|
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 ... |
13-539 |
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: 788.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 13 PLTLLGFLERAATVYGDCTSIVYGnSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAIL 92
Cdd:cd12118 3 PLTPLSFLERAAAVYPDRTSIVYG-DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 93 NNINTRLDARTVSVLLRHCESKLLFVDFFYsdlaveaitmllnppilvlianeeeeeggaevterskfcyLYSDLITRGN 172
Cdd:cd12118 82 NALNTRLDAEEIAFILRHSEAKVLFVDREF----------------------------------------EYEDLLAEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 173 PDFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGT 252
Cdd:cd12118 122 PDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 253 NVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQ-PLKSPVNFLTAGSSPPATVLLRAESLGFIVSHGYGLT 331
Cdd:cd12118 202 NVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDArPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 332 ETAGVIVSCAWKPNWNRLPASDQAQLKSRQGVRTVGFSEIDVVDPESGRSVERDGETVGEIVLRGSSIMLGYLKNPIGTQ 411
Cdd:cd12118 282 ETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLKNPEATA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 412 NSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPG 491
Cdd:cd12118 362 EAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEG 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15222924 492 ltRKPTDKEIIEYCKYKMPRYMAPKTVSFlEELPKTSTGKIIKSLLKE 539
Cdd:cd12118 442 --AKVTEEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
2-542 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 728.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 2 EDLKPSAANSLPLTLLGFLERAATVYGDCTSIVYGnSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYEL 81
Cdd:PRK08162 6 QGLDRNAANYVPLTPLSFLERAAEVYPDRPAVIHG-DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 82 QFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITMLLNPPILVLIANEEEEEGGAEVTERSkfc 161
Cdd:PRK08162 85 HFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALD--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 162 ylYSDLITRGNPDFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWT 241
Cdd:PRK08162 162 --YEAFLASGDPDFAWTLPADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNGWC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 242 YPWGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQIL-SASQESDQPLKSPVNFLTAGSSPPATVLLRAESL 320
Cdd:PRK08162 240 FPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALiNAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 321 GFIVSHGYGLTETAGVIVSCAWKPNWNRLPASDQAQLKSRQGVRTVGFSEIDVVDPESGRSVERDGETVGEIVLRGSSIM 400
Cdd:PRK08162 320 GFDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIMFRGNIVM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 401 LGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGE 480
Cdd:PRK08162 400 KGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGE 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222924 481 TPCAFVSLKPGLTrkPTDKEIIEYCKYKMPRYMAPKTVSFlEELPKTSTGKIIKSLLKEIAK 542
Cdd:PRK08162 480 VPCAFVELKDGAS--ATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAK 538
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1-544 |
0e+00 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 627.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 1 MEDLKPSAANSLPLTLLGFLERAATVYGDCTSIVYGNsTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYE 80
Cdd:PLN03102 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGK-TRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 81 LQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITML------LNPPILVLIANEEeeeggaev 154
Cdd:PLN03102 80 MHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLssedsnLNLPVIFIHEIDF-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 155 TERSKFCYL-YSDLITRGNPD----FKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYL 229
Cdd:PLN03102 152 PKRPSSEELdYECLIQRGEPTpslvARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 230 WTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQ-PLKSPVNFLTAGSS 308
Cdd:PLN03102 232 WTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLsPRSGPVHVLTGGSP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 309 PPATVLLRAESLGFIVSHGYGLTETAGVIVSCAWKPNWNRLPASDQAQLKSRQGVRTVGFSEIDVVDPESGRSVERDGET 388
Cdd:PLN03102 312 PPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPRDGKT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 389 VGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEA 468
Cdd:PLN03102 392 MGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLET 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 469 AVVARPDEFWGETPCAFVSLKPGLTRKPTD--------KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEI 540
Cdd:PLN03102 472 AVVAMPHPTWGETPCAFVVLEKGETTKEDRvdklvtreRDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
....
gi 15222924 541 AKNM 544
Cdd:PLN03102 552 AKGL 555
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1-544 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 626.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 1 MEDLKPSAANSLPLTLLGFLERAATVYGDCTSIVYGnSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYE 80
Cdd:PLN02479 7 IDDLPKNAANYTALTPLWFLERAAVVHPTRKSVVHG-SVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 81 LQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITML-------LNPPILVLIANEEEEEGGAE 153
Cdd:PLN02479 86 AHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILaekkkssFKPPLLIVIGDPTCDPKSLQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 154 VTERsKFCYLYSDLITRGNPDFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLP 233
Cdd:PLN02479 166 YALG-KGAIEYEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 234 IFHANGWTYPWGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQ--PLKSPVNFLTAGSSPPA 311
Cdd:PLN02479 245 MFHCNGWCFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETilPLPRVVHVMTAGAAPPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 312 TVLLRAESLGFIVSHGYGLTETAGVIVSCAWKPNWNRLPASDQAQLKSRQGVRTVGFSEIDVVDPESGRSVERDGETVGE 391
Cdd:PLN02479 325 SVLFAMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPADGKTMGE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 392 IVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVV 471
Cdd:PLN02479 405 IVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVV 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222924 472 ARPDEFWGETPCAFVSLKPGLTRKP---TDKEIIEYCKYKMPRYMAPKTVSFlEELPKTSTGKIIKSLLKEIAKNM 544
Cdd:PLN02479 485 ARPDERWGESPCAFVTLKPGVDKSDeaaLAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKAKEM 559
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
16-542 |
5.00e-144 |
|
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: 422.68 E-value: 5.00e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 16 LLGFLERAATVYGDCTSIVYGNSTvYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNI 95
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR-LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 96 NTRLDARTVSVLLRHCESKLLFVdffysdlaveaitmllnppilvlianeeeeeggaevterskfcylysdlitrgnpdf 175
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 176 kwirpgsewdpIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIA-AVGGTNV 254
Cdd:COG0318 103 -----------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPlLAGATLV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 255 CVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSP-PATVLLRAES-LGFIVSHGYGLTE 332
Cdd:COG0318 172 LLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPlPPELLERFEErFGVRIVEGYGLTE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 333 TAGViVSCAWKPNWNRLPASdqaqlksrQGvRTVGFSEIDVVDPEsGRSVErDGEtVGEIVLRGSSIMLGYLKNPIGTQN 412
Cdd:COG0318 252 TSPV-VTVNPEDPGERRPGS--------VG-RPLPGVEVRIVDED-GRELP-PGE-VGEIVVRGPNVMKGYWNDPEATAE 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 413 SFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGl 492
Cdd:COG0318 319 AFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG- 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15222924 493 tRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAK 542
Cdd:COG0318 398 -AELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYA 446
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-539 |
3.84e-141 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 417.67 E-value: 3.84e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 9 ANSLPLTLLGFLERAATVYGDCTsIVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMS 88
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKE-AVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 89 GAILNNINTRLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITMLLNPPILVLIANEEEEEGGAEVTErskfcylYSDLI 168
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGE-------YEELL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 169 TRGNPDFKWIRPGsEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTypWGIAA 248
Cdd:PRK06187 153 AAASDTFDFPDID-ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWG--LPYLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 249 V--GGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSAsqesdQPLKSPVNF-----LTAGSSPPATVLLRA--ES 319
Cdd:PRK06187 230 LmaGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLK-----APRAYFVDFsslrlVIYGGAALPPALLREfkEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 320 LGFIVSHGYGLTETAGVIVScawkpnwNRLPASDQAQLKSRqgvRTVGFS----EIDVVDPEsGRSVERDGETVGEIVLR 395
Cdd:PRK06187 305 FGIDLVQGYGMTETSPVVSV-------LPPEDQLPGQWTKR---RSAGRPlpgvEARIVDDD-GDELPPDGGEVGEIIVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 396 GSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPD 475
Cdd:PRK06187 374 GPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPD 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 476 EFWGETPCAFVSLKPGLTrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK06187 454 EKWGERPVAVVVLKPGAT--LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
13-539 |
1.15e-136 |
|
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: 406.05 E-value: 1.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 13 PLTLLGFLERAATVYGDCTsivYGNsTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAIL 92
Cdd:cd05915 1 LERAAALFGRKEVVSRLHT---GEV-HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 93 NNINTRLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITMLLNppilvlianeeeeeGGAEVTERSKFcYLYSDLITRGN 172
Cdd:cd05915 77 HTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKT--------------VQHFVVMDEKA-PEGYLAYEEAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 173 PDFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFV--MTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVG 250
Cdd:cd05915 142 GEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLhsLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 251 GTNVCVRKLHAPS-IYHLIRDHGVTHMYGAPIVLQILSASQES-DQPLKSPVNFLTAGSSPPAtVLLRAESLG-FIVSHG 327
Cdd:cd05915 222 AKQVLPGPRLDPAsLVELFDGEGVTFTAGVPTVWLALADYLEStGHRLKTLRRLVVGGSAAPR-SLIARFERMgVEVRQG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 YGLTETAGVIVSCAWKPNWNRLPASDQAQLKSRQGVRTvgFSE-IDVVDPESgRSVERDGETVGEIVLRGSSIMLGYLKN 406
Cdd:cd05915 301 YGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPI--PLVrLRVADEEG-RPVPKDGKALGEVQLKGPWITGGYYGN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 407 PIGTQ-NSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAF 485
Cdd:cd05915 378 EEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 486 VSLKPGLTRkptDKEIIEYCKYKMPRY-MAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05915 458 VVPRGEKPT---PEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
20-534 |
1.17e-132 |
|
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: 392.74 E-value: 1.17e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 20 LERAATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRL 99
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSL-TYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 100 DARTVSVLLRHCESKLLFvdffysdlaveaitmllnppilvlianeeeeeggaevterskfcylysdlitrgnpDfkwir 179
Cdd:cd17631 80 TPPEVAYILADSGAKVLF--------------------------------------------------------D----- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 180 pgsewDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFH---ANGWTYPwgIAAVGGTNVCV 256
Cdd:cd17631 99 -----DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHiggLGVFTLP--TLLRGGTVVIL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 257 RKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRA-ESLGFIVSHGYGLTETAG 335
Cdd:cd17631 172 RKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRAlQARGVKFVQGYGMTETSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 336 VIVScawkpnwnrLPASDQaqlksRQGVRTVG----FSEIDVVDPEsGRSVErDGEtVGEIVLRGSSIMLGYLKNPIGTQ 411
Cdd:cd17631 252 GVTF---------LSPEDH-----RRKLGSAGrpvfFVEVRIVDPD-GREVP-PGE-VGEIVVRGPHVMAGYWNRPEATA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 412 NSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPG 491
Cdd:cd17631 315 AAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG 394
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15222924 492 ltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIK 534
Cdd:cd17631 395 --AELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
19-539 |
4.12e-125 |
|
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: 376.59 E-value: 4.12e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 19 FLERAATVYGDcTSIVYGNS----TVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNN 94
Cdd:cd12119 1 LLEHAARLHGD-REIVSRTHegevHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 95 INTRLDARTVSVLLRHCESKLLFVDFFYSDLaVEAITMLLnPPILVLIANEEEEEGGAEVTERSkfcYLYSDLITRGNPD 174
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPL-LEAIAPRL-PTVEHVVVMTDDAAMPEPAGVGV---LAYEELLAAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 175 FKWIRpGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTP--VYLWTLPIFHANGWTYPWGIAAVGGT 252
Cdd:cd12119 155 YDWPD-FDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSEsdVVLPVVPMFHVNAWGLPYAAAMVGAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 253 NVCV-RKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLT-AGSSPPATVLLRAESLGFIVSHGYGL 330
Cdd:cd12119 234 LVLPgPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVViGGSAVPRSLIEAFEERGVRVIHAWGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 331 TETAGVIVSCAWKPNWNRLPASDQAQLKSRQGvRTVGFSEIDVVDPEsGRSVERDGETVGEIVLRGSSIMLGYLKNPIGT 410
Cdd:cd12119 314 TETSPLGTVARPPSEHSNLSEDEQLALRAKQG-RPVPGVELRIVDDD-GRELPWDGKAVGELQVRGPWVTKSYYKNDEES 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 411 QNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKP 490
Cdd:cd12119 392 EALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15222924 491 GLTrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd12119 472 GAT--VTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
185-532 |
3.55e-98 |
|
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: 300.74 E-value: 3.55e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPSI 264
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 265 YHLIRDHGVTHMYGAPIVLQ-ILSASQESDQPLKSPVNFLTAGSSPPATVLLRAESL-GFIVSHGYGLTETAGViVSCAW 342
Cdd:cd04433 81 LELIEREKVTILLGVPTLLArLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGT-VATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 343 KPNWNRLPASDQaqlksrqgvRTVGFSEIDVVDPESGRsvERDGEtVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTG 422
Cdd:cd04433 160 PDDDARKPGSVG---------RPVPGVEVRIVDPDGGE--LPPGE-IGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 423 DLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGltRKPTDKEII 502
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG--ADLDAEELR 305
|
330 340 350
....*....|....*....|....*....|
gi 15222924 503 EYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd04433 306 AHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
20-446 |
3.28e-97 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 301.15 E-value: 3.28e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 20 LERAATVYGDCTSIVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRL 99
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 100 DARTVSVLLRHCESKLLFVDFFYSDLAVEAITMLLNPPILVLIANEEEEEGGAEVTERSKfcylysdlitRGNPDFKWIR 179
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAK----------PADVPPPPPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 180 PGSEWDPIVVNYTSGTTSSPKGVVHCHRGI--FVMTLDSL--TDWAVPKTPVYLWTLPIFHANGWTY-PWGIAAVGGTNV 254
Cdd:pfam00501 151 PPDPDDLAYIIYTSGTTGKPKGVMLTHRNLvaNVLSIKRVrpRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 255 CVRK---LHAPSIYHLIRDHGVTHMYGAP-IVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRAES-LGFIVSHGYG 329
Cdd:pfam00501 231 LPPGfpaLDPAALLELIERYKVTVLYGVPtLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRElFGGALVNGYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 330 LTETAGVIVscawkpnwNRLPASDQAQLKSRQGvRTVGFSEIDVVDPESGRSVErDGEtVGEIVLRGSSIMLGYLKNPIG 409
Cdd:pfam00501 311 LTETTGVVT--------TPLPLDEDLRSLGSVG-RPLPGTEVKIVDDETGEPVP-PGE-PGELCVRGPGVMKGYLNDPEL 379
|
410 420 430
....*....|....*....|....*....|....*...
gi 15222924 410 TQNSFKN-GWFFTGDLGVIHGDGYLEIKDRSKDVIISG 446
Cdd:pfam00501 380 TAEAFDEdGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
16-538 |
3.46e-97 |
|
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: 302.95 E-value: 3.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 16 LLGFLERAATVYGDCTSIVYGNSTvYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNI 95
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK-LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 96 NTRLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITMLLNPPIlvlianeeeeeggaevterskfcylysdlitrgNPDf 175
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVAL---------------------------------TPE- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 176 kwirpgsewDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLtDWAVPKTP---VYLWTLPIFHANGWT----YPWgiaA 248
Cdd:cd05936 126 ---------DVAVLQYTSGTTGVPKGAMLTHRNLVANALQIK-AWLEDLLEgddVVLAALPLFHVFGLTvallLPL---A 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 249 VGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSP-PATVLLR-AESLGFIVSH 326
Cdd:cd05936 193 LGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPlPVEVAERfEELTGVPIVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 327 GYGLTETAGVIvsCAWKPNWNRlpasdqaqlksRQGvrTVGFS----EIDVVDPEsGRSVErDGEtVGEIVLRGSSIMLG 402
Cdd:cd05936 273 GYGLTETSPVV--AVNPLDGPR-----------KPG--SIGIPlpgtEVKIVDDD-GEELP-PGE-VGELWVRGPQVMKG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 403 YLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETP 482
Cdd:cd05936 335 YWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAV 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15222924 483 CAFVSLKPGltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:cd05936 415 KAFVVLKEG--ASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
10-539 |
5.20e-91 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 288.34 E-value: 5.20e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 10 NSLPLTLLGFLERAATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSG 89
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRL-TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 90 AILNNINTRLDARTVSVLLRHCESKLLFVdffYSDLAVEAITMLLNPPILVLIANEEEEEGGAEVTERSKFcylySDLIT 169
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFV---LGLFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTF----TDFLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 170 RGNPDFKwIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGifvmTLDSLTDWA----VPKTPVYLWTLPIFHANGWTYPWg 245
Cdd:PRK07656 153 AGDPAER-APEVDPDDVADILFTSGTTGRPKGAMLTHRQ----LLSNAADWAeylgLTEGDRYLAANPFFHVFGYKAGV- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 246 IAAV--GGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQ-ILSASQESDQPLKSPVNFLTAGSSPPATVLLRAES-LG 321
Cdd:PRK07656 227 NAPLmrGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNsLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESeLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 322 F-IVSHGYGLTETAGVIVSCawkpnwnrlPASDqaqlkSRQGV-RTVGFS----EIDVVDpESGRSVErDGEtVGEIVLR 395
Cdd:PRK07656 307 VdIVLTGYGLSEASGVTTFN---------RLDD-----DRKTVaGTIGTAiagvENKIVN-ELGEEVP-VGE-VGELLVR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 396 GSSIMLGYLKNPIGTQNSFKN-GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARP 474
Cdd:PRK07656 370 GPNVMKGYYDDPEATAAAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVP 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 475 DEFWGETPCAFVSLKPGLTRkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK07656 450 DERLGEVGKAYVVLKPGAEL--TEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
15-542 |
4.23e-87 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 278.35 E-value: 4.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 15 TLLGFLERAATVYGDCTSIVYGnSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNN 94
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFG-DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 95 INTRLDARTVSVLLRHCESKLLFVDffySDLAVEAITMLLNPPILVLIANEEEEEggaevTERSKFCYLYSDLITRGNPD 174
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAFLVD---PALAPTAEAALALLPVDTLILSLVLGG-----REAPGGWLDFADWAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 175 FKWIRPGSEwDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANG---WTYPWgiAAVGG 251
Cdd:PRK08316 163 EPDVELADD-DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQldvFLGPY--LYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 252 TNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILsasqesdqpLKSPvNFLTA----------GSSP-PATVLLR-AES 319
Cdd:PRK08316 240 TNVILDAPDPELILRTIEAERITSFFAPPTVWISL---------LRHP-DFDTRdlsslrkgyyGASImPVEVLKElRER 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 320 L-GFIVSHGYGLTETAgvivscawkPNWNRLPASDQAQLKSRQGvRTVGFSEIDVVDpESGRSVErDGEtVGEIVLRGSS 398
Cdd:PRK08316 310 LpGLRFYNCYGQTEIA---------PLATVLGPEEHLRRPGSAG-RPVLNVETRVVD-DDGNDVA-PGE-VGEIVHRSPQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 399 IMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFW 478
Cdd:PRK08316 377 LMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKW 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 479 GETPCAFVSLKPGLTRkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAK 542
Cdd:PRK08316 457 IEAVTAVVVPKAGATV--TEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYA 518
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
41-538 |
8.20e-82 |
|
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: 261.46 E-value: 8.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDF 120
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 121 FysdlaveaitMLLnppilvlianeeeeeggaevterskfcylysdlitrgnpdfkwirpgsewdpivvnYTSGTTSSPK 200
Cdd:cd05934 84 A----------SIL--------------------------------------------------------YTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 201 GVVHCHRgiFVMTLDSLTDWAVPKTP--VYLWTLPIFHANGWTYPWGIA-AVGGTNVCVRKLHAPSIYHLIRDHGVTHMY 277
Cdd:cd05934 98 GVVITHA--NLTFAGYYSARRFGLGEddVYLTVLPLFHINAQAVSVLAAlSVGATLVLLPRFSASRFWSDVRRYGATVTN 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 278 GAPIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRAESLGFIVSHGYGLTETAGVIVScawkpnwnrlpASDQAQL 357
Cdd:cd05934 176 YLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIG-----------PRDEPRR 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 358 KSRQGVRTVGFsEIDVVDPEsGRSVErDGETvGEIVLR---GSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLE 434
Cdd:cd05934 245 PGSIGRPAPGY-EVRIVDDD-GQELP-AGEP-GELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFY 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 435 IKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKPTdkEIIEYCKYKMPRYMA 514
Cdd:cd05934 321 FVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE--ELFAFCEGQLAYFKV 398
|
490 500
....*....|....*....|....
gi 15222924 515 PKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:cd05934 399 PRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
11-542 |
1.06e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 256.94 E-value: 1.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 11 SLPLTLLGFLERAATVYGDcTSIVY----GNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVP 86
Cdd:PRK07008 7 DMPLLISSLIAHAARHAGD-TEIVSrrveGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 87 MSGAILNNINTRLDARTVSVLLRHCESKLLFVDFFYSDLaVEAITMLLnPPILVLIAneeeeeggaeVTERSKF------ 160
Cdd:PRK07008 86 GSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTFLPL-VDALAPQC-PNVKGWVA----------MTDAAHLpagstp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 161 --CylYSDLITRGNPDFKWIRpGSEWDPIVVNYTSGTTSSPKGVVHCHRGIF----------VMTLdSLTDWAVPktpvy 228
Cdd:PRK07008 154 llC--YETLVGAQDGDYDWPR-FDENQASSLCYTSGTTGNPKGALYSHRSTVlhaygaalpdAMGL-SARDAVLP----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 229 lwTLPIFHANGWTYPWGIAAVGGTNVCV-RKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGS 307
Cdd:PRK07008 225 --VVPMFHVNAWGLPYSAPLTGAKLVLPgPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 308 S--PPATVLLRAESLGFIVSHGYGLTETAGVIVSCAWKPNWNRLPASDQAQLKSRQGvRTVGFSEIDVVDPEsGRSVERD 385
Cdd:PRK07008 303 SacPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQLPLDEQRKLLEKQG-RVIYGVDMKIVGDD-GRELPWD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 386 GETVGEIVLRGSSIMLGYLKnpiGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAV 465
Cdd:PRK07008 381 GKAFGDLQVRGPWVIDRYFR---GDASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222924 466 NEAAVVARPDEFWGETPCAFVSLKPG--LTRkptdKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAK 542
Cdd:PRK07008 458 AEAACIACAHPKWDERPLLVVVKRPGaeVTR----EELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR 532
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
13-543 |
1.88e-78 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 256.60 E-value: 1.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 13 PLTLLGFLERAATVYGD---CTSIVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSG 89
Cdd:PRK06018 9 PLLCHRIIDHAARIHGNrevVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 90 AILNNINTRLDARTVSVLLRHCESKLLFVDffysdlaveaITMLlnpPILVLIANEEEEEGGAEV-TERS-------KFC 161
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIINHAEDRVVITD----------LTFV---PILEKIADKLPSVERYVVlTDAAhmpqttlKNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 162 YLYSDLITRGNPDFKWiRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTL-----DSLtdwAVPKTPVYLWTLPIFH 236
Cdd:PRK06018 156 VAYEEWIAEADGDFAW-KTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALmanngDAL---GTSAADTMLPVVPLFH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 237 ANGWtypwGIAAVG---GTNVCV--RKLHAPSIYHLIRDHGVTHMYGAPIV-LQILSASQESDQPLKSPVNFLTAGSSPP 310
Cdd:PRK06018 232 ANSW----GIAFSApsmGTKLVMpgAKLDGASVYELLDTEKVTFTAGVPTVwLMLLQYMEKEGLKLPHLKMVVCGGSAMP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 311 ATVLLRAESLGFIVSHGYGLTETAGVIVSCAWKPNWNRLPASDQAQLKSRQGVRTVGFsEIDVVDPEsGRSVERDGETVG 390
Cdd:PRK06018 308 RSMIKAFEDMGVEVRHAWGMTEMSPLGTLAALKPPFSKLPGDARLDVLQKQGYPPFGV-EMKITDDA-GKELPWDGKTFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 391 EIVLRGSSIMLGYLKnpIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAV 470
Cdd:PRK06018 386 RLKVRGPAVAAAYYR--VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222924 471 VARPDEFWGETPCAFVSLKPGLTrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAKN 543
Cdd:PRK06018 464 IGVYHPKWDERPLLIVQLKPGET--ATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKD 534
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
40-539 |
8.46e-78 |
|
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: 251.53 E-value: 8.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 40 VYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVd 119
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 120 ffysdlaveaitmllnppilvlianeeeeeggaevTERskfcylysdlitrgnpdFKWIRPGSEWDPI-VVNYTSGTTSS 198
Cdd:cd05903 80 -----------------------------------PER-----------------FRQFDPAAMPDAVaLLLFTSGTTGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 199 PKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPS-IYHLIRDHGVTHMY 277
Cdd:cd05903 108 PKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDkALALMREHGVTFMM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 278 GA-PIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRA-ESLGFIVSHGYGLTETAGVIVSCAwkpnwnrlpaSDQA 355
Cdd:cd05903 188 GAtPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAaELLGAKVCSAYGSTECPGAVTSIT----------PAPE 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 356 QLKSRQGVRTVGFSEIDVVDpesGRSVERDGETVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEI 435
Cdd:cd05903 258 DRRLYTDGRPLPGVEIKVVD---DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRI 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 436 KDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTrkPTDKEIIEYC-KYKMPRYMA 514
Cdd:cd05903 335 TGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGAL--LTFDELVAYLdRQGVAKQYW 412
|
490 500
....*....|....*....|....*
gi 15222924 515 PKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05903 413 PERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
19-543 |
1.28e-76 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 252.34 E-value: 1.28e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 19 FLERAATVYGDCTSIVY----GNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNN 94
Cdd:COG0365 14 CLDRHAEGRGDKVALIWegedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 95 INTRLDARTVSVLLRHCESKLLFVD---------FFYSDLAVEAITMLLNPPILVLIANEEEEEGGAEVterskfcYLYS 165
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITAdgglrggkvIDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGD-------LDWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 166 DLITRGNPDFKWIRPGSEwDPIVVNYTSGTTSSPKGVVHCHRGIFV---MTLDSLTDWavpkTP--VYLWTLPIfhanGW 240
Cdd:COG0365 167 ELLAAASAEFEPEPTDAD-DPLFILYTSGTTGKPKGVVHTHGGYLVhaaTTAKYVLDL----KPgdVFWCTADI----GW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 241 TY-PWGIA----AVGGTNVCVR-KLHAPS---IYHLIRDHGVTHMYGAPIVLQILSasQESDQPLK----SPVNFL-TAG 306
Cdd:COG0365 238 ATgHSYIVygplLNGATVVLYEgRPDFPDpgrLWELIEKYGVTVFFTAPTAIRALM--KAGDEPLKkydlSSLRLLgSAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 307 SSPPATVLLRA-ESLGFIVSHGYGLTETAGVIVSCAW----KPNWNrlpasdqaqlksrqGVRTVGFsEIDVVDPEsGRS 381
Cdd:COG0365 316 EPLNPEVWEWWyEAVGVPIVDGWGQTETGGIFISNLPglpvKPGSM--------------GKPVPGY-DVAVVDED-GNP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 382 VERDgeTVGEIVLRGS--SIMLGYLKNPIGTQNSFKN---GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVE 456
Cdd:COG0365 380 VPPG--EEGELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 457 AVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTrkPTD---KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKII 533
Cdd:COG0365 458 SALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVE--PSDelaKELQAHVREELGPYAYPREIEFVDELPKTRSGKIM 535
|
570
....*....|
gi 15222924 534 KSLLKEIAKN 543
Cdd:COG0365 536 RRLLRKIAEG 545
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
19-544 |
1.13e-74 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 245.15 E-value: 1.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 19 FLERAATVYGDCTSIVyGNSTVYTWRETNHRCLCVASAL-SSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINT 97
Cdd:PRK06839 7 WIEKRAYLHPDRIAII-TEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 98 RLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITML-LNPPIlvlianeeeeeggaEVTErskfcylYSDLITRGNPDFK 176
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSyVQRVI--------------SITS-------LKEIEDRKIDNFV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 177 wirPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANG---WTYPWGIAavGGTN 253
Cdd:PRK06839 145 ---EKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGiglFAFPTLFA--GGVI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 254 VCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRA-ESLGFIVSHGYGLTE 332
Cdd:PRK06839 220 IVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREfIDRGFLFGQGFGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 333 TAGVIVscawkpnwnrLPASDQAQLKSRQGVRTVGFSEIDVVDPESGRsVERDGetVGEIVLRGSSIMLGYLKNPIGTQN 412
Cdd:PRK06839 300 TSPTVF----------MLSEEDARRKVGSIGKPVLFCDYELIDENKNK-VEVGE--VGELLIRGPNVMKEYWNRPDATEE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 413 SFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGL 492
Cdd:PRK06839 367 TIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSS 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15222924 493 TRkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAKNM 544
Cdd:PRK06839 447 VL--IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKSR 496
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
33-539 |
1.50e-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: 239.52 E-value: 1.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 33 IVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCE 112
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 113 SKLLFVDffySDLAVEAITMLLNPPILVLianeeeeeggaEVTERSKFCYLYSDLITRGNPDFKWIRPGSEW-----DPI 187
Cdd:cd05926 87 SKLVLTP---KGELGPASRAASKLGLAIL-----------ELALDVGVLIRAPSAESLSNLLADKKNAKSEGvplpdDLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 188 VVNYTSGTTSSPKGVVHCHRGIFVMTLD-----SLTdwavPKTPVYLwTLPIFHANGWtypwgIAAV------GGTNVCV 256
Cdd:cd05926 153 LILHTSGTTGRPKGVPLTHRNLAASATNitntyKLT----PDDRTLV-VMPLFHVHGL-----VASLlstlaaGGSVVLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 257 RKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPL-KSPVNFLTAGSSP-PATVLLRAE-SLGFIVSHGYGLTET 333
Cdd:cd05926 223 PRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASlPPAVLEALEaTFGAPVLEAYGMTEA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 334 AGVIVScawkpnwNRLPASdqaqlKSRQGvrTVGFS---EIDVVDpESGRSVErDGEtVGEIVLRGSSIMLGYLKNPIGT 410
Cdd:cd05926 303 AHQMTS-------NPLPPG-----PRKPG--SVGKPvgvEVRILD-EDGEILP-PGV-VGEICLRGPNVTRGYLNNPEAN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 411 Q-NSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLK 489
Cdd:cd05926 366 AeAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLR 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15222924 490 PGltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05926 446 EG--ASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
41-539 |
5.20e-71 |
|
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: 233.01 E-value: 5.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLdarTVSVLLRHCESkllfvdf 120
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRL---TPNELAFQLKD------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 121 fySDLAVEAITMLLnppilvlianeeeeeggaevterskfcylysdlitrgnpdfkwirpgsewdpivvnYTSGTTSSPK 200
Cdd:cd05912 72 --SDVKLDDIATIM--------------------------------------------------------YTSGTTGKPK 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 201 GVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAP 280
Cdd:cd05912 94 GVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVP 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 281 IVLQILSAsqesDQPLKSPVNF---LTAGSSPPATVLLRAESLGFIVSHGYGLTETAGVIVSCAWKPNWNRLPASDQAqL 357
Cdd:cd05912 174 TMLQRLLE----ILGEGYPNNLrciLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKP-L 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 358 KSrqgvrtvgfSEIDVVDPESGRsverdgETVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKD 437
Cdd:cd05912 249 FP---------VELKIEDDGQPP------YEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 438 RSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKpgltRKPTDKEIIEYCKYKMPRYMAPKT 517
Cdd:cd05912 314 RRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE----RPISEEELIAYCSEKLAKYKVPKK 389
|
490 500
....*....|....*....|..
gi 15222924 518 VSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05912 390 IYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
31-544 |
2.01e-70 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 233.70 E-value: 2.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 31 TSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRH 110
Cdd:PRK03640 19 TAIEFEEKKV-TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 111 CESKLLFVDFFYSDLAVEAITMLlnppilvlianeeeeeggaevterskfcylYSDLITRGNPDFKWIRPGSEWDPIVVN 190
Cdd:PRK03640 98 AEVKCLITDDDFEAKLIPGISVK------------------------------FAELMNGPKEEAEIQEEFDLDEVATIM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGIFVMTLDS-----LTD---WavpktpvyLWTLPIFHANGWT-------YpwgiaavGGTNVC 255
Cdd:PRK03640 148 YTSGTTGKPKGVIQTYGNHWWSAVGSalnlgLTEddcW--------LAAVPIFHISGLSilmrsviY-------GMRVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 256 VRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQplkSPVNF---LTAGSSPPATVLLRAESLGFIVSHGYGLTE 332
Cdd:PRK03640 213 VEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGT---YPSSFrcmLLGGGPAPKPLLEQCKEKGIPVYQSYGMTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 333 TAGVIVScawkpnwnrLPASDqaqlkSRQGVRTVG---FS-EIDVV-DPESGRSVErdgetVGEIVLRGSSIMLGYLKNP 407
Cdd:PRK03640 290 TASQIVT---------LSPED-----ALTKLGSAGkplFPcELKIEkDGVVVPPFE-----EGEIVVKGPNVTKGYLNRE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 408 IGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVS 487
Cdd:PRK03640 351 DATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 488 lkpgLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAKNM 544
Cdd:PRK03640 431 ----KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
15-542 |
7.48e-68 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 228.40 E-value: 7.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 15 TLLGFLERAATVYGDCTSIV-----YGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSG 89
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 90 AILNNINTRLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITMLLNP--PIL--VLIANEEEEEGgaevterskFCYLYS 165
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPelPALrhVVVVGGDGADS---------FEALLI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 166 DLITRGNPDFKWI----RPGSEwDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWT 241
Cdd:PRK13295 176 TPAWEQEPDAPAIlarlRPGPD-DVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 242 YPWGIAAVGGTNVCVRKLHAPSIY-HLIRDHGVTHMYGA-PIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRA-E 318
Cdd:PRK13295 255 YGLMMPVMLGATAVLQDIWDPARAaELIRTEGVTFTMAStPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERArA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 319 SLGFIVSHGYGLTETAGVIVSCawkpnwnrlPASDQAQLKSRQGVRTVGFsEIDVVDPEsGRSVERDgeTVGEIVLRGSS 398
Cdd:PRK13295 335 ALGAKIVSAWGMTENGAVTLTK---------LDDPDERASTTDGCPLPGV-EVRVVDAD-GAPLPAG--QIGRLQVRGCS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 399 IMLGYLKNPIGTQNSFkNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFW 478
Cdd:PRK13295 402 NFGGYLKRPQLNGTDA-DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 479 GETPCAFVSLKPGLTRkpTDKEIIEYCK-YKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAK 542
Cdd:PRK13295 481 GERACAFVVPRPGQSL--DFEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLR 543
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
6-540 |
9.06e-68 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 228.10 E-value: 9.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 6 PSAANSLPL---TLLGFLERAATVYGDCTsIVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQ 82
Cdd:PRK06155 10 ARAVDPLPPserTLPAMLARQAERYPDRP-LLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 83 FSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFFYSDlAVEAITMLLNPPILVLIANEEEEEGGAEVterskfcY 162
Cdd:PRK06155 89 LGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLA-ALEAADPGDLPLPAVWLLDAPASVSVPAG-------W 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 163 LYSDLITRGNP-DFKWIRPGsewDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWT 241
Cdd:PRK06155 161 STAPLPPLDAPaPAAAVQPG---DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 242 YPWGIAAVGGTNVCVRKLHAPSIYHLIRDHG--VTHMYGApiVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRAES 319
Cdd:PRK06155 238 AFFQALLAGATYVLEPRFSASGFWPAVRRHGatVTYLLGA--MVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 320 LGFIVSHGYGLTETAGVIVscawkpnwnrlpASDQAQLKSRQGVRTVGFsEIDVVDpESGRSVErDGEtVGEIVLRGS-- 397
Cdd:PRK06155 316 FGVDLLDGYGSTETNFVIA------------VTHGSQRPGSMGRLAPGF-EARVVD-EHDQELP-DGE-PGELLLRADep 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 398 -SIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDE 476
Cdd:PRK06155 380 fAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSE 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 477 FWGETPCAFVSLKPGLTRKPTDkeIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEI 540
Cdd:PRK06155 460 LGEDEVMAAVVLRDGTALEPVA--LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
12-544 |
1.45e-67 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 228.16 E-value: 1.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 12 LPLTLLGFLERAATVYGDCTSIVYGNSTV-YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGA 90
Cdd:PRK08315 14 LEQTIGQLLDRTAARYPDREALVYRDQGLrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 91 ILNNINTRLDARTVSVLLRHCESKLLF-VDFF----YSDLAVEAITMLLNPPILVLIANEEEEEGGAEV--TERSKFCYL 163
Cdd:PRK08315 94 ILVTINPAYRLSELEYALNQSGCKALIaADGFkdsdYVAMLYELAPELATCEPGQLQSARLPELRRVIFlgDEKHPGMLN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 164 YSDLITRGN--PDFKWIRPGSE---WDPIVVNYTSGTTSSPKGVVHCHRGI-----FV---MTL---DSLTdwavpkTPV 227
Cdd:PRK08315 174 FDELLALGRavDDAELAARQATldpDDPINIQYTSGTTGFPKGATLTHRNIlnngyFIgeaMKLteeDRLC------IPV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 228 ylwtlPIFHANGwtypwgiaAVGGTNVCVrklhapsiyhlirdhgvTHmyGAPIV--------LQILSASQ--------- 290
Cdd:PRK08315 248 -----PLYHCFG--------MVLGNLACV-----------------TH--GATMVypgegfdpLATLAAVEeerctalyg 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 291 -------ESDQPLKSPVNFLT------AGSSPPATVLLRAESLGFI--VSHGYGLTETAgvivscawkpnwnrlPASDQA 355
Cdd:PRK08315 296 vptmfiaELDHPDFARFDLSSlrtgimAGSPCPIEVMKRVIDKMHMseVTIAYGMTETS---------------PVSTQT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 356 Q----LKSRqgVRTVG----FSEIDVVDPESGRSVERdGETvGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGV 426
Cdd:PRK08315 361 RtddpLEKR--VTTVGralpHLEVKIVDPETGETVPR-GEQ-GELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 427 IHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTrkPTDKEIIEYCK 506
Cdd:PRK08315 437 MDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGAT--LTEEDVRDFCR 514
|
570 580 590
....*....|....*....|....*....|....*...
gi 15222924 507 YKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAKNM 544
Cdd:PRK08315 515 GKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
37-532 |
2.87e-67 |
|
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: 225.17 E-value: 2.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 37 NSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLL 116
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 117 FVD-FFYSDL--AVEAITMllNPPILVL-IANEEEEEGGAEVTERSKFC--YLYSDLITRGNpdfkwirpgsewDPIVVN 190
Cdd:cd05911 87 FTDpDGLEKVkeAAKELGP--KDKIIVLdDKPDGVLSIEDLLSPTLGEEdeDLPPPLKDGKD------------DTAAIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGI---FVMTLDSLTDWAVPKTPVYLwTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPSIYHL 267
Cdd:cd05911 153 YSSGTTGLPKGVCLSHRNLianLSQVQTFLYGNDGSNDVILG-FLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 268 IRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSPpatVLLRAESL------GFIVSHGYGLTETAGVivsCA 341
Cdd:cd05911 232 IEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAP---LSKELQELlakrfpNATIKQGYGMTETGGI---LT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 342 WKPNWNRLPASdqaqlksrqgvrtVG----FSEIDVVDPESGRSVERDgeTVGEIVLRGSSIMLGYLKNPIGTQNSF-KN 416
Cdd:cd05911 306 VNPDGDDKPGS-------------VGrllpNVEAKIVDDDGKDSLGPN--EPGEICVRGPQVMKGYYNNPEATKETFdED 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 417 GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGltRKP 496
Cdd:cd05911 371 GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG--EKL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15222924 497 TDKEIIEYCKYKMPRYmapK----TVSFLEELPKTSTGKI 532
Cdd:cd05911 449 TEKEVKDYVAKKVASY---KqlrgGVVFVDEIPKSASGKI 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
10-537 |
3.71e-66 |
|
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: 222.88 E-value: 3.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 10 NSLPLTLLGFLerAATVYGDCTSIVYG-NSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMS 88
Cdd:cd05904 3 TDLPLDSVSFL--FASAHPSRPALIDAaTGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 89 GAILNNINTRLDARTVSVLLRHCESKLLFVDffySDLaVEAITMLLNPPILVlianeeeeeggAEVTERSKFCYLYSDLI 168
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFTT---AEL-AEKLASLALPVVLL-----------DSAEFDSLSFSDLLFEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 169 TRGNPDFKWIRPGsewDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWA--VPKTPVYLWTLPIFHANGWT-YPWG 245
Cdd:cd05904 146 DEAEPPVVVIKQD---DVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSsFALG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 246 IAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAP-IVLQILSASQESDQPLKSpVNFLTAGSSPPATVLLRAESLGF-- 322
Cdd:cd05904 223 LLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPpIVLALVKSPIVDKYDLSS-LRQIMSGAAPLGKELIEAFRAKFpn 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 323 -IVSHGYGLTETAGVIVSCawkpnwnrlpaSDQAQLKSRQGvrTVGF----SEIDVVDPESGRSVERdGETvGEIVLRGS 397
Cdd:cd05904 302 vDLGQGYGMTESTGVVAMC-----------FAPEKDRAKYG--SVGRlvpnVEAKIVDPETGESLPP-NQT-GELWIRGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 398 SIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDE 476
Cdd:cd05904 367 SIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDE 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222924 477 FWGETPCAFVSLKPGLTRkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:cd05904 447 EAGEVPMAFVVRKPGSSL--TEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
42-537 |
1.62e-65 |
|
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: 219.24 E-value: 1.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFF 121
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 122 YSDLAVEAITMllnppilvlianeeeeeggaevterskfcylySDLITRGNPDFKWIRPGSEWDPIVVNYTSGTTSSPKG 201
Cdd:TIGR01923 81 LEEKDFQADSL--------------------------------DRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 202 VVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRKLHApsIYHLIRDHGVTHMYGAPI 281
Cdd:TIGR01923 129 VPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 282 VLQILSASQESDQPLKSpvnFLTAGSSPPATVLLRAESLGFIVSHGYGLTETAGVIVScawkpnwnrlpasdqaqlksrq 361
Cdd:TIGR01923 207 QLNRLLDEGGHNENLRK---ILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTT---------------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 362 gVRTVGFSE-IDVVDPESGRSV--ERDG-ETVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKD 437
Cdd:TIGR01923 262 -ATPEMLHArPDVGRPLAGREIkiKVDNkEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 438 RSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKpgltRKPTDKEIIEYCKYKMPRYMAPKT 517
Cdd:TIGR01923 341 RRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE----SDISQAKLIAYLTEKLAKYKVPIA 416
|
490 500
....*....|....*....|
gi 15222924 518 VSFLEELPKTSTGKIIKSLL 537
Cdd:TIGR01923 417 FEKLDELPYNASGKILRNQL 436
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
185-532 |
6.32e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 218.72 E-value: 6.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTdWaVP----KTPVYLWTLPIFHANGWTYPWGIA-AVGGTNVCVRKL 259
Cdd:PRK05605 220 DVALILYTSGTTGKPKGAQLTHRNLFANAAQGKA-W-VPglgdGPERVLAALPMFHAYGLTLCLTLAvSIGGELVLLPAP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 260 HAPSIYHLIRDHGVTHMYGAPIVLQ-ILSASQESDQPLKSPVNFLTAGSSPPATVLLRAESL--GFIVsHGYGLTETAGV 336
Cdd:PRK05605 298 DIDLILDAMKKHPPTWLPGVPPLYEkIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLtgGLLV-EGYGLTETSPI 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 337 IVScawkpnwNrlPASDQAqlksRQGVRTVGF--SEIDVVDPESGRSVERDGETvGEIVLRGSSIMLGYLKNPIGTQNSF 414
Cdd:PRK05605 377 IVG-------N--PMSDDR----RPGYVGVPFpdTEVRIVDPEDPDETMPDGEE-GELLVRGPQVFKGYWNRPEETAKSF 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 415 KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTr 494
Cdd:PRK05605 443 LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAA- 521
|
330 340 350
....*....|....*....|....*....|....*....
gi 15222924 495 kpTDKEII-EYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:PRK05605 522 --LDPEGLrAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
20-539 |
1.22e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 217.34 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 20 LERAATVYGDCTSIVY-GNSTvyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTR 98
Cdd:PRK07786 23 LARHALMQPDAPALRFlGNTT--TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 99 LDARTVSVLLRHCESKLLFVDFFYSDLA--VEAITMLLNppiLVLIANEEEEEGGAEvterskfcylYSDLITRGNPDFK 176
Cdd:PRK07786 101 LTPPEIAFLVSDCGAHVVVTEAALAPVAtaVRDIVPLLS---TVVVAGGSSDDSVLG----------YEDLLAEAGPAHA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 177 WIR-PgsEWDPIVVNYTSGTTSSPKGVVHCH--------RGIFVMTLDSLTDwavpktpVYLWTLPIFHangwtypwgIA 247
Cdd:PRK07786 168 PVDiP--NDSPALIMYTSGTTGRPKGAVLTHanltgqamTCLRTNGADINSD-------VGFVGVPLFH---------IA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 248 AVGGTNVCVRkLHAPSIYH------------LIRDHGVTHMYGAPIVLQILSASQESdQPLKSPVNFLTAGSSPPATVLL 315
Cdd:PRK07786 230 GIGSMLPGLL-LGAPTVIYplgafdpgqlldVLEAEKVTGIFLVPAQWQAVCAEQQA-RPRDLALRVLSWGAAPASDTLL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 316 RAESLGF----IVShGYGLTETAGVivSCAwkpnwnrlpasdqaqLKSRQGVRTVGfSEIDVVDPESGRSVERD------ 385
Cdd:PRK07786 308 RQMAATFpeaqILA-AFGQTEMSPV--TCM---------------LLGEDAIRKLG-SVGKVIPTVAARVVDENmndvpv 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 386 GEtVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAV 465
Cdd:PRK07786 369 GE-VGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDI 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 466 NEAAVVARPDEFWGETPCAFVSLKPGLTRKPTDkEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK07786 448 VEVAVIGRADEKWGEVPVAVAAVRNDDAALTLE-DLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
21-539 |
2.08e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 215.52 E-value: 2.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 21 ERAATVYGDcTSIVYGnstvytwrETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLD 100
Cdd:PRK06145 17 DRAALVYRD-QEISYA--------EFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 101 ARTVSVLLRHCESKLLFVDffySDLAVEAItmlLNPPILVLIANEEEEeggaevterskfcylySDLITRGNPDFKWIRP 180
Cdd:PRK06145 88 ADEVAYILGDAGAKLLLVD---EEFDAIVA---LETPKIVIDAAAQAD----------------SRRLAQGGLEIPPQAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 181 GSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPwGIA--AVGGTNVCVRK 258
Cdd:PRK06145 146 VAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLP-GIAvlWVGGTLRIHRE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 LHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRAESLGFIVSH---GYGLTETAG 335
Cdd:PRK06145 225 FDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARyidAYGLTETCS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 336 vivscawkpnWNRLPASDQAQLKSRQGVRTVGFSEIDVVDpESGRSVERDGEtvGEIVLRGSSIMLGYLKNPIGTQNSFK 415
Cdd:PRK06145 305 ----------GDTLMEAGREIEKIGSTGRALAHVEIRIAD-GAGRWLPPNMK--GEICMRGPKVTKGYWKDPEKTAEAFY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 416 NGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRk 495
Cdd:PRK06145 372 GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATL- 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15222924 496 pTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK06145 451 -TLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
15-541 |
2.15e-62 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 214.25 E-value: 2.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 15 TLLGFLERAATVYGDCTSIVYGNSTV-YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILN 93
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALrYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 94 NINTRLDARTVSVLLRHCESKLLF-VDFFYSDlavEAITMLLNppilvLIANEEEEEGGAEVTERSKF----CYL----- 163
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVIcADAFKTS---DYHAMLQE-----LLPGLAEGQPGALACERLPElrgvVSLapapp 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 164 -----YSDLITRG---NPDFKWIRPGS--EWDPIVVNYTSGTTSSPKGVVHCHRGI-----FVMTLDSLTDWAVPKTPVy 228
Cdd:PRK12583 171 pgflaWHELQARGetvSREALAERQASldRDDPINIQYTSGTTGFPKGATLSHHNIlnngyFVAESLGLTEHDRLCVPV- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 229 lwtlPIFHANGWTYP-WGIAAVGGTNVCVRKLHAP-SIYHLIRDHGVTHMYGAP-IVLQILSASQESDQPLKSPVNFLTA 305
Cdd:PRK12583 250 ----PLYHCFGMVLAnLGCMTVGACLVYPNEAFDPlATLQAVEEERCTALYGVPtMFIAELDHPQRGNFDLSSLRTGIMA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 306 GSSPPATVLLR--AESLGFIVSHGYGLTETAGVIVSCAwkpnwnrlpASDQAQLKsrqgVRTVGFS----EIDVVDPEsG 379
Cdd:PRK12583 326 GAPCPIEVMRRvmDEMHMAEVQIAYGMTETSPVSLQTT---------AADDLERR----VETVGRTqphlEVKVVDPD-G 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 380 RSVERdGEtVGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAV 458
Cdd:PRK12583 392 ATVPR-GE-IGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 459 LYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:PRK12583 470 LFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPG--HAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
...
gi 15222924 539 EIA 541
Cdd:PRK12583 548 EIS 550
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
7-539 |
2.79e-62 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 214.26 E-value: 2.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 7 SAANSLPLTLLGFLERAATVYGDCTSIVYGNST--VYTWRETNHRCLCVASAL-SSIGIGRSDVVSVLSANTPEMYELQF 83
Cdd:PRK05620 3 STMQDVPLSLTRILEYGSTVHGDTTVTTWGGAEqeQTTFAAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 84 SVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDffySDLAVEAITMLLNPPIL--VLIANEEEEEGGAEVTERSKFC 161
Cdd:PRK05620 83 AVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD---PRLAEQLGEILKECPCVraVVFIGPSDADSAAAHMPEGIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 162 YLYSDLITRGNPDFKWirPG-SEWDPIVVNYTSGTTSSPKGVVHCHRGIFV--MTLDSLTDWAVPKTPVYLWTLPIFHAN 238
Cdd:PRK05620 160 YSYEALLDGRSTVYDW--PElDETTAAAICYSTGTTGAPKGVVYSHRSLYLqsLSLRTTDSLAVTHGESFLCCVPIYHVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 239 GWTYPwgIAA-VGGTNVCV--RKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSS--PPATV 313
Cdd:PRK05620 238 SWGVP--LAAfMSGTPLVFpgPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSavPPILI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 314 LLRAESLGFIVSHGYGLTETAGV-IVScawkpnwnRLPA--SDQAQLKSR--QGVRTVGFsEIDVVDpeSGRSVERDGET 388
Cdd:PRK05620 316 KAWEERYGVDVVHVWGMTETSPVgTVA--------RPPSgvSGEARWAYRvsQGRFPASL-EYRIVN--DGQVMESTDRN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 389 VGEIVLRGSSIMLGYLKNPI----GTQNSFK-------------NGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVS 451
Cdd:PRK05620 385 EGEIQVRGNWVTASYYHSPTeeggGAASTFRgedvedandrftaDGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIY 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 452 SVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTR-KPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTG 530
Cdd:PRK05620 465 SAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPtRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVG 544
|
....*....
gi 15222924 531 KIIKSLLKE 539
Cdd:PRK05620 545 KFDKKDLRQ 553
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
15-539 |
2.10e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 211.36 E-value: 2.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 15 TLLGFLERAATVYGDCTSIV-YGNStvYTWRETNHRCLCVASALSS-IGIGRSDVVSVLSANTPEMYELQFSVPMSGAIL 92
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIVfYGRA--ISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 93 NNINTRLDARTVSVLLRHCESKLLFVDffySDLAVEAITMLLNPPILVLI---------ANEEEEEGGAEVTERSKFCYL 163
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVG---SELAPKVAPAVGNLRLRHVIvaqysdylpAEPEIAVPAWLRAEPPLQALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 164 YSDLITrgnpdfkW-------IRPGSEW----DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSlTDWA-VPKTPVYLWT 231
Cdd:PRK08314 166 PGGVVA-------WkealaagLAPPPHTagpdDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS-VLWSnSTPESVVLAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 232 LPIFHANGWTYPWGIAAVGGTNVCV-----RKLHApsiyHLIRDHGVTHMYGAP-IVLQILSASQESDQPLKSPVNFLTA 305
Cdd:PRK08314 238 LPLFHVTGMVHSMNAPIYAGATVVLmprwdREAAA----RLIERYRVTHWTNIPtMVVDFLASPGLAERDLSSLRYIGGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 306 GSSPPATV---LLRAESLGFIvsHGYGLTETAGVIVScawkpnwNRLPASDQAQLksrqGVRTVGfseID--VVDPESGR 380
Cdd:PRK08314 314 GAAMPEAVaerLKELTGLDYV--EGYGLTETMAQTHS-------NPPDRPKLQCL----GIPTFG---VDarVIDPETLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 381 SVErDGEtVGEIVLRGSSIMLGYLKNPIGTQNSF--KNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVE 456
Cdd:PRK08314 378 ELP-PGE-VGEIVVHGPQVFKGYWNRPEATAEAFieIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 457 AVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSL 536
Cdd:PRK08314 456 NLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQ 535
|
...
gi 15222924 537 LKE 539
Cdd:PRK08314 536 LQE 538
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
181-537 |
6.88e-61 |
|
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: 206.95 E-value: 6.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 181 GSEWDPI-VVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIA-AVGGTNVCVRK 258
Cdd:cd05935 80 GSELDDLaLIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAvYVGGTYVLMAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 LHAPSIYHLIRDHGVTHMYGAPIVLQILSASQE-SDQPLKSPVNFLTAGSSPPATVLLRAESL-GFIVSHGYGLTETagv 336
Cdd:cd05935 160 WDRETALELIEKYKVTFWTNIPTMLVDLLATPEfKTRDLSSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTET--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 337 ivsCAwkPNWNRLPASDQAQLksrQGVrtvGFSEID--VVDPESGRsvERDGETVGEIVLRGSSIMLGYLKNPIGTQNSF 414
Cdd:cd05935 237 ---MS--QTHTNPPLRPKLQC---LGI---P*FGVDarVIDIETGR--ELPPNEVGEIVVRGPQIFKGYWNRPEETEESF 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 415 --KNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKP 490
Cdd:cd05935 304 ieIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15222924 491 GLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:cd05935 384 EYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
22-539 |
1.27e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 208.69 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 22 RAATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMyelqFSVPMSGAILNNINTRL-- 99
Cdd:PRK06188 20 SALKRYPDRPALVLGDTRL-TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEV----LMAIGAAQLAGLRRTALhp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 100 -----DARTVsvlLRHCESKLLFVD---FFYSDLAVEAITMLLnPPILVLIAneeeeeggaevterskfCYLYSDLITRG 171
Cdd:PRK06188 95 lgsldDHAYV---LEDAGISTLIVDpapFVERALALLARVPSL-KHVLTLGP-----------------VPDGVDLLAAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 172 NP-DFKWIRPGSEW-DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWT-YPwgIAA 248
Cdd:PRK06188 154 AKfGPAPLVAAALPpDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFfLP--TLL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 249 VGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVL-QILSASQESDQPLKSpVNFLTAGSSPPATVLLRA--ESLGFIVS 325
Cdd:PRK06188 232 RGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIyALLDHPDLRTRDLSS-LETVYYGASPMSPVRLAEaiERFGPIFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 326 HGYGLTETAGVIVSCAWKPNwnrlPASDQAQLKSrQGvRTVGFSEIDVVDPEsGRSVERdGEtVGEIVLRGSSIMLGYLK 405
Cdd:PRK06188 311 QYYGQTEAPMVITYLRKRDH----DPDDPKRLTS-CG-RPTPGLRVALLDED-GREVAQ-GE-VGEICVRGPLVMDGYWN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 406 NPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAF 485
Cdd:PRK06188 382 RPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15222924 486 VSLKPGLTRKPTdkEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK06188 462 VVLRPGAAVDAA--ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
185-538 |
5.04e-60 |
|
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: 202.12 E-value: 5.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGI-----FVMTLDSLTDWAVPKTPVylwtlPIFHANGwtypwgiaAVGGTNVCVRK- 258
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIvnngyFIGERLGLTEQDRLCIPV-----PLFHCFG--------SVLGVLACLTHg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 ---------LHAPSIYHLIRDHGVTHMYGAP-IVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRAESLGFI--VSH 326
Cdd:cd05917 70 atmvfpspsFDPLAVLEAIEKEKCTALHGVPtMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkdVTI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 327 GYGLTETAgvivscawkpnwnrlPASDQAQLKSRQGVR--TVG----FSEIDVVDPEsGRSVERDGEtVGEIVLRGSSIM 400
Cdd:cd05917 150 AYGMTETS---------------PVSTQTRTDDSIEKRvnTVGrimpHTEAKIVDPE-GGIVPPVGV-PGELCIRGYSVM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 401 LGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWG 479
Cdd:cd05917 213 KGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYG 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15222924 480 ETPCAFVSLKPGltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:cd05917 293 EEVCAWIRLKEG--AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
185-539 |
3.24e-58 |
|
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: 200.21 E-value: 3.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMtLDSLTD-WAVPKTPVYLWTLPIFHA----NGWTYPwgiAAVGGTNVCVRKL 259
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAAN-VRALVDaWRWTEDDVLLHVLPLHHVhglvNALLCP---LFAGASVEFLPKF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 260 HAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQP--------LKSPVNFLTAGSSP-PATVLLRAESL-GFIVSHGYG 329
Cdd:cd05941 166 DPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTdpqfaraaAAERLRLMVSGSAAlPVPTLEEWEAItGHTLLERYG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 330 LTETaGVIVScawkpnwNRLPAsdqaqlKSRQGvrTVGFS----EIDVVDPESGRSVerDGETVGEIVLRGSSIMLGYLK 405
Cdd:cd05941 246 MTEI-GMALS-------NPLDG------ERRPG--TVGMPlpgvQARIVDEETGEPL--PRGEVGEIQVRGPSVFKEYWN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 406 NPIGTQNSFK-NGWFFTGDLGVIHGDGYLEIKDRSKDVII-SGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPC 483
Cdd:cd05941 308 KPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15222924 484 AFVSLKPGLTRKPTDkEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05941 388 AVVVLRAGAAALSLE-ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
19-539 |
1.23e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 200.65 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 19 FLERAATVYGDCTSIVYGNSTvYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTR 98
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 99 LDARTVSVLLRHCESKLLFV--DFFYSDLAVEAITMLLNPPIlvlianeeeeeggaeVTERSKFCYLYSDLITRGnpdfk 176
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMIChaDFPEHAAAVRAASPDLTHVV---------------AIGGARAGLDYEALVARH----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 177 wirPGSEWDPIVVN--------YTSGTTSSPKGVVHCHRGI-FVMTlDSLTDwAVPKTP---VYLWTLPIFHANGWTYPW 244
Cdd:PRK07470 151 ---LGARVANAAVDhddpcwffFTSGTTGRPKAAVLTHGQMaFVIT-NHLAD-LMPGTTeqdASLVVAPLSHGAGIHQLC 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 245 GIAAvGGTNVCV--RKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSPpatvLLRA----- 317
Cdd:PRK07470 226 QVAR-GAATVLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAP----MYRAdqkra 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 318 -ESLGFIVSHGYGLTETAGVIVScawkpnwnrLPASDQAqLKSRQGVR--TVGFS----EIDVVDPEsGRSVErDGETvG 390
Cdd:PRK07470 301 lAKLGKVLVQYFGLGEVTGNITV---------LPPALHD-AEDGPDARigTCGFErtgmEVQIQDDE-GRELP-PGET-G 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 391 EIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAV 470
Cdd:PRK07470 368 EICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAV 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222924 471 VARPDEFWGETPCAFVSLKPGLTrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK07470 448 LGVPDPVWGEVGVAVCVARDGAP--VDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
191-534 |
1.64e-57 |
|
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: 195.03 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRgifvMTLDSLTDWA----VPKTPVYLWTLPIFHANGwtYPWGIAAV---GGTNVCVRKLHAPS 263
Cdd:cd17638 7 FTSGTTGRSKGVMCAHR----QTLRAAAAWAdcadLTEDDRYLIINPFFHTFG--YKAGIVAClltGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 264 IYHLIRDHGVTHMYGAPIVLQ-ILSASQESDQPLKSPVNFLTAGSSPPATVLLRAES-LGF-IVSHGYGLTEtAGVIVSC 340
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSeLGFeTVLTAYGLTE-AGVATMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 341 AwkpnwnrlPASDQAQLKSRQGVRTVGFsEIDVVDPesgrsverdgetvGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWF 419
Cdd:cd17638 160 R--------PGDDAETVATTCGRACPGF-EVRIADD-------------GEVLVRGYNVMQGYLDDPEATAEAIdADGWL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 420 FTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRkpTDK 499
Cdd:cd17638 218 HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTL--TEE 295
|
330 340 350
....*....|....*....|....*....|....*
gi 15222924 500 EIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIK 534
Cdd:cd17638 296 DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
185-532 |
6.28e-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: 193.64 E-value: 6.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPSI 264
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 265 YHLIRDHGVTHMYG-APIVLQILSASQESDQPLKSPVNFLtaGSSPPATVLLRAESLGFIVSHGYGLTETAGVIVSCawk 343
Cdd:cd17637 81 LELIEEEKVTLMGSfPPILSNLLDAAEKSGVDLSSLRHVL--GLDAPETIQRFEETTGATFWSLYGQTETSGLVTLS--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 344 pnwnrlPASDqaqlksRQGV--RTVGFSEIDVVDpESGRSVERDgeTVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFT 421
Cdd:cd17637 156 ------PYRE------RPGSagRPGPLVRVRIVD-DNDRPVPAG--ETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 422 GDLGVIHGDGYLEIKDRS--KDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGltRKPTDK 499
Cdd:cd17637 221 GDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG--ATLTAD 298
|
330 340 350
....*....|....*....|....*....|...
gi 15222924 500 EIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17637 299 ELIEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
6-541 |
1.54e-56 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 200.18 E-value: 1.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 6 PSAANSLPLTLLGFLERAATVYGDCTSIVY-------GNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEM 78
Cdd:PRK07529 17 PLAARDLPASTYELLSRAAARHPDAPALSFlldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 79 YelqfsVPMSGA----ILNNINTRLDARTVSVLLRHCESKLL-----FVDFFYSDLAVEAITMLLN-------------P 136
Cdd:PRK07529 97 H-----FALWGGeaagIANPINPLLEPEQIAELLRAAGAKVLvtlgpFPGTDIWQKVAEVLAALPElrtvvevdlarylP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 137 PILVLIANEEEEEGGAEV----TERSKFcylYSDLITRGnpdfkwiRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVM 212
Cdd:PRK07529 172 GPKRLAVPLIRRKAHARIldfdAELARQ---PGDRLFSG-------RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 213 -----TLDSLTDwavpkTPVYLWTLPIFHANGwTYPWGIAAV--GGTNVcvrkLHAPS----------IYHLIRDHGVTH 275
Cdd:PRK07529 242 awlgaLLLGLGP-----GDTVFCGLPLFHVNA-LLVTGLAPLarGAHVV----LATPQgyrgpgvianFWKIVERYRINF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 276 MYGAPIVLQILsasqesdqpLKSPVN--------FLTAGSSP-PATVLLRAES-LGFIVSHGYGLTETAGViVSCAW--- 342
Cdd:PRK07529 312 LSGVPTVYAAL---------LQVPVDghdisslrYALCGAAPlPVEVFRRFEAaTGVRIVEGYGLTEATCV-SSVNPpdg 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 343 --KPNW--NRLPAsdqaqlksrQGVRTVgfseidVVDPESGRSVERDGETVGEIVLRGSSIMLGYLKnpiGTQNS---FK 415
Cdd:PRK07529 382 erRIGSvgLRLPY---------QRVRVV------ILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYLE---AAHNKglwLE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 416 NGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTrk 495
Cdd:PRK07529 444 DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGAS-- 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 15222924 496 PTDKEIIEYCKYKMP-RYMAPKTVSFLEELPKTSTGKIIKSLLKEIA 541
Cdd:PRK07529 522 ATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
53-538 |
2.36e-56 |
|
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: 194.86 E-value: 2.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 53 VASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAIlnnintrldartvsvllrhceskllfvdffysdlAVEAITM 132
Cdd:cd05972 13 AANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAV----------------------------------YVPLTTL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 133 LLNPPILVLIaneeeeeggaevtERSKFCYLYSDlitrgnpdfkwirpgsEWDPIVVNYTSGTTSSPKGVVHCHRgIFVM 212
Cdd:cd05972 59 LGPKDIEYRL-------------EAAGAKAIVTD----------------AEDPALIYFTSGTTGLPKGVLHTHS-YPLG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 213 TLDSLTDWAVPKTPVYLWTLPifhANGWTY--------PWgiaAVGGTNVCV--RKLHAPSIYHLIRDHGVTHMYGAPIV 282
Cdd:cd05972 109 HIPTAAYWLGLRPDDIHWNIA---DPGWAKgawssffgPW---LLGATVFVYegPRFDAERILELLERYGVTSFCGPPTA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 283 LQILSAsQESDQPLKSPVNFLTAGSSP--PATVLLRAESLGFIVSHGYGLTETAGVIVSCAWKPnwnRLPASdqaqlksr 360
Cdd:cd05972 183 YRMLIK-QDLSSYKFSHLRLVVSAGEPlnPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMP---VKPGS-------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 361 QGVRTVGFsEIDVVDpESGRSVErDGEtVGEIVLRGS--SIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDR 438
Cdd:cd05972 251 MGRPTPGY-DVAIID-DDGRELP-PGE-EGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 439 SKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKPTD-KEIIEYCKYKMPRYMAPKT 517
Cdd:cd05972 327 ADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELaEELQGHVKKVLAPYKYPRE 406
|
490 500
....*....|....*....|.
gi 15222924 518 VSFLEELPKTSTGKIIKSLLK 538
Cdd:cd05972 407 IEFVEELPKTISGKIRRVELR 427
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
36-538 |
2.31e-54 |
|
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: 189.95 E-value: 2.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 36 GNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKL 115
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 116 LFVDffysdlaveaitmllnppilvlianeeeeeggaevterskfcylysdlitrgnpdfkwirpGSEwDPIVVNYTSGT 195
Cdd:cd05971 82 LVTD-------------------------------------------------------------GSD-DPALIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 196 TSSPKGVVHCHR------GIFVMTLDSL----------TDWAvpktpvylWT-------LPIFHangwtypWGIAAVGGT 252
Cdd:cd05971 100 TGPPKGALHAHRvllghlPGVQFPFNLFprdgdlywtpADWA--------WIgglldvlLPSLY-------FGVPVLAHR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 253 nvcVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQEsdqPLKSPVNFLTA---GSSPPATVLLR--AESLGFIVSHG 327
Cdd:cd05971 165 ---MTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGE---QLKHAQVKLRAiatGGESLGEELLGwaREQFGVEVNEF 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 YGLTETAGVIVSCAwkpnwNRLPASDQAQLKSRQGVRtvgfseIDVVDpESGRSVERDgeTVGEIVLR--GSSIMLGYLK 405
Cdd:cd05971 239 YGQTECNLVIGNCS-----ALFPIKPGSMGKPIPGHR------VAIVD-DNGTPLPPG--EVGEIAVElpDPVAFLGYWN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 406 NPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAF 485
Cdd:cd05971 305 NPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAF 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15222924 486 VSLKPGLTrkPTD---KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:cd05971 385 VVLNPGET--PSDalaREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
41-541 |
4.16e-54 |
|
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: 189.25 E-value: 4.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKllfvdf 120
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 121 fysdlaveaitmllnppilVLIaneeeeeggaeVTERskfcylysdLITRGNPDfkwirpgsewDPIVVNYTSGTTSSPK 200
Cdd:cd05969 75 -------------------VLI-----------TTEE---------LYERTDPE----------DPTLLHYTSGTTGTPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 201 GVVHCHRgifVMTLDSLT-DWAVPKTP--VYLWTLPIFHANGWTYP-WGIAAVGGTNVCVR-KLHAPSIYHLIRDHGVTH 275
Cdd:cd05969 106 GVLHVHD---AMIFYYFTgKYVLDLHPddIYWCTADPGWVTGTVYGiWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 276 MYGAPIVLQILSasQESDQPLK----SPVNFLTAGSSP--PATVLLRAESLGFIVSHGYGLTETAGVIVScawkpNWNRL 349
Cdd:cd05969 183 WYTAPTAIRMLM--KEGDELARkydlSSLRFIHSVGEPlnPEAIRWGMEVFGVPIHDTWWQTETGSIMIA-----NYPCM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 350 PASDQAQLKSRQGVrtvgfsEIDVVDpESGRSVERDgeTVGEIVLRGS--SIMLGYLKNPIGTQNSFKNGWFFTGDLGVI 427
Cdd:cd05969 256 PIKPGSMGKPLPGV------KAAVVD-ENGNELPPG--TKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 428 HGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLtrKPTDK---EIIEY 504
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF--EPSDElkeEIINF 404
|
490 500 510
....*....|....*....|....*....|....*..
gi 15222924 505 CKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIA 541
Cdd:cd05969 405 VRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
24-532 |
2.95e-53 |
|
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: 188.35 E-value: 2.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 24 ATVYGDCTSIVYGNSTvYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDART 103
Cdd:cd05959 14 NEGRGDKTAFIDDAGS-LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 104 VSVLLRHCESKLLFVDFFYSDLAVEAITmLLNPPILVLIANEEEEEGGAEVterskfcyLYSDLITRGNPDFKwirPGSE 183
Cdd:cd05959 93 YAYYLEDSRARVVVVSGELAPVLAAALT-KSEHTLVVLIVSGGAGPEAGAL--------LLAELVAAEAEQLK---PAAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 184 W--DPIVVNYTSGTTSSPKGVVHCHRGIFVM-------TLdsltdwAVPKTPVYLWTLPIFHA----NGWTYPWGiaaVG 250
Cdd:cd05959 161 HadDPAFWLYSSGSTGRPKGVVHLHADIYWTaelyarnVL------GIREDDVCFSAAKLFFAyglgNSLTFPLS---VG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 251 GTNVCVRKLHAP-SIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNF-LTAGSSPPATVLLRAESL-GFIVSHG 327
Cdd:cd05959 232 ATTVLMPERPTPaAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLcVSAGEALPAEVGERWKARfGLDILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 YGLTETAGVIVSCAwkPNWNRLPASdqaqlksrqGVRTVGFsEIDVVDpESGRSVErDGEtVGEIVLRGSSIMLGYLKNP 407
Cdd:cd05959 312 IGSTEMLHIFLSNR--PGRVRYGTT---------GKPVPGY-EVELRD-EDGGDVA-DGE-PGELYVRGPSSATMYWNNR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 408 IGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVS 487
Cdd:cd05959 377 DKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVV 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15222924 488 LKPGLTRKPTD-KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd05959 457 LRPGYEDSEALeEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKI 502
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
15-544 |
4.77e-53 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 188.80 E-value: 4.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 15 TLLGFLERAATVYGDCTSIVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNN 94
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 95 INTRLDARTVSVLLRHCESKLLFVDFFYS-----DLAVEAITMLLNPPILVLIANEEEEEGGAEvterskfcylYSDLIT 169
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAKMFFAPTLFKqtrpvDLILPLQNQLPQLQQIVGVDKLAPATSSLS----------LSQIIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 170 RGNPDFKWIRPGSEwDPIVVNYTSGTTSSPKGVVHCHRGI------FVMTLDsLTdwavpKTPVYLWTLPIFHANGWTYp 243
Cdd:PRK06087 174 DYEPLTTAITTHGD-ELAAVLFTSGTEGLPKGVMLTHNNIlaseraYCARLN-LT-----WQDVFMMPAPLGHATGFLH- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 244 wGIAA---VGGTNVCVRKLHAPSIYHLIRDHGVTHMYGA-PIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRAES 319
Cdd:PRK06087 246 -GVTApflIGARSVLLDIFTPDACLALLEQQRCTCMLGAtPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 320 LGFIVSHGYGLTETAGVIV-----SCAWKPNWNRLPAsdqaqlksrQGVrtvgfsEIDVVDpESGRSVERDGEtvGEIVL 394
Cdd:PRK06087 325 RGIKLLSVYGSTESSPHAVvnlddPLSRFMHTDGYAA---------AGV------EIKVVD-EARKTLPPGCE--GEEAS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 395 RGSSIMLGYLKNPIGTQNSFKN-GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVAR 473
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARALDEeGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222924 474 PDEFWGETPCAFVSLKPGlTRKPTDKEIIEY-CKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL-KEIAKNM 544
Cdd:PRK06087 467 PDERLGERSCAYVVLKAP-HHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLrKDIMRRL 538
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-539 |
7.13e-53 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 188.27 E-value: 7.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 9 ANSLPLTLLGFlERAATVYGDCTSIVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMS 88
Cdd:PLN02246 20 PNHLPLHDYCF-ERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 89 GAILNNINTRLDARTVSVLLRHCESKLLFVDFFYsdlaVEAITMLLNPPILVLIAneeeeeggaeVTERSKFCYLYSDLI 168
Cdd:PLN02246 99 GAVTTTANPFYTPAEIAKQAKASGAKLIITQSCY----VDKLKGLAEDDGVTVVT----------IDDPPEGCLHFSELT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 169 TRGN---PDFKwIRPGsewDPIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTDWAVP-----KTPVYLWTLPIFHangw 240
Cdd:PLN02246 165 QADEnelPEVE-ISPD---DVVALPYSSGTTGLPKGVMLTHKGL-VTSVAQQVDGENPnlyfhSDDVILCVLPMFH---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 241 typwgIAA----------VGGTNVCVRKLHAPSIYHLIRDHGVTHmygAPIVLQILSASQESDQPLK---SPVNFLTAGS 307
Cdd:PLN02246 236 -----IYSlnsvllcglrVGAAILIMPKFEIGALLELIQRHKVTI---APFVPPIVLAIAKSPVVEKydlSSIRMVLSGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 308 SPPATVL---LRAESLGFIVSHGYGLTETAGVIVSC-AWkpnwnrlpASDQAQLKSRQGVRTVGFSEIDVVDPESGRSVE 383
Cdd:PLN02246 308 APLGKELedaFRAKLPNAVLGQGYGMTEAGPVLAMClAF--------AKEPFPVKSGSCGTVVRNAELKIVDPETGASLP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 384 RDgeTVGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTN 462
Cdd:PLN02246 380 RN--QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISH 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 463 PAVNEAAVVARPDEFWGETPCAFVSLKPGLtrKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PLN02246 458 PSIADAAVVPMKDEVAGEVPVAFVVRSNGS--EITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
15-537 |
1.03e-52 |
|
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: 186.56 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 15 TLLGFLERAATVYGDCTSIVY-GNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILN 93
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 94 NINTRLDARTVSVLLRHCESKLLFVdffysdlAVEAitmllnpPILVLIANEEEEEGGAEVTERSKFCYLYSDLItrgnp 173
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTAAVI-------AVDA-------QVMDAIFQSGVRVLALSDLVGLGEPESAGPLI----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 174 DFKWIRPGsewDPIVVNYTSGTTSSPKGVVHCHRGI-----FVMTLDSLTDWAVPKTpvyLWTLPIFHANGWTYPWGIA- 247
Cdd:cd05923 143 EDPPREPE---QPAFVFYTSGTTGLPKGAVIPQRAAesrvlFMSTQAGLRHGRHNVV---LGLMPLYHVIGFFAVLVAAl 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 248 AVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQE-SDQPLKSPVNFLTAGSSPPATVLLRAESL--GFIV 324
Cdd:cd05923 217 ALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEfAGLKLSSLRHVTFAGATMPDAVLERVNQHlpGEKV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 325 SHgYGLTETagvivscawkpnWNRLPASDQAQlksRQGVRTVGFSEIDVVdPESGRSVE--RDGETvGEIV--LRGSSIM 400
Cdd:cd05923 297 NI-YGTTEA------------MNSLYMRDART---GTEMRPGFFSEVRIV-RIGGSPDEalANGEE-GELIvaAAADAAF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 401 LGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGE 480
Cdd:cd05923 359 TGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQ 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15222924 481 TPCAFVSLKPGltrKPTDKEIIEYCK-YKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:cd05923 439 SVTACVVPREG---TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
24-538 |
2.46e-52 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 186.04 E-value: 2.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 24 ATVYGDCTSIVY----GNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRL 99
Cdd:PRK08008 17 ADVYGHKTALIFessgGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 100 DARTVSVLLRHCESKLLFVD--FF--YSDLAVEAITMLLNppILVLIANEEEeeggaeVTERSKFcylySDLITRGNPDF 175
Cdd:PRK08008 97 LREESAWILQNSQASLLVTSaqFYpmYRQIQQEDATPLRH--ICLTRVALPA------DDGVSSF----TQLKAQQPATL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 176 KWIRPGSEWDPIVVNYTSGTTSSPKGVV--HCH---RGIFvmtldslTDW--AVPKTPVYLWTLPIFHAN-GWTYPWGIA 247
Cdd:PRK08008 165 CYAPPLSTDDTAEILFTSGTTSRPKGVVitHYNlrfAGYY-------SAWqcALRDDDVYLTVMPAFHIDcQCTAAMAAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 248 AVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQIL----SASQESDQPLKSPVNFLTagssppatvLLRAESLGFI 323
Cdd:PRK08008 238 SAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLmvqpPSANDRQHCLREVMFYLN---------LSDQEKDAFE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 324 VSHG------YGLTET-AGVIVScawkpnwnrlPASDQAQLKSrqgVRTVGFS-EIDVVDpESGRSVerDGETVGEIVLR 395
Cdd:PRK08008 309 ERFGvrlltsYGMTETiVGIIGD----------RPGDKRRWPS---IGRPGFCyEAEIRD-DHNRPL--PAGEIGEICIK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 396 G---SSIMLGYLKNPIGTQNSFK-NGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVV 471
Cdd:PRK08008 373 GvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 472 ARPDEFWGETPCAFVSLKPGLTRkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:PRK08008 453 GIKDSIRDEAIKAFVVLNEGETL--SEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
34-538 |
1.99e-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: 181.89 E-value: 1.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 34 VYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCES 113
Cdd:cd05919 4 FYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 114 KLLfvdffysdlaveaitmllnppilvlianeeeeeggaeVTERSKFCYLysdlitrgnpdfkwirpgsewdpivvNYTS 193
Cdd:cd05919 84 RLV-------------------------------------VTSADDIAYL--------------------------LYSS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 194 GTTSSPKGVVHCHRGiFVMTLDSLTDWAVPKTP--VYLWTLPIFHA----NGWTYPWgiaAVGGTNVCVRKLHAPS-IYH 266
Cdd:cd05919 101 GTTGPPKGVMHAHRD-PLLFADAMAREALGLTPgdRVFSSAKMFFGyglgNSLWFPL---AVGASAVLNPGWPTAErVLA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 267 LIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVN-FLTAGSSPPATVLLR-AESLGFIVSHGYGLTETAGVIVScawkp 344
Cdd:cd05919 177 TLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRlCVSAGEALPRGLGERwMEHFGGPILDGIGATEVGHIFLS----- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 345 nwNRlpaSDQAQLKSrQGVRTVGFsEIDVVDPEsGRSVERDgeTVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDL 424
Cdd:cd05919 252 --NR---PGAWRLGS-TGRPVPGY-EIRLVDEE-GHTIPPG--EEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 425 GVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLT-RKPTDKEIIE 503
Cdd:cd05919 322 FCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAApQESLARDIHR 401
|
490 500 510
....*....|....*....|....*....|....*
gi 15222924 504 YCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:cd05919 402 HLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
20-538 |
2.60e-51 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 184.23 E-value: 2.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 20 LERAATVYGDCTSIVYGNStVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRL 99
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNR-RRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 100 DARTVSVLLRHCESKLLFVD----FFYSDLAVEAItmllnPPIL--VLIANeeeeeggaevTERSKFCYLYSDLitrgNP 173
Cdd:PLN02860 92 SFEEAKSAMLLVRPVMLVTDetcsSWYEELQNDRL-----PSLMwqVFLES----------PSSSVFIFLNSFL----TT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 174 DFKWIRPGSE------WDP---IVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPW 244
Cdd:PLN02860 153 EMLKQRALGTteldyaWAPddaVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 245 GIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQIL---SASQESDQPLKSPVNFLTAGSSPPATvLLRAESLG 321
Cdd:PLN02860 233 AMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLislTRKSMTWKVFPSVRKILNGGGSLSSR-LLPDAKKL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 322 F----IVShGYGLTETagvivsCAwkpNWNRLPASDQAQLKSRQGVRTVGFSEIDVVDPESGRSVER------------D 385
Cdd:PLN02860 312 FpnakLFS-AYGMTEA------CS---SLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKpaphvelkigldE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 386 GETVGEIVLRGSSIMLGYLKNPIGTQNSFKN-GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPA 464
Cdd:PLN02860 382 SSRVGRILTRGPHVMLGYWGQNSETASVLSNdGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 465 VNEAAVVARPDEFWGETPCAFVSLKPGLT----RKPTDKEIIE--------YCKYK-MPRYMAPKT-VSFLEELPKTSTG 530
Cdd:PLN02860 462 VASVVVVGVPDSRLTEMVVACVRLRDGWIwsdnEKENAKKNLTlssetlrhHCREKnLSRFKIPKLfVQWRKPFPLTTTG 541
|
....*...
gi 15222924 531 KIIKSLLK 538
Cdd:PLN02860 542 KIRRDEVR 549
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
19-539 |
1.48e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 182.54 E-value: 1.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 19 FLERAATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTR 98
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDI-TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 99 LDARTVSVLLRHCESK-LLFVDFFYSDLAVEAITMLLNPPILVLIAN-------------EEEEEGGAEVTERSKFCYLY 164
Cdd:PRK06710 108 YTERELEYQLHDSGAKvILCLDLVFPRVTNVQSATKIEHVIVTRIADflpfpknllypfvQKKQSNLVVKVSESETIHLW 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 165 SDLITRGNPDFKwIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLtDW---AVPKTPVYLWTLPIFHANGWT 241
Cdd:PRK06710 188 NSVEKEVNTGVE-VPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGV-QWlynCKEGEEVVLGVLPFFHVYGMT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 242 YPWGIAAVGGTN-VCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSP-PATVLLRAES 319
Cdd:PRK06710 266 AVMNLSIMQGYKmVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPlPVEVQEKFET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 320 L-GFIVSHGYGLTETAGVIVS-CAWKpnwNRLPASDQAQLKSrqgvrtvgfSEIDVVDPESGRSVeRDGEtVGEIVLRGS 397
Cdd:PRK06710 346 VtGGKLVEGYGLTESSPVTHSnFLWE---KRVPGSIGVPWPD---------TEAMIMSLETGEAL-PPGE-IGEIVVKGP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 398 SIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEF 477
Cdd:PRK06710 412 QIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPY 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222924 478 WGETPCAFVSLKPGltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK06710 492 RGETVKAFVVLKEG--TECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
185-541 |
4.68e-50 |
|
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: 174.83 E-value: 4.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGI---FVMTLDSLtdwAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRKLHA 261
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLlasAAGLHSRL---GFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 262 PSIYHLirDHGVTHMYGAPIVLQ-ILSASQESDQPLKSPVNFLTAGSSPPAtVLLRAESLGFIVSHGYGLTETAGVIvsC 340
Cdd:cd17630 78 LAEDLA--PPGVTHVSLVPTQLQrLLDSGQGPAALKSLRAVLLGGAPIPPE-LLERAADRGIPLYTTYGMTETASQV--A 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 341 AWKPNwnrlpasdqaqLKSRQGV-RTVGFSEIDVVDPesgrsverdgetvGEIVLRGSSIMLGYLKNPIgTQNSFKNGWF 419
Cdd:cd17630 153 TKRPD-----------GFGRGGVgVLLPGRELRIVED-------------GEIWVGGASLAMGYLRGQL-VPEFNEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 420 FTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGltrkPTDK 499
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP----ADPA 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15222924 500 EIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIA 541
Cdd:cd17630 284 ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
54-539 |
5.25e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 179.23 E-value: 5.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 54 ASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITML 133
Cdd:PRK09088 36 AAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 134 lnppilVLIANeeeeeggaevterskfcylysdlITRGNPDFkwiRPGSEWD-PIVVNYTSGTTSSPKGVVHCHRGIFVM 212
Cdd:PRK09088 116 ------AFIAS-----------------------ADALEPAD---TPSIPPErVSLILFTSGTSGQPKGVMLSERNLQQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 213 TLDSLTDWAVPKTPVYLWTLPIFHANGW-TYPWGIAAVGGT---------NVCVRKLHAPSIyhlirdhGVTHMYGAPIV 282
Cdd:PRK09088 164 AHNFGVLGRVDAHSSFLCDAPMFHIIGLiTSVRPVLAVGGSilvsngfepKRTLGRLGDPAL-------GITHYFCVPQM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 283 LQILSASQESD-QPLKSPVNFLTAGSSPPATVLLRAESLGFIVSHGYGLTEtAGVIVScawkpnwnrLPAsDQAQLKSRQ 361
Cdd:PRK09088 237 AQAFRAQPGFDaAALRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSE-AGTVFG---------MSV-DCDVIRAKA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 362 GvrTVGFS----EIDVVDpESGRSVeRDGETvGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIK 436
Cdd:PRK09088 306 G--AAGIPtptvQTRVVD-DQGNDC-PAGVP-GELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDADGFFWVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 437 DRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKPtdKEIIEYCKYKMPRYMAPK 516
Cdd:PRK09088 381 DRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDL--ERIRSHLSTRLAKYKVPK 458
|
490 500
....*....|....*....|...
gi 15222924 517 TVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK09088 459 HLRLVDALPRTASGKLQKARLRD 481
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
31-539 |
7.11e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 178.94 E-value: 7.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 31 TSIVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRH 110
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 111 CESKLLFVDFFYSDLAVEAITMLLNP-PILVLIANEEEeeggaevTERSkfcylYSDLITrGNPDFkwiRPGSEWDPIVV 189
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGvPLLLVVAGPVP-------GFRS-----YEEALA-AQPDT---PIADETAGADM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 190 NYTSGTTSSPKGVVHCHRGIFV-------MTLDSLTDWAVPKTpVYLWTLPIFHangwTYP--WGIAA--VGGTNVCVRK 258
Cdd:PRK08276 146 LYSSGTTGRPKGIKRPLPGLDPdeapgmmLALLGFGMYGGPDS-VYLSPAPLYH----TAPlrFGMSAlaLGGTVVVMEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 LHAPSIYHLIRDHGVTHMYGAPIVLQILsasqesdqpLK-----------SPVNFLTAGSSPPATVLLRA--ESLGFIVS 325
Cdd:PRK08276 221 FDAEEALALIERYRVTHSQLVPTMFVRM---------LKlpeevrarydvSSLRVAIHAAAPCPVEVKRAmiDWWGPIIH 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 326 HGYGLTETAGVIVSCAwkPNWNRLPASdqaqlksrqgvrtVG---FSEIDVVDPesgrsverDGE-----TVGEIVLRGS 397
Cdd:PRK08276 292 EYYASSEGGGVTVITS--EDWLAHPGS-------------VGkavLGEVRILDE--------DGNelppgEIGTVYFEMD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 398 SIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDE 476
Cdd:PRK08276 349 GYPFEYHNDPEKTAAARnPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDE 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 477 FWGETPCAFVSLKPGLTRKP-TDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK08276 429 EMGERVKAVVQPADGADAGDaLAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
41-474 |
1.11e-49 |
|
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: 177.40 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDf 120
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 121 fysdlaveaitmllnppilvlianeeeeeggaevterskfcylysdlitrgNPDfkwirpgsewDPIVVNYTSGTTSSPK 200
Cdd:cd05907 85 ---------------------------------------------------DPD----------DLATIIYTSGTTGRPK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 201 GVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYpwGIAAVGGTNVCVRklHAPSIYHLIRDHGV---THMY 277
Cdd:cd05907 104 GVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRA--GLYVPLLAGARIY--FASSAETLLDDLSEvrpTVFL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 278 GAPIVLQ--ILSASQESDQPLK---------SPVNFLTAGSSP-PATVLLRAESLGFIVSHGYGLTETAGVIvsCAWKPN 345
Cdd:cd05907 180 AVPRVWEkvYAAIKVKAVPGLKrklfdlavgGRLRFAASGGAPlPAELLHFFRALGIPVYEGYGLTETSAVV--TLNPPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 346 WNRLpasdqaqlksrqgvRTVGfseiDVVDPESGRSVERdgetvGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDL 424
Cdd:cd05907 258 DNRI--------------GTVG----KPLPGVEVRIADD-----GEILVRGPNVMLGYYKNPEATAEALdADGWLHTGDL 314
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15222924 425 GVIHGDGYLEIKDRSKDVII-SGGENVSSVEVEAVLYTNPAVNEAAVVA--RP 474
Cdd:cd05907 315 GEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIGdgRP 367
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
185-530 |
4.17e-48 |
|
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: 169.79 E-value: 4.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPSI 264
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 265 YHLIRDHGVTHMY-GAPIVLQILSASQESDQPLKSpvnfLTAGSSPPATVLLRA--ESLGFIVSHGYGLTETAGVIVsca 341
Cdd:cd17636 81 LELIEAERCTHAFlLPPTIDQIVELNADGLYDLSS----LRSSPAAPEWNDMATvdTSPWGRKPGGYGQTEVMGLAT--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 342 wkpnWNRLPASDqaqlKSRQGvRTVGFSEIDVVDPEsGRSVErDGETvGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFT 421
Cdd:cd17636 154 ----FAALGGGA----IGGAG-RPSPLVQVRILDED-GREVP-DGEV-GEIVARGPTVMAGYWNRPEVNARRTRGGWHHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 422 GDLGVIHGDGYLEI---KDRskdVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTrkPTD 498
Cdd:cd17636 222 NDLGRREPDGSLSFvgpKTR---MIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS--VTE 296
|
330 340 350
....*....|....*....|....*....|..
gi 15222924 499 KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTG 530
Cdd:cd17636 297 AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
186-538 |
5.69e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 170.56 E-value: 5.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 186 PIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTD-WAvpktpvylWT--------LPIFHANGWTYpwGIAA---VGGTN 253
Cdd:PRK07787 130 PALIVYTSGTTGPPKGVVLSRRAI-AADLDALAEaWQ--------WTaddvlvhgLPLFHVHGLVL--GVLGplrIGNRF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 254 VCVRKLhAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLkSPVNFLTAGSSP-PATVLLRAESL-GFIVSHGYGLT 331
Cdd:PRK07787 199 VHTGRP-TPEAYAQALSEGGTLYFGVPTVWSRIAADPEAARAL-RGARLLVSGSAAlPVPVFDRLAALtGHRPVERYGMT 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 332 ET---AGVIVSCAWKPNWNRLPAsdqaqlksrQGVRTvgfseiDVVDpESGRSVERDGETVGEIVLRGSSIMLGYLKNPI 408
Cdd:PRK07787 277 ETlitLSTRADGERRPGWVGLPL---------AGVET------RLVD-EDGGPVPHDGETVGELQVRGPTLFDGYLNRPD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 409 GTQNSF-KNGWFFTGDLGVIHGDGYLEIKDR-SKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFV 486
Cdd:PRK07787 341 ATAAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYV 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15222924 487 SLKPGltrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:PRK07787 421 VGADD----VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
13-537 |
2.15e-46 |
|
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: 169.05 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 13 PLTLLGFLERAATVYGDCTSIVYGNsTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAIL 92
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDGD-RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 93 NNINTRLDARTVSVLLRHCESKLLFVD-----FFYSDLAVEAITMLLNPPILVLianeeeeeggaevterskfcylysdl 167
Cdd:cd05920 93 VLALPSHRRSELSAFCAHAEAVAYIVPdrhagFDHRALARELAESIPEVALFLL-------------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 168 itrgnpdfkwirpgsewdpivvnyTSGTTSSPKGVVHCHRGIF--------VMTLDSLTdwavpktpVYLWTLPIFHANG 239
Cdd:cd05920 147 ------------------------SGGTTGTPKLIPRTHNDYAynvrasaeVCGLDQDT--------VYLAVLPAAHNFP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 240 WTYP--WGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAP-IVLQILSASQESDQPLKSpVNFLTAGSSP-PATVLL 315
Cdd:cd05920 195 LACPgvLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPaLVSLWLDAAASRRADLSS-LRLLQVGGARlSPALAR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 316 RA-ESLGFIVSHGYGLTEtaGVIvscawkpNWNRLPASDqAQLKSRQGVRTVGFSEIDVVDpESGRSVErDGETvGEIVL 394
Cdd:cd05920 274 RVpPVLGCTLQQVFGMAE--GLL-------NYTRLDDPD-EVIIHTQGRPMSPDDEIRVVD-EEGNPVP-PGEE-GELLT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 395 RGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVAR 473
Cdd:cd05920 341 RGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAM 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 474 PDEFWGETPCAFVSLKPGLTRKPTDKEIIEYCkyKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:cd05920 421 PDELLGERSCAFVVLRDPPPSAAQLRRFLRER--GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
191-541 |
4.27e-46 |
|
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: 165.35 E-value: 4.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGI----FVMTLDSLTDwavpKTPVYLWTLPIFHANGwTYPWGIAAV--GGTNVcvrkLHAPS- 263
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEvynaWMLALNSLFD----PDDVLLCGLPLFHVNG-SVVTLLTPLasGAHVV----LAGPAg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 264 ---------IYHLIRDHGVTHMYGAPIVLQILSasQESDQPLKSPVNFLTAGSSP-PATVLLRAE-SLGFIVSHGYGLTE 332
Cdd:cd05944 80 yrnpglfdnFWKLVERYRITSLSTVPTVYAALL--QVPVNADISSLRFAMSGAAPlPVELRARFEdATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 333 TAGViVSCAWkPNWNRLPASDQAQLKSRQgVRtvgfseIDVVDPESGRSVERDGETVGEIVLRGSSIMLGYLkNPIGTQN 412
Cdd:cd05944 158 ATCL-VAVNP-PDGPKRPGSVGLRLPYAR-VR------IKVLDGVGRLLRDCAPDEVGEICVAGPGVFGGYL-YTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 413 SF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPG 491
Cdd:cd05944 228 AFvADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15222924 492 LTRKPTdkEIIEYCKYKMP-RYMAPKTVSFLEELPKTSTGKIIKSLLKEIA 541
Cdd:cd05944 308 AVVEEE--ELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
185-538 |
1.04e-45 |
|
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: 166.50 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIfvmtLDSLTDWAV-----PKTPVYLWTLPIFHANGW----TYPWGiaaVGGTNVC 255
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDP----LASADRYAVnvlrlREDDRFVGSPPLAFTFGLggvlLFPFG---VGASGVL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 256 VRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSS--PPATVLLRAESLGFIVSHGYGLTET 333
Cdd:cd05958 171 LEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEalPAALHRAWKEATGIPIIDGIGSTEM 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 334 AGVIVScawkpnwnrlpASDQAQLKSRQGVRTVGFsEIDVVDpESGRSVErDGeTVGEIVLRGSSIMLgYLKNPiGTQNS 413
Cdd:cd05958 251 FHIFIS-----------ARPGDARPGATGKPVPGY-EAKVVD-DEGNPVP-DG-TIGRLAVRGPTGCR-YLADK-RQRTY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 414 FKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLT 493
Cdd:cd05958 314 VQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15222924 494 RKPT-DKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:cd05958 394 PGPVlARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
23-540 |
1.76e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 168.18 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 23 AATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDA- 101
Cdd:PRK07788 58 AARRAPDRAALIDERGTL-TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGp 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 102 RTVSVLLRHcESKLLFVDFFYSDLAVEAITMLlnPPILVLIANEEEEEGGAEVTERskfcylYSDLITRG--NPDFKWIR 179
Cdd:PRK07788 137 QLAEVAARE-GVKALVYDDEFTDLLSALPPDL--GRLRAWGGNPDDDEPSGSTDET------LDDLIAGSstAPLPKPPK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 180 PGSewdpIVVnYTSGTTSSPKGVVHCHRGIFVmTLDSLTDWaVP--KTPVYLWTLPIFHANGWTYpWGIA-AVGGTNVCV 256
Cdd:PRK07788 208 PGG----IVI-LTSGTTGTPKGAPRPEPSPLA-PLAGLLSR-VPfrAGETTLLPAPMFHATGWAH-LTLAmALGSTVVLR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 257 RKLHAPSIYHLIRDHGVTHMYGAPIVLQ-ILSASQESDQ-PLKSPVNFL-TAGSSPPATVLLRA-ESLGFIVSHGYGLTE 332
Cdd:PRK07788 280 RRFDPEATLEDIAKHKATALVVVPVMLSrILDLGPEVLAkYDTSSLKIIfVSGSALSPELATRAlEAFGPVLYNLYGSTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 333 TAgvIVSCAWKPNWNRLPAsdqaqlksrqgvrTVG----FSEIDVVDpESGRSVERdgETVGEIVLRGSSIMLGYlKNPi 408
Cdd:PRK07788 360 VA--FATIATPEDLAEAPG-------------TVGrppkGVTVKILD-ENGNEVPR--GVVGRIFVGNGFPFEGY-TDG- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 409 GTQNSfKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSL 488
Cdd:PRK07788 420 RDKQI-IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVK 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15222924 489 KPGLTRkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEI 540
Cdd:PRK07788 499 APGAAL--DEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
33-539 |
2.97e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 164.09 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 33 IVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCE 112
Cdd:PRK13391 17 IMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 113 SKLLFVDFFYSDLAVEAITMLLN-PPILVLIANEeeeeggaevtERSKFcYLYSDlITRGNPDFKwIRPGSEWDPIVvnY 191
Cdd:PRK13391 97 ARALITSAAKLDVARALLKQCPGvRHRLVLDGDG----------ELEGF-VGYAE-AVAGLPATP-IADESLGTDML--Y 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 192 TSGTTSSPKGVVHCHRGIFVMTLDSLTD-----WAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPSIYH 266
Cdd:PRK13391 162 SSGTTGRPKGIKRPLPEQPPDTPLPLTAflqrlWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 267 LIRDHGVTHMYGAPIVL-QILSASQEsdQPLKSPVNFL-----TAGSSPPATVLLRAESLGFIVSHGYGLTETAGVIvsc 340
Cdd:PRK13391 242 LIEEYGVTHTQLVPTMFsRMLKLPEE--VRDKYDLSSLevaihAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFT--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 341 awkpnwnrlpASDQAQLKSRQGvrTVG---FSEIDVVDpESGRSVERDgeTVGEIVLRGSSiMLGYLKNPIGTQNSF--K 415
Cdd:PRK13391 317 ----------ACDSEEWLAHPG--TVGramFGDLHILD-DDGAELPPG--EPGTIWFEGGR-PFEYLNDPAKTAEARhpD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 416 NGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLtrK 495
Cdd:PRK13391 381 GTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGV--D 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15222924 496 PTD---KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK13391 459 PGPalaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
13-531 |
8.47e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 163.13 E-value: 8.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 13 PLTLLGFLERAATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAIL 92
Cdd:PRK07798 2 AWNIADLFEAVADAVPDRVALVCGDRRL-TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 93 NNINTRLDARTVSVLLRHCESKLLFVDFFYSDLAVEAITMLLNPPILVLIANEEEEEGGAEVTErskfcylYSDLITRGN 172
Cdd:PRK07798 81 VNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVD-------YEDALAAGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 173 PDfkwiRPGSEW--DPIVVNYTSGTTSSPKGVVHCH--------------RGIFVMTLDSLTDWAVPKTP-VYLWTLPIF 235
Cdd:PRK07798 154 PE----RDFGERspDDLYLLYTGGTTGMPKGVMWRQedifrvllggrdfaTGEPIEDEEELAKRAAAGPGmRRFPAPPLM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 236 HANG-WTypwGIAAV--GGTNVC--VRKLHAPSIYHLIRDHGVTHM------YGAPIvLQILSASQESDqpLKSPVNFLT 304
Cdd:PRK07798 230 HGAGqWA---AFAALfsGQTVVLlpDVRFDADEVWRTIEREKVNVItivgdaMARPL-LDALEARGPYD--LSSLFAIAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 305 AGS--SPPATVLLRAESLGFIVSHGYGLTETaGVIVScawkpnwnrlpaSDQAQLKSRQGVRTVGFSEIDVVDPESGRSV 382
Cdd:PRK07798 304 GGAlfSPSVKEALLELLPNVVLTDSIGSSET-GFGGS------------GTVAKGAVHTGGPRFTIGPRTVVLDEDGNPV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 383 ERDGETVGEIVLRGSsIMLGYLKNPIGTQNSFK--NG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAV 458
Cdd:PRK07798 371 EPGSGEIGWIARRGH-IPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEA 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222924 459 LYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGK 531
Cdd:PRK07798 450 LKAHPDVADALVVGVPDERWGQEVVAVVQLREG--ARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
14-542 |
1.70e-43 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 162.24 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 14 LTLLGFLERAATVYGDCTSIVYGNSTvYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAI-- 91
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDGERR-LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 92 ----------LNNINTRLDARTVSVLLRHceskllfVDFFYSDLAVEaitmllnppilvLIANEEEEEGGAEVTERSKFC 161
Cdd:COG1021 104 falpahrraeISHFAEQSEAVAYIIPDRH-------RGFDYRALARE------------LQAEVPSLRHVLVVGDAGEFT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 162 YLySDLITRGNPDFKwIRPGSeWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWT 241
Cdd:COG1021 165 SL-DALLAAPADLSE-PRPDP-DDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 242 YPwGIAAV---GGTNVCVRKLHAPSIYHLIRDHGVTHMygA---PIVLQILSASQESDQPLKSpvnfLT----AGSSPPA 311
Cdd:COG1021 242 SP-GVLGVlyaGGTVVLAPDPSPDTAFPLIERERVTVT--AlvpPLALLWLDAAERSRYDLSS----LRvlqvGGAKLSP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 312 TVLLRAES-LGFIVSHGYGLTEtaGVIvscawkpNWNRLPASDQAQlksrqgVRTVG-----FSEIDVVDPEsGRSVErD 385
Cdd:COG1021 315 ELARRVRPaLGCTLQQVFGMAE--GLV-------NYTRLDDPEEVI------LTTQGrpispDDEVRIVDED-GNPVP-P 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 386 GEtVGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPA 464
Cdd:COG1021 378 GE-VGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 465 VNEAAVVARPDEFWGETPCAFVSLKpglTRKPTDKEIIEY------CKYKMP-RymapktVSFLEELPKTSTGKIIKSLL 537
Cdd:COG1021 457 VHDAAVVAMPDEYLGERSCAFVVPR---GEPLTLAELRRFlrerglAAFKLPdR------LEFVDALPLTAVGKIDKKAL 527
|
....*
gi 15222924 538 KEIAK 542
Cdd:COG1021 528 RAALA 532
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
6-544 |
4.87e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 158.37 E-value: 4.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 6 PSAANSLPLTLLGFLERAATVYGDCTSIVyGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSV 85
Cdd:PRK06164 2 PHDAAPRADTLASLLDAHARARPDAVALI-DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 86 PMSGAILNNINTRLDARTVSVLLRHCESKLLFV-------DFFySDLAVEAITMLLNPPILVLIANEEEEEGGAEVTERS 158
Cdd:PRK06164 81 ARLGATVIAVNTRYRSHEVAHILGRGRARWLVVwpgfkgiDFA-AILAAVPPDALPPLRAIAVVDDAADATPAPAPGARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 159 KFCylysDLITRGNPDFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHAN 238
Cdd:PRK06164 160 QLF----ALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 239 GWTYPWGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLL-RA 317
Cdd:PRK06164 236 GFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPALGELAaLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 318 ESLGFIVSHGYGLTET----AGVIVSCAWKPNWNR--LPASDQAQlksrqgVRtvgfseidVVDPESGRSVErDGETvGE 391
Cdd:PRK06164 316 RARGVPLTGLYGSSEVqalvALQPATDPVSVRIEGggRPASPEAR------VR--------ARDPQDGALLP-DGES-GE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 392 IVLRGSSIMLGYLKNPIGTQNSFK-NGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAV 470
Cdd:PRK06164 380 IEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQV 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222924 471 VARPDEfwGET-PCAFVSLKPGLtrKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTG---KIIKSLLKEIAKNM 544
Cdd:PRK06164 460 VGATRD--GKTvPVAFVIPTDGA--SPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQAR 533
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
8-533 |
6.79e-42 |
|
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: 158.51 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 8 AANSLPLTLLGFLERAATVY-GDCTSIVYGNSTVYTWRETNHrclcVASALSSIGIGRSDVVSVLSANTPEMYELQFSVP 86
Cdd:cd17634 55 AANALDRHLRENGDRTAIIYeGDDTSQSRTISYRELHREVCR----FAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 87 MSGAILNNINTRLDARTVSVLLRHCESKLLFV-DFFYS--------DLAVEAITMLLNPPILVLIANEEEEEGGAevTER 157
Cdd:cd17634 131 RIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITaDGGVRagrsvplkKNVDDALNPNVTSVEHVIVLKRTGSDIDW--QEG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 158 SKFcyLYSDLITRGNPDFKWIRPGSEwDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTD-WAVPKTPVYLWTLPIfh 236
Cdd:cd17634 209 RDL--WWRDLIAKASPEHQPEAMNAE-DPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYvFDYGPGDIYWCTADV-- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 237 anGWT--YPW---GIAAVGGTNVCVRKL----HAPSIYHLIRDHGVTHMYGAPIVLQILSASQES--DQPLKSPVNFLTA 305
Cdd:cd17634 284 --GWVtgHSYllyGPLACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDaiEGTDRSSLRILGS 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 306 GSSP--PATVLLRAESLGF----IVSHGYGlTETAGVIVScawkpnwnrlPASDQAQLKSRQGVRTVGFSEIDVVDPEsG 379
Cdd:cd17634 362 VGEPinPEAYEWYWKKIGKekcpVVDTWWQ-TETGGFMIT----------PLPGAIELKAGSATRPVFGVQPAVVDNE-G 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 380 RSVErdGETVGEIVLRGS--SIMLGYLKNPIGTQNS----FKNGWFfTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSV 453
Cdd:cd17634 430 HPQP--GGTEGNLVITDPwpGQTRTLFGDHERFEQTyfstFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTA 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 454 EVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKPT-DKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17634 507 EIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPElYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
.
gi 15222924 533 I 533
Cdd:cd17634 587 M 587
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
21-541 |
7.02e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 155.58 E-value: 7.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 21 ERAATVYgdctsivYGNSTVYT-WRETNHRClcvASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINT-- 97
Cdd:PRK06178 48 QRPAIIF-------YGHVITYAeLDELSDRF---AALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPlf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 98 -------RLDARTVSVLLrhCESKLL-FVDFFYSDLAVEAI------TMLLNPPILVLIAneeeeeggaEVTERSKFCYL 163
Cdd:PRK06178 118 rehelsyELNDAGAEVLL--ALDQLApVVEQVRAETSLRHVivtslaDVLPAEPTLPLPD---------SLRAPRLAAAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 164 YSDLIT--RGNPDFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTDWAVPKT--PVYLWTLPIF---- 235
Cdd:PRK06178 187 AIDLLPalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDM-VYTAAAAYAVAVVGGedSVFLSFLPEFwiag 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 236 HANGWTYPwgiAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGaPI--VLQILSASQESDQPLKS-----PVNF---LTa 305
Cdd:PRK06178 266 ENFGLLFP---LFSGATLVLLARWDAVAFMAAVERYRVTRTVM-LVdnAVELMDHPRFAEYDLSSlrqvrVVSFvkkLN- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 306 gsspPATVLLRAESLGFIVSHG-YGLTET-------AGVivscawkpnwnrlpASDQAQLKSRQ---GVRTVGfSEIDVV 374
Cdd:PRK06178 341 ----PDYRQRWRALTGSVLAEAaWGMTEThtcdtftAGF--------------QDDDFDLLSQPvfvGLPVPG-TEFKIC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 375 DPESGRSVERDGEtvGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVE 454
Cdd:PRK06178 402 DFETGELLPLGAE--GEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 455 VEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRkpTDKEIIEYCKYKMPRYMAPkTVSFLEELPKTSTGKIIK 534
Cdd:PRK06178 480 VEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADL--TAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRK 556
|
....*..
gi 15222924 535 SLLKEIA 541
Cdd:PRK06178 557 QDLQALA 563
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
15-474 |
8.59e-41 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 155.64 E-value: 8.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 15 TLLGFLERAATVYGDCTSIVY---GNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAI 91
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREkedGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 92 LNNINTRLDARTVSVLLRHCESKLLFV-DFFYSDLAVEAITMLLNPPILVLIANEEEEEGGAEVTerskfcylYSDLITR 170
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLLS--------LDELLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 171 G----NPDF--KWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFH--ANGWTY 242
Cdd:COG1022 164 GrevaDPAEleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHvfERTVSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 243 pwGIAAVGGTNVcvrklHAPSIYHL---IRDHGVTHMYGAPIVL-----QILSASQESDqPLKSPV------------NF 302
Cdd:COG1022 244 --YALAAGATVA-----FAESPDTLaedLREVKPTFMLAVPRVWekvyaGIQAKAEEAG-GLKRKLfrwalavgrryaRA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 303 LTAGSSPPA-----------TVL--LRA------------------------ESLGFIVSHGYGLTETAGVIvsCAWKPN 345
Cdd:COG1022 316 RLAGKSPSLllrlkhaladkLVFskLREalggrlrfavsggaalgpelarffRALGIPVLEGYGLTETSPVI--TVNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 346 WNRLpasdqaqlksrqgvRTVG--FSEIDVvdpesgrsveRDGETvGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTG 422
Cdd:COG1022 394 DNRI--------------GTVGppLPGVEV----------KIAED-GEILVRGPNVMKGYYKNPEATAEAFdADGWLHTG 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 423 DLGVIHGDGYLEIKDRSKDVII-SGGENVSSVEVEAVLYTNPAVNEAAVVA--RP 474
Cdd:COG1022 449 DIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVGdgRP 503
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
44-538 |
9.20e-41 |
|
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: 152.67 E-value: 9.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 44 RETNHRclcVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDffys 123
Cdd:cd05973 7 RALSAR---FANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 124 dlaveaitmllnppilvlianeeeeeggaeVTERSKFcylysdlitrgnpdfkwirpgsEWDPIVVNYTSGTTSSPKGVV 203
Cdd:cd05973 80 ------------------------------AANRHKL----------------------DSDPFVMMFTSGTTGLPKGVP 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 204 HCHRGIfvMTLDSLTDWAVPKTP--VYlWTL--PifhanGWTYPWGIAAVGGTNVCVRKL------HAPSIYHLIRDHGV 273
Cdd:cd05973 108 VPLRAL--AAFGAYLRDAVDLRPedSF-WNAadP-----GWAYGLYYAITGPLALGHPTIlleggfSVESTWRVIERLGV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 274 THMYGAPIVLQIL-SASQESDQPLKSPVNFLTAGSSP--PATVLLRAESLGFIVSHGYGLTETaGVIVSCAWKPnwnrlp 350
Cdd:cd05973 180 TNLAGSPTAYRLLmAAGAEVPARPKGRLRRVSSAGEPltPEVIRWFDAALGVPIHDHYGQTEL-GMVLANHHAL------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 351 aSDQAQLKSrQGVRTVGFSeIDVVDPESGRSVERDGETVGeIVLRGSSIML--GYLKNPigtQNSFKNGWFFTGDLGVIH 428
Cdd:cd05973 253 -EHPVHAGS-AGRAMPGWR-VAVLDDDGDELGPGEPGRLA-IDIANSPLMWfrGYQLPD---TPAIDGGYYLTGDTVEFD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 429 GDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKPT-DKEIIEYCKY 507
Cdd:cd05973 326 PDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAlADELQLHVKK 405
|
490 500 510
....*....|....*....|....*....|.
gi 15222924 508 KMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:cd05973 406 RLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
41-538 |
2.08e-40 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 154.28 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQ-------------FSVPMSGAI---LNN------INT- 97
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALlgalkngaivgplFEAFMEEAVrdrLEDseakvlITTp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 98 RLDARTVSVLLRHCESKLLFvdffysDLAVEAITMLLNppilvlianeeeeeggaevterskfcylYSDLITRGNPDFKw 177
Cdd:PRK04319 154 ALLERKPADDLPSLKHVLLV------GEDVEEGPGTLD----------------------------FNALMEQASDEFD- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 178 IRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGifvMTLDSLT-DWAVPKTP--VYLWTlpifhAN-GW----TYpwGIAA- 248
Cdd:PRK04319 199 IEWTDREDGAILHYTSGSTGKPKGVLHVHNA---MLQHYQTgKYVLDLHEddVYWCT-----ADpGWvtgtSY--GIFAp 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 249 --VGGTNVCVR-KLHAPSIYHLIRDHGVTHMYGAPIVLQILsasqesdqplkspvnfLTAGSSPPATVLLRaeSLGFIVS 325
Cdd:PRK04319 269 wlNGATNVIDGgRFSPERWYRILEDYKVTVWYTAPTAIRML----------------MGAGDDLVKKYDLS--SLRHILS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 326 HG--------------YGL--------TETAGVIVScawkpNWnrlPASDqaqLKSRQGVRTVGFSEIDVVDPESGrsvE 383
Cdd:PRK04319 331 VGeplnpevvrwgmkvFGLpihdnwwmTETGGIMIA-----NY---PAMD---IKPGSMGKPLPGIEAAIVDDQGN---E 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 384 RDGETVGEIVLRGS--SIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYT 461
Cdd:PRK04319 397 LPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLME 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 462 NPAVNEAAVVARPDEFWGETPCAFVSLKPGLTrkPTD---KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:PRK04319 477 HPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEelkEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
191-539 |
8.23e-40 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 151.18 E-value: 8.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGIFVMTLdSLTD-WAVPKTPVYLWTLPIFHANGWTYPWGIA-AVGGTNVCVRKLHAPSIYHLI 268
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNAL-TLVDyWRFTPDDVLIHALPIFHTHGLFVATNVAlLAGASMIFLPKFDPDAVLALM 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 269 RDhgVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSPpatvLL----RA--ESLGFIVSHGYGLTETaGVIVScaw 342
Cdd:PRK07514 242 PR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAP----LLaethREfqERTGHAILERYGMTET-NMNTS--- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 343 kpnwNRLpasdqaqlksrQGVR---TVGFS----EIDVVDPESGRSVERDGetVGEIVLRGSSIMLGYLKNPIGTQNSFK 415
Cdd:PRK07514 312 ----NPY-----------DGERragTVGFPlpgvSLRVTDPETGAELPPGE--IGMIEVKGPNVFKGYWRMPEKTAEEFR 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 416 -NGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTr 494
Cdd:PRK07514 375 aDGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAA- 453
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15222924 495 kPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK07514 454 -LDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
14-539 |
1.16e-39 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 151.67 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 14 LTLLGFLERAATVYGDCTSIVYG-NSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAIL 92
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVEAvTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 93 NNINTRLDARTVSVLLRHCESKLLFVDffysDLAVEAITMLlNPPILVL----IANEEEEEGGAEVTERSKFCYLYSDLI 168
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKLIVTN----DTNYGKVKGL-GLPVIVLgeekIEGAVNWKELLEAADRAGDTSDNEEIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 169 trgnpdfkwirpgsEWDPIVVNYTSGTTSSPKGVVHCHRGI---FVMTLDSLTDWAVPKTpVYLWTLPIFHANGWTypwG 245
Cdd:PLN02330 183 --------------QTDLCALPFSSGTTGISKGVMLTHRNLvanLCSSLFSVGPEMIGQV-VTLGLIPFFHIYGIT---G 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 246 IAAV----GGTNVCVRKLHAPSIYHLIRDHGVTHmygAPIVLQILSA------SQESDQPlKSPVNFLTAGSSPPATVLL 315
Cdd:PLN02330 245 ICCAtlrnKGKVVVMSRFELRTFLNALITQEVSF---APIVPPIILNlvknpiVEEFDLS-KLKLQAIMTAAAPLAPELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 316 RA---ESLGFIVSHGYGLTETAGVIVScawkpnwNRLPASDQAQLKSRqgvrTVGFS----EIDVVDPESGRSVERDgeT 388
Cdd:PLN02330 321 TAfeaKFPGVQVQEAYGLTEHSCITLT-------HGDPEKGHGIAKKN----SVGFIlpnlEVKFIDPDTGRSLPKN--T 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 389 VGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNE 467
Cdd:PLN02330 388 PGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVED 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222924 468 AAVVARPDEFWGETPCAFVSLKPGLTRKPTDkeIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PLN02330 468 AAVVPLPDEEAGEIPAACVVINPKAKESEED--ILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
53-540 |
1.30e-39 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 151.92 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 53 VASALS-SIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVdffySDLAVEAIT 131
Cdd:PLN02574 79 MAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT----SPENVEKLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 132 MLLNPPILVlianEEEEEGGAEVTERSKFCYLYSdlitrGNPDFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGiFV 211
Cdd:PLN02574 155 PLGVPVIGV----PENYDFDSKRIEFPKFYELIK-----EDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRN-LI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 212 MTLDSL-----TDWAVPKTP-VYLWTLPIFHANGWT-YPWGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQ 284
Cdd:PLN02574 225 AMVELFvrfeaSQYEYPGSDnVYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 285 IL--SASQESDQPLKSPVNfLTAGSSPPATVLLraESLGFIVSH-----GYGLTETAGVivscawkpnWNRLPASDQAQL 357
Cdd:PLN02574 305 ALtkKAKGVCGEVLKSLKQ-VSCGAAPLSGKFI--QDFVQTLPHvdfiqGYGMTESTAV---------GTRGFNTEKLSK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 358 KSRQGVRTVGFsEIDVVDPESGRSVERDGetVGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIK 436
Cdd:PLN02574 373 YSSVGLLAPNM-QAKVVDWSTGCLLPPGN--CGELWIQGPGVMKGYLNNPKATQSTIdKDGWLRTGDIAYFDEDGYLYIV 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 437 DRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKPTDkeIIEYCKYKMPRYMAPK 516
Cdd:PLN02574 450 DRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA--VINYVAKQVAPYKKVR 527
|
490 500
....*....|....*....|....
gi 15222924 517 TVSFLEELPKTSTGKIIKSLLKEI 540
Cdd:PLN02574 528 KVVFVQSIPKSPAGKILRRELKRS 551
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
20-540 |
7.44e-39 |
|
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: 149.21 E-value: 7.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 20 LERAATVyGDCTSIVYGNSTV-YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTpemyeLQFSVPMS-----GAILN 93
Cdd:cd17642 24 MKRYASV-PGTIAFTDAHTGVnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENS-----LQFFLPVIaglfiGVGVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 94 NINTRLDARTVSVLLRHCESKLLFVdffySDLAVEAITMLL--NPPILVLIAneeeeegGAEVTERSKFCYLYSdLITRG 171
Cdd:cd17642 98 PTNDIYNERELDHSLNISKPTIVFC----SKKGLQKVLNVQkkLKIIKTIII-------LDSKEDYKGYQCLYT-FITQN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 172 NP------DFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTD-----WAVPKTPVyLWTLPIFHANGW 240
Cdd:cd17642 166 LPpgfneyDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNI-VARFSHARDpifgnQIIPDTAI-LTVIPFHHGFGM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 241 TYPWGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRAESL 320
Cdd:cd17642 244 FTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 321 GF---IVSHGYGLTE-TAGVIVScawkPNWNRLPASdqaqlksrQGVRTVGFsEIDVVDPESGRSV---ERdgetvGEIV 393
Cdd:cd17642 324 RFklpGIRQGYGLTEtTSAILIT----PEGDDKPGA--------VGKVVPFF-YAKVVDLDTGKTLgpnER-----GELC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 394 LRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVA 472
Cdd:cd17642 386 VKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAG 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222924 473 RPDEFWGETPCAFVSLKPGLTRkpTDKEIIEYCKYKM-PRYMAPKTVSFLEELPKTSTGKIIKSLLKEI 540
Cdd:cd17642 466 IPDEDAGELPAAVVVLEAGKTM--TEKEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
22-539 |
8.88e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 149.02 E-value: 8.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 22 RAATVYGDCTsivygnstvYTWRETNHRCLCVASALSSIGI-GRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLD 100
Cdd:PRK13388 17 TIAVRYGDRT---------WTWREVLAEAAARAAALIALADpDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 101 ARTVSVLLRHCESKLLFVDFFYSDLaveaITMLLNPPILVLIANEEEeeggaevterskfcylYSDLITRGnPDFKWIRP 180
Cdd:PRK13388 88 GAALAADIRRADCQLLVTDAEHRPL----LDGLDLPGVRVLDVDTPA----------------YAELVAAA-GALTPHRE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 181 GSEWDPIVVNYTSGTTSSPKGVVhCHRGIFVMTLDSLTD-WAVPKTPVYLWTLPIFHANGWTYPWGIA-AVGGTNVCVRK 258
Cdd:PRK13388 147 VDAMDPFMLIFTSGTTGAPKAVR-CSHGRLAFAGRALTErFGLTRDDVCYVSMPLFHSNAVMAGWAPAvASGAAVALPAK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 LHAPSIYHLIRDHGVTHM-Y-GAPI--VLQILSASQESDQPLKspVNFLTAGSSPPATVLLRaeSLGFIVSHGYGLTETA 334
Cdd:PRK13388 226 FSASGFLDDVRRYGATYFnYvGKPLayILATPERPDDADNPLR--VAFGNEASPRDIAEFSR--RFGCQVEDGYGSSEGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 335 GVIVscawkpnwnRLPASDqaqlksrQGVRTVGFSEIDVVDPESGRSVER-----DG------ETVGEIV-LRGSSIMLG 402
Cdd:PRK13388 302 VIVV---------REPGTP-------PGSIGRGAPGVAIYNPETLTECAVarfdaHGallnadEAIGELVnTAGAGFFEG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 403 YLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETP 482
Cdd:PRK13388 366 YYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQV 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 483 CAFVSLKPGLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK13388 446 MAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
42-539 |
1.43e-38 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 148.37 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFF 121
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 122 YSDLAVEAitmLLNPPILVLIANEEEEEGGAEVTErskfcylysdLITrgNPDFKWIRPGSEWDPIVVnYTSGTTSSPKG 201
Cdd:PRK13382 150 FSATVDRA---LADCPQATRIVAWTDEDHDLTVEV----------LIA--AHAGQRPEPTGRKGRVIL-LTSGTTGTPKG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 202 VVHCHRGIFvMTLDSLTD---WAVPKtPVYLwTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYG 278
Cdd:PRK13382 214 ARRSGPGGI-GTLKAILDrtpWRAEE-PTVI-VAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLDLIDRHRATGLAV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 279 APIVL-QILSASQES-DQPLKSPVNFLTAGSS--PPATVLLRAESLGFIVSHGYGLTEtAGVIVSCAwkpnwnrlPASDQ 354
Cdd:PRK13382 291 VPVMFdRIMDLPAEVrNRYSGRSLRFAAASGSrmRPDVVIAFMDQFGDVIYNNYNATE-AGMIATAT--------PADLR 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 355 AQLKSrqGVRTVGFSEIDVVDPEsGRSVErDGEtVGEIVLRGSSIMLGYLKnpiGTQNSFKNGWFFTGDLGVIHGDGYLE 434
Cdd:PRK13382 362 AAPDT--AGRPAEGTEIRILDQD-FREVP-TGE-VGTIFVRNDTQFDGYTS---GSTKDFHDGFMASGDVGYLDENGRLF 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 435 IKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKPtdKEIIEYCKYKMPRYMA 514
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATP--ETLKQHVRDNLANYKV 511
|
490 500
....*....|....*....|....*
gi 15222924 515 PKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK13382 512 PRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
45-539 |
1.52e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 147.92 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 45 ETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLF--VDFFY 122
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahADLLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 123 S--DLAVEAITMLLNPPILVLIANEEEEEGGAEVTErskfcylysdlitrGNPDFK-WIRPGSEWDPIVVN------YTS 193
Cdd:PRK12406 96 GlaSALPAGVTVLSVPTPPEIAAAYRISPALLTPPA--------------GAIDWEgWLAQQEPYDGPPVPqpqsmiYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 194 GTTSSPKGVvhcHRgiFVMTLDSLTDWA--------VPKTPVYLWTLPIFHANGWTYpwGIAA--VGGTNVCVRKLHAPS 263
Cdd:PRK12406 162 GTTGHPKGV---RR--AAPTPEQAAAAEqmraliygLKPGIRALLTGPLYHSAPNAY--GLRAgrLGGVLVLQPRFDPEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 264 IYHLIRDHGVTHMYGAP---IVLQILSASQESDQPLKSpVNFLTAGSSP-PATVLlRA--ESLGFIVSHGYGLTETaGVI 337
Cdd:PRK12406 235 LLQLIERHRITHMHMVPtmfIRLLKLPEEVRAKYDVSS-LRHVIHAAAPcPADVK-RAmiEWWGPVIYEYYGSTES-GAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 338 VSCAwkpnwnrlpaSDQAQlkSRQGvrTVGF----SEIDVVDpESGRSVErDGEtVGEIVLRGSSIML-GYLKNPIGTQN 412
Cdd:PRK12406 312 TFAT----------SEDAL--SHPG--TVGKaapgAELRFVD-EDGRPLP-QGE-IGEIYSRIAGNPDfTYHNKPEKRAE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 413 SFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGL 492
Cdd:PRK12406 375 IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGA 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15222924 493 TrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK12406 455 T--LDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1-539 |
2.49e-38 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 147.73 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 1 MEDLKPSAANSLPlTLLGFLERAATVYGDCTS-IVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMY 79
Cdd:PRK05852 4 MGGAAPMASDFGP-RIADLVEVAATRLPEAPAlVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 80 ELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFF-YSDLAVEAITMLlnpPILVLIANEEEEEGGAevters 158
Cdd:PRK05852 83 VALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADgPHDRAEPTTRWW---PLTVNVGGDSGPSGGT------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 159 kfcyLYSDLITRGNPDFKWIRP-GSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHA 237
Cdd:PRK05852 154 ----LSVHLDAATEPTPATSTPeGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 238 NGWTYPWGIAAVGGTNVCVR---KLHAPSIYHLIRDHGVTHMYGAPIVLQIL--SASQESDQPLKSPVNFLTAGSSP--P 310
Cdd:PRK05852 230 HGLIAALLATLASGGAVLLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILleRAATEPSGRKPAALRFIRSCSAPltA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 311 ATVLLRAESLGFIVSHGYGLTETAGVIVScawkpnwNRLPASDQAQlKSRQGVRTVGFS---EIDVVDPEsGRSVERDge 387
Cdd:PRK05852 310 ETAQALQTEFAAPVVCAFGMTEATHQVTT-------TQIEGIGQTE-NPVVSTGLVGRStgaQIRIVGSD-GLPLPAG-- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 388 TVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNE 467
Cdd:PRK05852 379 AVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVME 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222924 468 AAVVARPDEFWGETPCAFVSlkPGLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK05852 459 AAVFGVPDQLYGEAVAAVIV--PRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
21-538 |
3.70e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 144.00 E-value: 3.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 21 ERAATVYGDCTSIVygnstvyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLD 100
Cdd:PRK13390 12 DRPAVIVAETGEQV-------SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 101 ARTVSVLLRHCESKLLFVDFFYSDLAVEAitmllNPPILVLIANEEeeeggaevtERSKFCYLYSDLITRGNPDFKwiRP 180
Cdd:PRK13390 85 APEADYIVGDSGARVLVASAALDGLAAKV-----GADLPLRLSFGG---------EIDGFGSFEAALAGAGPRLTE--QP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 181 GSEwdpiVVNYTSGTTSSPKG----------------VVHCHRGIFVMTldsltdwavpKTPVYLWTLPIFHANGWTYPW 244
Cdd:PRK13390 149 CGA----VMLYSSGTTGFPKGiqpdlpgrdvdapgdpIVAIARAFYDIS----------ESDIYYSSAPIYHAAPLRWCS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 245 GIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAP---IVLQILSASQESDQPLKSPVNFLTAGSSPPATVL-LRAESL 320
Cdd:PRK13390 215 MVHALGGTVVLAKRFDAQATLGHVERYRITVTQMVPtmfVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKhAMIDWL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 321 GFIVSHGYGLTETAGVIVSCAwkPNWNRLPASdqaqlKSRQGVRTVGFSEIDVVDPESGRsverdgetVGEIVLRGSSIM 400
Cdd:PRK13390 295 GPIVYEYYSSTEAHGMTFIDS--PDWLAHPGS-----VGRSVLGDLHICDDDGNELPAGR--------IGTVYFERDRLP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 401 LGYLKNPIGT---QNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEF 477
Cdd:PRK13390 360 FRYLNDPEKTaaaQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPE 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 478 WGETPCAFVSLKPGLtrKPTD---KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:PRK13390 440 MGEQVKAVIQLVEGI--RGSDelaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
31-532 |
4.45e-37 |
|
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: 142.67 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 31 TSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRL-DARtVSVLLR 109
Cdd:cd05930 4 VAVVDGDQSL-TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYpAER-LAYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 110 HCESKLLFVDffYSDLAveaitmllnppilvlianeeeeeggaevterskfcYLYsdlitrgnpdfkwirpgsewdpivv 189
Cdd:cd05930 82 DSGAKLVLTD--PDDLA-----------------------------------YVI------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 190 nYTSGTTSSPKGVVHCHRGIfVMTLDSLTDwAVPKTP---VYLWTLPIFHANGWTYPWGIAAvGGTNVCVRKLHAPSIYH 266
Cdd:cd05930 100 -YTSGSTGKPKGVMVEHRGL-VNLLLWMQE-AYPLTPgdrVLQFTSFSFDVSVWEIFGALLA-GATLVVLPEEVRKDPEA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 267 L---IRDHGVTHMYGAPIVLQILsASQESDQPLKSPVNFLTAGSSPPATVLLRAESLGF--IVSHGYGLTETAgvIVSCA 341
Cdd:cd05930 176 LadlLAEEGITVLHLTPSLLRLL-LQELELAALPSLRLVLVGGEALPPDLVRRWRELLPgaRLVNLYGPTEAT--VDATY 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 342 WkpnwnRLPASDQAQlksrqGVRTVGF----SEIDVVDPEsGRSVErDGEtVGEIVLRGSSIMLGYLKNPIGTQNSFKNG 417
Cdd:cd05930 253 Y-----RVPPDDEED-----GRVPIGRpipnTRVYVLDEN-LRPVP-PGV-PGELYIGGAGLARGYLNRPELTAERFVPN 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 418 WFF-------TGDLGVIHGDGYLEIKDRSKD-VIISG-----GEnvssveVEAVLYTNPAVNEAAVVARPDEFWGETPCA 484
Cdd:cd05930 320 PFGpgermyrTGDLVRWLPDGNLEFLGRIDDqVKIRGyrielGE------IEAALLAHPGVREAAVVAREDGDGEKRLVA 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15222924 485 FVSLKPGLTrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd05930 394 YVVPDEGGE--LDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
191-536 |
5.86e-37 |
|
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: 142.39 E-value: 5.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGifvmtLDSLTDWAVPKTPV-----------YLWTLPIFhangwtYPWGIAAVGGTNVCVRKL 259
Cdd:cd05945 104 FTSGSTGRPKGVQISHDN-----LVSFTNWMLSDFPLgpgdvflnqapFSFDLSVM------DLYPALASGATLVPVPRD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 260 HAPSIYHL---IRDHGVTHMYGAPIVLQILSASQESDQP-LKSPVNFLTAGSSPP---ATVLLRAESLGFIVShGYGLTE 332
Cdd:cd05945 173 ATADPKQLfrfLAEHGITVWVSTPSFAAMCLLSPTFTPEsLPSLRHFLFCGEVLPhktARALQQRFPDARIYN-TYGPTE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 333 TAGVIVSCAWKP----NWNRLPasdqaqlksrqgvrtVGF----SEIDVVDpESGRSVErDGETvGEIVLRGSSIMLGYL 404
Cdd:cd05945 252 ATVAVTYIEVTPevldGYDRLP---------------IGYakpgAKLVILD-EDGRPVP-PGEK-GELVISGPSVSKGYL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 405 KNPIGTQNSF----KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGE 480
Cdd:cd05945 314 NNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVT 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 481 TPCAFVSLKPGLTRKPTdKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI-IKSL 536
Cdd:cd05945 394 ELIAFVVPKPGAEAGLT-KAIKAELAERLPPYMIPRRFVYLDELPLNANGKIdRKAL 449
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
34-537 |
8.31e-37 |
|
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: 142.20 E-value: 8.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 34 VYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCES 113
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 114 KLLFVdffysdlaveaitmllnppilvlianeeeeeggaevterskfcylysdlitrGNPDfkwirpgsewDPIVVNYTS 193
Cdd:cd05914 81 KAIFV----------------------------------------------------SDED----------DVALINYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 194 GTTSSPKGVVHCHRGI-----FVMTLDSLTdwavpKTPVYLWTLPIFHANGWTYPWGIA-AVGGTNVCVRKLHAPSIyHL 267
Cdd:cd05914 99 GTTGNSKGVMLTYRNIvsnvdGVKEVVLLG-----KGDKILSILPLHHIYPLTFTLLLPlLNGAHVVFLDKIPSAKI-IA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 268 IRDHGVTHMYGAPIVLQILSASQESDQP----------LKSPVN----------------------FLTAGSSPPATVLL 315
Cdd:cd05914 173 LAFAQVTPTLGVPVPLVIEKIFKMDIIPkltlkkfkfkLAKKINnrkirklafkkvheafggnikeFVIGGAKINPDVEE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 316 RAESLGFIVSHGYGLTETAGVIvscAWKPnWNRLPASDQAQLKSRQGVRtvgfseIDVVDPESGRsverdgetvGEIVLR 395
Cdd:cd05914 253 FLRTIGFPYTIGYGMTETAPII---SYSP-PNRIRLGSAGKVIDGVEVR------IDSPDPATGE---------GEIIVR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 396 GSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISG-GENVSSVEVEAVLYTNPAVNEAAVVAR 473
Cdd:cd05914 314 GPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVVQ 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 474 -----------PDefwgetpcaFVSLKPGLTRKPTDK---EIIEYCKYKMPRYmapKTVS----FLEELPKTSTGKIIKS 535
Cdd:cd05914 394 ekklvalayidPD---------FLDVKALKQRNIIDAikwEVRDKVNQKVPNY---KKISkvkiVKEEFEKTPKGKIKRF 461
|
..
gi 15222924 536 LL 537
Cdd:cd05914 462 LY 463
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
41-539 |
2.74e-36 |
|
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: 141.51 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTpemyeLQFSVPMSGAILNNI-----NTRLDARTVSVLLRHCESKL 115
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDG-----VDFPIAFLGAIRAGIvpvalNTLLTADDYAYMLEDSRARV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 116 LFVDFFYSDLAVEAITMLlnPPILVLIANEEEEEGGAEVTErskfcylysdLITRGNPDFKwIRPGSEWDPIVVNYTSGT 195
Cdd:TIGR02262 106 VFVSGALLPVIKAALGKS--PHLEHRVVVGRPEAGEVQLAE----------LLATESEQFK-PAATQADDPAFWLYSSGS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 196 TSSPKGVVHCHRGIFVMT-LDSLTDWAVPKTPVYLWTLPIFHA----NGWTYPWGiaaVGGTNVCVRKLHAP-SIYHLIR 269
Cdd:TIGR02262 173 TGMPKGVVHTHSNPYWTAeLYARNTLGIREDDVCFSAAKLFFAyglgNALTFPMS---VGATTVLMGERPTPdAVFDRLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 270 DHGVTHMYGAPIVLQILSASQESdqPLKSPVNF---LTAGSSPPATVLLRAES-LGFIVSHGYGLTETAGVIVSCAwkPN 345
Cdd:TIGR02262 250 RHQPTIFYGVPTLYAAMLADPNL--PSEDQVRLrlcTSAGEALPAEVGQRWQArFGVDIVDGIGSTEMLHIFLSNL--PG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 346 WNRLPASdqaqlksrqGVRTVGFsEIDVVDpESGRSVErDGEtVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLG 425
Cdd:TIGR02262 326 DVRYGTS---------GKPVPGY-RLRLVG-DGGQDVA-DGE-PGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 426 VIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKPTdkEIIEYC 505
Cdd:TIGR02262 393 VRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALET--ELKEHV 470
|
490 500 510
....*....|....*....|....*....|....
gi 15222924 506 KYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:TIGR02262 471 KDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
191-542 |
3.68e-36 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 141.70 E-value: 3.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGIFVMTLDS-------LTDWAVPKTPVYLWTLPIFHANGWT--YPWGIAAvGGTNVC------ 255
Cdd:PRK07059 211 YTGGTTGVSKGATLLHRNIVANVLQMeawlqpaFEKKPRPDQLNFVCALPLYHIFALTvcGLLGMRT-GGRNILipnprd 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 256 ----VRKLHApsiYHLIRDHGVTHMYGApivlqiLSASQESDQPLKSPVNFLTAG----SSPPATVLLraESLGFIVSHG 327
Cdd:PRK07059 290 ipgfIKELKK---YQVHIFPAVNTLYNA------LLNNPDFDKLDFSKLIVANGGgmavQRPVAERWL--EMTGCPITEG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 YGLTETAGViVSCawkpnwNRLPASDQAQlksrqgvrTVGF----SEIDVVDpESGRSVERdGEtVGEIVLRGSSIMLGY 403
Cdd:PRK07059 359 YGLSETSPV-ATC------NPVDATEFSG--------TIGLplpsTEVSIRD-DDGNDLPL-GE-PGEICIRGPQVMAGY 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 404 LKNPIGTQNS-FKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETP 482
Cdd:PRK07059 421 WNRPDETAKVmTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAV 500
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222924 483 CAFVSLK-PGLtrkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAK 542
Cdd:PRK07059 501 KLFVVKKdPAL----TEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA 557
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
327-539 |
5.71e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 141.34 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 327 GYGLTETAGVIVSCAWkpnwnrlpasdqaQLKSRQGvrTVGF----SEIDVVDpESGRSVERdGETvGEIVLRGSSIMLG 402
Cdd:PRK08974 356 GYGLTECSPLVSVNPY-------------DLDYYSG--SIGLpvpsTEIKLVD-DDGNEVPP-GEP-GELWVKGPQVMLG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 403 YLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETP 482
Cdd:PRK08974 418 YWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAV 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15222924 483 CAFVSLK-PGLTRkptdKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK08974 498 KIFVVKKdPSLTE----EELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
183-539 |
8.28e-36 |
|
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: 139.43 E-value: 8.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 183 EWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTlDSLTDWAVPKTP----VYLWTLPIFHANGWTYPWGIAAVGGTNVCVRK 258
Cdd:cd05929 124 EAAGWKMLYSGGTTGRPKGIKRGLPGGPPDN-DTLMAAALGFGPgadsVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 LHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQ------PLKSPVNflTAGSSPPATVLLRAESLGFIVSHGYGLTE 332
Cdd:cd05929 203 FDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRnaydlsSLKRVIH--AAAPCPPWVKEQWIDWGGPIIWEYYGGTE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 333 TAG--VIVSCAWkpnwnrlpasdqaqLKSRQGVRTVGFSEIDVVDpESGRSVErDGETvGEIVLRGSSIMLgYLKNPIGT 410
Cdd:cd05929 281 GQGltIINGEEW--------------LTHPGSVGRAVLGKVHILD-EDGNEVP-PGEI-GEVYFANGPGFE-YTNDPEKT 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 411 QNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLK 489
Cdd:cd05929 343 AAARnEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPA 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15222924 490 PGLTRKPTD-KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05929 423 PGADAGTALaEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
185-532 |
1.73e-35 |
|
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: 138.34 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGwTYPWGIAAVGGTNVCVRKLHAP-- 262
Cdd:cd05922 118 DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLdd 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 263 SIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSpVNFLT--AGSSPPATV-LLRAESLGFIVSHGYGLTETagvivs 339
Cdd:cd05922 197 AFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPS-LRYLTqaGGRLPQETIaRLRELLPGAQVYVMYGQTEA------ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 340 cawKPNWNRLPASdqaQLKSRQGV--RTVGFSEIDVVDPESGRsvERDGEtVGEIVLRGSSIMLGYLKNPIG-TQNSFKN 416
Cdd:cd05922 270 ---TRRMTYLPPE---RILEKPGSigLAIPGGEFEILDDDGTP--TPPGE-PGEIVHRGPNVMKGYWNDPPYrRKEGRGG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 417 GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFwGETPCAFVSLKPgltrKP 496
Cdd:cd05922 341 GVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPD----KI 415
|
330 340 350
....*....|....*....|....*....|....*.
gi 15222924 497 TDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd05922 416 DPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKV 451
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
185-532 |
2.97e-35 |
|
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: 138.23 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTDWAVPKTP-VYLWTLPIFHANGWT----YP--WGIAAVGGTNvcvr 257
Cdd:cd05909 148 DPAVILFTSGSEGLPKGVVLSHKNL-LANVEQITAIFDPNPEdVVFGALPFFHSFGLTgclwLPllSGIKVVFHPN---- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 258 KLHAPSIYHLIRDHGVTHMYGAPIVL-QILSASQESDqpLKSpVNFLTAGSS--PPATVLLRAESLGFIVSHGYGLTETA 334
Cdd:cd05909 223 PLDYKKIPELIYDKKATILLGTPTFLrGYARAAHPED--FSS-LRLVVAGAEklKDTLRQEFQEKFGIRILEGYGTTECS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 335 GVIvSCawkpnwNRlPASDQaqlksRQGvrTVGFS----EIDVVDPESGRSVErDGETvGEIVLRGSSIMLGYLKNPIGT 410
Cdd:cd05909 300 PVI-SV------NT-PQSPN-----KEG--TVGRPlpgmEVKIVSVETHEEVP-IGEG-GLLLVRGPNVMLGYLNEPELT 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 411 QNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTN-PAVNEAAVVARPDEFWGETPCAFvslk 489
Cdd:cd05909 363 SFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL---- 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15222924 490 pgLTRKPTDK-EIIEYCK-YKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd05909 439 --TTTTDTDPsSLNDILKnAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
20-539 |
3.52e-35 |
|
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: 138.78 E-value: 3.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 20 LERAATVYGDCTSIV----YGNSTVYTWRETNHRCLCVASALSSIGIGRSD-VVSVLSANtpemYELQFSVP---MSGAI 91
Cdd:cd05970 23 VDAMAKEYPDKLALVwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDtVMLTLKRR----YEFWYSLLalhKLGAI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 92 LNNINTRLDARTVSVLLRHCESKLLFVD--FFYSDLAVEAITMLLNPPILVLIANEeeeeggaevtERSKFCYlYSDLIT 169
Cdd:cd05970 99 AIPATHQLTAKDIVYRIESADIKMIVAIaeDNIPEEIEKAAPECPSKPKLVWVGDP----------VPEGWID-FRKLIK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 170 RGNPDFKwiRPGSEW-----DPIVVNYTSGTTSSPKGVVHCH--------RGIFVMTL--DSL------TDWAVPktpvy 228
Cdd:cd05970 168 NASPDFE--RPTANSypcgeDILLVYFSSGTTGMPKMVEHDFtyplghivTAKYWQNVreGGLhltvadTGWGKA----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 229 LWtlpifhanGWTYPWGIAavgGTNVCV---RKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTA 305
Cdd:cd05970 241 VW--------GKIYGQWIA---GAAVFVydyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 306 GSSPPATVLLR-AESLGFIVSHGYGLTETAGVIVSCAW-KPNwnrlPASdqaqlksrQGVRTVGFsEIDVVDPEsGRSVE 383
Cdd:cd05970 310 GEALNPEVFNTfKEKTGIKLMEGFGQTETTLTIATFPWmEPK----PGS--------MGKPAPGY-EIDLIDRE-GRSCE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 384 RdGETvGEIVLRGSS-----IMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAV 458
Cdd:cd05970 376 A-GEE-GEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 459 LYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLtrKPTD---KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKS 535
Cdd:cd05970 454 LIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGY--EPSEelkKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRV 531
|
....
gi 15222924 536 LLKE 539
Cdd:cd05970 532 EIRE 535
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
21-543 |
1.51e-34 |
|
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: 137.83 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 21 ERAATVYgdcTSIVYGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLD 100
Cdd:cd05967 66 DQIALIY---DSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 101 ARTVSVLLRHCESKLLFVDFF---------YSDLAVEAITMLLNPPILVLIANEEEEEGGAEVTERSkfcYLYSDLITRG 171
Cdd:cd05967 143 AKELASRIDDAKPKLIVTASCgiepgkvvpYKPLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRD---LDWSELLAKA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 172 NP-DFKWIRPGsewDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSL-TDWAVPKTPVYLWTLPIfhanGW----TY-PW 244
Cdd:cd05967 220 EPvDCVPVAAT---DPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMrNIYGIKPGDVWWAASDV----GWvvghSYiVY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 245 GIAAVGGTNVC-----VRKLHAPSIYHLIRDHGVTHMYGAPIVLQIL-----SASQESDQPLKSPVNFLTAGSS-PPATV 313
Cdd:cd05967 293 GPLLHGATTVLyegkpVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIrkedpDGKYIKKYDLSSLRTLFLAGERlDPPTL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 314 LLRAESLGFIVSHGYGLTETaGVIVSCawkpnwnrlPASDQAQLKSRQGVRTV---GFsEIDVVDPEsGRSVERDgeTVG 390
Cdd:cd05967 373 EWAENTLGVPVIDHWWQTET-GWPITA---------NPVGLEPLPIKAGSPGKpvpGY-QVQVLDED-GEPVGPN--ELG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 391 EIVLRGS---SIMLGYLKNPIGTQNSFKN---GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPA 464
Cdd:cd05967 439 NIVIKLPlppGCLLTLWKNDERFKKLYLSkfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPA 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 465 VNEAAVVARPDEFWGETPCAFVSLKPGLTRKPTD--KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAK 542
Cdd:cd05967 519 VAECAVVGVRDELKGQVPLGLVVLKEGVKITAEEleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIAD 598
|
.
gi 15222924 543 N 543
Cdd:cd05967 599 G 599
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
36-540 |
2.56e-34 |
|
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: 137.24 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 36 GNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKL 115
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 116 LFV-DFFYSDlaveaiTMLLNPPILVLIANEEEEEGGAEVTER--------SKFCYLYSDLITRGNPDfKWIRPGSEwDP 186
Cdd:cd05968 167 LITaDGFTRR------GREVNLKEEADKACAQCPTVEKVVVVRhlgndftpAKGRDLSYDEEKETAGD-GAERTESE-DP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 187 IVVNYTSGTTSSPKGVVHCHRGIFV-MTLDSLTDWAVPKTPVYLWtlpiFHANGWTY-PW---GIAAVGGTNVCVRKL-- 259
Cdd:cd05968 239 LMIIYTSGTTGKPKGTVHVHAGFPLkAAQDMYFQFDLKPGDLLTW----FTDLGWMMgPWlifGGLILGATMVLYDGApd 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 260 --HAPSIYHLIRDHGVTHMYGAPIVLQILSAsqESDQPL----KSPVNFLTAGSSP--PATVLLRAESLGF----IVSHG 327
Cdd:cd05968 315 hpKADRLWRMVEDHEITHLGLSPTLIRALKP--RGDAPVnahdLSSLRVLGSTGEPwnPEPWNWLFETVGKgrnpIINYS 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 YGlTETAGVIVSCAW-KPnwnrlpasdqaqlksrqgVRTVGFS------EIDVVDpESGRSVErdgETVGEIVLRGSSIM 400
Cdd:cd05968 393 GG-TEISGGILGNVLiKP------------------IKPSSFNgpvpgmKADVLD-ESGKPAR---PEVGELVLLAPWPG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 401 L--GYLKNPIGTQNS----FKNGWFFtGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARP 474
Cdd:cd05968 450 MtrGFWRDEDRYLETywsrFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVP 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 475 DEFWGETPCAFVSLKPGLTRKPT-DKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEI 540
Cdd:cd05968 529 HPVKGEAIVCFVVLKPGVTPTEAlAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAA 595
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
34-539 |
7.23e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 134.81 E-value: 7.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 34 VYGNSTVYTWRETNHRCLCVASALSS-IGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCE 112
Cdd:PRK07867 22 LYFEDSFTSWREHIRGSAARAAALRArLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 113 SKLLFVDFFYSDLAVEaitmlLNPPILVLianeeeeeggaeVTERSKFCYLysdLITRGNPDFKWIRPGSEwDPIVVNYT 192
Cdd:PRK07867 102 CQLVLTESAHAELLDG-----LDPGVRVI------------NVDSPAWADE---LAAHRDAEPPFRVADPD-DLFMLIFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 193 SGTTSSPKGVVHCHR-----GIFVMTLDSLTdwavPKTPVYLwTLPIFHANGWTYPWGIA-AVGGTNVCVRKLHAPSIYH 266
Cdd:PRK07867 161 SGTSGDPKAVRCTHRkvasaGVMLAQRFGLG----PDDVCYV-SMPLFHSNAVMAGWAVAlAAGASIALRRKFSASGFLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 267 LIRDHGVTHM-Y-GAPivLQILSASQES----DQPLKspVNFLTAGSspPATVLLRAESLGFIVSHGYGLTETAgviVSC 340
Cdd:PRK07867 236 DVRRYGATYAnYvGKP--LSYVLATPERpddaDNPLR--IVYGNEGA--PGDIARFARRFGCVVVDGFGSTEGG---VAI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 341 AWKPNwnrlpasdqaqlkSRQGVRTVGFSEIDVVDPESGRSV-----ERDG-----ETVGEIV-LRGSSIMLGYLKNPIG 409
Cdd:PRK07867 307 TRTPD-------------TPPGALGPLPPGVAIVDPDTGTECppaedADGRllnadEAIGELVnTAGPGGFEGYYNDPEA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 410 TQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLK 489
Cdd:PRK07867 374 DAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15222924 490 PGLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK07867 454 PGAKFDPDAFAEFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
170-542 |
9.42e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 134.89 E-value: 9.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 170 RGNPdFKWIRPGSEwDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDS---LTDWAVPKTPVYLWTLPIFHANGWTYPWGI 246
Cdd:PRK05677 195 AGQP-VTEANPQAD-DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCralMGSNLNEGCEILIAPLPLYHIYAFTFHCMA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 247 AAV-GGTNVCV---RKLhaPSIYHLIRDHGVTHMYGAPIVLQILSASqESDQPLKSPVNFLTAgSSPPATVLLRAES--- 319
Cdd:PRK05677 273 MMLiGNHNILIsnpRDL--PAMVKELGKWKFSGFVGLNTLFVALCNN-EAFRKLDFSALKLTL-SGGMALQLATAERwke 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 320 -LGFIVSHGYGLTETAGVivscawkpnwnrlpasdqAQLKSRQGVR--TVGF----SEIDVVDPEsGRSVERdGEtVGEI 392
Cdd:PRK05677 349 vTGCAICEGYGMTETSPV------------------VSVNPSQAIQvgTIGIpvpsTLCKVIDDD-GNELPL-GE-VGEL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 393 VLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVV 471
Cdd:PRK05677 408 CVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAI 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222924 472 ARPDEFWGETPCAFVSLKPGLTRkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK--EIAK 542
Cdd:PRK05677 488 GVPDEKSGEAIKVFVVVKPGETL--TKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRdeELKK 558
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
185-531 |
1.30e-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: 130.97 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTL--------------PIFHANGWtYPWGIAAVG 250
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHKaaaaaagtvmfpapPLMHGTGS-WTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 251 GTNVCV--RKLHAPSIYHLIRDHGVTHM------YGAPIVLQILSASqesDQPLKSPVNFLTAGSSPPATV---LLRAES 319
Cdd:cd05924 83 GQTVVLpdDRFDPEEVWRTIEKHKVTSMtivgdaMARPLIDALRDAG---PYDLSSLFAISSGGALLSPEVkqgLLELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 320 lGFIVSHGYGLTET-AGVIVSCAWKPNwnrlpasdQAQLKSRQGVRTVgfseidVVDPeSGRSVERDGETVGEIVLRGSs 398
Cdd:cd05924 160 -NITLVDAFGSSETgFTGSGHSAGSGP--------ETGPFTRANPDTV------VLDD-DGRVVPPGSGGVGWIARRGH- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 399 IMLGYLKNPIGTQNSFK--NG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARP 474
Cdd:cd05924 223 IPLGYYGDEAKTAETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRP 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 475 DEFWGETPCAFVSLKPGLtrKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGK 531
Cdd:cd05924 303 DERWGQEVVAVVQLREGA--GVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
185-532 |
7.41e-33 |
|
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: 128.53 E-value: 7.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMT---LDSLTDWAVPKTpVYLwTLPIFHANGWTYPWGIAAVGGTNV--CVRKL 259
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPdilQKEGLNWVVGDV-TYL-PLPATHIGGLWWILTCLIHGGLCVtgGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 260 HApSIYHLIRDHGVTHMYGAP-----IVLQILSASQESDQplkspVNFLTAGSSPPATVLLR-AESLGFI-VSHGYGLTE 332
Cdd:cd17635 80 YK-SLFKILTTNAVTTTCLVPtllskLVSELKSANATVPS-----LRLIGYGGSRAIAADVRfIEATGLTnTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 333 TAGVIVscawkpnwnrLPASDQAQLKSRQGVRTVGfSEIDVVDPEsGRSVERDGEtvGEIVLRGSSIMLGYLKNPIGTQN 412
Cdd:cd17635 154 TGTALC----------LPTDDDSIEINAVGRPYPG-VDVYLAATD-GIAGPSASF--GTIWIKSPANMLGYWNNPERTAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 413 SFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVsLKPGL 492
Cdd:cd17635 220 VLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAV-VASAE 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15222924 493 TRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17635 299 LDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
164-539 |
1.60e-32 |
|
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: 131.05 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 164 YSDLITRGNPDFKWIRPGSEwDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPifhANGWTY- 242
Cdd:cd05928 155 FKELLNEASTEHHCVETGSQ-EPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTS---DTGWIKs 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 243 -------PWGIAAvggtnvCVRKLHAP-----SIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSSPP 310
Cdd:cd05928 231 awsslfePWIQGA------CVFVHHLPrfdplVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 311 ATVLLR-AESLGFIVSHGYGLTETaGVIvsCAWKPNWNRLPASdqaqlksrQGVRTVGFsEIDVVDpESGRSVERDGEtv 389
Cdd:cd05928 305 PEVLEKwKAQTGLDIYEGYGQTET-GLI--CANFKGMKIKPGS--------MGKASPPY-DVQIID-DNGNVLPPGTE-- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 390 GEIVLRGS-----SIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPA 464
Cdd:cd05928 370 GDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPA 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222924 465 VNEAAVVARPDEFWGETPCAFVSLKP---GLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05928 450 VVESAVVSSPDPIRGEVVKAFVVLAPqflSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
185-532 |
5.66e-32 |
|
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: 125.60 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHR---GIFV-----MTLDSLTDWAVPKTPVYLWTLpifhaNGWTYpwgIAAVGGTNVCV 256
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERswiESFVcnedlFNISGEDAILAPGPLSHSLFL-----YGAIS---ALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 257 RKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSpvnFLTAGSSPPATVL--LRAESLGFIVSHGYGLTETA 334
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKS---IFSSGQKLFESTKkkLKNIFPKANLIEFYGTSELS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 335 GVIVSC---AWKPNwnrlpasdqaqlksrqgvrTVG--FSEIDVvdpesgRSVERDGETVGEIVLRGSSIMLGYLKnpig 409
Cdd:cd17633 150 FITYNFnqeSRPPN-------------------SVGrpFPNVEI------EIRNADGGEIGKIFVKSEMVFSGYVR---- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 410 TQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLK 489
Cdd:cd17633 201 GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD 280
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15222924 490 pgltrKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17633 281 -----KLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
181-543 |
9.91e-31 |
|
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: 126.59 E-value: 9.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 181 GSEwDPIVVNYTSGTTSSPKGVVHCHRGIFV---MTLDSLTDwaVPKTPVYLWTLPIfhanGW----TY-PWGIAAVGGT 252
Cdd:TIGR02188 235 DSE-DPLFILYTSGSTGKPKGVLHTTGGYLLyaaMTMKYVFD--IKDGDIFWCTADV----GWitghSYiVYGPLANGAT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 253 NVCVRKL----HAPSIYHLIRDHGVTHMYGAPIVLQILSAsqESDQPLKS--------------PVN---------FLTA 305
Cdd:TIGR02188 308 TVMFEGVptypDPGRFWEIIEKHKVTIFYTAPTAIRALMR--LGDEWVKKhdlsslrllgsvgePINpeawmwyykVVGK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 306 GSSPPATVLLRAESLGFIVSHGYGLTETagvivscawKPNWNRLPASdqaqlksrqGVrtvgfsEIDVVDpESGRSVERD 385
Cdd:TIGR02188 386 ERCPIVDTWWQTETGGIMITPLPGATPT---------KPGSATLPFF---------GI------EPAVVD-EEGNPVEGP 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 386 GETvGEIVLRGS--SIMLGYLKNP---IGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLY 460
Cdd:TIGR02188 441 GEG-GYLVIKQPwpGMLRTIYGDHerfVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 461 TNPAVNEAAVVARPDEFWGETPCAFVSLKPGltRKPTD---KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:TIGR02188 520 SHPAVAEAAVVGIPDDIKGQAIYAFVTLKDG--YEPDDelrKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLL 597
|
....*.
gi 15222924 538 KEIAKN 543
Cdd:TIGR02188 598 RKIAAG 603
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
54-537 |
1.43e-30 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 125.51 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 54 ASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSvllRHCE----SKLLFVDFFYSDLAVEA 129
Cdd:PRK05857 55 AADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIE---RFCQitdpAAALVAPGSKMASSAVP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 130 ITMLLNPPILVLIANEEEEEGGAEVTERSKfcylysdlitrGNPDFkwirpGSEwDPIVVNYTSGTTSSPKGVVHCHRGI 209
Cdd:PRK05857 132 EALHSIPVIAVDIAAVTRESEHSLDAASLA-----------GNADQ-----GSE-DPLAMIFTSGTTGEPKAVLLANRTF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 210 FVMTlDSL-------TDWAVPKTPVYlwTLPIFHANG-WtypWGIAAVGGTNVCVRK-LHAPSIYHLIRDHGVTHMYGAP 280
Cdd:PRK05857 195 FAVP-DILqkeglnwVTWVVGETTYS--PLPATHIGGlW---WILTCLMHGGLCVTGgENTTSLLEILTTNAVATTCLVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 281 IVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLR-AESLGFIVSHGYGLTETaGVIVSCawkpnwnrLPASDQAQLKS 359
Cdd:PRK05857 269 TLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRfIEATGVRTAQVYGLSET-GCTALC--------LPTDDGSIVKI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 360 RQGV--RTVGFSEIDVVDPESGRSVERDG---ETVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLE 434
Cdd:PRK05857 340 EAGAvgRPYPGVDVYLAATDGIGPTAPGAgpsASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 435 IKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGetpcAFVSLKPGLTRKPTDKEIIEYCKYKMPRY-- 512
Cdd:PRK05857 420 IKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG----ALVGLAVVASAELDESAARALKHTIAARFrr 495
|
490 500 510
....*....|....*....|....*....|
gi 15222924 513 ----MA-PKTVSFLEELPKTSTGKIIKSLL 537
Cdd:PRK05857 496 esepMArPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
19-537 |
3.57e-30 |
|
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: 123.47 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 19 FLERAATvYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTR 98
Cdd:cd12117 3 FEEQAAR-TPDAVAVVYGDRSL-TYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 99 LDARTVSVLLRHCESKLLFvdffySDLAVEAITMLLNPPILVLIANEEEEEggaevterskfcylysdlitrGNPDfkwi 178
Cdd:cd12117 81 LPAERLAFMLADAGAKVLL-----TDRSLAGRAGGLEVAVVIDEALDAGPA---------------------GNPA---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 179 RPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDslTDWaVPKTP--VYLWTLPI-FHANgwTYP-WGIAAVGGTNV 254
Cdd:cd12117 131 VPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN--TNY-VTLGPddRVLQTSPLaFDAS--TFEiWGALLNGARLV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 255 CVRK---LHAPSIYHLIRDHGVTHMYgapivlqiLSAS------QESDQPLKSPVNFLTAGS--SPPA--TVLLRAESLG 321
Cdd:cd12117 206 LAPKgtlLDPDALGALIAEEGVTVLW--------LTAAlfnqlaDEDPECFAGLRELLTGGEvvSPPHvrRVLAACPGLR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 322 FIvsHGYGLTETAgvIVSCAWkpnwnRLPASDQAQLKSRQGvRTVGFSEIDVVDpESGRSVERDgeTVGEIVLRGSSIML 401
Cdd:cd12117 278 LV--NGYGPTENT--TFTTSH-----VVTELDEVAGSIPIG-RPIANTRVYVLD-EDGRPVPPG--VPGELYVGGDGLAL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 402 GYLKNPIGTQ-----NSFKNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARP 474
Cdd:cd12117 345 GYLNRPALTAerfvaDPFGPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVRE 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222924 475 DEFWGETPCAFVSlkpgLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:cd12117 425 DAGGDKRLVAYVV----AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
18-532 |
8.32e-30 |
|
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: 122.38 E-value: 8.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 18 GFLERAATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINT 97
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTL-TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 98 RLDARTVSVLLRHCESKLLFVDffySDLAvEAITMLLNPPILVLIANEEEEEGGAEVTERskfcylysdlitrgnPDfkw 177
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTT---ADLA-ARLPAGGDVALLGDEALAAPPATPPLVPPR---------------PD--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 178 irpgsewDPIVVNYTSGTTSSPKGVVHCHRGI----------FVMTLDsltDWAVPKTPVYlwtlpiFHANGWTYPWGIA 247
Cdd:cd17646 139 -------NLAYVIYTSGSTGRPKGVMVTHAGIvnrllwmqdeYPLGPG---DRVLQKTPLS------FDVSVWELFWPLV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 248 AvGGTNVCVR-KLHAPSIY--HLIRDHGVTHMYGAPIVLQILsaSQESDQPLKSPVNFLTAGSS--PPATVLLRAESLGF 322
Cdd:cd17646 203 A-GARLVVARpGGHRDPAYlaALIREHGVTTCHFVPSMLRVF--LAEPAAGSCASLRRVFCSGEalPPELAARFLALPGA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 323 IVSHGYGLTETAGVIVSCAWKPNWNRLPASdqaqlksrQGvRTVGFSEIDVVDpESGRSVErDGeTVGEIVLRGSSIMLG 402
Cdd:cd17646 280 ELHNLYGPTEAAIDVTHWPVRGPAETPSVP--------IG-RPVPNTRLYVLD-DALRPVP-VG-VPGELYLGGVQLARG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 403 YLKNPIGTQNSFKNGWF-------FTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPD 475
Cdd:cd17646 348 YLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAA 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 476 EFWGETPCAFVSLKPGLTrKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17646 428 PAGAARLVGYVVPAAGAA-GPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
20-532 |
9.26e-30 |
|
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: 122.45 E-value: 9.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 20 LERAATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRL 99
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRL-TYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 100 -DARTVSVLLRHCESKLLFVDFFYSDLAVEaitmlLNPPILVLIANEEEEEGGAEVTERSKFCYLYsdlitrgnpdfkwi 178
Cdd:cd17651 80 pAERLAFMLADAGPVLVLTHPALAGELAVE-----LVAVTLLDQPGAAAGADAEPDPALDADDLAY-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 179 rpgsewdpivVNYTSGTTSSPKGVVHCHRgifvmTLDSLTDW------AVPKTPVYLWTLPIFHANGWTYpWGIAAVGGT 252
Cdd:cd17651 141 ----------VIYTSGSTGRPKGVVMPHR-----SLANLVAWqarassLGPGARTLQFAGLGFDVSVQEI-FSTLCAGAT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 253 NVCVR---KLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQ-ESDQPLKSPVNFLTAGSSPPATVLLR---AESLGFIVS 325
Cdd:cd17651 205 LVLPPeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGrPLGVRLAALRYLLTGGEQLVLTEDLRefcAGLPGLRLH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 326 HGYGLTETAgvIVSCAWKPN----WNRLPASDqaqlksrqgvRTVGFSEIDVVDpESGRSVERDgeTVGEIVLRGSSIML 401
Cdd:cd17651 285 NHYGPTETH--VVTALSLPGdpaaWPAPPPIG----------RPIDNTRVYVLD-AALRPVPPG--VPGELYIGGAGLAR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 402 GYLKNPIGTQNSFKNGWFF-------TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARP 474
Cdd:cd17651 350 GYLNRPELTAERFVPDPFVpgarmyrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLARE 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15222924 475 DEFWGETPCAFVSLKPGltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17651 430 DRPGEKRLVAYVVGDPE--APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
41-479 |
1.39e-29 |
|
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: 121.70 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAIlnNI--NTRLDARTVSVLLRHCESKLLFV 118
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV--DVvrGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 119 DFFYSDLAveaiTMLlnppilvlianeeeeeggaevterskfcylysdlitrgnpdfkwirpgsewdpivvnYTSGTTSS 198
Cdd:cd17640 84 ENDSDDLA----TII---------------------------------------------------------YTSGTTGN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 199 PKGVVHCHRGiFVMTLDSLTDWAVPK-TPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVrklhapSIYHLIRD---HGVT 274
Cdd:cd17640 103 PKGVMLTHAN-LLHQIRSLSDIVPPQpGDRFLSILPIWHSYERSAEYFIFACGCSQAYT------SIRTLKDDlkrVKPH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 275 HMYGAPIVLQILSA---SQESDQP---------LKSPVNF---LTAGSSPPATVLLRAESLGFIVSHGYGLTETAGViVS 339
Cdd:cd17640 176 YIVSVPRLWESLYSgiqKQVSKSSpikqflflfFLSGGIFkfgISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPV-VS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 340 CawkpnwNRLPASdqaqlksrqgVR-TVGF----SEIDVVDPESGRSVERDGEtvGEIVLRGSSIMLGYLKNPIGTQNSF 414
Cdd:cd17640 255 A------RRLKCN----------VRgSVGRplpgTEIKIVDPEGNVVLPPGEK--GIVWVRGPQVMKGYYKNPEATSKVL 316
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 415 -KNGWFFTGDLGVIHGDGYLEIKDRSKDVII-SGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWG 479
Cdd:cd17640 317 dSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG 383
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
182-543 |
4.85e-29 |
|
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: 121.51 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 182 SEwDPIVVNYTSGTTSSPKGVVHCHRGIFV---MTLDSLTDwaVPKTPVYLWTLPIfhanGW----TY-PWGIAAVGGTN 253
Cdd:cd05966 230 SE-DPLFILYTSGSTGKPKGVVHTTGGYLLyaaTTFKYVFD--YHPDDIYWCTADI----GWitghSYiVYGPLANGATT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 254 VC---VRKLHAPSIY-HLIRDHGVTHMYGAPIVLQILSasQESDQPLKS--------------PVNfltagssPPATVLL 315
Cdd:cd05966 303 VMfegTPTYPDPGRYwDIVEKHKVTIFYTAPTAIRALM--KFGDEWVKKhdlsslrvlgsvgePIN-------PEAWMWY 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 316 RaESLGF----IVShGYGLTETAGVIVSCawkpnwnrLPASdqAQLKSrqGVRTVGFS--EIDVVDPESGrsvERDGETV 389
Cdd:cd05966 374 Y-EVIGKercpIVD-TWWQTETGGIMITP--------LPGA--TPLKP--GSATRPFFgiEPAILDEEGN---EVEGEVE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 390 GEIVLRGS--SIMLGYLKNP---IGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPA 464
Cdd:cd05966 437 GYLVIKRPwpGMARTIYGDHeryEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPA 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 465 VNEAAVVARPDEFWGETPCAFVSLKPGltRKPTD---KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIA 541
Cdd:cd05966 517 VAEAAVVGRPHDIKGEAIYAFVTLKDG--EEPSDelrKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIA 594
|
..
gi 15222924 542 KN 543
Cdd:cd05966 595 AG 596
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
37-486 |
6.12e-29 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 119.59 E-value: 6.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 37 NSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCesKLL 116
Cdd:PRK09029 25 NDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSL--TLD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 117 FVDFFYSDLAVEAITMLLNPPIlvlianeeeeeggaevterskfcylysdlitRGNPDFKW--IRPGSewdpivVNYTSG 194
Cdd:PRK09029 103 FALVLEGENTFSALTSLHLQLV-------------------------------EGAHAVAWqpQRLAT------MTLTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 195 TTSSPKGVVHCHR-------GIF-VMTLDSLTDWavpktpvyLWTLPIFHANGWTYPWGIAAVGGTnvcvrkLHAPSIYH 266
Cdd:PRK09029 146 STGLPKAAVHTAQahlasaeGVLsLMPFTAQDSW--------LLSLPLFHVSGQGIVWRWLYAGAT------LVVRDKQP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 267 LIRD-HGVTHMYGAPIVLQILSASQESDQPLKspvNFLTAGSSPPATVLLRAESLGfIVSH-GYGLTETAGVIvsCAwkp 344
Cdd:PRK09029 212 LEQAlAGCTHASLVPTQLWRLLDNRSEPLSLK---AVLLGGAAIPVELTEQAEQQG-IRCWcGYGLTEMASTV--CA--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 345 nwnrlpasdqaqlKSRQGVRTVGFseidvvdPESGRSVERDGetvGEIVLRGSSIMLGYLKNpiGTQNSFKN--GWFFTG 422
Cdd:PRK09029 283 -------------KRADGLAGVGS-------PLPGREVKLVD---GEIWLRGASLALGYWRQ--GQLVPLVNdeGWFATR 337
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 423 DLGVIHGdGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFV 486
Cdd:PRK09029 338 DRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV 400
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
185-532 |
1.02e-28 |
|
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: 120.04 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAV-PKTPVYLWtLPIFH----ANGWTYPWgiaAVGGTNVcvrkL 259
Cdd:cd05931 150 DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLdPGDVVVSW-LPLYHdmglIGGLLTPL---YSGGPSV----L 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 260 HAPSIY--------HLIRDHGVTHMyGAP-----IVLQILSASQESDQPLkSPVNFLTAGSSP--PATVL---------- 314
Cdd:cd05931 222 MSPAAFlrrplrwlRLISRYRATIS-AAPnfaydLCVRRVRDEDLEGLDL-SSWRVALNGAEPvrPATLRrfaeafapfg 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 315 LRAESlgfiVSHGYGLTEtAGVIVSCAWKPNWNRLPASDQAQLK---------SRQGVRTVG------FSEIDVVDPESG 379
Cdd:cd05931 300 FRPEA----FRPSYGLAE-ATLFVSGGPPGTGPVVLRVDRDALAgravavaadDPAARELVScgrplpDQEVRIVDPETG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 380 RSVErDGEtVGEIVLRGSSIMLGYLKNPIGTQNSFK-------NGWFFTGDLGVIHgDGYLEIKDRSKDVIISGGENVSS 452
Cdd:cd05931 375 RELP-DGE-VGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYP 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 453 VEVEA-VLYTNPAVNEAAVVA--RPDEfwGETPCAFVSLKPGLTRKPTDKEIIEYCKYKMPRY--MAPKTVSFLE--ELP 525
Cdd:cd05931 452 QDIEAtAEEAHPALRPGCVAAfsVPDD--GEERLVVVAEVERGADPADLAAIAAAIRAAVAREhgVAPADVVLVRpgSIP 529
|
....*..
gi 15222924 526 KTSTGKI 532
Cdd:cd05931 530 RTSSGKI 536
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
316-541 |
1.23e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 119.93 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 316 RAESL-GFIVSHGYGLTETAGVIVSCawkpnwnrlPASDQAQLKsrqgvrTVGF----SEIDVVDPESgrsVERDGETVG 390
Cdd:PRK12492 352 RWEQLtGCTIVEGYGLTETSPVASTN---------PYGELARLG------TVGIpvpgTALKVIDDDG---NELPLGERG 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 391 EIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAA 469
Cdd:PRK12492 414 ELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCA 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222924 470 VVARPDEFWGETPCAF-VSLKPGLTRkptdKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIA 541
Cdd:PRK12492 494 AIGVPDERSGEAVKLFvVARDPGLSV----EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
179-540 |
1.96e-28 |
|
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: 118.92 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 179 RPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDW-AVPKTPVYLWtLPIFHANGWTYpWGIAAV--GGTNVc 255
Cdd:cd05906 162 PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNgLTPQDVFLNW-VPLDHVGGLVE-LHLRAVylGCQQV- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 256 vrklHAPSIY---------HLIRDHGVTHMYgAP-----IVLQILSASQESDQPLKSPVNFLTAG---SSPPATVLLRA- 317
Cdd:cd05906 239 ----HVPTEEiladplrwlDLIDRYRVTITW-APnfafaLLNDLLEEIEDGTWDLSSLRYLVNAGeavVAKTIRRLLRLl 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 318 ESLG---FIVSHGYGLTET-AGVIvscawkpnWNRLPASDqaqlKSRQGVRTV-------GFsEIDVVDPEsGRSVERdg 386
Cdd:cd05906 314 EPYGlppDAIRPAFGMTETcSGVI--------YSRSFPTY----DHSQALEFVslgrpipGV-SMRIVDDE-GQLLPE-- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 387 ETVGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHgDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAV 465
Cdd:cd05906 378 GEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGV 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 466 NE---AAVVARPDEfwGETPCAFVSLKPGLTRKPTDKEIIEYCKYKMPRYM--APKTVSFL--EELPKTSTGKIIKSLLK 538
Cdd:cd05906 457 EPsftAAFAVRDPG--AETEELAIFFVPEYDLQDALSETLRAIRSVVSREVgvSPAYLIPLpkEEIPKTSLGKIQRSKLK 534
|
..
gi 15222924 539 EI 540
Cdd:cd05906 535 AA 536
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
185-544 |
8.47e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 118.49 E-value: 8.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTDWA-VPKTPVYLWTLPIFHANGWTYP-WGIAAVGGTNVCV-RKLHA 261
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNI-LSNIEQISDVFnLRNDDVILSSLPFFHSFGLTVTlWLPLLEGIKVVYHpDPTDA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 262 PSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSS--PPATVLLRAESLGFIVSHGYGLTETAGVI-V 338
Cdd:PRK08633 862 LGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEklKPEVADAFEEKFGIRILEGYGATETSPVAsV 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 339 SCawkPNwnRLPASDQAQLKSRQGvrTVGF----SEIDVVDPESGRSVErDGETvGEIVLRGSSIMLGYLKNPIGT---- 410
Cdd:PRK08633 942 NL---PD--VLAADFKRQTGSKEG--SVGMplpgVAVRIVDPETFEELP-PGED-GLILIGGPQVMKGYLGDPEKTaevi 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 411 QNSFKNGWFFTGDLGVIHGDGYLEIKDR----SKdviiSGGENVSSVEVE----AVLYTNPAVneAAVVARPDEFWGETP 482
Cdd:PRK08633 1013 KDIDGIGWYVTGDKGHLDEDGFLTITDRysrfAK----IGGEMVPLGAVEeelaKALGGEEVV--FAVTAVPDEKKGEKL 1086
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222924 483 CafVSLKPGLTRKPTDKEIIEYCkyKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAKNM 544
Cdd:PRK08633 1087 V--VLHTCGAEDVEELKRAIKES--GLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALAL 1144
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
41-541 |
1.92e-27 |
|
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: 114.97 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAIlnnintrldartvsvllrhceskllfvdf 120
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 121 fysdlaVEAITMLLNPPILvlianeeeeeggAEVTERSKFCYLYSDLITRGNpdfkwirpgsewDPIVVNYTSGTTSSPK 200
Cdd:cd05974 52 ------VIPATTLLTPDDL------------RDRVDRGGAVYAAVDENTHAD------------DPMLLYFTSGTTSKPK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 201 GVVHCHRGIFVMTLDSLTdWAVPKTPVYLWTL--PIFHANGWT---YPWGI-AAVGGTNVCvrKLHAPSIYHLIRDHGVT 274
Cdd:cd05974 102 LVEHTHRSYPVGHLSTMY-WIGLKPGDVHWNIssPGWAKHAWScffAPWNAgATVFLFNYA--RFDAKRVLAALVRYGVT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 275 HMYGAPIVLQILSasQESDQPLKSPVNFLTAGSSP--PATVLLRAESLGFIVSHGYGLTETAGVIVScawKPNWNRLPAS 352
Cdd:cd05974 179 TLCAPPTVWRMLI--QQDLASFDVKLREVVGAGEPlnPEVIEQVRRAWGLTIRDGYGQTETTALVGN---SPGQPVKAGS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 353 dqaqlksrQGVRTVGFsEIDVVDPESGRSVErdgetvGEIVL-----RGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVI 427
Cdd:cd05974 254 --------MGRPLPGY-RVALLDPDGAPATE------GEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 428 HGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTRKP-TDKEIIEYCK 506
Cdd:cd05974 319 DEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPeTALEIFRFSR 398
|
490 500 510
....*....|....*....|....*....|....*
gi 15222924 507 YKMPRYMAPKTVSFLeELPKTSTGKIIKSLLKEIA 541
Cdd:cd05974 399 ERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRRE 432
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
182-544 |
2.95e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.88 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 182 SEWDPIVVNYTSGTTSSPKGVVHCHRGiFVMTLD-SLTDWAVPKTPVYLWTLPIFHANgwtYPWG-IAA--VGGTNVCVR 257
Cdd:PRK07638 141 VQNAPFYMGFTSGSTGKPKAFLRAQQS-WLHSFDcNVHDFHMKREDSVLIAGTLVHSL---FLYGaISTlyVGQTVHLMR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 258 KLHAPSIYHLIRDHGVTHMYGAPIVLQILSasqESDQPLKSPVNFLTAGSSPPA-------TVLLRAESLGFivshgYGL 330
Cdd:PRK07638 217 KFIPNQVLDKLETENISVMYTVPTMLESLY---KENRVIENKMKIISSGAKWEAeakekikNIFPYAKLYEF-----YGA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 331 TE----TAGVIVSCAWKPNwnrlpasdqaqlksrqgvrTVG--FSEIDV-VDPESGRSVERdGETvGEIVLRGSSIMLGY 403
Cdd:PRK07638 289 SElsfvTALVDEESERRPN-------------------SVGrpFHNVQVrICNEAGEEVQK-GEI-GTVYVKSPQFFMGY 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 404 LKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPC 483
Cdd:PRK07638 348 IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPV 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222924 484 AFVSlkpgltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAKNM 544
Cdd:PRK07638 428 AIIK------GSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQ 482
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
185-532 |
4.86e-27 |
|
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: 113.94 E-value: 4.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGifVMTLDSLTDWAVPKTPVYLWTLpiFHANGWTYP----WGIAAVGGTNVCVRKLH 260
Cdd:cd17643 94 DLAYVIYTSGSTGRPKGVVVSHAN--VLALFAATQRWFGFNEDDVWTL--FHSYAFDFSvweiWGALLHGGRLVVVPYEV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 261 APS---IYHLIRDHGVThmygapiVL-QILSASQESDQPLKSPvnfltaGSSPPAT--VLLRAESL------GFIVSHG- 327
Cdd:cd17643 170 ARSpedFARLLRDEGVT-------VLnQTPSAFYQLVEAADRD------GRDPLALryVIFGGEALeaamlrPWAGRFGl 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 --------YGLTETAgVIVScawkpnWNRLPASD-QAQLKSRQGVRTVGFSeIDVVDpESGRSVERDGetVGEIVLRGSS 398
Cdd:cd17643 237 drpqlvnmYGITETT-VHVT------FRPLDAADlPAAAASPIGRPLPGLR-VYVLD-ADGRPVPPGV--VGELYVSGAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 399 IMLGYLKNPIGTQNSFKNGWFF--------TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAV 470
Cdd:cd17643 306 VARGYLGRPELTAERFVANPFGgpgsrmyrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAV 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222924 471 VARPDEFWGETPCAFVSLKPGLTRKPTdkEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17643 386 IVREDEPGDTRLVAYVVADDGAAADIA--ELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
41-471 |
1.63e-26 |
|
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: 112.95 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFV-- 118
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 119 ----DFFYSDLAVEAITMLLNPPilvlianeeeeeggaevtERSKFCYLYSDLITRGNPDFKWIRPGSEWDPIVVnYTSG 194
Cdd:cd05932 87 lddwKAMAPGVPEGLISISLPPP------------------SAANCQYQWDDLIAQHPPLEERPTRFPEQLATLI-YTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 195 TTSSPKGVVHCHrGIFVMTLDSL-TDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVcvrkLHAPSIYHLIRD--- 270
Cdd:cd05932 148 TTGQPKGVMLTF-GSFAWAAQAGiEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLV----AFAESLDTFVEDvqr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 271 HGVTHMYGAPI--------VLQILSAsQESDQPLKSPV------------------NFLTAGSSP-PATVLLRAESLGFI 323
Cdd:cd05932 223 ARPTLFFSVPRlwtkfqqgVQDKIPQ-QKLNLLLKIPVvnslvkrkvlkglgldqcRLAGCGSAPvPPALLEWYRSLGLN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 324 VSHGYGLTETAGVIVSCawKPnwnrlpasdqaqlkSRQGVRTVGfseidvvdpESGRSVE-RDGETvGEIVLRGSSIMLG 402
Cdd:cd05932 302 ILEAYGMTENFAYSHLN--YP--------------GRDKIGTVG---------NAGPGVEvRISED-GEILVRSPALMMG 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222924 403 YLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVI-ISGGENVSSVEVEAVLYTNPAVNEAAVV 471
Cdd:cd05932 356 YYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
5-539 |
1.69e-26 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 113.43 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 5 KPSAANSLPLTLlgflERAATVYGDCTSIVYGNsTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFS 84
Cdd:PRK08279 32 TPDSKRSLGDVF----EEAAARHPDRPALLFED-QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 85 VPMSGAILNNINTRLdartVSVLLRHC----ESKLLFVDffySDL--AVEAITMLLNPPILVLIANEEEEEGGAEVTERS 158
Cdd:PRK08279 107 LAKLGAVVALLNTQQ----RGAVLAHSlnlvDAKHLIVG---EELveAFEEARADLARPPRLWVAGGDTLDDPEGYEDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 159 KfcylYSDLITRGNPDfkwIRPGSEW-DPIVVNYTSGTTSSPKGVVHCHR------GIFVMTLDsltdwAVPKTPVYLwT 231
Cdd:PRK08279 180 A----AAAGAPTTNPA---SRSGVTAkDTAFYIYTSGTTGLPKAAVMSHMrwlkamGGFGGLLR-----LTPDDVLYC-C 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 232 LPIFHANGWTYPWGIA-AVGGTNVCVRKLHAPSIYHLIRDHGVTH-MYGAPIVLQILSA---SQESDQPLKspvnfLTAG 306
Cdd:PRK08279 247 LPLYHNTGGTVAWSSVlAAGATLALRRKFSASRFWDDVRRYRATAfQYIGELCRYLLNQppkPTDRDHRLR-----LMIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 307 SSppatvlLRAESLG-----FIVSH---GYGLTE--TA-----GVIVSCAWKPNWNRLPAsdqaqlksrqgvRTVGFsei 371
Cdd:PRK08279 322 NG------LRPDIWDefqqrFGIPRileFYAASEgnVGfinvfNFDGTVGRVPLWLAHPY------------AIVKY--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 372 dvvDPESGRSVeRD-------------GETVGEIVLRGSsiMLGYLkNPIGT-----QNSFKNG--WFFTGDLGVIHGDG 431
Cdd:PRK08279 381 ---DVDTGEPV-RDadgrcikvkpgevGLLIGRITDRGP--FDGYT-DPEASekkilRDVFKKGdaWFNTGDLMRDDGFG 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 432 YLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAV--VARPDEfwgETPCAFVSLKPGLTRKPTDKEIIEYCKYKM 509
Cdd:PRK08279 454 HAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVPGT---DGRAGMAAIVLADGAEFDLAALAAHLYERL 530
|
570 580 590
....*....|....*....|....*....|
gi 15222924 510 PRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK08279 531 PAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
454-531 |
4.27e-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: 101.47 E-value: 4.27e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222924 454 EVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGK 531
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG--VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
185-542 |
5.34e-26 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 111.89 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTDWAV------PKTPVYLWTLPIFH-----ANGWTYpwgiAAVGGTN 253
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAMLTHRNL-VANMQQAHQWLAgtgkleEGCEVVITALPLYHifaltANGLVF----MKIGGCN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 254 VCVRK-LHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNF-LTAGSSPPATVLLRAESL-GFIVSHGYGL 330
Cdd:PRK08751 284 HLISNpRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMtLGGGMAVQRSVAERWKQVtGLTLVEAYGL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 331 TETAgvivscawkpnwnrlPAS--DQAQLKSRQGVRTVGFSEIDVVDPESGRSVERDGEtVGEIVLRGSSIMLGYLKNPI 408
Cdd:PRK08751 364 TETS---------------PAAciNPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGE-IGELCIKGPQVMKGYWKRPE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 409 GTQNSFK-NGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGE-TPCAFV 486
Cdd:PRK08751 428 ETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEiVKVVIV 507
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15222924 487 SLKPGLTRkptdKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAK 542
Cdd:PRK08751 508 KKDPALTA----EDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
13-537 |
5.55e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 111.63 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 13 PLTLLGFlerAATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAIL 92
Cdd:PRK13383 37 PYTLLAV---TAARWPGRTAIIDDDGAL-SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 93 NNINTRLDARTVSVLLR-HCESKLLFVDFFYSDLAVEAITMLLNPPilvlianeeeeeggAEVTERSkfcylysdliTRG 171
Cdd:PRK13383 113 VPISTEFRSDALAAALRaHHISTVVADNEFAERIAGADDAVAVIDP--------------ATAGAEE----------SGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 172 NPdfKWIRPGSewdpiVVNYTSGTTSSPKGV-----VHCHRGIFVMTLDSLTDWAVPKTPVylwTLPIFHANGWTYPWGI 246
Cdd:PRK13383 169 RP--AVAAPGR-----IVLLTSGTTGKPKGVprapqLRSAVGVWVTILDRTRLRTGSRISV---AMPMFHGLGLGMLMLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 247 AAVGGTNVCVRKLHAPSIYHLIRDHGVTHMYGAPIVL-QILSASQE--SDQPLKSPVNFLTAGSSPPATVLLR-AESLGF 322
Cdd:PRK13383 239 IALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLaRILELPPRvrARNPLPQLRVVMSSGDRLDPTLGQRfMDTYGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 323 IVSHGYGLTETA-GVIVScawkpnwnrlPAsdqaqlKSRQGVRTVGfseidvvDPESG---RSVERDGETVG-----EIV 393
Cdd:PRK13383 319 ILYNGYGSTEVGiGALAT----------PA------DLRDAPETVG-------KPVAGcpvRILDRNNRPVGprvtgRIF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 394 LRGSSIMLGYLKnpiGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVAR 473
Cdd:PRK13383 376 VGGELAGTRYTD---GGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGV 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 474 PDEFWGETPCAFVSLKPGLTRKPTdkEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:PRK13383 453 PDERFGHRLAAFVVLHPGSGVDAA--QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
29-532 |
6.23e-26 |
|
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: 110.82 E-value: 6.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 29 DCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLL 108
Cdd:cd12114 2 DATAVICGDGTL-TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 109 RHCESKLLFVDFFYSDLAVEAITmllnPPILVLIANEEEEEGGAEVTErskfcylysdlitrgnPDfkwirpgsewDPIV 188
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFD----VLILDLDALAAPAPPPPVDVA----------------PD----------DLAY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 189 VNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAV-PKTPVY--------LWTLPIFhangwtypwGIAAVGGTNVCVRKL 259
Cdd:cd12114 131 VIFTSGSTGTPKGVMISHRAALNTILDINRRFAVgPDDRVLalsslsfdLSVYDIF---------GALSAGATLVLPDEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 260 HAPSIYH---LIRDHGVTHMYGAPIVLQILSASQESDQPLK-SPVNFLTAGSSPPATVLLRAESL---GFIVSHGyGLTE 332
Cdd:cd12114 202 RRRDPAHwaeLIERHGVTLWNSVPALLEMLLDVLEAAQALLpSLRLVLLSGDWIPLDLPARLRALapdARLISLG-GATE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 333 TAgvIVSCAWkpnwnrlpasdqaqlksrqgvrtvgfsEIDVVDPE-------------SGRSVERDGE-----TVGEIVL 394
Cdd:cd12114 281 AS--IWSIYH---------------------------PIDEVPPDwrsipygrplanqRYRVLDPRGRdcpdwVPGELWI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 395 RGSSIMLGYLKNPIGTQNSFKN-----GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAA 469
Cdd:cd12114 332 GGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAV 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222924 470 VVARPDEFwGETPCAFVSLKPGLTRkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd12114 412 VVVLGDPG-GKRLAAFVVPDNDGTP-IAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
167-486 |
1.84e-25 |
|
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: 109.61 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 167 LITRGNPDfkwirpgsewDPIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTDWaVPKTP----VYLWTLPIFHangwty 242
Cdd:cd17639 81 IFTDGKPD----------DLACIMYTSGSTGNPKGVMLTHGNL-VAGIAGLGDR-VPELLgpddRYLAYLPLAH------ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 243 pwgIAAVGGTNVC-----------VRKLHA---------------------PSIYHLIR------------------DHG 272
Cdd:cd17639 143 ---IFELAAENVClyrggtigygsPRTLTDkskrgckgdltefkptlmvgvPAIWDTIRkgvlaklnpmgglkrtlfWTA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 273 -------VTHMYGAP----IVLQILSASqesdqpLKSPVNFLTAGSSPpatvlLRAESLGFI------VSHGYGLTETag 335
Cdd:cd17639 220 yqsklkaLKEGPGTPlldeLVFKKVRAA------LGGRLRYMLSGGAP-----LSADTQEFLnivlcpVIQGYGLTET-- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 336 viVSCAWKPNWNRLpasdqaqLKSRQGvRTVGFSEIDVVDPESGRSVERDGETVGEIVLRGSSIMLGYLKNPIGTQNSFK 415
Cdd:cd17639 287 --CAGGTVQDPGDL-------ETGRVG-PPLPCCEIKLVDWEEGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFD 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222924 416 -NGWFFTGDLGVIHGDGYLEIKDRSKD-VIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWgetPCAFV 486
Cdd:cd17639 357 gDGWFHTGDIGEFHPDGTLKIIDRKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIV 426
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
301-541 |
3.09e-25 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 108.54 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 301 NFLTA--GSSPPATVLL-RAESLGFIVSHGYGLTETAGVIvsCAWKPnwnrlpasdQAQLksrQGVRTVG----FSEIDV 373
Cdd:PRK07445 231 QFRTIllGGAPAWPSLLeQARQLQLRLAPTYGMTETASQI--ATLKP---------DDFL---AGNNSSGqvlpHAQITI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 374 VDPesgrsverdgeTVGEIVLRGSSIMLGYLKNPIGTQNSFkngwfFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSV 453
Cdd:PRK07445 297 PAN-----------QTGNITIQAQSLALGYYPQILDSQGIF-----ETDDLGYLDAQGYLHILGRNSQKIITGGENVYPA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 454 EVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGltrkPTDKEIIEYC------KYKMPRYMAPktvsfLEELPKT 527
Cdd:PRK07445 361 EVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP----SISLEELKTAikdqlsPFKQPKHWIP-----VPQLPRN 431
|
250
....*....|....
gi 15222924 528 STGKIIKSLLKEIA 541
Cdd:PRK07445 432 PQGKINRQQLQQIA 445
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
42-470 |
3.92e-25 |
|
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: 107.74 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASAL-SSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDF 120
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 121 FYSDLAVEAITMLLNPPILVLIANEeeeeggaevterskfcylysDLITRGNPDfkwIRPGSEwDPIVVNYTSGTTSSPK 200
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALD--------------------DAPAPPPPD---APSGPD-DLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 201 GVVHCHRGIfVMTLDSLTD-WAVPKTPVYLWTLPI-FHANGWTYpWGIAAVGGTNVCV----RKLHAPSIYHLIRDHGVT 274
Cdd:TIGR01733 137 GVVVTHRSL-VNLLAWLARrYGLDPDDRVLQFASLsFDASVEEI-FGALLAGATLVVPpedeERDDAALLAALIAEHPVT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 275 HMYGAPIVLQILSASQESDQP-LKspvNFLTAGSSPPATVL--LRAESLGFIVSHGYGLTETAgviVSCAWKPnwnrlPA 351
Cdd:TIGR01733 215 VLNLTPSLLALLAAALPPALAsLR---LVILGGEALTPALVdrWRARGPGARLINLYGPTETT---VWSTATL-----VD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 352 SDQAQLKSRQGV-RTVGFSEIDVVDPEsGRSVErDGEtVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWF---------FT 421
Cdd:TIGR01733 284 PDDAPRESPVPIgRPLANTRLYVLDDD-LRPVP-VGV-VGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlyRT 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 422 GDLGVIHGDGYLEIKDRSKD-VIISG-----GenvssvEVEAVLYTNPAVNEAAV 470
Cdd:TIGR01733 361 GDLVRYLPDGNLEFLGRIDDqVKIRGyrielG------EIEAALLRHPGVREAVV 409
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
12-543 |
5.82e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 108.54 E-value: 5.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 12 LPLTLLgfLERAATvyGDCTSIVYGNSTvYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFS------V 85
Cdd:PRK10946 25 LPLTDI--LTRHAA--SDAIAVICGERQ-FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFAllklgvA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 86 PMSgAILNNINTRLDArtvsvLLRHCESKLLFVD----FFYSDLAVEAITMLLNPPILVLIANEEeeeggaevTERSkfc 161
Cdd:PRK10946 100 PVN-ALFSHQRSELNA-----YASQIEPALLIADrqhaLFSDDDFLNTLVAEHSSLRVVLLLNDD--------GEHS--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 162 ylYSDLITRGNPDFKWI-RPGSEwdpivVNY---TSGTTSSPKGVVHCH--------RGIFVMTLDSLTdwavpktpVYL 229
Cdd:PRK10946 163 --LDDAINHPAEDFTATpSPADE-----VAFfqlSGGSTGTPKLIPRTHndyyysvrRSVEICGFTPQT--------RYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 230 WTLPIFHangwTYP------WGIAAVGGTNVCVRKLHAPSIYHLIRDHGVTHmygAPIV-------LQILSASQESDQpL 296
Cdd:PRK10946 228 CALPAAH----NYPmsspgaLGVFLAGGTVVLAPDPSATLCFPLIEKHQVNV---TALVppavslwLQAIAEGGSRAQ-L 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 297 KSPVNFLTAGSSPPATVLLR-AESLGFIVSHGYGLTEtaGVIvscawkpNWNRLPASDQaQLKSRQGVRTVGFSEIDVVD 375
Cdd:PRK10946 300 ASLKLLQVGGARLSETLARRiPAELGCQLQQVFGMAE--GLV-------NYTRLDDSDE-RIFTTQGRPMSPDDEVWVAD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 376 pESGRSVERdGETvGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVE 454
Cdd:PRK10946 370 -ADGNPLPQ-GEV-GRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 455 VEAVLYTNPAVNEAAVVARPDEFWGETPCAFV----SLKPGLTRKPTDKEIIeyCKYKMprymaPKTVSFLEELPKTSTG 530
Cdd:PRK10946 447 IENLLLRHPAVIHAALVSMEDELMGEKSCAFLvvkePLKAVQLRRFLREQGI--AEFKL-----PDRVECVDSLPLTAVG 519
|
570
....*....|...
gi 15222924 531 KIIKSLLKEIAKN 543
Cdd:PRK10946 520 KVDKKQLRQWLAS 532
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
19-539 |
9.49e-24 |
|
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: 104.33 E-value: 9.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 19 FLERAATVyGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTR 98
Cdd:cd17655 3 FEEQAEKT-PDHTAVVFEDQTL-TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 99 LDARTVSVLLRHCESKLLfvdffysdLAVEAitmllnppilvLIANEEEEEGGAEVTERSKFCYLYSDLITRGNPDfkwi 178
Cdd:cd17655 81 YPEERIQYILEDSGADIL--------LTQSH-----------LQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSD---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 179 rpgsewDPIVVNYTSGTTSSPKGVVHCHRGifvmtLDSLTDWAV------PKTPVYLWTLPIFHANGWT-YPwgIAAVGG 251
Cdd:cd17655 138 ------DLAYVIYTSGSTGKPKGVMIEHRG-----VVNLVEWANkviyqgEHLRVALFASISFDASVTEiFA--SLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 252 TNVCVRK---LHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQ-PLKSpvnFLTAGSSPPATV---LLRAESLGFIV 324
Cdd:cd17655 205 TLYIVRKetvLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGlSLKH---LIVGGEALSTELakkIIELFGTNPTI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 325 SHGYGLTETagvIVSCAWkpnWNRLPASDQaQLKSRQGvRTVGFSEIDVVDpESGRSVErDGEtVGEIVLRGSSIMLGYL 404
Cdd:cd17655 282 TNAYGPTET---TVDASI---YQYEPETDQ-QVSVPIG-KPLGNTRIYILD-QYGRPQP-VGV-AGELYIGGEGVARGYL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 405 KNPIGTQNSFKNGWFF-------TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEF 477
Cdd:cd17655 351 NRPELTAEKFVDDPFVpgermyrTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQ 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222924 478 WGETPCAFVSLKPGLTRkptdKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd17655 431 GQNYLCAYIVSEKELPV----AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
179-532 |
6.21e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 100.12 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 179 RPGSEWDPIV--VNYTSGTTSSPKGVVhchrgifvMTLDSLTDWAvPKTPVYL-----W--TLPIFHangwtypwgiaaV 249
Cdd:PRK07824 28 RVGEPIDDDValVVATSGTTGTPKGAM--------LTAAALTASA-DATHDRLggpgqWllALPAHH------------I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 250 GGTNVCVRKLHA---PSIYHLIRDHGVTHM------------YGAPIVLQILSA--SQESDQPLKSPVNFLTAGSSPPAT 312
Cdd:PRK07824 87 AGLQVLVRSVIAgsePVELDVSAGFDPTALpravaelgggrrYTSLVPMQLAKAldDPAATAALAELDAVLVGGGPAPAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 313 VLLRAESLGFIVSHGYGLTETAGVIVscawkpnWNRLPASdqaqlksrqGVRtvgfseIDVVDpesgrsverdgetvGEI 392
Cdd:PRK07824 167 VLDAAAAAGINVVRTYGMSETSGGCV-------YDGVPLD---------GVR------VRVED--------------GRI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 393 VLRGSSIMLGYlKNPIGTQNSFKNGWFFTGDLGVIHgDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVA 472
Cdd:PRK07824 211 ALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFG 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 473 RPDEFWGETPCAFVSLKPGLTrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:PRK07824 289 LPDDRLGQRVVAAVVGDGGPA--PTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKV 346
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
185-532 |
1.07e-21 |
|
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: 97.71 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAV-PKTPVYLWTLPIFHANGWTYpWGIAAVGGTNVCV---RKLH 260
Cdd:cd17652 94 NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVgPGSRVLQFASPSFDASVWEL-LMALLAGATLVLApaeELLP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 261 APSIYHLIRDHGVTHMYGAPIVLQILSASQesdqpLKSPVNFLTAGSSPPATvLLRAESLGFIVSHGYGLTETAgvIVSC 340
Cdd:cd17652 173 GEPLADLLREHRITHVTLPPAALAALPPDD-----LPDLRTLVVAGEACPAE-LVDRWAPGRRMINAYGPTETT--VCAT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 341 AWKPnwnrLPASDQAQLKsrqgvRTVGFSEIDVVDPESgRSVErDGEtVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWF- 419
Cdd:cd17652 245 MAGP----LPGGGVPPIG-----RPVPGTRVYVLDARL-RPVP-PGV-PGELYIAGAGLARGYLNRPGLTAERFVADPFg 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 420 -------FTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGL 492
Cdd:cd17652 313 apgsrmyRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGA 392
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15222924 493 TrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17652 393 A--PTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
42-470 |
1.16e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 98.73 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCEskllfVDF- 120
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAE-----IDFv 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 121 FYSDLAVEAitmLLNP--------PILVLIANeeeeeggaeVTERSKF--------CYLYSDLITRGNPDFKWIRPGSEW 184
Cdd:PLN02430 153 FVQDKKIKE---LLEPdcksakrlKAIVSFTS---------VTEEESDkasqigvkTYSWIDFLHMGKENPSETNPPKPL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRG--IFVMTLDSLTDWAVPKTP---VYLWTLPIFH----ANGWTYPWGIAAVGGTNVC 255
Cdd:PLN02430 221 DICTIMYTSGTSGDPKGVVLTHEAvaTFVRGVDLFMEQFEDKMThddVYLSFLPLAHildrMIEEYFFRKGASVGYYHGD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 256 VRKLH-------------APSIYHLIRD-----------------------------HGVTHMYGAPivLQILSASQESD 293
Cdd:PLN02430 301 LNALRddlmelkptllagVPRVFERIHEgiqkalqelnprrrlifnalykyklawmnRGYSHKKASP--MADFLAFRKVK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 294 QPLKSPVNFLTAGSSPPATVL---LRAESLGFIVsHGYGLTETAGVIVSCawkpnwnrLPasDQAQLKSRQGVRTVgFSE 370
Cdd:PLN02430 379 AKLGGRLRLLISGGAPLSTEIeefLRVTSCAFVV-QGYGLTETLGPTTLG--------FP--DEMCMLGTVGAPAV-YNE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 371 IDVVD-PESGRSVERDgETVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVI-ISGGE 448
Cdd:PLN02430 447 LRLEEvPEMGYDPLGE-PPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGE 525
|
490 500
....*....|....*....|..
gi 15222924 449 NVSSVEVEAVLYTNPAVNEAAV 470
Cdd:PLN02430 526 YVALEYLENVYGQNPIVEDIWV 547
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
35-507 |
1.98e-21 |
|
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: 97.88 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 35 YGNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESK 114
Cdd:cd17641 6 FGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 115 LLFVDffySDLAVEAITMLLN--PPILVLI--------------ANEEEEEGGAEVTERSKFCYLYSDLITRGNPDfkwi 178
Cdd:cd17641 86 VVIAE---DEEQVDKLLEIADriPSVRYVIycdprgmrkyddprLISFEDVVALGRALDRRDPGLYEREVAAGKGE---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 179 rpgsewDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTdwAVPKTPV--YLWTLPIfhangwtyPW--------GIAA 248
Cdd:cd17641 159 ------DVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPLGPGdeYVSVLPL--------PWigeqmysvGQAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 249 VGG-----------------------------------TNVCVRKLHAPSIYHLIRDHGV--------THMYGAPIVLQI 285
Cdd:cd17641 223 VCGfivnfpeepetmmedlreigptfvllpprvwegiaADVRARMMDATPFKRFMFELGMklglraldRGKRGRPVSLWL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 286 LSASQESDQ----PLKSPVNFL------TAGSSPPATVLLRAESLGFIVSHGYGLTETAGVIVscawkpnwnrLPASDQA 355
Cdd:cd17641 303 RLASWLADAllfrPLRDRLGFSrlrsaaTGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYT----------VHRDGDV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 356 QLKsrqgvrTVGFseidvvdPESGRSVERDgeTVGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLE 434
Cdd:cd17641 373 DPD------TVGV-------PFPGTEVRID--EVGEILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 435 IKDRSKDV-IISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGetpcAFVSLKPGLTRKPTDKEIIEYCKY 507
Cdd:cd17641 438 VIDRAKDVgTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLT----AFICIDYAIVGKWAEQRGIAFTTY 507
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
42-532 |
3.61e-21 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 96.22 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLfvdff 121
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 122 ysdlaveaitmllnppilvlianeeeeeggaevterskfcylysdlITRGNPDfkwirpgsewDPIVVNYTSGTTSSPKG 201
Cdd:cd17653 99 ----------------------------------------------LTTDSPD----------DLAYIIFTSGSTGIPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 202 VVHCHRGI--FVMTLDSLTDwAVPKTPVYLWTLPIFHANGWTYpWGIAAVGGTnVCVRKlHAPSIYHLIRDHGVTHMygA 279
Cdd:cd17653 123 VMVPHRGVlnYVSQPPARLD-VGPGSRVAQVLSIAFDACIGEI-FSTLCNGGT-LVLAD-PSDPFAHVARTVDALMS--T 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 280 PIVLQILSAsqeSDQP-LKSpvnFLTAGSSPPAtVLLRAESLGFIVSHGYGLTETAgviVSCAWKpnwnRLPASDQAQLK 358
Cdd:cd17653 197 PSILSTLSP---QDFPnLKT---IFLGGEAVPP-SLLDRWSPGRRLYNAYGPTECT---ISSTMT----ELLPGQPVTIG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 359 srqgvRTVGFSEIDVVDPESGRSVErdgETVGEIVLRGSSIMLGYLKNPIGTQNSFK-----NGW--FFTGDLGVIHGDG 431
Cdd:cd17653 263 -----KPIPNSTCYILDADLQPVPE---GVVGEICISGVQVARGYLGNPALTASKFVpdpfwPGSrmYRTGDYGRWTEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 432 YLEIKDRSKDVIISGGENVSSVEVEAVLYTN-PAVNEAAVVARpdefwGETPCAFVslkpglTRKPTDKEII-EYCKYKM 509
Cdd:cd17653 335 GLEFLGREDNQVKVRGFRINLEEIEEVVLQSqPEVTQAAAIVV-----NGRLVAFV------TPETVDVDGLrSELAKHL 403
|
490 500
....*....|....*....|...
gi 15222924 510 PRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17653 404 PSYAVPDRIIALDSFPLTANGKV 426
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
181-543 |
4.10e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 97.13 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 181 GSEwDPIVVNYTSGTTSSPKGVVHCHRGifVMTLDSLTDWAV----PkTPVYLWTLPIfhanGW----TY-PWGIAAVGG 251
Cdd:PRK00174 243 DAE-DPLFILYTSGSTGKPKGVLHTTGG--YLVYAAMTMKYVfdykD-GDVYWCTADV----GWvtghSYiVYGPLANGA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 252 TNVcvrkLH--APS------IYHLIRDHGVTHMYGAPIVlqILSASQESDQPLKS--------------PVNfltagssP 309
Cdd:PRK00174 315 TTL----MFegVPNypdpgrFWEVIDKHKVTIFYTAPTA--IRALMKEGDEHPKKydlsslrllgsvgePIN-------P 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 310 PA---------------------TvllraESLGFIVSHGYGLTETagvivscawKPNWNRLPASdqaqlksrqGVrtvgf 368
Cdd:PRK00174 382 EAwewyykvvggercpivdtwwqT-----ETGGIMITPLPGATPL---------KPGSATRPLP---------GI----- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 369 sEIDVVDpESGRSVErdGETVGEIVLRGS--SIMLGYLKNPigtqNSFKN-------GWFFTGDLGVIHGDGYLEIKDRS 439
Cdd:PRK00174 434 -QPAVVD-EEGNPLE--GGEGGNLVIKDPwpGMMRTIYGDH----ERFVKtyfstfkGMYFTGDGARRDEDGYYWITGRV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 440 KDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGltRKPTD---KEIIEYCKYKMPRYMAPK 516
Cdd:PRK00174 506 DDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGG--EEPSDelrKELRNWVRKEIGPIAKPD 583
|
410 420
....*....|....*....|....*..
gi 15222924 517 TVSFLEELPKTSTGKIIKSLLKEIAKN 543
Cdd:PRK00174 584 VIQFAPGLPKTRSGKIMRRILRKIAEG 610
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
41-470 |
5.79e-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: 96.13 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSD--VVSVLSANTPE--MYEL---QFS---VPMsgailnnINTrLDARTVSVLLRH 110
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPAPasFVGIYSINRPEwiISELacyAYSlvtVPL-------YDT-LGPEAIEYILNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 111 CESKLLFVDffySDLAVeaitmllnppilvlianeeeeeggaevterskfcYLYSDLITRGNPDFKWIRPGSEWDPIVVN 190
Cdd:cd05927 78 AEISIVFCD---AGVKV----------------------------------YSLEEFEKLGKKNKVPPPPPKPEDLATIC 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGI--FVMTLDSLTDWAVPKTP--VYLWTLPIFHANGWTYPWGIAAVGG--------------- 251
Cdd:cd05927 121 YTSGTTGNPKGVMLTHGNIvsNVAGVFKILEILNKINPtdVYISYLPLAHIFERVVEALFLYHGAkigfysgdirllldd 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 252 ------TNVCVrklhAPSIYHLIRDHGVTHMYGAPIVLQIL--------SASQESDQPLKSP-----------------V 300
Cdd:cd05927 201 ikalkpTVFPG----VPRVLNRIYDKIFNKVQAKGPLKRKLfnfalnykLAELRSGVVRASPfwdklvfnkikqalggnV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 301 NFLTAGSSP-PATVL--LRAeSLGFIVSHGYGLTETAGVIVScawkpnwnrlpasdqaqlkSRQGVRTVG-------FSE 370
Cdd:cd05927 277 RLMLTGSAPlSPEVLefLRV-ALGCPVLEGYGQTECTAGATL-------------------TLPGDTSVGhvggplpCAE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 371 IDVVD-PESGRSVERDGETvGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVI-ISGG 447
Cdd:cd05927 337 VKLVDvPEMNYDAKDPNPR-GEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQG 415
|
490 500
....*....|....*....|...
gi 15222924 448 ENVSSVEVEAVLYTNPAVNEAAV 470
Cdd:cd05927 416 EYVAPEKIENIYARSPFVAQIFV 438
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
189-532 |
8.89e-21 |
|
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: 95.13 E-value: 8.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 189 VNYTSGTTSSPKGVVHCHrgifvmtlDSLTDWAVPKTPVY--------LWTLPI-FHA--NGWTYPWgiaAVGGTnVCVR 257
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSH--------GPLAAHCQATAERYgltpgdreLQFASFnFDGahEQLLPPL---ICGAC-VVLR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 258 --KLHAPS--IYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPV--NFLTAGSSPPATVLLRAESLGFIVSHGYGLT 331
Cdd:cd17649 167 pdELWASAdeLAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSlrLYIFGGEALSPELLRRWLKAPVRLFNAYGPT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 332 ETagVIVSCAWKPN------WNRLPASdqaqlksrqgvRTVGFSEIDVVDpESGRSVErDGETvGEIVLRGSSIMLGYLK 405
Cdd:cd17649 247 EA--TVTPLVWKCEagaaraGASMPIG-----------RPLGGRSAYILD-ADLNPVP-VGVT-GELYIGGEGLARGYLG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 406 NPIGTQNSF------KNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEF 477
Cdd:cd17649 311 RPELTAERFvpdpfgAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 478 wGETPCAFVSLKPGLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17649 391 -GKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
185-537 |
3.08e-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: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGifvmtLDSLTDWAvpktpvylwtLPIFHANGWTypwgiAAVGGTNVCVrKLhapSI 264
Cdd:cd12115 106 DLAYVIYTSGSTGRPKGVAIEHRN-----AAAFLQWA----------AAAFSAEELA-----GVLASTSICF-DL---SV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 265 YHLIrdhgVTHMYGAPIVLqILSASQESDQPLKSPVNFLTAGSSPpATVLLRAESLGFIVShgygltetagvIVSCAWKP 344
Cdd:cd12115 162 FELF----GPLATGGKVVL-ADNVLALPDLPAAAEVTLINTVPSA-AAELLRHDALPASVR-----------VVNLAGEP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 345 NWNRLPASDQAQLKSRQGVRTVGFSE------IDVVDPESGRSV--------------ERDGE-----TVGEIVLRGSSI 399
Cdd:cd12115 225 LPRDLVQRLYARLQVERVVNLYGPSEdttystVAPVPPGASGEVsigrplantqayvlDRALQpvplgVPGELYIGGAGV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 400 MLGYLKNPIGTQNSFKNGWFF-------TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVA 472
Cdd:cd12115 305 ARGYLGRPGLTAERFLPDPFGpgarlyrTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVA 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 473 RPDEFWGETPCAFVSLKPGltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:cd12115 385 IGDAAGERRLVAYIVAEPG--AAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
42-539 |
3.46e-20 |
|
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: 93.19 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDff 121
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 122 ysdlaveaitmllnppILVLIaneeeeeggaevterskfcylysdlitrgnpdfkwirpgsewdpivvnYTSGTTSSPKG 201
Cdd:cd05940 83 ----------------AALYI------------------------------------------------YTSGTTGLPKA 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 202 --VVHcHRGIFVMTLDSLTDWAVPKTPVYLwTLPIFHANGWTYPWGIA-AVGGTNVCVRKLHAPSIYHLIRDHGVTHMYG 278
Cdd:cd05940 99 aiISH-RRAWRGGAFFAGSGGALPSDVLYT-CLPLYHSTALIVGWSAClASGATLVIRKKFSASNFWDDIRKYQATIFQY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 279 APIVLQILSASQESDQPLKSPVNfLTAGSSppatvlLRAESLG-----FIVSH---GYGLTEtaGVIVScawkpnWNRlP 350
Cdd:cd05940 177 IGELCRYLLNQPPKPTERKHKVR-MIFGNG------LRPDIWEefkerFGVPRiaeFYAATE--GNSGF------INF-F 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 351 ASDQAQLKSRQGVRTVGFSEIDVVDPESGRSVeRD-------------GETVGEIVLRGSSImlGYLKNPIGT----QNS 413
Cdd:cd05940 241 GKPGAIGRNPSLLRKVAPLALVKYDLESGEPI-RDaegrcikvprgepGLLISRINPLEPFD--GYTDPAATEkkilRDV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 414 FKNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAV----VARPDefwGETPCAFVS 487
Cdd:cd05940 318 FKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTD---GRAGMAAIV 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15222924 488 LKPGltrKPTD-KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05940 395 LQPN---EEFDlSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
185-542 |
5.54e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 94.26 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIfvmtldsLTDWA-----VPKTP--VYLWTLPIFHANGWTYPWGIAAVGGTNVCV- 256
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRNL-------LANRAqvaarIDFSPedKVFNALPVFHSFGLTGGLVLPLLSGVKVFLy 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 257 -RKLHAPSIYHLIRDHGVTHMYGAPIvlqILSASQESDQP--LKSpVNFLTAGSSP--PATVLLRAESLGFIVSHGYGLT 331
Cdd:PRK06814 867 pSPLHYRIIPELIYDTNATILFGTDT---FLNGYARYAHPydFRS-LRYVFAGAEKvkEETRQTWMEKFGIRILEGYGVT 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 332 ETAGVIvSCAwKPNWNR-------LPASDqAQLKSRQGVrtvgfseidvvdPESGRsverdgetvgeIVLRGSSIMLGYL 404
Cdd:PRK06814 943 ETAPVI-ALN-TPMHNKagtvgrlLPGIE-YRLEPVPGI------------DEGGR-----------LFVRGPNVMLGYL 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 405 K--NPiGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETp 482
Cdd:PRK06814 997 RaeNP-GVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGER- 1074
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222924 483 CAFVSLKPGLTRkptdKEIIEYCKYK-MPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIAK 542
Cdd:PRK06814 1075 IILLTTASDATR----AAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAE 1131
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
42-456 |
7.90e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 92.75 E-value: 7.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINT---RLD-----ARTVSVLlRHCES 113
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQptpRTDlavwaEDTLRVI-GMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 114 KLLFVdffySDLAVEAITMLLNPPILVLianeeeeeggaevterskfcyLYSDLITRGNPDfkwIRPGSEWDPIVVNYTS 193
Cdd:PRK07768 110 KAVVV----GEPFLAAAPVLEEKGIRVL---------------------TVADLLAADPID---PVETGEDDLALMQLTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 194 GTTSSPKGVVHCHRGIFV----MTLDSLTDwavPKTPVYLWTLPIFHANG----WTYPwgiAAVGGTNVCVRK---LHAP 262
Cdd:PRK07768 162 GSTGSPKAVQITHGNLYAnaeaMFVAAEFD---VETDVMVSWLPLFHDMGmvgfLTVP---MYFGAELVKVTPmdfLRDP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 263 SIY-HLIRDHGVThMYGAP-----IVLQILSASQESDQPLKSPVNFLTAGSSP--PATV--LLRAESlGFIVSHG----- 327
Cdd:PRK07768 236 LLWaELISKYRGT-MTAAPnfayaLLARRLRRQAKPGAFDLSSLRFALNGAEPidPADVedLLDAGA-RFGLRPEailpa 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 YGLTETAgVIVSCAWKPNWNRLPASDqAQLKSRQGvRTVGFSEIDV---------VDPESGRSVERDGET-----VGEIV 393
Cdd:PRK07768 314 YGMAEAT-LAVSFSPCGAGLVVDEVD-ADLLAALR-RAVPATKGNTrrlatlgppLPGLEVRVVDEDGQVlpprgVGVIE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 394 LRGSSIMLGYLK--NPIGTQNSfkNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVE 456
Cdd:PRK07768 391 LRGESVTPGYLTmdGFIPAQDA--DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
185-532 |
1.19e-19 |
|
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: 91.97 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTDwavpktpvylwTLPIFHANGW----TYPWGIAA--------VGGT 252
Cdd:cd12116 127 DLAYVIYTSGSTGRPKGVVVSHRNL-VNFLHSMRE-----------RLGLGPGDRLlavtTYAFDISLlelllpllAGAR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 253 NVCVRKLH---APSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPlksPVNFLTAGSSPPATVLLRAESLGFIVSHGYG 329
Cdd:cd12116 195 VVIAPRETqrdPEALARLIEAHSITVMQATPATWRMLLDAGWQGRA---GLTALCGGEALPPDLAARLLSRVGSLWNLYG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 330 LTETAgvIVSCawkpnWNRLPASDqaqlksrqGVRTVGFS----EIDVVDpESGRSVERdGEtVGEIVLRGSSIMLGYLK 405
Cdd:cd12116 272 PTETT--IWST-----AARVTAAA--------GPIPIGRPlantQVYVLD-AALRPVPP-GV-PGELYIGGDGVAQGYLG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 406 NPIGTQNSF------KNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEf 477
Cdd:cd12116 334 RPALTAERFvpdpfaGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG- 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 478 WGETPCAFVSLKPGLTrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd12116 413 GDRRLVAYVVLKAGAA--PDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
185-474 |
3.79e-19 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 90.95 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIF-----VMTldsltdwAVPK---TPVYLWTLPIFHANGWTYPWGIAAVG------ 250
Cdd:PLN02387 251 DIAVIMYTSGSTGLPKGVMMTHGNIVatvagVMT-------VVPKlgkNDVYLAYLPLAHILELAAESVMAAVGaaigyg 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 251 --------------GTNVCVRKLH------APSIYHLIRDhGVTHMYGAP--IVLQI--------LSASQES-------- 292
Cdd:PLN02387 324 spltltdtsnkikkGTKGDASALKptlmtaVPAILDRVRD-GVRKKVDAKggLAKKLfdiaykrrLAAIEGSwfgawgle 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 293 ------------DQPLKSPVNFLTAGSSPpatvlLRAES-------LGFIVSHGYGLTET-AGVIVScawkpNWNrlpas 352
Cdd:PLN02387 403 kllwdalvfkkiRAVLGGRIRFMLSGGAP-----LSGDTqrfinicLGAPIGQGYGLTETcAGATFS-----EWD----- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 353 DQAqlksrqgVRTVG----FSEIDVVD-PESGRSVERDGETVGEIVLRGSSIMLGYLKNPIGTQNSFK---NG--WFFTG 422
Cdd:PLN02387 468 DTS-------VGRVGpplpCCYVKLVSwEEGGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKvdeRGmrWFYTG 540
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15222924 423 DLGVIHGDGYLEIKDRSKDVI-ISGGENVSSVEVEAVLYTNPAVNEAAVVARP 474
Cdd:PLN02387 541 DIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAALSVSPYVDNIMVHADP 593
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
42-506 |
6.55e-19 |
|
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: 90.11 E-value: 6.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFF 121
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVENQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 122 YSDLAVEAITMLLnPPILVLIaneeeeEGGAEVTERSKFCYLYSDLITRGNPDfkwirPGSEWDPIVVN----------Y 191
Cdd:cd05933 90 KQLQKILQIQDKL-PHLKAII------QYKEPLKEKEPNLYSWDEFMELGRSI-----PDEQLDAIISSqkpnqcctliY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 192 TSGTTSSPKGVVHCHRGIfVMTLDSLT-----DWAVPKTPVYLWTLPIFHANGWTYP-WGIAAVGGTnVCVRKLHA--PS 263
Cdd:cd05933 158 TSGTTGMPKGVMLSHDNI-TWTAKAASqhmdlRPATVGQESVVSYLPLSHIAAQILDiWLPIKVGGQ-VYFAQPDAlkGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 264 IYHLIRDHGVTHMYGAPIV-------LQILSASQ-------------------------ESDQPLK---------SPVN- 301
Cdd:cd05933 236 LVKTLREVRPTAFMGVPRVwekiqekMKAVGAKSgtlkrkiaswakgvgletnlklmggESPSPLFyrlakklvfKKVRk 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 302 ---------FLTAGSSPPATVLLRAESLGFIVSHGYGLTETAGVIVSCawKPNWNRLPASDQAQlksrQGVRTvgfseid 372
Cdd:cd05933 316 algldrcqkFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTIS--NPQAYRLLSCGKAL----PGCKT------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 373 vvdpesgRSVERDGETVGEIVLRGSSIMLGYLKNPIGTQNSFK-NGWFFTGDLGVIHGDGYLEIKDRSKDVII-SGGENV 450
Cdd:cd05933 383 -------KIHNPDADGIGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENV 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222924 451 SSVEVE-AVLYTNPAVNEAAVVARPDEFWgetpCAFVSLKPGL---TRKPTDK---EIIEYCK 506
Cdd:cd05933 456 PPVPIEdAVKKELPIISNAMLIGDKRKFL----SMLLTLKCEVnpeTGEPLDElteEAIEFCR 514
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
185-539 |
1.40e-18 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 89.92 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIfVMTLDSLTDW-AVPKTPVYLWTLPI-FHANGWTYpWGIAAVGGTNVCVRK---L 259
Cdd:COG1020 618 DLAYVIYTSGSTGRPKGVMVEHRAL-VNLLAWMQRRyGLGPGDRVLQFASLsFDASVWEI-FGALLSGATLVLAPPearR 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 260 HAPSIYHLIRDHGVTHMYGAPIVLQILsaSQESDQPLKSPVNFLTAGSSPPATVL--LRAESLGFIVSHGYGLTETAgvI 337
Cdd:COG1020 696 DPAALAELLARHRVTVLNLTPSLLRAL--LDAAPEALPSLRLVLVGGEALPPELVrrWRARLPGARLVNLYGPTETT--V 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 338 VSCAWkpnwnRLPASDQAQLKSRQGvRTVGFSEIDVVDpESGRSVeRDGEtVGEIVLRGSSIMLGYLKNPIGTQNSF-KN 416
Cdd:COG1020 772 DSTYY-----EVTPPDADGGSVPIG-RPIANTRVYVLD-AHLQPV-PVGV-PGELYIGGAGLARGYLNRPELTAERFvAD 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 417 GWFF-------TGDLGVIHGDGYLEIKDRSKD-VIISG-----GenvssvEVEAVLYTNPAVNEAAVVARPDEfwGETP- 482
Cdd:COG1020 843 PFGFpgarlyrTGDLARWLPDGNLEFLGRADDqVKIRGfrielG------EIEAALLQHPGVREAVVVAREDA--PGDKr 914
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15222924 483 -CAFVSLKPGLTrkPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:COG1020 915 lVAYVVPEAGAA--AAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
37-532 |
6.39e-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: 86.37 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 37 NSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLL 116
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 117 FVDffysdlaveaitmllnppilvlianeeeeeggaevterskfcylysdlitrgnPDfkwirpgsewDPIVVNYTSGTT 196
Cdd:cd17650 89 LTQ-----------------------------------------------------PE----------DLAYVIYTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 197 SSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAV-GGTNV-CVR--KLHAPSIYHLIRDHG 272
Cdd:cd17650 106 GKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLnGGTLViCPDevKLDPAALYDLILKSR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 273 VTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGS-----SPPATVLLRAESLGFIVShGYGLTETAgvIVSCAWKPNWN 347
Cdd:cd17650 186 ITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSdgckaQDFKTLAARFGQGMRIIN-SYGVTEAT--IDSTYYEEGRD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 348 RLPASDQAQLKsrqgvRTVGFSEIDVVDPEsgRSVERDGeTVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFF------- 420
Cdd:cd17650 263 PLGDSANVPIG-----RPLPNTAMYVLDER--LQPQPVG-VAGELYIGGAGVARGYLNRPELTAERFVENPFApgermyr 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 421 TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKpgltRKPTDKE 500
Cdd:cd17650 335 TGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA----ATLNTAE 410
|
490 500 510
....*....|....*....|....*....|..
gi 15222924 501 IIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17650 411 LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
183-541 |
8.81e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 86.88 E-value: 8.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 183 EW----DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTdWAVPKTP--VYLWTLPIFHANGWTY-PWGIAAVGGTNVC 255
Cdd:PLN02654 270 EWvdaeDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFK-YAFDYKPtdVYWCTADCGWITGHSYvTYGPMLNGATVLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 256 VRKlhAPS------IYHLIRDHGVTHMYGAPIVLQILSA---------SQESDQPLKS---PVN-------FLTAGSS-- 308
Cdd:PLN02654 349 FEG--APNypdsgrCWDIVDKYKVTIFYTAPTLVRSLMRdgdeyvtrhSRKSLRVLGSvgePINpsawrwfFNVVGDSrc 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 309 PPATVLLRAESLGFIVSHGYGltetagvivscAW--KPNWNRLPASdqaqlksrqGVRTVgfseidVVDpESGRSVErdG 386
Cdd:PLN02654 427 PISDTWWQTETGGFMITPLPG-----------AWpqKPGSATFPFF---------GVQPV------IVD-EKGKEIE--G 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 387 ETVGEIVLRGSsiMLGYLKNPIGTQNSFKN-------GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVL 459
Cdd:PLN02654 478 ECSGYLCVKKS--WPGAFRTLYGDHERYETtyfkpfaGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESAL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 460 YTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLT-RKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:PLN02654 556 VSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
...
gi 15222924 539 EIA 541
Cdd:PLN02654 636 KIA 638
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
189-532 |
1.60e-17 |
|
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: 85.14 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 189 VNYTSGTTSSPKGVVHCHRGI--FVMTLDSLTDWAVPKTPVYLwtlpiFHANgwtYPWG-------IAAVGGTNVCV--- 256
Cdd:cd17648 99 AIYTSGTTGKPKGVLVEHGSVvnLRTSLSERYFGRDNGDEAVL-----FFSN---YVFDffveqmtLALLNGQKLVVppd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 257 -RKLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQesdqpLKSPVNFLTAGS--SPPATVLLRAESLGFIVShGYGLTET 333
Cdd:cd17648 171 eMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLAR-----LPHLKRVDAAGEefTAPVFEKLRSRFAGLIIN-AYGPTET 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 334 AgviVSCAWKPnwnrLPASDQAQLKSRQGVRTVgfsEIDVVDPESGRsVERDGetVGEIVLRGSSIMLGYLKNPIGTQNS 413
Cdd:cd17648 245 T---VTNHKRF----FPGDQRFDKSLGRPVRNT---KCYVLNDAMKR-VPVGA--VGELYLGGDGVARGYLNRPELTAER 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 414 F--------------KNGWFF-TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFW 478
Cdd:cd17648 312 FlpnpfqteqerargRNARLYkTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQ 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15222924 479 GETP-----CAFVSLKPGLTrkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17648 392 AQSRiqkylVGYYLPEPGHV---PESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
180-538 |
1.91e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 84.70 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 180 PGSEWDPIVVNYTSGTTSSPKGVVHCHRGI------FVMTLDSLTDwavpKTPVYLwtLPIFHANGWtypwgiaaVGGTN 253
Cdd:PRK08308 97 NYLAEEPSLLQYSSGTTGEPKLIRRSWTEIdreieaYNEALNCEQD----ETPIVA--CPVTHSYGL--------ICGVL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 254 VCVRKLHAPSI-------YHL--IRDHGVTHMYGAPIVLQILSASQESDQPLKSpvnFLTAGSSPPATVLLRAESLGFIV 324
Cdd:PRK08308 163 AALTRGSKPVIitnknpkFALniLRNTPQHILYAVPLMLHILGRLLPGTFQFHA---VMTSGTPLPEAWFYKLRERTTYM 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 325 SHGYGLTEtAGVIVSCawkPNwnrlpasdqaqlksrqgVRTVGfsEIDVVDPESGRSVERDGETVGEIVLRgssimlgyl 404
Cdd:PRK08308 240 MQQYGCSE-AGCVSIC---PD-----------------MKSHL--DLGNPLPHVSVSAGSDENAPEEIVVK--------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 405 knpIGTQNsfkngwFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCA 484
Cdd:PRK08308 288 ---MGDKE------IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15222924 485 FVSLKPGLtrkpTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:PRK08308 359 KVISHEEI----DPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
189-537 |
2.46e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.16 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 189 VNYTSGTTSSPKGVVHCHrGIFVMTLDSL--------TDWAVPKTPvylwtlpiFHANGWTYPWGIAAVGGTNVCVR--K 258
Cdd:PRK12316 2151 VIYTSGSTGLPKGVAVSH-GALVAHCQAAgeryelspADCELQFMS--------FSFDGAHEQWFHPLLNGARVLIRddE 2221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 LHAPS-IYHLIRDHGVTHMYGAPIVLQILSASQESD-QPLKSPVNFLTAGSSPPATVLLRAESLGFI-VSHGYGLTETag 335
Cdd:PRK12316 2222 LWDPEqLYDEMERHGVTILDFPPVYLQQLAEHAERDgRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEA-- 2299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 336 VIVSCAWKPNWNRLPASDQAQLKSRQGVRT--VGFSEIDVVDPEsgrsverdgeTVGEIVLRGSSIMLGYLKNPIGTQNS 413
Cdd:PRK12316 2300 VVTPLLWKCRPQDPCGAAYVPIGRALGNRRayILDADLNLLAPG----------MAGELYLGGEGLARGYLNRPGLTAER 2369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 414 FKNGWFF--------TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARpDEFWGETPCAF 485
Cdd:PRK12316 2370 FVPDPFSasgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAY 2448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15222924 486 VSLKPGLTRKPtdKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:PRK12316 2449 VVPDDAAEDLL--AELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
35-539 |
4.68e-16 |
|
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: 80.55 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 35 YGNSTvYTWRETNHRCLCVASAL-SSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCES 113
Cdd:cd05937 1 FEGKT-WTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 114 KLLFVDffysdlaveaitmllnppilvlianeeeeeggaevterskfcylysdlitrgnPDfkwirpgsewDPIVVNYTS 193
Cdd:cd05937 80 RFVIVD-----------------------------------------------------PD----------DPAILIYTS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 194 GTTSSPKGVvhchrgIFVMTLDSLTDWAVPKT-----PVYLWT-LPIFHANGWTypwgIAAV-----GGTNVCVRKLHAP 262
Cdd:cd05937 97 GTTGLPKAA------AISWRRTLVTSNLLSHDlnlknGDRTYTcMPLYHGTAAF----LGACnclmsGGTLALSRKFSAS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 263 SIYHLIRDHGVTHM-YGAPIVLQILSASQESDQPLKSPVNFLTAGSSPPATVLLRaESLGF-IVSHGYGLTEtaGVIVSc 340
Cdd:cd05937 167 QFWKDVRDSGATIIqYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFR-ERFNVpEIGEFYAATE--GVFAL- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 341 awkpnWNRLPASDQAQLKSRQGV---RTVGFSEIDV-VDPESGR-------------SVERDGETVGEIVLRGSSIMLGY 403
Cdd:cd05937 243 -----TNHNVGDFGAGAIGHHGLirrWKFENQVVLVkMDPETDDpirdpktgfcvraPVGEPGEMLGRVPFKNREAFQGY 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 404 LKNPIGTQ-----NSFKNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAV--VARP 474
Cdd:cd05937 318 LHNEDATEsklvrDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVP 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222924 475 DeFWGETPCAFVSLKPGLTrKPTDKEIIEYCKYK---MPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05937 398 G-HDGRAGCAAITLEESSA-VPTEFTKSLLASLArknLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
191-538 |
1.55e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 79.69 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGIFVMtLDSLTDWAVPKTP--VYLWTLPIFHANGW-TYPWGIAAVGGTNVCVR-KLHAPSIYH 266
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPLTF-VDAMCRKALRLTPedTGLCSARMYFAYGLgNSVWFPLATGGSAVINSaPVTPEAAAI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 267 LIRDHGVTHMYGAP-IVLQILSA-SQESDQPLKSPVnflTAGSS-PPATVLLRAESLGFI-VSHGYGLTETAGVIVSCA- 341
Cdd:PRK06060 231 LSARFGPSVLYGVPnFFARVIDScSPDSFRSLRCVV---SAGEAlELGLAERLMEFFGGIpILDGIGSTEVGQTFVSNRv 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 342 --WKPNwnrlpasdqaqlksrqgvrTVGfseiDVVDPESGRSVERDGETVG-----EIVLRGSSIMLGYLKNPIGTQNSf 414
Cdd:PRK06060 308 deWRLG-------------------TLG----RVLPPYEIRVVAPDGTTAGpgvegDLWVRGPAIAKGYWNRPDSPVAN- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 415 kNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVArPDEFWGET-------PCAFVS 487
Cdd:PRK06060 364 -EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVA-VRESTGAStlqaflvATSGAT 441
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15222924 488 LKPGLTRKPTDKEIIEYCKYKMPRYMApktvsFLEELPKTSTGKIIKSLLK 538
Cdd:PRK06060 442 IDGSVMRDLHRGLLNRLSAFKVPHRFA-----VVDRLPRTPNGKLVRGALR 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
189-532 |
2.92e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.43 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 189 VNYTSGTTSSPKGVVHCHRGIfVMTLDSLTDWA--VPKTPVYLWTLPIFHANGWTYPWGIAAvGGTNVCVRK---LHAPS 263
Cdd:PRK12467 661 VIYTSGSTGQPKGVAISHGAL-ANYVCVIAERLqlAADDSMLMVSTFAFDLGVTELFGALAS-GATLHLLPPdcaRDAEA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 264 IYHLIRDHGVTHMYGAPIVLQILSASQESDQPlkSPVNFLTAGS---SPPATVLLRAESLGFIVSHGYGLTETAgvIVSC 340
Cdd:PRK12467 739 FAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGealQVDLLARVRALGPGARLINHYGPTETT--VGVS 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 341 AWkpnwnrlPASDQAqlksrqgvRTVGFSEIDVvdPESGRSVER-DGE-------TVGEIVLRGSSIMLGYLKNPIGTQN 412
Cdd:PRK12467 815 TY-------ELSDEE--------RDFGNVPIGQ--PLANLGLYIlDHYlnpvpvgVVGELYIGGAGLARGYHRRPALTAE 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 413 SF------KNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCA 484
Cdd:PRK12467 878 RFvpdpfgADGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAY 957
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15222924 485 FVSLKP--GLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:PRK12467 958 LVPAAVadGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
381-532 |
4.30e-15 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 77.88 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 381 SVERDGETVGEIVLRGSSIMLGYL-KNPIGTQNsfkngWFFTGDLGVIhGDGYLEIKDRSKDVIISGGENVSSVEVEAVL 459
Cdd:PRK05851 364 AAGVAGREIGEIEIRGASMMSGYLgQAPIDPDD-----WFPTGDLGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERVA 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 460 YTNPAVNEAAVVA-RPDEfwgetpcafVSLKPGL-------------TRKPTDKEIIEYCKykmpryMAPKTVSFLE--E 523
Cdd:PRK05851 438 AQVRGVREGAVVAvGTGE---------GSARPGLviaaefrgpdeagARSEVVQRVASECG------VVPSDVVFVApgS 502
|
....*....
gi 15222924 524 LPKTSTGKI 532
Cdd:PRK05851 503 LPRTSSGKL 511
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
185-531 |
6.21e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 77.83 E-value: 6.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIF--VMTLDSLTDWavpkTP--VYLWTLPIFHANGWTYPWGIAAVGGTNVCV--RK 258
Cdd:PRK08043 366 DAALILFTSGSEGHPKGVVHSHKSLLanVEQIKTIADF----TPndRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypSP 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 LHAPSIYHLIRDHGVTHMYGAPIVLQILSAsqesdqpLKSPVNF-----LTAGSSP--PATVLLRAESLGFIVSHGYGLT 331
Cdd:PRK08043 442 LHYRIVPELVYDRNCTVLFGTSTFLGNYAR-------FANPYDFarlryVVAGAEKlqESTKQLWQDKFGLRILEGYGVT 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 332 ETAGVI---VSCAWKPNW-NR-LPASDqAQLKSRQGVrtvgfseidvvdpESGrsverdgetvGEIVLRGSSIMLGYLK- 405
Cdd:PRK08043 515 ECAPVVsinVPMAAKPGTvGRiLPGMD-ARLLSVPGI-------------EQG----------GRLQLKGPNIMNGYLRv 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 406 -NP--------IGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAV-LYTNPAVNEAAvVARPD 475
Cdd:PRK08043 571 eKPgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHAT-AIKSD 649
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15222924 476 EFWGETPCAFVSlKPGLTRkptDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGK 531
Cdd:PRK08043 650 ASKGEALVLFTT-DSELTR---EKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
164-458 |
7.59e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 77.45 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 164 YSDLITRGNPDFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFH----ANG 239
Cdd:PLN02736 201 YSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyerVNQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 240 WTYPWGIAAVGGTNVCVRKL-------------HAPSIYHLIRDhGVTHMYGAPIVLQ---ILSASQESDQPL---KSP- 299
Cdd:PLN02736 281 IVMLHYGVAVGFYQGDNLKLmddlaalrptifcSVPRLYNRIYD-GITNAVKESGGLKerlFNAAYNAKKQALengKNPs 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 300 ------------------VNFLTAGSSPpatvlLRAESLGFI-------VSHGYGLTETAGVIVSCawkpnwnrlpasdq 354
Cdd:PLN02736 360 pmwdrlvfnkikaklggrVRFMSSGASP-----LSPDVMEFLricfggrVLEGYGMTETSCVISGM-------------- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 355 aqlksRQGVRTVGF-------SEIDVVD-PESGRSVERDGETVGEIVLRGSSIMLGYLKNPIGTQNSFKN-GWFFTGDLG 425
Cdd:PLN02736 421 -----DEGDNLSGHvgspnpaCEVKLVDvPEMNYTSEDQPYPRGEICVRGPIIFKGYYKDEVQTREVIDEdGWLHTGDIG 495
|
330 340 350
....*....|....*....|....*....|....
gi 15222924 426 VIHGDGYLEIKDRSKDVI-ISGGENVSSVEVEAV 458
Cdd:PLN02736 496 LWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
29-537 |
1.36e-14 |
|
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: 76.36 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 29 DCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLL 108
Cdd:cd17656 3 DAVAVVFENQKL-TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 109 RHCESKLLFVDFFYSD-LAVEAITMLLNPPILvlianeeeeegGAEVTERSKFCYLYSDLItrgnpdfkwirpgsewdpi 187
Cdd:cd17656 82 LDSGVRVVLTQRHLKSkLSFNKSTILLEDPSI-----------SQEDTSNIDYINNSDDLL------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 188 VVNYTSGTTSSPKGVVHCHRgifvmTLDSLTDWAVPKT------PVYLWTLPIFHAngwTYPWGIAAV--GGTNVCVR-- 257
Cdd:cd17656 132 YIIYTSGTTGKPKGVQLEHK-----NMVNLLHFEREKTninfsdKVLQFATCSFDV---CYQEIFSTLlsGGTLYIIRee 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 258 -KLHAPSIYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPV-NFLTAGSSPPATVLLRAeslgFIVSHG------YG 329
Cdd:cd17656 204 tKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVkHIITAGEQLVITNEFKE----MLHEHNvhlhnhYG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 330 LTETAgVIVSCAWKPN--WNRLPASDqaqlksrqgvRTVGFSEIDVVDPEsgRSVERDGeTVGEIVLRGSSIMLGYLKNP 407
Cdd:cd17656 280 PSETH-VVTTYTINPEaeIPELPPIG----------KPISNTWIYILDQE--QQLQPQG-IVGELYISGASVARGYLNRQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 408 IGTQNSFKNGWF-------FTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGE 480
Cdd:cd17656 346 ELTAEKFFPDPFdpnermyRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEK 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15222924 481 TPCA-FVSLKpgltrKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:cd17656 426 YLCAyFVMEQ-----ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
189-532 |
2.73e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 189 VNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAV-PKTPVYLWTLPIFHANGWTYPWGIAAvgGTNVCVRK--LHAP-SI 264
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELtPDDRVLQFMSFSFDGSHEGLYHPLIN--GASVVIRDdsLWDPeRL 4776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 265 YHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNFLTAGSS-PPATVLLRAESLGFIVSH-GYGLTETagVIVSCAW 342
Cdd:PRK12316 4777 YAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAvAQASYDLAWRALKPVYLFnGYGPTET--TVTVLLW 4854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 343 KpnwnrLPASDQAqlksrqgvrtvGFSEIDVVDPESGRSVE-RDGE-------TVGEIVLRGSSIMLGYLKNPIGTQNSF 414
Cdd:PRK12316 4855 K-----ARDGDAC-----------GAAYMPIGTPLGNRSGYvLDGQlnplpvgVAGELYLGGEGVARGYLERPALTAERF 4918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 415 ------KNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFV 486
Cdd:PRK12316 4919 vpdpfgAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVV 4998
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15222924 487 SLKPGLTRKPTDK-----EIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:PRK12316 4999 PQDPALADADEAQaelrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-532 |
3.69e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.15 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 6 PSAANSLPLtllgfLERAATVYGDCTSIVYGNSTVyTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSV 85
Cdd:PRK12316 508 PLQRGVHRL-----FEEQVERTPEAPALAFGEETL-DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAI 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 86 PMSGAILNNINTRLDARTVSVLLRHCESKLLFVDFFYSD---LAVEAITMLLNPPILVLIAneeeeeggaevterskfcy 162
Cdd:PRK12316 582 LKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRklpLAAGVQVLDLDRPAAWLEG------------------- 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 163 lYSDlitrGNPDfkwIRPGSEwDPIVVNYTSGTTSSPKGVVHCHRGifvmtLDSLTDWA------------VPKTPVYlw 230
Cdd:PRK12316 643 -YSE----ENPG---TELNPE-NLAYVIYTSGSTGKPKGAGNRHRA-----LSNRLCWMqqayglgvgdtvLQKTPFS-- 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 231 tlpiFHANGWTYPWGIAAVGGTNVCVRKLH--APSIYHLIRDHGVTHMYGAPIVLQILSasQESDQPLKSPVNFLT-AGS 307
Cdd:PRK12316 707 ----FDVSVWEFFWPLMSGARLVVAAPGDHrdPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVASCTSLRRIVcSGE 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 308 SPPATVLLRAESL---GFIVSHgYGLTETAgvIVSCAWKpnwnrlpasdqaqlksrqgVRTVGFSEIDVVDPESG---RS 381
Cdd:PRK12316 781 ALPADAQEQVFAKlpqAGLYNL-YGPTEAA--IDVTHWT-------------------CVEEGGDSVPIGRPIANlacYI 838
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 382 VERDGETV-----GEIVLRGSSIMLGYLKNPIGTQ-----NSFKNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGEN 449
Cdd:PRK12316 839 LDANLEPVpvgvlGELYLAGRGLARGYHGRPGLTAerfvpSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 450 VSSVEVEAVLYTNPAVNEAAVVAR----------PDEFWGETPcafVSLKPGLtrkptdkeiieycKYKMPRYMAPKTVS 519
Cdd:PRK12316 919 IELGEIEARLLEHPWVREAAVLAVdgkqlvgyvvLESEGGDWR---EALKAHL-------------AASLPEYMVPAQWL 982
|
570
....*....|...
gi 15222924 520 FLEELPKTSTGKI 532
Cdd:PRK12316 983 ALERLPLTPNGKL 995
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
387-532 |
5.18e-14 |
|
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: 74.39 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 387 ETVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFF---------TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEA 457
Cdd:cd17644 307 GVPGELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEA 386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222924 458 VLYTNPAVNEAAVVARPDEFWGETPCAFVSlkPGLTRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:cd17644 387 VLSQHNDVKTAVVIVREDQPGNKRLVAYIV--PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
185-544 |
5.35e-14 |
|
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: 74.12 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRgIFVMTLDSLTDwAVPKTPV--------YLWTLPIFHAngwtypWGIAAVGGTnVCV 256
Cdd:cd05918 107 DAAYVIFTSGSTGKPKGVVIEHR-ALSTSALAHGR-ALGLTSEsrvlqfasYTFDVSILEI------FTTLAAGGC-LCI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 257 rklhaPS-------IYHLIRDHGVTHMYGAPIVLQILSASQesdqpLKSPVNFLTAGSSPPATVLLRAESLGFIVShGYG 329
Cdd:cd05918 178 -----PSeedrlndLAGFINRLRVTWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTWADRVRLIN-AYG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 330 LTETAgviVSCAWKPNwnrLPASDqaqlksrqgVRTVGFSeID----VVDPESGRSVERDGEtVGEIVLRGSSIMLGYLK 405
Cdd:cd05918 247 PAECT---IAATVSPV---VPSTD---------PRNIGRP-LGatcwVVDPDNHDRLVPIGA-VGELLIEGPILARGYLN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 406 NPIGTQNSFKNGWFF--------------TGDLGVIHGDGYLEIKDRsKD--VIIsGGENVSSVEVEAVLYTNPAVNE-- 467
Cdd:cd05918 310 DPEKTAAAFIEDPAWlkqegsgrgrrlyrTGDLVRYNPDGSLEYVGR-KDtqVKI-RGQRVELGEIEHHLRQSLPGAKev 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 468 -AAVVARPDEFWGETPCAFVSLKPGLTRKPTD---------------KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGK 531
Cdd:cd05918 388 vVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGK 467
|
410
....*....|...
gi 15222924 532 IIKSLLKEIAKNM 544
Cdd:cd05918 468 IDRRALRELAESL 480
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
42-465 |
1.26e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 73.72 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEmYELQFSVPMSGAILN-NINTRLDARTVSVLLRHCESKLLFVdf 120
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPE-WIIAMEACNSQGITYvPLYDTLGANAVEFIINHAEVSIAFV-- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 121 fySDLAVEAITMLLNPPILVLIANEEEEEGGAEVTERSK----FCYLYSDLITRGNPDFKwIRPGSEWDPIVVNYTSGTT 196
Cdd:PLN02861 156 --QESKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEAEelgvSCFSWEEFSLMGSLDCE-LPPKQKTDICTIMYTSGTT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 197 SSPKGVVHCHRGIF--VMTLDSL---TDWAVPKTPVYLWTLPIFHangwTYPWGI--------AAVGGTNVCVRKLH--- 260
Cdd:PLN02861 233 GEPKGVILTNRAIIaeVLSTDHLlkvTDRVATEEDSYFSYLPLAH----VYDQVIetyciskgASIGFWQGDIRYLMedv 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 261 ----------APSIYH--------------LIRDH---------------GVTHMYGAPIVLQILSasQESDQPLKSPVN 301
Cdd:PLN02861 309 qalkptifcgVPRVYDriytgimqkissggMLRKKlfdfaynyklgnlrkGLKQEEASPRLDRLVF--DKIKEGLGGRVR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 302 FLTAGSSP-PATV--LLRAESLGfIVSHGYGLTET-AGVIVSCAwkpnwNRLPAsdqaqlksrqgVRTVGF------SEI 371
Cdd:PLN02861 387 LLLSGAAPlPRHVeeFLRVTSCS-VLSQGYGLTEScGGCFTSIA-----NVFSM-----------VGTVGVpmttieARL 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 372 DVVdPESG----RSVERdgetvGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVI-ISG 446
Cdd:PLN02861 450 ESV-PEMGydalSDVPR-----GEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQ 523
|
490
....*....|....*....
gi 15222924 447 GENVSSVEVEAVLYTNPAV 465
Cdd:PLN02861 524 GEYVAVENLENTYSRCPLI 542
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
185-471 |
2.36e-13 |
|
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: 72.11 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHrGIFVMTLDSL-TDWAVPKTPVYLWTLPIFHANGwtypwgiAAVGGTNVC-------- 255
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRH-GTFAAQIDALrQLYGIRPGEVDLATFPLFALFG-------PALGLTSVIpdmdptrp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 256 ----VRKLHAPsiyhlIRDHGVTHMYGAPIVLQILSASQES-DQPLKSPVNFLTAGSSPPATVllrAESLGFIVSHG--- 327
Cdd:cd05910 158 aradPQKLVGA-----IRQYGVSIVFGSPALLERVARYCAQhGITLPSLRRVLSAGAPVPIAL---AARLRKMLSDEaei 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 ---YGLTETagvivscawkpnwnrLPAS---DQAQLKSRQ----------------GVRtVGFSEIDVVD-PESGRSVER 384
Cdd:cd05910 230 ltpYGATEA---------------LPVSsigSRELLATTTaatsggagtcvgrpipGVR-VRIIEIDDEPiAEWDDTLEL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 385 DGETVGEIVLRGSSIMLGYLKNPIGT--------QNSFkngWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVE 456
Cdd:cd05910 294 PRGEIGEITVTGPTVTPTYVNRPVATalakiddnSEGF---WHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVE 370
|
330
....*....|....*
gi 15222924 457 AVLYTNPAVNEAAVV 471
Cdd:cd05910 371 RVFNTHPGVRRSALV 385
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
328-540 |
7.85e-13 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 70.69 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 YGLTETAGVIVSCAWKP----NWNRLPasdqaqlksrqgvrtVGFSEID---VVDPESGRSVErDGETvGEIVLRGSSIM 400
Cdd:PRK04813 293 YGPTEATVAVTSIEITDemldQYKRLP---------------IGYAKPDsplLIIDEEGTKLP-DGEQ-GEIVISGPSVS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 401 LGYLKNPIGTQNSFK--NGW--FFTGDLGVIHgDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDE 476
Cdd:PRK04813 356 KGYLNNPEKTAEAFFtfDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKD 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 477 FWGETPCAFVSLKPGLTRKPTD--KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI-IKSLLKEI 540
Cdd:PRK04813 435 HKVQYLIAYVVPKEEDFEREFEltKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIdRKALIEEV 501
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
42-511 |
8.99e-13 |
|
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: 70.95 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 42 TWRETNHRCLCVASALSSIG-IGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKLLFVDF 120
Cdd:cd17632 69 TYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 121 FYSDLAVEAITMLLNPPILVLIANEEEEEGGAEVTERS------KFC-YLYSDLIT---RGNPDFKWIRPGSEWDPIV-V 189
Cdd:cd17632 149 EHLDLAVEAVLEGGTPPRLVVFDHRPEVDAHRAALESArerlaaVGIpVTTLTLIAvrgRDLPPAPLFRPEPDDDPLAlL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 190 NYTSGTTSSPKGVVHCHRGI--FVMTLDSLTDwAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRklhAPSIYHL 267
Cdd:cd17632 229 IYTSGSTGTPKGAMYTERLVatFWLKVSSIQD-IRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAA---ASDMSTL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 268 IRDHGV---THMYGAPIVLQIL--------------SASQESDQP-----LKSPV---NFLTA--GSSPPATVlLRA--E 318
Cdd:cd17632 305 FDDLALvrpTELFLVPRVCDMLfqryqaeldrrsvaGADAETLAErvkaeLRERVlggRLLAAvcGSAPLSAE-MKAfmE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 319 S-LGFIVSHGYGLTETAGVIVSCAWKpnwnRLPASDqaqlksrqgvrtvgFSEIDVvdPESGRSVERDGETVGEIVLRGS 397
Cdd:cd17632 384 SlLDLDLHDGYGSTEAGAVILDGVIV----RPPVLD--------------YKLVDV--PELGYFRTDRPHPRGELLVKTD 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 398 SIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDRSKDVI-ISGGENVSSVEVEAVLYTNPAVNE-------- 467
Cdd:cd17632 444 TLFPGYYKRPEVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLkLSQGEFVTVARLEAVFAASPLVRQifvygnse 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15222924 468 -----AAVVARPDEFWGETPCAFVS-LKPGLTRKPTDKEIieyCKYKMPR 511
Cdd:cd17632 524 rayllAVVVPTQDALAGEDTARLRAaLAESLQRIAREAGL---QSYEIPR 570
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
173-537 |
9.13e-13 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 71.23 E-value: 9.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 173 PDFKWIRPGSEWDPIVVNYTSGTTSSPKGVVHCHRGIfVMTLD--------SLTDWAVPKTPVylwtlpIFHANGWTYPW 244
Cdd:PRK10252 587 QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI-VNRLLwmqnhyplTADDVVLQKTPC------SFDVSVWEFFW 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 245 GIAAvGGTNVCvrklhAP--------SIYHLIRDHGVTHMYGAPIVLQILSASQESD---QPLKSPVNFLTAGSSPPATV 313
Cdd:PRK10252 660 PFIA-GAKLVM-----AEpeahrdplAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEgarQSCASLRQVFCSGEALPADL 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 314 LLRAESLGFIVSHG-YGLTEtAGVIVScAWkpnwnrlPASDQAQLKSRQGVRTVGF----SEIDVVDpESGRSVERDgeT 388
Cdd:PRK10252 734 CREWQQLTGAPLHNlYGPTE-AAVDVS-WY-------PAFGEELAAVRGSSVPIGYpvwnTGLRILD-ARMRPVPPG--V 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 389 VGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFF-------TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYT 461
Cdd:PRK10252 802 AGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyrTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQA 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 462 NPAVNEAAVVARPDEFWGETP------CAFVSLKPGLtrkPTDKEII-EYCKYKMPRYMAPKTVSFLEELPKTSTGKIIK 534
Cdd:PRK10252 882 LPDVEQAVTHACVINQAAATGgdarqlVGYLVSQSGL---PLDTSALqAQLRERLPPHMVPVVLLQLDQLPLSANGKLDR 958
|
...
gi 15222924 535 SLL 537
Cdd:PRK10252 959 KAL 961
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
41-538 |
2.53e-12 |
|
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: 68.99 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 41 YTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAI--LNNINTRLDARTVSVLLRHCESkllfv 118
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVEtaLINSNLRLESLLHCITVSKAKA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 119 dffysdlaveAITMLLNPpilVLIANEEEEEGGAEVTERSKFCYLysdlitrgnpdfkwirpgsewdpivvnYTSGTTSS 198
Cdd:cd05939 79 ----------LIFNLLDP---LLTQSSTEPPSQDDVNFRDKLFYI---------------------------YTSGTTGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 199 PKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNVCVRKLHAPSIYHL--IRDHGVTHM 276
Cdd:cd05939 119 PKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDdcVKYNCTIVQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 277 YGAPIVLQILSAS-QESDQplKSPV-----NFLTAGSSPPATVLLRAESLGFIvshgYGLTETAGVIV-------SCAWK 343
Cdd:cd05939 199 YIGEICRYLLAQPpSEEEQ--KHNVrlavgNGLRPQIWEQFVRRFGIPQIGEF----YGATEGNSSLVnidnhvgACGFN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 344 PnwnRLPASdqaqLKSRQGVRtvgfseidvVDPESGRsVERD-------------GETVGEIVLRG-SSIMLGYLK---- 405
Cdd:cd05939 273 S---RILPS----VYPIRLIK---------VDEDTGE-LIRDsdglcipcqpgepGLLVGKIIQNDpLRRFDGYVNegat 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 406 NPIGTQNSFKNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVvarpdefWG-ETP 482
Cdd:cd05939 336 NKKIARDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVV-------YGvEVP 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222924 483 caFVSLKPGLTR--KPTDKEIIEY----CKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLK 538
Cdd:cd05939 409 --GVEGRAGMAAivDPERKVDLDRfsavLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
185-537 |
4.23e-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: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRgifvmTLDSLTDWAVP--------KTPVYlwTLPIFHANGW-TYP-WGIAAVGGTNV 254
Cdd:cd17645 105 DLAYVIYTSGSTGLPKGVMIEHH-----NLVNLCEWHRPyfgvtpadKSLVY--ASFSFDASAWeIFPhLTAGAALHVVP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 255 CVRKLHAPSIYHLIRDHGVTHMY-GAPIVLQILSASQESDQPLkspvnfLTAGSsppatVLLRAESLGFIVSHGYGLTET 333
Cdd:cd17645 178 SERRLDLDALNDYFNQEGITISFlPTGAAEQFMQLDNQSLRVL------LTGGD-----KLKKIERKGYKLVNNYGPTEN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 334 AGVIVSCAWKPNWNRLPASdqaqlKSRQGVRTVGFSEIDVVDPESgrsverdgeTVGEIVLRGSSIMLGYLKNPIGTQNS 413
Cdd:cd17645 247 TVVATSFEIDKPYANIPIG-----KPIDNTRVYILDEALQLQPIG---------VAGELCIAGEGLARGYLNRPELTAEK 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 414 FKNGWFF-------TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFV 486
Cdd:cd17645 313 FIVHPFVpgermyrTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYV 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15222924 487 SLKpgltRKPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:cd17645 393 TAP----EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
370-486 |
6.57e-12 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 68.11 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 370 EIDVVDpESGRSV-ERdgeTVGEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHgDGYLEIKDRSKDVIISGGE 448
Cdd:PRK09192 395 EIEIRN-EAGMPLpER---VVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLL-DGYLYITGRAKDLIIINGR 469
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15222924 449 NVSSVEVEAVLYTNPAVN--EAAVVARPDEfWGETPCAFV 486
Cdd:PRK09192 470 NIWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGEKIVLLV 508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
167-532 |
8.58e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.45 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 167 LITRGNPDFKWIRPGSEWDP---IVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPI-FHANGWTY 242
Cdd:PRK12316 3176 DLDRGDENYAEANPAIRTMPenlAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFsFDVFVEEL 3255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 243 PWGIAaVGGTNVC--VRKLHAPSIY-HLIRDHGVTHMYGAPIVLQILSASqESDQPLKSPVNFLTAGSSPPATVLLRAeS 319
Cdd:PRK12316 3256 FWPLM-SGARVVLagPEDWRDPALLvELINSEGVDVLHAYPSMLQAFLEE-EDAHRCTSLKRIVCGGEALPADLQQQV-F 3332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 320 LGFIVSHGYGLTETagVIVSCAWKPNWnrlPASDQAQLKSRQGVRTVGFSEIDVVDPESGrsverdgeTVGEIVLRGSSI 399
Cdd:PRK12316 3333 AGLPLYNLYGPTEA--TITVTHWQCVE---EGKDAVPIGRPIANRACYILDGSLEPVPVG--------ALGELYLGGEGL 3399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 400 MLGYLKNPIGTQNSFKNGWFF-------TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVA 472
Cdd:PRK12316 3400 ARGYHNRPGLTAERFVPDPFVpgerlyrTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA 3479
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 473 RPdefwGETPCAFVSLKPGLTRKPtdKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKI 532
Cdd:PRK12316 3480 VD----GRQLVAYVVPEDEAGDLR--EALKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
185-468 |
1.63e-11 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 66.76 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWT----YPW--GIAAVGGTNvcvrK 258
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNsctlFPLlsGVPVVFAYN----P 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 LHAPSIYHLIRDHGVTHMYGAPIVLQ-ILSASQESDQPLKSPVNFLTAGSSPPATvlLRAESLGF----IVSHGYGLTET 333
Cdd:PRK06334 260 LYPKKIVEMIDEAKVTFLGSTPVFFDyILKTAKKQESCLPSLRFVVIGGDAFKDS--LYQEALKTfphiQLRQGYGTTEC 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 334 AGVIVscawkpnwnrLPASDQAQLKSRQGVRTVGFsEIDVVDPESGRSVErDGEtVGEIVLRGSSIMLGYLKNPIGTQNS 413
Cdd:PRK06334 338 SPVIT----------INTVNSPKHESCVGMPIRGM-DVLIVSEETKVPVS-SGE-TGLVLTRGTSLFSGYLGEDFGQGFV 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 414 FKNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEA 468
Cdd:PRK06334 405 ELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA 461
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
421-541 |
1.68e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 66.90 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 421 TGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLT------R 494
Cdd:PRK10524 477 TFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSladreaR 556
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15222924 495 KPTDKEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKEIA 541
Cdd:PRK10524 557 LALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIA 603
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
189-458 |
2.00e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 66.36 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 189 VNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGG-------TNVCVRKlha 261
Cdd:cd05908 111 IQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGmnqylmpTRLFIRR--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 262 PSIY-HLIRDHGVTHM----YGAPIVLQILSASQESDQPLkSPVNFLTAGSSPPATVLLRaESLGFIVSHG--------- 327
Cdd:cd05908 188 PILWlKKASEHKATIVsspnFGYKYFLKTLKPEKANDWDL-SSIRMILNGAEPIDYELCH-EFLDHMSKYGlkrnailpv 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 YGLTE-TAGVIVSCAWKP------------NWNRLPASDQaqlKSRQGVRTV------GFSEIDVVDPESGrsvERDGET 388
Cdd:cd05908 266 YGLAEaSVGASLPKAQSPfktitlgrrhvtHGEPEPEVDK---KDSECLTFVevgkpiDETDIRICDEDNK---ILPDGY 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15222924 389 VGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHgDGYLEIKDRSKDVIISGGENVSSVEVEAV 458
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERI 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
189-539 |
3.56e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.35 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 189 VNYTSGTTSSPKGVVHCHRGIfVMTLDSLTD-WAVPKTPVYLWTLPI-FHANGWTYPWGIaaVGGtnvCVRKLHAPS--- 263
Cdd:PRK05691 1278 VIYTSGSTGQPKGVGNTHAAL-AERLQWMQAtYALDDSDVLMQKAPIsFDVSVWECFWPL--ITG---CRLVLAGPGehr 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 264 ----IYHLIRDHGVTHMYGAPIVLQILSasqesDQPLKSPVNFL----TAGSSPPATVLLRA-ESLGFIVSHG-YGLTET 333
Cdd:PRK05691 1352 dpqrIAELVQQYGVTTLHFVPPLLQLFI-----DEPLAAACTSLrrlfSGGEALPAELRNRVlQRLPQVQLHNrYGPTET 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 334 AgvIVSCAWkpnwnRLPASDQAqlKSRQGvRTVGFSEIDVVDPESGRSverDGETVGEIVLRGSSIMLGYLKNPIGTQNS 413
Cdd:PRK05691 1427 A--INVTHW-----QCQAEDGE--RSPIG-RPLGNVLCRVLDAELNLL---PPGVAGELCIGGAGLARGYLGRPALTAER 1493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 414 F------KNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARpDEFWGETPCAF 485
Cdd:PRK05691 1494 FvpdplgEDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGY 1572
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15222924 486 VSLKPGLTRKPTDkeIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:PRK05691 1573 YTGEAGQEAEAER--LKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
177-532 |
3.71e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 66.34 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 177 WIRPGSEWDPIV---------VNYTSGTTSSPKGVVHCHrGIFVMTLDSLTDW--AVPKTPVYLWTLPIFHANGWTYPWg 245
Cdd:PRK12467 1702 WLEGYSDSNPAVnlapqnlayVIYTSGSTGRPKGAGNRH-GALVNRLCATQEAyqLSAADVVLQFTSFAFDVSVWELFW- 1779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 246 iAAVGGTNVCVRklhAPSI-------YHLIRDHGVTHMYGAPIVLQILSASQESD-QPLKSPVNFLTAGSSPPATVLLRA 317
Cdd:PRK12467 1780 -PLINGARLVIA---PPGAhrdpeqlIQLIERQQVTTLHFVPSMLQQLLQMDEQVeHPLSLRRVVCGGEALEVEALRPWL 1855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 318 ESLGFI-VSHGYGLTETAgvIVSCAWKpnwnrlpasdqaqlksrqgvrtvgfseIDVVDPESGRSVE------------R 384
Cdd:PRK12467 1856 ERLPDTgLFNLYGPTETA--VDVTHWT---------------------------CRRKDLEGRDSVPigqpianlstyiL 1906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 385 DGE-------TVGEIVLRGSSIMLGYLKNPIGTQNSF------KNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGEN 449
Cdd:PRK12467 1907 DASlnpvpigVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFR 1986
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 450 VSSVEVEAVLYTNPAVNEAAVVARpDEFWGETPCAFV-----SLKPGLTRKPTDKEII-EYCKYKMPRYMAPKTVSFLEE 523
Cdd:PRK12467 1987 IELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVvptdpGLVDDDEAQVALRAILkNHLKASLPEYMVPAHLVFLAR 2065
|
....*....
gi 15222924 524 LPKTSTGKI 532
Cdd:PRK12467 2066 MPLTPNGKL 2074
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
177-449 |
1.99e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 63.21 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 177 WIRPGSEWDPIV-VNYTSGTTSSPKGVVHCHRGifVMT-----LDSL----TDWAVPktpvylWtLPIFHANGWTYPWgI 246
Cdd:PRK07769 172 WVPPEANEDTIAyLQYTSGSTRIPAGVQITHLN--LPTnvlqvIDALegqeGDRGVS------W-LPFFHDMGLITVL-L 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 247 AAVGGTNVC-------VRKlhaPS--IYHLIRDHGVTH--MYGAPIVLQILSAS----QESDQPLK-SPVNFLTAGSSPP 310
Cdd:PRK07769 242 PALLGHYITfmspaafVRR---PGrwIRELARKPGGTGgtFSAAPNFAFEHAAArglpKDGEPPLDlSNVKGLLNGSEPV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 311 ATVLLRA-----ESLGF---IVSHGYGLTEtAGVIVSCAWKPNWNRLPASDQAQLKSRQGVRT---------------VG 367
Cdd:PRK07769 319 SPASMRKfneafAPYGLpptAIKPSYGMAE-ATLFVSTTPMDEEPTVIYVDRDELNAGRFVEVpadapnavaqvsagkVG 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 368 FSEIDV-VDPESGRSVErDGEtVGEIVLRGSSIMLGYLKNPIGTQNSFKN------------------GWFFTGDLGVIH 428
Cdd:PRK07769 398 VSEWAViVDPETASELP-DGQ-IGEIWLHGNNIGTGYWGKPEETAATFQNilksrlseshaegapddaLWVRTGDYGVYF 475
|
330 340
....*....|....*....|.
gi 15222924 429 gDGYLEIKDRSKDVIISGGEN 449
Cdd:PRK07769 476 -DGELYITGRVKDLVIIDGRN 495
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
185-458 |
9.20e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 61.19 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 185 DPIVVNYTSGTTSSPKGVVHCHRGIF-----VMTLDSLTDWAVPKTPVYLWTLPIFHANGWTYPWGIAAVGGT------- 252
Cdd:PLN02614 224 DICTIMYTSGTTGDPKGVMISNESIVtliagVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAigfwrgd 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 253 -NVCVRKLH--APSIYHLI------------------------------------RDHGVTHMYGAPIVLQILSAsqESD 293
Cdd:PLN02614 304 vKLLIEDLGelKPTIFCAVprvldrvysglqkklsdggflkkfvfdsafsykfgnMKKGQSHVEASPLCDKLVFN--KVK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 294 QPLKSPVNFLTAGSSPPATvllRAESLGFIVS-----HGYGLTET-AGVIVScawkpnwnrLPasDQAQLksrqgVRTVG 367
Cdd:PLN02614 382 QGLGGNVRIILSGAAPLAS---HVESFLRVVAcchvlQGYGLTEScAGTFVS---------LP--DELDM-----LGTVG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 368 FSEIDV-VDPESGRSVERD--GETV-GEIVLRGSSIMLGYLKNPIGTQNSFKNGWFFTGDLGVIHGDGYLEIKDRSKDVI 443
Cdd:PLN02614 443 PPVPNVdIRLESVPEMEYDalASTPrGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIF 522
|
330
....*....|....*.
gi 15222924 444 -ISGGENVSSVEVEAV 458
Cdd:PLN02614 523 kLSQGEYVAVENIENI 538
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
177-535 |
1.27e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 177 WIRPGSEWDPIV-VNYTSGTTSSPKGVVHCHR-------------GIFVMTLDSLTDWavpktpvylwtLPIFHANGwty 242
Cdd:PRK05691 158 WQEPALQPDDIAfLQYTSGSTALPKGVQVSHGnlvaneqlirhgfGIDLNPDDVIVSW-----------LPLYHDMG--- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 243 pwgiaAVGG------TNV-CVrkLHAPSiYHL---------IRDHGVThMYGAPIVLQILSASQESDQPLKS------PV 300
Cdd:PRK05691 224 -----LIGGllqpifSGVpCV--LMSPA-YFLerplrwleaISEYGGT-ISGGPDFAYRLCSERVSESALERldlsrwRV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 301 NFltAGSSPpatvlLRAESL----------GFIVSH---GYGLTEtAGVIVS--------CAWKPNWNRLpASDQAQLKS 359
Cdd:PRK05691 295 AY--SGSEP-----IRQDSLerfaekfaacGFDPDSffaSYGLAE-ATLFVSggrrgqgiPALELDAEAL-ARNRAEPGT 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 360 RQGVRTVGFS----EIDVVDPESGRsvERDGETVGEIVLRGSSIMLGYLKNPIGTQNSFKN----GWFFTGDLGVIHgDG 431
Cdd:PRK05691 366 GSVLMSCGRSqpghAVLIVDPQSLE--VLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhdgrTWLRTGDLGFLR-DG 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 432 YLEIKDRSKDVIISGGENVSSVEVEAVLYTN-PAVNEAAVVARPDEFWGETPCAFV---------SLKPGLTRKPTDKEI 501
Cdd:PRK05691 443 ELFVTGRLKDMLIVRGHNLYPQDIEKTVEREvEVVRKGRVAAFAVNHQGEEGIGIAaeisrsvqkILPPQALIKSIRQAV 522
|
410 420 430
....*....|....*....|....*....|....*.
gi 15222924 502 IEYCKykmpryMAPKTVSFLE--ELPKTSTGKIIKS 535
Cdd:PRK05691 523 AEACQ------EAPSVVLLLNpgALPKTSSGKLQRS 552
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
36-540 |
1.36e-08 |
|
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: 57.67 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 36 GNSTVYTWRETNHRCLCVASALSSIGIGRSDVVSVLSANTPEMYELQFSVPMSGAILNNINTRLDARTVSVLLRHCESKL 115
Cdd:cd05943 94 GERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 116 LFVD--FFYSDLAVEAITMLLN-----PPILVLIANEEEEEGGAEVTERSKFCYLYSDLITRGN---PDFKWIRPGsewD 185
Cdd:cd05943 174 LFAVdaYTYNGKRHDVREKVAElvkglPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDFLATGAageLEFEPLPFD---H 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 186 PIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLtdwavpktpvylwtlpIFHAN-------------GW-TYPWGIA--AV 249
Cdd:cd05943 251 PLYILYSSGTTGLPKCIVHGAGGTLLQHLKEH----------------ILHCDlrpgdrlfyyttcGWmMWNWLVSglAV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 250 GGTNVC------VRKLHApsIYHLIRDHGVTHM-YGAPivlqILSASQESDQPLKSPVNF------LTAGSSppatvlLR 316
Cdd:cd05943 315 GATIVLydgspfYPDTNA--LWDLADEEGITVFgTSAK----YLDALEKAGLKPAETHDLsslrtiLSTGSP------LK 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 317 AESLGFIVSHGY---------GLTETAGVIVSCAwkPNWNRLPASDQAqlksrqgvRTVGFSeIDVVDPEsGRSVErdGE 387
Cdd:cd05943 383 PESFDYVYDHIKpdvllasisGGTDIISCFVGGN--PLLPVYRGEIQC--------RGLGMA-VEAFDEE-GKPVW--GE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 388 tVGEIVLRGS--SIMLGYLKNPIGTQnsFKNGWFFT-------GDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAV 458
Cdd:cd05943 449 -KGELVCTKPfpSMPVGFWNDPDGSR--YRAAYFAKypgvwahGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRV 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 459 LYTNPAVNEAAVVARPDEFWGETPCAFVSLKPGLTrkpTDKEIIEYCKYKMPRYMAPKTV--SFLE--ELPKTSTGKIIK 534
Cdd:cd05943 526 VEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVE---LDDELRKRIRSTIRSALSPRHVpaKIIAvpDIPRTLSGKKVE 602
|
....*.
gi 15222924 535 SLLKEI 540
Cdd:cd05943 603 VAVKKI 608
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
373-457 |
1.78e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 57.26 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 373 VVDPESGRsvERDGETVGEIVLRGSSIMLGYLKNPIGTQNSF------------KNGWFFTGDLGVIHgDGYLEIKDRSK 440
Cdd:PRK05850 383 IVDPDTCI--ECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtpEGPWLRTGDLGFIS-EGELFIVGRIK 459
|
90
....*....|....*..
gi 15222924 441 DVIISGGENVSSVEVEA 457
Cdd:PRK05850 460 DLLIVDGRNHYPDDIEA 476
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
191-475 |
2.13e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 56.98 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHR---GIFVMTLDSLTDWAVPKTPVYLWTLP---------IFHANGWTypwgiaavGGTnvcvrk 258
Cdd:PRK12582 227 FTSGSTGMPKAVINTQRmmcANIAMQEQLRPREPDPPPPVSLDWMPwnhtmggnaNFNGLLWG--------GGT------ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 259 LH-----------APSIYHLiRDHGVTHMYGAPIVLQILSASQESDQPLKSpvNFLT-------AGSSPPATVLLRAESL 320
Cdd:PRK12582 293 LYiddgkplpgmfEETIRNL-REISPTVYGNVPAGYAMLAEAMEKDDALRR--SFFKnlrlmayGGATLSDDLYERMQAL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 321 G-------FIVSHGYGLTETAGVIVSCAWKPNwnrlpasdqaqlksRQGvrTVGFseidvvdPESGrsVERDGETVG--- 390
Cdd:PRK12582 370 AvrttghrIPFYTGYGATETAPTTTGTHWDTE--------------RVG--LIGL-------PLPG--VELKLAPVGdky 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 391 EIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVihgdgYLEIKDRSKDVIISG--GEN----------VSSVEVEA 457
Cdd:PRK12582 425 EVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAAR-----FVDPDDPEKGLIFDGrvAEDfklstgtwvsVGTLRPDA 499
|
330
....*....|....*...
gi 15222924 458 VLYTNPAVNEaAVVARPD 475
Cdd:PRK12582 500 VAACSPVIHD-AVVAGQD 516
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
191-475 |
2.89e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 56.52 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGIF--VMTL-DSLTDWAVPKTP--VYLWTLPIFHangwtypwgIAAVGGTNVCV--------- 256
Cdd:PTZ00216 271 YTSGTTGDPKGVMHTHGSLTagILALeDRLNDLIGPPEEdeTYCSYLPLAH---------IMEFGVTNIFLargaligfg 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 257 --RKLHAPSIyhliRDHGVTHMY------GAPIVLQILSASQESDQP----LK---------SPVNFLTAGS-------- 307
Cdd:PTZ00216 342 spRTLTDTFA----RPHGDLTEFrpvfliGVPRIFDTIKKAVEAKLPpvgsLKrrvfdhayqSRLRALKEGKdtpywnek 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 308 --SPPATVL-------------LRAESLGFI------VSHGYGLTETagviVSCAWKPNWNRLPASDQAQLksrqgVRTV 366
Cdd:PTZ00216 418 vfSAPRAVLggrvramlsgggpLSAATQEFVnvvfgmVIQGWGLTET----VCCGGIQRTGDLEPNAVGQL-----LKGV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 367 gfsEIDVVDPESGRSVERDgETVGEIVLRGSSIMLGYLKNPIGTQNSF-KNGWFFTGDLGVIHGDGYLEIKDR----SKD 441
Cdd:PTZ00216 489 ---EMKLLDTEEYKHTDTP-EPRGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRvkalAKN 564
|
330 340 350
....*....|....*....|....*....|....*.
gi 15222924 442 VIisgGENVSSVEVEAVLYTNPAV--NEAAVVARPD 475
Cdd:PTZ00216 565 CL---GEYIALEALEALYGQNELVvpNGVCVLVHPA 597
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
191-448 |
1.40e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 54.34 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGIFvMTLDSLTDWAV-----PKTpvYLWTLPIFHANGWTYPWGIAAVGGT------------- 252
Cdd:PTZ00342 311 YTSGTSGKPKGVMLSNKNLY-NTVVPLCKHSIfkkynPKT--HLSYLPISHIYERVIAYLSFMLGGTiniwskdinyfsk 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 253 NVCVRK----LHAPSIYHLIRDHGVTHMYGAP-----IVLQILSASQESD---------------QPLKSPVN-----FL 303
Cdd:PTZ00342 388 DIYNSKgnilAGVPKVFNRIYTNIMTEINNLPplkrfLVKKILSLRKSNNnggfskflegithisSKIKDKVNpnlevIL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 304 TAGSSPPATVllrAESLGFIVS----HGYGLTETAGVI-VSCAWKPNWNRL--PASDQAQLKsrqgVRTvgFSEIDVVDp 376
Cdd:PTZ00342 468 NGGGKLSPKI---AEELSVLLNvnyyQGYGLTETTGPIfVQHADDNNTESIggPISPNTKYK----VRT--WETYKATD- 537
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222924 377 esgrSVERdgetvGEIVLRGSSIMLGYLKNPIGTQNSFKN-GWFFTGDLGVIHGDGYLEIKDRSKDVI-ISGGE 448
Cdd:PTZ00342 538 ----TLPK-----GELLIKSDSIFSGYFLEKEQTKNAFTEdGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGE 602
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
373-472 |
2.20e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 53.59 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 373 VVDPESGRSVeRDGEtVGEIVLRGSSIMLGYLKNPIGTQNSFKN-------------------GWFFTGDLGViHGDGYL 433
Cdd:PRK12476 415 IVDPDTGAEL-PDGE-VGEIWLHGDNIGRGYWGRPEETERTFGAklqsrlaegshadgaaddgTWLRTGDLGV-YLDGEL 491
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15222924 434 EIKDRSKDVIISGGENVSSVEVEA-VLYTNPAVNEAAVVA 472
Cdd:PRK12476 492 YITGRIADLIVIDGRNHYPQDIEAtVAEASPMVRRGYVTA 531
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
401-539 |
2.44e-07 |
|
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: 53.45 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 401 LGYLKNPIGTQ-----NSFKNG--WFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAV--V 471
Cdd:cd05938 363 LGYAGDKEQTEkkllrDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygV 442
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15222924 472 ARPDeFWGETPCAFVSLKPGLTrkpTD-KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLLKE 539
Cdd:cd05938 443 TVPG-HEGRIGMAAVKLKPGHE---FDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVE 507
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
189-540 |
1.76e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 189 VNYTSGTTSSPKGVVHCHRGIFVMTL-----------DSLTDWAVPKTPVYLWTL---PIFHANGWTYPWGIAavggtnv 254
Cdd:PRK05691 3874 VIYTSGSTGLPKGVMVEQRGMLNNQLskvpylalseaDVIAQTASQSFDISVWQFlaaPLFGARVEIVPNAIA------- 3946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 255 cvrklHAP-SIYHLIRDHGVTHMYGAPIVLQILSASQEsdQPLKSPVNFLTAGSS-PP---ATVLLRAESLGFIVSHG-- 327
Cdd:PRK05691 3947 -----HDPqGLLAHVQAQGITVLESVPSLIQGMLAEDR--QALDGLRWMLPTGEAmPPelaRQWLQRYPQIGLVNAYGpa 4019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 ----------YGLTETAGVIVSCAWKPNWNRLPASDQAQLKSRQGvrtvgfseidvvdpesgrsverdgeTVGEIVLRGS 397
Cdd:PRK05691 4020 ecsddvaffrVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLG-------------------------AVGELCVAGT 4074
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 398 SIMLGYLKNPIGTQNSFKNGWF--------FTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAA 469
Cdd:PRK05691 4075 GVGRGYVGDPLRTALAFVPHPFgapgerlyRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA 4154
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15222924 470 V--VARPDefwGETPCAFvsLKPGLTRKpTDKEIIEYCKYKM----PRYMAPKTVSFLEELPKTSTGKIIKSLLKEI 540
Cdd:PRK05691 4155 VavQEGVN---GKHLVGY--LVPHQTVL-AQGALLERIKQRLraelPDYMVPLHWLWLDRLPLNANGKLDRKALPAL 4225
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
192-537 |
4.58e-06 |
|
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: 49.01 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 192 TSGTTSSPKGVVHCHRGI--FVMTLDSLTDwaVPKTPVYLWTLPIFHANGWTYPWGIAAVGGTNV----CVRKLHAPSIY 265
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCIlpNIQHFRSLFN--ITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLivptSVKVLPSKLAD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 266 HLIRDHGVTHMYGAPIVLQILSASQESDQPLK--SPVNFLTAGSSP-PATVLLRA---ESLGFIVSHGYGLTETagvivs 339
Cdd:cd17654 204 ILFKRHRITVLQATPTLFRRFGSQSIKSTVLSatSSLRVLALGGEPfPSLVILSSwrgKGNRTRIFNIYGITEV------ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 340 CAWKpNWNRLPASDQAQlksrQGVRTVGFSEIDVVDpESGRSVErdGETVGEIVLRGSsIMLGYLKNPIGTqnsfkngWF 419
Cdd:cd17654 278 SCWA-LAYKVPEEDSPV----QLGSPLLGTVIEVRD-QNGSEGT--GQVFLGGLNRVC-ILDDEVTVPKGT-------MR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 420 FTGDLgVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVnEAAVVARPDEfwgETPCAFVSLKPglTRKPTDK 499
Cdd:cd17654 342 ATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGES--SSSRIHK 414
|
330 340 350
....*....|....*....|....*....|....*...
gi 15222924 500 EIIeycKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:cd17654 415 ELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
186-537 |
1.17e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 48.20 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 186 PIVVNYTSGTTSSPKGVVHCHRGIFVMTLDSLTDWAVPKTPVYLWTlpifHAN-GWT----YPWGIAAVGGTNV-----C 255
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFS----HSSiGWVsfhgFLYGSLSLGNTFVmfeggI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 256 VRKLHAPS-IYHLIRDHGVTHMYGAPIVLQILSASQESDQPLKSPVNF------LTAGSSPPATVLLRAES-LGFIVSHG 327
Cdd:PTZ00237 332 IKNKHIEDdLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKYDLsnlkeiWCGGEVIEESIPEYIENkLKIKSSRG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 328 YGLTETAgvivsCAWKPNWNRLPASDQAQLKSRQGVRTVGFSEIDVVDPESgrsverdgeTVGEIVLR---GSSIMLGYL 404
Cdd:PTZ00237 412 YGQTEIG-----ITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVN---------EIGEVAFKlpmPPSFATTFY 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 405 KNPIGTQNSFKN--GWFFTGDLGVIHGDGYLEIKDRSKDVIISGGENVSSVEVEAVLYTNPAVNEAAVVARPDEFWGETP 482
Cdd:PTZ00237 478 KNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVP 557
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 483 CAFVSLKPGLTRKPTD-----KEIIEYCKYKMPRYMAPKTVSFLEELPKTSTGKIIKSLL 537
Cdd:PTZ00237 558 IGLLVLKQDQSNQSIDlnklkNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
191-423 |
1.20e-05 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 48.20 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 191 YTSGTTSSPKGVVHCHRGI---FVMTLDSLTDWAvPKTPVYLWTLP---------IFHA---NGWTY--PWGIAAVGGTN 253
Cdd:cd05921 172 FTSGSTGLPKAVINTQRMLcanQAMLEQTYPFFG-EEPPVLVDWLPwnhtfggnhNFNLvlyNGGTLyiDDGKPMPGGFE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 254 VCVRKLH--APSIYhlirdhgvthmYGAPIVLQILSASQESDQPLK----SPVNFLT-AGSSPPATVLLRAESLGfiVSH 326
Cdd:cd05921 251 ETLRNLReiSPTVY-----------FNVPAGWEMLVAALEKDEALRrrffKRLKLMFyAGAGLSQDVWDRLQALA--VAT 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222924 327 ---------GYGLTETAGVIVSCAWkpnwnrlpasdqaqLKSRQGVRTVGFSEIDVvdpesgRSVERDGETvgEIVLRGS 397
Cdd:cd05921 318 vgeripmmaGLGATETAPTATFTHW--------------PTERSGLIGLPAPGTEL------KLVPSGGKY--EVRVKGP 375
|
250 260
....*....|....*....|....*..
gi 15222924 398 SIMLGYLKNPIGTQNSF-KNGWFFTGD 423
Cdd:cd05921 376 NVTPGYWRQPELTAQAFdEEGFYCLGD 402
|
|
| |
