|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
13-550 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 794.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 13 AYQYPLLIKSLMLSGRRYEKSHEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIG 92
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 93 AVLHTINIRLSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAEksAELPGLVGEYESLLAAASPR 172
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPA--APLAPEVGEYEELLAAASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 173 YDFPDFDENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATM 252
Cdd:PRK06187 159 FDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLK-------LSRDDVYLVIVPMFHVHAWGLPYLALM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 253 LGVKQVYPGRYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWK-VIIGGSALNRSLYEAAKAR-GIQLTA 330
Cdd:PRK06187 232 AGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRlVIYGGAALPPALLREFKEKfGIDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 331 AYGMSETCPLISCAYLNDELLAgsedeRTTYRIKAGVPVPLVDAAIMDEQGRFLPADGESQGELVLRSPWLTQGYFREPE 410
Cdd:PRK06187 312 GYGMTETSPVVSVLPPEDQLPG-----QWTKRRSAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 411 RGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVV 490
Cdd:PRK06187 387 ATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 491 REGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQWQ 550
Cdd:PRK06187 467 KPGATLDAKELRAFLR-----GRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
23-543 |
0e+00 |
|
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: 769.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 23 LMLSGRRYEKSHEIVYRD----QVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTI 98
Cdd:cd12119 1 LLEHAARLHGDREIVSRThegeVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 99 NIRLSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAEKSAELPGLVGEYESLLAAASPRYDFPDF 178
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 179 DENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGsldsiRLLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQV 258
Cdd:cd12119 161 DENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDG-----LGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 259 YPGRY-DPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVD-FKGWKVIIGGSALNRSLYEAAKARGIQLTAAYGMSE 336
Cdd:cd12119 236 LPGPYlDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDlSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 337 TCPLISCAYLNDELLAGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADGESQGELVLRSPWLTQGYFREPERGEELW 416
Cdd:cd12119 316 TSPLGTVARPPSEHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEALT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 417 RGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQL 496
Cdd:cd12119 396 EDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATV 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15599119 497 DARGLKEHLKPFVeqgniNKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd12119 476 TAEELLEFLADKV-----AKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
17-543 |
3.53e-155 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 454.93 E-value: 3.53e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 17 PLLIKSLMLSGRRYEKSHEIVYR----DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIG 92
Cdd:PRK07008 9 PLLISSLIAHAARHAGDTEIVSRrvegDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 93 AVLHTINIRLSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAEKSAELPGLVGeYESLLAAASPR 172
Cdd:PRK07008 89 AVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTFLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTPLLC-YETLVGAQDGD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 173 YDFPDFDENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMAstigsLDSIRLLGTSDVYMPITPMFHVHAWGTPYVATM 252
Cdd:PRK07008 168 YDWPRFDENQASSLCYTSGTTGNPKGALYSHRSTVLHAYGAA-----LPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 253 LGVKQVYPG-RYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWK-VIIGGSALNRSLYEA-AKARGIQLT 329
Cdd:PRK07008 243 TGAKLVLPGpDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRrTVIGGSACPPAMIRTfEDEYGVEVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 330 AAYGMSETCPLISCAYLNDELLAGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADGESQGELVLRSPWLTQGYFRep 409
Cdd:PRK07008 323 HAWGMTEMSPLGTLCKLKWKHSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWDGKAFGDLQVRGPWVIDRYFR-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 410 eRGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLV 489
Cdd:PRK07008 401 -GDASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15599119 490 VREGQQLDarglKEHLKPFVEqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK07008 480 KRPGAEVT----REELLAFYE-GKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
16-543 |
6.18e-139 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 413.38 E-value: 6.18e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 16 YPLLIKSLMLSGRRYEKSHEIVYRDQ----VRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMI 91
Cdd:PRK06018 8 WPLLCHRIIDHAARIHGNREVVTRSVegpiVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 92 GAVLHTINIRLSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAEKSA-ELPGLVGeYESLLAAAS 170
Cdd:PRK06018 88 GAICHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPSVERYVVLTDAAHMPQtTLKNAVA-YEEWIAEAD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 171 PRYDFPDFDENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLaMASTIGSLDsirlLGTSDVYMPITPMFHVHAWGTPYVA 250
Cdd:PRK06018 167 GDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHAL-MANNGDALG----TSAADTMLPVVPLFHANSWGIAFSA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 251 TMLGVKQVYPG-RYDPELLVELWKREKVTFSHCVPTILQMV---MNARAAQGVDFKgwKVIIGGSALNRSLYEAAKARGI 326
Cdd:PRK06018 242 PSMGTKLVMPGaKLDGASVYELLDTEKVTFTAGVPTVWLMLlqyMEKEGLKLPHLK--MVVCGGSAMPRSMIKAFEDMGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 327 QLTAAYGMSETCPLISCAYLNDELLAGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADGESQGELVLRSPWLTQGYF 406
Cdd:PRK06018 320 EVRHAWGMTEMSPLGTLAALKPPFSKLPGDARLDVLQKQGYPPFGVEMKITDDAGKELPWDGKTFGRLKVRGPAVAAAYY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 407 RepERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFA 486
Cdd:PRK06018 400 R--VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLL 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599119 487 LLVVREGQQLDarglKEHLKPFVEqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK06018 478 IVQLKPGETAT----REEILKYMD-GKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
34-553 |
1.10e-136 |
|
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: 404.19 E-value: 1.10e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 34 HEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNH 113
Cdd:COG0318 15 RPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILED 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 114 AEDRFVLVnsefvplyqavagqlatveRTILLTDGAEksaelpglvGeyesllaaasprydfpdfdensiattfyttgtt 193
Cdd:COG0318 95 SGARALVT-------------------ALILYTSGTT---------G--------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 194 gNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWG-TPYVATMLGVKQVYPGRYDPELLVELW 272
Cdd:COG0318 114 -RPKGVMLTHRNLLANAAAIAAALG-------LTPGDVVLVALPLFHVFGLTvGLLAPLLAGATLVLLPRFDPERVLELI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCaylndel 350
Cdd:COG0318 186 ERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVTV------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 351 laGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPaDGEsQGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLD 430
Cdd:COG0318 259 --NPEDPGERRPGSVGRPLPGVEVRIVDEDGRELP-PGE-VGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 431 GMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfve 510
Cdd:COG0318 335 EDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLR---- 410
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15599119 511 qGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQWQEAG 553
Cdd:COG0318 411 -ERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
36-539 |
2.48e-108 |
|
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: 331.11 E-value: 2.48e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDqVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:cd17631 14 LVFGG-RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRfVLVNSEFVPLYqavagqlatvertillTDGAEksaelpGLvgeyesllaaasprydfpdfdensiattfyttgttgn 195
Cdd:cd17631 93 AK-VLFDDLALLMY----------------TSGTT------GR------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLamaSTIGSLDsirlLGTSDVYMPITPMFHVHAWGTPYVAT-MLGVKQVYPGRYDPELLVELWKR 274
Cdd:cd17631 113 PKGAMLTHRNLLWNAV---NALAALD----LGPDDVLLVVAPLFHIGGLGVFTLPTlLRGGTVVILRKFDPETVLDLIER 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKARGIQLTAAYGMSETCPLIScaylndelLAG 353
Cdd:cd17631 186 HRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIyGGAPMPERLLRALQARGVKFVQGYGMTETSPGVT--------FLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 354 SEDERTTYRiKAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMG 433
Cdd:cd17631 258 PEDHRRKLG-SAGRPVFFVEVRIVDPDGREVP-PGEV-GEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 434 FIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKPfveqgN 513
Cdd:cd17631 335 YLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRE-----R 409
|
490 500
....*....|....*....|....*.
gi 15599119 514 INKWAIPSQIAVVTDIPKTSVGKLDK 539
Cdd:cd17631 410 LARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
36-543 |
1.43e-104 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 324.98 E-value: 1.43e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDqVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK08162 37 VIHGD-RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFVPLYQAVAGQLAtvERTILLTDGAEKSAELPGLVG--EYESLLAAASPRYD--FPDfDE-NSIATTFYTT 190
Cdd:PRK08162 116 AKVLIVDTEFAEVAREALALLP--GPKPLVIDVDDPEYPGGRFIGalDYEAFLASGDPDFAwtLPA-DEwDAIALNYTSG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 191 GTTgNPKGVYFSHRQLVLHTLamaSTIGSLDsirlLGTSDVYMPITPMFHVHAWGTPY-VATMLGVkQVYPGRYDPELLV 269
Cdd:PRK08162 193 TTG-NPKGVVYHHRGAYLNAL---SNILAWG----MPKHPVYLWTLPMFHCNGWCFPWtVAARAGT-NVCLRKVDPKLIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 270 ELWKREKVTFSHCVPTILQMVMNARAA--QGVDFKgWKVIIGGSALNRSLYEAAKARGIQLTAAYGMSETC-PLISCAYl 346
Cdd:PRK08162 264 DLIREHGVTHYCGAPIVLSALINAPAEwrAGIDHP-VHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETYgPATVCAW- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 347 NDELLAGSEDERTTYRIKAGVPVPLVDA-AIMD-EQGRFLPADGESQGELVLRSPWLTQGYFREPERGEELWRGGWMHTG 424
Cdd:PRK08162 342 QPEWDALPLDERAQLKARQGVRYPLQEGvTVLDpDTMQPVPADGETIGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 425 DVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGL--- 501
Cdd:PRK08162 422 DLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIiah 501
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15599119 502 -KEHLKPFveqgninkwAIPSQIaVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK08162 502 cREHLAGF---------KVPKAV-VFGELPKTSTGKIQKFVLR 534
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
36-543 |
6.12e-104 |
|
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: 321.56 E-value: 6.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDqVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:cd12118 23 IVYGD-RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFvplyqavagqlatvertilltdgaeksaelpglvgEYESLLAAASPRYDF-PDFDENSIATTFYTTGTTG 194
Cdd:cd12118 102 AKVLFVDREF-----------------------------------EYEDLLAEGDPDFEWiPPADEWDPIALNYTSGTTG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKR 274
Cdd:cd12118 147 RPKGVVYHHRGAYLNALANILEWE-------MKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKVDAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVPTILQMVMNARAAQGVDFKGW-KVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLISCAYLNDELLAG 353
Cdd:cd12118 220 HKVTHFCGAPTVLNMLANAPPSDARPLPHRvHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYGPATVCAWKPEWDEL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 354 SEDERttYRIKA--GVPVPLVDAA--IMDEQGRFLPADGESQGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATL 429
Cdd:cd12118 300 PTEER--ARLKArqGVRYVGLEEVdvLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 430 DGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKPfv 509
Cdd:cd12118 378 HPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCRE-- 455
|
490 500 510
....*....|....*....|....*....|....
gi 15599119 510 eqgNINKWAIPSQIaVVTDIPKTSVGKLDKKRIR 543
Cdd:cd12118 456 ---HLAGFMVPKTV-VFGELPKTSTGKIQKFVLR 485
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
195-538 |
1.85e-92 |
|
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: 286.49 E-value: 1.85e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKR 274
Cdd:cd04433 14 KPKGVVLSHRNLLAAAAALAASGG-------LTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAALELIER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAYL-NDELL 351
Cdd:cd04433 87 EKVTILLGVPTLLARLLKAPESAGYDLSSLRALVsGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPdDDARK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 352 AGSederttyrikAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDG 431
Cdd:cd04433 167 PGS----------VGRPVPGVEVRIVDPDGGELP-PGEI-GELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 432 MGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKPfveq 511
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRE---- 310
|
330 340
....*....|....*....|....*..
gi 15599119 512 gNINKWAIPSQIAVVTDIPKTSVGKLD 538
Cdd:cd04433 311 -RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
40-448 |
1.81e-85 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 271.49 E-value: 1.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFV 119
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 120 LVNSEFVPLYQAVAGQLATVERTILLTDGAEKSAELPglvgEYESLLAAASPRYDFPDFDENSIAttfyttgttgNPKGV 199
Cdd:pfam00501 98 ITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP----LPEEAKPADVPPPPPPPPDPDDLAyiiytsgttgKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 200 YFSHRQLVlhtlAMASTIGSLDSIRL-LGTSDVYMPITPMFHVHAWGT-PYVATMLGVKQVYPG---RYDPELLVELWKR 274
Cdd:pfam00501 174 MLTHRNLV----ANVLSIKRVRPRGFgLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPgfpALDPAALLELIER 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCaylndellA 352
Cdd:pfam00501 250 YKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsGGAPLPPELARRFRELfGGALVNGYGLTETTGVVTT--------P 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 353 GSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADGEsQGELVLRSPWLTQGYFREPERGEE-LWRGGWMHTGDVATLDG 431
Cdd:pfam00501 322 LPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGE-PGELCVRGPGVMKGYLNDPELTAEaFDEDGWYRTGDLGRRDE 400
|
410
....*....|....*..
gi 15599119 432 MGFIEIRDRIKDVIKTG 448
Cdd:pfam00501 401 DGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
34-543 |
1.71e-84 |
|
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: 270.59 E-value: 1.71e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 34 HEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNH 113
Cdd:cd05936 15 KTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILND 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 114 AEDRFVLVNSEFvplyqavagqlatvertilltdgaeksaelpglvgeyESLLAAASPRYDFPDFDENSIATTFYTTGTT 193
Cdd:cd05936 95 SGAKALIVAVSF-------------------------------------TDLLAAGAPLGERVALTPEDVAVLQYTSGTT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 194 GNPKGVYFSHRQLVLHTLAMASTIGSLDSIRllgtsDVYMPITPMFHVHAWGTPYVA-TMLGVKQVYPGRYDPELLVELW 272
Cdd:cd05936 138 GVPKGAMLTHRNLVANALQIKAWLEDLLEGD-----DVVLAALPLFHVFGLTVALLLpLALGATIVLIPRFRPIGVLKEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAYLNDEL 350
Cdd:cd05936 213 RKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCIsGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPLDGPR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 351 LAGSederttyrikAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLD 430
Cdd:cd05936 293 KPGS----------IGIPLPGTEVKIVDDDGEELP-PGEV-GELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 431 GMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfve 510
Cdd:cd05936 361 EDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCR---- 436
|
490 500 510
....*....|....*....|....*....|...
gi 15599119 511 qGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05936 437 -EQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
26-548 |
3.16e-84 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 271.42 E-value: 3.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 26 SGRRYEKSHEIVYRDqVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPE 105
Cdd:PRK08316 20 SARRYPDKTALVFGD-RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 106 QILYTMNHAEDRFVLVNSEFVPLYQAVAgQLATVERTILltDGAEKSAELPGLVGEYESLLAAASPRYDFPDFDENSIAT 185
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAPTAEAAL-ALLPVDTLIL--SLVLGGREAPGGWLDFADWAEAGSVAEPDVELADDDLAQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 186 TFYTTGTTGNPKGVYFSHRQLVLHTLamaSTIGSLDsirlLGTSDVYMPITPMFH---VHAWGTPYVatMLGVKQVYPGR 262
Cdd:PRK08316 176 ILYTSGTESLPKGAMLTHRALIAEYV---SCIVAGD----MSADDIPLHALPLYHcaqLDVFLGPYL--YVGATNVILDA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 263 YDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGW-KVIIGGSALNRSLYEAAKAR--GIQLTAAYGMSETCP 339
Cdd:PRK08316 247 PDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLrKGYYGASIMPVEVLKELRERlpGLRFYNCYGQTEIAP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 340 LISCaylndeLLAGSEDERTTyriKAGVPVPLVDAAIMDEQGRFLPaDGEsQGELVLRSPWLTQGYFREPERGEELWRGG 419
Cdd:PRK08316 327 LATV------LGPEEHLRRPG---SAGRPVLNVETRVVDDDGNDVA-PGE-VGEIVHRSPQLMLGYWDDPEKTAEAFRGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 420 WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDAR 499
Cdd:PRK08316 396 WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15599119 500 GL----KEHLKPFveqgninkwAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQ 548
Cdd:PRK08316 476 ELiahcRARLAGF---------KVPKRVIFVDELPRNPSGKILKRELRERYAG 519
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
45-547 |
4.53e-81 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 264.72 E-value: 4.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVL-SEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNs 123
Cdd:PRK05620 40 TFAAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 efvplyQAVAGQLAT-------VERTILL--TDGAEKSAELPG--LVGEYESLLAAASPRYDFPDFDENSIATTFYTTGT 192
Cdd:PRK05620 119 ------PRLAEQLGEilkecpcVRAVVFIgpSDADSAAAHMPEgiKVYSYEALLDGRSTVYDWPELDETTAAAICYSTGT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 193 TGNPKGVYFSHRQLVLHTLAMASTigslDSIRLL-GTSdvYMPITPMFHVHAWGTPYVATMLGVKQVYPGR-YDPELLVE 270
Cdd:PRK05620 193 TGAPKGVVYSHRSLYLQSLSLRTT----DSLAVThGES--FLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPdLSAPTLAK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 271 LWKREKVTFSHCVPTI-LQMVMNARAAQGVDFKGWKVIIGGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAYLNd 348
Cdd:PRK05620 267 IIATAMPRVAHGVPTLwIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERyGVDVVHVWGMTETSPVGTVARPP- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 349 ellAG-SEDERTTYRIKAG-VPVPLvDAAIMDEqGRFLPADGESQGELVLRSPWLTQGYFREPE----------RGEELW 416
Cdd:PRK05620 346 ---SGvSGEARWAYRVSQGrFPASL-EYRIVND-GQVMESTDRNEGEIQVRGNWVTASYYHSPTeegggaastfRGEDVE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 417 RG-------GWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLV 489
Cdd:PRK05620 421 DAndrftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTV 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599119 490 VREGQQLD---ARGLKEHLKPfveqgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIA 547
Cdd:PRK05620 501 LAPGIEPTretAERLRDQLRD-----RLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLA 556
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
40-553 |
2.17e-73 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 244.25 E-value: 2.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFV 119
Cdd:COG0365 36 EERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 120 LVNSEFV---------PLYQAVAGQLATVERTILLtDGAEKSAELPGLVgEYESLLAAASPRYDFPDFDENSIAttfytt 190
Cdd:COG0365 116 ITADGGLrggkvidlkEKVDEALEELPSLEHVIVV-GRTGADVPMEGDL-DWDELLAAASAEFEPEPTDADDPLfilyts 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 191 gttgNPKGVYFSHRQLVLHTLAMASTIgsLDsirlLGTSDVYMPITPM-FHVHAWGTPYVATMLGVKQV-YPGRY---DP 265
Cdd:COG0365 194 gttgKPKGVVHTHGGYLVHAATTAKYV--LD----LKPGDVFWCTADIgWATGHSYIVYGPLLNGATVVlYEGRPdfpDP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 266 ELLVELWKREKVTFSHCVPTILQMVMNA--RAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLI 341
Cdd:COG0365 268 GRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGsAGEPLNPEVWEWWYEAvGVPIVDGWGQTETGGIF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 342 SCAYLNDELLAGSederttyrikAGVPVPLVDAAIMDEQGRFLPADGEsqGELVLRSPW--LTQGYFREPERGEELWRG- 418
Cdd:COG0365 348 ISNLPGLPVKPGS----------MGKPVPGYDVAVVDEDGNPVPPGEE--GELVIKGPWpgMFRGYWNDPERYRETYFGr 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 419 --GWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQL 496
Cdd:COG0365 416 fpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEP 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599119 497 DARgLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRiEIAQWQEAG 553
Cdd:COG0365 496 SDE-LAKELQAHVRE-ELGPYAYPREIEFVDELPKTRSGKIMRRLLR-KIAEGRPLG 549
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
19-543 |
2.35e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 239.81 E-value: 2.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 19 LIKSLMLSGRRYeKSHEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTI 98
Cdd:PRK07656 7 LPELLARAARRF-GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 99 NIRLSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAekSAELPGLVGEYESLLAAASPRYDFPDF 178
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEE--DDPHTEKMKTFTDFLAAGDPAERAPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 179 DENSIATTFYTTGTTGNPKGVYFSHRQLvlhtLAMASTIGSLDSIRllgTSDVYMPITPMFHVH----AWGTPYV--ATM 252
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHRQL----LSNAADWAEYLGLT---EGDRYLAANPFFHVFgykaGVNAPLMrgATI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 253 LGVKQvypgrYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQ-LT 329
Cdd:PRK07656 237 LPLPV-----FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVtGAASMPVALLERFESElGVDiVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 330 AAYGMSETCPLIScaylndelLAGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPAdGEsQGELVLRSPWLTQGYFREP 409
Cdd:PRK07656 312 TGYGLSEASGVTT--------FNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPV-GE-VGELLVRGPNVMKGYYDDP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 410 ERGEELWRG-GWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALL 488
Cdd:PRK07656 382 EATAAAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15599119 489 VVREGQQLDARGL----KEHLKpfveqgninKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK07656 462 VLKPGAELTEEELiaycREHLA---------KYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
45-544 |
5.84e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 236.98 E-value: 5.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSE 124
Cdd:PRK07786 44 TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 125 FVPLYQAVAGQLATVERTILLTDGAEKSaelpglVGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKGVYFSHR 204
Cdd:PRK07786 124 LAPVATAVRDIVPLLSTVVVAGGSSDDS------VLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 205 QLVlhtlamASTIGSLDSIRLLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQV-YP-GRYDPELLVELWKREKVTFSHC 282
Cdd:PRK07786 198 NLT------GQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTViYPlGAFDPGQLLDVLEAEKVTGIFL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 283 VPTILQMVMNARAAQGVDFK----GWKVIIGGSALNRSLYEAAKarGIQLTAAYGMSETCPlISCAYLNDELLA--GSed 356
Cdd:PRK07786 272 VPAQWQAVCAEQQARPRDLAlrvlSWGAAPASDTLLRQMAATFP--EAQILAAFGQTEMSP-VTCMLLGEDAIRklGS-- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 357 erttyrikAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIE 436
Cdd:PRK07786 347 --------VGKVIPTVAARVVDENMNDVPV-GEV-GEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 437 IRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGqqLDARGLKEhLKPFVEqGNINK 516
Cdd:PRK07786 417 VVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND--DAALTLED-LAEFLT-DRLAR 492
|
490 500
....*....|....*....|....*...
gi 15599119 517 WAIPSQIAVVTDIPKTSVGKLDKKRIRI 544
Cdd:PRK07786 493 YKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
42-543 |
2.31e-70 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 236.28 E-value: 2.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 42 VRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLV 121
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 122 NSEFVPL----YQAVAGQLATVERTILLTDGAEKSAELPGL-------VGEYESLLAAASPRYDF-PDFDE-NSIATTFY 188
Cdd:PLN02479 124 DQEFFTLaeeaLKILAEKKKSSFKPPLLIVIGDPTCDPKSLqyalgkgAIEYEKFLETGDPEFAWkPPADEwQSIALGYT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 189 TTGTTgNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELL 268
Cdd:PLN02479 204 SGTTA-SPKGVVLHHRGAYLMALSNALIWG-------MNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNICLRQVTAKAI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 269 VELWKREKVTFSHCVPTILQMVMNARAAQGVD--FKGWKVIIGGSALNRSLYEAAKARGIQLTAAYGMSETC-PLISCAY 345
Cdd:PLN02479 276 YSAIANYGVTHFCAAPVVLNTIVNAPKSETILplPRVVHVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETYgPSTVCAW 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 346 LN--DELlagSEDERTTYRIKAGVP-VPLVDAAIMDEQ-GRFLPADGESQGELVLRSPWLTQGYFREPERGEELWRGGWM 421
Cdd:PLN02479 356 KPewDSL---PPEEQARLNARQGVRyIGLEGLDVVDTKtMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWF 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 422 HTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREG-QQLDARG 500
Cdd:PLN02479 433 HSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGvDKSDEAA 512
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15599119 501 LKEHLKPFVEQGNINKWaIPSQIaVVTDIPKTSVGKLDKKRIR 543
Cdd:PLN02479 513 LAEDIMKFCRERLPAYW-VPKSV-VFGPLPKTATGKIQKHVLR 553
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
19-546 |
3.03e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 228.62 E-value: 3.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 19 LIKSLMLSGRRYEKSHEIVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTI 98
Cdd:PRK06145 4 LSASIAFHARRTPDRAALVYRDQ-EISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 99 NIRLSPEQILYTMNHAEDRFVLVNSEFvplyqavAGQLATVERTILLTDGAEKSAELPGLVGEYESLLAAASPrydfpdf 178
Cdd:PRK06145 83 NYRLAADEVAYILGDAGAKLLLVDEEF-------DAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAP------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 179 deNSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGSLDSIRLLgtsdvymPITPMFHVHAWGTPYVAT-----ML 253
Cdd:PRK06145 149 --TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLL-------VVGPLYHVGAFDLPGIAVlwvggTL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 254 GVKQvypgRYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSALNRSLYEAAKAR---GIQLTA 330
Cdd:PRK06145 220 RIHR----EFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRvftRARYID 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 331 AYGMSETCPliscaylNDELL-AGSEDERTTyriKAGVPVPLVDAAIMDEQGRFLPADgeSQGELVLRSPWLTQGYFREP 409
Cdd:PRK06145 296 AYGLTETCS-------GDTLMeAGREIEKIG---STGRALAHVEIRIADGAGRWLPPN--MKGEICMRGPKVTKGYWKDP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 410 ERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLV 489
Cdd:PRK06145 364 EKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599119 490 VREGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEI 546
Cdd:PRK06145 444 LNPGATLTLEALDRHCR-----QRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
44-537 |
7.52e-68 |
|
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: 227.48 E-value: 7.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNS 123
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 EFVPLYQAVAGQLATVERTILLTDGAEKSAELPGLVGEYesLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKGVYFSH 203
Cdd:cd05911 91 DGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPT--LGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 204 RQLVLHTLAMASTIGSLDsirllGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKREKVTFSHCV 283
Cdd:cd05911 169 RNLIANLSQVQTFLYGND-----GSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 284 PTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKARGIQ--LTAAYGMSETCPLISCAYLNDELLaGSedertt 360
Cdd:cd05911 244 PPIAAALAKSPLLDKYDLSSLRVILsGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDDKP-GS------ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 361 yrikAGVPVPLVDAAIMDEQGRFLPADGEsQGELVLRSPWLTQGYFREPERGEELW-RGGWMHTGDVATLDGMGFIEIRD 439
Cdd:cd05911 317 ----VGRLLPNVEAKIVDDDGKDSLGPNE-PGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 440 RIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDArglkEHLKPFVEQGNINKWAI 519
Cdd:cd05911 392 RKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE----KEVKDYVAKKVASYKQL 467
|
490
....*....|....*...
gi 15599119 520 PSQIAVVTDIPKTSVGKL 537
Cdd:cd05911 468 RGGVVFVDEIPKSASGKI 485
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
30-548 |
8.41e-67 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 227.21 E-value: 8.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 30 YEKSHEIVYrDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILY 109
Cdd:PLN03102 27 YPNRTSIIY-GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 110 TMNHAEDRFVLVNSEFVPLYQAVAGQLATVE-----RTILL------TDGAEKSAELPGLV--GEYESLLAAASprydFP 176
Cdd:PLN03102 106 ILRHAKPKILFVDRSFEPLAREVLHLLSSEDsnlnlPVIFIheidfpKRPSSEELDYECLIqrGEPTPSLVARM----FR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 177 DFDENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAmaSTIGsldsiRLLGTSDVYMPITPMFHVHAWGTPY-VATMLGV 255
Cdd:PLN03102 182 IQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLS--AIIG-----WEMGTCPVYLWTLPMFHCNGWTFTWgTAARGGT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 256 KQVYPGRYDPELL--VELwkrEKVTFSHCVPTILQMVMNA-RAAQGVDFKGWKVIIGGSALNRSLYEAAKARGIQLTAAY 332
Cdd:PLN03102 255 SVCMRHVTAPEIYknIEM---HNVTHMCCVPTVFNILLKGnSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 333 GMSE-TCPLISCAYlNDELLAGSEDERTTYRIKAGVPV-PLVDAAIMD-EQGRFLPADGESQGELVLRSPWLTQGYFREP 409
Cdd:PLN03102 332 GLTEaTGPVLFCEW-QDEWNRLPENQQMELKARQGVSIlGLADVDVKNkETQESVPRDGKTMGEIVIKGSSIMKGYLKNP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 410 ERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLV 489
Cdd:PLN03102 411 KATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599119 490 VREGQQldarGLKEHLKPFV-EQGNINKWA--------IPSQIAVVTDIPKTSVGKLDKKRIRiEIAQ 548
Cdd:PLN03102 491 LEKGET----TKEDRVDKLVtRERDLIEYCrenlphfmCPRKVVFLQELPKNGNGKILKPKLR-DIAK 553
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
43-543 |
3.31e-66 |
|
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: 221.01 E-value: 3.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 sefvplyqavagqlatvERTILLTDGAeksaelpglvgeyesllaaasprydfpdfdensiattfyttgtTGNPKGVYFS 202
Cdd:cd05934 83 -----------------PASILYTSGT-------------------------------------------TGPPKGVVIT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 203 HRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFH----VHAWgtpYVATMLGVKQVYPGRYDPELLVELWKREKVT 278
Cdd:cd05934 103 HANLTFAGYYSARRFG-------LGEDDVYLTVLPLFHinaqAVSV---LAALSVGATLVLLPRFSASRFWSDVRRYGAT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 279 FSHCVPTILQMVMnaRAAQGVDFKGWKV-IIGGSALNRSLYEAAKAR-GIQLTAAYGMSET-CPLIScaylndellAGSE 355
Cdd:cd05934 173 VTNYLGAMLSYLL--AQPPSPDDRAHRLrAAYGAPNPPELHEEFEERfGVRLLEGYGMTETiVGVIG---------PRDE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 356 DERTTyriKAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRS--PW-LTQGYFREPERGEELWRGGWMHTGDVATLDGM 432
Cdd:cd05934 242 PRRPG---SIGRPAPGYEVRIVDDDGQELP-AGEP-GELVIRGlrGWgFFKGYYNMPEATAEAMRNGWFHTGDLGYRDAD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 433 GFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLkpfveQG 512
Cdd:cd05934 317 GFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFC-----EG 391
|
490 500 510
....*....|....*....|....*....|.
gi 15599119 513 NINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05934 392 QLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
43-543 |
2.34e-64 |
|
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: 216.86 E-value: 2.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEFVPL-YQAVAGQLATvertILLTDGAEksaelpglvGEyesllaaasprydfpdfdensiattfyttgttgnPKGVYF 201
Cdd:cd05903 81 ERFRQFdPAAMPDAVAL----LLFTSGTT---------GE----------------------------------PKGVMH 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 202 SHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFH----VHAWGTPyvaTMLGVKQVYPGRYDPELLVELWKREKV 277
Cdd:cd05903 114 SHNTLSASIRQYAERLG-------LGPGDVFLVASPMAHqtgfVYGFTLP---LLLGAPVVLQDIWDPDKALALMREHGV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 278 TFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKARGIQLTA-AYGMSETCPLISCAYLNDELLAGSE 355
Cdd:cd05903 184 TFMMGATPFLTDLLNAVEEAGEPLSRLRTFVcGGATVPRSLARRAAELLGAKVCsAYGSTECPGAVTSITPAPEDRRLYT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 356 DerttyrikaGVPVPLVDAAIMDEQGRFLPADGEsqGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFI 435
Cdd:cd05903 264 D---------GRPLPGVEIKVVDDTGATLAPGVE--GELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 436 EIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfvEQGnIN 515
Cdd:cd05903 333 RITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLD---RQG-VA 408
|
490 500
....*....|....*....|....*...
gi 15599119 516 KWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05903 409 KQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
44-542 |
4.25e-64 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 217.81 E-value: 4.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVL-SEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEFVPLYQAVAGQlATVERTILLTDGAEKSAELPGlvgeyesllaaaspryDFPDFDENSIATTFYTTGTTGNPKGVYFS 202
Cdd:PRK06839 108 KTFQNMALSMQKV-SYVQRVISITSLKEIEDRKID----------------NFVEKNESASFIICYTSGTTGKPKGAVLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 203 HRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATML-GVKQVYPGRYDPELLVELWKREKVTFSH 281
Cdd:PRK06839 171 QENMFWNALNNTFAID-------LTMHDRSIVLLPLFHIGGIGLFAFPTLFaGGVIIVPRKFEPTKALSMIEKHKVTVVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 282 CVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKARGIQLTAAYGMSETCPLIScaylndeLLAGSEDERTT 360
Cdd:PRK06839 244 GVPTIHQALINCSKFETTNLQSVRWFYnGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVF-------MLSEEDARRKV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 361 YRIkaGVPVPLVDAAIMDEQGRFLPADGesQGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDR 440
Cdd:PRK06839 317 GSI--GKPVLFCDYELIDENKNKVEVGE--VGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 441 IKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKPFveqgnINKWAIP 520
Cdd:PRK06839 393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLF-----LAKYKIP 467
|
490 500
....*....|....*....|..
gi 15599119 521 SQIAVVTDIPKTSVGKLDKKRI 542
Cdd:PRK06839 468 KEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
22-543 |
1.05e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 214.85 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 22 SLMLSGRRYEKSHEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIR 101
Cdd:PRK06188 16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 102 LSPEQILYTMNHAE-DRFVLVNSEFVPLYQAVAGQLATVERtiLLTDGAeksaelpglVGEYESLLAAASPRYDFPDFDE 180
Cdd:PRK06188 96 GSLDDHAYVLEDAGiSTLIVDPAPFVERALALLARVPSLKH--VLTLGP---------VPDGVDLLAAAAKFGPAPLVAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 181 N---SIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGSLDSIRLLGTsdvympiTPMfhVHAWGTPYVATML--GV 255
Cdd:PRK06188 165 AlppDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMC-------TPL--SHAGGAFFLPTLLrgGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 256 KQVYPGrYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRS-LYEAAKARGIQLTAAYG 333
Cdd:PRK06188 236 VIVLAK-FDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYyGASPMSPVrLAEAIERFGPIFAQYYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 334 MSEtCPLISCaYLNDELLAGSEDERTTyriKAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGE 413
Cdd:PRK06188 315 QTE-APMVIT-YLRKRDHDPDDPKRLT---SCGRPTPGLRVALLDEDGREVAQ-GEV-GEICVRGPLVMDGYWNRPEETA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 414 ELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREG 493
Cdd:PRK06188 388 EAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15599119 494 QQLDARGLKEHLKPfvEQGNInkWAiPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK06188 468 AAVDAAELQAHVKE--RKGSV--HA-PKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
45-547 |
2.91e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 203.69 E-value: 2.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGA--VLHtinirlSPeqiLYTMNHAEDRF---- 118
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAvvVEH------NP---LYTAHELEHPFedhg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 119 ---VLVNSEFVPLYQAVAGQLA--------------TVERTIL---LTDGAEKSAEL----PGLVgEYESLLAAASPRY- 173
Cdd:PRK05605 130 arvAIVWDKVAPTVERLRRTTPletivsvnmiaampLLQRLALrlpIPALRKARAALtgpaPGTV-PWETLVDAAIGGDg 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 174 ---DFPDFDENSIATTFYTTGTTGNPKGVYFSHRQLvlhtlaMASTIGSLDSIRLLGTSD-VYMPITPMFHvhAWGTPYV 249
Cdd:PRK05605 209 sdvSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNL------FANAAQGKAWVPGLGDGPeRVLAALPMFH--AYGLTLC 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 250 AT---MLGVKQVYPGRYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEA-AKAR 324
Cdd:PRK05605 281 LTlavSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFsGAMALPVSTVELwEKLT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 325 GIQLTAAYGMSETCPLISCAYLNDELLAGSederttyrikAGVPVPLVDAAIMDEQ--GRFLPaDGEsQGELVLRSPWLT 402
Cdd:PRK05605 361 GGLLVEGYGLTETSPIIVGNPMSDDRRPGY----------VGVPFPDTEVRIVDPEdpDETMP-DGE-EGELLVRGPQVF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 403 QGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGE 482
Cdd:PRK05605 429 KGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSE 508
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599119 483 RPFALLVVREGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIA 547
Cdd:PRK05605 509 EVVAAVVLEPGAALDPEGLRAYCR-----EHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELL 568
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
43-548 |
3.23e-58 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 203.06 E-value: 3.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVM--DWDSHR--YLECMfaipMIGAVLHTINIRLSPEQILYTMNHAEDRF 118
Cdd:PRK06087 49 SYTYSALDHAASRLANWLLAKGIEPGDRVAFQlpGWCEFTiiYLACL----KVGAVSVPLLPSWREAELVWVLNKCQAKM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 119 VLV-----NSEFVPLYQAVAGQLATVERTILLTDGAEKSAELpglvgEYESLLAAASPRYDFPDFDENSIATTFYTTGTT 193
Cdd:PRK06087 125 FFAptlfkQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSL-----SLSQIIADYEPLTTAITTHGDELAAVLFTSGTE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 194 GNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATML-GVKQVYPGRYDPELLVELW 272
Cdd:PRK06087 200 GLPKGVMLTHNNILASERAYCARLN-------LTWQDVFMMPAPLGHATGFLHGVTAPFLiGARSVLLDIFTPDACLALL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSH-CVPTILQMvMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKARGIQLTAAYGMSETCPLiscAYLN-DE 349
Cdd:PRK06087 273 EQQRCTCMLgATPFIYDL-LNLLEKQPADLSALRFFLcGGTTIPKKVARECQQRGIKLLSVYGSTESSPH---AVVNlDD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 350 LLagsedERTTYriKAGVPVPLVDAAIMDEQGRFLPAdGEsQGELVLRSPWLTQGYFREPER-GEELWRGGWMHTGDVAT 428
Cdd:PRK06087 349 PL-----SRFMH--TDGYAAAGVEIKVVDEARKTLPP-GC-EGEEASRGPNVFMGYLDEPELtARALDEEGWYYSGDLCR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 429 LDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQldaRGLKEHLKPF 508
Cdd:PRK06087 420 MDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHH---SLTLEEVVAF 496
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599119 509 VEQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQ 548
Cdd:PRK06087 497 FSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMR 536
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
36-543 |
6.58e-58 |
|
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: 201.00 E-value: 6.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLV-NSEFVP-LYQAVAGQLATVERTILLTDG--AEKSAELPGLvgeyESLLAAASPRydfPDFDENSIATTFYTTG 191
Cdd:cd05926 87 SKLVLTpKGELGPaSRAASKLGLAILELALDVGVLirAPSAESLSNL----LADKKNAKSE---GVPLPDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 192 TTGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAwgtpYVATML-----GVKQVYPGRYDPE 266
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNTYK-------LTPDDRTLVVMPLFHVHG----LVASLLstlaaGGSVVLPPRFSAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 267 LLVELWKREKVTFSHCVPTILQ-MVMNARAAQGVDFKGWKVIIGGSA-LNRSLYEAAKAR-GIQLTAAYGMSETCPLISC 343
Cdd:cd05926 229 TFWPDVRDYNATWYTAVPTIHQiLLNRPEPNPESPPPKLRFIRSCSAsLPPAVLEALEATfGAPVLEAYGMTEAAHQMTS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 344 AYLNdellagsEDERttyriKAG-VPVPL-VDAAIMDEQGRFLPADGEsqGELVLRSPWLTQGYFREPE-RGEELWRGGW 420
Cdd:cd05926 309 NPLP-------PGPR-----KPGsVGKPVgVEVRILDEDGEILPPGVV--GEICLRGPNVTRGYLNNPEaNAEAAFKDGW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 421 MHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARG 500
Cdd:cd05926 375 FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEE 454
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15599119 501 LKEHLKPfveqgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05926 455 LRAFCRK-----HLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
43-548 |
2.61e-56 |
|
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: 197.68 E-value: 2.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAV------LHtiniRLSpeQILYTMNHAE- 115
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvfalpAH----RRA--EISHFAEQSEa 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 ------DRFVLVNseFVPLYQAVAGQLATVERTILLTDGAEKSAelpglvgeYESLLAAASPRyDFPDFDENSIATTFYT 189
Cdd:COG1021 124 vayiipDRHRGFD--YRALARELQAEVPSLRHVLVVGDAGEFTS--------LDALLAAPADL-SEPRPDPDDVAFFQLS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 190 TGTTGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPyvaTMLGV-----KQVYPGRYD 264
Cdd:COG1021 193 GGTTGLPKLIPRTHDDYLYSVRASAEICG-------LDADTVYLAALPAAHNFPLSSP---GVLGVlyaggTVVLAPDPS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 265 PELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVI-IGGSALNRSLyeAAKAR---GIQLTAAYGMSETcpL 340
Cdd:COG1021 263 PDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLqVGGAKLSPEL--ARRVRpalGCTLQQVFGMAEG--L 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 341 ISCAYLNDellagSEDERTTYRikaGVPV-PLVDAAIMDEQGRFLPaDGEsQGELVLRSPWLTQGYFREPERGEELW-RG 418
Cdd:COG1021 339 VNYTRLDD-----PEEVILTTQ---GRPIsPDDEVRIVDEDGNPVP-PGE-VGELLTRGPYTIRGYYRAPEHNARAFtPD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 419 GWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVReGQQLDA 498
Cdd:COG1021 409 GFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTL 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15599119 499 RGLKEHLKpfvEQGnINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQ 548
Cdd:COG1021 488 AELRRFLR---ERG-LAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
43-548 |
1.16e-55 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 196.43 E-value: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVM---DWD-SHRYLECMfaipMIGAVLHTINIRLSPEQILYTMNHAEDRF 118
Cdd:PRK13295 55 RFTYRELAALVDRVAVGLARLGVGRGDVVSCQlpnWWEfTVLYLACS----RIGAVLNPLMPIFRERELSFMLKHAESKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 119 VLVNSEFVPL-YQAVAGQL---ATVERTILLTDGA-EKSAE--LPGLVGEYESLLAA--ASPRydfPDFDEnsIATTFYT 189
Cdd:PRK13295 131 LVVPKTFRGFdHAAMARRLrpeLPALRHVVVVGGDgADSFEalLITPAWEQEPDAPAilARLR---PGPDD--VTQLIYT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 190 TGTTGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMfhVHAWGTPY---VATMLGVKQVYPGRYDPE 266
Cdd:PRK13295 206 SGTTGEPKGVMHTANTLMANIVPYAERLG-------LGADDVILMASPM--AHQTGFMYglmMPVMLGATAVLQDIWDPA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 267 LLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQLTAAYGMSEtCPLISCA 344
Cdd:PRK13295 277 RAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLcAGAPIPGALVERARAAlGAKIVSAWGMTE-NGAVTLT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 345 YLNDEL-LAGSEDerttyrikaGVPVPLVDAAIMDEQGRFLPADGEsqGELVLRSPWLTQGYFREPErgeelWRG----G 419
Cdd:PRK13295 356 KLDDPDeRASTTD---------GCPLPGVEVRVVDADGAPLPAGQI--GRLQVRGCSNFGGYLKRPQ-----LNGtdadG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 420 WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDAR 499
Cdd:PRK13295 420 WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFE 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15599119 500 GLKEHLKpfvEQGnINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQ 548
Cdd:PRK13295 500 EMVEFLK---AQK-VAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
196-539 |
1.47e-55 |
|
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: 190.17 E-value: 1.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKRE 275
Cdd:cd17637 15 PRGAVLSHGNLIAANLQLIHAMG-------LTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEALELIEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSA-LNRSLYEaaKARGIQLTAAYGMSETCPLISCAYLNDEllAGS 354
Cdd:cd17637 88 KVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDApETIQRFE--ETTGATFWSLYGQTETSGLVTLSPYRER--PGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 355 ederttyrikAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGF 434
Cdd:cd17637 164 ----------AGRPGPLVRVRIVDDNDRPVPA-GET-GEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 435 IEIRDRI--KDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfveqG 512
Cdd:cd17637 232 LWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVG-----S 306
|
330 340
....*....|....*....|....*..
gi 15599119 513 NINKWAIPSQIAVVTDIPKTSVGKLDK 539
Cdd:cd17637 307 RIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
37-543 |
4.75e-55 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 193.74 E-value: 4.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 37 VYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAED 116
Cdd:cd05959 23 FIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 117 RFVLVNSEFVPLYQAVAGQLATVERTILLTDGAEKSAelpgLVGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNP 196
Cdd:cd05959 103 RVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEA----GALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 197 KGVYFSHRQLVlhtlAMASTIGSldsiRLLGT--SDVYMPITPMFHVHAWGTP-YVATMLGVKQV-YPGRYDPELLVELW 272
Cdd:cd05959 179 KGVVHLHADIY----WTAELYAR----NVLGIreDDVCFSAAKLFFAYGLGNSlTFPLSVGATTVlMPERPTPAAVFKRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQLTAAYGMSETCPlISCAYLNDEL 350
Cdd:cd05959 251 RRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsAGEALPAEVGERWKARfGLDILDGIGSTEMLH-IFLSNRPGRV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 351 LAGSederttyrikAGVPVPLVDAAIMDEQGRFLpADGESqGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLD 430
Cdd:cd05959 330 RYGT----------TGKPVPGYEVELRDEDGGDV-ADGEP-GELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 431 GMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQ---LDARGLKEHLKp 507
Cdd:cd05959 398 DDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEdseALEEELKEFVK- 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 15599119 508 fveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05959 477 ----DRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
44-543 |
1.00e-54 |
|
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: 190.25 E-value: 1.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEdrfvlvns 123
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 efvPLYQAVAgqlatverTILLTDGAeksaelpglVGEyesllaaasprydfpdfdensiattfyttgttgnPKGVyfsh 203
Cdd:cd05912 74 ---VKLDDIA--------TIMYTSGT---------TGK----------------------------------PKGV---- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 204 rqlvLHTLAM--ASTIGSLDSirlLGTS--DVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKREKVTF 279
Cdd:cd05912 96 ----QQTFGNhwWSAIGSALN---LGLTedDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTI 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 280 SHCVPTILQMVMnARAAQGVDFKGWKVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLIscAYLNDELLA---GSed 356
Cdd:cd05912 169 ISVVPTMLQRLL-EILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQI--VTLSPEDALnkiGS-- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 357 erttyrikAGVPVPLVDAAIMDEQGRflpadGESQGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIE 436
Cdd:cd05912 244 --------AGKPLFPVELKIEDDGQP-----PYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 437 IRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFAlLVVREgQQLDARGLKEHLkpfveQGNINK 516
Cdd:cd05912 311 VLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVA-FVVSE-RPISEEELIAYC-----SEKLAK 383
|
490 500
....*....|....*....|....*..
gi 15599119 517 WAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05912 384 YKVPKKIYFVDELPRTASGKLLRHELK 410
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
26-548 |
1.34e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 192.95 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 26 SGRRYEKSHEIVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPE 105
Cdd:PRK07470 16 AARRFPDRIALVWGDR-SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 106 QILYTMNHAEDRFVLVNSEFvPLYQAVAGQLATVERTILLTDGAEKSAElpglvgeYESLLAA-ASPRYDFPDFDENSIA 184
Cdd:PRK07470 95 EVAYLAEASGARAMICHADF-PEHAAAVRAASPDLTHVVAIGGARAGLD-------YEALVARhLGARVANAAVDHDDPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 185 TTFYTTGTTGNPKGVYFSHRQlvlhtlaMASTIGS--LDSIRLLGTSDVYMPITPMFH---VHAwgtpYVATMLGVKQVY 259
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLTHGQ-------MAFVITNhlADLMPGTTEQDASLVVAPLSHgagIHQ----LCQVARGAATVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 260 PG--RYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWK-VIIGGSALNRSLYEAAKAR-GIQLTAAYGMS 335
Cdd:PRK07470 236 LPseRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRyVIYAGAPMYRADQKRALAKlGKVLVQYFGLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 336 ETCPLISC--AYLNDEllagsEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGE 413
Cdd:PRK07470 316 EVTGNITVlpPALHDA-----EDGPDARIGTCGFERTGMEVQIQDDEGRELPP-GET-GEICVIGPAVFAGYYNNPEANA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 414 ELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREG 493
Cdd:PRK07470 389 KAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDG 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15599119 494 QQLDARGLKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQ 548
Cdd:PRK07470 469 APVDEAELLAWL-----DGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEE 518
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
28-543 |
3.21e-53 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 189.12 E-value: 3.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 28 RRYEKSHEIVYRDQV----RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLS 103
Cdd:PRK08008 18 DVYGHKTALIFESSGgvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 104 PEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDgaEKSAELPGlVGEYESLLAAASPRYDF-PDFDENS 182
Cdd:PRK08008 98 REESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTR--VALPADDG-VSSFTQLKAQQPATLCYaPPLSTDD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 183 IATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVAT-MLGVKQVYPG 261
Cdd:PRK08008 175 TAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCA-------LRDDDVYLTVMPAFHIDCQCTAAMAAfSAGATFVLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 262 RYDPEllvELWK---REKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSALNRSLYEAAKAR-GIQLTAAYGMSET 337
Cdd:PRK08008 248 KYSAR---AFWGqvcKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMFYLNLSDQEKDAFEERfGVRLLTSYGMTET 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 338 CPLIscayLNDEllagSEDERTTYRIkaGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRS-PWLT--QGYFREPERGEE 414
Cdd:PRK08008 325 IVGI----IGDR----PGDKRRWPSI--GRPGFCYEAEIRDDHNRPLPA-GEI-GEICIKGvPGKTifKEYYLDPKATAK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 415 -LWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREG 493
Cdd:PRK08008 393 vLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15599119 494 QQLDarglKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK08008 473 ETLS----EEEFFAFCEQ-NMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
41-547 |
2.01e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 186.17 E-value: 2.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 41 QVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVL 120
Cdd:PRK09088 20 GRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 121 VNSEfvplyqavagqlatvertilLTDGAEKSAELPGLVGEYESLLAAASPRYDfPDfdenSIATTFYTTGTTGNPKGVY 200
Cdd:PRK09088 100 GDDA--------------------VAAGRTDVEDLAAFIASADALEPADTPSIP-PE----RVSLILFTSGTSGQPKGVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 201 FSHRQLvLHTLAMASTIGSLDSirllgtSDVYMPITPMFHVHAWGTPYVATML--GVKQVYPGrYDPELLVELWKREKVT 278
Cdd:PRK09088 155 LSERNL-QQTAHNFGVLGRVDA------HSSFLCDAPMFHIIGLITSVRPVLAvgGSILVSNG-FEPKRTLGRLGDPALG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 279 FSH--CVPTILQMVmnaRAAQGVDFKGWK----VIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLISCAyLNDELLA 352
Cdd:PRK09088 227 ITHyfCVPQMAQAF---RAQPGFDAAALRhltaLFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVFGMS-VDCDVIR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 353 GSEDerttyriKAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGEELWRG-GWMHTGDVATLDG 431
Cdd:PRK09088 303 AKAG-------AAGIPTPTVQTRVVDDQGNDCPA-GVP-GELLLRGPNLSPGYWRRPQATARAFTGdGWFRTGDIARRDA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 432 MGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLkpfveQ 511
Cdd:PRK09088 374 DGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHL-----S 448
|
490 500 510
....*....|....*....|....*....|....*.
gi 15599119 512 GNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIA 547
Cdd:PRK09088 449 TRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALA 484
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
44-543 |
2.33e-52 |
|
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: 184.46 E-value: 2.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMdwdSHRYLE---CMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVL 120
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVL---LPRVPElwaVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 121 VNSEFVPLyqavagqlatvertILLTDGAEksaelpGLvgeyesllaaasprydfpdfdensiattfyttgttgnPKGVY 200
Cdd:cd05972 78 TDAEDPAL--------------IYFTSGTT------GL-------------------------------------PKGVL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 201 FSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPIT-PMFHVHAWGTPYVATMLGVKQV--YPGRYDPELLVELWKREKV 277
Cdd:cd05972 101 HTHSYPLGHIPTAAYWLG-------LRPDDIHWNIAdPGWAKGAWSSFFGPWLLGATVFvyEGPRFDAERILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 278 TFSHCVPTILQMVMNARAAQGvDFKGWK-VIIGGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLIScAYLNDELLAGSe 355
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDLSSY-KFSHLRlVVSAGEPLNPEVIEWWRAAtGLPIRDGYGQTETGLTVG-NFPDMPVKPGS- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 356 derttyrikAGVPVPLVDAAIMDEQGRFLPAdGEsQGELVLRSPW--LTQGYFREPERGEELWRGGWMHTGDVATLDGMG 433
Cdd:cd05972 251 ---------MGRPTPGYDVAIIDDDGRELPP-GE-EGDIAIKLPPpgLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 434 FIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQlDARGLKEHLKPFVEQgN 513
Cdd:cd05972 320 YFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE-PSEELAEELQGHVKK-V 397
|
490 500 510
....*....|....*....|....*....|
gi 15599119 514 INKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05972 398 LAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
10-542 |
4.77e-52 |
|
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: 184.84 E-value: 4.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 10 AAGAYQYPLLIKSLMLSGRRYeKSHEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIP 89
Cdd:cd05920 8 AAGYWQDEPLGDLLARSAARH-PDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 90 MIGA--VLHTINIRLSpeQILYTMNHAEDRFVLVNSEFVPL-YQAVAGQLATVERTI---LLTDGaekSAELPGLVgeye 163
Cdd:cd05920 87 RLGAvpVLALPSHRRS--ELSAFCAHAEAVAYIVPDRHAGFdHRALARELAESIPEValfLLSGG---TTGTPKLI---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 164 sllaaasPRydfpdfdensiattfyttgttgnpkgvyfSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHA 243
Cdd:cd05920 158 -------PR-----------------------------THNDYAYNVRASAEVCG-------LDQDTVYLAVLPAAHNFP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 244 WGTPYV--ATMLGVKQVYPGRYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVI-IGGSALNRSL-YE 319
Cdd:cd05920 195 LACPGVlgTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLqVGGARLSPALaRR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 320 AAKARGIQLTAAYGMSETcpLISCAYLND--ELLAGSEderttyrikaGVPV-PLVDAAIMDEQGRFLPaDGEsQGELVL 396
Cdd:cd05920 275 VPPVLGCTLQQVFGMAEG--LLNYTRLDDpdEVIIHTQ----------GRPMsPDDEIRVVDEEGNPVP-PGE-EGELLT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 397 RSPWLTQGYFREPERGEELWRG-GWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGV 475
Cdd:cd05920 341 RGPYTIRGYYRAPEHNARAFTPdGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAM 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599119 476 PDPQWGERPFALLVVReGQQLDARGLKEHLKpfvEQGnINKWAIPSQIAVVTDIPKTSVGKLDKKRI 542
Cdd:cd05920 421 PDELLGERSCAFVVLR-DPPPSAAQLRRFLR---ERG-LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
36-543 |
4.89e-52 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 186.12 E-value: 4.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK06155 39 LLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAEKSAELPGLVGEYESLLAAASPrydfPDFDENSIATTFYTTGTTGN 195
Cdd:PRK06155 119 ARLLVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPA----AAVQPGDTAAILYTSGTTGP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKRE 275
Cdd:PRK06155 195 SKGVCCPHAQFYWWGRNSAEDLE-------IGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAVRRH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTILQMVMNARAaqGVDFKGWKVIIG-GSALNRSLYEAAKAR-GIQLTAAYGMSETCplISCAYLNDELLAG 353
Cdd:PRK06155 268 GATVTYLLGAMVSILLSQPA--RESDRAHRVRVAlGPGVPAALHAAFRERfGVDLLDGYGSTETN--FVIAVTHGSQRPG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 354 SederttyrikAGVPVPLVDAAIMDEQGRFLPADgeSQGELVLRS--PW-LTQGYFREPERGEELWRGGWMHTGDVATLD 430
Cdd:PRK06155 344 S----------MGRLAPGFEARVVDEHDQELPDG--EPGELLLRAdePFaFATGYFGMPEKTVEAWRNLWFHTGDRVVRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 431 GMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKPfve 510
Cdd:PRK06155 412 ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEP--- 488
|
490 500 510
....*....|....*....|....*....|...
gi 15599119 511 qgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK06155 489 --RLAYFAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-543 |
6.87e-52 |
|
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: 180.94 E-value: 6.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHtlamASTIGsldsIRLLGTSDVYMPI-TPMFHVHAWGTPYVATML-GVKQVYPGR-YDPELLVEL 271
Cdd:cd05917 16 SPKGATLTHHNIVNN----GYFIG----ERLGLTEQDRLCIpVPLFHCFGSVLGVLACLThGATMVFPSPsFDPLAVLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 272 WKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKV-IIGGS----ALNRSLYEAAKARgiQLTAAYGMSETCPLISCAYL 346
Cdd:cd05917 88 IEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTgIMAGApcppELMKRVIEVMNMK--DVTIAYGMTETSPVSTQTRT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 347 NDELlagseDERTTyriKAGVPVPLVDAAIMDEQGRFLPADGEsQGELVLRSPWLTQGYFREPER-GEELWRGGWMHTGD 425
Cdd:cd05917 166 DDSI-----EKRVN---TVGRIMPHTEAKIVDPEGGIVPPVGV-PGELCIRGYSVMKGYWNDPEKtAEAIDGDGWLHTGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 426 VATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDArglkEHL 505
Cdd:cd05917 237 LAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE----EDI 312
|
330 340 350
....*....|....*....|....*....|....*...
gi 15599119 506 KPFVeQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05917 313 KAYC-KGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
28-547 |
1.23e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 185.36 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 28 RRYEKSHEIVYRDQ-VRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQ 106
Cdd:PRK12583 29 ARFPDREALVVRHQaLRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 107 ILYTMNHAEDRFVLV-----NSEFVPLYQAVAGQLATVERtilltdGAEKSAELPGLVG-------------EYESLLAA 168
Cdd:PRK12583 109 LEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQP------GALACERLPELRGvvslapapppgflAWHELQAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 169 ASPRYDfPDFDENSIATTFY-------TTGTTGNPKGVYFSHRQLVLHTLAMASTIGSLDSIRLLgtsdvyMPItPMFHV 241
Cdd:PRK12583 183 GETVSR-EALAERQASLDRDdpiniqyTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLC------VPV-PLYHC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 242 HAWGTPYVATM-LGVKQVYPGRY-DPELLVELWKREKVTFSHCVPT--ILQMVMNARAAqgVDFKGWKV-IIGGSALNRS 316
Cdd:PRK12583 255 FGMVLANLGCMtVGACLVYPNEAfDPLATLQAVEEERCTALYGVPTmfIAELDHPQRGN--FDLSSLRTgIMAGAPCPIE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 317 LYE--AAKARGIQLTAAYGMSETCPLISCAYLNDELlagseDERTTyriKAGVPVPLVDAAIMDEQGRFLPADgeSQGEL 394
Cdd:PRK12583 333 VMRrvMDEMHMAEVQIAYGMTETSPVSLQTTAADDL-----ERRVE---TVGRTQPHLEVKVVDPDGATVPRG--EIGEL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 395 VLRSPWLTQGYFREPER-GEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVV 473
Cdd:PRK12583 403 CTRGYSVMKGYWNNPEAtAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVF 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599119 474 GVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRiEIA 547
Cdd:PRK12583 483 GVPDEKYGEEIVAWVRLHPGHAASEEELREFCK-----ARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR-EIS 550
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
43-536 |
4.35e-51 |
|
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: 182.82 E-value: 4.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEFVPlyqavagQLATVERTILLTDGAEKsaelpGLVGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKGVYFS 202
Cdd:cd05904 112 AELAE-------KLASLALPVVLLDSAEF-----DSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 203 HRQLVlhtlamASTIGSLDSIRLLGTS-DVYMPITPMFHVHAWGTPYVATM-LGVKQVYPGRYDPELLVELWKREKVTFS 280
Cdd:cd05904 180 HRNLI------AMVAQFVAGEGSNSDSeDVFLCVLPMFHIYGLSSFALGLLrLGATVVVMPRFDLEELLAAIERYKVTHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 281 HCVPTI-LQMVMNArAAQGVDFKGWKVIIGGSA-LNRSLYEAAKAR--GIQLTAAYGMSETCPLISCAYLNDELLA--GS 354
Cdd:cd05904 254 PVVPPIvLALVKSP-IVDKYDLSSLRQIMSGAApLGKELIEAFRAKfpNVDLGQGYGMTESTGVVAMCFAPEKDRAkyGS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 355 ederttyrikAGVPVPLVDAAIMD-EQGRFLPADgeSQGELVLRSPWLTQGYFREPERGEELWRG-GWMHTGDVATLDGM 432
Cdd:cd05904 333 ----------VGRLVPNVEAKIVDpETGESLPPN--QTGELWIRGPSIMKGYLNNPEATAATIDKeGWLHTGDLCYIDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 433 GFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDArglkEHLKPFVEqg 512
Cdd:cd05904 401 GYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTE----DEIMDFVA-- 474
|
490 500
....*....|....*....|....*...
gi 15599119 513 ninKWAIP----SQIAVVTDIPKTSVGK 536
Cdd:cd05904 475 ---KQVAPykkvRKVAFVDAIPKSPSGK 499
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
48-546 |
5.63e-51 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 182.08 E-value: 5.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 48 TF---NERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSE 124
Cdd:PRK03640 29 TFmelHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 125 FVplyqavagQLATVERTILLTDGAEKSAELPGLVgeyesllaaasprydfPDFDENSIATTFYTTGTTGNPKGV---YF 201
Cdd:PRK03640 109 FE--------AKLIPGISVKFAELMNGPKEEAEIQ----------------EEFDLDEVATIMYTSGTTGKPKGViqtYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 202 SHrqlvlhtlaMASTIGSldSIRL-LGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKREKVTFS 280
Cdd:PRK03640 165 NH---------WWSAVGS--ALNLgLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 281 HCVPTILQMVMnARAAQG---VDFKGwkVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLIsCAylndelLAgSEDE 357
Cdd:PRK03640 234 SVVSTMLQRLL-ERLGEGtypSSFRC--MLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQI-VT------LS-PEDA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 358 RTtyriKAG-VPVPLVDAAI-MDEQGRFLPAdgESQGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFI 435
Cdd:PRK03640 303 LT----KLGsAGKPLFPCELkIEKDGVVVPP--FEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 436 EIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVreGQQLDARGLKEHLkpfveQGNIN 515
Cdd:PRK03640 377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFC-----EEKLA 449
|
490 500 510
....*....|....*....|....*....|.
gi 15599119 516 KWAIPSQIAVVTDIPKTSVGKLDKKRIRIEI 546
Cdd:PRK03640 450 KYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
45-542 |
8.80e-51 |
|
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: 180.34 E-value: 8.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSE 124
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 125 FVplyqavagqlatvERTILLTDGAEKSAElpglvGEYESLLAAasprydfpDFDENSIATTFYTTGTTGNPKGVYFSHR 204
Cdd:TIGR01923 81 LE-------------EKDFQADSLDRIEAA-----GRYETSLSA--------SFNMDQIATLMFTSGTTGKPKAVPHTFR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 205 QLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPelLVELWKREKVTFSHCVP 284
Cdd:TIGR01923 135 NHYASAVGSKENLG-------FTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 285 TILQMVMNARaaqGVDFKGWKVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLIsCAYLNDELLAgsederttyRIK 364
Cdd:TIGR01923 206 TQLNRLLDEG---GHNENLRKILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQV-TTATPEMLHA---------RPD 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 365 AGVPVPLVDAAIMDEqgrflpaDGESQGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDV 444
Cdd:TIGR01923 273 VGRPLAGREIKIKVD-------NKEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 445 IKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREG---QQLDARgLKEHLKpfveqgninKWAIPS 521
Cdd:TIGR01923 346 IISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDisqAKLIAY-LTEKLA---------KYKVPI 415
|
490 500
....*....|....*....|.
gi 15599119 522 QIAVVTDIPKTSVGKLDKKRI 542
Cdd:TIGR01923 416 AFEKLDELPYNASGKILRNQL 436
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
36-543 |
6.77e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 180.78 E-value: 6.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQ-VRYSYATFNERVARLANVLSEAGVKAGDTVAVmdWDSHRY--LECMFAIPMIGAVLHTINIRLSPEQILYTMN 112
Cdd:PRK08315 35 LVYRDQgLRWTYREFNEEVDALAKGLLALGIEKGDRVGI--WAPNVPewVLTQFATAKIGAILVTINPAYRLSELEYALN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 113 HAEDRFVLV-----NSEFVPLYQAVAGQLATVERtilltdGAEKSAELPGLvgEYESLLAAASPR--YDFPDFDENSIAT 185
Cdd:PRK08315 113 QSGCKALIAadgfkDSDYVAMLYELAPELATCEP------GQLQSARLPEL--RRVIFLGDEKHPgmLNFDELLALGRAV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 186 TFYTTGTTG-------------------NPKGVYFSHRQLVLHtlamASTIGslDSIRLLGTSDVYMPItPMFH------ 240
Cdd:PRK08315 185 DDAELAARQatldpddpiniqytsgttgFPKGATLTHRNILNN----GYFIG--EAMKLTEEDRLCIPV-PLYHcfgmvl 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 241 ------VHAwgtpyvATMlgvkqVYPG-RYDPELLVELWKREKVTFSHCVPTILQMVMNARaaqgvDFKGWKV------I 307
Cdd:PRK08315 258 gnlacvTHG------ATM-----VYPGeGFDPLATLAAVEEERCTALYGVPTMFIAELDHP-----DFARFDLsslrtgI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 308 IGGSA----LNRSLYEAAKARGIqlTAAYGMSETCPLISCAYLNDELlagseDERTTY--RIKAGVPVPLVDAaimdEQG 381
Cdd:PRK08315 322 MAGSPcpieVMKRVIDKMHMSEV--TIAYGMTETSPVSTQTRTDDPL-----EKRVTTvgRALPHLEVKIVDP----ETG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 382 RFLPAdGEsQGELVLRSPWLTQGYFREPERGEE-LWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDL 460
Cdd:PRK08315 391 ETVPR-GE-QGELCTRGYSVMKGYWNDPEKTAEaIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 461 ISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:PRK08315 469 LYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCR-----GKIAHYKIPRYIRFVDEFPMTVTGKIQKF 543
|
...
gi 15599119 541 RIR 543
Cdd:PRK08315 544 KMR 546
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
44-543 |
9.64e-50 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 177.69 E-value: 9.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNS 123
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 EfvpLYqavagqlatvERTilltdgaekSAELPGLVgEYESllaaasprydfpdfdensiattfyttGTTGNPKGVYFSH 203
Cdd:cd05969 81 E---LY----------ERT---------DPEDPTLL-HYTS--------------------------GTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 204 RQLVLHTLAMASTIGSLDSIRLLGTSD-------VYMPITPMFHvhawGTPYVatmlgvkqVYPGRYDPELLVELWKREK 276
Cdd:cd05969 112 DAMIFYYFTGKYVLDLHPDDIYWCTADpgwvtgtVYGIWAPWLN----GVTNV--------VYEGRFDAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 277 VTFSHCVPTILQMVMNARA--AQGVDFKGWKVII-GGSALNRSLYE-AAKARGIQLTAAYGMSETCPLISCAYLNDELLA 352
Cdd:cd05969 180 VTVWYTAPTAIRMLMKEGDelARKYDLSSLRFIHsVGEPLNPEAIRwGMEVFGVPIHDTWWQTETGSIMIANYPCMPIKP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 353 GSederttyrikAGVPVPLVDAAIMDEQGRFLPADgeSQGELVLRSPW--LTQGYFREPERGEELWRGGWMHTGDVATLD 430
Cdd:cd05969 260 GS----------MGKPLPGVKAAVVDENGNELPPG--TKGILALKPGWpsMFRGIWNDEERYKNSFIDGWYLTGDLAYRD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 431 GMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQlDARGLKEHLKPFVE 510
Cdd:cd05969 328 EDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE-PSDELKEEIINFVR 406
|
490 500 510
....*....|....*....|....*....|...
gi 15599119 511 QGnINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05969 407 QK-LGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
42-543 |
1.34e-49 |
|
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: 179.16 E-value: 1.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 42 VRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLV 121
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 122 NSEFVPLYQavagqlatvERTILLTDGAEKSAElPGLVGEYESLLAAASPRYD-FPDFDENSIATTFYTTGTTGNPKGVY 200
Cdd:cd05915 103 DPNLLPLVE---------AIRGELKTVQHFVVM-DEKAPEGYLAYEEALGEEAdPVRVPERAACGMAYTTGTTGLPKGVV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 201 FSHRQLVLHtlamASTIGSLDSIRLlGTSDVYMPITPMFHVHAWGTPYVATMLG-----VKQVYpgryDPELLVELWKRE 275
Cdd:cd05915 173 YSHRALVLH----SLAASLVDGTAL-SEKDVVLPVVPMFHVNAWCLPYAATLVGakqvlPGPRL----DPASLVELFDGE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTILQMVMNARAAQGVDFKgW--KVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLISCAYLNDELLAG 353
Cdd:cd05915 244 GVTFTAGVPTVWLALADYLESTGHRLK-TlrRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETSPVVVQNFVKSHLESL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 354 SEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADGESQGELVLRSPWLTQGYFREPERGEEL-WRGGWMHTGDVATLDGM 432
Cdd:cd05915 323 SEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSAlTPDGFFRTGDIAVWDEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 433 GFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREgqqldARGLKEHLKPFVEQG 512
Cdd:cd05915 403 GYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG-----EKPTPEELNEHLLKA 477
|
490 500 510
....*....|....*....|....*....|.
gi 15599119 513 NINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05915 478 GFAKWQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
45-542 |
4.01e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 178.70 E-value: 4.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINiRLSPEQ-ILYTMNHAEDRFVLVNS 123
Cdd:PRK06178 60 TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS-PLFREHeLSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 EFVPLYQAVAGQLATveRTILLTD-----GAEKSAELPGLV-------GEYESLLAA-----ASPRYDFPDFDenSIATT 186
Cdd:PRK06178 139 QLAPVVEQVRAETSL--RHVIVTSladvlPAEPTLPLPDSLraprlaaAGAIDLLPAlractAPVPLPPPALD--ALAAL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 187 FYTTGTTGNPKGVYFSHRQLVlHTLAMASTIGSLdsirlLGTSDVYMPITPMFhvhaW--GTPY---VATMLGVKQVYPG 261
Cdd:PRK06178 215 NYTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAVV-----GGEDSVFLSFLPEF----WiaGENFgllFPLFSGATLVLLA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 262 RYDPELLVELWKREKVTfsHCVPTILQMV--MNARAAQGVDFKGWKVIiGGSALNRSLYEAAKARGIQLT------AAYG 333
Cdd:PRK06178 285 RWDAVAFMAAVERYRVT--RTVMLVDNAVelMDHPRFAEYDLSSLRQV-RVVSFVKKLNPDYRQRWRALTgsvlaeAAWG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 334 MSET--CPLISCAYLNDELlagseDERTTyRIKAGVPVPLVDAAIMD-EQGRFLPADGEsqGELVLRSPWLTQGYFREPE 410
Cdd:PRK06178 362 MTEThtCDTFTAGFQDDDF-----DLLSQ-PVFVGLPVPGTEFKICDfETGELLPLGAE--GEIVVRTPSLLKGYWNKPE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 411 RGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVV 490
Cdd:PRK06178 434 ATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQL 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15599119 491 REGQQLDARGLKEHLKpfveqGNINKWAIPsQIAVVTDIPKTSVGKLDKKRI 542
Cdd:PRK06178 514 KPGADLTAAALQAWCR-----ENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
45-545 |
1.24e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 177.53 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSE 124
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 125 FVPLYQAVagQLATVERTILLTDGAE---------------KSAELPGLVGE------YESLLAAASPRYDFPDFDENSI 183
Cdd:PRK06710 131 VFPRVTNV--QSATKIEHVIVTRIADflpfpknllypfvqkKQSNLVVKVSEsetihlWNSVEKEVNTGVEVPCDPENDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 184 ATTFYTTGTTGNPKGVYFSHRQLVLHTLamastIGSLDSIRLLGTSDVYMPITPMFHVHAW-GTPYVATMLGVKQVYPGR 262
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLVSNTL-----MGVQWLYNCKEGEEVVLGVLPFFHVYGMtAVMNLSIMQGYKMVLIPK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 263 YDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSA-LNRSLYEA-AKARGIQLTAAYGMSETCPL 340
Cdd:PRK06710 284 FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSApLPVEVQEKfETVTGGKLVEGYGLTESSPV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 341 ISCAYLNDELLAGSederttyrikAGVPVPLVDAAIMD-EQGRFLPAdGESqGELVLRSPWLTQGYFREPERGEELWRGG 419
Cdd:PRK06710 364 THSNFLWEKRVPGS----------IGVPWPDTEAMIMSlETGEALPP-GEI-GEIVVKGPQIMKGYWNKPEETAAVLQDG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 420 WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDAR 499
Cdd:PRK06710 432 WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEE 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15599119 500 GLKEHLKPFveqgnINKWAIPSQIAVVTDIPKTSVGKLdKKRIRIE 545
Cdd:PRK06710 512 ELNQFARKY-----LAAYKVPKVYEFRDELPKTTVGKI-LRRVLIE 551
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
40-543 |
2.75e-48 |
|
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: 173.63 E-value: 2.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKA-GDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRF 118
Cdd:cd05941 8 DGDSITYADLVARAARLANRLLALGKDLrGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 119 VLVNSefvplyqavagqlatverTILLTDGAEKSaelpglvgeyesllaaasprydfpdfdensiattfyttgttgnPKG 198
Cdd:cd05941 88 VLDPA------------------LILYTSGTTGR-------------------------------------------PKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 199 VYFSHRQLvlhtlamASTIGSLDSIRLLGTSDVYMPITPMFHVHAWGTPYVATML-GVKQVYPGRYDPELlVELWKREK- 276
Cdd:cd05941 107 VVLTHANL-------AANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFaGASVEFLPKFDPKE-VAISRLMPs 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 277 VTFSHCVPTIL--------QMVMNARAAQGVDFKGWKVIIGGSA-LNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAyL 346
Cdd:cd05941 179 ITVFMGVPTIYtrllqyyeAHFTDPQFARAAAAERLRLMVSGSAaLPVPTLEEWEAItGHTLLERYGMTEIGMALSNP-L 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 347 NDELLAGSederttyrikAGVPVPLVDAAIMDEQGRfLPADGESQGELVLRSPWLTQGYFREPERGEELWRG-GWMHTGD 425
Cdd:cd05941 258 DGERRPGT----------VGMPLPGVQARIVDEETG-EPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDdGWFKTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 426 VATLDGMGFIEIRDRIK-DVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREG-QQLDARGLKE 503
Cdd:cd05941 327 LGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599119 504 HLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05941 407 WAK-----QRLAPYKRPRRLILVDELPRNAMGKVNKKELR 441
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
42-501 |
1.12e-47 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 175.29 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 42 VRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLV 121
Cdd:COG1022 39 QSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 122 -NSEFVPLYQAVAGQLATVERTILLTDGAEKSAelPGLVGeYESLLAAASPRYDFPDFDEnsiattfYTTGTTG------ 194
Cdd:COG1022 119 eDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDD--PRLLS-LDELLALGREVADPAELEA-------RRAAVKPddlati 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 --------NPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHV--HAWGtpYVATMLGVKQVYPGryD 264
Cdd:COG1022 189 iytsgttgRPKGVMLTHRNLLSNARALLERLP-------LGPGDRTLSFLPLAHVfeRTVS--YYALAAGATVAFAE--S 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 265 PELLVELWKREKVTFSHCVPTILQMVMN---ARAAQGVDFKGW------------------------------------- 304
Cdd:COG1022 258 PDTLAEDLREVKPTFMLAVPRVWEKVYAgiqAKAEEAGGLKRKlfrwalavgrryararlagkspslllrlkhaladklv 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 305 ------------KVII-GGSALNRSL---YEAAkarGIQLTAAYGMSETCPLISCaYLNDELLAGSederttyrikAGVP 368
Cdd:COG1022 338 fsklrealggrlRFAVsGGAALGPELarfFRAL---GIPVLEGYGLTETSPVITV-NRPGDNRIGT----------VGPP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 369 VPLVDAAIMDEqgrflpadgesqGELVLRSPWLTQGYFREPERGEE-LWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKT 447
Cdd:COG1022 404 LPGVEVKIAED------------GEILVRGPNVMKGYYKNPEATAEaFDADGWLHTGDIGELDEDGFLRITGRKKDLIVT 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 448 -GGEWLSSLELEDLISRHPAVREVAVVGvpDpqwgERPF--ALLVVRE---GQQLDARGL 501
Cdd:COG1022 472 sGGKNVAPQPIENALKASPLIEQAVVVG--D----GRPFlaALIVPDFealGEWAEENGL 525
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
43-537 |
1.29e-46 |
|
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: 168.81 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEFVPLyqavagqlatveRTILLTDGAEksaelpGLvgeyesllaaasprydfpdfdensiattfyttgttgnPKGVYFS 202
Cdd:cd05935 81 SELDDL------------ALIPYTSGTT------GL-------------------------------------PKGCMHT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 203 HRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHV----HAWGTPYVAtmlGVKQVYPGRYDPELLVELWKREKVT 278
Cdd:cd05935 106 HFSAAANALQSAVWTG-------LTPSDVILACLPLFHVtgfvGSLNTAVYV---GGTYVLMARWDRETALELIEKYKVT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 279 FSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSAlnrSLYEAAKARGIQLTA-----AYGMSETCPLIscaYLNDELlag 353
Cdd:cd05935 176 FWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGA---PMPPAVAEKLLKLTGlrfveGYGLTETMSQT---HTNPPL--- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 354 sederttyRIKA---GVPVPLVDAAIMD-EQGRFLPaDGESqGELVLRSPWLTQGYFREPERGEELW--RGG--WMHTGD 425
Cdd:cd05935 247 --------RPKLqclGIP*FGVDARVIDiETGRELP-PNEV-GEIVVRGPQIFKGYWNRPEETEESFieIKGrrFFRTGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 426 VATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDarglkehl 505
Cdd:cd05935 317 LGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGK-------- 388
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599119 506 kpfVEQGNINKWA--------IPSQIAVVTDIPKTSVGKL 537
Cdd:cd05935 389 ---VTEEDIIEWAreqmaaykYPREVEFVDELPRSASGKI 425
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
196-543 |
1.22e-45 |
|
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: 167.51 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLvLHTLAMASTIGSLDsirllgTSDVYMPITPMFHVHAW-GTPYVATMLGVKQV-YPGRYDPELLVELWK 273
Cdd:cd05909 162 PKGVVLSHKNL-LANVEQITAIFDPN------PEDVVFGALPFFHSFGLtGCLWLPLLSGIKVVfHPNPLDYKKIPELIY 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 274 REKVTFSHCVPTILQMVmnARAAQGVDFKGWK-VIIGGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAYLNDELL 351
Cdd:cd05909 235 DKKATILLGTPTFLRGY--ARAAHPEDFSSLRlVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTPQSPNK 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 352 AGSederttyrikAGVPVPLVDAAIMDEQGRFLPADGEsQGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDG 431
Cdd:cd05909 313 EGT----------VGRPLPGMEVKIVSVETHEEVPIGE-GGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 432 MGFIEIRDRIKDVIKTGGEWLSSLELEDLISRH-PAVREVAVVGVPDPQWGERPFALLVVREGQQLDargLKEHLKpfvE 510
Cdd:cd05909 382 EGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSS---LNDILK---N 455
|
330 340 350
....*....|....*....|....*....|...
gi 15599119 511 QGNINKWaIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05909 456 AGISNLA-KPSYIHQVEEIPLLGTGKPDYVTLK 487
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
37-546 |
1.22e-45 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 169.21 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 37 VYRDQVRySYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAED 116
Cdd:PLN02860 27 ISGNRRR-TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 117 RFVLVNSEFVPLYQAV-AGQLATVERTILLTDGAEKSA-ELPGLVGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTG 194
Cdd:PLN02860 106 VMLVTDETCSSWYEELqNDRLPSLMWQVFLESPSSSVFiFLNSFLTTEMLKQRALGTTELDYAWAPDDAVLICFTSGTTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKR 274
Cdd:PLN02860 186 RPKGVTISHSALIVQSLAKIAIVG-------YGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDAKAALQAIKQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVPTILQ--MVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAK-----ARgiqLTAAYGMSETCPLISCAYL 346
Cdd:PLN02860 259 HNVTSMITVPAMMAdlISLTRKSMTWKVFPSVRKILnGGGSLSSRLLPDAKklfpnAK---LFSAYGMTEACSSLTFMTL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 347 NDELLAGSEDERTTYRI--------KAGV----PVPLVDAAI-MDEQGRflpadgesQGELVLRSPWLTQGYFRE-PERG 412
Cdd:PLN02860 336 HDPTLESPKQTLQTVNQtksssvhqPQGVcvgkPAPHVELKIgLDESSR--------VGRILTRGPHVMLGYWGQnSETA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 413 EELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVRE 492
Cdd:PLN02860 408 SVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRD 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599119 493 GQQ------LDARGLK----EHLKPFVEQGNINKWAIPSQIAVVTD-IPKTSVGKLDKKRIRIEI 546
Cdd:PLN02860 488 GWIwsdnekENAKKNLtlssETLRHHCREKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRREV 552
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
38-543 |
5.75e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 168.21 E-value: 5.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 38 YRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMdwdSHRYLECMFAI--PMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK07529 53 LDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFL---LPNLPETHFALwgGEAAGIANPINPLLEPEQIAELLRAAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRfVLVNSEFVP---LYQAVAGQLATVE--RTILLTDGAEKsaeLPGLVGEYESLLAAASPRYDFpDFDEnSIATTFYTT 190
Cdd:PRK07529 130 AK-VLVTLGPFPgtdIWQKVAEVLAALPelRTVVEVDLARY---LPGPKRLAVPLIRRKAHARIL-DFDA-ELARQPGDR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 191 GTTGNPKG-----VYFsHR-------QLVLHT----LAMASTIGSLDSirlLGTSDVYMPITPMFHVHA-WGTPYVATML 253
Cdd:PRK07529 204 LFSGRPIGpddvaAYF-HTggttgmpKLAQHThgneVANAWLGALLLG---LGPGDTVFCGLPLFHVNAlLVTGLAPLAR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 254 GVKQVYP---GRYDPELLVELWK---REKVTFSHCVPTILQMVMNaRAAQGVDFKGWKVIIGGSA-LNRSLYEAAKAR-G 325
Cdd:PRK07529 280 GAHVVLAtpqGYRGPGVIANFWKiveRYRINFLSGVPTVYAALLQ-VPVDGHDISSLRYALCGAApLPVEVFRRFEAAtG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 326 IQLTAAYGMSETCPLISCAYLNDELLAGSederttyrikAGVPVPL--VDAAIMDEQGRFL-PADGESQGELVLRSPWLT 402
Cdd:PRK07529 359 VRIVEGYGLTEATCVSSVNPPDGERRIGS----------VGLRLPYqrVRVVILDDAGRYLrDCAVDEVGVLCIAGPNVF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 403 QGYFrEPERGEELW-RGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWG 481
Cdd:PRK07529 429 SGYL-EAAHNKGLWlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAG 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599119 482 ERPFALLVVREGQQLDARGLKEHLKPFVEQgninKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK07529 508 ELPVAYVQLKPGASATEAELLAFARDHIAE----RAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
40-494 |
1.34e-44 |
|
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: 163.92 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVM-----DW---DshrylecmFAIPMIGAVLHTINIRLSPEQILYTM 111
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILsrnrpEWtiaD--------LAILAIGAVPVPIYPTSSAEQIAYIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 112 NHAEDRFVLVNSefvplyqavAGQLATvertILLTDGAeksaelpglVGeyesllaaasprydfpdfdensiattfyttg 191
Cdd:cd05907 74 NDSEAKALFVED---------PDDLAT----IIYTSGT---------TG------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 192 ttgNPKGVYFSHRQLVLHTLAMASTIGSLDSIRLLgtsdVYMPITPMFHVHAWgtPYVATMLGVKQVYPGryDPELLVEL 271
Cdd:cd05907 101 ---RPKGVMLSHRNILSNALALAERLPATEGDRHL----SFLPLAHVFERRAG--LYVPLLAGARIYFAS--SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 272 WKREKVTFSHCVPTILQMV-MNARAAQGVDFKGW-----------KVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCP 339
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVyAAIKVKAVPGLKRKlfdlavggrlrFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 340 LISCAYLNDeLLAGSEderttyrikaGVPVPLVDAAIMDEqgrflpadgesqGELVLRSPWLTQGYFREPERG-EELWRG 418
Cdd:cd05907 250 VVTLNPPGD-NRIGTV----------GKPLPGVEVRIADD------------GEILVRGPNVMLGYYKNPEATaEALDAD 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599119 419 GWMHTGDVATLDGMGFIEIRDRIKDVIKT-GGEWLSSLELEDLISRHPAVREVAVVGvpDpqwgERPF--ALLVVREGQ 494
Cdd:cd05907 307 GWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG--D----GRPFlvALIVPDPEA 379
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
42-543 |
3.90e-44 |
|
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: 164.24 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 42 VRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLV 121
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 122 NSEFVPLYQAVAGQLATVErTILLTDGAEKSAELPGLVGEYESLLAAASPRYDF--PDFD-ENSIATTFYTTGTTGNPKG 198
Cdd:cd17642 123 SKKGLQKVLNVQKKLKIIK-TIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFkpPSFDrDEQVALIMNSSGSTGLPKG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 199 VYFSHRQLVLhtlamastigSLDSIRLLGTSDVYMPITPMFHV----HAWGTPYVATML--GVKQVYPGRYDPELLVELW 272
Cdd:cd17642 202 VQLTHKNIVA----------RFSHARDPIFGNQIIPDTAILTVipfhHGFGMFTTLGYLicGFRVVLMYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR----GIQltAAYGMSETCPLIscayln 347
Cdd:cd17642 272 QDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIAsGGAPLSKEVGEAVAKRfklpGIR--QGYGLTETTSAI------ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 348 deLLAGSEDERTTyriKAGVPVPLVDAAIMD-EQGRFLPADgeSQGELVLRSPWLTQGYFREPERGEELW-RGGWMHTGD 425
Cdd:cd17642 344 --LITPEGDDKPG---AVGKVVPFFYAKVVDlDTGKTLGPN--ERGELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 426 VATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDArglKEHL 505
Cdd:cd17642 417 IAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTE---KEVM 493
|
490 500 510
....*....|....*....|....*....|....*...
gi 15599119 506 KPFVEQGNINKWaIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd17642 494 DYVASQVSTAKR-LRGGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
39-540 |
8.25e-44 |
|
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: 162.68 E-value: 8.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 39 RDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRF 118
Cdd:cd05923 24 ARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 119 VLVNSEFVPLyQAVAGQLATVERTilltdgaeksAELPGLvGEYESllaaASPRYDFPDFDENSIATTFYTTGTTGNPKG 198
Cdd:cd05923 104 AVIAVDAQVM-DAIFQSGVRVLAL----------SDLVGL-GEPES----AGPLIEDPPREPEQPAFVFYTSGTTGLPKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 199 VYFSHRQLVLHTLAMASTIGSLdsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRY-DPELLVELWKREKV 277
Cdd:cd05923 168 AVIPQRAAESRVLFMSTQAGLR-----HGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEfDPADALKLIEQERV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 278 TFSHCVPTILQMVMNARAAQGVDFKGW-KVIIGGSALNRSLYEAA-KARGIQLTAAYGMSETcplISCAYLND-----EL 350
Cdd:cd05923 243 TSLFATPTHLDALAAAAEFAGLKLSSLrHVTFAGATMPDAVLERVnQHLPGEKVNIYGTTEA---MNSLYMRDartgtEM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 351 LAGSEDERTTYRIKAGVPVPLvdaaimdeqgrflpADGEsQGELV--LRSPWLTQGYFREPERGEELWRGGWMHTGDVAT 428
Cdd:cd05923 320 RPGFFSEVRIVRIGGSPDEAL--------------ANGE-EGELIvaAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 429 LDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGqqldaRGLKEHLKPF 508
Cdd:cd05923 385 VDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-----TLSADELDQF 459
|
490 500 510
....*....|....*....|....*....|..
gi 15599119 509 VEQGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd05923 460 CRASELADFKRPRRYFFLDELPKNAMNKVLRR 491
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
41-536 |
2.43e-43 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 162.76 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 41 QVRYSYATFNERVARLANVLSEAGVKAGDTVAVMdwdSHRYLECMFA---IPMIGAVLHTINIRLSPEQILYTMNHAEDR 117
Cdd:PRK04319 71 KEKYTYKELKELSNKFANVLKELGVEKGDRVFIF---MPRIPELYFAllgALKNGAIVGPLFEAFMEEAVRDRLEDSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 118 fVLVNSEfvPLYQ-AVAGQLATVErTILLTDgaEKSAELPGLVgEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNP 196
Cdd:PRK04319 148 -VLITTP--ALLErKPADDLPSLK-HVLLVG--EDVEEGPGTL-DFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 197 KGVYFSHRQLVLHtlaMASTIGSLDsirlLGTSDVYmpitpmfhvhaW---------GTPY--VATML-GVKQV-YPGRY 263
Cdd:PRK04319 221 KGVLHVHNAMLQH---YQTGKYVLD----LHEDDVY-----------WctadpgwvtGTSYgiFAPWLnGATNViDGGRF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 264 DPELLVELWKREKVTFSHCVPTILQMVMNARA--AQGVDFKGWKVIIG-GSALNRslyEAA----KARGIQLTAAYGMSE 336
Cdd:PRK04319 283 SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDdlVKKYDLSSLRHILSvGEPLNP---EVVrwgmKVFGLPIHDNWWMTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 337 TCPLISCAYLNDELLAGSederttyrikAGVPVPLVDAAIMDEQGRFLPADGEsqGELVLRSPW--LTQGYFREPERGEE 414
Cdd:PRK04319 360 TGGIMIANYPAMDIKPGS----------MGKPLPGIEAAIVDDQGNELPPNRM--GNLAIKKGWpsMMRGIWNNPEKYES 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 415 LWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQ 494
Cdd:PRK04319 428 YFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY 507
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15599119 495 QLDARgLKEHLKPFVEQGnINKWAIPSQIAVVTDIPKTSVGK 536
Cdd:PRK04319 508 EPSEE-LKEEIRGFVKKG-LGAHAAPREIEFKDKLPKTRSGK 547
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
40-543 |
1.36e-42 |
|
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: 159.62 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFV 119
Cdd:TIGR02262 27 DISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 120 LVNSEFVPLYQAVAGQLATVERTILLTDGAEKSAELPGLVGEYESLLAAASPRYDFPDFDENSIATTFYttgttgnPKGV 199
Cdd:TIGR02262 107 FVSGALLPVIKAALGKSPHLEHRVVVGRPEAGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGM-------PKGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 200 YFSHRQLVlhtlAMASTIGSldsiRLLG--TSDVYMPITPMFHVHAWGTPYVATM-LGVKQV-YPGRYDPELLVELWKRE 275
Cdd:TIGR02262 180 VHTHSNPY----WTAELYAR----NTLGirEDDVCFSAAKLFFAYGLGNALTFPMsVGATTVlMGERPTPDAVFDRLRRH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLiscaYLNDelLAG 353
Cdd:TIGR02262 252 QPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTsAGEALPAEVGQRWQARfGVDIVDGIGSTEMLHI----FLSN--LPG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 354 SEDERTTyrikaGVPVPLVDAAIMDEQGRFLpADGESqGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMG 433
Cdd:TIGR02262 326 DVRYGTS-----GKPVPGYRLRLVGDGGQDV-ADGEP-GELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 434 FIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfveqGN 513
Cdd:TIGR02262 399 SYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVK-----DR 473
|
490 500 510
....*....|....*....|....*....|
gi 15599119 514 INKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:TIGR02262 474 LAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
37-543 |
4.86e-42 |
|
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: 156.47 E-value: 4.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 37 VYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAED 116
Cdd:cd05919 4 FYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 117 RFVLVNSEFVPLYQAVAGqlatvertillTDGAeksaelpglvgeyesllaaasprydfpdfdensiattfyttgttgnP 196
Cdd:cd05919 84 RLVVTSADDIAYLLYSSG-----------TTGP----------------------------------------------P 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 197 KGVYFSHRQLVLHTLAMASTIGSLDSirllgtSDVYMPITPMFHvhAWGT------PYV--ATMLgvkqVYPGRYDPELL 268
Cdd:cd05919 107 KGVMHAHRDPLLFADAMAREALGLTP------GDRVFSSAKMFF--GYGLgnslwfPLAvgASAV----LNPGWPTAERV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 269 VELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAYL 346
Cdd:cd05919 175 LATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsAGEALPRGLGERWMEHfGGPILDGIGATEVGHIFLSNRP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 347 nDELLAGSederttyrikAGVPVPLVDAAIMDEQGRFLPADgeSQGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDV 426
Cdd:cd05919 255 -GAWRLGS----------TGRPVPGYEIRLVDEEGHTIPPG--EEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 427 ATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREG---QQLDARGLKE 503
Cdd:cd05919 322 FCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaapQESLARDIHR 401
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599119 504 HLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05919 402 HLL-----ERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
45-543 |
5.20e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 158.55 E-value: 5.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSE 124
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 125 FVPLYQAVAGQLATVERTILLTDGAEKS-AELPGLvgeyESLLAAASPRyDFPDFDENSiATTFYTTGTTGNPKGVYFSH 203
Cdd:PRK07788 156 FTDLLSALPPDLGRLRAWGGNPDDDEPSgSTDETL----DDLIAGSSTA-PLPKPPKPG-GIVILTSGTTGTPKGAPRPE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 204 rqlvlhTLAMASTIGSLDSIRLLGTSDVYMPiTPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKREKVTFSHCV 283
Cdd:PRK07788 230 ------PSPLAPLAGLLSRVPFRAGETTLLP-APMFHATGWAHLTLAMALGSTVVLRRRFDPEATLEDIAKHKATALVVV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 284 PTILQMVMN--ARAAQGVDFKGWKVI-IGGSALNRSLYEAAKAR-GIQLTAAYGMSEtcplISCAylndeLLAGSEDER- 358
Cdd:PRK07788 303 PVMLSRILDlgPEVLAKYDTSSLKIIfVSGSALSPELATRALEAfGPVLYNLYGSTE----VAFA-----TIATPEDLAe 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 359 --TTyrikAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYF--REPERgeelwRGGWMHTGDVATLDGMGF 434
Cdd:PRK07788 374 apGT----VGRPPKGVTVKILDENGNEVPR-GVV-GRIFVGNGFPFEGYTdgRDKQI-----IDGLLSSGDVGYFDEDGL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 435 IEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfveqGNI 514
Cdd:PRK07788 443 LFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVR-----DNL 517
|
490 500
....*....|....*....|....*....
gi 15599119 515 NKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK07788 518 ARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
36-541 |
1.21e-41 |
|
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: 155.38 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:cd05930 6 VVDGDQ-SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNsefvplyqavAGQLATVertiLLTDGAEksaelpGlvgeyesllaaasprydfpdfdensiattfyttgttgN 195
Cdd:cd05930 85 AKLVLTD----------PDDLAYV----IYTSGST------G-------------------------------------K 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWGTpYVATMLGVKQVYPG---RYDPELLVEL 271
Cdd:cd05930 108 PKGVMVEHRGLVNLLLWMQEAYP-------LTPGDRVLQFTSFsFDVSVWEI-FGALLAGATLVVLPeevRKDPEALADL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 272 WKREKVTFSHCVPTILQMVMNARAAQgvDFKGWK-VIIGGSALNRSLYEA--AKARGIQLTAAYGMSETCplISCAYLNd 348
Cdd:cd05930 180 LAEEGITVLHLTPSLLRLLLQELELA--ALPSLRlVLVGGEALPPDLVRRwrELLPGARLVNLYGPTEAT--VDATYYR- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 349 ellaGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPERGEELW------RGGWMH 422
Cdd:cd05930 255 ----VPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVP-PGVP-GELYIGGAGLARGYLNRPELTAERFvpnpfgPGERMY 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 423 -TGDVATLDGMGFIEIRDRIKDVIKTGG---EwLSslELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDA 498
Cdd:cd05930 329 rTGDLVRWLPDGNLEFLGRIDDQVKIRGyriE-LG--EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDE 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15599119 499 RGLKEHLK---PFveqgninkWAIPSQIAVVTDIPKTSVGKLDKKR 541
Cdd:cd05930 406 EELRAHLAerlPD--------YMVPSAFVVLDALPLTPNGKVDRKA 443
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
57-543 |
9.86e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 155.42 E-value: 9.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 57 ANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSEF-VPLYQAVAG- 134
Cdd:PRK08751 65 AYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFgTTVQQVIADt 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 135 ---QLATVERTILLtdGAEKSA----------------ELPGLVGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGN 195
Cdd:PRK08751 145 pvkQVITTGLGDML--GFPKAAlvnfvvkyvkklvpeyRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGSldSIRLLGTSDVYMPITPMFHVHAWGTPYVATML--GVKQVYPGRYDPELLVELWK 273
Cdd:PRK08751 223 AKGAMLTHRNLVANMQQAHQWLAG--TGKLEEGCEVVITALPLYHIFALTANGLVFMKigGCNHLISNPRDMPGFVKELK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 274 REKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGS-ALNRSLYEA-AKARGIQLTAAYGMSETCPLISCAYLNDELL 351
Cdd:PRK08751 301 KTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGmAVQRSVAERwKQVTGLTLVEAYGLTETSPAACINPLTLKEY 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 352 AGSederttyrikAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGEELWRG-GWMHTGDVATLD 430
Cdd:PRK08751 381 NGS----------IGLPIPSTDACIKDDAGTVLAI-GEI-GELCIKGPQVMKGYWKRPEETAKVMDAdGWLHTGDIARMD 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 431 GMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGErPFALLVVREGQQLDARGLKEHLKpfve 510
Cdd:PRK08751 449 EQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE-IVKVVIVKKDPALTAEDVKAHAR---- 523
|
490 500 510
....*....|....*....|....*....|...
gi 15599119 511 qGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK08751 524 -ANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
196-538 |
1.45e-40 |
|
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: 149.76 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMAStigsldsIRLLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVELWKRE 275
Cdd:cd17636 15 PNGALLSHQALLAQALVLAV-------LQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLELIEAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCV-PTILQMVmNARAAQGVDFKG---------WK--VIIGGSALNRSLYeaakargiqltaAYGMSETCPLISC 343
Cdd:cd17636 88 RCTHAFLLpPTIDQIV-ELNADGLYDLSSlrsspaapeWNdmATVDTSPWGRKPG------------GYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 344 AYLNDELLAGsederttyrikAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPERGEELWRGGWMHT 423
Cdd:cd17636 155 AALGGGAIGG-----------AGRPSPLVQVRILDEDGREVP-DGEV-GEIVARGPTVMAGYWNRPEVNARRTRGGWHHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 424 GDVA--TLDG-MGFIEIRDRIkdvIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARG 500
Cdd:cd17636 222 NDLGrrEPDGsLSFVGPKTRM---IKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAE 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 15599119 501 LKEHLKPfveqgNINKWAIPSQIAVVTDIPKTSVGKLD 538
Cdd:cd17636 299 LIEHCRA-----RIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
36-538 |
1.85e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 153.89 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK07798 22 LVCGDR-RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAEkSAELPGLVgEYESLLAAASPRYDF----PD------------Fd 179
Cdd:PRK07798 101 AVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSG-NDLLPGAV-DYEDALAAGSPERDFgersPDdlyllytggttgM- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 180 ensiattfyttgttgnPKGVYFSHRQLVlHTLAMASTIGSLDSIRLL---------GTSDVYMPITPMFHVHAWGTPYVA 250
Cdd:PRK07798 178 ----------------PKGVMWRQEDIF-RVLLGGRDFATGEPIEDEeelakraaaGPGMRRFPAPPLMHGAGQWAAFAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 251 TMLGVKQV-YPG-RYDPELLVELWKREKVtfshcvpTILQMVMNA---------RAAQGVDFKGWKVIIGGSALnrsLYE 319
Cdd:PRK07798 241 LFSGQTVVlLPDvRFDADEVWRTIEREKV-------NVITIVGDAmarplldalEARGPYDLSSLFAIASGGAL---FSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 320 AAKAR------GIQLTAAYGMSETcpliscAYLNDELLAGSEDERTTYRIKAGvpvplVDAAIMDEQGRFLPAdGESQGE 393
Cdd:PRK07798 311 SVKEAllellpNVVLTDSIGSSET------GFGGSGTVAKGAVHTGGPRFTIG-----PRTVVLDEDGNPVEP-GSGEIG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 394 LVLRSPWLTQGYFREPERGEELWR--GG--WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVRE 469
Cdd:PRK07798 379 WIARRGHIPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAD 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599119 470 VAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLD 538
Cdd:PRK07798 459 ALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHC-----RSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
43-543 |
9.41e-40 |
|
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: 150.28 E-value: 9.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTInirlspeqilytmnhaedrFVLVN 122
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL-------------------FALFG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEfvplyqAVAGQLATVERTILLTDGAEKSAEL---PGLVGeyesllaaasprydfpdfdensiattfyttgttgNPKGV 199
Cdd:cd05971 67 PE------ALEYRLSNSGASALVTDGSDDPALIiytSGTTG----------------------------------PPKGA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 200 YFSHRQLVLH------TLAMASTIGSL-----DSIRLLGTSDVYMPITpmfhvhAWGTPYVATMlgvkqvyPGRYDPELL 268
Cdd:cd05971 107 LHAHRVLLGHlpgvqfPFNLFPRDGDLywtpaDWAWIGGLLDVLLPSL------YFGVPVLAHR-------MTKFDPKAA 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 269 VELWKREKVTFSHCVPTILQMVmnarAAQGVDFKGWK-----VIIGGSALNRSLYEAAK-ARGIQLTAAYGMSETCPLI- 341
Cdd:cd05971 174 LDLMSRYGVTTAFLPPTALKMM----RQQGEQLKHAQvklraIATGGESLGEELLGWAReQFGVEVNEFYGQTECNLVIg 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 342 SCAYLNDeLLAGSederttyrikAGVPVPLVDAAIMDEQGRFLPADGEsqGELVLRSPWLTQ--GYFREPERGEELWRGG 419
Cdd:cd05971 250 NCSALFP-IKPGS----------MGKPIPGHRVAIVDDNGTPLPPGEV--GEIAVELPDPVAflGYWNNPSATEKKMAGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 420 WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGqQLDAR 499
Cdd:cd05971 317 WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPG-ETPSD 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15599119 500 GLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05971 396 ALAREIQELVKT-RLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
41-537 |
1.10e-39 |
|
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: 152.73 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 41 QVR-YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFV 119
Cdd:cd17634 81 QSRtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 120 LVNSEF------VPLYQAVAGQL---ATVERTILLTD--GAEKSAElPGLVGEYESLLAAASPRYDFPDFDENSIATTFY 188
Cdd:cd17634 161 ITADGGvragrsVPLKKNVDDALnpnVTSVEHVIVLKrtGSDIDWQ-EGRDLWWRDLIAKASPEHQPEAMNAEDPLFILY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 189 TTGTTGNPKGVYFSHRQlvlHTLAMASTIGSLDSIrllGTSDVYMPITPMFHV--HAWgTPYVATMLGVKQVY----PGR 262
Cdd:cd17634 240 TSGTTGKPKGVLHTTGG---YLVYAATTMKYVFDY---GPGDIYWCTADVGWVtgHSY-LLYGPLACGATTLLyegvPNW 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 263 YDPELLVELWKREKVTFSHCVPTILQMVMNA--RAAQGVDFKGWKVIIG-GSALNRSLYE-AAKARGiqltaaygmSETC 338
Cdd:cd17634 313 PTPARMWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSvGEPINPEAYEwYWKKIG---------KEKC 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 339 PLISCAYLNDELLAGSEDERTTYRIKAG---VPVPLVDAAIMDEQGRflPADGESQGELVLRSPW--LTQGYFREPERGE 413
Cdd:cd17634 384 PVVDTWWQTETGGFMITPLPGAIELKAGsatRPVFGVQPAVVDNEGH--PQPGGTEGNLVITDPWpgQTRTLFGDHERFE 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 414 E-LWR---GGWMHtGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLV 489
Cdd:cd17634 462 QtYFStfkGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVV 540
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15599119 490 VREGQQlDARGLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKL 537
Cdd:cd17634 541 LNHGVE-PSPELYAELRNWVRK-EIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
7-545 |
3.88e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 150.59 E-value: 3.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 7 IPAAAGAYQYPLLIKSLMLSGRRYEksheivyrDQVRY-------SYATFNERVARLANVL-SEAGVKAGDTVAVMDWDS 78
Cdd:PRK08974 13 VPAEINPDRYQSLVDMFEQAVARYA--------DQPAFinmgevmTFRKLEERSRAFAAYLqNGLGLKKGDRVALMMPNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 79 HRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLAtVERTILLTDGAEKSA----- 153
Cdd:PRK08974 85 LQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTP-VKHVILTRMGDQLSTakgtl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 154 ---------------ELPGLVGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIG 218
Cdd:PRK08974 164 vnfvvkyikrlvpkyHLPDAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 219 SL--DSIRLLGTSdvympiTPMFHVHAwgtpyvATM-------LGVKQVY---PgRYDPELLVELwKREKVTFSHCVPTI 286
Cdd:PRK08974 244 PLlhPGKELVVTA------LPLYHIFA------LTVncllfieLGGQNLLitnP-RDIPGFVKEL-KKYPFTAITGVNTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 287 LQMVMNARAAQGVDFKGWKVIIGGS-ALNRSLYEA-AKARGIQLTAAYGMSETCPLISCAYLNDELLAGSederttyrik 364
Cdd:PRK08974 310 FNALLNNEEFQELDFSSLKLSVGGGmAVQQAVAERwVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGS---------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 365 AGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDV 444
Cdd:PRK08974 380 IGLPVPSTEIKLVDDDGNEVPP-GEP-GELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDM 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 445 IKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERpFALLVVREGQQLDARGLKEHLKPfveqgNINKWAIPSQIA 524
Cdd:PRK08974 458 ILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLTEEELITHCRR-----HLTGYKVPKLVE 531
|
570 580
....*....|....*....|.
gi 15599119 525 VVTDIPKTSVGKLDKKRIRIE 545
Cdd:PRK08974 532 FRDELPKSNVGKILRRELRDE 552
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
195-543 |
6.07e-39 |
|
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: 145.17 E-value: 6.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVlhtlamASTIGSLDSIRLLGtSDVYMPITPMFHVHAWGtPYVATMLGVKQVYPGRYDPELLVELwKR 274
Cdd:cd17630 14 TPKAVVHTAANLL------ASAAGLHSRLGFGG-GDSWLLSLPLYHVGGLA-ILVRSLLAGAELVLLERNQALAEDL-AP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVPTILQMVMNARAAQGvDFKGWKVI-IGGSALNRSLYEAAKARGIQLTAAYGMSETCPLISCAYLNDELLAG 353
Cdd:cd17630 85 PGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVlLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 354 SederttyrikaGVPVPLVDAAIMDeqgrflpadgesQGELVLRSPWLTQGYFREPERgEELWRGGWMHTGDVATLDGMG 433
Cdd:cd17630 164 V-----------GVLLPGRELRIVE------------DGEIWVGGASLAMGYLRGQLV-PEFNEDGWFTTKDLGELHADG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 434 FIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDArgLKEHLkpfveQGN 513
Cdd:cd17630 220 RLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAE--LRAWL-----KDK 292
|
330 340 350
....*....|....*....|....*....|
gi 15599119 514 INKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd17630 293 LARFKLPKRIYPVPELPRTGGGKVDRRALR 322
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
40-543 |
7.80e-39 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 148.87 E-value: 7.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHR----YLECMFAipmiGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK07514 25 DGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEalalYLATLRA----GAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFVPLYQAVAGQLATverTILLTDGAEKSAELPglvgeyeSLLAAASPRYDFPDFDENSIATTFYTTGTTGN 195
Cdd:PRK07514 101 PALVVCDPANFAWLSKIAAAAGA---PHVETLDADGTGSLL-------EAAAAAPDDFETVPRGADDLAAILYTSGTTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWgtpYVAT----MLGVKQVYPGRYDPELLVEL 271
Cdd:PRK07514 171 SKGAMLSHGNLLSNALTLVDYWR-------FTPDDVLIHALPIFHTHGL---FVATnvalLAGASMIFLPKFDPDAVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 272 WKREKVTFShcVPTI-LQMVMNAR----AAQGVdfkgwKVIIGGSA-LNRSLYEAAKAR-GIQLTAAYGMSETCPLISCA 344
Cdd:PRK07514 241 MPRATVMMG--VPTFyTRLLQEPRltreAAAHM-----RLFISGSApLLAETHREFQERtGHAILERYGMTETNMNTSNP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 345 YlNDELLAGSederttyrikAGVPVPLVDAAIMD-EQGRFLPAdGESqGELVLRSPWLTQGYFREPER-GEELWRGGWMH 422
Cdd:PRK07514 314 Y-DGERRAGT----------VGFPLPGVSLRVTDpETGAELPP-GEI-GMIEVKGPNVFKGYWRMPEKtAEEFRADGFFI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 423 TGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLK 502
Cdd:PRK07514 381 TGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAIL 460
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15599119 503 EHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK07514 461 AALK-----GRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
43-543 |
2.57e-38 |
|
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: 148.03 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:cd05970 47 IFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SE-FVP-LYQAVAGQLATVERTILLTDgaeksAELPGLVgEYESLLAAASPryDFPDFDENS------IATTFYTTGTTG 194
Cdd:cd05970 127 AEdNIPeEIEKAAPECPSKPKLVWVGD-----PVPEGWI-DFRKLIKNASP--DFERPTANSypcgedILLVYFSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHtLAMASTIGSLDSirllgtSDVYMPITPMFHVHA-WGTPYVATMLGVKQ-VYP-GRYDPELLVEL 271
Cdd:cd05970 199 MPKMVEHDFTYPLGH-IVTAKYWQNVRE------GGLHLTVADTGWGKAvWGKIYGQWIAGAAVfVYDyDKFDPKALLEK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 272 WKREKVTfSHCVP-TILQMVMNARAAQgVDFKGWK-VIIGGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLIScAYLND 348
Cdd:cd05970 272 LSKYGVT-TFCAPpTIYRFLIREDLSR-YDLSSLRyCTTAGEALNPEVFNTFKEKtGIKLMEGFGQTETTLTIA-TFPWM 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 349 ELLAGSederttyrikAGVPVPLVDAAIMDEQGRFLPAdGEsQGELVLRS----PW-LTQGYFREPERGEELWRGGWMHT 423
Cdd:cd05970 349 EPKPGS----------MGKPAPGYEIDLIDREGRSCEA-GE-EGEIVIRTskgkPVgLFGGYYKDAEKTAEVWHDGYYHT 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 424 GDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQlDARGLKE 503
Cdd:cd05970 417 GDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYE-PSEELKK 495
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599119 504 HLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05970 496 ELQDHVKK-VTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
196-539 |
3.09e-38 |
|
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: 143.41 E-value: 3.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQlvlhTLAMASTIGSLDSIRllgTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYP-GRYDPELLVELWKR 274
Cdd:cd17638 15 SKGVMCAHRQ----TLRAAAAWADCADLT---EDDRYLIINPFFHTFGYKAGIVACLLTGATVVPvAVFDVDAILEAIER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVPTILQMVMNARAAQGVDFKGWKV-IIGGSALNRSLYEAAKAR-GIQ-LTAAYGMSETCPLISCAylndell 351
Cdd:cd17638 88 ERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAaVTGAATVPVELVRRMRSElGFEtVLTAYGLTEAGVATMCR------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 352 agSEDERTTYRIKAGVPVPLVDAAIMDeqgrflpadgesQGELVLRSPWLTQGYFREPERGEE-LWRGGWMHTGDVATLD 430
Cdd:cd17638 161 --PGDDAETVATTCGRACPGFEVRIAD------------DGEVLVRGYNVMQGYLDDPEATAEaIDADGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 431 GMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGL----KEHLK 506
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDViawcRERLA 306
|
330 340 350
....*....|....*....|....*....|...
gi 15599119 507 PFveqgninkwAIPSQIAVVTDIPKTSVGKLDK 539
Cdd:cd17638 307 NY---------KVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
34-553 |
7.21e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 146.38 E-value: 7.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 34 HEIVYRDQVRySYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNH 113
Cdd:PRK12406 3 ATIISGDRRR-SFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 114 AEDRfVLVNSefVPLYQAVAGQL-ATVERTILLTDG--------AEKSAELPGLVGEYESLLAAASPrYDFPDFDENsiA 184
Cdd:PRK12406 82 SGAR-VLIAH--ADLLHGLASALpAGVTVLSVPTPPeiaaayriSPALLTPPAGAIDWEGWLAQQEP-YDGPPVPQP--Q 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 185 TTFYTTGTTGNPKGVyfsHR-----QLVLHTLAMASTI-GSLDSIRLLGTSdvympitPMFHVHAWGTPYVATMLGVKQV 258
Cdd:PRK12406 156 SMIYTSGTTGHPKGV---RRaaptpEQAAAAEQMRALIyGLKPGIRALLTG-------PLYHSAPNAYGLRAGRLGGVLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 259 YPGRYDPELLVELWKREKVTFSHCVPTILQMVMNARAA--QGVDFKGWKVIIGGSA-----LNRSLYEAAkarGIQLTAA 331
Cdd:PRK12406 226 LQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAApcpadVKRAMIEWW---GPVIYEY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 332 YGMSETCPLIscaylndelLAGSEDErTTYRIKAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQ-GYFREPE 410
Cdd:PRK12406 303 YGSTESGAVT---------FATSEDA-LSHPGTVGKAAPGAELRFVDEDGRPLP-QGEI-GEIYSRIAGNPDfTYHNKPE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 411 RGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVV 490
Cdd:PRK12406 371 KRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEP 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599119 491 REGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRieIAQWQEAG 553
Cdd:PRK12406 451 QPGATLDEADIRAQLK-----ARLAGYKVPKHIEIMAELPREDSGKIFKRRLR--DPYWANAG 506
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
23-537 |
8.28e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 146.64 E-value: 8.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 23 LMLSGRRYEKSHEIVYRDQvRYSYATFNERVARLANVL-SEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIR 101
Cdd:PRK08314 16 LEVSARRYPDKTAIVFYGR-AISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 102 LSPEQILYTMNHAEDRFVLVNSEFVP----------LYQAVAGQLA---TVERTILLTDGAEKSAELPGLVGE-----YE 163
Cdd:PRK08314 95 NREEELAHYVTDSGARVAIVGSELAPkvapavgnlrLRHVIVAQYSdylPAEPEIAVPAWLRAEPPLQALAPGgvvawKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 164 SLLAAASPRYDFPDFDEnsIATTFYTTGTTGNPKGVYFSHRQlVLHTLAMASTIGSLDSirllgtSDVYMPITPMFHVha 243
Cdd:PRK08314 175 ALAAGLAPPPHTAGPDD--LAVLPYTSGTTGVPKGCMHTHRT-VMANAVGSVLWSNSTP------ESVVLAVLPLFHV-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 244 wgTPYVATMLGvkQVYPG-------RYDPELLVELWKREKVTFSHCVPTilqMVMNARAAQGV---DFKGWKVIIGGSAl 313
Cdd:PRK08314 244 --TGMVHSMNA--PIYAGatvvlmpRWDREAAARLIERYRVTHWTNIPT---MVVDFLASPGLaerDLSSLRYIGGGGA- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 314 nrSLYEAAKAR-----GIQLTAAYGMSETcplISCAYLNdellagsederTTYRIK---AGVPVPLVDAAIMD-EQGRFL 384
Cdd:PRK08314 316 --AMPEAVAERlkeltGLDYVEGYGLTET---MAQTHSN-----------PPDRPKlqcLGIPTFGVDARVIDpETLEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 385 PaDGEsQGELVLRSPWLTQGYFREPERGEELW--RGG--WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDL 460
Cdd:PRK08314 380 P-PGE-VGEIVVHGPQVFKGYWNRPEATAEAFieIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 461 ISRHPAVREVAVVGVPDPQWGERPFALLVVREGqqldARGLkehlkpfVEQGNINKWA--------IPSQIAVVTDIPKT 532
Cdd:PRK08314 458 LYKHPAIQEACVIATPDPRRGETVKAVVVLRPE----ARGK-------TTEEEIIAWArehmaaykYPRIVEFVDSLPKS 526
|
....*
gi 15599119 533 SVGKL 537
Cdd:PRK08314 527 GSGKI 531
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
7-543 |
2.68e-36 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 142.47 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 7 IPAAAGAYQYPLLIKSLMLSGRRYEKSHEIVYRDQVrYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMF 86
Cdd:PRK07059 13 VPAEIDASQYPSLADLLEESFRQYADRPAFICMGKA-ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 87 AIPMIGAVLHTINIRLSPEQILYTMNH--AEDRFVLVNseFVPLYQAVAGQLAtVERTILLTDG---------------- 148
Cdd:PRK07059 92 AVLRAGYVVVNVNPLYTPRELEHQLKDsgAEAIVVLEN--FATTVQQVLAKTA-VKHVVVASMGdllgfkghivnfvvrr 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 149 AEK---SAELPGLVGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGSLDSIRL 225
Cdd:PRK07059 169 VKKmvpAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 226 LGTSDVYMPITPMFHVHAWGTPYVATML--GVKQVYPGRYD-PELLVELwKREKVTFSHCVPTILQMVMNARAAQGVDFK 302
Cdd:PRK07059 249 RPDQLNFVCALPLYHIFALTVCGLLGMRtgGRNILIPNPRDiPGFIKEL-KKYQVHIFPAVNTLYNALLNNPDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 303 GWKVIIGGS-ALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAYLNDELLAGSederttyrikAGVPVPLVDAAIMDEQ 380
Cdd:PRK07059 328 KLIVANGGGmAVQRPVAERWLEMtGCPITEGYGLSETSPVATCNPVDATEFSGT----------IGLPLPSTEVSIRDDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 381 GRFLPAdGESqGELVLRSPWLTQGYFREP-ERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELED 459
Cdd:PRK07059 398 GNDLPL-GEP-GEICIRGPQVMAGYWNRPdETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 460 LISRHPAVREVAVVGVPDPQWGERPfALLVVREGQQLDARGLKEHLKPfveqgNINKWAIPSQIAVVTDIPKTSVGKLDK 539
Cdd:PRK07059 476 VVASHPGVLEVAAVGVPDEHSGEAV-KLFVVKKDPALTEEDVKAFCKE-----RLTNYKRPKFVEFRTELPKTNVGKILR 549
|
....
gi 15599119 540 KRIR 543
Cdd:PRK07059 550 RELR 553
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-548 |
1.81e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 136.46 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 225 LLGTSDVYMPITPMFHVHAwGTPYVATML--GVKQVYP---GRYDPELLVELWK---REKVTFSHCVPTILQMVMnaRAA 296
Cdd:cd05944 39 LFDPDDVLLCGLPLFHVNG-SVVTLLTPLasGAHVVLAgpaGYRNPGLFDNFWKlveRYRITSLSTVPTVYAALL--QVP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 297 QGVDFKGWK-VIIGGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAYLNDELLAGSederttyrikAGVPVP--LV 372
Cdd:cd05944 116 VNADISSLRfAMSGAAPLPVELRARFEDAtGLPVVEGYGLTEATCLVAVNPPDGPKRPGS----------VGLRLPyaRV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 373 DAAIMDEQGRFL-PADGESQGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEW 451
Cdd:cd05944 186 RIKVLDGVGRLLrDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHN 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 452 LSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKPFVEQgninKWAIPSQIAVVTDIPK 531
Cdd:cd05944 266 IDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARDHVPE----RAAVPKHIEVLEELPV 341
|
330
....*....|....*..
gi 15599119 532 TSVGKLDKKRIRIEIAQ 548
Cdd:cd05944 342 TAVGKVFKPALRADAIH 358
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
37-543 |
4.57e-35 |
|
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: 137.22 E-value: 4.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 37 VYRDQVRYSYATFNERVARLANVL-SEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:cd05958 4 LRSPEREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVnsefvplyqavAGQLATVERTILLtdgaeksAELPGLVGEyesllaaasprydfpdfdensiattfyttgttgn 195
Cdd:cd05958 84 ITVALC-----------AHALTASDDICIL-------AFTSGTTGA---------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLvlhtLAMASTIGsldsIRLLG--TSDVYMPITPMFHVHAWGTPYVATM-LGVKQVYPGRYDPELLVELW 272
Cdd:cd05958 112 PKATMHFHRDP----LASADRYA----VNVLRlrEDDRFVGSPPLAFTFGLGGVLLFPFgVGASGVLLEEATPDLLLSAI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSHCVPTILQMVMNARAAQGVDFKGW-KVIIGGSALNRSLYEAAK-ARGIQLTAAYGMSETCPL-ISCAylNDE 349
Cdd:cd05958 184 ARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLrKCVSAGEALPAALHRAWKeATGIPIIDGIGSTEMFHIfISAR--PGD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 350 LLAGSederttyrikAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPERgeELWRGGWMHTGDVATL 429
Cdd:cd05958 262 ARPGA----------TGKPVPGYEAKVVDDEGNPVP-DGTI-GRLAVRGPTGCRYLADKRQR--TYVQGGWNITGDTYSR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 430 DGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLD---ARGLKEHLK 506
Cdd:cd05958 328 DPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpvlARELQDHAK 407
|
490 500 510
....*....|....*....|....*....|....*..
gi 15599119 507 pfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05958 408 -----AHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
140-543 |
7.48e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 137.04 E-value: 7.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 140 ERTILLTDGA------EKSAELPGLVGEYESLLAAASPRYDFPDfdENSIATTFYTTGTTGNPKGVYFSHRqlvlhtlAM 213
Cdd:PRK07787 83 ERRHILADSGaqawlgPAPDDPAGLPHVPVRLHARSWHRYPEPD--PDAPALIVYTSGTTGPPKGVVLSRR-------AI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 214 ASTIGSLDSIRLLGTSDVYMPITPMFHVHAwgtpyvaTMLGV--------KQVYPGRYDPELLV-ELWKREKVTFShcVP 284
Cdd:PRK07787 154 AADLDALAEAWQWTADDVLVHGLPLFHVHG-------LVLGVlgplrignRFVHTGRPTPEAYAqALSEGGTLYFG--VP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 285 TILQMVMNARAAQGVdFKGWKVIIGGSA-LNRSLYEA-AKARGIQLTAAYGMSETcpLISCAYLND-ELLAGSedertty 361
Cdd:PRK07787 225 TVWSRIAADPEAARA-LRGARLLVSGSAaLPVPVFDRlAALTGHRPVERYGMTET--LITLSTRADgERRPGW------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 362 rikAGVPVPLVDAAIMDEQGRFLPADGESQGELVLRSPWLTQGYFREPERGEELWRG-GWMHTGDVATLDGMGFIEIRDR 440
Cdd:PRK07787 295 ---VGLPLAGVETRLVDEDGGPVPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTAdGWFRTGDVAVVDPDGMHRIVGR 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 441 IK-DVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGqqLDARGLKEHLkpfVEQGNINKWai 519
Cdd:PRK07787 372 EStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD--VAADELIDFV---AQQLSVHKR-- 444
|
410 420
....*....|....*....|....
gi 15599119 520 PSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK07787 445 PREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
196-545 |
6.09e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 135.66 E-value: 6.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGSldsiRLLGTSDVYMPITPMFHVHAWGTPYVATML-GVKQVY-PGRYD-PELLVELW 272
Cdd:PRK05677 222 AKGAMLTHRNLVANMLQCRALMGS----NLNEGCEILIAPLPLYHIYAFTFHCMAMMLiGNHNILiSNPRDlPAMVKELG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREkvtFSHCV--PTILQMVMNARAAQGVDFKGWKVII-GGSALNRSLYEAAKA-RGIQLTAAYGMSETCPLISCAYLND 348
Cdd:PRK05677 298 KWK---FSGFVglNTLFVALCNNEAFRKLDFSALKLTLsGGMALQLATAERWKEvTGCAICEGYGMTETSPVVSVNPSQA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 349 ELLAgsederttyriKAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGEE-LWRGGWMHTGDVA 427
Cdd:PRK05677 375 IQVG-----------TIGIPVPSTLCKVIDDDGNELPL-GEV-GELCVKGPQVMKGYWQRPEATDEiLDSDGWLKTGDIA 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 428 TLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKp 507
Cdd:PRK05677 442 LIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMR- 520
|
330 340 350
....*....|....*....|....*....|....*...
gi 15599119 508 fveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIE 545
Cdd:PRK05677 521 ----ANLTGYKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
36-543 |
1.10e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 134.26 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK08276 4 IMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFVPLYQAVAGQLATVERTILLTDGaeksaELPGlVGEYESLLAAASPrYDFPdfDENSIATTFYTTGTTGN 195
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAG-----PVPG-FRSYEEALAAQPD-TPIA--DETAGADMLYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVY--FSHRQlVLHTLAMASTIGSLDsiRLLGTSDVYMPITPMFH--VHAWGTpyVATMLGVKQVYPGRYDPELLVEL 271
Cdd:PRK08276 155 PKGIKrpLPGLD-PDEAPGMMLALLGFG--MYGGPDSVYLSPAPLYHtaPLRFGM--SALALGGTVVVMEKFDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 272 WKREKVTFSHCVPT----ILQMVMNARAAQGVdfkgwkviiggSALNRSLYEAA------KARGIQ-----LTAAYGMSE 336
Cdd:PRK08276 230 IERYRVTHSQLVPTmfvrMLKLPEEVRARYDV-----------SSLRVAIHAAApcpvevKRAMIDwwgpiIHEYYASSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 337 TcpliscaylNDELLAGSEDERtTYRIKAGVPVpLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGEELW 416
Cdd:PRK08276 299 G---------GGVTVITSEDWL-AHPGSVGKAV-LGEVRILDEDGNELPP-GEI-GTVYFEMDGYPFEYHNDPEKTAAAR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 417 RG-GWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQ 495
Cdd:PRK08276 366 NPhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15599119 496 LDArGLKEHLKPFVEqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK08276 446 AGD-ALAAELIAWLR-GRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
37-541 |
1.13e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 130.64 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 37 VYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAED 116
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 117 RFVLVNSEfvplyqavagqlatvertilltdgaEKSAELPglvgeYESllaaasprydfpdfdensiattfyttGTTGNP 196
Cdd:cd05914 81 KAIFVSDE-------------------------DDVALIN-----YTS--------------------------GTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 197 KGVYFSHRQLVlhtlamaSTIGSLDSIRLLGTSDVYMPITPMFHVHAWGTPYV-ATMLGVKQVYPGRYdPELLVELWKRE 275
Cdd:cd05914 105 KGVMLTYRNIV-------SNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLlPLLNGAHVVFLDKI-PSAKIIALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTILQM-------VMNARAAQGVDFK--------------GWKV-----------IIGGSALNRSLYEAAKA 323
Cdd:cd05914 177 QVTPTLGVPVPLVIekifkmdIIPKLTLKKFKFKlakkinnrkirklaFKKVheafggnikefVIGGAKINPDVEEFLRT 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 324 RGIQLTAAYGMSETCPLISCAYLNDELLAgsederttyriKAGVPVPLVDAAIMDEQgrflPADGEsqGELVLRSPWLTQ 403
Cdd:cd05914 257 IGFPYTIGYGMTETAPIISYSPPNRIRLG-----------SAGKVIDGVEVRIDSPD----PATGE--GEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 404 GYFREPERGEELW-RGGWMHTGDVATLDGMGFIEIRDRIKDVIKTG-GEWLSSLELEDLISRHPAV----------REVA 471
Cdd:cd05914 320 GYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVleslvvvqekKLVA 399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599119 472 VVgVPDPQwgerpfALLVVREGQQLDARGLKEHLKPFVEQgNINKWAIPSQIAVV-TDIPKTSVGKLdkKR 541
Cdd:cd05914 400 LA-YIDPD------FLDVKALKQRNIIDAIKWEVRDKVNQ-KVPNYKKISKVKIVkEEFEKTPKGKI--KR 460
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
37-540 |
3.69e-32 |
|
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: 129.70 E-value: 3.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 37 VYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLhtinIRLSPEqilytmnHAED 116
Cdd:cd17646 17 VVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAY----LPLDPG-------YPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 117 RfvlvnsefvplyqaVAGQLATVERTILLTDG--AEKSAELPGLVGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTG 194
Cdd:cd17646 86 R--------------LAYMLADAGPAVVLTTAdlAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWGTpYVATMLGVKQVYP---GRYDPELLVE 270
Cdd:cd17646 152 RPKGVMVTHAGIVNRLLWMQDEYP-------LGPGDRVLQKTPLsFDVSVWEL-FWPLVAGARLVVArpgGHRDPAYLAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 271 LWKREKVTFSHCVPTILQMVMNARAAQgvdfkGW----KVIIGGSALNRSLYEAAKAR-GIQLTAAYGMSETCPliscay 345
Cdd:cd17646 224 LIREHGVTTCHFVPSMLRVFLAEPAAG-----SCaslrRVFCSGEALPPELAARFLALpGAELHNLYGPTEAAI------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 346 lnDELLAGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREP----ER--------GE 413
Cdd:cd17646 293 --DVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPV-GVP-GELYLGGVQLARGYLGRPaltaERfvpdpfgpGS 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 414 ELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREG 493
Cdd:cd17646 369 RMYR-----TGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15599119 494 QQ-LDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd17646 444 AAgPDTAALRAHLA-----ERLPEYMVPAAFVVLDALPLTANGKLDRA 486
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
33-541 |
8.98e-32 |
|
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: 128.18 E-value: 8.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 33 SHEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMN 112
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 113 HAEDRFVLVNSEfvpLYQAVAGQLATVERTilltdgaeksaeLPGLVGEYESLLAAASPrydfpdfdeNSIATTFYTTGT 192
Cdd:cd12116 82 DAEPALVLTDDA---LPDRLPAGLPVLLLA------------LAAAAAAPAAPRTPVSP---------DDLAYVIYTSGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 193 TGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITP---------MFhvhawgTPYVATmlGVKQVYPG-- 261
Cdd:cd12116 138 TGRPKGVVVSHRNLVNFLHSMRERLG-------LGPGDRLLAVTTyafdislleLL------LPLLAG--ARVVIAPRet 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 262 RYDPELLVELWKREKVTFSHCVPTILQMVMnarAAQGVDFKGWKVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLI 341
Cdd:cd12116 203 QRDPEALARLIEAHSITVMQATPATWRMLL---DAGWQGRAGLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWS 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 342 SCAYLNDELLAgsederttyrIKAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPER---------- 411
Cdd:cd12116 280 TAARVTAAAGP----------IPIGRPLANTQVYVLDAALRPVPP-GVP-GELYIGGDGVAQGYLGRPALtaerfvpdpf 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 412 ---GEELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQwGERPFALL 488
Cdd:cd12116 348 agpGSRLYR-----TGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG-DRRLVAYV 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15599119 489 VVREGQQLDARGLKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKKR 541
Cdd:cd12116 422 VLKAGAAPDAAALRAHL-----RATLPAYMVPSAFVRLDALPLTANGKLDRKA 469
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
44-552 |
1.88e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 128.17 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNS 123
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTND 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 efvplyqavagqlatvertilLTDGAEKSAELPGLV-GE--------YESLLAAASPRYDFPDFDE---NSIATTFYTTG 191
Cdd:PLN02330 136 ---------------------TNYGKVKGLGLPVIVlGEekiegavnWKELLEAADRAGDTSDNEEilqTDLCALPFSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 192 TTGNPKGVYFSHRQLVlhtlamASTIGSLDSIR--LLGTSdVYMPITPMFHVHAWGTPYVATMLGV-KQVYPGRYDPELL 268
Cdd:PLN02330 195 TTGISKGVMLTHRNLV------ANLCSSLFSVGpeMIGQV-VTLGLIPFFHIYGITGICCATLRNKgKVVVMSRFELRTF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 269 VELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWK---VIIGGSALNRSLYEA--AKARGIQLTAAYGMSETcpliSC 343
Cdd:PLN02330 268 LNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlqaIMTAAAPLAPELLTAfeAKFPGVQVQEAYGLTEH----SC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 344 AYLNDEllAGSEDERTTYRIKAGVPVPLVDAAIMD-EQGRFLPADgeSQGELVLRSPWLTQGYF-REPERGEELWRGGWM 421
Cdd:PLN02330 344 ITLTHG--DPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKN--TPGELCVRSQCVMQGYYnNKEETDRTIDEDGWL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 422 HTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREgqqlDARGL 501
Cdd:PLN02330 420 HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINP----KAKES 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15599119 502 KEHLKPFVeQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQWQEA 552
Cdd:PLN02330 496 EEDILNFV-AANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINKA 545
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
42-546 |
2.07e-31 |
|
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: 127.09 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 42 VRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLV 121
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 122 -NSEfvplyqavaGQLATvertILLTDGAeksaelpglvgeyesllaaasprydfpdfdensiattfyttgtTGNPKGVY 200
Cdd:cd17640 84 eNDS---------DDLAT----IIYTSGT-------------------------------------------TGNPKGVM 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 201 FSHRQLVlhtlamaSTIGSLDSIRLLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPG---------RYDPELLVE- 270
Cdd:cd17640 108 LTHANLL-------HQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSirtlkddlkRVKPHYIVSv 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 271 --LWK------REKVTFShcvPTILQMVMNArAAQGVDFKgwKVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLIS 342
Cdd:cd17640 181 prLWEslysgiQKQVSKS---SPIKQFLFLF-FLSGGIFK--FGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 343 CAYLnDELLAGSederttyrikAGVPVPLVDAAIMDEQGR-FLPAdgESQGELVLRSPWLTQGYFREPERGEE-LWRGGW 420
Cdd:cd17640 255 ARRL-KCNVRGS----------VGRPLPGTEIKIVDPEGNvVLPP--GEKGIVWVRGPQVMKGYYKNPEATSKvLDSDGW 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 421 MHTGDVATLDGMGFIEIRDRIKDVIK-TGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGerpfALLVvregqqldar 499
Cdd:cd17640 322 FNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG----ALIV---------- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15599119 500 glkehlkPFVEQgnINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEI 546
Cdd:cd17640 388 -------PNFEE--LEKWAKESGVKLANDRSQLLASKKVLKLYKNEI 425
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
196-548 |
4.29e-31 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 128.89 E-value: 4.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLvlhtlamASTIGSLDSIRLLGTSDVYMPITPMFHvhAWG---TPYVATMLGVKQVY-PGRYDPELLVEL 271
Cdd:PRK08633 797 PKGVMLSHHNI-------LSNIEQISDVFNLRNDDVILSSLPFFH--SFGltvTLWLPLLEGIKVVYhPDPTDALGIAKL 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 272 WKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGS-ALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAyLNDE 349
Cdd:PRK08633 868 VAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAeKLKPEVADAFEEKfGIRILEGYGATETSPVASVN-LPDV 946
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 350 LLAGSEDERTTYRIKAGVPVPLVDAAIMD-EQGRFLPAdGEsQGELVLRSPWLTQGYFREPERGEELWR----GGWMHTG 424
Cdd:PRK08633 947 LAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPP-GE-DGLILIGGPQVMKGYLGDPEKTAEVIKdidgIGWYVTG 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 425 DVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISR--HPAVREVAVVGVPDPQWGERpfaLLVVREGQQLDARGLK 502
Cdd:PRK08633 1025 DKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGEK---LVVLHTCGAEDVEELK 1101
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15599119 503 EHLKpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRiEIAQ 548
Cdd:PRK08633 1102 RAIK----ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLK-ELAL 1142
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
197-547 |
5.33e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 126.86 E-value: 5.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 197 KGVYFSHRQLV---LHTLAMASTIGSLDSIRLLGTSDVYMPITPMFHVHAWGTPYVATML----GVKQVYPgRYDPELLV 269
Cdd:PRK12492 223 KGAMLTHGNLVanmLQVRACLSQLGPDGQPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVsgnhNVLITNP-RDIPGFIK 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 270 ELwKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVI-IGGSALNRSLYEA-AKARGIQLTAAYGMSETCPLISCAYLN 347
Cdd:PRK12492 302 EL-GKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTnSGGTALVKATAERwEQLTGCTIVEGYGLTETSPVASTNPYG 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 348 DELLAGSederttyrikAGVPVPLVDAAIMDEQGRFLPAdGEsQGELVLRSPWLTQGYFREPERGEE-LWRGGWMHTGDV 426
Cdd:PRK12492 381 ELARLGT----------VGIPVPGTALKVIDDDGNELPL-GE-RGELCIKGPQVMKGYWQQPEATAEaLDAEGWFKTGDI 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 427 ATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGqqldarGLK-EHL 505
Cdd:PRK12492 449 AVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP------GLSvEEL 522
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15599119 506 KPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRiEIA 547
Cdd:PRK12492 523 KAYCKE-NFTGYKVPKHIVLRDSLPMTPVGKILRRELR-DIA 562
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
44-548 |
8.68e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 126.25 E-value: 8.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNS 123
Cdd:PLN02246 51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 EFVPlyqAVAGQLATVERTILLTDGAEKsaelpGLVgEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKGVYFSH 203
Cdd:PLN02246 131 CYVD---KLKGLAEDDGVTVVTIDDPPE-----GCL-HFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTH 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 204 RQLVlhtlamaSTIGSL---DSIRL-LGTSDVYMPITPMFHVHAWGTPYVATM-LGVKQVYPGRYDPELLVELWKREKVT 278
Cdd:PLN02246 202 KGLV-------TSVAQQvdgENPNLyFHSDDVILCVLPMFHIYSLNSVLLCGLrVGAAILIMPKFEIGALLELIQRHKVT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 279 FSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSA-LNRSLYEAAKAR--GIQLTAAYGMSETCPLIS-CaylndelLAGS 354
Cdd:PLN02246 275 IAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAApLGKELEDAFRAKlpNAVLGQGYGMTEAGPVLAmC-------LAFA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 355 edeRTTYRIKAGVPVPLV---DAAIMD-EQGRFLPADgeSQGELVLRSPWLTQGYFREPERGEE-LWRGGWMHTGDVATL 429
Cdd:PLN02246 348 ---KEPFPVKSGSCGTVVrnaELKIVDpETGASLPRN--QPGEICIRGPQIMKGYLNDPEATANtIDKDGWLHTGDIGYI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 430 DGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHL-KPF 508
Cdd:PLN02246 423 DDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVaKQV 502
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599119 509 VEQGNINKwaipsqIAVVTDIPKTSVGKLDKKRIRIEIAQ 548
Cdd:PLN02246 503 VFYKRIHK------VFFVDSIPKAPSGKILRKDLRAKLAA 536
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
230-543 |
1.28e-30 |
|
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: 124.80 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 230 DVYMPITPMFHvhawGTPYVATM----LGVKQVYPGRYDPELLVELWKREKVTFSHCVPTILQMVM----NARAAQGVdf 301
Cdd:cd05929 170 SVYLSPAPLYH----AAPFRWSMtalfMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLklpeAVRNAYDL-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 302 kgwkviiggSALNRSLYEAA------KARGIQLTAaygmsetcPLIscaylnDELLAGSE---------DERTTYRIKAG 366
Cdd:cd05929 244 ---------SSLKRVIHAAApcppwvKEQWIDWGG--------PII------WEYYGGTEgqgltiingEEWLTHPGSVG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 367 VPVpLVDAAIMDEQGRFLPAdGESqGELVLRSPWlTQGYFREPER-GEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVI 445
Cdd:cd05929 301 RAV-LGKVHILDEDGNEVPP-GEI-GEVYFANGP-GFEYTNDPEKtAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 446 KTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREG---QQLDARGLKEHLKpfveqGNINKWAIPSQ 522
Cdd:cd05929 377 ISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGadaGTALAEELIAFLR-----DRLSRYKCPRS 451
|
330 340
....*....|....*....|.
gi 15599119 523 IAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05929 452 IEFVAELPRDDTGKLYRRLLR 472
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
36-540 |
1.99e-30 |
|
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: 124.36 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMdwdSHRYLECMFAIPMI----GAVLhTINIRLSPEQILYTM 111
Cdd:cd17655 16 VVFEDQ-TLTYRELNERANQLARTLREKGVGPDTIVGIM---AERSLEMIVGILGIlkagGAYL-PIDPDYPEERIQYIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 112 NHAEDRFVLVNSEFVPLyqavagqLATVERTILLTDGAEKSaelpglvGEYESLLAAASPRydfpdfdenSIATTFYTTG 191
Cdd:cd17655 91 EDSGADILLTQSHLQPP-------IAFIGLIDLLDEDTIYH-------EESENLEPVSKSD---------DLAYVIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 192 TTGNPKGVYFSHRQLV-LHT-------LAMASTIGSLDSIRLLGTsdvympITPMFHVHAWGtpyvATMLGVKQVypGRY 263
Cdd:cd17655 148 STGKPKGVMIEHRGVVnLVEwankviyQGEHLRVALFASISFDAS------VTEIFASLLSG----NTLYIVRKE--TVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 264 DPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKgwKVIIGGSALNRSLYEAAKAR---GIQLTAAYGMSETCpl 340
Cdd:cd17655 216 DGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLK--HLIVGGEALSTELAKKIIELfgtNPTITNAYGPTETT-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 341 ISCAYLNDEllagSEDERTTYrIKAGVPVPLVDAAIMDEQGRFLPADgeSQGELVLRSPWLTQGYFREPE---------- 410
Cdd:cd17655 292 VDASIYQYE----PETDQQVS-VPIGKPLGNTRIYILDQYGRPQPVG--VAGELYIGGEGVARGYLNRPEltaekfvddp 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 411 --RGEELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALL 488
Cdd:cd17655 365 fvPGERMYR-----TGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYI 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15599119 489 VVREgqQLDARGLKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd17655 440 VSEK--ELPVAQLREFL-----ARELPDYMIPSYFIKLDEIPLTPNGKVDRK 484
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
196-538 |
2.01e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 122.11 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQL-------VLHTLAMASTIGSLDSIRLLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPG-RYDPEL 267
Cdd:cd05924 18 PKGVMWRQEDIfrmlmggADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVVLPDdRFDPEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 268 LVELWKREKVTfshcvptILQMVMNA---------RAAQGVDFKGWKVII-GGSALNRSLYEA--AKARGIQLTAAYGMS 335
Cdd:cd05924 98 VWRTIEKHKVT-------SMTIVGDAmarplidalRDAGPYDLSSLFAISsGGALLSPEVKQGllELVPNITLVDAFGSS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 336 ETcpliscAYLNDELLAGSEDERTTYRIKAGvpvplvDAAIMDEQGRFLPADGESQGeLVLRSPWLTQGYFREPERGEEL 415
Cdd:cd05924 171 ET------GFTGSGHSAGSGPETGPFTRANP------DTVVLDDDGRVVPPGSGGVG-WIARRGHIPLGYYGDEAKTAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 416 WR--GG--WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVR 491
Cdd:cd05924 238 FPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15599119 492 EGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLD 538
Cdd:cd05924 318 EGAGVDLEELREHCR-----TRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
31-543 |
5.75e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 123.20 E-value: 5.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 31 EKSHEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYT 110
Cdd:PRK13390 12 DRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 111 MNHAEDRFVLVNSEFVPLYQAVAGQLAtvertILLTDGAEksaeLPGLvGEYESLLAAASPRYDfpdfDENSIATTFYTT 190
Cdd:PRK13390 92 VGDSGARVLVASAALDGLAAKVGADLP-----LRLSFGGE----IDGF-GSFEAALAGAGPRLT----EQPCGAVMLYSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 191 GTTGNPKGVY--FSHRQLVLHTLAMASTIGSLDSIrllGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELL 268
Cdd:PRK13390 158 GTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDI---SESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 269 VELWKREKVTFSHCVPTILQMVMNARAAQgvdfkgwkviiggsalnRSLYEAAKARGIQLTAAygmseTCPLISCAYLND 348
Cdd:PRK13390 235 LGHVERYRITVTQMVPTMFVRLLKLDADV-----------------RTRYDVSSLRAVIHAAA-----PCPVDVKHAMID 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 349 -------ELLAGSEDERTT---------YRIKAGVPVpLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERG 412
Cdd:PRK13390 293 wlgpivyEYYSSTEAHGMTfidspdwlaHPGSVGRSV-LGDLHICDDDGNELPA-GRI-GTVYFERDRLPFRYLNDPEKT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 413 EELWRGG---WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLV 489
Cdd:PRK13390 370 AAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQ 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599119 490 VREGqqldARGLKEHLKPFVE--QGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK13390 450 LVEG----IRGSDELARELIDytRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
196-539 |
5.77e-30 |
|
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: 120.44 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMAS---TIGSLDSIRLLgtsdvyMPITpmfhvHAWGTPYVATML---GVKQVYPGRYDPELLV 269
Cdd:cd17635 16 PKAVLLANKTFFAVPDILQKeglNWVVGDVTYLP------LPAT-----HIGGLWWILTCLihgGLCVTGGENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 270 ELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSAlnRSLyeAAKARGIQLTA------AYGMSETCPLISC 343
Cdd:cd17635 85 KILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGS--RAI--AADVRFIEATGltntaqVYGLSETGTALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 344 AYLNDELLAGSederttyrikAGVPVPLVDAAIMDEQGRFLPADGEsqGELVLRSPWLTQGYFREPERGEELWRGGWMHT 423
Cdd:cd17635 161 PTDDDSIEINA----------VGRPYPGVDVYLAATDGIAGPSASF--GTIWIKSPANMLGYWNNPERTAEVLIDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 424 GDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERpFALLVVREGQQLD--ARGL 501
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGEL-VGLAVVASAELDEnaIRAL 307
|
330 340 350
....*....|....*....|....*....|....*...
gi 15599119 502 KEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDK 539
Cdd:cd17635 308 KHTIR-----RELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
264-552 |
6.77e-30 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 123.56 E-value: 6.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 264 DPELLV--ELWKREKVTFSHCVPTILQMVMNARAAQGV--DFKGWKVI-IGGSALNRSLyeaakAR------GIQLTAAY 332
Cdd:PRK10946 258 DPSATLcfPLIEKHQVNVTALVPPAVSLWLQAIAEGGSraQLASLKLLqVGGARLSETL-----ARripaelGCQLQQVF 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 333 GMSETcpLISCAYLNDEllagseDER--TTyrikAGVPVPLVDAA-IMDEQGRFLPaDGESqGELVLRSPWLTQGYFREP 409
Cdd:PRK10946 333 GMAEG--LVNYTRLDDS------DERifTT----QGRPMSPDDEVwVADADGNPLP-QGEV-GRLMTRGPYTFRGYYKSP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 410 ERGEELW-RGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALL 488
Cdd:PRK10946 399 QHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFL 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599119 489 VVREGqqLDARGLKEHLKpfvEQGnINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQWQEA 552
Cdd:PRK10946 479 VVKEP--LKAVQLRRFLR---EQG-IAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA 536
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
40-536 |
7.37e-30 |
|
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: 123.83 E-value: 7.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVmdwdshrYLE-------CMFAIPMIGAVlHTINIR-LSPEQILYTM 111
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAI-------YMPmipelviAMLACARIGAV-HSVVFAgFSAESLADRI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 112 NHAEDRFVLVNSEF------VPLYQAV---AGQLATVERTILLTDGAEKSAELPGLVGEYESLLAAASPRYDFPDFDENS 182
Cdd:cd05966 153 NDAQCKLVITADGGyrggkvIPLKEIVdeaLEKCPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSED 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 183 IATTFYTTGTTGNPKGVyfshrqlvLHTLA--MASTIGSL-------DSIRLLGTSD----------VYMPI-----TPM 238
Cdd:cd05966 233 PLFILYTSGSTGKPKGV--------VHTTGgyLLYAATTFkyvfdyhPDDIYWCTADigwitghsyiVYGPLangatTVM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 239 FHvhawGTPyvatmlgvkqVYPgryDPELLVELWKREKVTFSHCVPTILQMVMNARAA--QGVDFKGWKVIiG--GSALN 314
Cdd:cd05966 305 FE----GTP----------TYP---DPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEwvKKHDLSSLRVL-GsvGEPIN 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 315 ----RSLYEAAKARGIQLTAAYGMSET-----CPLISCAylndELLAGSederttyrikAGVPVPLVDAAIMDEQGRflP 385
Cdd:cd05966 367 peawMWYYEVIGKERCPIVDTWWQTETggimiTPLPGAT----PLKPGS----------ATRPFFGIEPAILDEEGN--E 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 386 ADGESQGELVLRSPW--LTQGYFREPERGEEL-WR--GGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDL 460
Cdd:cd05966 431 VEGEVEGYLVIKRPWpgMARTIYGDHERYEDTyFSkfPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599119 461 ISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARgLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGK 536
Cdd:cd05966 511 LVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDE-LRKELRKHVRK-EIGPIATPDKIQFVPGLPKTRSGK 584
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
45-543 |
9.64e-30 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 123.41 E-value: 9.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEA-GVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNS 123
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 EFVPLYQAVAGQLATVERTILLTDGAEKSAELPGLVGEYESLLAAasprydfPDFDENSIATTFYTTGTTGNPKGVYFSH 203
Cdd:PLN02574 148 ENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPK-------PVIKQDDVAAIMYSSGTTGASKGVVLTH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 204 RQLVlhtlAMASTIGSLDSIRLL--GTSDVYMPITPMFHVHAWGTPYVATM-LGVKQVYPGRYDPELLVELWKREKVTFS 280
Cdd:PLN02574 221 RNLI----AMVELFVRFEASQYEypGSDNVYLAALPMFHIYGLSLFVVGLLsLGSTIVVMRRFDASDMVKVIDRFKVTHF 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 281 HCVPTILQ-MVMNARAAQGVDFKGWKVIIGGSA--LNRSLYEAAKA-RGIQLTAAYGMSETCPLIScaylndellAGSED 356
Cdd:PLN02574 297 PVVPPILMaLTKKAKGVCGEVLKSLKQVSCGAAplSGKFIQDFVQTlPHVDFIQGYGMTESTAVGT---------RGFNT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 357 ERTTYRIKAGVPVPLVDAAIMD-EQGRFLPADGesQGELVLRSPWLTQGYFREPERGE-ELWRGGWMHTGDVATLDGMGF 434
Cdd:PLN02574 368 EKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGN--CGELWIQGPGVMKGYLNNPKATQsTIDKDGWLRTGDIAYFDEDGY 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 435 IEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDarglKEHLKPFVEQgNI 514
Cdd:PLN02574 446 LYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLS----QEAVINYVAK-QV 520
|
490 500
....*....|....*....|....*....
gi 15599119 515 NKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PLN02574 521 APYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
36-543 |
3.98e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 120.95 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK13391 17 IMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFVPLYQAVAGQLATVERTILLtdgaEKSAELPGLVGeYESLLAAASpryDFPDFDENSIATTFYTTGTTGN 195
Cdd:PRK13391 97 ARALITSAAKLDVARALLKQCPGVRHRLVL----DGDGELEGFVG-YAEAVAGLP---ATPIADESLGTDMLYSSGTTGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYfshRQLVLHTLAMASTIGSLDSiRLLG-TSD-VYMPITPMFHvhawGTPYVATM----LGVKQVYPGRYDPELLV 269
Cdd:PRK13391 169 PKGIK---RPLPEQPPDTPLPLTAFLQ-RLWGfRSDmVYLSPAPLYH----SAPQRAVMlvirLGGTVIVMEHFDAEQYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 270 ELWKREKVTFSHCVPT----ILQMVMNARAAQGVdfkgwkviiggSALNRSLYEAA------KArgiQLTAAYGmsetcP 339
Cdd:PRK13391 241 ALIEEYGVTHTQLVPTmfsrMLKLPEEVRDKYDL-----------SSLEVAIHAAApcppqvKE---QMIDWWG-----P 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 340 LIscaylnDELLAGSEDERTTY-------RIKAGVPVPLV-DAAIMDEQGRFLPAdGESqGELvlrspWLTQG----YFR 407
Cdd:PRK13391 302 II------HEYYAATEGLGFTAcdseewlAHPGTVGRAMFgDLHILDDDGAELPP-GEP-GTI-----WFEGGrpfeYLN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 408 EPERGEELW--RGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPF 485
Cdd:PRK13391 369 DPAKTAEARhpDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVK 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15599119 486 ALLVVREGQQLDArGLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK13391 449 AVVQPVDGVDPGP-ALAAELIAFCRQ-RLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
43-543 |
5.33e-29 |
|
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: 121.65 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTV---------AVMdwdshryleCMFAIPMIGAVLHTINIRLSPEQILYTMNH 113
Cdd:cd05967 82 TYTYAELLDEVSRLAGVLRKLGVVKGDRViiympmipeAAI---------AMLACARIGAIHSVVFGGFAAKELASRIDD 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 114 AEDRFVLVNS---------EFVPLYQAvAGQLATV--ERTILLTDG-AEKSAELPGLVGEYESLLAAASPRyDFPDFDEN 181
Cdd:cd05967 153 AKPKLIVTAScgiepgkvvPYKPLLDK-ALELSGHkpHHVLVLNRPqVPADLTKPGRDLDWSELLAKAEPV-DCVPVAAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 182 SIATTFYTTGTTGNPKGVYfshRQLVLHTLAMAStigSLDSIRLLGTSDVYMPITPMFHV--HAWgTPYVATMLGVKQV- 258
Cdd:cd05967 231 DPLYILYTSGTTGKPKGVV---RDNGGHAVALNW---SMRNIYGIKPGDVWWAASDVGWVvgHSY-IVYGPLLHGATTVl 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 259 YPGRY----DPELLVELWKREKVTFSHCVPTILQMV----MNARAAQGVDFKGWKVI-IGGSALNRSLYE-AAKARGIQL 328
Cdd:cd05967 304 YEGKPvgtpDPGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLfLAGERLDPPTLEwAENTLGVPV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 329 TAAYGMSETCPLISCAYLNDELL---AGSederttyrikAGVPVPLVDAAIMDEQGRFLPADgeSQGELVLR---SPWLT 402
Cdd:cd05967 384 IDHWWQTETGWPITANPVGLEPLpikAGS----------PGKPVPGYQVQVLDEDGEPVGPN--ELGNIVIKlplPPGCL 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 403 QGYFREPERGEELWRG---GWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQ 479
Cdd:cd05967 452 LTLWKNDERFKKLYLSkfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDEL 531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599119 480 WGERPFALLVVREGQQLDARGLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05967 532 KGQVPLGLVVLKEGVKITAEELEKELVALVRE-QIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
45-556 |
1.71e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 119.46 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNS- 123
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPg 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 ----EFVPLYQAVAGQLATVERTILLTDGAekSAELPG---------LVGEYESLLAAASPRYDfpdfDENSIATTFYTT 190
Cdd:PRK06164 117 fkgiDFAAILAAVPPDALPPLRAIAVVDDA--ADATPApapgarvqlFALPDPAPPAAAGERAA----DPDAGALLFTTS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 191 GTTGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYDPELLVE 270
Cdd:PRK06164 191 GTTSGPKLVLHRQATLLRHARAIARAYG-------YDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTAR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 271 LWKREKVTfsHCVPTILQMV-MNARAAQGVDFKGWKVIIGGSALNRS--LYEAAKARGIQLTAAYGMSETCPLISCAYLN 347
Cdd:PRK06164 264 ALRRHRVT--HTFGNDEMLRrILDTAGERADFPSARLFGFASFAPALgeLAALARARGVPLTGLYGSSEVQALVALQPAT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 348 DEllagsEDERttyRIKAGVPV-PLVDAAIMDEQGRFLPADGESqGELVLRSPWLTQGYFREPE-RGEELWRGGWMHTGD 425
Cdd:PRK06164 342 DP-----VSVR---IEGGGRPAsPEARVRARDPQDGALLPDGES-GEIEIRAPSLMRGYLDNPDaTARALTDDGYFRTGD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 426 VATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVpDPQWGERPFALLVVREGQQLDARGLKEHL 505
Cdd:PRK06164 413 LGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAAC 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15599119 506 kpfveQGNINKWAIPSQIAVVTDIPKTSVG---KLDKKRIRIEIAQWQEAGSAF 556
Cdd:PRK06164 492 -----REALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARLAAERAA 540
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
368-543 |
3.26e-28 |
|
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: 119.13 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 368 PVPLVDAAIMDEQGRflPADGEsQGELVLRSPW--LTQGYFREPERGEEL----WRGGWMHtGDVATLDGMGFIEIRDRI 441
Cdd:cd05968 418 PVPGMKADVLDESGK--PARPE-VGELVLLAPWpgMTRGFWRDEDRYLETywsrFDNVWVH-GDFAYYDEEGYFYILGRS 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 442 KDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDArGLKEHLKPFVeQGNINKWAIPS 521
Cdd:cd05968 494 DDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTE-ALAEELMERV-ADELGKPLSPE 571
|
170 180
....*....|....*....|..
gi 15599119 522 QIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05968 572 RILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1-547 |
4.66e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 118.07 E-value: 4.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 1 MLKTRLIPAAAGayqyPLLIKSLMLSGRRY-EKSHEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSH 79
Cdd:PRK05852 4 MGGAAPMASDFG----PRIADLVEVAATRLpEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 80 RYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAEKSAELPGLV 159
Cdd:PRK05852 80 EFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 160 GEYESLLAAASPRYDFPDfdensIATTFYTTGTTGNPKGVYFSHRQLvlhtlamASTIGSLDSIRLLGTSDVYMPITPMF 239
Cdd:PRK05852 160 AATEPTPATSTPEGLRPD-----DAMIMFTGGTTGLPKMVPWTHANI-------ASSVRAIITGYRLSPRDATVAVMPLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 240 HVHAWGTPYVATML-GVKQVYP--GRYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFK--GWKVIIGGSA-L 313
Cdd:PRK05852 228 HGHGLIAALLATLAsGGAVLLParGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKpaALRFIRSCSApL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 314 NRSLYEAAKAR-GIQLTAAYGMSETCPLISCAylNDELLAGSEDERTTYRIKAGVPVPlvDAAIMDEQGRFLPADgeSQG 392
Cdd:PRK05852 308 TAETAQALQTEfAAPVVCAFGMTEATHQVTTT--QIEGIGQTENPVVSTGLVGRSTGA--QIRIVGSDGLPLPAG--AVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 393 ELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAV 472
Cdd:PRK05852 382 EVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAV 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599119 473 VGVPDPQWGERPFALLVVREGQQLDARGL----KEHLKPFveqgninkwAIPSQIAVVTDIPKTSVGKLDKKRIRIEIA 547
Cdd:PRK05852 462 FGVPDQLYGEAVAAVIVPRESAPPTAEELvqfcRERLAAF---------EIPASFQEASGLPHTAKGSLDRRAVAEQFG 531
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
40-543 |
5.08e-28 |
|
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: 117.95 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEA-GVKAGDTVAVM-----DWdshrYL---ECMFAipmiGAVLHTINIRLSPEQILYT 110
Cdd:cd05928 38 DEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVIlprvpEW----WLvnvACIRT----GLVFIPGTIQLTAKDILYR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 111 MNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAeksaeLPGLvGEYESLLAAASPRYDFPDFDENSIATTFYTT 190
Cdd:cd05928 110 LQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKS-----RDGW-LNFKELLNEASTEHHCVETGSQEPMAIYFTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 191 GTTGNPKGVYFSHRqlvlhTLAMASTIGS---LDsirlLGTSDVYMPITPM-FHVHAWGTPYVATMLG--VKQVYPGRYD 264
Cdd:cd05928 184 GTTGSPKMAEHSHS-----SLGLGLKVNGrywLD----LTASDIMWNTSDTgWIKSAWSSLFEPWIQGacVFVHHLPRFD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 265 PELLVELWKREKVTFSHCVPTILQMVMNAraaqgvDFKGWK------VIIGGSALNRSLYEAAKAR-GIQLTAAYGMSET 337
Cdd:cd05928 255 PLVILKTLSSYPITTFCGAPTVYRMLVQQ------DLSSYKfpslqhCVTGGEPLNPEVLEKWKAQtGLDIYEGYGQTET 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 338 CpLISCAYLNDELLAGSederttyrikAGVPVPLVDAAIMDEQGRFLPADGEsqGELVLR-SP----WLTQGYFREPERG 412
Cdd:cd05928 329 G-LICANFKGMKIKPGS----------MGKASPPYDVQIIDDNGNVLPPGTE--GDIGIRvKPirpfGLFSGYVDNPEKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 413 EELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVV-- 490
Cdd:cd05928 396 AATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLap 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599119 491 ----REGQQLdARGLKEHLKPFVEqgninKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05928 476 qflsHDPEQL-TKELQQHVKSVTA-----PYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
306-543 |
6.82e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 114.76 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 306 VIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPliSCAYlndellagsederttyrikAGVPVPLVDAAIMDeqgrflp 385
Cdd:PRK07824 156 VLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSG--GCVY-------------------DGVPLDGVRVRVED------- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 386 adgesqGELVLRSPWLTQGYfREPERGEELWRGGWMHTGDVATLDGmGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHP 465
Cdd:PRK07824 208 ------GRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHP 279
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599119 466 AVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK07824 280 AVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHV-----ARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
51-543 |
1.02e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 113.30 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 51 ERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGA----VLHTINIRLSPEQILYTMNHAEDRFVLVNSEFV 126
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 127 PLYQAVAGQLATvertilltdgaeksaelPGLVGEYESLLAAASPRYDFPDFDENsIATTFYTTGTTGNPKGVYFSHRQL 206
Cdd:cd05922 81 DRLRDALPASPD-----------------PGTVLDADGIRAARASAPAHEVSHED-LALLLYTSGSTGSPKLVRLSHQNL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 207 VLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGRYD-PELLVELWKREKVTFSHCVPT 285
Cdd:cd05922 143 LANARSIAEYLG-------ITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATGLAGVPS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 286 ILQMVMNaraaqgVDFKGWK------VIIGGSALNRSLYEA--AKARGIQLTAAYGMSETCPLIScaYLNDELlagsEDE 357
Cdd:cd05922 216 TYAMLTR------LGFDPAKlpslryLTQAGGRLPQETIARlrELLPGAQVYVMYGQTEATRRMT--YLPPER----ILE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 358 RTTyriKAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFR-EPERGEELWRGGWMHTGDVATLDGMGFIE 436
Cdd:cd05922 284 KPG---SIGLAIPGGEFEILDDDGTPTPP-GEP-GEIVHRGPNVMKGYWNdPPYRRKEGRGGGVLHTGDLARRDEDGFLF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 437 IRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQwGERPFALLVVREGQQLDA--RGLKEHLKPFveqgni 514
Cdd:cd05922 359 IVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDvlRSLAERLPPY------ 431
|
490 500
....*....|....*....|....*....
gi 15599119 515 nkwAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05922 432 ---KVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1-543 |
2.03e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 112.93 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 1 MLKTRLIPAAAGAYQYPLLIKSLMLSGRRYEKSHEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHR 80
Cdd:PRK13382 26 MRPDRYLRIVAAMRREGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 81 YLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSEFVPLY-QAVAGQLATVeRTILLTDGaEKSAELPGLV 159
Cdd:PRK13382 106 FVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVdRALADCPQAT-RIVAWTDE-DHDLTVEVLI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 160 GEYESLLAAASPRydfpdfdenSIATTFYTTGTTGNPKGVyfshRQLVLHTLAMASTIgsLDSIRLLGTSDVYMpITPMF 239
Cdd:PRK13382 184 AAHAGQRPEPTGR---------KGRVILLTSGTTGTPKGA----RRSGPGGIGTLKAI--LDRTPWRAEEPTVI-VAPMF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 240 HvhAWGTPYV--ATMLGVKQVYPGRYDPELLVELWKREKVTFSHCVPTILQMVMNARAA--QGVDFKGWKVIIG-GSALN 314
Cdd:PRK13382 248 H--AWGFSQLvlAASLACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEvrNRYSGRSLRFAAAsGSRMR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 315 RSLYEAAKAR-GIQLTAAYGMSETcPLISCAylNDELLAGSEDerttyriKAGVPVPLVDAAIMDEQGRFLPaDGESqGE 393
Cdd:PRK13382 326 PDVVIAFMDQfGDVIYNNYNATEA-GMIATA--TPADLRAAPD-------TAGRPAEGTEIRILDQDFREVP-TGEV-GT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 394 LVLRSPWLTQGYfrEPERGEELwRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVV 473
Cdd:PRK13382 394 IFVRNDTQFDGY--TSGSTKDF-HDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVI 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 474 GVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK13382 471 GVDDEQYGQRLAAFVVLKPGASATPETLKQHVR-----DNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
36-551 |
4.15e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 111.79 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQVRySYATFNERVARLANVLSEAGVKAgDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILytmnhae 115
Cdd:PRK07638 20 IKENDRVL-TYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFVPLYQAVAGQLATVERTILLTDgaeksaelpglvgEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGN 195
Cdd:PRK07638 91 ERLAISNADMIVTERYKLNDLPDEEGRVIEID-------------EWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLV------LHTLAMASTigslDSIRLLGTsdvympitpMFHVH----AWGTPYVATMLGVKQvypgRYDP 265
Cdd:PRK07638 158 PKAFLRAQQSWLhsfdcnVHDFHMKRE----DSVLIAGT---------LVHSLflygAISTLYVGQTVHLMR----KFIP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 266 ELLVELWKREKVTFSHCVPTILQMVMNARAA-QGVDfkgwKVIIGGSALNRSLYEAAKAR--GIQLTAAYGMSEtcpLIS 342
Cdd:PRK07638 221 NQVLDKLETENISVMYTVPTMLESLYKENRViENKM----KIISSGAKWEAEAKEKIKNIfpYAKLYEFYGASE---LSF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 343 CAYLNDEllagsEDERTTYriKAGVPVPLVDAAIMDEQGRFLPADGEsqGELVLRSPWLTQGYFREPERGEELWRGGWMH 422
Cdd:PRK07638 294 VTALVDE-----ESERRPN--SVGRPFHNVQVRICNEAGEEVQKGEI--GTVYVKSPQFFMGYIIGGVLARELNADGWMT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 423 TGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVRE-GQQLDARgL 501
Cdd:PRK07638 365 VRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSAtKQQLKSF-C 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15599119 502 KEHLKPFveqgninkwAIPSQIAVVTDIPKTSVGKLDKKRIRieiaQWQE 551
Cdd:PRK07638 444 LQRLSSF---------KIPKEWHFVDEIPYTNSGKIARMEAK----SWIE 480
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
36-542 |
4.29e-26 |
|
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: 111.18 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQIlytmnhae 115
Cdd:cd05945 10 VVEGGR-TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 drfvlvnsefvplyQAVagqLATVERTILLTDGAEKSAEL--PGLVGeyesllaaasprydfpdfdensiattfyttgtt 193
Cdd:cd05945 81 --------------REI---LDAAKPALLIADGDDNAYIIftSGSTG--------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 194 gNPKGVYFSHRQLVLHTLAMastigslDSIRLLGTSDVYMPiTPMFH----VHAWgtpYVATMLGVKQVYPGR---YDPE 266
Cdd:cd05945 111 -RPKGVQISHDNLVSFTNWM-------LSDFPLGPGDVFLN-QAPFSfdlsVMDL---YPALASGATLVPVPRdatADPK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 267 LLVELWKREKVTFSHCVPTILQMVM--NARAAQGVDFKGWkVIIGGSALNRSLYEAAKAR--GIQLTAAYGMSETCplIS 342
Cdd:cd05945 179 QLFRFLAEHGITVWVSTPSFAAMCLlsPTFTPESLPSLRH-FLFCGEVLPHKTARALQQRfpDARIYNTYGPTEAT--VA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 343 CAY--LNDELLAGSEderttyRIKAGVPVPLVDAAIMDEQGRFLPAdGEsQGELVLRSPWLTQGYFREPERGEELWR--- 417
Cdd:cd05945 256 VTYieVTPEVLDGYD------RLPIGYAKPGAKLVILDEDGRPVPP-GE-KGELVISGPSVSKGYLNNPEKTAAAFFpde 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 418 -GGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEwlsSLELEDL---ISRHPAVREVAVVGVPDPQWGERPFALLVVREG 493
Cdd:cd05945 328 gQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY---RIELEEIeaaLRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPG 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15599119 494 -QQLDARGLKEHLKPfveqgNINKWAIPSQIAVVTDIPKTSVGKLDKKRI 542
Cdd:cd05945 405 aEAGLTKAIKAELAE-----RLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
113-545 |
1.27e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 110.54 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 113 HAEDRFVLVNSEFVPLyqaVAGQLATVErtILLTDGAEKSAELPGLVGeyesllAAASPRYDFPD------FDENSiatt 186
Cdd:PRK07867 99 HADCQLVLTESAHAEL---LDGLDPGVR--VINVDSPAWADELAAHRD------AEPPFRVADPDdlfmliFTSGT---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 187 fyttgtTGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDV-YMPItPMFHVHA----WgTPYVATmlGVKQVYPG 261
Cdd:PRK07867 164 ------SGDPKAVRCTHRKVASAGVMLAQRFG-------LGPDDVcYVSM-PLFHSNAvmagW-AVALAA--GASIALRR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 262 RYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLI 341
Cdd:PRK07867 227 KFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGVAI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 342 SCAylnDELLAGS----EDERTTYRIKAGVPVPlvdAAIMDEQGRfLPADgESQGELV-LRSPWLTQGYFREPERGEELW 416
Cdd:PRK07867 307 TRT---PDTPPGAlgplPPGVAIVDPDTGTECP---PAEDADGRL-LNAD-EAIGELVnTAGPGGFEGYYNDPEADAERM 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 417 RGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQL 496
Cdd:PRK07867 379 RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKF 458
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 15599119 497 DARGLKEHLkpfVEQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIE 545
Cdd:PRK07867 459 DPDAFAEFL---AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
45-472 |
1.43e-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: 108.89 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVL-SEAGVKAGDTVAVMdwdSHRYLE---CMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVL 120
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVL---LERSAElvvAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 121 VNSEFVPLyqavagQLATVERTILLTDGAEKSAElpglvgeyESLLAAASPRYDFPDfdenSIATTFYTTGTTGNPKGVY 200
Cdd:TIGR01733 78 TDSALASR------LAGLVLPVILLDPLELAALD--------DAPAPPPPDAPSGPD----DLAYVIYTSGSTGRPKGVV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 201 FSHRQLVLHTLAMASTIGSLDSIRLLGTS----DV-YMPItpmfhvhaWGTPYVatmlGVKQVYP---GRYDPELLVELW 272
Cdd:TIGR01733 140 VTHRSLVNLLAWLARRYGLDPDDRVLQFAslsfDAsVEEI--------FGALLA----GATLVVPpedEERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KRE-KVTFSHCVPTILQMVMNARAAQGVDFKgwKVIIGGSALNRSLYE--AAKARGIQLTAAYGMSETCpLISCAYLNDE 349
Cdd:TIGR01733 208 IAEhPVTVLNLTPSLLALLAAALPPALASLR--LVILGGEALTPALVDrwRARGPGARLINLYGPTETT-VWSTATLVDP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 350 llagsEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADGEsqGELVLRSPWLTQGYFREPERGEE-----LWRGG----W 420
Cdd:TIGR01733 285 -----DDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVV--GELYIGGPGVARGYLNRPELTAErfvpdPFAGGdgarL 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15599119 421 MHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAV 472
Cdd:TIGR01733 358 YRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
44-543 |
1.60e-25 |
|
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: 109.14 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLhtinirlspeQILYTmnhaedrfvlvns 123
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVY----------QPLFT------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 EFVPlyQAVAGQLATVERTILLTDGAEKSAELPGLVGEYESLLAAASPrydfpdfdensiattfyttgttgnpKGVYFSH 203
Cdd:cd05973 58 AFGP--KAIEHRLRTSGARLVVTDAANRHKLDSDPFVMMFTSGTTGLP-------------------------KGVPVPL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 204 RqlvlhtlAMASTIGSLDSIRLLGTSDVYMPIT-PMFhvhAWGTPYVAT---MLGVKQV-YPGRYDPELLVELWKREKVT 278
Cdd:cd05973 111 R-------ALAAFGAYLRDAVDLRPEDSFWNAAdPGW---AYGLYYAITgplALGHPTIlLEGGFSVESTWRVIERLGVT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 279 FSHCVPTILQMVMNARAAQGVDFKG--WKVIIGGSALNRSLYEAAKAR-GIQLTAAYGMSETCPLISCAY-LNDELLAGS 354
Cdd:cd05973 181 NLAGSPTAYRLLMAAGAEVPARPKGrlRRVSSAGEPLTPEVIRWFDAAlGVPIHDHYGQTELGMVLANHHaLEHPVHAGS 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 355 ederttyrikAGVPVPLVDAAIMDEQGRfLPADGEsQGELVL---RSPWLT-QGYFREPERGEElwrGGWMHTGDVATLD 430
Cdd:cd05973 261 ----------AGRAMPGWRVAVLDDDGD-ELGPGE-PGRLAIdiaNSPLMWfRGYQLPDTPAID---GGYYLTGDTVEFD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 431 GMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQlDARGLKEHLKPFVE 510
Cdd:cd05973 326 PDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHE-GTPALADELQLHVK 404
|
490 500 510
....*....|....*....|....*....|...
gi 15599119 511 QgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd05973 405 K-RLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-540 |
1.72e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.97 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFV 119
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 120 LVNSEFVPLYQAVAG-QLATVERTilltdgaeksaelpglvGEYESLLAAASPRYDFPDfdenSIATTFYTTGTTGNPKG 198
Cdd:PRK12316 4653 LTQSHLLQRLPIPDGlASLALDRD-----------------EDWEGFPAHDPAVRLHPD----NLAYVIYTSGSTGRPKG 4711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 199 VYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWGTpYVATMLGVKQVY--PGRYDPELLVELWKRE 275
Cdd:PRK12316 4712 VAVSHGSLVNHLHATGERYE-------LTPDDRVLQFMSFsFDGSHEGL-YHPLINGASVVIrdDSLWDPERLYAEIHEH 4783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSALNRSLYEAA--KARGIQLTAAYGMSETCPLISCAYLNDELLAG 353
Cdd:PRK12316 4784 RVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAwrALKPVYLFNGYGPTETTVTVLLWKARDGDACG 4863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 354 SEderttyRIKAGVPVPLVDAAIMDEQGRFLPADGesQGELVLRSPWLTQGYFREP----ER---------GEELWRggw 420
Cdd:PRK12316 4864 AA------YMPIGTPLGNRSGYVLDGQLNPLPVGV--AGELYLGGEGVARGYLERPaltaERfvpdpfgapGGRLYR--- 4932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 421 mhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQwGERPFALLVVREGQQLDARG 500
Cdd:PRK12316 4933 --TGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQDPALADADE 5009
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15599119 501 --------LKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:PRK12316 5010 aqaelrdeLKAALR-----ERLPEYMVPAHLVFLARMPLTPNGKLDRK 5052
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
36-540 |
1.78e-25 |
|
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: 109.32 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:cd17643 6 VVDEDR-RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEfvplyqavagQLATVERTilltdgaeksaelPGLVGeyesllaaasprydfpdfdensiattfyttgttgN 195
Cdd:cd17643 85 PSLLLTDPD----------DLAYVIYT-------------SGSTG----------------------------------R 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLvlhtlamastigsldsIRLLGTSDVYMPITP-----MFHVHA--------WGtpyvATMLGVKQV---Y 259
Cdd:cd17643 108 PKGVVVSHANV----------------LALFAATQRWFGFNEddvwtLFHSYAfdfsvweiWG----ALLHGGRLVvvpY 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 260 PGRYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWK-VIIGGSALN----RSLYEAAKARGIQLTAAYGM 334
Cdd:cd17643 168 EVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRyVIFGGEALEaamlRPWAGRFGLDRPQLVNMYGI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 335 SETCPLISCAYLNDELLAGSEDERTtyrikaGVPVPLVDAAIMDEQGRFLPADGesQGELVLRSPWLTQGYFREPER--- 411
Cdd:cd17643 248 TETTVHVTFRPLDAADLPAAAASPI------GRPLPGLRVYVLDADGRPVPPGV--VGELYVSGAGVARGYLGRPELtae 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 412 ----------GEELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWG 481
Cdd:cd17643 320 rfvanpfggpGSRMYR-----TGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGD 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599119 482 ERPFALLVVREGQQLDARGLKEHLK---PFveqgninkWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd17643 395 TRLVAYVVADDGAAADIAELRALLKellPD--------YMVPARYVPLDALPLTVNGKLDRA 448
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
23-542 |
2.26e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 109.70 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 23 LMLSGRRYEKSHEIVyRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRL 102
Cdd:PRK13383 41 LAVTAARWPGRTAII-DDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 103 SPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTillTDGAEKSAELPGLvgeyesllaAASPRydfpdfdens 182
Cdd:PRK13383 120 RSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPA---TAGAEESGGRPAV---------AAPGR---------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 183 iaTTFYTTGTTGNPKGVyfSHRQLVLHTLAMASTIgsLDSIRLLGTSDVYMPiTPMFHVHAWGTPYVATMLGVKQVYPGR 262
Cdd:PRK13383 178 --IVLLTSGTTGKPKGV--PRAPQLRSAVGVWVTI--LDRTRLRTGSRISVA-MPMFHGLGLGMLMLTIALGGTVLTHRH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 263 YDPELLVELWKREKVTFSHCVPTILQMVMN----ARAAQgvDFKGWKVIIG-GSALNRSLYEA-AKARGIQLTAAYGMSE 336
Cdd:PRK13383 251 FDAEAALAQASLHRADAFTAVPVVLARILElpprVRARN--PLPQLRVVMSsGDRLDPTLGQRfMDTYGDILYNGYGSTE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 337 TC--PLISCAYLNDEllagsedERTTYRIKAGVPVplvdaAIMDEQGRflPADGESQGELVLRSPWLTQGYfrePERGEE 414
Cdd:PRK13383 329 VGigALATPADLRDA-------PETVGKPVAGCPV-----RILDRNNR--PVGPRVTGRIFVGGELAGTRY---TDGGGK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 415 LWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQ 494
Cdd:PRK13383 392 AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGS 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15599119 495 QLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRI 542
Cdd:PRK13383 472 GVDAAQLRDYLK-----DRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
261-539 |
8.89e-25 |
|
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: 105.18 E-value: 8.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 261 GRYDPELLVELWKREKVTFSHCVPTILQMVMNaraaqgVDFKGWKVII---GGSALNRSLYEAAKA--RGIQLTAAYGMS 335
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPTMLQALAR------TLEPESKIKSifsSGQKLFESTKKKLKNifPKANLIEFYGTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 336 ETcPLIScaYLNDEllagseDERTTYriKAGVPVPLVDAAIMDeqgrflpADGESQGELVLRSPWLTQGYFReperGEEL 415
Cdd:cd17633 147 EL-SFIT--YNFNQ------ESRPPN--SVGRPFPNVEIEIRN-------ADGGEIGKIFVKSEMVFSGYVR----GGFS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 416 WRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLvvrEGQQ 495
Cdd:cd17633 205 NPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDK 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15599119 496 LDARGLKEHLKPfveqgNINKWAIPSQIAVVTDIPKTSVGKLDK 539
Cdd:cd17633 282 LTYKQLKRFLKQ-----KLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
81-545 |
1.07e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 107.81 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 81 YLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSEFVPLYQAVagQLATVerTILLTDGAEksaelpglvg 160
Cdd:PRK13388 65 MLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGL--DLPGV--RVLDVDTPA---------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 161 eYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKGVYFSHrqlvlhtlAMASTIGSLDSIRL-LGTSDV-YMPItPM 238
Cdd:PRK13388 131 -YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSH--------GRLAFAGRALTERFgLTRDDVcYVSM-PL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 239 FHVHA----WGtPYVATmlGVKQVYPGRYDPELLVELWKREKVTFSHCVPTILQMVMnARAAQGVDFKG-WKVIIGGSAL 313
Cdd:PRK13388 201 FHSNAvmagWA-PAVAS--GAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYIL-ATPERPDDADNpLRVAFGNEAS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 314 NRSLYEAAKARGIQLTAAYGMSETCPLIScayLNDELLAGSederttyrIKAGVP-VPLVD--------AAIMDEQGRFL 384
Cdd:PRK13388 277 PRDIAEFSRRFGCQVEDGYGSSEGAVIVV---REPGTPPGS--------IGRGAPgVAIYNpetltecaVARFDAHGALL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 385 PADgESQGELVLRS-PWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISR 463
Cdd:PRK13388 346 NAD-EAIGELVNTAgAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLR 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 464 HPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLkpfVEQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK13388 425 HPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFL---AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
..
gi 15599119 544 IE 545
Cdd:PRK13388 502 AQ 503
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
36-541 |
1.08e-24 |
|
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: 109.18 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:COG1020 495 VVFGDQ-SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSefvplyqAVAGQLATVERTILLTDGAEKSAELPglvgeyESLLAAASPRydfpdfdensiattfyttgttgN 195
Cdd:COG1020 574 ARLVLTQS-------ALAARLPELGVPVLALDALALAAEPA------TNPPVPVTPD----------------------D 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 -------------PKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWGTpYVATMLGVKQVYP- 260
Cdd:COG1020 619 layviytsgstgrPKGVMVEHRALVNLLAWMQRRYG-------LGPGDRVLQFASLsFDASVWEI-FGALLSGATLVLAp 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 261 --GRYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKgwKVIIGGSALNRSLYEAAKAR--GIQLTAAYGMSE 336
Cdd:COG1020 691 peARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLR--LVLVGGEALPPELVRRWRARlpGARLVNLYGPTE 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 337 TCpLISCAYlndELLAGSEDERTtyrIKAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPER----- 411
Cdd:COG1020 769 TT-VDSTYY---EVTPPDADGGS---VPIGRPIANTRVYVLDAHLQPVP-VGVP-GELYIGGAGLARGYLNRPELtaerf 839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 412 --------GEELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGG---EwLSslELEDLISRHPAVREVAVVGVPDPQW 480
Cdd:COG1020 840 vadpfgfpGARLYR-----TGDLARWLPDGNLEFLGRADDQVKIRGfriE-LG--EIEAALLQHPGVREAVVVAREDAPG 911
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599119 481 GERPFALLVVREGQQLDARGLKEHLKPFVEQgninkWAIPSQIAVVTDIPKTSVGKLDKKR 541
Cdd:COG1020 912 DKRLVAYVVPEAGAAAAAALLRLALALLLPP-----YMVPAAVVLLLPLPLTGNGKLDRLA 967
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
42-506 |
1.68e-24 |
|
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: 107.17 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 42 VRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLV 121
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 122 NS--EFVPLYQAVAGQLATVERTILLTDGAEKsaelpglvgEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKGV 199
Cdd:cd05932 85 GKldDWKAMAPGVPEGLISISLPPPSAANCQY---------QWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 200 YFSHRQLVLHTLAMASTIGSLDSIRLLGtsdvYMPITpmfHVhawgTPYVATMLGvkQVYPGR--YDPELL---VELWKR 274
Cdd:cd05932 156 MLTFGSFAWAAQAGIEHIGTEENDRMLS----YLPLA---HV----TERVFVEGG--SLYGGVlvAFAESLdtfVEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVP---TILQM------------------VMNA----RAAQGVDFKGWKVIIGGSA-LNRSLYEAAKARGIQL 328
Cdd:cd05932 223 ARPTLFFSVPrlwTKFQQgvqdkipqqklnlllkipVVNSlvkrKVLKGLGLDQCRLAGCGSApVPPALLEWYRSLGLNI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 329 TAAYGMSEtcpliSCAYlndELLAGSEDERTTYrikAGVPVPLVDAAIMDeqgrflpadgesQGELVLRSPWLTQGYFRE 408
Cdd:cd05932 303 LEAYGMTE-----NFAY---SHLNYPGRDKIGT---VGNAGPGVEVRISE------------DGEILVRSPALMMGYYKD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 409 PER-GEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTG-GEWLSSLELEDLISRHPAVREVAVVGVPDPQwgerPFA 486
Cdd:cd05932 360 PEAtAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA----PLA 435
|
490 500
....*....|....*....|....*....
gi 15599119 487 LLVVREGQQLDA---------RGLKEHLK 506
Cdd:cd05932 436 LVVLSEEARLRAdafaraeleASLRAHLA 464
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
40-540 |
6.96e-24 |
|
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: 105.12 E-value: 6.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFV 119
Cdd:cd17651 17 EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 120 LvnsefvpLYQAVAGQLATVERTILLTDGAEKSAELPGlvgEYESLLAAASPRYDFpdFDENSIATtfyttgttgnPKGV 199
Cdd:cd17651 97 L-------THPALAGELAVELVAVTLLDQPGAAAGADA---EPDPALDADDLAYVI--YTSGSTGR----------PKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 200 YFSHRQLVLHTLAMASTIGSLDSIRLLGTSdvympiTPMFHVHAWGT-PYVATmlGVKQVYPG---RYDPELLVELWKRE 275
Cdd:cd17651 155 VMPHRSLANLVAWQARASSLGPGARTLQFA------GLGFDVSVQEIfSTLCA--GATLVLPPeevRTDPPALAAWLDEQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTILQMVMNARAAQGVDFKGWK-VIIGGSALNRSL---YEAAKARGIQLTAAYGMSETcPLISCaylndELL 351
Cdd:cd17651 227 RISRVFLPTVALRALAEHGRPLGVRLAALRyLLTGGEQLVLTEdlrEFCAGLPGLRLHNHYGPTET-HVVTA-----LSL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 352 AGSEDERTTyRIKAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPERGEELW------RGGWMH-TG 424
Cdd:cd17651 301 PGDPAAWPA-PPPIGRPIDNTRVYVLDAALRPVP-PGVP-GELYIGGAGLARGYLNRPELTAERFvpdpfvPGARMYrTG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 425 DVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEH 504
Cdd:cd17651 378 DLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAA 457
|
490 500 510
....*....|....*....|....*....|....*.
gi 15599119 505 LKPFVEQgninkWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd17651 458 LATHLPE-----YMVPSAFVLLDALPLTPNGKLDRR 488
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
41-543 |
3.22e-23 |
|
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: 103.52 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 41 QVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLE----CMFA--IPMIGAVLHTI-NIRLSPEQILYTMNH 113
Cdd:cd05906 37 EEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPafwaCVLAgfVPAPLTVPPTYdEPNARLRKLRHIWQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 114 AEDRFVLVNSEFVPLYQAVAGQLATVERTILltdgaeksaelpglvgEYESLLAAASPrYDFPDFDENSIATTFYTTGTT 193
Cdd:cd05906 117 LGSPVVLTDAELVAEFAGLETLSGLPGIRVL----------------SIEELLDTAAD-HDLPQSRPDDLALLMLTSGST 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 194 GNPKGVYFSHRQLvLHTLAMASTigsldsIRLLGTSDVYMPITPMFHVHAWGTPYV-ATMLGVKQVY-PGRY---DPELL 268
Cdd:cd05906 180 GFPKAVPLTHRNI-LARSAGKIQ------HNGLTPQDVFLNWVPLDHVGGLVELHLrAVYLGCQQVHvPTEEilaDPLRW 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 269 VELWKREKVTFSHcVPTILQMVMNARAAQGVDFKgW-----KVII-GGSALN----RSLYEAAKARGIQLTA---AYGMS 335
Cdd:cd05906 253 LDLIDRYRVTITW-APNFAFALLNDLLEEIEDGT-WdlsslRYLVnAGEAVVaktiRRLLRLLEPYGLPPDAirpAFGMT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 336 ETCPliSCAYlNDELLAGSEDERTTYrIKAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPERGEEL 415
Cdd:cd05906 331 ETCS--GVIY-SRSFPTYDHSQALEF-VSLGRPIPGVSMRIVDDEGQLLPE-GEV-GRLQVRGPVVTKGYYNNPEANAEA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 416 WR-GGWMHTGDVATLDGmGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVRE--VAVVGVPDPQWGERPFALLVVRE 492
Cdd:cd05906 405 FTeDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIFFVPE 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599119 493 GQQLDARG-----------LKEHLKPfveqgninKWAIPSQiavVTDIPKTSVGKLDKKRIR 543
Cdd:cd05906 484 YDLQDALSetlrairsvvsREVGVSP--------AYLIPLP---KEEIPKTSLGKIQRSKLK 534
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
283-552 |
3.25e-23 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 102.77 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 283 VPTILQMVMNARAAQGVDFKGwkVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLIsCAYLNDELLAGSederttyr 362
Cdd:PRK07445 214 VPTQLQRLLQLRPQWLAQFRT--ILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQI-ATLKPDDFLAGN-------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 363 IKAGVPVPLVDAAIMDEQgrflpadgesQGELVLRSPWLTQGYFREPERGEELWRggwmhTGDVATLDGMGFIEIRDRIK 442
Cdd:PRK07445 283 NSSGQVLPHAQITIPANQ----------TGNITIQAQSLALGYYPQILDSQGIFE-----TDDLGYLDAQGYLHILGRNS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 443 DVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGqQLDARGLKEHLKPfveqgNINKWAIPSQ 522
Cdd:PRK07445 348 QKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKD-----QLSPFKQPKH 421
|
250 260 270
....*....|....*....|....*....|
gi 15599119 523 IAVVTDIPKTSVGKLDkkriRIEIAQWQEA 552
Cdd:PRK07445 422 WIPVPQLPRNPQGKIN----RQQLQQIAVQ 447
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
36-541 |
3.46e-23 |
|
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: 102.66 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:cd12117 16 VVYGDR-SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVnsefvplyQAVAGQLATVERTILLTDGAEKSAElpglvgeyesllaAASPRydfPDFDENSIATTFYTTGTTGN 195
Cdd:cd12117 95 AKVLLT--------DRSLAGRAGGLEVAVVIDEALDAGP-------------AGNPA---VPVSPDDLAYVMYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHR---QLVLHTLAMASTigslDSIRLLGTSdvymPIT---PMFHVhaWGtpyvATMLGVKQV-YPGR--YDPE 266
Cdd:cd12117 151 PKGVAVTHRgvvRLVKNTNYVTLG----PDDRVLQTS----PLAfdaSTFEI--WG----ALLNGARLVlAPKGtlLDPD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 267 LLVELWKREKVT--------FSHCVPTILQMVMNARaaqgvdfkgwKVIIGGSALNRSLYEAAKAR--GIQLTAAYGMSE 336
Cdd:cd12117 217 ALGALIAEEGVTvlwltaalFNQLADEDPECFAGLR----------ELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 337 TCpLISCAYLNDELlagsEDERTTYRIkaGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPE------ 410
Cdd:cd12117 287 NT-TFTTSHVVTEL----DEVAGSIPI--GRPIANTRVYVLDEDGRPVPP-GVP-GELYVGGDGLALGYLNRPAltaerf 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 411 ------RGEELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERP 484
Cdd:cd12117 358 vadpfgPGERLYR-----TGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRL 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15599119 485 FALLVVREGqqLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKR 541
Cdd:cd12117 433 VAYVVAEGA--LDAAELRAFLR-----ERLPAYMVPAAFVVLDELPLTANGKVDRRA 482
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
19-538 |
4.42e-23 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 104.28 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 19 LIKSLMLSGRRYEKSHEIVyRDQVRYSyATFNERVARlANVLS---EAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVL 95
Cdd:PRK06814 633 LFEALIEAAKIHGFKKLAV-EDPVNGP-LTYRKLLTG-AFVLGrklKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVP 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 96 HTINIRLSPEQILYTMNHAEDRFVLVNSEFV------PLYQAVAGQLatveRTILLTDGAeksAELpGLVGEYESLLAAA 169
Cdd:PRK06814 710 AMINFSAGIANILSACKAAQVKTVLTSRAFIekarlgPLIEALEFGI----RIIYLEDVR---AQI-GLADKIKGLLAGR 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 170 SPRYDFPDFDENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYV 249
Cdd:PRK06814 782 FPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-------FSPEDKVFNALPVFHSFGLTGGLV 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 250 ATML-GVKQV-YPG----RYDPELLVElwkrekvTFShcvpTIL----QMVMN-ARAAQGVDFKGWKVIIGGS----ALN 314
Cdd:PRK06814 855 LPLLsGVKVFlYPSplhyRIIPELIYD-------TNA----TILfgtdTFLNGyARYAHPYDFRSLRYVFAGAekvkEET 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 315 RSLYeaAKARGIQLTAAYGMSETCPLISCaylndellagsedeRTTYRIKAGVP---VPLVDAaimdeqgRFLPADG-ES 390
Cdd:PRK06814 924 RQTW--MEKFGIRILEGYGVTETAPVIAL--------------NTPMHNKAGTVgrlLPGIEY-------RLEPVPGiDE 980
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 391 QGELVLRSPWLTQGYFREPERG--EELwRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVR 468
Cdd:PRK06814 981 GGRLFVRGPNVMLGYLRAENPGvlEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDA 1059
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 469 EVAVVGVPDPQWGERpfaLLVVREGQQLDARGLKEHLKpfvEQGnINKWAIPSQIAVVTDIPKTSVGKLD 538
Cdd:PRK06814 1060 LHAAVSIPDARKGER---IILLTTASDATRAAFLAHAK---AAG-ASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
36-540 |
5.20e-23 |
|
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: 102.06 E-value: 5.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:cd17649 6 LVFGDQ-SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSefvplyqavAGQLATVERTilltdgaeksaelPGLVGeyesllaaasprydfpdfdensiattfyttgttgN 195
Cdd:cd17649 85 AGLLLTHH---------PRQLAYVIYT-------------SGSTG----------------------------------T 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVYPGR---YDPELLVELW 272
Cdd:cd17649 109 PKGVAVSHGPLAAHCQATAERYG-------LTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDelwASADELAEMV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSHCVPTILQMVmnaraAQGVDFKGWKV-------IIGGSALNRSLYEAAKARGIQLTAAYGMSETCpLISCAY 345
Cdd:cd17649 182 RELGVTVLDLPPAYLQQL-----AEEADRTGDGRppslrlyIFGGEALSPELLRRWLKAPVRLFNAYGPTEAT-VTPLVW 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 346 lndelLAGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADGesQGELVLRSPWLTQGYFREPE-------------RG 412
Cdd:cd17649 256 -----KCEAGAARAGASMPIGRPLGGRSAYILDADLNPVPVGV--TGELYIGGEGLARGYLGRPEltaerfvpdpfgaPG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 413 EELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQwGERPFALLVVRE 492
Cdd:cd17649 329 SRLYR-----TGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRA 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15599119 493 G--QQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd17649 403 AaaQPELRAQLRTALR-----ASLPDYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
36-506 |
8.41e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 102.26 E-value: 8.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK08279 56 LLFEDQ-SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFVPLYQAVAGQLaTVERTILLTDGAEKSAelPGLVGEYESLLAaaspryDFPDFDENSIATTFYTTGTTG- 194
Cdd:PRK08279 135 AKHLIVGEELVEAFEEARADL-ARPPRLWVAGGDTLDD--PEGYEDLAAAAA------GAPTTNPASRSGVTAKDTAFYi 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 -------NPKGVYFSHRQLvlhTLAMASTIGSLDsirlLGTSDV-YMPItPMFH----VHAWGTPYV--ATM-LGVKqvY 259
Cdd:PRK08279 206 ytsgttgLPKAAVMSHMRW---LKAMGGFGGLLR----LTPDDVlYCCL-PLYHntggTVAWSSVLAagATLaLRRK--F 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 260 PGRydpellvELWK---REKVTFSHCVPTILQMVMNARAAQgvDFKGWKV-IIGGSALNRSLYEAAKAR-GI-QLTAAYG 333
Cdd:PRK08279 276 SAS-------RFWDdvrRYRATAFQYIGELCRYLLNQPPKP--TDRDHRLrLMIGNGLRPDIWDEFQQRfGIpRILEFYA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 334 MSETcpliSCAYLNDELLAGSEDeRTTYRIKAgvPVPLV------DAAIMDEQGRFLP-ADGEsQGELV----LRSPWlt 402
Cdd:PRK08279 347 ASEG----NVGFINVFNFDGTVG-RVPLWLAH--PYAIVkydvdtGEPVRDADGRCIKvKPGE-VGLLIgritDRGPF-- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 403 QGYfREPERGEE-LWRGG------WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGV 475
Cdd:PRK08279 417 DGY-TDPEASEKkILRDVfkkgdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGV 495
|
490 500 510
....*....|....*....|....*....|..
gi 15599119 476 PDPQWGERP-FALLVVREGQQLDARGLKEHLK 506
Cdd:PRK08279 496 EVPGTDGRAgMAAIVLADGAEFDLAALAAHLY 527
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
40-540 |
1.23e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 102.93 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFV 119
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 120 LVNSEfvplyQAVAGQLATVERTILLTDGAEKSAELPGLVGEyesllaaasprydfPDFDENSIATTFYTTGTTGNPKGV 199
Cdd:PRK12467 614 LTQSH-----LLAQLPVPAGLRSLCLDEPADLLCGYSGHNPE--------------VALDPDNLAYVIYTSGSTGQPKGV 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 200 YFSHRQLVLHTLAMAStigsldSIRLLGTSDVYMPITPMFHVHAWGTpYVATMLGVKQVYPGR---YDPELLVELWKREK 276
Cdd:PRK12467 675 AISHGALANYVCVIAE------RLQLAADDSMLMVSTFAFDLGVTEL-FGALASGATLHLLPPdcaRDAEAFAALMADQG 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 277 VTFSHCVPTILQMVMNArAAQGVDFKGWKVIIGGSALNRSLYEA--AKARGIQLTAAYGMSETCPLISCAYLndellagS 354
Cdd:PRK12467 748 VTVLKIVPSHLQALLQA-SRVALPRPQRALVCGGEALQVDLLARvrALGPGARLINHYGPTETTVGVSTYEL-------S 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 355 EDERTTYRIKAGVPVPLVDAAIMDEQgrFLPADGESQGELVLRSPWLTQGYFREP----ER---------GEELWRggwm 421
Cdd:PRK12467 820 DEERDFGNVPIGQPLANLGLYILDHY--LNPVPVGVVGELYIGGAGLARGYHRRPaltaERfvpdpfgadGGRLYR---- 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 422 hTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQwGERPFALLV---VREGQQLDA 498
Cdd:PRK12467 894 -TGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYLVpaaVADGAEHQA 971
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15599119 499 RG--LKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:PRK12467 972 TRdeLKAQL-----RQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-555 |
1.73e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.73 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK12316 2022 VVFGDQ-HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSG 2100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNS---EFVPLYQAVAgqlatverTILLTDGAEksaelpglvgeyeslLAAASPRYDFPDFDENSIATTFYTTGT 192
Cdd:PRK12316 2101 AALLLTQRhllERLPLPAGVA--------RLPLDRDAE---------------WADYPDTAPAVQLAGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 193 TGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWGTpYVATMLGVKQVY--PGRYDPELLV 269
Cdd:PRK12316 2158 TGLPKGVAVSHGALVAHCQAAGERYE-------LSPADCELQFMSFsFDGAHEQW-FHPLLNGARVLIrdDELWDPEQLY 2229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 270 ELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSALNRSLYEAAKA--RGIQLTAAYGMSETC--PLIscay 345
Cdd:PRK12316 2230 DEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEalRPVYLFNGYGPTEAVvtPLL---- 2305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 346 lndeLLAGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADGesQGELVLRSPWLTQGYFREP----ER---------G 412
Cdd:PRK12316 2306 ----WKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGM--AGELYLGGEGLARGYLNRPgltaERfvpdpfsasG 2379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 413 EELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQwGERPFALLVVRE 492
Cdd:PRK12316 2380 ERLYR-----TGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVVPDD 2453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599119 493 GQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRI-RIEIAQWQEAGSA 555
Cdd:PRK12316 2454 AAEDLLAELRAWLA-----ARLPAYMVPAHWVVLERLPLNPNGKLDRKALpKPDVSQLRQAYVA 2512
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
44-543 |
1.83e-22 |
|
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: 99.95 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQIlytmnhaEDRFvlvns 123
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDL-------RDRV----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 efvplyQAVAGQLATVERTIlltdgaeksaelpglvgeyesllAAASPRYDFpdFDENSIAttfyttgttgNPKGVYFSH 203
Cdd:cd05974 69 ------DRGGAVYAAVDENT-----------------------HADDPMLLY--FTSGTTS----------KPKLVEHTH 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 204 RQLVLHTLAMASTIGsldsirlLGTSDVYMPIT-PMFHVHAWGT---PYVATMLGVKQVYPgRYDPELLVELWKREKVTF 279
Cdd:cd05974 108 RSYPVGHLSTMYWIG-------LKPGDVHWNISsPGWAKHAWSCffaPWNAGATVFLFNYA-RFDAKRVLAALVRYGVTT 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 280 SHCVPTILQMVMNARAAqGVDFKGWKVIIGGSALNRSLYEAAK-ARGIQLTAAYGMSETCPLISCAyLNDELLAGSeder 358
Cdd:cd05974 180 LCAPPTVWRMLIQQDLA-SFDVKLREVVGAGEPLNPEVIEQVRrAWGLTIRDGYGQTETTALVGNS-PGQPVKAGS---- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 359 ttyrikAGVPVPLVDAAIMDEQGRflPADgesQGELVL-----RSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMG 433
Cdd:cd05974 254 ------MGRPLPGYRVALLDPDGA--PAT---EGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 434 FIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQ------LDA-RGLKEHLK 506
Cdd:cd05974 323 YLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEpspetaLEIfRFSRERLA 402
|
490 500 510
....*....|....*....|....*....|....*..
gi 15599119 507 PFveqGNINKWAIpsqiavvTDIPKTSVGKLDKKRIR 543
Cdd:cd05974 403 PY---KRIRRLEF-------AELPKTISGKIRRVELR 429
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
37-541 |
2.48e-22 |
|
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: 100.04 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 37 VYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAED 116
Cdd:cd12114 6 VICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 117 RFVLVNSEfvplyqaVAGQLATVERTILLTDGAEKSAELPGLVgeyesLLAAASPRYDFpdFDENSIATtfyttgttgnP 196
Cdd:cd12114 86 RLVLTDGP-------DAQLDVAVFDVLILDLDALAAPAPPPPV-----DVAPDDLAYVI--FTSGSTGT----------P 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 197 KGVYFSHRqlvlhtlAMASTIGSLDSIRLLGTSDVYMPITPM-FHVHAWGTpYVATMLGVKQVYPG---RYDPELLVELW 272
Cdd:cd12114 142 KGVMISHR-------AALNTILDINRRFAVGPDDRVLALSSLsFDLSVYDI-FGALSAGATLVLPDearRRDPAHWAELI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSHCVPTILQMVMN-ARAAQGVDFKGWKVIIGGSALNRSLYEAAKAR--GIQLTAAYGMSETCpLISCAYLNDE 349
Cdd:cd12114 214 ERHGVTLWNSVPALLEMLLDvLEAAQALLPSLRLVLLSGDWIPLDLPARLRALapDARLISLGGATEAS-IWSIYHPIDE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 350 LlagsEDERTTyrIKAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPERGEELW-----RGGWMHTG 424
Cdd:cd12114 293 V----PPDWRS--IPYGRPLANQRYRVLDPRGRDCP-DWVP-GELWIGGRGVALGYLGDPELTAARFvthpdGERLYRTG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 425 DVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPqwGERPFALLVVREGQQldARGLKEH 504
Cdd:cd12114 365 DLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP--GGKRLAAFVVPDNDG--TPIAPDA 440
|
490 500 510
....*....|....*....|....*....|....*..
gi 15599119 505 LKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKKR 541
Cdd:cd12114 441 LRAFLAQ-TLPAYMIPSRVIALEALPLTANGKVDRAA 476
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
365-536 |
1.73e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 98.29 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 365 AGVPVPLVDAAIMDEQGRflPADGESQGELVLRSPWLTQ--GYFREPERGEE-LWR--GGWMHTGDVATLDGMGFIEIRD 439
Cdd:PRK00174 426 ATRPLPGIQPAVVDEEGN--PLEGGEGGNLVIKDPWPGMmrTIYGDHERFVKtYFStfKGMYFTGDGARRDEDGYYWITG 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 440 RIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARgLKEHLKPFV--EQGNInkw 517
Cdd:PRK00174 504 RVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDE-LRKELRNWVrkEIGPI--- 579
|
170
....*....|....*....
gi 15599119 518 AIPSQIAVVTDIPKTSVGK 536
Cdd:PRK00174 580 AKPDVIQFAPGLPKTRSGK 598
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
456-536 |
9.49e-21 |
|
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: 86.44 E-value: 9.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 456 ELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVG 535
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVR-----EELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 15599119 536 K 536
Cdd:pfam13193 76 K 76
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
195-537 |
2.42e-20 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 94.69 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRqlvlhTLAMASTIGSLDSIRLLGTSDVYMPITPMFHVHAWGTPYVAT--MLGVKQVYPGRYDPELLvELW 272
Cdd:PRK05857 183 EPKAVLLANR-----TFFAVPDILQKEGLNWVTWVVGETTYSPLPATHIGGLWWILTclMHGGLCVTGGENTTSLL-EIL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGS---ALNRSLYEAAKARGIQLtaaYGMSETCPLISCAYLND 348
Cdd:PRK05857 257 TTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGyGGSraiAADVRFIEATGVRTAQV---YGLSETGCTALCLPTDD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 349 ELLAgsederttyRIKAGV---PVPLVDAAIMDEQGR--FLPADGESQ--GELVLRSPWLTQGYFREPERGEELWRGGWM 421
Cdd:PRK05857 334 GSIV---------KIEAGAvgrPYPGVDVYLAATDGIgpTAPGAGPSAsfGTLWIKSPANMLGYWNNPERTAEVLIDGWV 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 422 HTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGerpfAL--LVVREGQQLD-- 497
Cdd:PRK05857 405 NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG----ALvgLAVVASAELDes 480
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15599119 498 -ARGLKEHLKPFVEQGNiNKWAIPSQIAVVTDIPKTSVGKL 537
Cdd:PRK05857 481 aARALKHTIAARFRRES-EPMARPSTIVIVTDIPRTQSGKV 520
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
43-552 |
2.48e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.79 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRfVLVN 122
Cdd:PRK12316 3082 RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQ-LLLS 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEFVPLYQAVAGQLATVERtilltdGAEKSAElpglvgeyesllaAASPRYDFPDfdenSIATTFYTTGTTGNPKGVYFS 202
Cdd:PRK12316 3161 QSHLRLPLAQGVQVLDLDR------GDENYAE-------------ANPAIRTMPE----NLAYVIYTSGSTGKPKGVGIR 3217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 203 HRQLVLHTLAMASTIGSLDSIRLLGTSdvympiTPMFHVHAWgTPYVATMLGVKQVYPGR---YDPELLVELWKREKVTF 279
Cdd:PRK12316 3218 HSALSNHLCWMQQAYGLGVGDRVLQFT------TFSFDVFVE-ELFWPLMSGARVVLAGPedwRDPALLVELINSEGVDV 3290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 280 SHCVPTILQMVMNARAAQgvDFKGWKVII-GGSALNRSLYEAAKArGIQLTAAYGMSETCPLISCAYLNDEllagseder 358
Cdd:PRK12316 3291 LHAYPSMLQAFLEEEDAH--RCTSLKRIVcGGEALPADLQQQVFA-GLPLYNLYGPTEATITVTHWQCVEE--------- 3358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 359 TTYRIKAGVPVPLVDAAIMDEQGRflPADGESQGELVLRSPWLTQGYFREP----ER--------GEELWRggwmhTGDV 426
Cdd:PRK12316 3359 GKDAVPIGRPIANRACYILDGSLE--PVPVGALGELYLGGEGLARGYHNRPgltaERfvpdpfvpGERLYR-----TGDL 3431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 427 ATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPdpqwGERPFALLVVREGQQLDARGLKEHLK 506
Cdd:PRK12316 3432 ARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLK 3507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15599119 507 pfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRI-RIEIAQWQEA 552
Cdd:PRK12316 3508 -----ASLPEYMVPAHLLFLERMPLTPNGKLDRKALpRPDAALLQQD 3549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-540 |
3.38e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 95.23 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:PRK12467 3114 LVFGDQ-QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSG 3192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEFVPLYQAVAGqlatvERTILLTDGAeksaelpglvgeyeslLAAASPRYDFPDFDENSIATTFYTTGTTGN 195
Cdd:PRK12467 3193 VKLLLTQAHLLEQLPAPAG-----DTALTLDRLD----------------LNGYSENNPSTRVMGENLAYVIYTSGSTGK 3251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWGTpYVATMLGVKQVY-PGR-YDPELLVELW 272
Cdd:PRK12467 3252 PKGVGVRHGALANHLCWIAEAYE-------LDANDRVLLFMSFsFDGAQERF-LWTLICGGCLVVrDNDlWDPEELWQAI 3323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 273 KREKVTFSHCVPTILQMVmnARAAQGVDFKGWKVII-GGSALNRSLYEA--AKARGIQLTAAYGMSEtcplisCAYLNDE 349
Cdd:PRK12467 3324 HAHRISIACFPPAYLQQF--AEDAGGADCASLDIYVfGGEAVPPAAFEQvkRKLKPRGLTNGYGPTE------AVVTVTL 3395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 350 LLAGSEDERTTYRIKAGVPVPLVDAAIMDEQGRflPADGESQGELVLRSPWLTQGYFREP----ER---------GEELW 416
Cdd:PRK12467 3396 WKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLN--PVPVGVAGELYIGGVGLARGYHQRPsltaERfvadpfsgsGGRLY 3473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 417 RggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVpDPQWGERPFALLVVREGQQL 496
Cdd:PRK12467 3474 R-----TGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGD 3547
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15599119 497 DARGLKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:PRK12467 3548 WRETLRDHL-----AASLPDYMVPAQLLVLAAMPLGPNGKVDRK 3586
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-555 |
5.06e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 94.84 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMdwdSHRYLECM---FAIPMIGAVLHTINIRLSPEQILYTMN 112
Cdd:PRK12467 1593 LVFGEQ-ELTYGELNRRANRLAHRLIALGVGPEVLVGIA---VERSLEMVvglLAILKAGGAYVPLDPEYPRERLAYMIE 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 113 HAEDRFVLVNSEFVPLYQAVAGQlatveRTILLTDGAEksaelpGLVGEYESLLAAAsprydfpdFDENSIATTFYTTGT 192
Cdd:PRK12467 1669 DSGIELLLTQSHLQARLPLPDGL-----RSLVLDQEDD------WLEGYSDSNPAVN--------LAPQNLAYVIYTSGS 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 193 TGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWGTpYVATMLGVKQVY--PGRY-DPELL 268
Cdd:PRK12467 1730 TGRPKGAGNRHGALVNRLCATQEAYQ-------LSAADVVLQFTSFaFDVSVWEL-FWPLINGARLVIapPGAHrDPEQL 1801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 269 VELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSALNRSLYEAAKAR--GIQLTAAYGMSETCplISCAYL 346
Cdd:PRK12467 1802 IQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERlpDTGLFNLYGPTETA--VDVTHW 1879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 347 NdeLLAGSEDERTTYRIkaGVPVPLVDAAIMDEQGRFLPADgeSQGELVLRSPWLTQGYFREP----ER---------GE 413
Cdd:PRK12467 1880 T--CRRKDLEGRDSVPI--GQPIANLSTYILDASLNPVPIG--VAGELYLGGVGLARGYLNRPaltaERfvadpfgtvGS 1953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 414 ELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVpDPQWGERPFALLV---- 489
Cdd:PRK12467 1954 RLYR-----TGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVptdp 2027
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599119 490 ----VREGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRI-RIEIAQWQEAGSA 555
Cdd:PRK12467 2028 glvdDDEAQVALRAILKNHLK-----ASLPEYMVPAHLVFLARMPLTPNGKLDRKALpAPDASELQQAYVA 2093
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
43-540 |
6.94e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 94.64 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 S---EFVPLYQAVagQLATVERTILLTDGAEKSAELPGLVGEyesllaaasprydfpdfdenSIATTFYTTGTTGNPKGV 199
Cdd:PRK12316 616 ShlgRKLPLAAGV--QVLDLDRPAAWLEGYSEENPGTELNPE--------------------NLAYVIYTSGSTGKPKGA 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 200 YFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWGTpYVATMLGVKQVY--PGRY-DPELLVELWKRE 275
Cdd:PRK12316 674 GNRHRALSNRLCWMQQAYG-------LGVGDTVLQKTPFsFDVSVWEF-FWPLMSGARLVVaaPGDHrDPAKLVELINRE 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTILQMVMNARAAQGVDFKGwKVIIGGSALNRSLYEAAKARGIQ--LTAAYGMSETCPLISCAYLNDEllAG 353
Cdd:PRK12316 746 GVDTLHFVPSMLQAFLQDEDVASCTSLR-RIVCSGEALPADAQEQVFAKLPQagLYNLYGPTEAAIDVTHWTCVEE--GG 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 354 SEderttyrIKAGVPVPLVDAAIMDEQGRFLPAdgESQGELVLRSPWLTQGYFREP----ER--------GEELWRggwm 421
Cdd:PRK12316 823 DS-------VPIGRPIANLACYILDANLEPVPV--GVLGELYLAGRGLARGYHGRPgltaERfvpspfvaGERMYR---- 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 422 hTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVpdpqwGERPFALLVVREGQQLDAR-G 500
Cdd:PRK12316 890 -TGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGKQLVGYVVLESEGGDWReA 963
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15599119 501 LKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:PRK12316 964 LKAHL-----AASLPEYMVPAQWLALERLPLTPNGKLDRK 998
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
195-479 |
2.98e-19 |
|
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: 91.12 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHTLAMASTIGSLDSIrllGTSDVYMPITPMFHVHAWGTPYVATMLGVK-QVYPGryDPELLVELWK 273
Cdd:cd05927 128 NPKGVMLTHGNIVSNVAGVFKILEILNKI---NPTDVYISYLPLAHIFERVVEALFLYHGAKiGFYSG--DIRLLLDDIK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 274 REKVTFSHCVP----------------------TILQMVMNARAAQ----GVDFKGW-----------------KVIIGG 310
Cdd:cd05927 203 ALKPTVFPGVPrvlnriydkifnkvqakgplkrKLFNFALNYKLAElrsgVVRASPFwdklvfnkikqalggnvRLMLTG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 311 SA-LNRSLYEAAK-ARGIQLTAAYGMSETCPLISCAYLnDELLAGSederttyrikAGVPVP-----LVDAAIMDeqgrF 383
Cdd:cd05927 283 SApLSPEVLEFLRvALGCPVLEGYGQTECTAGATLTLP-GDTSVGH----------VGGPLPcaevkLVDVPEMN----Y 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 384 LPADGESQGELVLRSPWLTQGYFREPER-GEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIK-TGGEWLSSLELEDLI 461
Cdd:cd05927 348 DAKDPNPRGEVCIRGPNVFSGYYKDPEKtAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIY 427
|
330 340 350
....*....|....*....|....*....|
gi 15599119 462 SRHPAVRE------------VAVVgVPDPQ 479
Cdd:cd05927 428 ARSPFVAQifvygdslksflVAIV-VPDPD 456
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
34-540 |
6.85e-19 |
|
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: 89.45 E-value: 6.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 34 HEIVYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNH 113
Cdd:cd17650 3 AIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 114 AEDRFVLVNSEfvplyqavagQLATVERTilltdgaeksaelPGLVGeyesllaaasprydfpdfdensiattfyttgtt 193
Cdd:cd17650 83 SGAKLLLTQPE----------DLAYVIYT-------------SGTTG--------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 194 gNPKGVYFSHRQlVLHTLAMASTIGSLDS--IRLLGTSDvympitpmFHVHAWGTPYVATMLGVKQVYP----GRYDPEL 267
Cdd:cd17650 107 -KPKGVMVEHRN-VAHAAHAWRREYELDSfpVRLLQMAS--------FSFDVFAGDFARSLLNGGTLVIcpdeVKLDPAA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 268 LVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSALNRSLYEAAKAR----GIQLTAAYGMSETCplISC 343
Cdd:cd17650 177 LYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAArfgqGMRIINSYGVTEAT--IDS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 344 AYLnDELLAGSEDERTTyriKAGVPVPLVDAAIMDEQGRFLPADgeSQGELVLRSPWLTQGYFREPERGEE------LWR 417
Cdd:cd17650 255 TYY-EEGRDPLGDSANV---PIGRPLPNTAMYVLDERLQPQPVG--VAGELYIGGAGVARGYLNRPELTAErfvenpFAP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 418 GGWMH-TGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREgqQL 496
Cdd:cd17650 329 GERMYrTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA--TL 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15599119 497 DARGLKEHLKPFVEQgninkWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd17650 407 NTAELRAFLAKELPS-----YMIPSYYVQLDALPLTPNGKVDRR 445
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
195-494 |
8.00e-19 |
|
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: 89.58 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHTLAMASTIGSLdsirlLGTSDVYMPITPMFHVH---------AWG---------TPYVATMLGVK 256
Cdd:cd17639 102 NPKGVMLTHGNLVAGIAGLGDRVPEL-----LGPDDRYLAYLPLAHIFelaaenvclYRGgtigygsprTLTDKSKRGCK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 257 qvypG---RYDPELLV---ELWKR------EKVTfshCVPTILQMV----MNARAAQ---GVD--------FK------G 303
Cdd:cd17639 177 ----GdltEFKPTLMVgvpAIWDTirkgvlAKLN---PMGGLKRTLfwtaYQSKLKAlkeGPGtplldelvFKkvraalG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 304 WKVII---GGSALNRSLYEAAKARGIQLTAAYGMSETCpliSCAYLND--ELLAGSederttyrikAGVPVPLVDAAIMD 378
Cdd:cd17639 250 GRLRYmlsGGAPLSADTQEFLNIVLCPVIQGYGLTETC---AGGTVQDpgDLETGR----------VGPPLPCCEIKLVD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 379 -EQGRFLPADGESQGELVLRSPWLTQGYFREPERGEELWRG-GWMHTGDVATLDGMGFIEIRDRIKDVIKT-GGEWLSSL 455
Cdd:cd17639 317 wEEGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGdGWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNGEYIALE 396
|
330 340 350
....*....|....*....|....*....|....*....
gi 15599119 456 ELEDLISRHPAVREVAVVGVPDPQwgeRPFALLVVREGQ 494
Cdd:cd17639 397 KLESIYRSNPLVNNICVYADPDKS---YPVAIVVPNEKH 432
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
42-537 |
2.44e-18 |
|
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: 88.45 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 42 VRYSYATFNERVARLANVLSEAGvKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAED---RF 118
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLAAILADagpRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 119 VLVNSEFVPLYQAVAGQLATVERTILLTDgaeksaelpglvgeyESLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKG 198
Cdd:cd05931 102 VLTTAAALAAVRAFAASRPAAGTPRLLVV---------------DLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 199 VYFSHRQLVLHTLAMASTIGSLDSIRLLGTsdvympiTPMFH----VHAWGTPYVAtmlGVKQVY--PGRY--DPELLVE 270
Cdd:cd05931 167 VVVTHRNLLANVRQIRRAYGLDPGDVVVSW-------LPLYHdmglIGGLLTPLYS---GGPSVLmsPAAFlrRPLRWLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 271 LWKREKVTFS--------HCVptilQMVmNARAAQGVDFKGWKVIIGGS-----ALNRSLYEAAKARGIQ---LTAAYGM 334
Cdd:cd05931 237 LISRYRATISaapnfaydLCV----RRV-RDEDLEGLDLSSWRVALNGAepvrpATLRRFAEAFAPFGFRpeaFRPSYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 335 SETCPLISCA---------YLNDELLAG------SEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADGESqGELVLRSP 399
Cdd:cd05931 312 AEATLFVSGGppgtgpvvlRVDRDALAGravavaADDPAARELVSCGRPLPDQEVRIVDPETGRELPDGEV-GEIWVRGP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 400 WLTQGYFREPERGEELWR-------GGWMHTGDVATLDGmGFIEIRDRIKDVIKTGGEWLSSLELEDLISR-HPAVRE-- 469
Cdd:cd05931 391 SVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPgc 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599119 470 VAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLKPFV--EQGninkwAIPSQIAVVT--DIPKTSVGKL 537
Cdd:cd05931 470 VAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVarEHG-----VAPADVVLVRpgSIPRTSSGKI 536
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
43-545 |
7.14e-18 |
|
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: 86.25 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEFvplyqavagqlatvertILLTDGAEksaelpGLvgeyesllaaasprydfpdfdensiattfyttgttgnPKGVYFS 202
Cdd:cd05940 83 AAL-----------------YIYTSGTT------GL-------------------------------------PKAAIIS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 203 HRQLVLHTLAMASTIGSLDSIRLLGTsdvympiTPMFH----VHAWGTPYVATM-LGVKQVYPGRydpellvELWK---R 274
Cdd:cd05940 103 HRRAWRGGAFFAGSGGALPSDVLYTC-------LPLYHstalIVGWSACLASGAtLVIRKKFSAS-------NFWDdirK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVPTILQMVMNARAAQgvDFKGWKV-IIGGSALNRSLYEAAKAR-GI-QLTAAYGMSE-TCPLIScaYLNDEL 350
Cdd:cd05940 169 YQATIFQYIGELCRYLLNQPPKP--TERKHKVrMIFGNGLRPDIWEEFKERfGVpRIAEFYAATEgNSGFIN--FFGKPG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 351 LAGsedeRTTYRIKAGVPVPLV------DAAIMDEQGRFLPA-DGESqGELVLR-SP-WLTQGYFREPERGEELWRG--- 418
Cdd:cd05940 245 AIG----RNPSLLRKVAPLALVkydlesGEPIRDAEGRCIKVpRGEP-GLLISRiNPlEPFDGYTDPAATEKKILRDvfk 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 419 ---GWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERP-FALLVVREGQ 494
Cdd:cd05940 320 kgdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAgMAAIVLQPNE 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15599119 495 QLDARGLKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIE 545
Cdd:cd05940 400 EFDLSALAAHL-----EKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
34-542 |
1.13e-17 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 85.99 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 34 HEIVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMdwdSHRYLECMFAIPMI----GAVLhTINIRLSPEQILY 109
Cdd:cd17656 5 VAVVFENQ-KLTYRELNERSNQLARFLREKGVKKDSIVAIM---MERSAEMIVGILGIlkagGAFV-PIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 110 TMNHAEDRFVLVNSEfvplyqaVAGQLATVERTILLTDGAEKSAELPGLVGEYEsllaaasprydfpdfdENSIATTFYT 189
Cdd:cd17656 80 IMLDSGVRVVLTQRH-------LKSKLSFNKSTILLEDPSISQEDTSNIDYINN----------------SDDLLYIIYT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 190 TGTTGNPKGVYFSHRQLVlHTLAMastigSLDSIRLLGTSDVYMPITPMFHVHAwgTPYVATMLGVKQVY----PGRYDP 265
Cdd:cd17656 137 SGTTGKPKGVQLEHKNMV-NLLHF-----EREKTNINFSDKVLQFATCSFDVCY--QEIFSTLLSGGTLYiireETKRDV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 266 ELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVII-GGSAL--NRSLYEAAKARGIQLTAAYGMSETcplis 342
Cdd:cd17656 209 EQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIItAGEQLviTNEFKEMLHEHNVHLHNHYGPSET----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 343 caylndellagseDERTTYRIKAGVPVPL----------VDAAIMDEQGRFLPADgeSQGELVLRSPWLTQGYFREPERG 412
Cdd:cd17656 284 -------------HVVTTYTINPEAEIPElppigkpisnTWIYILDQEQQLQPQG--IVGELYISGASVARGYLNRQELT 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 413 EE------------LWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREvAVVGVPDPQW 480
Cdd:cd17656 349 AEkffpdpfdpnerMYR-----TGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE-AVVLDKADDK 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599119 481 GERPFALLVVREgQQLDARGLKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRI 542
Cdd:cd17656 423 GEKYLCAYFVME-QELNISQLREYL-----AKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
44-491 |
3.07e-17 |
|
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: 84.78 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLV-N 122
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAeD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEFVPLYQAVAGQLATVERTI--------------------LLTDGAEKSAELPGLvgeYESLLAAASPrydfpdfdeNS 182
Cdd:cd17641 92 EEQVDKLLEIADRIPSVRYVIycdprgmrkyddprlisfedVVALGRALDRRDPGL---YEREVAAGKG---------ED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 183 IATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITP----MFHVHAWGTPYVA-------- 250
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADP-------LGPGDEYVSVLPlpwiGEQMYSVGQALVCgfivnfpe 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 251 ----TMLGVKQVYPG------RYDPELLVELWKR--EKVTFSHCVPTILQMVMNARAAQGVDFK------------GWKV 306
Cdd:cd17641 233 epetMMEDLREIGPTfvllppRVWEGIAADVRARmmDATPFKRFMFELGMKLGLRALDRGKRGRpvslwlrlaswlADAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 307 II-----------------GGSALNRSLYEAAKARGIQLTAAYGMSETCPLISCAYlndellAGSEDERTTyrikaGVPV 369
Cdd:cd17641 313 LFrplrdrlgfsrlrsaatGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHR------DGDVDPDTV-----GVPF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 370 PLVDAAIMDEqgrflpadgesqGELVLRSPWLTQGYFREPE-RGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTG 448
Cdd:cd17641 382 PGTEVRIDEV------------GEILVRSPGVFVGYYKNPEaTAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTS 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15599119 449 -GEWLSSLELEDLISRHPAVREVAVVGvpdpqwGERPF--ALLVVR 491
Cdd:cd17641 450 dGTRFSPQFIENKLKFSPYIAEAVVLG------AGRPYltAFICID 489
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
196-483 |
5.11e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 81.02 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLvlhtlaMASTIGSLDSIRLLgTSDVYMPITPMFHVHAWGTPYVATML-GVKQVYPgrYDP---ELLVEL 271
Cdd:PRK06334 198 PKGVPLTHANL------LANQRACLKFFSPK-EDDVMMSFLPPFHAYGFNSCTLFPLLsGVPVVFA--YNPlypKKIVEM 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 272 WKREKVTFSHCVPTILQMVMNARAAQGVDFKGWK-VIIGGSALNRSLYEAAKAR--GIQLTAAYGMSETCPLIScayLND 348
Cdd:PRK06334 269 IDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRfVVIGGDAFKDSLYQEALKTfpHIQLRQGYGTTECSPVIT---INT 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 349 EllAGSEDERTTyrikaGVPVPLVDAAIMDEQGRFLPADGEsQGELVLRSPWLTQGYFREPERGEELWRGG--WMHTGDV 426
Cdd:PRK06334 346 V--NSPKHESCV-----GMPIRGMDVLIVSEETKVPVSSGE-TGLVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTGDL 417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599119 427 ATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRH---PAVRE---VAVVGVPdpqwGER 483
Cdd:PRK06334 418 GYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHagpLVVCGLP----GEK 476
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
42-537 |
1.63e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 79.27 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 42 VRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVL-------HTINIRLSPEQILYTMNHA 114
Cdd:PRK07768 28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLtmlhqptPRTDLAVWAEDTLRVIGMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 115 EDRFVLVNSEFVPLYQAVAGQLATVertILLTDgaeksaelpglvgeyesLLAAASPryDFPDFDENSIATTFYTTGTTG 194
Cdd:PRK07768 108 GAKAVVVGEPFLAAAPVLEEKGIRV---LTVAD-----------------LLAADPI--DPVETGEDDLALMQLTSGSTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHTLAMastigsLDSIRLLGTSDVYMPITPMFH----VHAWGTPYVATMLGVKqVYPGRY--DPELL 268
Cdd:PRK07768 166 SPKAVQITHGNLYANAEAM------FVAAEFDVETDVMVSWLPLFHdmgmVGFLTVPMYFGAELVK-VTPMDFlrDPLLW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 269 VELWKREKVTFShCVP----TILQMVMNARAAQG-VDFKGWKVIIGGS-----ALNRSLYEAAKARGIQLTA---AYGMS 335
Cdd:PRK07768 239 AELISKYRGTMT-AAPnfayALLARRLRRQAKPGaFDLSSLRFALNGAepidpADVEDLLDAGARFGLRPEAilpAYGMA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 336 ET----------CPLISCaYLNDELLAG------SEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPAdgESQGELVLRSP 399
Cdd:PRK07768 318 EAtlavsfspcgAGLVVD-EVDADLLAAlrravpATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPP--RGVGVIELRGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 400 WLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVRE--VAVVGVPD 477
Cdd:PRK07768 395 SVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgnAVAVRLDA 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599119 478 PQWGERpFALLV-VREGQQLDARGLKEHL---KPFVEQGninkwAIPSQIAVVT--DIPKTSVGKL 537
Cdd:PRK07768 475 GHSREG-FAVAVeSNAFEDPAEVRRIRHQvahEVVAEVG-----VRPRNVVVLGpgSIPKTPSGKL 534
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
43-542 |
2.72e-15 |
|
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: 78.13 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:cd12115 24 SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEfvplyqavagQLATVertiLLTDGAeksaelpglVGEyesllaaasprydfpdfdensiattfyttgttgnPKGVYFS 202
Cdd:cd12115 104 PD----------DLAYV----IYTSGS---------TGR----------------------------------PKGVAIE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 203 HRQLVLHTLAMASTIGSLDSIRLLGTSDVY--MPITPMFHVHAWGtpyvATMLGVKQVYPgrydpelLVELWKREKVTFS 280
Cdd:cd12115 127 HRNAAAFLQWAAAAFSAEELAGVLASTSICfdLSVFELFGPLATG----GKVVLADNVLA-------LPDLPAAAEVTLI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 281 HCVPTILQMVMNARAAQgvdfKGWKVI-IGGSALNRSLYE--AAKARGIQLTAAYGMSETCPLISCAylndELLAGSEDE 357
Cdd:cd12115 196 NTVPSAAAELLRHDALP----ASVRVVnLAGEPLPRDLVQrlYARLQVERVVNLYGPSEDTTYSTVA----PVPPGASGE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 358 RTTyrikaGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPER------------GEELWRggwmhTGD 425
Cdd:cd12115 268 VSI-----GRPLANTQAYVLDRALQPVP-LGVP-GELYIGGAGVARGYLGRPGLtaerflpdpfgpGARLYR-----TGD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 426 VATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREvAVVGVPDPQWGERPFALLVVRE-GQQLDARGLKEH 504
Cdd:cd12115 336 LVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVRE-AVVVAIGDAAGERRLVAYIVAEpGAAGLVEDLRRH 414
|
490 500 510
....*....|....*....|....*....|....*...
gi 15599119 505 LkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRI 542
Cdd:cd12115 415 L-----GTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
27-474 |
3.57e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 78.52 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 27 GRRyekshEIVYRDQVRYSYATFNER---VARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLS 103
Cdd:PLN02614 65 GRR-----EIVDGKPGKYVWQTYQEVydiVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 104 PEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDGA----EKSAELPGLV--GEYESLLAAASPRYDFPD 177
Cdd:PLN02614 140 AGAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGGVsreqKEEAETFGLViyAWDEFLKLGEGKQYDLPI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 178 FDENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGSLDSIrlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQ 257
Cdd:PLN02614 220 KKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAA--LTVKDVYLSYLPLAHIFDRVIEECFIQHGAAI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 258 VYpGRYDPELLVELWKREKVTFSHCVPTILQMV---MNARAAQGVDFKGW------------------------------ 304
Cdd:PLN02614 298 GF-WRGDVKLLIEDLGELKPTIFCAVPRVLDRVysgLQKKLSDGGFLKKFvfdsafsykfgnmkkgqshveasplcdklv 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 305 ------------KVIIGGSALNRSLYEA--AKARGIQLTAAYGMSETCPLiSCAYLNDEL-LAGSederttyrikAGVPV 369
Cdd:PLN02614 377 fnkvkqglggnvRIILSGAAPLASHVESflRVVACCHVLQGYGLTESCAG-TFVSLPDELdMLGT----------VGPPV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 370 PLVDAAIMDEQGRFLPADGES-QGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIK-T 447
Cdd:PLN02614 446 PNVDIRLESVPEMEYDALASTpRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKlS 525
|
490 500
....*....|....*....|....*..
gi 15599119 448 GGEWLSSLELEDLISRHPAVREVAVVG 474
Cdd:PLN02614 526 QGEYVAVENIENIYGEVQAVDSVWVYG 552
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
195-540 |
5.33e-15 |
|
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: 77.48 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHTLAMASTIGSLDSIRLLGTS----DVYMP-ITPMFHVHAwgTPYVATmlgvKQVYPgryDPELLV 269
Cdd:cd17644 120 KPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFAsiafDVAAEeIYVTLLSGA--TLVLRP----EEMRS---SLEDFV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 270 ELWKREKVTFSHCVPTILQMVMNARAAQGVDF--KGWKVIIGGSALNRSLYEA-AKARG--IQLTAAYGMSETCPLISCA 344
Cdd:cd17644 191 QYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQwQKNVGnfIQLINVYGPTEATIAATVC 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 345 YLNDEllagseDERTTYRIKAGVPVPLVDAAIMDEQGRFLPAdgESQGELVLRSPWLTQGYFREPE-------------- 410
Cdd:cd17644 271 RLTQL------TERNITSVPIGRPIANTQVYILDENLQPVPV--GVPGELHIGGVGLARGYLNRPEltaekfishpfnss 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 411 RGEELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVV 490
Cdd:cd17644 343 ESERLYK-----TGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVP 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15599119 491 REGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd17644 418 HYEESPSTVELRQFLK-----AKLPDYMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
20-543 |
6.82e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 77.76 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 20 IKSLMLSGRRYEKSHEIVYRDQVRY------SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGA 93
Cdd:PRK06060 1 MRNGNLAGLLAEQASEAGWYDRPAFyaadvvTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 94 VLHTINIRLSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAgqlaTVERTILLTDGAEKSAelpglvGEYESLLAAAsprY 173
Cdd:PRK06060 81 MAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSR----VAEAAELMSEAARVAP------GGYEPMGGDA---L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 174 DFPDFDENSIATtfyttgttgnPKGVYFSHRQLVLHTLAMA--------STIGsLDSIRL-----LGTSdVYMPItpmfh 240
Cdd:PRK06060 148 AYATYTSGTTGP----------PKAAIHRHADPLTFVDAMCrkalrltpEDTG-LCSARMyfaygLGNS-VWFPL----- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 241 vhAWGTPYVATMLGV----KQVYPGRYDPELLvelwkrekvtfsHCVPTILQMVMNARAAQgvDFKGWK-VIIGGSALNR 315
Cdd:PRK06060 211 --ATGGSAVINSAPVtpeaAAILSARFGPSVL------------YGVPNFFARVIDSCSPD--SFRSLRcVVSAGEALEL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 316 SLYEaakargiQLTAAYGMSETCPLISCAYLNDELLAGSEDErttYRIKA-GVPVPLVDAAIMDEQGRFLPADGEsqGEL 394
Cdd:PRK06060 275 GLAE-------RLMEFFGGIPILDGIGSTEVGQTFVSNRVDE---WRLGTlGRVLPPYEIRVVAPDGTTAGPGVE--GDL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 395 VLRSPWLTQGYFREPErgEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVG 474
Cdd:PRK06060 343 WVRGPAIAKGYWNRPD--SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVA 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599119 475 VPDPQWGERPFALLVVREGQQLDARGLKEHLKPFVEQgnINKWAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:PRK06060 421 VRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNR--LSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
43-507 |
1.33e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 76.06 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQIlytmnhaedrfvlvn 122
Cdd:PRK09029 28 VLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL--------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEFVPLYQAvagqlatveRTILLTDGAEKSAELPglvgeyeSLLAAASPRYDFPDFDENSIATTFYTTGTTGNPKGVYFS 202
Cdd:PRK09029 93 EELLPSLTL---------DFALVLEGENTFSALT-------SLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 203 HRQlvlHtlaMASTIGSLDSIRLlGTSDVYMPITPMFHVHA----WGTPYVATMLGVKQVYPgrydpeLLVELwkrEKVT 278
Cdd:PRK09029 157 AQA---H---LASAEGVLSLMPF-TAQDSWLLSLPLFHVSGqgivWRWLYAGATLVVRDKQP------LEQAL---AGCT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 279 FSHCVPTILQMVMNARAAQgVDFKgwKVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLIsCAYLNDEllagseder 358
Cdd:PRK09029 221 HASLVPTQLWRLLDNRSEP-LSLK--AVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTV-CAKRADG--------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 359 ttyriKAGVPVPLvdaaimdeQGRflpadgESQ---GELVLRSPWLTQGYFRE----PERGEElwrgGWMHTGDVATLDG 431
Cdd:PRK09029 288 -----LAGVGSPL--------PGR------EVKlvdGEIWLRGASLALGYWRQgqlvPLVNDE----GWFATRDRGEWQN 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599119 432 mGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDArgLKEHLKP 507
Cdd:PRK09029 345 -GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVN--LAEWLQD 417
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
306-537 |
1.63e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 76.32 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 306 VIIGGSALNRSLYEAAKAR-GIQLTAAYGMSET--CPLISCAYLNdellagsederTTYRiKAGVPVPLVDAAIMDEQGR 382
Cdd:PTZ00237 385 IWCGGEVIEESIPEYIENKlKIKSSRGYGQTEIgiTYLYCYGHIN-----------IPYN-ATGVPSIFIKPSILSEDGK 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 383 FLPadgESQ-GELVLR---SPWLTQGYFREPERGEELWRG--GWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLE 456
Cdd:PTZ00237 453 ELN---VNEiGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNT 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 457 LEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQ---QLDARGLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTS 533
Cdd:PTZ00237 530 IETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQsnqSIDLNKLKNEINNIITQ-DIESLAVLRKIIIVNQLPKTK 608
|
....
gi 15599119 534 VGKL 537
Cdd:PTZ00237 609 TGKI 612
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
40-540 |
3.53e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 75.85 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 40 DQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFV 119
Cdd:PRK10252 480 ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 120 LVNSEFvplyqavAGQLATVERTILLTdgaeKSAELPGLVGEYESLLAAASPRYDFpdFDENSIATtfyttgttgnPKGV 199
Cdd:PRK10252 560 ITTADQ-------LPRFADVPDLTSLC----YNAPLAPQGAAPLQLSQPHHTAYII--FTSGSTGR----------PKGV 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 200 YFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWG--TPYVAtmlGVKQVY--PGRY-DPELLVELWK 273
Cdd:PRK10252 617 MVGQTAIVNRLLWMQNHYP-------LTADDVVLQKTPCsFDVSVWEffWPFIA---GAKLVMaePEAHrDPLAMQQFFA 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 274 REKVTFSHCVPTILQMVMNARAAQGVDFKGW---KVIIGGSALNRSLYEaakaRGIQLTAA-----YGMSETCPLIScAY 345
Cdd:PRK10252 687 EYGVTTTHFVPSMLAAFVASLTPEGARQSCAslrQVFCSGEALPADLCR----EWQQLTGAplhnlYGPTEAAVDVS-WY 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 346 lndelLAGSED--ERTTYRIKAGVPVPLVDAAIMDEQGRFLPAdGESqGELVLRSPWLTQGYFREPE------------R 411
Cdd:PRK10252 762 -----PAFGEElaAVRGSSVPIGYPVWNTGLRILDARMRPVPP-GVA-GDLYLTGIQLAQGYLGRPDltasrfiadpfaP 834
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 412 GEELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVV------GVPDPQWGERPF 485
Cdd:PRK10252 835 GERMYR-----TGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHacvinqAAATGGDARQLV 909
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15599119 486 ALLVVREGQQLDARGLKEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:PRK10252 910 GYLVSQSGLPLDTSALQAQL-----RERLPPHMVPVVLLQLDQLPLSANGKLDRK 959
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
45-507 |
3.69e-14 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 75.18 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLS-EAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNS 123
Cdd:cd17632 69 TYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 124 EFVPLYQAVAGQLATVERTILL---------TDGAEKSAELPGLVGEYESLLAAASPRY--------DFPDFDENSIATT 186
Cdd:cd17632 149 EHLDLAVEAVLEGGTPPRLVVFdhrpevdahRAALESARERLAAVGIPVTTLTLIAVRGrdlppaplFRPEPDDDPLALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 187 FYTTGTTGNPKGVYFSHRqLVLHTLAMASTIGSLD---SIRLlgtsdVYMpitPMFHVHAWGTPYVATMLGVKQVYPGRY 263
Cdd:cd17632 229 IYTSGSTGTPKGAMYTER-LVATFWLKVSSIQDIRppaSITL-----NFM---PMSHIAGRISLYGTLARGGTAYFAAAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 264 DPELLVELWKREKVTFSHCVPTILQMVMNaRAAQGVDfkgWKVIIGGSALnrSLYEAAKA------RGIQLTAAygMSET 337
Cdd:cd17632 300 DMSTLFDDLALVRPTELFLVPRVCDMLFQ-RYQAELD---RRSVAGADAE--TLAERVKAelrervLGGRLLAA--VCGS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 338 CPLI--------SCayLNDELLAGSEDERTTYRIKAGVPV--PLVDAAIMD--EQGRFLPADGESQGELVLRSPWLTQGY 405
Cdd:cd17632 372 APLSaemkafmeSL--LDLDLHDGYGSTEAGAVILDGVIVrpPVLDYKLVDvpELGYFRTDRPHPRGELLVKTDTLFPGY 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 406 FREPERGEELW-RGGWMHTGDVATLDGMGFIEIRDRIKDVIK-TGGEWLSSLELEDLISRHPAVREVAVVGVpdpqwGER 483
Cdd:cd17632 450 YKRPEVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLKlSQGEFVTVARLEAVFAASPLVRQIFVYGN-----SER 524
|
490 500
....*....|....*....|....
gi 15599119 484 PFALLVVREGQQLDARGLKEHLKP 507
Cdd:cd17632 525 AYLLAVVVPTQDALAGEDTARLRA 548
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
423-560 |
4.84e-14 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 74.99 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 423 TGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLD----A 498
Cdd:PRK10524 477 TFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdreaR 556
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599119 499 RGLKEHLKPFVEQ--GNInkwAIPSQIAVVTDIPKTSVGKLDKKRIRiEIAQWQEAGSafLSTV 560
Cdd:PRK10524 557 LALEKEIMALVDSqlGAV---ARPARVWFVSALPKTRSGKLLRRAIQ-AIAEGRDPGD--LTTI 614
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
27-472 |
6.97e-14 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 74.38 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 27 GRRYEKSHeivYRDQVRYSYATFNERVARLANVLSEAGVKAGDTVAVMdwdSHRYLECMFAIPM-----IGAVlhTINIR 101
Cdd:PLN02387 93 GRKFEKLH---LGEYEWITYGQVFERVCNFASGLVALGHNKEERVAIF---ADTRAEWLIALQGcfrqnITVV--TIYAS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 102 LSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVERTILLTDGAEKSAELPGLVG--------EYESLLAAASPRY 173
Cdd:PLN02387 165 LGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSnwtvssfsEVEKLGKENPVDP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 174 DFPDfdENSIATTFYTTGTTGNPKGVYFSHRQlVLHTLAMASTIgsldsIRLLGTSDVYMPITPMFHVH----------- 242
Cdd:PLN02387 245 DLPS--PNDIAVIMYTSGSTGLPKGVMMTHGN-IVATVAGVMTV-----VPKLGKNDVYLAYLPLAHILelaaesvmaav 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 243 ----AWGTPYVATMLGVKQVYPGRYDPELLvelwkreKVTFSHCVPTILQMVMNArAAQGVDFKG--------------- 303
Cdd:PLN02387 317 gaaiGYGSPLTLTDTSNKIKKGTKGDASAL-------KPTLMTAVPAILDRVRDG-VRKKVDAKGglakklfdiaykrrl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 304 ------WkviIGGSALNRSLYEA---AKAR-----------------------------GIQLTAAYGMSETCpliscay 345
Cdd:PLN02387 389 aaiegsW---FGAWGLEKLLWDAlvfKKIRavlggrirfmlsggaplsgdtqrfiniclGAPIGQGYGLTETC------- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 346 lndellAG---SE-DERTTYRIKAGVP---VPLVDAaimdEQGRFLPADGE-SQGELVLRSPWLTQGYFREPERGEELW- 416
Cdd:PLN02387 459 ------AGatfSEwDDTSVGRVGPPLPccyVKLVSW----EEGGYLISDKPmPRGEIVIGGPSVTLGYFKNQEKTDEVYk 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599119 417 ---RG-GWMHTGDVATLDGMGFIEIRDRIKDVIK-TGGEWLSSLELEDLISRHPAVREVAV 472
Cdd:PLN02387 529 vdeRGmRWFYTGDIGQFHPDGCLEIIDRKKDIVKlQHGEYVSLGKVEAALSVSPYVDNIMV 589
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
44-543 |
7.27e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 74.27 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLS-------PEQILYTMNHAED 116
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 117 RFVLVNSEFVPLYQAVAGQLATVertilltdgaeksaelpgLVGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGNP 196
Cdd:PRK09192 130 AAIITPDELLPWVNEATHGNPLL------------------HVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 197 KGVYFSHRQLvlhtlaMASTIG-SLDSIRLlGTSDVYMPITPMFH----VHAWGTPyVATMLGVKQVYPGRY--DPELLV 269
Cdd:PRK09192 192 RGVIITHRAL------MANLRAiSHDGLKV-RPGDRCVSWLPFYHdmglVGFLLTP-VATQLSVDYLPTRDFarRPLQWL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 270 ELWKREKVTFSHCvPT----ILQMVMNARAAQGVDFKGWKVI-IGGSALN----RSLYEAAKARGIQ---LTAAYGMSET 337
Cdd:PRK09192 264 DLISRNRGTISYS-PPfgyeLCARRVNSKDLAELDLSCWRVAgIGADMIRpdvlHQFAEAFAPAGFDdkaFMPSYGLAEA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 338 CPLISCAYLN---------------DELLAGSEDERTTYR--IKAGVPVPLVDAAIMDEQGRFLPadgESQ-GELVLRSP 399
Cdd:PRK09192 343 TLAVSFSPLGsgivveevdrdrleyQGKAVAPGAETRRVRtfVNCGKALPGHEIEIRNEAGMPLP---ERVvGHICVRGP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 400 WLTQGYFREPERGEELWRGGWMHTGDVATLDGmGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVR--EVAVVGVPD 477
Cdd:PRK09192 420 SLMSGYFRDEESQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQ 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599119 478 PQwGERPFALLVVREGQQLDARGLKEHLKPFVEQGNinkwAIPSQIAVVT--DIPKTSVGKLDKKRIR 543
Cdd:PRK09192 499 EN-GEKIVLLVQCRISDEERRGQLIHALAALVRSEF----GVEAAVELVPphSLPRTSSGKLSRAKAK 561
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
293-474 |
1.27e-13 |
|
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: 73.55 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 293 ARAAQGVDfKGWKVIIGGSALNRSLYEAAKARGIQLTAAYGMSETCPLISCAYLNdellagsedertTYRI-KAGVPVPL 371
Cdd:cd05933 313 VRKALGLD-RCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQ------------AYRLlSCGKALPG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 372 VDAAIMDEqgrflpaDGESQGELVLRSPWLTQGYFREPERGEE-LWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKT-GG 449
Cdd:cd05933 380 CKTKIHNP-------DADGIGEICFWGRHVFMGYLNMEDKTEEaIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGG 452
|
170 180
....*....|....*....|....*.
gi 15599119 450 EWLSSLELEDLI-SRHPAVREVAVVG 474
Cdd:cd05933 453 ENVPPVPIEDAVkKELPIISNAMLIG 478
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
45-540 |
1.28e-13 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 73.06 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLvnse 124
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 125 fvplyqAVAGQLATVertiLLTDGAeksaelpglvgeyesllaaasprydfpdfdensiattfyttgtTGNPKGVYFSHR 204
Cdd:cd17652 90 ------TTPDNLAYV----IYTSGS-------------------------------------------TGRPKGVVVTHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 205 QlvLHTLAMASTigslDSIRLLGTSDVYMPITPMFHVHAWgtPYVATML-GVKQVYPGRYD---PELLVELWKREKVTFS 280
Cdd:cd17652 117 G--LANLAAAQI----AAFDVGPGSRVLQFASPSFDASVW--ELLMALLaGATLVLAPAEEllpGEPLADLLREHRITHV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 281 HCVPTILqMVMNARAAQGVDfkgwKVIIGGSALNRSLyeAAK-ARGIQLTAAYGMSETcplISCAYLNDELLAGSEdert 359
Cdd:cd17652 189 TLPPAAL-AALPPDDLPDLR----TLVVAGEACPAEL--VDRwAPGRRMINAYGPTET---TVCATMAGPLPGGGV---- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 360 tyrIKAGVPVPLVDAAIMDEQGRFLPAdGEsQGELVLRSPWLTQGYFREP----ER---------GEELWRggwmhTGDV 426
Cdd:cd17652 255 ---PPIGRPVPGTRVYVLDARLRPVPP-GV-PGELYIAGAGLARGYLNRPgltaERfvadpfgapGSRMYR-----TGDL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 427 ATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARGLKEHLK 506
Cdd:cd17652 325 ARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLA 404
|
490 500 510
....*....|....*....|....*....|....
gi 15599119 507 PFVEqgninKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd17652 405 ERLP-----GYMVPAAFVVLDALPLTPNGKLDRR 433
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
45-498 |
1.35e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 73.39 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 45 SYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEdrfvlvnse 124
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQ--------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 125 fvPlyQAVAGQ-LATVERTILLtdGAEKSAELPGLVGE--------YESLLAAASPR-YDFPDFDENSIATTFYTTGTTG 194
Cdd:PRK09274 114 --P--DAFIGIpKAHLARRLFG--WGKPSVRRLVTVGGrllwggttLATLLRDGAAApFPMADLAPDDMAAILFTSGSTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRqlvlHTLAMASTIGSLDSIRllgTSDVYMPITPMFHVHawgtpyvATMLGVKQV-------YPGRYDPEL 267
Cdd:PRK09274 188 TPKGVVYTHG----MFEAQIEALREDYGIE---PGEIDLPTFPLFALF-------GPALGMTSVipdmdptRPATVDPAK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 268 LVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWK-VIIGGSALNRSLYEAAKA---RGIQLTAAYGMSETCPLISC 343
Cdd:PRK09274 254 LFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRrVISAGAPVPIAVIERFRAmlpPDAEILTPYGATEALPISSI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 344 AylNDELLAGsederTTYR------IKAGVPVPLVDAAIMD---------EQGRFLPADGesQGELVLRSPWLTQGYFRE 408
Cdd:PRK09274 334 E--SREILFA-----TRAAtdngagICVGRPVDGVEVRIIAisdapipewDDALRLATGE--IGEIVVAGPMVTRSYYNR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 409 PE--RGEELWRGG---WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQwGER 483
Cdd:PRK09274 405 PEatRLAKIPDGQgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPG-AQR 483
|
490
....*....|....*
gi 15599119 484 PfaLLVVrEGQQLDA 498
Cdd:PRK09274 484 P--VLCV-ELEPGVA 495
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
195-538 |
5.44e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 71.66 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLvlhtLAMASTIgslDSIRLLGTSDVYMPITPMFHvhAWG------TPYvatMLGVKQ-VYPG----RY 263
Cdd:PRK08043 379 HPKGVVHSHKSL----LANVEQI---KTIADFTPNDRFMSALPLFH--SFGltvglfTPL---LTGAEVfLYPSplhyRI 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 264 DPELLVElwKREKVTFShcVPTILQMVmnARAAQGVDFKGWKVIIGGSalnRSLYEAAKAR-----GIQLTAAYGMSETC 338
Cdd:PRK08043 447 VPELVYD--RNCTVLFG--TSTFLGNY--ARFANPYDFARLRYVVAGA---EKLQESTKQLwqdkfGLRILEGYGVTECA 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 339 PLIScayLNDELLAGSEderTTYRIKAGvpvplvdaaiMDeqGRFLPADG-ESQGELVLRSPWLTQGYFR---------- 407
Cdd:PRK08043 518 PVVS---INVPMAAKPG---TVGRILPG----------MD--ARLLSVPGiEQGGRLQLKGPNIMNGYLRvekpgvlevp 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 408 --EPERGEElwRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGErpf 485
Cdd:PRK08043 580 taENARGEM--ERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE--- 654
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15599119 486 ALLVVREGQQLDarglKEHLKPFVEQGNINKWAIPSQIAVVTDIPKTSVGKLD 538
Cdd:PRK08043 655 ALVLFTTDSELT----REKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
102-479 |
6.14e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 71.67 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 102 LSPEQILYTMNHAEDRFVLVNSEFVPLYQAVAGQLATVeRTILLTDGAEKS-AELPGLVG----EYESLLAA--ASPRYD 174
Cdd:PLN02736 137 LGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCLSEIPSV-RLIVVVGGADEPlPSLPSGTGveivTYSKLLAQgrSSPQPF 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 175 FPDFDENsIATTFYTTGTTGNPKGVYFSHRQLVlhtlamASTIGSLDSIRlLGTSDVYMPITPMFHVHAWGTPYVATMLG 254
Cdd:PLN02736 216 RPPKPED-VATICYTSGTTGTPKGVVLTHGNLI------ANVAGSSLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 255 VK-QVYPGryDPELLVELWKREKVTFSHCVP----TILQMVMNA-RAAQGVDFKGW--------KVIIGG---SAL-NRS 316
Cdd:PLN02736 288 VAvGFYQG--DNLKLMDDLAALRPTIFCSVPrlynRIYDGITNAvKESGGLKERLFnaaynakkQALENGknpSPMwDRL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 317 LYEAAKAR---------------------------GIQLTAAYGMSETCPLIScaylndellAGSEDERTTYRIKAGVP- 368
Cdd:PLN02736 366 VFNKIKAKlggrvrfmssgasplspdvmeflricfGGRVLEGYGMTETSCVIS---------GMDEGDNLSGHVGSPNPa 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 369 --VPLVDAAIMDEQGRFLPAdgeSQGELVLRSPWLTQGYFREPERGEELWRG-GWMHTGDVAT-LDGmGFIEIRDRIKDV 444
Cdd:PLN02736 437 ceVKLVDVPEMNYTSEDQPY---PRGEICVRGPIIFKGYYKDEVQTREVIDEdGWLHTGDIGLwLPG-GRLKIIDRKKNI 512
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15599119 445 IKTG-GEWLSSLELEDLISRHPAVRE------------VAVVgVPDPQ 479
Cdd:PLN02736 513 FKLAqGEYIAPEKIENVYAKCKFVAQcfvygdslnsslVAVV-VVDPE 559
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
276-543 |
7.20e-13 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 70.80 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTILQMVmNARAAQGVDfkgwKVIIGGSALNRSLYEAAKArGIQLTAAYGMSETCplISCAYLndELLAGSe 355
Cdd:cd17653 189 TVDALMSTPSILSTL-SPQDFPNLK----TIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTECT--ISSTMT--ELLPGQ- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 356 derttyRIKAGVPVPLVDAAIMDEQGRFLPADGEsqGELVLRSPWLTQGYFREPERG-----EELWRGGWMH--TGDVAT 428
Cdd:cd17653 258 ------PVTIGKPIPNSTCYILDADLQPVPEGVV--GEICISGVQVARGYLGNPALTaskfvPDPFWPGSRMyrTGDYGR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 429 LDGMGFIEIRDRIKDVIKTGGeWLSSLE--LEDLISRHPAVREVAVVGVpdpqwGERPFAlLVVREGqqLDARGLKE--- 503
Cdd:cd17653 330 WTEDGGLEFLGREDNQVKVRG-FRINLEeiEEVVLQSQPEVTQAAAIVV-----NGRLVA-FVTPET--VDVDGLRSela 400
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15599119 504 -HLKPFveqgninkwAIPSQIAVVTDIPKTSVGKLDKKRIR 543
Cdd:cd17653 401 kHLPSY---------AVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
328-474 |
7.70e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 71.38 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 328 LTAAYGMSETCPLISCAYLNDELLAGSEDERTTYRIKAGVPVPlvdaaimdEQGrFLPADGESQGELVLRSPWLTQGYFR 407
Cdd:PLN02430 411 VVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVP--------EMG-YDPLGEPPRGEICVRGKCLFSGYYK 481
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599119 408 EPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIK-TGGEWLSSLELEDLISRHPAVREVAVVG 474
Cdd:PLN02430 482 NPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEYLENVYGQNPIVEDIWVYG 549
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
43-478 |
9.30e-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: 70.57 E-value: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 43 RYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE-DRFVlv 121
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEpDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 122 nseFVPLYQAVAgqlatverTILLTDGAeksaelpglvgeyesllaaasprydfpdfdensiattfyttgtTGNPKGVYF 201
Cdd:cd05910 80 ---GIPKADEPA--------AILFTSGS-------------------------------------------TGTPKGVVY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 202 SHRQLVLHTLAMASTIGsldsIRllgTSDVYMPITPMFHVhawgtpyVATMLGVKQVY-------PGRYDPELLVELWKR 274
Cdd:cd05910 106 RHGTFAAQIDALRQLYG----IR---PGEVDLATFPLFAL-------FGPALGLTSVIpdmdptrPARADPQKLVGAIRQ 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 275 EKVTFSHCVPTILQMVMNARAAQGVDFKGWK-VIIGGSALNRSLYEAAKA---RGIQLTAAYGMSETCPLisCAYLNDEL 350
Cdd:cd05910 172 YGVSIVFGSPALLERVARYCAQHGITLPSLRrVLSAGAPVPIALAARLRKmlsDEAEILTPYGATEALPV--SSIGSREL 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 351 LAgsedERTTYRIK-AGV----PVPLVDAAIM---DE-----QGRFLPADGESqGELVLRSPWLTQGYFREPE--RGEEL 415
Cdd:cd05910 250 LA----TTTAATSGgAGTcvgrPIPGVRVRIIeidDEpiaewDDTLELPRGEI-GEITVTGPTVTPTYVNRPVatALAKI 324
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599119 416 WRGG---WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDP 478
Cdd:cd05910 325 DDNSegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKP 390
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
36-540 |
1.12e-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: 69.89 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAE 115
Cdd:cd17645 17 VVDRGQ-SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 116 DRFVLVNSEfvplyqavagQLATVERTilltdgaeksaelPGLVGEyesllaaasprydfpdfdensiattfyttgttgn 195
Cdd:cd17645 96 AKILLTNPD----------DLAYVIYT-------------SGSTGL---------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVlhtlAMASTIGSLDSIRLLGTSDVYMPITpmFHVHAWGT-PYV---ATMLGVKQVYpgRYDPELLVEL 271
Cdd:cd17645 119 PKGVMIEHHNLV----NLCEWHRPYFGVTPADKSLVYASFS--FDASAWEIfPHLtagAALHVVPSER--RLDLDALNDY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 272 WKREKVTFSHcVPTILqmvmnARAAQGVDFKGWKVII-GGSALNRslyeaAKARGIQLTAAYGMSEtcpliscaylNDEL 350
Cdd:cd17645 191 FNQEGITISF-LPTGA-----AEQFMQLDNQSLRVLLtGGDKLKK-----IERKGYKLVNNYGPTE----------NTVV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 351 LAGSEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPaDGESqGELVLRSPWLTQGYFREPER------------GEELWRg 418
Cdd:cd17645 250 ATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQP-IGVA-GELCIAGEGLARGYLNRPELtaekfivhpfvpGERMYR- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 419 gwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPqwGERPFALLVVREGQQLDA 498
Cdd:cd17645 327 ----TGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDA--DGRKYLVAYVTAPEEIPH 400
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15599119 499 RGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:cd17645 401 EELREWLK-----NDLPDYMIPTYFVHLKALPLTANGKVDRK 437
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
331-542 |
1.83e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 69.54 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 331 AYGMSETCPLISCAYLNDELLAgsedertTY-RIKAGVPVPLVDAAIMDEQGRFLPaDGEsQGELVLRSPWLTQGYFREP 409
Cdd:PRK04813 292 TYGPTEATVAVTSIEITDEMLD-------QYkRLPIGYAKPDSPLLIIDEEGTKLP-DGE-QGEIVISGPSVSKGYLNNP 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 410 ERGEELW---RGGWM-HTGDVATLDGmGFIEIRDRIKDVIKTGGewlSSLELEDlISRH----PAVREVAVVgvpdpqwg 481
Cdd:PRK04813 363 EKTAEAFftfDGQPAyHTGDAGYLED-GLLFYQGRIDFQIKLNG---YRIELEE-IEQNlrqsSYVESAVVV-------- 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599119 482 erPF----------ALLVVREGQQLDARGL----KEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRI 542
Cdd:PRK04813 430 --PYnkdhkvqyliAYVVPKEEDFEREFELtkaiKKELK-----ERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
365-550 |
1.06e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 67.62 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 365 AGVPVPLVDAAIMDEQGRFLpaDGESQGELVLRSPWltQGYFR----EPERGEELWR---GGWMHTGDVATLDGMGFIEI 437
Cdd:PLN02654 456 ATFPFFGVQPVIVDEKGKEI--EGECSGYLCVKKSW--PGAFRtlygDHERYETTYFkpfAGYYFSGDGCSRDKDGYYWL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 438 RDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARgLKEHLKPFVeQGNINKW 517
Cdd:PLN02654 532 TGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE-LRKSLILTV-RNQIGAF 609
|
170 180 190
....*....|....*....|....*....|...
gi 15599119 518 AIPSQIAVVTDIPKTSVGKLdKKRIRIEIAQWQ 550
Cdd:PLN02654 610 AAPDKIHWAPGLPKTRSGKI-MRRILRKIASRQ 641
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
195-553 |
1.12e-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: 67.13 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 195 NPKGVYFSHRQLVLHTLAMASTIGSLDSIRLLGtsdvYMPIT-----PMFHVhawgTPYVAtmlGVKQ-VYPGRY---DP 265
Cdd:cd05908 120 DPKGVMLTHENLVHNMFAILNSTEWKTKDRILS----WMPLThdmglIAFHL----APLIA---GMNQyLMPTRLfirRP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 266 ELLVELWKREKVTFSHCvPT----ILQMVMNARAAQGVDFKGWKVIIGGS-----ALNRSLYEAAKARGIQLTA---AYG 333
Cdd:cd05908 189 ILWLKKASEHKATIVSS-PNfgykYFLKTLKPEKANDWDLSSIRMILNGAepidyELCHEFLDHMSKYGLKRNAilpVYG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 334 MSETC----------PLISCAYLNDELLAG-------SEDERTTYRIKAGVPVPLVDAAIMDEQGRFLPADgeSQGELVL 396
Cdd:cd05908 268 LAEASvgaslpkaqsPFKTITLGRRHVTHGepepevdKKDSECLTFVEVGKPIDETDIRICDEDNKILPDG--YIGHIQI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 397 RSPWLTQGYFREPERGEE-LWRGGWMHTGDvatldgMGFIE-----IRDRIKDVIKTGGEWLSSLELEDLISRHPAVR-- 468
Cdd:cd05908 346 RGKNVTPGYYNNPEATAKvFTDDGWLKTGD------LGFIRngrlvITGREKDIIFVNGQNVYPHDIERIAEELEGVElg 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 469 EVAVVGVPDPQWGERPFALLVVREGQQLD----ARGLKEHLKPFveqgniNKWAIpSQIAVVTDIPKTSVGKLDkkriRI 544
Cdd:cd05908 420 RVVACGVNNSNTRNEEIFCFIEHRKSEDDfyplGKKIKKHLNKR------GGWQI-NEVLPIRRIPKTTSGKVK----RY 488
|
....*....
gi 15599119 545 EIAQWQEAG 553
Cdd:cd05908 489 ELAQRYQSG 497
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
46-550 |
2.28e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.12 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 46 YATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVNSEF 125
Cdd:PRK05691 1159 YAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHL 1238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 126 VPLYQAVAGqLATVERTILLTDGAEKSAelPGLvgeyesllaaasprydfpDFDENSIATTFYTTGTTGNPKGVYFSHRQ 205
Cdd:PRK05691 1239 LERLPQAEG-VSAIALDSLHLDSWPSQA--PGL------------------HLHGDNLAYVIYTSGSTGQPKGVGNTHAA 1297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 206 LVLHTLAMASTIGsldsirlLGTSDVYMPITPM-FHVHAWGT--PYVAtmlGVKQVYPG---RYDPELLVELWKREKVTF 279
Cdd:PRK05691 1298 LAERLQWMQATYA-------LDDSDVLMQKAPIsFDVSVWECfwPLIT---GCRLVLAGpgeHRDPQRIAELVQQYGVTT 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 280 SHCVPTILQM-VMNARAAQGVDFKgwKVIIGGSALNRSLYEAAKAR--GIQLTAAYGMSETCplISCAYLNdelLAGSED 356
Cdd:PRK05691 1368 LHFVPPLLQLfIDEPLAAACTSLR--RLFSGGEALPAELRNRVLQRlpQVQLHNRYGPTETA--INVTHWQ---CQAEDG 1440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 357 ERTtyriKAGVPVPLVDAAIMDEQgrFLPADGESQGELVLRSPWLTQGYFREP-------------ERGEELWRggwmhT 423
Cdd:PRK05691 1441 ERS----PIGRPLGNVLCRVLDAE--LNLLPPGVAGELCIGGAGLARGYLGRPaltaerfvpdplgEDGARLYR-----T 1509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 424 GDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREvAVVGVPDPQWGERPFALLVVREGQQLDARGLKE 503
Cdd:PRK05691 1510 GDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQ-AAVLVREGAAGAQLVGYYTGEAGQEAEAERLKA 1588
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15599119 504 HLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKriRIEIAQWQ 550
Cdd:PRK05691 1589 ALA-----AELPEYMVPAQLIRLDQMPLGPSGKLDRR--ALPEPVWQ 1628
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
36-542 |
1.07e-10 |
|
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: 63.96 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQvRYSYATFNERVARLAN-VLSEAGVKAGDTVA-VMDwDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNH 113
Cdd:cd17648 6 VVYGDK-RLTYRELNERANRLAHyLLSVAEIRPDDLVGlVLD-KSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 114 AEDRFVLVNSEfvplyqavagQLATvertILLTDGAeksaelpglvgeyesllaaasprydfpdfdensiattfyttgtT 193
Cdd:cd17648 84 TGARVVITNST----------DLAY----AIYTSGT-------------------------------------------T 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 194 GNPKGVYFSHRQLVlhtlamaSTIGSLdsirllgtSDVYMPITPMFHVHAWGTPYV----------ATMLGVKQVYP--- 260
Cdd:cd17648 107 GKPKGVLVEHGSVV-------NLRTSL--------SERYFGRDNGDEAVLFFSNYVfdffveqmtlALLNGQKLVVPpde 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 261 GRYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQgvdFKgwKVIIGGSALNRSLYEAAKAR-GIQLTAAYGMSETcp 339
Cdd:cd17648 172 MRFDPDRFYAYINREKVTYLSGTPSVLQQYDLARLPH---LK--RVDAAGEEFTAPVFEKLRSRfAGLIINAYGPTET-- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 340 liSCAYLNDELLAGSEDERTTyrikaGVPVPLVDAAIMDEQGRFLPADGesQGELVLRSPWLTQGYFREPE--------- 410
Cdd:cd17648 245 --TVTNHKRFFPGDQRFDKSL-----GRPVRNTKCYVLNDAMKRVPVGA--VGELYLGGDGVARGYLNRPEltaerflpn 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 411 -----------RGEELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQ 479
Cdd:cd17648 316 pfqteqerargRNARLYK-----TGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAS 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599119 480 WGERPFA-LLV---VREGQQLDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRI 542
Cdd:cd17648 391 QAQSRIQkYLVgyyLPEPGHVPESDLLSFLR-----AKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
44-474 |
2.82e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 62.94 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNE---RVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVL 120
Cdd:PLN02861 75 YVWLTYKEvydAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 121 VNSEFVPLYQAVAGQLATVERTIL----LTDGAEKSAELPGL-VGEYESLLAAASPRYDFPDFDENSIATTFYTTGTTGN 195
Cdd:PLN02861 155 VQESKISSILSCLPKCSSNLKTIVsfgdVSSEQKEEAEELGVsCFSWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGSLDsiRLLGTSDVYMPITPMFHVHA----------------WGTPYVATM------- 252
Cdd:PLN02861 235 PKGVILTNRAIIAEVLSTDHLLKVTD--RVATEEDSYFSYLPLAHVYDqvietyciskgasigfWQGDIRYLMedvqalk 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 253 ----LGVKQVYPGRY------------------DPELLVELWKREKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGG 310
Cdd:PLN02861 313 ptifCGVPRVYDRIYtgimqkissggmlrkklfDFAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVRLLLSGA 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 311 SALNRSLYEAAKARGIQ-LTAAYGMSETCPLISCAYLNDELLAGSederttyrikAGVPVPLVDAAI--MDEQGRflpaD 387
Cdd:PLN02861 393 APLPRHVEEFLRVTSCSvLSQGYGLTESCGGCFTSIANVFSMVGT----------VGVPMTTIEARLesVPEMGY----D 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 388 GES---QGELVLRSPWLTQGYFREPERGEELWRGGWMHTGDVATLDGMGFIEIRDRIKDVIK-TGGEWLSSLELEDLISR 463
Cdd:PLN02861 459 ALSdvpRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAVENLENTYSR 538
|
490
....*....|.
gi 15599119 464 HPAVREVAVVG 474
Cdd:PLN02861 539 CPLIASIWVYG 549
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
196-540 |
4.34e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.88 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 196 PKGVYFSHRQLVLHTLAMASTIGsldsirlLGTSDVYMPITPMFHVHAWGTPYVATMLGVKQVY--PGRYDPELLVELWK 273
Cdd:PRK05691 2348 PKGVVVSHGEIAMHCQAVIERFG-------MRADDCELHFYSINFDAASERLLVPLLCGARVVLraQGQWGAEEICQLIR 2420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 274 REKVTFSHCVPTILQMVMNARAAQGVDFKGWKVIIGGSALNRSLYEAAKA--RGIQLTAAYGMSETC--PLISCAylNDE 349
Cdd:PRK05691 2421 EQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQafAPQLFFNAYGPTETVvmPLACLA--PEQ 2498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 350 LLAGSederttyrikAGVPVPLV----DAAIMDEQGRFLPADGesQGELVLRSPWLTQGYFREP----ER---------G 412
Cdd:PRK05691 2499 LEEGA----------ASVPIGRVvgarVAYILDADLALVPQGA--TGELYVGGAGLAQGYHDRPgltaERfvadpfaadG 2566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 413 EELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQwGERPFALLVVRE 492
Cdd:PRK05691 2567 GRLYR-----TGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPS-GKQLAGYLVSAV 2640
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15599119 493 GQQLDAR--GLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:PRK05691 2641 AGQDDEAqaALREALKAHLKQ-QLPDYMVPAHLILLDSLPLTANGKLDRR 2689
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
36-547 |
6.70e-10 |
|
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: 61.90 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 36 IVYRDQVR--YSYATFNERVARLANVLSEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTInirlSPEqilYTMNH 113
Cdd:cd05943 89 YAAEDGERteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSC----SPD---FGVPG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 114 AEDRFVLVNSEF---VPLY-------------QAVAGQLATVERTILLTD-GAEKSAELPGL--VGEYESLLA---AASP 171
Cdd:cd05943 162 VLDRFGQIEPKVlfaVDAYtyngkrhdvrekvAELVKGLPSLLAVVVVPYtVAAGQPDLSKIakALTLEDFLAtgaAGEL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 172 RYDFPDFDE------NSIATTFyttgttgnPKGVYFSH--------RQLVLHTlamastigslDsirlLGTSDVYMPITP 237
Cdd:cd05943 242 EFEPLPFDHplyilySSGTTGL--------PKCIVHGAggtllqhlKEHILHC----------D----LRPGDRLFYYTT 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 238 ----MFHVHAWGTPYVATMLgvkqVY---PGRYDPELLVELWKREKVTFSHCVPTILQMVMNARAAQG--VDFKGWKVI- 307
Cdd:cd05943 300 cgwmMWNWLVSGLAVGATIV----LYdgsPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAetHDLSSLRTIl 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 308 IGGSALNRS----LYEAAKARgIQLTAAYGMSEtcpLISCAYLNDELLAgsedertTYRIKAGVPVPLVDAAIMDEQGRf 383
Cdd:cd05943 376 STGSPLKPEsfdyVYDHIKPD-VLLASISGGTD---IISCFVGGNPLLP-------VYRGEIQCRGLGMAVEAFDEEGK- 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 384 lPADGESqGELVLRSPWLTQG-YFREPERGE-------ELWRGGWMHtGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSL 455
Cdd:cd05943 444 -PVWGEK-GELVCTKPFPSMPvGFWNDPDGSryraayfAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTA 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 456 ELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLDARgLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVG 535
Cdd:cd05943 521 EIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDE-LRKRIRSTIRS-ALSPRHVPAKIIAVPDIPRTLSG 598
|
570
....*....|..
gi 15599119 536 KldkkriRIEIA 547
Cdd:cd05943 599 K------KVEVA 604
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
373-508 |
9.37e-10 |
|
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: 61.15 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 373 DAAIMDEQGRFLPADGESQGELVLR----SPWLtqGYFREPERGEE------LWRGG-WMHTGDVATLDGMGFIEIRDRI 441
Cdd:cd05938 331 EEPVRDAQGFCIPVAKGEPGLLVAKitqqSPFL--GYAGDKEQTEKkllrdvFKKGDvYFNTGDLLVQDQQNFLYFHDRV 408
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599119 442 KDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQW-GERPFALLVVREGQQLDARGLKEHLKPF 508
Cdd:cd05938 409 GDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHeGRIGMAAVKLKPGHEFDGKKLYQHVREY 476
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
389-467 |
1.84e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 60.38 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 389 ESQGELVLRSPWLTQGYFREPERGEE-LWRGGWMHTGDVATLDGMGFIEIRDRIKDVIKTG-GEWLSSLELEDLISRHPA 466
Cdd:PTZ00216 505 EPRGEILLRGPFLFKGYYKQEELTREvLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNClGEYIALEALEALYGQNEL 584
|
.
gi 15599119 467 V 467
Cdd:PTZ00216 585 V 585
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
44-545 |
4.63e-09 |
|
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: 58.60 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 44 YSYATFNERVARLANVL-SEAGVKAGDTVAVMDWDSHRYLECMFAIPMIGAVLHTINIRLSPEQILYTMNHAEDRFVLVN 122
Cdd:cd05937 6 WTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 123 SEFVPLYQAVAGqlatvertillTDGAEKSA------ELPG-------LVGEYESLLAAASPRYDFPDFDENSIATTFYT 189
Cdd:cd05937 86 PDDPAILIYTSG-----------TTGLPKAAaiswrrTLVTsnllshdLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 190 TGTTGNPKgvyFSHRQLVLHTLAMASTIgsldsIRLLGTSDVYMPITPMfhvhawgTPYvATMLGVKQVYPGRYDPELlv 269
Cdd:cd05937 155 GTLALSRK---FSASQFWKDVRDSGATI-----IQYVGELCRYLLSTPP-------SPY-DRDHKVRVAWGNGLRPDI-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 270 elWKREKVTFShcVPTILQMVmnaRAAQGVdfkgwkviigGSALNRSlyeaAKARGIQLTAAYGmsetcPLISCAYLNDE 349
Cdd:cd05937 217 --WERFRERFN--VPEIGEFY---AATEGV----------FALTNHN----VGDFGAGAIGHHG-----LIRRWKFENQV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 350 LLA--GSEDERTTYRIKAG--VPVPLvdaaimdeqgrflpadgESQGELVLRSPWLT----QGYFR-----EPERGEELW 416
Cdd:cd05937 271 VLVkmDPETDDPIRDPKTGfcVRAPV-----------------GEPGEMLGRVPFKNreafQGYLHnedatESKLVRDVF 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 417 RGG--WMHTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQW-GERPFALLVVREG 493
Cdd:cd05937 334 RKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGRAGCAAITLEES 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599119 494 QQ----LDARGLKEHLKpfveqGNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIE 545
Cdd:cd05937 414 SAvpteFTKSLLASLAR-----KNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
422-540 |
1.12e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 57.35 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 422 HTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGqqLDARGL 501
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEE--IDPVQL 371
|
90 100 110
....*....|....*....|....*....|....*....
gi 15599119 502 KEHLkpfveQGNINKWAIPSQIAVVTDIPKTSVGKLDKK 540
Cdd:PRK08308 372 REWC-----IQHLAPYQVPHEIESVTEIPKNANGKVSRK 405
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
376-548 |
2.16e-08 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 57.01 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 376 IMDEQGRFLPADGESQGELVL------RSPWLTQG-----YFrepeRGEELWRGGWM--HtGDVATLDGMGFIEIRDRIK 442
Cdd:PLN03052 538 ILDDSGNPYPDDAPCTGELALfplmfgASSTLLNAdhykvYF----KGMPVFNGKILrrH-GDIFERTSGGYYRAHGRAD 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 443 DVIKTGGEWLSSLELEDLISR-HPAVREVAVVGVPDPQWGERPFALLVV---REGQQLDARGLKEHLKPFVeQGNINKWA 518
Cdd:PLN03052 613 DTMNLGGIKVSSVEIERVCNAaDESVLETAAIGVPPPGGGPEQLVIAAVlkdPPGSNPDLNELKKIFNSAI-QKKLNPLF 691
|
170 180 190
....*....|....*....|....*....|
gi 15599119 519 IPSQIAVVTDIPKTSVGKLDKKRIRIEIAQ 548
Cdd:PLN03052 692 KVSAVVIVPSFPRTASNKVMRRVLRQQLAQ 721
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
276-549 |
1.28e-07 |
|
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: 54.09 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 276 KVTFSHCVPTIlqmvmnARAAQGVDFKGWKVII-GGSALNRSLYEAAkARGIQLTAAYGMSETCplISCAylndelLAGS 354
Cdd:cd05918 195 RVTWAFLTPSV------ARLLDPEDVPSLRTLVlGGEALTQSDVDTW-ADRVRLINAYGPAECT--IAAT------VSPV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 355 EDERTTYRIkaGVPVP----LVDAaimDEQGRFLPADGEsqGELVLRSPWLTQGYFREPER-------------GEELWR 417
Cdd:cd05918 260 VPSTDPRNI--GRPLGatcwVVDP---DNHDRLVPIGAV--GELLIEGPILARGYLNDPEKtaaafiedpawlkQEGSGR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 418 GGWM-HTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGV---PDPQWGERPFALLVVRE- 492
Cdd:cd05918 333 GRRLyRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGs 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599119 493 ------GQQL------DARGLKEHLKPFVEQgNINKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQW 549
Cdd:cd05918 413 ssgsgdGDSLflepsdEFRALVAELRSKLRQ-RLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESL 480
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
263-551 |
1.33e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.71 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 263 YDPELLVELWKREKVTFSHCVPTILQMvMNARAAQGVDFKGWkVIIGGSALNRSLYEAAKAR--GIQLTAAYGMSEtCPL 340
Cdd:PRK05691 3947 HDPQGLLAHVQAQGITVLESVPSLIQG-MLAEDRQALDGLRW-MLPTGEAMPPELARQWLQRypQIGLVNAYGPAE-CSD 4023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 341 ISCAYLNDEllagsEDERTTYrIKAGVPVPLVDAAIMDEQGRFLPADgeSQGELVLRSPWLTQGYFREPER--------- 411
Cdd:PRK05691 4024 DVAFFRVDL-----ASTRGSY-LPIGSPTDNNRLYLLDEALELVPLG--AVGELCVAGTGVGRGYVGDPLRtalafvphp 4095
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 412 ----GEELWRggwmhTGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREvAVVGVPDPQWGERPFAL 487
Cdd:PRK05691 4096 fgapGERLYR-----TGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGY 4169
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599119 488 LVVREGQQLDARgLKEHLKPFVeQGNINKWAIPSQIAVVTDIPKTSVGKLDKKRI-RIEIAQWQE 551
Cdd:PRK05691 4170 LVPHQTVLAQGA-LLERIKQRL-RAELPDYMVPLHWLWLDRLPLNANGKLDRKALpALDIGQLQS 4232
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
423-545 |
1.76e-06 |
|
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: 50.50 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 423 TGDVATLDGMGFIEIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERP--FALLVVREGQQLD--A 498
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAgmAAIVDPERKVDLDrfS 432
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15599119 499 RGLKEHLKPFveqgninkwAIPSQIAVVTDIPKTSVGKLDKKRIRIE 545
Cdd:cd05939 433 AVLAKSLPPY---------ARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
328-555 |
3.45e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 49.76 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 328 LTAAYGMSE-TC----PLISCAYLNDELLAGSEDERTTYRIkAGVPVPLVDAAIMDEQGRfLPADGESQGELVLRSPWLT 402
Cdd:PRK05851 306 AAPSYGLAEsTCavtvPVPGIGLRVDEVTTDDGSGARRHAV-LGNPIPGMEVRISPGDGA-AGVAGREIGEIEIRGASMM 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 403 QGYFREPErgeeLWRGGWMHTGDVATLDGMGFIeIRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGE 482
Cdd:PRK05851 384 SGYLGQAP----IDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSA 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599119 483 RPfALLVVREGQQLDARGLKEHLkpfVEQGNINKWAIPSQIAVVT--DIPKTSVGKLDkkriRIEIAQWQEAGSA 555
Cdd:PRK05851 459 RP-GLVIAAEFRGPDEAGARSEV---VQRVASECGVVPSDVVFVApgSLPRTSSGKLR----RLAVKRSLEAADG 525
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
372-537 |
3.84e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 46.71 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 372 VDAAIMDEQGRflPADGEsQGELVLRSP--------W-------LTQGYFrepergeELWRGGWMHtGDVATLDGMGFIE 436
Cdd:PRK03584 447 MAVEAWDEDGR--PVVGE-VGELVCTKPfpsmplgfWndpdgsrYRDAYF-------DTFPGVWRH-GDWIEITEHGGVV 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 437 IRDRIKDVIKTGGEWLSSLELEDLISRHPAVREVAVVGVPDPQWGERPFALLVVREGQQLD-------ARGLKEHLKP-F 508
Cdd:PRK03584 516 IYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDdalrariRTTIRTNLSPrH 595
|
170 180
....*....|....*....|....*....
gi 15599119 509 VeqgninkwaiPSQIAVVTDIPKTSVGKL 537
Cdd:PRK03584 596 V----------PDKIIAVPDIPRTLSGKK 614
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
176-445 |
8.69e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 45.49 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 176 PDFDENSIATTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGSLDSIRllGTSDVympitPMFHVHAWGTPYVATMLG- 254
Cdd:PRK07769 175 PEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDR--GVSWL-----PFFHDMGLITVLLPALLGh 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 255 ----------VKQvyPGRYDPELLVELWKREKV-------TFSHCvptilqmvmnarAAQGV--------DFKGWKVIIG 309
Cdd:PRK07769 248 yitfmspaafVRR--PGRWIRELARKPGGTGGTfsaapnfAFEHA------------AARGLpkdgepplDLSNVKGLLN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 310 GS-----ALNRSLYEAAKARGIQLTA---AYGMSETCPLISCAYLNDE--LLAGSEDERTTYRI---KAGVP--VPLVD- 373
Cdd:PRK07769 314 GSepvspASMRKFNEAFAPYGLPPTAikpSYGMAEATLFVSTTPMDEEptVIYVDRDELNAGRFvevPADAPnaVAQVSa 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 374 --------AAIMD-EQGRFLPaDGESqGELVLRSPWLTQGYFREPERGEELWR------------------GGWMHTGDV 426
Cdd:PRK07769 394 gkvgvsewAVIVDpETASELP-DGQI-GEIWLHGNNIGTGYWGKPEETAATFQnilksrlseshaegapddALWVRTGDY 471
|
330 340
....*....|....*....|
gi 15599119 427 AT-LDGMGFIEirDRIKDVI 445
Cdd:PRK07769 472 GVyFDGELYIT--GRVKDLV 489
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
375-548 |
3.37e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 43.27 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 375 AIMDEQGRFLPADGESQGELVLRSPWL-----------TQGYF----REPERGEELWRggwmHTGDVATLDGMGFIEIRd 439
Cdd:PLN03051 303 VLLNDNGVPYPDDQPCVGEVALAPPMLgasdrllnadhDKVYYkgmpMYGSKGMPLRR----HGDIMKRTPGGYFCVQG- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 440 RIKDVIKTGGEWLSSLELEDLISR-HPAVREVAVVGVPDPQWGERPFALLVVR--EGQQLDARGLKEHLKPFVE--QGNI 514
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPELLVIFLVLgeEKKGFDQARPEALQKKFQEaiQTNL 457
|
170 180 190
....*....|....*....|....*....|....
gi 15599119 515 NKWAIPSQIAVVTDIPKTSVGKLDKKRIRIEIAQ 548
Cdd:PLN03051 458 NPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKK 491
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
309-411 |
3.80e-04 |
|
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: 43.19 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 309 GGSALNRSLYEAAKA-------RGIQLTAAYGMSETCPLIS-CAYLNdellagsedERTTYrikAGVPVPLVDAaimdeq 380
Cdd:cd05921 298 AGAGLSQDVWDRLQAlavatvgERIPMMAGLGATETAPTATfTHWPT---------ERSGL---IGLPAPGTEL------ 359
|
90 100 110
....*....|....*....|....*....|.
gi 15599119 381 gRFLPADGESqgELVLRSPWLTQGYFREPER 411
Cdd:cd05921 360 -KLVPSGGKY--EVRVKGPNVTPGYWRQPEL 387
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
309-429 |
1.62e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 41.40 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 309 GGSALNRSLYE-----AAKARG--IQLTAAYGMSETCPL-ISCAYLNDelLAGSederttyrikAGVPVPLVDAaimdeq 380
Cdd:PRK08180 342 AGAALSQDVWDrldrvAEATCGerIRMMTGLGMTETAPSaTFTTGPLS--RAGN----------IGLPAPGCEV------ 403
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15599119 381 gRFLPADGESqgELVLRSPWLTQGYFREPER-----GEElwrgGWMHTGDVATL 429
Cdd:PRK08180 404 -KLVPVGGKL--EVRVKGPNVTPGYWRAPELtaeafDEE----GYYRSGDAVRF 450
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
309-490 |
2.14e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 40.80 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 309 GGSALNRSLYE-----AAKARG--IQLTAAYGMSETCPLISCAYLNDELLAgsederttyriKAGVPVPLVdaaimdeQG 381
Cdd:PRK12582 354 GGATLSDDLYErmqalAVRTTGhrIPFYTGYGATETAPTTTGTHWDTERVG-----------LIGLPLPGV-------EL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 382 RFLPADgeSQGELVLRSPWLTQGYFREPERGEELW-RGGWMHTGDVATldgmgFIEIRDRIKDVIKTG----------GE 450
Cdd:PRK12582 416 KLAPVG--DKYEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAAR-----FVDPDDPEKGLIFDGrvaedfklstGT 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15599119 451 WLS--SLELEDLISRHPAVREVAVVGVpdpqwgERPFALLVV 490
Cdd:PRK12582 489 WVSvgTLRPDAVAACSPVIHDAVVAGQ------DRAFIGLLA 524
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
105-547 |
6.73e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 39.77 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 105 EQILYTMNHAEDRFVLVNSEFVPLYQAVagqlatvertilltdGAEKSAELPGLVGeYESLLAAASPRYDFPDFDENSIA 184
Cdd:PRK05691 106 ERLLSIIADAEPRLLLTVADLRDSLLQM---------------EELAAANAPELLC-VDTLDPALAEAWQEPALQPDDIA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 185 TTFYTTGTTGNPKGVYFSHRQLVLHTLAMASTIGsLDsirlLGTSDVYMPITPMFHVHAW----------GTPYVatmLG 254
Cdd:PRK05691 170 FLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFG-ID----LNPDDVIVSWLPLYHDMGLiggllqpifsGVPCV---LM 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 255 VKQVYPGRydPELLVELWKREKVTFSHCvPTILQMVMNAR----AAQGVDFKGWKVIIGGSALNR--SL------YEAAK 322
Cdd:PRK05691 242 SPAYFLER--PLRWLEAISEYGGTISGG-PDFAYRLCSERvsesALERLDLSRWRVAYSGSEPIRqdSLerfaekFAACG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 323 ARGIQLTAAYGMSETCPL---------ISCAYLNDELLAGSEDERTTYR--IKAGVPVPLVDAAIMDEQGRFLPADGESq 391
Cdd:PRK05691 319 FDPDSFFASYGLAEATLFvsggrrgqgIPALELDAEALARNRAEPGTGSvlMSCGRSQPGHAVLIVDPQSLEVLGDNRV- 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 392 GELVLRSPWLTQGYFREPERGEELW--RGG--WMHTGDVATL-DGMGFIEirDRIKDVIKTGGEWLSSLELEDLISRH-P 465
Cdd:PRK05691 398 GEIWASGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDLGFLrDGELFVT--GRLKDMLIVRGHNLYPQDIEKTVEREvE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599119 466 AVRE--VAVVGVPDPqwGErpfallvvrEGQQLDA---RGLKEHLKPFVEQGNINKWA------IPSQIAVVTD--IPKT 532
Cdd:PRK05691 476 VVRKgrVAAFAVNHQ--GE---------EGIGIAAeisRSVQKILPPQALIKSIRQAVaeacqeAPSVVLLLNPgaLPKT 544
|
490
....*....|....*
gi 15599119 533 SVGKLDKKRIRIEIA 547
Cdd:PRK05691 545 SSGKLQRSACRLRLA 559
|
|
| |
