNTRVYVLD-AALRPVPP-GV-PGELYIGGAGLAR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 402 GYLKDPVGTEK------ALKNGWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARP 474
Cdd:cd17651 350 GYLNRPELTAErfvpdpFVPGARMYrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLARE 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 475 DVFWGETPCAFVSlkSGLTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17651 430 DRPGEKRLVAYVV--GDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
13-534 |
5.97e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 114.32 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 13 PLTPIGFlerAATVYGDCTSIVyGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAIL 92
Cdd:PRK13383 37 PYTLLAV---TAARWPGRTAII-DDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 93 NNINTRLDARTVSVLLR-HCGSKLLFVDVFSVDLAVEAISMMTTDPPIlvfiADKEEEGGDADVADRTKfsytyddlihr 171
Cdd:PRK13383 113 VPISTEFRSDALAAALRaHHISTVVADNEFAERIAGADDAVAVIDPAT----AGAEESGGRPAVAAPGR----------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 172 gdldfkwirpesewdpVVLnYTSGTTSAPKGV-----VHCHRGIFVMSIDSLIDWTVPKNPVylwTLPIFHANGWSYPWG 246
Cdd:PRK13383 178 ----------------IVL-LTSGTTGKPKGVprapqLRSAVGVWVTILDRTRLRTGSRISV---AMPMFHGLGLGMLML 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 247 IAAVGGTNVCLRKFDAPLIYRLIRDHGVTHMCGAPVVL-------NMLSATNefqPLNRPVNILTAGAPPPAAVLLR-AE 318
Cdd:PRK13383 238 TIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLarilelpPRVRARN---PLPQLRVVMSSGDRLDPTLGQRfMD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 319 SIGFVISHGYGLTETaGLNVSCAwkpqwnrlPAsdrarlKARQGVRTVGfteidvvDPESG---RSVERNGETVG----- 390
Cdd:PRK13383 315 TYGDILYNGYGSTEV-GIGALAT--------PA------DLRDAPETVG-------KPVAGcpvRILDRNNRPVGprvtg 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 391 EIVMRGSSIMLGYLKdpvGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAV 470
Cdd:PRK13383 373 RIFVGGELAGTRYTD---GGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAV 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9759119 471 VARPDVFWGETPCAFVSLKSGLTQRPTEVEmiEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMK 534
Cdd:PRK13383 450 IGVPDERFGHRLAAFVVLHPGSGVDAAQLR--DYLKDRVSRFEQPRDINIVSSIPRNPTGKVLR 511
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
454-531 |
6.05e-26 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 101.08 E-value: 6.05e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 454 EVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGK 531
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG--VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
302-541 |
5.23e-25 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 107.77 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 302 ILTAGAPPPAAVLLRAESIGFVISHGYGLTETAGLnvSCAWKPQwnrlpasdrarlKARQGVRTVGfteidVVDPESGRS 381
Cdd:PRK07445 235 ILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQ--IATLKPD------------DFLAGNNSSG-----QVLPHAQIT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 382 VERNgeTVGEIVMRGSSIMLGY---LKDPvgtekalkNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETV 458
Cdd:PRK07445 296 IPAN--QTGNITIQAQSLALGYypqILDS--------QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 459 LYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltqrPTEVEMIEYCRK------KMPKYMVPktvsfVDELPKTSTGKV 532
Cdd:PRK07445 366 ILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP----SISLEELKTAIKdqlspfKQPKHWIP-----VPQLPRNPQGKI 436
|
....*....
gi 9759119 533 MKFVLREIA 541
Cdd:PRK07445 437 NRQQLQQIA 445
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
35-471 |
6.79e-25 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 108.66 E-value: 6.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 35 YGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSK 114
Cdd:cd17641 6 FGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 115 LLFV-DVFSVD---------------LAVEAISMMTTDPPILVFIADKEEEGGDADVADRTKfsytYDDLIHRGDLDfkw 178
Cdd:cd17641 86 VVIAeDEEQVDklleiadripsvryvIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGL----YEREVAAGKGE--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 179 irpesewDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSL-IDwtvPKNPV--YLWTLPIfhangwsyPW--------GI 247
Cdd:cd17641 159 -------DVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLaAD---PLGPGdeYVSVLPL--------PWigeqmysvGQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 248 AAVGG-----------------------------------TNVCLRKFDAPLIYRLIRDHGV--------THMCGAPV-- 282
Cdd:cd17641 221 ALVCGfivnfpeepetmmedlreigptfvllpprvwegiaADVRARMMDATPFKRFMFELGMklglraldRGKRGRPVsl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 283 ------------VLNMLSATNEFQPLNRPVnilTAGAPPPAAVLLRAESIGFVISHGYGLTETAGLNVscawkpqwnrlp 350
Cdd:cd17641 301 wlrlaswladalLFRPLRDRLGFSRLRSAA---TGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYT------------ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 351 asdrarlkarqgVRTVGFTEIDVVDPESGRSVERNGEtVGEIVMRGSSIMLGYLKDPVGT-EKALKNGWFYTGDVGVIHS 429
Cdd:cd17641 366 ------------VHRDGDVDPDTVGVPFPGTEVRIDE-VGEILVRSPGVFVGYYKNPEATaEDFDEDGWLHTGDAGYFKE 432
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 9759119 430 DGYLEIKDRSKDIIITG-GENVSSVEVETVLYTNPAVNEvAVV 471
Cdd:cd17641 433 NGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAE-AVV 474
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
42-539 |
1.19e-24 |
|
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: 106.62 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLfvdvf 121
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 122 svdlaveaismmttdppilvfiadkeeeggdadvadrtkfsytyddlihrgdldfkwIRPESEWDPVVLNYTSGTTSAPK 201
Cdd:cd17653 99 ---------------------------------------------------------LTTDSPDDLAYIIFTSGSTGIPK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 202 GVVHCHRGIFvmsidSLIDW------TVPKNPVYLWTLPIFHANGWSYpWGIAAVGGTnVCLRKFDAPLIYrLIRDHGVT 275
Cdd:cd17653 122 GVMVPHRGVL-----NYVSQpparldVGPGSRVAQVLSIAFDACIGEI-FSTLCNGGT-LVLADPSDPFAH-VARTVDAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 276 HMcgAPVVLNMLSATnEFQPLNRpvnILTAGAPPPAAvLLRAESIGFVISHGYGLTETAglnVSCAWkpqwnrlpasdrA 355
Cdd:cd17653 194 MS--TPSILSTLSPQ-DFPNLKT---IFLGGEAVPPS-LLDRWSPGRRLYNAYGPTECT---ISSTM------------T 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 356 RLKARQGV---RTVGFTEIDVVDPESGRSVErngETVGEIVMRGSSIMLGYLKDPVGTEKALKNGWFY-------TGDVG 425
Cdd:cd17653 252 ELLPGQPVtigKPIPNSTCYILDADLQPVPE---GVVGEICISGVQVARGYLGNPALTASKFVPDPFWpgsrmyrTGDYG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 426 VIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTN-PAVNEVAVVARPDVFwgetpCAFVslksglTQRPTEVEMI-E 503
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSqPEVTQAAAIVVNGRL-----VAFV------TPETVDVDGLrS 397
|
490 500 510
....*....|....*....|....*....|....*.
gi 9759119 504 YCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd17653 398 ELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
139-470 |
2.50e-24 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 107.21 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 139 ILVFIADKEEEggdADVADRTKF-SYTYDDLIHRGDLDFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRG--IFVMSI 215
Cdd:PLN02430 176 IVSFTSVTEEE---SDKASQIGVkTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAvaTFVRGV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 216 DSLIDWTVPK---NPVYLWTLPIFH----ANGWSYPWGIAAVG---GTNVCLRKfDapliyrlIRDHGVTHMCGAPVVLN 285
Cdd:PLN02430 253 DLFMEQFEDKmthDDVYLSFLPLAHildrMIEEYFFRKGASVGyyhGDLNALRD-D-------LMELKPTLLAGVPRVFE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 286 -----MLSATNEFQPLNR------------------------PVN------------------ILTAGAPPPAAV--LLR 316
Cdd:PLN02430 325 rihegIQKALQELNPRRRlifnalykyklawmnrgyshkkasPMAdflafrkvkaklggrlrlLISGGAPLSTEIeeFLR 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 317 AESIGFVIsHGYGLTETAGLNVSCawkpqwnrLPasDRARLKARQGVRTVgFTEIDVVD-PESGRSVERNgETVGEIVMR 395
Cdd:PLN02430 405 VTSCAFVV-QGYGLTETLGPTTLG--------FP--DEMCMLGTVGAPAV-YNELRLEEvPEMGYDPLGE-PPRGEICVR 471
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 396 GSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDII-ITGGENVSSVEVETVLYTNPAVNEVAV 470
Cdd:PLN02430 472 GKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPIVEDIWV 547
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
186-543 |
5.65e-24 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 106.97 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIF--VMSIDSLIDWTVpkNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLrkFDAP 263
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRNLLanRAQVAARIDFSP--EDKVFNALPVFHSFGLTGGLVLPLLSGVKVFL--YPSP 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 264 LIYR----LIRDHGVTHMCGAPVVLNMLSATN---EFqplnRPVNILTAGAPP--PAAVLLRAESIGFVISHGYGLTETA 334
Cdd:PRK06814 870 LHYRiipeLIYDTNATILFGTDTFLNGYARYAhpyDF----RSLRYVFAGAEKvkEETRQTWMEKFGIRILEGYGVTETA 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 335 ---GLNVscawkPQWNR-------LPASDrARLKARQGVrtvgfteidvvdPESGRsverngetvgeIVMRGSSIMLGYL 404
Cdd:PRK06814 946 pviALNT-----PMHNKagtvgrlLPGIE-YRLEPVPGI------------DEGGR-----------LFVRGPNVMLGYL 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 405 K-DPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETvlytnpAVNEV------AVVARPDVF 477
Cdd:PRK06814 997 RaENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE------LAAELwpdalhAAVSIPDAR 1070
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9759119 478 WGETpcafVSLksgLTQRP--TEVEMIEYCRKK-MPKYMVPKTVSFVDELPKTSTGK-----VMKFVLREIAKK 543
Cdd:PRK06814 1071 KGER----IIL---LTTASdaTRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKidyvaVTKLAEEAAAKP 1137
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
38-494 |
5.97e-24 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 104.95 E-value: 5.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 38 NTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGskLLF 117
Cdd:PRK09029 26 DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLT--LDF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 118 VDVFSVDLAVEAISMMTTDPPILVfiadkeeeggdadvadrtkfsytyddlihrgdldfkwirPESEWDP---VVLNYTS 194
Cdd:PRK09029 104 ALVLEGENTFSALTSLHLQLVEGA---------------------------------------HAVAWQPqrlATMTLTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 195 GTTSAPKGVVHCHR-------GIF-VMSIDSLIDWtvpknpvyLWTLPIFHANGWSYPWGIAAVGGTNVcLRKfDAPLIY 266
Cdd:PRK09029 145 GSTGLPKAAVHTAQahlasaeGVLsLMPFTAQDSW--------LLSLPLFHVSGQGIVWRWLYAGATLV-VRD-KQPLEQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 267 RLirdHGVTHMCGAPVVLNMLSATNEFQPLNRpvNILTAGAPPPAAVLLRAESIGFVISHGYGLTETAglnvS--CAwkp 344
Cdd:PRK09029 215 AL---AGCTHASLVPTQLWRLLDNRSEPLSLK--AVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMA----StvCA--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 345 qwnrlpasdrarlKARQGVRTVGFT----EIDVVDpesgrsverngetvGEIVMRGSSIMLGYLKDpvGTEKALKN--GW 418
Cdd:PRK09029 283 -------------KRADGLAGVGSPlpgrEVKLVD--------------GEIWLRGASLALGYWRQ--GQLVPLVNdeGW 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 419 FYTGDVGVIHsDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQ 494
Cdd:PRK09029 334 FATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAV 408
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
42-507 |
1.08e-23 |
|
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: 105.13 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDVf 121
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 122 svDLAVEAISMMTTDPPILVFIADKEEEggdadVADRTKFSYTYDDLIHRGDLDfkwirPESEWDPV----------VLN 191
Cdd:cd05933 89 --QKQLQKILQIQDKLPHLKAIIQYKEP-----LKEKEPNLYSWDEFMELGRSI-----PDEQLDAIissqkpnqccTLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRGI------FVMSIDsLIDWTVPKNPVYLWtLPIFHANGWSYP-WGIAAVGGTnVCLRKFDA-- 262
Cdd:cd05933 157 YTSGTTGMPKGVMLSHDNItwtakaASQHMD-LRPATVGQESVVSY-LPLSHIAAQILDiWLPIKVGGQ-VYFAQPDAlk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 263 -PLIyRLIRDHGVTHMCGAPVVLN-----------------------------------MLSATNEFQP----------- 295
Cdd:cd05933 234 gTLV-KTLREVRPTAFMGVPRVWEkiqekmkavgaksgtlkrkiaswakgvgletnlklMGGESPSPLFyrlakklvfkk 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 296 ------LNRPVNILTAGAPPPAAVLLRAESIGFVISHGYGLTETAGLNVSCawKPQWNRLPASDrarlKARQGVRTvgft 369
Cdd:cd05933 313 vrkalgLDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTIS--NPQAYRLLSCG----KALPGCKT---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 370 eidvvdpesgRSVERNGETVGEIVMRGSSIMLGYLKDPVGTEKALK-NGWFYTGDVGVIHSDGYLEIKDRSKDIIIT-GG 447
Cdd:cd05933 383 ----------KIHNPDADGIGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKELIITaGG 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9759119 448 ENVSSVEVETVLYTN-PAVNEVAVVARPDVFWgetpCAFVSLKSGLTQRPTE------VEMIEYCRK 507
Cdd:cd05933 453 ENVPPVPIEDAVKKElPIISNAMLIGDKRKFL----SMLLTLKCEVNPETGEpldeltEEAIEFCRK 515
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
29-532 |
1.16e-23 |
|
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: 104.28 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 29 DCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLL 108
Cdd:cd12114 2 DATAVICGDGTL-TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 109 RHCGSKLLFVDvfSVDLAVEaismmttDPPILVFIADKEEEGGDADVADRtkfsytyddlihRGDLDfkwirpesewDPV 188
Cdd:cd12114 81 ADAGARLVLTD--GPDAQLD-------VAVFDVLILDLDALAAPAPPPPV------------DVAPD----------DLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 189 VLNYTSGTTSAPKGVVHCHRGIF-----------------VMSIDSL-IDWTVpknpvylwtLPIFhangwsypwGIAAV 250
Cdd:cd12114 130 YVIFTSGSTGTPKGVMISHRAALntildinrrfavgpddrVLALSSLsFDLSV---------YDIF---------GALSA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 251 GGTNV---CLRKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEfQPLNRPvniltagaPPPAAVLLraesigfvishg 327
Cdd:cd12114 192 GATLVlpdEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLE-AAQALL--------PSLRLVLL------------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 328 ygltetaglnvSCAWKPQwnRLPASDRARLKARQGVRTVGFTE---------IDVVDPE-------------SGRSVERN 385
Cdd:cd12114 251 -----------SGDWIPL--DLPARLRALAPDARLISLGGATEasiwsiyhpIDEVPPDwrsipygrplanqRYRVLDPR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 386 GE-----TVGEIVMRGSSIMLGYLKDPVGTEK-----ALKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEV 455
Cdd:cd12114 318 GRdcpdwVPGELWIGGRGVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEI 397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9759119 456 ETVLYTNPAVNEVAVVARPDVFwGETPCAFVSLKSGLTQrPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd12114 398 EAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPDNDGTP-IAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
13-542 |
2.23e-23 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 103.92 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 13 PLTPIgfLERAATvyGDCTSIVYGSNTvYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFA------VP 86
Cdd:PRK10946 26 PLTDI--LTRHAA--SDAIAVICGERQ-FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFAllklgvAP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 87 MSgAILNNINTRLDArtvsvLLRHCGSKLLFVD----VFSVDLAVEAISMMTTDPPILVFIADKEEEGgdadvadrtkfs 162
Cdd:PRK10946 101 VN-ALFSHQRSELNA-----YASQIEPALLIADrqhaLFSDDDFLNTLVAEHSSLRVVLLLNDDGEHS------------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 163 ytYDDLIHRGDLDFkWIRPeSEWDPVVLNYTSG-TTSAPKGVVHCH--------RGIFVMSIDSlidwtvpkNPVYLWTL 233
Cdd:PRK10946 163 --LDDAINHPAEDF-TATP-SPADEVAFFQLSGgSTGTPKLIPRTHndyyysvrRSVEICGFTP--------QTRYLCAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 234 PIFHANGWSYP--WGIAAVGGTNVCLRKFDAPLIYRLIRDHGVThMCG--APVVLNMLSATNEFQPLN--RPVNILTAGA 307
Cdd:PRK10946 231 PAAHNYPMSSPgaLGVFLAGGTVVLAPDPSATLCFPLIEKHQVN-VTAlvPPAVSLWLQAIAEGGSRAqlASLKLLQVGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 308 PPPAAVLLR--AESIGFVISHGYGLTEtaGL-NvscawkpqWNRLPASDRaRLKARQGVRTVGFTEIDVVDpESGRSVER 384
Cdd:PRK10946 310 ARLSETLARriPAELGCQLQQVFGMAE--GLvN--------YTRLDDSDE-RIFTTQGRPMSPDDEVWVAD-ADGNPLPQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 385 nGETvGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNP 463
Cdd:PRK10946 378 -GEV-GRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHP 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 464 AVNEVAVVARPDVFWGETPCAFVSLKSGLtqRPteVEMIEYCRKK-MPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAK 542
Cdd:PRK10946 456 AVIHAALVSMEDELMGEKSCAFLVVKEPL--KA--VQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLA 531
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
42-539 |
6.05e-23 |
|
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: 101.66 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTvsvlLRHCgskllfvdvf 121
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGES----LAHC---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 122 sVDLAveaismmttDPPILVFiadkeeeggdadvadrtkfsytyddlihrgdldfkwirpesewDPVVLNYTSGTTSAPK 201
Cdd:cd05940 71 -LNVS---------SAKHLVV-------------------------------------------DAALYIYTSGTTGLPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 202 GVVHCHR-----GIFVMSidSLIdwTVPKNPVYLwTLPIFHANGWSYPWGIAAVGGTNVCLR-KFDAPLIYRLIRDHGVT 275
Cdd:cd05940 98 AAIISHRrawrgGAFFAG--SGG--ALPSDVLYT-CLPLYHSTALIVGWSACLASGATLVIRkKFSASNFWDDIRKYQAT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 276 ----------HMCGAPVVlnmlsatnefqPLNRPVN---ILTAGapppaavlLRAESIG-----FVISH---GYGLTE-T 333
Cdd:cd05940 173 ifqyigelcrYLLNQPPK-----------PTERKHKvrmIFGNG--------LRPDIWEefkerFGVPRiaeFYAATEgN 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 334 AGLnvscawkpqWNRlPASDRARLKARQGVRTVGFTEIDVVDPESGRSVeRN-------------GETVGEIVMRGSSIm 400
Cdd:cd05940 234 SGF---------INF-FGKPGAIGRNPSLLRKVAPLALVKYDLESGEPI-RDaegrcikvprgepGLLISRINPLEPFD- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 401 lGYLkDPVGTEK-----ALKNG--WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAV--V 471
Cdd:cd05940 302 -GYT-DPAATEKkilrdVFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygV 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9759119 472 ARPDVFwGETPCAFVSLKSGltqRPTEVE-MIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05940 380 QVPGTD-GRAGMAAIVLQPN---EEFDLSaLAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
192-532 |
1.42e-22 |
|
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: 100.40 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRGIFVMSiDSLIDW--TVPKNPVYLWTLPIFHANGWSYpWGIAAVGGTNVC----LRKFDAPLI 265
Cdd:cd17652 100 YTSGSTGRPKGVVVTHRGLANLA-AAQIAAfdVGPGSRVLQFASPSFDASVWEL-LMALLAGATLVLapaeELLPGEPLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 266 yRLIRDHGVTHMCGAPVVLNMLSATNefqpLNRPVNILTAGAPPPAAvLLRAESIGFVISHGYGLTETAglnVSCAWKPq 345
Cdd:cd17652 178 -DLLREHRITHVTLPPAALAALPPDD----LPDLRTLVVAGEACPAE-LVDRWAPGRRMINAYGPTETT---VCATMAG- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 346 wnrlPASDRARLKArqGvRTVGFTEIDVVDPESgRSVErNGEtVGEIVMRGSSIMLGYLKDPVGT-EKALKN------GW 418
Cdd:cd17652 248 ----PLPGGGVPPI--G-RPVPGTRVYVLDARL-RPVP-PGV-PGELYIAGAGLARGYLNRPGLTaERFVADpfgapgSR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 419 FY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPT 497
Cdd:cd17652 318 MYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPG--AAPT 395
|
330 340 350
....*....|....*....|....*....|....*
gi 9759119 498 EVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17652 396 AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
28-532 |
4.51e-22 |
|
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: 99.29 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 28 GDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAIlnnintrldartvsvl 107
Cdd:cd12116 1 PDATAVRDDDRSL-SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAA---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 108 lrhcgskllFVDVfSVDLAVEAISMMTTDP-PILVFIADKEEEGGDADVAdrtkfsyTYDDLIHRGDLDFKWIRPE-SEW 185
Cdd:cd12116 64 ---------YVPL-DPDYPADRLRYILEDAePALVLTDDALPDRLPAGLP-------VLLLALAAAAAAPAAPRTPvSPD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGI--FVMSI---------DSLIDWTvpknpvylwtlpifhangwSYPWGIAA----- 249
Cdd:cd12116 127 DLAYVIYTSGSTGRPKGVVVSHRNLvnFLHSMrerlglgpgDRLLAVT-------------------TYAFDISLlelll 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 250 ---VGGTNVCLRK---FDAPLIYRLIRDHGVTHMCGAPVVLNMLsATNEFQPLnRPVNILTAG-APPP---AAVLLRAES 319
Cdd:cd12116 188 pllAGARVVIAPRetqRDPEALARLIEAHSITVMQATPATWRML-LDAGWQGR-AGLTALCGGeALPPdlaARLLSRVGS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 320 IGFVishgYGLTETAglnvscAWkpqwnrlpaSDRARLKARQGVRTVGF----TEIDVVDpESGRSVERnGEtVGEIVMR 395
Cdd:cd12116 266 LWNL----YGPTETT------IW---------STAARVTAAAGPIPIGRplanTQVYVLD-AALRPVPP-GV-PGELYIG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 396 GSSIMLGYLKDPVGTEK------ALKNG--WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNE 467
Cdd:cd12116 324 GDGVAQGYLGRPALTAErfvpdpFAGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQ 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9759119 468 VAVVARPDvfwGETP--CAFVSLKSGLTqrPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd12116 404 AAVVVRED---GGDRrlVAYVVLKAGAA--PDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
186-540 |
5.20e-22 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 99.66 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYpWGIAAV--GGTNV------CL 257
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVE-LHLRAVylGCQQVhvpteeIL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 RkfDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQP-----LNRPVNILTAGAPPPAAV---LLRA-ESIG---FVIS 325
Cdd:cd05906 247 A--DPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEdgtwdLSSLRYLVNAGEAVVAKTirrLLRLlEPYGlppDAIR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 326 HGYGLTET-AGLNvscawkpqWNRLPASDRARlkarQGVRTV-------GFtEIDVVDPEsGRSVERngETVGEIVMRGS 397
Cdd:cd05906 325 PAFGMTETcSGVI--------YSRSFPTYDHS----QALEFVslgrpipGV-SMRIVDDE-GQLLPE--GEVGRLQVRGP 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 398 SIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHsDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNP--AVNEVAVVA-R 473
Cdd:cd05906 389 VVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPgvEPSFTAAFAvR 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9759119 474 PDVFWGETPCAFVSLKSGLTQRPteVEMIEYCRKKM-------PKYMVPKTvsfVDELPKTSTGKVMKFVLREI 540
Cdd:cd05906 468 DPGAETEELAIFFVPEYDLQDAL--SETLRAIRSVVsrevgvsPAYLIPLP---KEEIPKTSLGKIQRSKLKAA 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
186-532 |
6.30e-22 |
|
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: 98.53 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGifVMSIDSLIDWTVPKNPVYLWTLpiFHANGWSYP----WGIAAVGGTNVCLRKF- 260
Cdd:cd17643 94 DLAYVIYTSGSTGRPKGVVVSHAN--VLALFAATQRWFGFNEDDVWTL--FHSYAFDFSvweiWGALLHGGRLVVVPYEv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 261 --DAPLIYRLIRDHGVThmcgapvVLNML-SAtneFQPLNRPVNILTAGAPPPAAVLLRAESI------GFVISHG---- 327
Cdd:cd17643 170 arSPEDFARLLRDEGVT-------VLNQTpSA---FYQLVEAADRDGRDPLALRYVIFGGEALeaamlrPWAGRFGldrp 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 328 -----YGLTETAglnVSCAWKPqwnrLPASDrARLKARQGV-RTVGFTEIDVVDpESGRSVERNGetVGEIVMRGSSIML 401
Cdd:cd17643 240 qlvnmYGITETT---VHVTFRP----LDAAD-LPAAAASPIgRPLPGLRVYVLD-ADGRPVPPGV--VGELYVSGAGVAR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 402 GYLKDPvgtekALKNGWF------------Y-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEV 468
Cdd:cd17643 309 GYLGRP-----ELTAERFvanpfggpgsrmYrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDA 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9759119 469 AVVARPDVFWGETPCAFVSLKSGLTQRPTEVEmiEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17643 384 AVIVREDEPGDTRLVAYVVADDGAAADIAELR--ALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
163-470 |
1.55e-21 |
|
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: 98.06 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 163 YTYDDLIHRGDLD-FKWIRPESEwDPVVLNYTSGTTSAPKGVVHCHRGI--FVMSIDSLIDWTVPKNP--VYLWTLPIFH 237
Cdd:cd05927 92 YSLEEFEKLGKKNkVPPPPPKPE-DLATICYTSGTTGNPKGVMLTHGNIvsNVAGVFKILEILNKINPtdVYISYLPLAH 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 238 ANGWSYPWGIAAVGGtnvCLRKFDAPLiyRLIRDHGV----THMCGAPVVLNML-------------------------- 287
Cdd:cd05927 171 IFERVVEALFLYHGA---KIGFYSGDI--RLLLDDIKalkpTVFPGVPRVLNRIydkifnkvqakgplkrklfnfalnyk 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 288 -SATNEFQPLNRPV------------------NILTAGAPPPAAVLLRAESI-GFVISHGYGLTETAGLnVSCAWKPQWN 347
Cdd:cd05927 246 lAELRSGVVRASPFwdklvfnkikqalggnvrLMLTGSAPLSPEVLEFLRVAlGCPVLEGYGQTECTAG-ATLTLPGDTS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 348 rlpasdrarlkarqgVRTVG----FTEIDVVD-PESGRSVER-NGEtvGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFY 420
Cdd:cd05927 325 ---------------VGHVGgplpCAEVKLVDvPEMNYDAKDpNPR--GEVCIRGPNVFSGYYKDPEKTAEALdEDGWLH 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 421 TGDVGVIHSDGYLEIKDRSKDII-ITGGENVSSVEVETVLYTNPAVNEVAV 470
Cdd:cd05927 388 TGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV 438
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
192-532 |
3.79e-21 |
|
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: 96.32 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRGIfVMSIDSLIDWTVPKNPVYLWTLpiFHANgwsYPWG-------IAAVGGTNVCL----RKF 260
Cdd:cd17648 101 YTSGTTGKPKGVLVEHGSV-VNLRTSLSERYFGRDNGDEAVL--FFSN---YVFDffveqmtLALLNGQKLVVppdeMRF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 261 DAPLIYRLIRDHGVTHMCGAPVVLNMLsatnEFQPLNRPVNILTAGAPPPAAVL--LRAESIGFVIShGYGLTETAGLNV 338
Cdd:cd17648 175 DPDRFYAYINREKVTYLSGTPSVLQQY----DLARLPHLKRVDAAGEEFTAPVFekLRSRFAGLIIN-AYGPTETTVTNH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 339 ScawkpqwNRLPASDRARLKARQGVRTvgfTEIDVVDPESGRsVERNGetVGEIVMRGSSIMLGYLKDPVGT-------- 410
Cdd:cd17648 250 K-------RFFPGDQRFDKSLGRPVRN---TKCYVLNDAMKR-VPVGA--VGELYLGGDGVARGYLNRPELTaerflpnp 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 411 -----EKAL-KNGWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETP- 482
Cdd:cd17648 317 fqteqERARgRNARLYkTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRi 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 483 -----CAFVSLKSGLTqrptEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17648 397 qkylvGYYLPEPGHVP----ESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
19-532 |
6.86e-21 |
|
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: 95.86 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 19 FLERAATVyGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTR 98
Cdd:cd17655 3 FEEQAEKT-PDHTAVVFEDQTL-TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 99 LDARTVSVLLRHCGSKLLfvdvfsvdLAVEAIsmmttDPPILvFIadkeeegGDAD-VADRTKFSYTYDDLIHRGDLDfk 177
Cdd:cd17655 81 YPEERIQYILEDSGADIL--------LTQSHL-----QPPIA-FI-------GLIDlLDEDTIYHEESENLEPVSKSD-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 178 wirpesewDPVVLNYTSGTTSAPKGVVHCHRGIfvmsiDSLIDW---TVPKNP---VYLWTLPIFHANGWS-YPwgIAAV 250
Cdd:cd17655 138 --------DLAYVIYTSGSTGKPKGVMIEHRGV-----VNLVEWankVIYQGEhlrVALFASISFDASVTEiFA--SLLS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 251 GGTNVCLRK---FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATN--EFQPLNRpvnILTAG-APPPAAV--LLRAESIGF 322
Cdd:cd17655 203 GNTLYIVRKetvLDGQALTQYIRQNRITIIDLTPAHLKLLDAADdsEGLSLKH---LIVGGeALSTELAkkIIELFGTNP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 323 VISHGYGLTETAglnVSCAWkpqWNRLPASDRarlKARQGV-RTVGFTEIDVVDpESGRSVERnGEtVGEIVMRGSSIML 401
Cdd:cd17655 280 TITNAYGPTETT---VDASI---YQYEPETDQ---QVSVPIgKPLGNTRIYILD-QYGRPQPV-GV-AGELYIGGEGVAR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 402 GYLKDPVGTEKALKNGWF------Y-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARP 474
Cdd:cd17655 348 GYLNRPELTAEKFVDDPFvpgermYrTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARK 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 475 DVFWGETPCAFVSLKSGLTQRptevEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17655 428 DEQGQNYLCAYIVSEKELPVA----QLREFLARELPDYMIPSYFIKLDEIPLTPNGKV 481
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
372-542 |
1.17e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 95.59 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 372 DVVDpESGRSVERNGEtvGEIVMRGS--SIMLGYLKDP-------VGTEKalknGWFYTGDVGVIHSDGYLEIKDRSKDI 442
Cdd:PRK00174 436 AVVD-EEGNPLEGGEG--GNLVIKDPwpGMMRTIYGDHerfvktyFSTFK----GMYFTGDGARRDEDGYYWITGRVDDV 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 443 IITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTqrPTEV---EMIEYCRKKMPKYMVPKTVS 519
Cdd:PRK00174 509 LNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEE--PSDElrkELRNWVRKEIGPIAKPDVIQ 586
|
170 180
....*....|....*....|...
gi 9759119 520 FVDELPKTSTGKVMKFVLREIAK 542
Cdd:PRK00174 587 FAPGLPKTRSGKIMRRILRKIAE 609
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
186-532 |
2.67e-20 |
|
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: 93.54 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRgifvmSIDSLIDWTvpknpvylwtLPIFHANGWSypwgiAAVGGTNVClrkFDAPlI 265
Cdd:cd12115 106 DLAYVIYTSGSTGRPKGVAIEHR-----NAAAFLQWA----------AAAFSAEELA-----GVLASTSIC---FDLS-V 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 266 YRLIrdhgVTHMCGAPVVLnmlsATNEFQPLNRP----VNILTAgAPPPAAVLLRAESIgfvishgyglteTAGLNVSC- 340
Cdd:cd12115 162 FELF----GPLATGGKVVL----ADNVLALPDLPaaaeVTLINT-VPSAAAELLRHDAL------------PASVRVVNl 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 341 AWKPQWNRLPASDRARLKARQGVRTVGFTE------IDVVDPESGRSV--------------ERNGE-----TVGEIVMR 395
Cdd:cd12115 221 AGEPLPRDLVQRLYARLQVERVVNLYGPSEdttystVAPVPPGASGEVsigrplantqayvlDRALQpvplgVPGELYIG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 396 GSSIMLGYLKDPVGT-EKALKNGWF-----Y-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEV 468
Cdd:cd12115 301 GAGVARGYLGRPGLTaERFLPDPFGpgarlYrTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9759119 469 AVVARPDVFWGETPCAFVSLKSGLTqrPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd12115 381 VVVAIGDAAGERRLVAYIVAEPGAA--GLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKI 442
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
179-541 |
7.91e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 93.24 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 179 IRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIF--VMSIDSLIDWTvpKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVC 256
Cdd:PRK08043 359 QVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLanVEQIKTIADFT--PNDRFMSALPLFHSFGLTVGLFTPLLTGAEVF 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 257 LrkFDAPLIYR----LIRDHGVTHMCGAPVVLN---MLSATNEFQPLNRPVniltAGAPP--PAAVLLRAESIGFVISHG 327
Cdd:PRK08043 437 L--YPSPLHYRivpeLVYDRNCTVLFGTSTFLGnyaRFANPYDFARLRYVV----AGAEKlqESTKQLWQDKFGLRILEG 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 328 YGLTETA---GLNVSCAWKPQW-NR-LPASDrARLKARQGVrtvgfteidvvdpESGrsverngetvGEIVMRGSSIMLG 402
Cdd:PRK08043 511 YGVTECApvvSINVPMAAKPGTvGRiLPGMD-ARLLSVPGI-------------EQG----------GRLQLKGPNIMNG 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 403 YLK-------DPVGTEKA---LKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVA 472
Cdd:PRK08043 567 YLRvekpgvlEVPTAENArgeMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAI 646
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 473 RPDVFWGETPCAFVSlKSGLTQRptevEMIEYCRKK-MPKYMVPKTVSFVDELPKTSTGKVMKFVLREIA 541
Cdd:PRK08043 647 KSDASKGEALVLFTT-DSELTRE----KLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMV 711
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
186-474 |
1.10e-19 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 92.87 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIF-----VMSIdslidwtVPK---NPVYLWTLPIFHANGWSYPWGIAAVG-----G 252
Cdd:PLN02387 251 DIAVIMYTSGSTGLPKGVMMTHGNIVatvagVMTV-------VPKlgkNDVYLAYLPLAHILELAAESVMAAVGaaigyG 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 253 TNVCL----------RKFDA-----------PLIYRLIRDhGVTHMCGAPVVL----------NMLSATNE--------- 292
Cdd:PLN02387 324 SPLTLtdtsnkikkgTKGDAsalkptlmtavPAILDRVRD-GVRKKVDAKGGLakklfdiaykRRLAAIEGswfgawgle 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 293 --------FQPLNRPVN-----ILTAGAPppaavlLRAES-------IGFVISHGYGLTET-AGLNVScawkpQWNrlpa 351
Cdd:PLN02387 403 kllwdalvFKKIRAVLGgrirfMLSGGAP------LSGDTqrfinicLGAPIGQGYGLTETcAGATFS-----EWD---- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 352 sDRArlkarqgVRTVG----FTEIDVVD-PESGRSVERNGETVGEIVMRGSSIMLGYLKDPVGTEKALK---NG--WFYT 421
Cdd:PLN02387 468 -DTS-------VGRVGpplpCCYVKLVSwEEGGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKvdeRGmrWFYT 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 9759119 422 GDVGVIHSDGYLEIKDRSKDII-ITGGENVSSVEVETVLYTNPAVNEVAVVARP 474
Cdd:PLN02387 540 GDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAALSVSPYVDNIMVHADP 593
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
41-539 |
1.19e-19 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 91.72 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 41 YTWRETNLRCLRVASSL-SSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVD 119
Cdd:cd05937 6 WTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 120 vfsvdlaveaismmttdppilvfiadkeeeggdadvadrtkfsytyDDlihrgdldfkwirpesewDPVVLNYTSGTTSA 199
Cdd:cd05937 86 ----------------------------------------------PD------------------DPAILIYTSGTTGL 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 200 PKGVvhchrgIFVMSIDSLIDWTVP-----KNPVYLWT-LPIFHANGWSYPWGIAAVGGTNVCL-RKFDAPLIYRLIRDH 272
Cdd:cd05937 102 PKAA------AISWRRTLVTSNLLShdlnlKNGDRTYTcMPLYHGTAAFLGACNCLMSGGTLALsRKFSASQFWKDVRDS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 273 GVTHMCGAPVVLNMLSATNEfQPLNRPVNILTA---GAPPPAAVLLRaESIGF-VISHGYGLTEtaglNVSCAWKPQWNR 348
Cdd:cd05937 176 GATIIQYVGELCRYLLSTPP-SPYDRDHKVRVAwgnGLRPDIWERFR-ERFNVpEIGEFYAATE----GVFALTNHNVGD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 349 LPASDRA------RLKARQGVRTVGF---TEIDVVDPESGRSVERNGETVGEIVMR----GSSIMLGYLKDPVGTEKAL- 414
Cdd:cd05937 250 FGAGAIGhhglirRWKFENQVVLVKMdpeTDDPIRDPKTGFCVRAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLv 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 415 ----KNG--WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAV--VARPDvFWGETPCAFV 486
Cdd:cd05937 330 rdvfRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPG-HDGRAGCAAI 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 487 SLKSGLTQRPTEV--EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05937 409 TLEESSAVPTEFTksLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
302-546 |
2.87e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 89.33 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 302 ILTAGAPPPAAVLLRAESIGFVISHGYGLTETAGlnvSCAWkpqwnrlpasdrarlkarQGVRTVGfTEIDVVDpesgrs 381
Cdd:PRK07824 156 VLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSG---GCVY------------------DGVPLDG-VRVRVED------ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 382 verngetvGEIVMRGSSIMLGYlKDPVGTEKALKNGWFYTGDVGVIHsDGYLEIKDRSKDIIITGGENVSSVEVETVLYT 461
Cdd:PRK07824 208 --------GRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALAT 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 462 NPAVNEVAVVARPDVFWGETPCAFVSLKSGLTqrPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKfvlREIA 541
Cdd:PRK07824 278 HPAVADCAVFGLPDDRLGQRVVAAVVGDGGPA--PTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDR---RALV 352
|
....*
gi 9759119 542 KKMGT 546
Cdd:PRK07824 353 RRFAG 357
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
192-538 |
1.03e-18 |
|
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: 88.96 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVV--------HCH--RGIFVMSIDsliDWTVPKNPVylwTLPIFHaNGWSYPWgiaAVGGTnVCLRkfD 261
Cdd:cd17649 101 YTSGSTGTPKGVAvshgplaaHCQatAERYGLTPG---DRELQFASF---NFDGAH-EQLLPPL---ICGAC-VVLR--P 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 262 APL------IYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVN---ILTAGAPPPAAVLLRAESIGFVISHGYGLTE 332
Cdd:cd17649 168 DELwasadeLAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSlrlYIFGGEALSPELLRRWLKAPVRLFNAYGPTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 TagLNVSCAWKPqwnrlpASDRARLKARQGV-RTVGFTEIDVVDpESGRSVErNGETvGEIVMRGSSIMLGYLK------ 405
Cdd:cd17649 248 A--TVTPLVWKC------EAGAARAGASMPIgRPLGGRSAYILD-ADLNPVP-VGVT-GELYIGGEGLARGYLGrpelta 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 406 -----DPVGTEKALkngWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFwGE 480
Cdd:cd17649 317 erfvpDPFGAPGSR---LYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GK 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 481 TPCAFVSLKSGLTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd17649 393 QLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
38-532 |
3.18e-18 |
|
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: 87.14 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 38 NTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLF 117
Cdd:cd17650 10 TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 118 VDvfsvdlaveaismmttdppilvfiadkeeeggdadvadrtkfsytyddlihrgdldfkwirPEsewDPVVLNYTSGTT 197
Cdd:cd17650 90 TQ-------------------------------------------------------------PE---DLAYVIYTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 198 SAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAV-GGTNV-CLR--KFDAPLIYRLIRDHG 273
Cdd:cd17650 106 GKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLnGGTLViCPDevKLDPAALYDLILKSR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 274 VTHMCGAPVVLNMLSAT---NEFQPLNRPVNILTAGAPPPA--AVLLRAESIGFVISHGYGLTETAglNVSCAWKPQWNR 348
Cdd:cd17650 186 ITLMESTPALIRPVMAYvyrNGLDLSAMRLLIVGSDGCKAQdfKTLAARFGQGMRIINSYGVTEAT--IDSTYYEEGRDP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 349 LPASDRARLKarqgvRTVGFTEIDVVDPEsgRSVERNGeTVGEIVMRGSSIMLGYLKDPVGT-EKALKNGW------FYT 421
Cdd:cd17650 264 LGDSANVPIG-----RPLPNTAMYVLDER--LQPQPVG-VAGELYIGGAGVARGYLNRPELTaERFVENPFapgermYRT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 422 GDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRptevEM 501
Cdd:cd17650 336 GDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTA----EL 411
|
490 500 510
....*....|....*....|....*....|.
gi 9759119 502 IEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17650 412 RAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
173-532 |
1.21e-17 |
|
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: 86.83 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 173 DLDFKWIRPESEWDPVVLN---------YTSGTTSAPKGVVHCHRGIfVMSIDSLIDW-TVPKNPVYLWTLPI-FHANGW 241
Cdd:COG1020 596 ALDALALAAEPATNPPVPVtpddlayviYTSGSTGRPKGVMVEHRAL-VNLLAWMQRRyGLGPGDRVLQFASLsFDASVW 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 242 SYpWGIAAVGGTNVCLRK---FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATnEFQPLNRPVNILTAG-APPPAAV-LLR 316
Cdd:COG1020 675 EI-FGALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDA-APEALPSLRLVLVGGeALPPELVrRWR 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 317 AESIGFVISHGYGLTETAglnVSCAWKPqwnrLPASDrarlkARQGVRTVGF----TEIDVVDpESGRSVeRNGEtVGEI 392
Cdd:COG1020 753 ARLPGARLVNLYGPTETT---VDSTYYE----VTPPD-----ADGGSVPIGRpianTRVYVLD-AHLQPV-PVGV-PGEL 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 393 VMRGSSIMLGYLKDPVGTEKA------LKNG--WFYTGDVGVIHSDGYLEIKDRS----KdiiITG-----GenvssvEV 455
Cdd:COG1020 818 YIGGAGLARGYLNRPELTAERfvadpfGFPGarLYRTGDLARWLPDGNLEFLGRAddqvK---IRGfrielG------EI 888
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9759119 456 ETVLYTNPAVNEVAVVARPDVfwGETP--CAFVSLKSGLTQRPTEVEMIEycRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:COG1020 889 EAALLQHPGVREAVVVAREDA--PGDKrlVAYVVPEAGAAAAAALLRLAL--ALLLPPYMVPAAVVLLLPLPLTGNGKL 963
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
21-532 |
1.60e-17 |
|
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: 85.22 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 21 ERAATVYGDCTsivygsntvYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLD 100
Cdd:cd17656 3 DAVAVVFENQK---------LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 101 ARTVSVLLRHCGSKLLFVdvfsvdlAVEAISMMTTDPPILVFIADKEEEGGDADVadrtKFSYTYDDLIHrgdldfkwir 180
Cdd:cd17656 74 EERRIYIMLDSGVRVVLT-------QRHLKSKLSFNKSTILLEDPSISQEDTSNI----DYINNSDDLLY---------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 181 pesewdpvvLNYTSGTTSAPKGVVHCHRgifvmSIDSLIDWTVPK------NPVYLWTLPIFHAngwSYPWGIAAV--GG 252
Cdd:cd17656 133 ---------IIYTSGTTGKPKGVQLEHK-----NMVNLLHFEREKtninfsDKVLQFATCSFDV---CYQEIFSTLlsGG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 253 TNVCLR---KFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEF-QPLNRPV-NILTAGApppaAVLLRAESIGFVISHG 327
Cdd:cd17656 196 TLYIIReetKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFiNRFPTCVkHIITAGE----QLVITNEFKEMLHEHN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 328 ------YGLTETAgLNVSCAWKPQ--WNRLPASDRArlkarqgvrtVGFTEIDVVDPEsgRSVERNGeTVGEIVMRGSSI 399
Cdd:cd17656 272 vhlhnhYGPSETH-VVTTYTINPEaeIPELPPIGKP----------ISNTWIYILDQE--QQLQPQG-IVGELYISGASV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 400 MLGYLKDP-VGTEKALKNGW------FYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVA 472
Cdd:cd17656 338 ARGYLNRQeLTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLD 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9759119 473 RPDVFWGETPCA-FVSLksgltQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17656 418 KADDKGEKYLCAyFVME-----QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKV 473
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
187-532 |
7.94e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 82.78 E-value: 7.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 187 PVVLNYTSGTTSAPKGVVHCHRgifvmSIDSLID-----WTVPKNPVYLWTLPIFHangwSYpwGIaaVGGTNVCLRKFD 261
Cdd:PRK08308 103 PSLLQYSSGTTGEPKLIRRSWT-----EIDREIEayneaLNCEQDETPIVACPVTH----SY--GL--ICGVLAALTRGS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 262 APLI-------YRL--IRDHGVTHMCGAPVVLNMLSA-TNEFQPLNRpvnILTAGAPPPAAVLLRAESIGFVISHGYGLT 331
Cdd:PRK08308 170 KPVIitnknpkFALniLRNTPQHILYAVPLMLHILGRlLPGTFQFHA---VMTSGTPLPEAWFYKLRERTTYMMQQYGCS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 332 EtAGlnvsC-AWKPQwnrlpasdrarlkarqgVRTVGftEIDVVDPESGRSVERNGETVGEIVMRgssimlgylkdpVGT 410
Cdd:PRK08308 247 E-AG----CvSICPD-----------------MKSHL--DLGNPLPHVSVSAGSDENAPEEIVVK------------MGD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 411 EKalkngwFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKS 490
Cdd:PRK08308 291 KE------IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE 364
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 9759119 491 GLtqrpTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK08308 365 EI----DPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
36-543 |
9.08e-17 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 83.79 E-value: 9.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 36 GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKL 115
Cdd:PLN02654 116 GFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 116 LfVDVFSVDLAVEAISMMTTdppILVFIADKEEEGGDADVAdrtkfsYTYDDLIHRGDLDFKW----------------I 179
Cdd:PLN02654 196 V-ITCNAVKRGPKTINLKDI---VDAALDESAKNGVSVGIC------LTYENQLAMKREDTKWqegrdvwwqdvvpnypT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 180 RPESEW----DPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSL---IDWTvpKNPVYLWTLPIFHANGWSY-PWGIAAVG 251
Cdd:PLN02654 266 KCEVEWvdaeDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFkyaFDYK--PTDVYWCTADCGWITGHSYvTYGPMLNG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 252 GTNVCLRKF----DAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEfQPLNR----PVNILTAGAPP--PAAVLLRAESIG 321
Cdd:PLN02654 344 ATVLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGD-EYVTRhsrkSLRVLGSVGEPinPSAWRWFFNVVG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 322 ---FVISHGYGLTETAGLNVS---CAW--KPQWNRLPASdrarlkarqGVRTVgfteidVVDpESGRSVErnGETVGEIV 393
Cdd:PLN02654 423 dsrCPISDTWWQTETGGFMITplpGAWpqKPGSATFPFF---------GVQPV------IVD-EKGKEIE--GECSGYLC 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 394 MRGSsiMLGYLKDPVGTEKALKN-------GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVN 466
Cdd:PLN02654 485 VKKS--WPGAFRTLYGDHERYETtyfkpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCA 562
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 467 EVAVVARPDVFWGETPCAFVSLKSGLT-QRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKK 543
Cdd:PLN02654 563 EAAVVGIEHEVKGQGIYAFVTLVEGVPySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASR 640
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
42-532 |
2.62e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 81.97 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINT---RLD-----ARTVSVLlRHCGS 113
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQptpRTDlavwaEDTLRVI-GMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 114 KLLFVDvfsvdlaveaismmttdPPILVFIADKEEEGGDADvadrtkfsyTYDDLIHRGDLDfkwIRPESEWDPVVLNYT 193
Cdd:PRK07768 110 KAVVVG-----------------EPFLAAAPVLEEKGIRVL---------TVADLLAADPID---PVETGEDDLALMQLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 194 SGTTSAPKGVVHCHRGIFV----MSIDSLIDwtvPKNPVYLWTLPIFHANGWSypwGIAAV----GGTNVCLRKFD---A 262
Cdd:PRK07768 161 SGSTGSPKAVQITHGNLYAnaeaMFVAAEFD---VETDVMVSWLPLFHDMGMV---GFLTVpmyfGAELVKVTPMDflrD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 263 PLIY-RLIRDHGVThMCGAP-----VVLNMLSATNEFQPLN-----------RPV------NILTAGAP---PPAAVLlr 316
Cdd:PRK07768 235 PLLWaELISKYRGT-MTAAPnfayaLLARRLRRQAKPGAFDlsslrfalngaEPIdpadveDLLDAGARfglRPEAIL-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 317 aesigfvisHGYGLTETAgLNVSCAWKPQWNRLPASDRARLKARQgvRTVGFTEIDV---------VDPESGRSVERNGE 387
Cdd:PRK07768 312 ---------PAYGMAEAT-LAVSFSPCGAGLVVDEVDADLLAALR--RAVPATKGNTrrlatlgppLPGLEVRVVDEDGQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 388 T-----VGEIVMRGSSIMLGYLkDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYT 461
Cdd:PRK07768 380 VlpprgVGVIELRGESVTPGYL-TMDGFIPAQdADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAAR 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 462 NPAV---NEVAV-VARPDVfwGETpcaF-VSLKSGLTQRPTEVEMIeycRKKMPKYMV------PKTVSFVD--ELPKTS 528
Cdd:PRK07768 459 VEGVrpgNAVAVrLDAGHS--REG---FaVAVESNAFEDPAEVRRI---RHQVAHEVVaevgvrPRNVVVLGpgSIPKTP 530
|
....
gi 9759119 529 TGKV 532
Cdd:PRK07768 531 SGKL 534
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
42-470 |
3.58e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 81.81 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDVF 121
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 122 SVDlaveaiSMMTTDP-------PILVFIADKEEEGGDADVADRTKFSYtyDDLIHRGDLDFKwIRPESEWDPVVLNYTS 194
Cdd:PLN02861 159 KIS------SILSCLPkcssnlkTIVSFGDVSSEQKEEAEELGVSCFSW--EEFSLMGSLDCE-LPPKQKTDICTIMYTS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 195 GTTSAPKGVVHCHRGIF--VMSIDSLI---DWTVPKNPVYLWTLPIFH-----------ANGWSYP-WG---------IA 248
Cdd:PLN02861 230 GTTGEPKGVILTNRAIIaeVLSTDHLLkvtDRVATEEDSYFSYLPLAHvydqvietyciSKGASIGfWQgdirylmedVQ 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 249 AVGGTNVC----------------------LRK--FDAPLIYRLIR-DHGVTHMCGAPVvLNMLSATNEFQPLNRPVNIL 303
Cdd:PLN02861 310 ALKPTIFCgvprvydriytgimqkissggmLRKklFDFAYNYKLGNlRKGLKQEEASPR-LDRLVFDKIKEGLGGRVRLL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 304 TAGAPP-PAAV--LLRAESIGfVISHGYGLTET-AGLNVSCAwkpqwNRLPAsdrarlkarqgVRTVG--FTEIDV---V 374
Cdd:PLN02861 389 LSGAAPlPRHVeeFLRVTSCS-VLSQGYGLTEScGGCFTSIA-----NVFSM-----------VGTVGvpMTTIEArleS 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 375 DPESG----RSVERngetvGEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDII-ITGGEN 449
Cdd:PLN02861 452 VPEMGydalSDVPR-----GEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEY 526
|
490 500
....*....|....*....|.
gi 9759119 450 VSSVEVETVLYTNPAVNEVAV 470
Cdd:PLN02861 527 VAVENLENTYSRCPLIASIWV 547
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
192-544 |
6.85e-16 |
|
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: 80.28 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRgIFVMSIDSLIDwTVPKNPV--------YLWTLPIFHAngwsypWGIAAVGGTnVCL-----R 258
Cdd:cd05918 113 FTSGSTGKPKGVVIEHR-ALSTSALAHGR-ALGLTSEsrvlqfasYTFDVSILEI------FTTLAAGGC-LCIpseedR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 259 KFDAPliyRLIRDHGVTHMCGAPVVLNMLSATnEFQPLNRpvnILTAGAPPPAAVLLRAESIGFVIShGYGLTETAglnV 338
Cdd:cd05918 184 LNDLA---GFINRLRVTWAFLTPSVARLLDPE-DVPSLRT---LVLGGEALTQSDVDTWADRVRLIN-AYGPAECT---I 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 339 SCAWKPQwnrlPASDRARLKARqGVRTVGFteidVVDPESGRSVERNGEtVGEIVMRGSSIMLGYLKDPVGTEKA----- 413
Cdd:cd05918 253 AATVSPV----VPSTDPRNIGR-PLGATCW----VVDPDNHDRLVPIGA-VGELLIEGPILARGYLNDPEKTAAAfiedp 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 414 --------LKNGWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNE---VAVVARPDVFWGET 481
Cdd:cd05918 323 awlkqegsGRGRRLYrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQ 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 482 PCAFVSLKSGLTQRPTEV---------------EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREIAKKM 544
Cdd:cd05918 403 LVAFVVLDGSSSGSGDGDslflepsdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESL 480
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
42-471 |
9.64e-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: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 42 TWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTvsvlLRHCgskllfvdvf 121
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKN----LKQC---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 122 svdlaveaISMMTTDPPILVFIADkeeeggdadvadrtkfsytyddlihrgdldfkwirpesewDPVVLNYTSGTTSAPK 201
Cdd:cd05910 70 --------LQEAEPDAFIGIPKAD----------------------------------------EPAAILFTSGSTGTPK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 202 GVVHCHrGIFVMSIDSL-IDWTVPKNPVYLWTLPIFHANGwsypwgiAAVGGTNV-------CLRKFDAPLIYRLIRDHG 273
Cdd:cd05910 102 GVVYRH-GTFAAQIDALrQLYGIRPGEVDLATFPLFALFG-------PALGLTSVipdmdptRPARADPQKLVGAIRQYG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 274 VTHMCGAPVVLNMLSATNEFQPLNRPV--NILTAGAPPPAAV---LLRAESIGFVISHGYGLTETaglnvscawkpqwnr 348
Cdd:cd05910 174 VSIVFGSPALLERVARYCAQHGITLPSlrRVLSAGAPVPIALaarLRKMLSDEAEILTPYGATEA--------------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 349 LPAS---DRARLKARQ----------------GVRtVGFTEIDVVD-PESGRSVERNGETVGEIVMRGSSIMLGYLKDPV 408
Cdd:cd05910 239 LPVSsigSRELLATTTaatsggagtcvgrpipGVR-VRIIEIDDEPiAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPV 317
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 409 GT--EKALKNG---WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVV 471
Cdd:cd05910 318 ATalAKIDDNSegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
164-458 |
2.00e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 79.37 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 164 TYDDLIHRGDLDFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFH----AN 239
Cdd:PLN02736 200 TYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyerVN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 240 GWSYPWGIAAVG---GTNvcLRKFD------------APLIYRLIRDhGVTH------------------------MCGA 280
Cdd:PLN02736 280 QIVMLHYGVAVGfyqGDN--LKLMDdlaalrptifcsVPRLYNRIYD-GITNavkesgglkerlfnaaynakkqalENGK 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 281 P-------VVLNMLSATnefqpLNRPVNILTAGAPPPAAVLLRAESIGF--VISHGYGLTETAGLNVSCawkpqwnrlpa 351
Cdd:PLN02736 357 NpspmwdrLVFNKIKAK-----LGGRVRFMSSGASPLSPDVMEFLRICFggRVLEGYGMTETSCVISGM----------- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 352 sdrarlkaRQGVRTVGFT-------EIDVVD-PESGRSVERNGETVGEIVMRGSSIMLGYLKDPVGTEKALKN-GWFYTG 422
Cdd:PLN02736 421 --------DEGDNLSGHVgspnpacEVKLVDvPEMNYTSEDQPYPRGEICVRGPIIFKGYYKDEVQTREVIDEdGWLHTG 492
|
330 340 350
....*....|....*....|....*....|....*..
gi 9759119 423 DVGVIHSDGYLEIKDRSKDII-ITGGENVSSVEVETV 458
Cdd:PLN02736 493 DIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
21-532 |
3.83e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 79.23 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 21 ERAATVYGD-CTSivYGsntvytwrETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRL 99
Cdd:PRK12316 2018 EAIAVVFGDqHLS--YA--------ELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 100 DARTVSVLLRHCGSKLLFVDVfsvdlAVEAISMMTTDPPILVFIADKEEEggdadvadrtkfsytyddlihrgdlDFKWI 179
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLTQR-----HLLERLPLPAGVARLPLDRDAEWA-------------------------DYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 180 RPESEWDPVVLNY---TSGTTSAPKGVVHCHrGIFVMSIDSLIDW--TVPKNPVYLWTLPIFHANGWSYPWGIAAvgGTN 254
Cdd:PRK12316 2138 APAVQLAGENLAYviyTSGSTGLPKGVAVSH-GALVAHCQAAGERyeLSPADCELQFMSFSFDGAHEQWFHPLLN--GAR 2214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 255 VCLRK---FDAPLIYRLIRDHGVTHMCGAPVVLNMLS--ATNEFQPLNRPVNILTAGAPPPAAVLLRAESIGFV-ISHGY 328
Cdd:PRK12316 2215 VLIRDdelWDPEQLYDEMERHGVTILDFPPVYLQQLAehAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGY 2294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 329 GLTETAglNVSCAWKPQWNRLPASDRARLKARQGVRT--VGFTEIDVVDPEsgrsverngeTVGEIVMRGSSIMLGYLKD 406
Cdd:PRK12316 2295 GPTEAV--VTPLLWKCRPQDPCGAAYVPIGRALGNRRayILDADLNLLAPG----------MAGELYLGGEGLARGYLNR 2362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 407 PVGT-EKALKN------GWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARpDVFW 478
Cdd:PRK12316 2363 PGLTaERFVPDpfsasgERLYrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGAS 2441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 9759119 479 GETPCAFVSLKSGLTQRPTEVEmiEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK12316 2442 GKQLVAYVVPDDAAEDLLAELR--AWLAARLPAYMVPAHWVVLERLPLNPNGKL 2493
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
18-538 |
6.95e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 77.76 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 18 GFLERAATVYGDCTSIVYGSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSG--AILNNI 95
Cdd:PRK06060 8 GLLAEQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGvmAFLANP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 96 NTRLDAR------TVSVLLRHCGSkllFVDVFSVDLAVEAISMMT----TDPpilvfiADKEEEGGDAdvadrtkfsYTY 165
Cdd:PRK06060 88 ELHRDDHalaarnTEPALVVTSDA---LRDRFQPSRVAEAAELMSeaarVAP------GGYEPMGGDA---------LAY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 166 ddlihrgdldfkwirpesewdpvvLNYTSGTTSAPKGVVHCHRGIFVMsIDSLIDWTVPKNP--VYLWTLPIFHANGWSY 243
Cdd:PRK06060 150 ------------------------ATYTSGTTGPPKAAIHRHADPLTF-VDAMCRKALRLTPedTGLCSARMYFAYGLGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 244 P-WGIAAVGGTNVC-------------LRKFDAPLIYrlirdhGVTHMCGApvVLNMLSAtNEFQPLNrpvNILTAGAPP 309
Cdd:PRK06060 205 SvWFPLATGGSAVInsapvtpeaaailSARFGPSVLY------GVPNFFAR--VIDSCSP-DSFRSLR---CVVSAGEAL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 310 PAAVLLRAESI--GFVISHGYGLTETAGLNVSCA---WKPQ--WNRLPAsdrarlkarqgvrtvgfTEIDVVDPEsGRSV 382
Cdd:PRK06060 273 ELGLAERLMEFfgGIPILDGIGSTEVGQTFVSNRvdeWRLGtlGRVLPP-----------------YEIRVVAPD-GTTA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 383 ERNGEtvGEIVMRGSSIMLGYLKDPvgtEKALKN-GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYT 461
Cdd:PRK06060 335 GPGVE--GDLWVRGPAIAKGYWNRP---DSPVANeGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 462 NPAVNEVAVVARPDVFWGETPCAFVSLKSGltQRPTEVEMIEYCRK---KMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:PRK06060 410 DEAVAEAAVVAVRESTGASTLQAFLVATSG--ATIDGSVMRDLHRGllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
192-532 |
1.58e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.12 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRGI--FVMSIDSLIDWTvPKNPVYLWTLPIFHANGWSYPWGIAAvGGTNVCLRK---FDAPLIY 266
Cdd:PRK12467 663 YTSGSTGQPKGVAISHGALanYVCVIAERLQLA-ADDSMLMVSTFAFDLGVTELFGALAS-GATLHLLPPdcaRDAEAFA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 267 RLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGA--PPPAAVLLRAESIGFVISHGYGLTETAglnvscAWKP 344
Cdd:PRK12467 741 ALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEalQVDLLARVRALGPGARLINHYGPTETT------VGVS 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 345 QWnrlPASDRARlkarqgvrtvGFTEIDVVDPESGRSVER--------NGETVGEIVMRGSSIMLGYLK----------- 405
Cdd:PRK12467 815 TY---ELSDEER----------DFGNVPIGQPLANLGLYIldhylnpvPVGVVGELYIGGAGLARGYHRrpaltaerfvp 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 406 DPVGTEkalkNGWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPdvfwGETPCA 484
Cdd:PRK12467 882 DPFGAD----GGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP----GDAGLQ 953
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 9759119 485 FVS------LKSGLTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK12467 954 LVAylvpaaVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
350-543 |
4.96e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 74.80 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 350 PASDRARLKARQGVRTVGfTEIDVVDPESGRSVerNGETVGEIVMRGSSIMLGYLkdpvGTEKALKNGWFYTGDVGVIhS 429
Cdd:PRK05851 336 DDGSGARRHAVLGNPIPG-MEVRISPGDGAAGV--AGREIGEIEIRGASMMSGYL----GQAPIDPDDWFPTGDLGYL-V 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 430 DGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVArpdvfwgetpcafVSLKSGLTqRPTEVEMIEY----- 504
Cdd:PRK05851 408 DGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVA-------------VGTGEGSA-RPGLVIAAEFrgpde 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9759119 505 --CRKKMPKY------MVPKTVSFVD--ELPKTSTGKvmkfvLREIAKK 543
Cdd:PRK05851 474 agARSEVVQRvasecgVVPSDVVFVApgSLPRTSSGK-----LRRLAVK 517
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
36-541 |
5.03e-14 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 74.99 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 36 GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTP-AMYELqFAVPMSGAI---------LNNINTRL-DARTV 104
Cdd:PRK10524 80 DEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAeAAFAM-LACARIGAIhsvvfggfaSHSLAARIdDAKPV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 105 SVLLRHCGS--------KLLfvdvfsVDlavEAISMMTTDPPiLVFIADK------EEEGGDADVAD-RTKfsytyddli 169
Cdd:PRK10524 159 LIVSADAGSrggkvvpyKPL------LD---EAIALAQHKPR-HVLLVDRglapmaRVAGRDVDYATlRAQ--------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 170 HRG-DLDFKWIrpESEwDPVVLNYTSGTTSAPKGVVHCHRG-----------IF------VMSIDSLIDWTVpknpvylw 231
Cdd:PRK10524 220 HLGaRVPVEWL--ESN-EPSYILYTSGTTGKPKGVQRDTGGyavalatsmdtIFggkageTFFCASDIGWVV-------- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 232 tlpifhanGWSY----PW--GIAAV--GGTNVclrKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQ----PLNRP 299
Cdd:PRK10524 289 --------GHSYivyaPLlaGMATImyEGLPT---RPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALlrkhDLSSL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 300 VNILTAGAP---PPAAVLlrAESIGFVISHGYGLTETAglnvscaWkPQWNRLPASDRARLK-ARQGVRTVGFtEIDVVD 375
Cdd:PRK10524 358 RALFLAGEPldePTASWI--SEALGVPVIDNYWQTETG-------W-PILAIARGVEDRPTRlGSPGVPMYGY-NVKLLN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 376 PESGRSVERNgeTVGEIVMRGS------SIMLGYLKDPVGTEKALKNGWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGE 448
Cdd:PRK10524 427 EVTGEPCGPN--EKGVLVIEGPlppgcmQTVWGDDDRFVKTYWSLFGRQVYsTFDWGIRDADGYYFILGRTDDVINVAGH 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 449 NVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLT------QRPTEVEMIEYCRKKMPKYMVPKTVSFVD 522
Cdd:PRK10524 505 RLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSladreaRLALEKEIMALVDSQLGAVARPARVWFVS 584
|
570
....*....|....*....
gi 9759119 523 ELPKTSTGKVMKFVLREIA 541
Cdd:PRK10524 585 ALPKTRSGKLLRRAIQAIA 603
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
62-470 |
8.29e-14 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 74.03 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 62 IGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFVDVFSVDLAVEAISMMTTDPPILV 141
Cdd:cd17632 90 VRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEGGTPPRLVV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 142 FiaDKEEEGG---DADVADRTKFS-----YTYDDLIHRGDLDFK---WIRPESEWDPVV-LNYTSGTTSAPKGVVHCHRG 209
Cdd:cd17632 170 F--DHRPEVDahrAALESARERLAavgipVTTLTLIAVRGRDLPpapLFRPEPDDDPLAlLIYTSGSTGTPKGAMYTERL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 210 I--FVMSIDSLIDWTvPKNPVYLWTLPIFHANGWSYPWGIAAVGGTNVCLRKFDAPLIYR---LIRDhgvTHMCGAPVVL 284
Cdd:cd17632 248 VatFWLKVSSIQDIR-PPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMSTLFDdlaLVRP---TELFLVPRVC 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 285 NMLsatneFQPLNRPVN-ILTAGAPPPAA-----------VL-------------LRAESIGFV-------ISHGYGLTE 332
Cdd:cd17632 324 DML-----FQRYQAELDrRSVAGADAETLaervkaelrerVLggrllaavcgsapLSAEMKAFMeslldldLHDGYGSTE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 TAGLNVSCAWKpqwnRLPASDrarlkarqgvrtvgFTEIDVvdPESGRSVERNGETVGEIVMRGSSIMLGYLKDPVGTEK 412
Cdd:cd17632 399 AGAVILDGVIV----RPPVLD--------------YKLVDV--PELGYFRTDRPHPRGELLVKTDTLFPGYYKRPEVTAE 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 413 AL-KNGWFYTGDVGVIHSDGYLEIKDRSKDII-ITGGENVSSVEVETVLYTNPAVNEVAV 470
Cdd:cd17632 459 VFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLkLSQGEFVTVARLEAVFAASPLVRQIFV 518
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
40-544 |
2.34e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 72.73 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 40 VYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFA------VPMSGAILNNINTRlDA--RTVSVLLRHC 111
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFAcqyaglVPVPLPLPMGFGGR-ESyiAQLRGMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 112 GSKLLFVDVFSVDLAVEAIsmmttdppilvfiadkeeeggdadVADRTKFSYTYDDLIHR--GDLDFKWIRPEsewDPVV 189
Cdd:PRK09192 128 QPAAIITPDELLPWVNEAT------------------------HGNPLLHVLSHAWFKALpeADVALPRPTPD---DIAY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 190 LNYTSGTTSAPKGVV------------HCHRGIFVMSIDSLIDWtvpknpvylwtLPIFHANGwsypwgiaAVGgtnvCL 257
Cdd:PRK09192 181 LQYSSGSTRFPRGVIithralmanlraISHDGLKVRPGDRCVSW-----------LPFYHDMG--------LVG----FL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 ---------------RKFDA-PLIY-RLIRDHGVT--------------HMCGAPVVLNMLS----ATNEFQPLnRPvNI 302
Cdd:PRK09192 238 ltpvatqlsvdylptRDFARrPLQWlDLISRNRGTisysppfgyelcarRVNSKDLAELDLScwrvAGIGADMI-RP-DV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 303 LTAGAPPPAAVLLRAESigFVIShgYGLTEtAGLNVSCAWKPQWNRLPASDRARLKARQGVRTVGF-------------- 368
Cdd:PRK09192 316 LHQFAEAFAPAGFDDKA--FMPS--YGLAE-ATLAVSFSPLGSGIVVEEVDRDRLEYQGKAVAPGAetrrvrtfvncgka 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 369 ---TEIDVVDpESGRSV-ERngeTVGEIVMRGSSIMLGYLKDPVgTEKALK-NGWFYTGDVGVIhSDGYLEIKDRSKDII 443
Cdd:PRK09192 391 lpgHEIEIRN-EAGMPLpER---VVGHICVRGPSLMSGYFRDEE-SQDVLAaDGWLDTGDLGYL-LDGYLYITGRAKDLI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 444 ITGGENVSSVEVETVLYTNPAVN--EVAV--VARPDvfwGETPCAFVSLKSGltqRPTEVEMIEYCRKKMPKYM--VPKT 517
Cdd:PRK09192 465 IINGRNIWPQDIEWIAEQEPELRsgDAAAfsIAQEN---GEKIVLLVQCRIS---DEERRGQLIHALAALVRSEfgVEAA 538
|
570 580
....*....|....*....|....*....
gi 9759119 518 VSFV--DELPKTSTGKVMkfvlREIAKKM 544
Cdd:PRK09192 539 VELVppHSLPRTSSGKLS----RAKAKKR 563
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
192-497 |
3.07e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 72.24 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHrGIFVMSIDSL-IDWTVPKNPVYLWTLPIF--HAngwsypwgiAAVGGTNVcLRKFDA--PL-- 264
Cdd:PRK09274 181 FTSGSTGTPKGVVYTH-GMFEAQIEALrEDYGIEPGEIDLPTFPLFalFG---------PALGMTSV-IPDMDPtrPAtv 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 265 ----IYRLIRDHGVTHMCGAPVVLNMLS--ATNEFQPLNRPVNILTAGAPPPAAVLLRAESigfVISHG------YGLTE 332
Cdd:PRK09274 250 dpakLFAAIERYGVTNLFGSPALLERLGryGEANGIKLPSLRRVISAGAPVPIAVIERFRA---MLPPDaeiltpYGATE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 333 TaglnvscawkpqwnrLPAS--------DRARLKARQG----V-RTVGFTEIDVVD------PESGRSVERNGETVGEIV 393
Cdd:PRK09274 327 A---------------LPISsiesreilFATRAATDNGagicVgRPVDGVEVRIIAisdapiPEWDDALRLATGEIGEIV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 394 MRGSSIMLGYLKDPVGTEKA-LKNG----WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAvnev 468
Cdd:PRK09274 392 VAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPG---- 467
|
330 340
....*....|....*....|....*....
gi 9759119 469 avVARpdvfwgetpCAFVSLKSGLTQRPT 497
Cdd:PRK09274 468 --VKR---------SALVGVGVPGAQRPV 485
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
192-532 |
1.42e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.14 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRgifvmSIDSLIDWT------VPKNPVYLWTLPIFHANGWSYPWGIAAvgGTNVCLRK---FDA 262
Cdd:PRK12316 4701 YTSGSTGRPKGVAVSHG-----SLVNHLHATgeryelTPDDRVLQFMSFSFDGSHEGLYHPLIN--GASVVIRDdslWDP 4773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 263 PLIYRLIRDHGVTHMCGAPVVLNMLS--ATNEFQPLNRPVNILTAGAPPPAAVLLRAESIGFV-ISHGYGLTETAglNVS 339
Cdd:PRK12316 4774 ERLYAEIHEHRVTVLVFPPVYLQQLAehAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVyLFNGYGPTETT--VTV 4851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 340 CAWKpqwnrLPASDRARLKARQGVRTVGFTEIDVVDpESGRSVERNGetVGEIVMRGSSIMLGYLKDPVGT-EKALKN-- 416
Cdd:PRK12316 4852 LLWK-----ARDGDACGAAYMPIGTPLGNRSGYVLD-GQLNPLPVGV--AGELYLGGEGVARGYLERPALTaERFVPDpf 4923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 417 ----GWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSG 491
Cdd:PRK12316 4924 gapgGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPA 5003
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 9759119 492 L---TQRPTEV--EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK12316 5004 LadaDEAQAELrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
186-537 |
3.64e-12 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 68.35 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRgifvmSIDSLIDW------TVPKNPVYLWTLPIFHANGWS-YP-WGIAAVGGTNVCL 257
Cdd:cd17645 105 DLAYVIYTSGSTGLPKGVMIEHH-----NLVNLCEWhrpyfgVTPADKSLVYASFSFDASAWEiFPhLTAGAALHVVPSE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 RKFDAPLIYRLIRDHGVThmcgapVVLNMLSATNEFQPL-NRPVNILTAGAPppaaVLLRAESIGFVISHGYGLTETAGL 336
Cdd:cd17645 180 RRLDLDALNDYFNQEGIT------ISFLPTGAAEQFMQLdNQSLRVLLTGGD----KLKKIERKGYKLVNNYGPTENTVV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 337 NVSCAWKPQWNRLPASdrarlKARQGVRTVGFTEIDVVDPESgrsverngeTVGEIVMRGSSIMLGYLKDPVGT-EKALK 415
Cdd:cd17645 250 ATSFEIDKPYANIPIG-----KPIDNTRVYILDEALQLQPIG---------VAGELCIAGEGLARGYLNRPELTaEKFIV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 416 NGW------FYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLK 489
Cdd:cd17645 316 HPFvpgermYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 9759119 490 sglTQRPTEvEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVL 537
Cdd:cd17645 396 ---EEIPHE-ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
12-531 |
5.87e-12 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 68.92 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 12 PPLTPIGFLERAATVYGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVlspntpamyelqfAVPMSgai 91
Cdd:PRK10252 456 PETTLSALVAQQAAKTPDAPALADARYQF-SYREMREQVVALANLLRERGVKPGDSVAV-------------ALPRS--- 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 92 lnnintrLDARTVSVLLRHCGSKLLFVDVFSVDlavEAISMMTTDP-PILVfIADKEEEGGDADVADRTkfSYTYDDLIH 170
Cdd:PRK10252 519 -------VFLTLALHAIVEAGAAWLPLDTGYPD---DRLKMMLEDArPSLL-ITTADQLPRFADVPDLT--SLCYNAPLA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 171 RGDldFKWIRPESEWDPVVLNYTSGTTSAPKGVVHCHRGI----------FVMSIDsliDWTVPKNPVylwtlpIFHANG 240
Cdd:PRK10252 586 PQG--AAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIvnrllwmqnhYPLTAD---DVVLQKTPC------SFDVSV 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 241 WSYPWGIAAvgGTNVCLRKFDA---PL-IYRLIRDHGVTHMCGAPvvlNMLSA-----TNE-----FQPLNRpvnILTAG 306
Cdd:PRK10252 655 WEFFWPFIA--GAKLVMAEPEAhrdPLaMQQFFAEYGVTTTHFVP---SMLAAfvaslTPEgarqsCASLRQ---VFCSG 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 307 APPPAAVLLRAESIGFVISHG-YGLTETAglnVSCAWkpqWnrlPASDRARLKARQGVRTVGF----TEIDVVDpESGRS 381
Cdd:PRK10252 727 EALPADLCREWQQLTGAPLHNlYGPTEAA---VDVSW---Y---PAFGEELAAVRGSSVPIGYpvwnTGLRILD-ARMRP 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 382 VERNgeTVGEIVMRGSSIMLGYLKDPVGT-EKALKNGW------FYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVE 454
Cdd:PRK10252 797 VPPG--VAGDLYLTGIQLAQGYLGRPDLTaSRFIADPFapgermYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGE 874
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 455 VETVLYTNPAVNEVAVVARPDVFWGETP------CAFVSLKSGLtqrPTEVEMI-EYCRKKMPKYMVPKTVSFVDELPKT 527
Cdd:PRK10252 875 IDRAMQALPDVEQAVTHACVINQAAATGgdarqlVGYLVSQSGL---PLDTSALqAQLRERLPPHMVPVVLLQLDQLPLS 951
|
....
gi 9759119 528 STGK 531
Cdd:PRK10252 952 ANGK 955
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
33-470 |
1.19e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 67.35 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 33 IVYGSNTVYTWR---ETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLR 109
Cdd:PLN02614 69 IVDGKPGKYVWQtyqEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIIS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 110 HCGSKLLFVDVFSV----DLAVEAISMMTTdppILVFIADKEEEGGDADvadrtKFS---YTYDDLIHRGDLDFKWIRPE 182
Cdd:PLN02614 149 HSEVSIVFVEEKKIselfKTCPNSTEYMKT---VVSFGGVSREQKEEAE-----TFGlviYAWDEFLKLGEGKQYDLPIK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 183 SEWDPVVLNYTSGTTSAPKGVVHCHRGIF-----VMSIDSLIDWTVPKNPVYLWTLPIFHANGWSYPWGIAAVGG----- 252
Cdd:PLN02614 221 KKSDICTIMYTSGTTGDPKGVMISNESIVtliagVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAaigfw 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 253 ----------------TNVC----------------------LRK--FDAPLIYRL-IRDHGVTHMCGAPVvLNMLSATN 291
Cdd:PLN02614 301 rgdvklliedlgelkpTIFCavprvldrvysglqkklsdggfLKKfvFDSAFSYKFgNMKKGQSHVEASPL-CDKLVFNK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 292 EFQPLNRPVNILTAGAPPPAA---VLLRAESIGFVIsHGYGLTEtaglnvSCAwkPQWNRLPasDRARLkarqgVRTVGf 368
Cdd:PLN02614 380 VKQGLGGNVRIILSGAAPLAShveSFLRVVACCHVL-QGYGLTE------SCA--GTFVSLP--DELDM-----LGTVG- 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 369 TEIDVVDPESGRSVERNGETV-----GEIVMRGSSIMLGYLKDPVGTEKALKNGWFYTGDVGVIHSDGYLEIKDRSKDII 443
Cdd:PLN02614 443 PPVPNVDIRLESVPEMEYDALastprGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIF 522
|
490 500
....*....|....*....|....*...
gi 9759119 444 -ITGGENVSSVEVETVLYTNPAVNEVAV 470
Cdd:PLN02614 523 kLSQGEYVAVENIENIYGEVQAVDSVWV 550
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
188-539 |
1.44e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 66.74 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 188 VVLNYTSGTTSAPKGVVHCHRGIF--VMSIDSLIDWTVPKNpvYLWTLPIFHANGWSYPWGIAAVGGTNVCL---RKF-D 261
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENLVhnMFAILNSTEWKTKDR--ILSWMPLTHDMGLIAFHLAPLIAGMNQYLmptRLFiR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 262 APLIY-RLIRDHGVTHMC----GAPVVLNMLSATNEFQPLNRPVNILTAGAPPPAAVL------------LRAESIGFVi 324
Cdd:cd05908 187 RPILWlKKASEHKATIVSspnfGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELchefldhmskygLKRNAILPV- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 325 shgYGLTE-TAGLNVSCAWKP------------QWNRLPASDRARLKARQGV---RTVGFTEIDVVDPESGrsvERNGET 388
Cdd:cd05908 266 ---YGLAEaSVGASLPKAQSPfktitlgrrhvtHGEPEPEVDKKDSECLTFVevgKPIDETDIRICDEDNK---ILPDGY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 389 VGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHsDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVnE 467
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGV-E 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 468 VAVVARPDVFWGETP----CAFVslksglTQRPTEVEMIEYCrKKMPKYMVPKT------VSFVDELPKTSTGKVMKFVL 537
Cdd:cd05908 418 LGRVVACGVNNSNTRneeiFCFI------EHRKSEDDFYPLG-KKIKKHLNKRGgwqineVLPIRRIPKTTSGKVKRYEL 490
|
..
gi 9759119 538 RE 539
Cdd:cd05908 491 AQ 492
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
36-540 |
1.74e-11 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 66.91 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 36 GSNTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKL 115
Cdd:cd05943 94 GERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 116 LFVD--------VFSVDLAVEAI--SMMTTDPPILVFIADKEEEggdADVADRTKFSyTYDDLIHRGD---LDFKWIRPE 182
Cdd:cd05943 174 LFAVdaytyngkRHDVREKVAELvkGLPSLLAVVVVPYTVAAGQ---PDLSKIAKAL-TLEDFLATGAageLEFEPLPFD 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 183 sewDPVVLNYTSGTTSAPKGVVHCHRGIFVMSIDSLI-DWTVPKNPVYLWtlpiFHANGW-SYPWGIA--AVGGTNVClr 258
Cdd:cd05943 250 ---HPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHIlHCDLRPGDRLFY----YTTCGWmMWNWLVSglAVGATIVL-- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 259 kFDAPLIY-------RLIRDHGVTHM-CGAPVVLNMLSAtnEFQPlNRPVN------ILTAGAPppaavlLRAESIGFVI 324
Cdd:cd05943 321 -YDGSPFYpdtnalwDLADEEGITVFgTSAKYLDALEKA--GLKP-AETHDlsslrtILSTGSP------LKPESFDYVY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 325 SHGY---------GLTETAGLNV-SCAWKPQWnrlpasdRARLKARQ-GVRTVGFteidvvdPESGRSVErnGEtVGEIV 393
Cdd:cd05943 391 DHIKpdvllasisGGTDIISCFVgGNPLLPVY-------RGEIQCRGlGMAVEAF-------DEEGKPVW--GE-KGELV 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 394 MRGS--SIMLGYLKDPVGT--EKA---LKNGWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVN 466
Cdd:cd05943 454 CTKPfpSMPVGFWNDPDGSryRAAyfaKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVE 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 467 EVAVVARPDVFWGETPCAFVSLKSGLTQRPTEVEMIE-YCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLREI 540
Cdd:cd05943 534 DSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRsTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKI 608
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
40-539 |
2.20e-11 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 66.16 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 40 VYTWRETNLRCLRVASSL-SSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLDARTVSVLLRHCGSKLLFV 118
Cdd:cd05938 5 TYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 119 DVFSVDlAVEAISMMTTDPPILVFIADKEEEggDADVADRT-KFSYTYDDLI---HRGDLDFKwirpesewDPVVLNYTS 194
Cdd:cd05938 85 APELQE-AVEEVLPALRADGVSVWYLSHTSN--TEGVISLLdKVDAASDEPVpasLRAHVTIK--------SPALYIYTS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 195 GTTSAPKGVVHCHRGIFVMS-IDSLIDWTVpKNPVYLwTLPIFHANGWSYpwGIAA---VGGTNVCLRKFDAPLIYRLIR 270
Cdd:cd05938 154 GTTGLPKAARISHLRVLQCSgFLSLCGVTA-DDVIYI-TLPLYHSSGFLL--GIGGcieLGATCVLKPKFSASQFWDDCR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 271 DHGVT----------HMCGAPVVLN------MLSATNEFQP------LNR--PVNILTAgapppaavllraesigfvish 326
Cdd:cd05938 230 KHNVTviqyigellrYLCNQPQSPNdrdhkvRLAIGNGLRAdvwrefLRRfgPIRIREF--------------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 327 gYGLTE--TAGLNVScawkpqwNRLPASDRARLKARQgVRTVGFTEIDV-----VDPESGRSVE-RNGET---VGEIVMR 395
Cdd:cd05938 289 -YGSTEgnIGFFNYT-------GKIGAVGRVSYLYKL-LFPFELIKFDVekeepVRDAQGFCIPvAKGEPgllVAKITQQ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 396 gsSIMLGYLKDPVGTEKAL-----KNG--WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEV 468
Cdd:cd05938 360 --SPFLGYAGDKEQTEKKLlrdvfKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 469 AV--VARPDvFWGETPCAFVSLKSGltqrpTEVE---MIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLRE 539
Cdd:cd05938 438 NVygVTVPG-HEGRIGMAAVKLKPG-----HEFDgkkLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVE 507
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
38-538 |
3.00e-11 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 65.52 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 38 NTVYTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAI--LNNINTRLDARTVSVLLRHCgSKL 115
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVEtaLINSNLRLESLLHCITVSKA-KAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 116 LFvdvfsvDLAVEAISMMTTDPPILVfiadkeeeggdadvadrtkfsytyddlihrgDLDFKwirpesewDPVVLNYTSG 195
Cdd:cd05939 80 IF------NLLDPLLTQSSTEPPSQD-------------------------------DVNFR--------DKLFYIYTSG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 196 TTSAPKGVVHCHRGIFVMSIDSLIDWTVPKNPVYLWTLPIFHANGwsypwGIAAVG-----GTNVCLRK-FDAPLIYRLI 269
Cdd:cd05939 115 TTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAG-----GIMGVGqallhGSTVVIRKkFSASNFWDDC 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 270 RDHGVT------HMCgaPVVLNMLSATNEFQPLNRPV--NILTAGAPPPAAVLLRAESIGFVishgYGLTE-TAGL-NV- 338
Cdd:cd05939 190 VKYNCTivqyigEIC--RYLLAQPPSEEEQKHNVRLAvgNGLRPQIWEQFVRRFGIPQIGEF----YGATEgNSSLvNId 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 339 ----SCAWKPQWnrLPASDRARLkarqgVRtvgfteidvVDPESGRSVE------------RNGETVGEIVMRG-SSIML 401
Cdd:cd05939 264 nhvgACGFNSRI--LPSVYPIRL-----IK---------VDEDTGELIRdsdglcipcqpgEPGLLVGKIIQNDpLRRFD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 402 GYLKDPVGTEKALKNGW------FYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAV--VAR 473
Cdd:cd05939 328 GYVNEGATNKKIARDVFkkgdsaFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEV 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 474 PDVfWGETPCAFVSLKsgltQRPTEVE-MIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVLR 538
Cdd:cd05939 408 PGV-EGRAGMAAIVDP----ERKVDLDrFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
168-532 |
4.44e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.13 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 168 LIHRGDLDFKWIRPESEWDPVVLNY---TSGTTSAPKGVVHCHRGI--FVMSIDSLIDWTVpKNPVYLWTLPIFHANGWS 242
Cdd:PRK12316 3176 DLDRGDENYAEANPAIRTMPENLAYviyTSGSTGKPKGVGIRHSALsnHLCWMQQAYGLGV-GDRVLQFTTFSFDVFVEE 3254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 243 YPWGIAAvgGTNVCLRK----FDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGAPPPAAVLLRAE 318
Cdd:PRK12316 3255 LFWPLMS--GARVVLAGpedwRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVF 3332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 319 SiGFVISHGYGLTETAglnvscAWKPQWNRLPASDRARLKARQGVRTVGFTEIDVVDPESGRSVerngetvGEIVMRGSS 398
Cdd:PRK12316 3333 A-GLPLYNLYGPTEAT------ITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGAL-------GELYLGGEG 3398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 399 IMLGYLKDPVGT-EKALKNGW------FYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVV 471
Cdd:PRK12316 3399 LARGYHNRPGLTaERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL 3478
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9759119 472 ARPdvfwGETPCAFVSLKSGLTQRPTEVEmiEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK12316 3479 AVD----GRQLVAYVVPEDEAGDLREALK--AHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
181-475 |
5.63e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 65.38 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 181 PESEWDPVVLNYTSGTTSAPKGVVHCHR----GIFVMSiDSLIDWTVPKNP--VYLWTLPIFHangwsypwgIAAVGGTN 254
Cdd:PTZ00216 260 PENNDDLALIMYTSGTTGDPKGVMHTHGsltaGILALE-DRLNDLIGPPEEdeTYCSYLPLAH---------IMEFGVTN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 255 V-----CLRKFDAP--LIYRLIRDHG------VTHMCGAPVVLNMLSATNE-----------------FQ---------- 294
Cdd:PTZ00216 330 IflargALIGFGSPrtLTDTFARPHGdltefrPVFLIGVPRIFDTIKKAVEaklppvgslkrrvfdhaYQsrlralkegk 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 295 --P-LNRPV-------------NILTAGAPppaavlLRAESIGFV------ISHGYGLTETaglnVSCAWKPQWNRLPAS 352
Cdd:PTZ00216 410 dtPyWNEKVfsapravlggrvrAMLSGGGP------LSAATQEFVnvvfgmVIQGWGLTET----VCCGGIQRTGDLEPN 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 353 DRARLKARQGVR---TVGFTEIDVVDPEsgrsverngetvGEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIH 428
Cdd:PTZ00216 480 AVGQLLKGVEMKlldTEEYKHTDTPEPR------------GEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIA 547
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 9759119 429 SDGYLEIKDRSKDIIITG-GENVSSVEVETVLYTNPAV--NEVAVVARPD 475
Cdd:PTZ00216 548 ANGTLRIIGRVKALAKNClGEYIALEALEALYGQNELVvpNGVCVLVHPA 597
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
387-532 |
1.16e-10 |
|
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: 63.99 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 387 ETVGEIVMRGSSIMLGYLKDPVGT-EKALKNGW-------FY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVET 457
Cdd:cd17644 307 GVPGELHIGGVGLARGYLNRPELTaEKFISHPFnsseserLYkTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEA 386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 458 VLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSglTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:cd17644 387 VLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHY--EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
21-532 |
1.69e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 21 ERAATVYGDCTSIVYGSNTVyTWRETNLRCLRVASSLSSIGIGRSDVVSVLSPNTPAMYELQFAVPMSGAILNNINTRLD 100
Cdd:PRK12316 518 EEQVERTPEAPALAFGEETL-DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYP 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 101 ARTVSVLLRHCGSKLLFVDVFSVD-LAVEA-ISMMTTDPPILVFIADKEEEggdadvadrtkfsytyddlihrgdldfkw 178
Cdd:PRK12316 597 AERLAYMLEDSGVQLLLSQSHLGRkLPLAAgVQVLDLDRPAAWLEGYSEEN----------------------------- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 179 irPESEWDPVVLNY---TSGTTSAPKGVVHCHRgifvmSIDSLIDWT-----VPKNPVYLWTLPI-FHANGWSYPWGIAA 249
Cdd:PRK12316 648 --PGTELNPENLAYviyTSGSTGKPKGAGNRHR-----ALSNRLCWMqqaygLGVGDTVLQKTPFsFDVSVWEFFWPLMS 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 250 vGGTNVCLRK---FDAPLIYRLIRDHGVThmcgapvVLNML-SATNEFQPLNRPVN------ILTAGAPPPAAVLLRAE- 318
Cdd:PRK12316 721 -GARLVVAAPgdhRDPAKLVELINREGVD-------TLHFVpSMLQAFLQDEDVASctslrrIVCSGEALPADAQEQVFa 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 319 --SIGFVISHgYGLTETAgLNVSCawkpqWNRLpasdrarlkaRQGVRTVgfteiDVVDPESG---RSVERNGETV---- 389
Cdd:PRK12316 793 klPQAGLYNL-YGPTEAA-IDVTH-----WTCV----------EEGGDSV-----PIGRPIANlacYILDANLEPVpvgv 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 390 -GEIVMRGSSIMLGYLKDPVGT-EKALKNGW------FYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYT 461
Cdd:PRK12316 851 lGELYLAGRGLARGYHGRPGLTaERFVPSPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 930
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9759119 462 NPAVNEVAVVARPdvfwGETPCAFVSLKSGLTQRPteVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK12316 931 HPWVREAAVLAVD----GKQLVGYVVLESEGGDWR--EALKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
345-540 |
1.37e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 60.68 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 345 QWNRLPasdrarlkarqgvrtVGFTEID---VVDPESGRSVErNGETvGEIVMRGSSIMLGYLKDPVGTEKALK--NG-W 418
Cdd:PRK04813 314 QYKRLP---------------IGYAKPDsplLIIDEEGTKLP-DGEQ-GEIVISGPSVSKGYLNNPEKTAEAFFtfDGqP 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 419 FY-TGDVGVIhSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVarpdvfwgetP----------CAFVS 487
Cdd:PRK04813 377 AYhTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV----------PynkdhkvqylIAYVV 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9759119 488 LKSGLTQRptEVEMIEYCRKK----MPKYMVPKTVSFVDELPKTSTGKV-MKFVLREI 540
Cdd:PRK04813 446 PKEEDFER--EFELTKAIKKElkerLMEYMIPRKFIYRDSLPLTPNGKIdRKALIEEV 501
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
173-532 |
2.87e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.17 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 173 DLDFKWIRPESEWDPVV-------LNYTSGTTSAPKGVVHCHrGIFVM---SIDSLIDWTVpKNPVYLWTLPIFHANGWS 242
Cdd:PRK12467 3218 DRLDLNGYSENNPSTRVmgenlayVIYTSGSTGKPKGVGVRH-GALANhlcWIAEAYELDA-NDRVLLFMSFSFDGAQER 3295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 243 YPWGIAAvGGtnvCL-----RKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAG-APPPAAV-LL 315
Cdd:PRK12467 3296 FLWTLIC-GG---CLvvrdnDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGGeAVPPAAFeQV 3371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 316 RAESIGFVISHGYGLTETAglNVSCAWKPQWNRLPASDRARLKARQGVRTvgfteIDVVDpesgrsveRNGETV-----G 390
Cdd:PRK12467 3372 KRKLKPRGLTNGYGPTEAV--VTVTLWKCGGDAVCEAPYAPIGRPVAGRS-----IYVLD--------GQLNPVpvgvaG 3436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 391 EIVMRGSSIMLGYLKDPVGT-EKALKN------GWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTN 462
Cdd:PRK12467 3437 ELYIGGVGLARGYHQRPSLTaERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQH 3516
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 463 PAVNEVAVVARpDVFWGETPCAFVSLKSglTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK12467 3517 PSVREAVVLAR-DGAGGKQLVAYVVPAD--PQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKV 3583
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
192-532 |
4.36e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.80 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRgifvmSIDSLIDW-----TVPKNPVYLWTLPI-FHANGWSYPWG--------IAAVGgtnvcl 257
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHA-----ALAERLQWmqatyALDDSDVLMQKAPIsFDVSVWECFWPlitgcrlvLAGPG------ 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 258 RKFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGAPPPAAVLLRA-ESIGFVISHG-YGLTETAg 335
Cdd:PRK05691 1349 EHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVlQRLPQVQLHNrYGPTETA- 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 336 LNVScAWKPQwnrlpASDRARLKARqgvRTVGFTEIDVVDPESGRSVernGETVGEIVMRGSSIMLGYLK---------- 405
Cdd:PRK05691 1428 INVT-HWQCQ-----AEDGERSPIG---RPLGNVLCRVLDAELNLLP---PGVAGELCIGGAGLARGYLGrpaltaerfv 1495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 406 -DPVGTEKALkngWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGEtpca 484
Cdd:PRK05691 1496 pDPLGEDGAR---LYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQ---- 1568
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 9759119 485 FVSLKSGLTQRPTEVEMIEYCRK-KMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK05691 1569 LVGYYTGEAGQEAEAERLKAALAaELPEYMVPAQLIRLDQMPLGPSGKL 1617
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
351-538 |
7.23e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.03 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 351 ASDRARLKARQGVRTVGFT----EIDVVDPESGRSVERNgeTVGEIVMRGSSIMLGYLKDPVGTEKALKN----GWFYTG 422
Cdd:PRK05691 357 ARNRAEPGTGSVLMSCGRSqpghAVLIVDPQSLEVLGDN--RVGEIWASGPSIAHGYWRNPEASAKTFVEhdgrTWLRTG 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 423 DVGVIHsDGYLEIKDRSKDIIITGGENVSSVEVETVLYtnpavNEVAVVARPDV------FWGETPCAFVSLKSGLTQR- 495
Cdd:PRK05691 435 DLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVE-----REVEVVRKGRVaafavnHQGEEGIGIAAEISRSVQKi 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9759119 496 -PTEvEMIEYCRKKMPK--YMVPKTVSFVD--ELPKTSTGKVMKFVLR 538
Cdd:PRK05691 509 lPPQ-ALIKSIRQAVAEacQEAPSVVLLLNpgALPKTSSGKLQRSACR 555
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
192-531 |
1.43e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.86 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 192 YTSGTTSAPKGVVHCHRGIFvmsidSLIDWT------VPKNPVYLWTLPIFHANGWSYPWgiAAVGGTNVCLRKFDAPL- 264
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGALV-----NRLCATqeayqlSAADVVLQFTSFAFDVSVWELFW--PLINGARLVIAPPGAHRd 1797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 265 ---IYRLIRDHGVTHMCGAPVVLNML--SATNEFQPLNRPVNILTAGAPPPAAVLLRAESIGFV-ISHGYGLTETAgLNV 338
Cdd:PRK12467 1798 peqLIQLIERQQVTTLHFVPSMLQQLlqMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETA-VDV 1876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 339 ScAWKpqwnrlpaSDRARLKARQGVrtvgftEIDVVDPESGRSVERNG------ETVGEIVMRGSSIMLGYLKDP----- 407
Cdd:PRK12467 1877 T-HWT--------CRRKDLEGRDSV------PIGQPIANLSTYILDASlnpvpiGVAGELYLGGVGLARGYLNRPaltae 1941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 408 --VGTEKALKNGWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARpDVFWGETPCA 484
Cdd:PRK12467 1942 rfVADPFGTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVA 2020
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 9759119 485 FVS------LKSGLTQRPTEVEMIEYCRKKMPKYMVPKTVSFVDELPKTSTGK 531
Cdd:PRK12467 2021 YVVptdpglVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGK 2073
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
178-449 |
1.55e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 57.43 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 178 WIRPESEWDPVV-LNYTSGTTSAPKGVVHCHRGI---FVMSIDSL--------IDWtvpknpvylwtLPIFHANGWSYPW 245
Cdd:PRK07769 172 WVPPEANEDTIAyLQYTSGSTRIPAGVQITHLNLptnVLQVIDALegqegdrgVSW-----------LPFFHDMGLITVL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 246 gIAAVGGTNVclrKFDAPLI-----YRLIR------DHGVTHMCGAPvvlNM-----------------LSATNEFQPLN 297
Cdd:PRK07769 241 -LPALLGHYI---TFMSPAAfvrrpGRWIRelarkpGGTGGTFSAAP---NFafehaaarglpkdgeppLDLSNVKGLLN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 298 --RPVNILT------AGAP---PPAAvllraesigfvISHGYGLTEtAGLNVScawKPQWNRLPA---SDRARLKARQGV 363
Cdd:PRK07769 314 gsEPVSPASmrkfneAFAPyglPPTA-----------IKPSYGMAE-ATLFVS---TTPMDEEPTviyVDRDELNAGRFV 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 364 RT---------------VGFTEIDV-VDPESGRSVErNGEtVGEIVMRGSSIMLGYLKDPVGTEKALKN----------- 416
Cdd:PRK07769 379 EVpadapnavaqvsagkVGVSEWAViVDPETASELP-DGQ-IGEIWLHGNNIGTGYWGKPEETAATFQNilksrlsesha 456
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 9759119 417 -------GWFYTGDVGVIHsDGYLEIKDRSKDIIITGGEN 449
Cdd:PRK07769 457 egapddaLWVRTGDYGVYF-DGELYITGRVKDLVIIDGRN 495
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
190-532 |
2.75e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 190 LNYTSGTTSAPKGVVHCHrGIFVMSIDSLID-WTVPKNPVYLWTLPI-FHANgwSYPWGIAAVGGTNVCLR---KFDAPL 264
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSH-GEIAMHCQAVIErFGMRADDCELHFYSInFDAA--SERLLVPLLCGARVVLRaqgQWGAEE 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 265 IYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGAPPPAAVLLRAESIGFVIS---HGYGLTETAGLNVSCa 341
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQlffNAYGPTETVVMPLAC- 2493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 342 wkpqwnrlPASDRARLKARQ-------GVRTVGFTEIDVVDPESGRSverngetvGEIVMRGSSIMLGYLKDP------- 407
Cdd:PRK05691 2494 --------LAPEQLEEGAASvpigrvvGARVAYILDADLALVPQGAT--------GELYVGGAGLAQGYHDRPgltaerf 2557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 408 VGTEKALKNGWFY-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARpDVFWGETPCAFV 486
Cdd:PRK05691 2558 VADPFAADGGRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYL 2636
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 9759119 487 SLKSGLTQRPTEVEMIE----YCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK05691 2637 VSAVAGQDDEAQAALREalkaHLKQQLPDYMVPAHLILLDSLPLTANGKL 2686
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
422-549 |
7.76e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 52.00 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 422 GDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYT-NPAVNEVAVVARPDVFWG-ETPCAFVSLK--SGLTQRPT 497
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDESVLETAAIGVPPPGGGpEQLVIAAVLKdpPGSNPDLN 673
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 9759119 498 EVEMI---EYCRKKMPKYMVpKTVSFVDELPKTSTGKVMKFVLR-EIAKKMGTTRL 549
Cdd:PLN03052 674 ELKKIfnsAIQKKLNPLFKV-SAVVIVPSFPRTASNKVMRRVLRqQLAQELSRSKL 728
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
193-532 |
8.93e-07 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 51.32 E-value: 8.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 193 TSGTTSAPKGVVHCHRGI--FVMSIDSLIDWTvpKNPVYLWTLPIFHANGWSYPWGIAAVGGTNV----CLRKFDAPLIY 266
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCIlpNIQHFRSLFNIT--SEDILFLTSPLTFDPSVVEIFLSLSSGATLLivptSVKVLPSKLAD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 267 RLIRDHGVTHMCGAPVVLNML-SATNEFQPLNRPVNI---LTAGAPPPAAVLLRA---ESIGFVISHGYGLTETaglnvs 339
Cdd:cd17654 204 ILFKRHRITVLQATPTLFRRFgSQSIKSTVLSATSSLrvlALGGEPFPSLVILSSwrgKGNRTRIFNIYGITEV------ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 340 CAWKpQWNRLPASDrarlKARQGVRTVGFTEIDVVDpesgrsvERNGETVGEiVMRGSSIMLGYLKDPVGTEKALkngWF 419
Cdd:cd17654 278 SCWA-LAYKVPEED----SPVQLGSPLLGTVIEVRD-------QNGSEGTGQ-VFLGGLNRVCILDDEVTVPKGT---MR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 420 YTGDVgVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVarpdVFWGETPCAFVSLKSGLTQRPTEV 499
Cdd:cd17654 342 ATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT----LSDQQRLIAFIVGESSSSRIHKEL 416
|
330 340 350
....*....|....*....|....*....|...
gi 9759119 500 EMIEYCRKKMPKYMVpktvsFVDELPKTSTGKV 532
Cdd:cd17654 417 QLTLLSSHAIPDTFV-----QIDKLPLTSHGKV 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
389-532 |
1.57e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 389 VGEIVMRGSSIMLGYLKDPVGTEKALKNGWF-------Y-TGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLY 460
Cdd:PRK05691 4066 VGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYrTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLH 4145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 461 TNPAVNE--VAVVARPDvfwGETPCAFVSLKSGLTQRPTEVEMI-EYCRKKMPKYMVPKTVSFVDELPKTSTGKV 532
Cdd:PRK05691 4146 EQAEVREaaVAVQEGVN---GKHLVGYLVPHQTVLAQGALLERIkQRLRAELPDYMVPLHWLWLDRLPLNANGKL 4217
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
186-459 |
4.25e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 49.43 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 186 DPVVLNYTSGTTSAPKGVVHCHRGIfVMSIDSLIDWTVPK-NPVYLWTLPIFHANGWS----YPW--GIAAVGGTNvclr 258
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHANL-LANQRACLKFFSPKeDDVMMSFLPPFHAYGFNsctlFPLlsGVPVVFAYN---- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 259 KFDAPLIYRLIRDHGVTHMCGAPVVLNMLSATNEFQPLNRPVNILTAGAPPPAAVLLRAESIGF----VISHGYGLTEta 334
Cdd:PRK06334 259 PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfphiQLRQGYGTTE-- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 335 glnvsCAwkpqwnrlPASDRARLKARQGVRTVGF----TEIDVVDPESGRSVErNGEtVGEIVMRGSSIMLGYLKDPVGT 410
Cdd:PRK06334 337 -----CS--------PVITINTVNSPKHESCVGMpirgMDVLIVSEETKVPVS-SGE-TGLVLTRGTSLFSGYLGEDFGQ 401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 9759119 411 EKALKNG--WFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVL 459
Cdd:PRK06334 402 GFVELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
373-449 |
5.31e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 49.17 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 373 VVDPESGRsvERNGETVGEIVMRGSSIMLGYLKDPVGTEKAL------------KNGWFYTGDVGVIhSDGYLEIKDRSK 440
Cdd:PRK05850 383 IVDPDTCI--ECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtpEGPWLRTGDLGFI-SEGELFIVGRIK 459
|
....*....
gi 9759119 441 DIIITGGEN 449
Cdd:PRK05850 460 DLLIVDGRN 468
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
417-537 |
3.22e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 46.66 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 417 GWFYTGDVGVIHSDGYLEIKDRSKDIIITGGENVSSVEVETVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGLTQRP 496
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQS 571
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 9759119 497 TEV-----EMIEYCRKKMPKYMVPKTVSFVDELPKTSTGKVMKFVL 537
Cdd:PTZ00237 572 IDLnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
390-443 |
1.60e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 44.71 E-value: 1.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 9759119 390 GEIVMRGSSIMLGYLKDPVGTEKAL-KNGWFYTGDVGVIHSDGYLEIKDRSKDII 443
Cdd:PTZ00342 542 GELLIKSDSIFSGYFLEKEQTKNAFtEDGYFKTGDIVQINKNGSLTFLDRSKGLV 596
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
431-548 |
3.00e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 40.18 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9759119 431 GYLEIKDRSKDIIITGGENVSSVEVE-TVLYTNPAVNEVAVVARPDVFWGETPCAFVSLKSGL-----TQRPTEVEMI-- 502
Cdd:PLN03051 371 GYFCVQGRADDTMNLGGIKTSSVEIErACDRAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEkkgfdQARPEALQKKfq 450
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 9759119 503 EYCRKKM-PKYMVPKtVSFVDELPKTSTGKVMKFVLREIAKKMGTTR 548
Cdd:PLN03051 451 EAIQTNLnPLFKVSR-VKIVPELPRNASNKLLRRVLRDQLKKELSGR 496
|
|
| |
