|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
12-360 |
0e+00 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 585.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------- 66
Cdd:PRK08256 1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYgdstsgqralyevgmtgipivnvnn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 67 ------------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHME 128
Cdd:PRK08256 79 ncstgstalflarqavrsGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 129 KYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKAV 208
Cdd:PRK08256 159 KYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 209 EILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVD 288
Cdd:PRK08256 238 EIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFID 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302344762 289 RGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLYK 360
Cdd:PRK08256 318 DGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLGGACVVTLYQ 389
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
17-359 |
1.36e-168 |
|
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238422 [Multi-domain] Cd Length: 393 Bit Score: 481.61 E-value: 1.36e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 17 VGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYS----AVDQACVGYVF-------------------------- 66
Cdd:cd00826 1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLgagegqncaqqaamhagglqeapaig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 67 ---------------------GVAECVLALGFEKMSkgslgikFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKE 125
Cdd:cd00826 81 mnnlcgsglralalamqliagGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 126 HMEKYGTKIEHFAKIGWKN---HKHSVNNPYSQFQDEYSLDEVMASKEVFD---FLTILQCCPTSDGAAAAILASEAFVQ 199
Cdd:cd00826 154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 200 KYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCP 279
Cdd:cd00826 234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 280 EGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLY 359
Cdd:cd00826 314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQGAGAGLALLCIGGGGGAAMCIES 393
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
17-359 |
7.07e-126 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 371.98 E-value: 7.07e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 17 VGVGMTKFVKPGaenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------------ 66
Cdd:cd00829 1 VGVGMTPFGRRS---DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAggrfqsfpgaliaeylgllgkpatrveaag 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 67 ----------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLInkYGLSAhpvaPQMFGYAGKEHMEKY 130
Cdd:cd00829 78 asgsaavraaaaaiasGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPP--GGLTP----PALYALAARRYMHRY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 131 GTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqsKAVEI 210
Cdd:cd00829 152 GTTREDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTD--RPVWI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 211 LAQEMMTDLPSSFEEKSiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRG 290
Cdd:cd00829 230 LGVGAASDTPSLSERDD---FLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREG 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302344762 291 DNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLY 359
Cdd:cd00829 307 DTAIGGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGTGSAAVVTI 375
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
11-359 |
6.54e-82 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 259.44 E-value: 6.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 11 LRRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQ-------------------------------------IP 53
Cdd:PRK06064 1 MRDVAIIGVGQTKF---GELWDVSLRDLAVEAGLEALEDAGidgkdidamyvgnmsaglfvsqehiaaliadyaglapIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 54 YSAVDQAC--------VGYVF---GVAECVLALGFEKMSKgslgikfsdrtIPTDKHVDLLI--------NKYGLSAhpv 114
Cdd:PRK06064 78 ATRVEAACasggaalrQAYLAvasGEADVVLAAGVEKMTD-----------VPTPDATEAIAragdyeweEFFGATF--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 115 aPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILAS 194
Cdd:PRK06064 144 -PGLYALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILAS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 195 EAFVQKYglQSKAVEILAQEMMTDLPSSFEEKSIikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 274
Cdd:PRK06064 223 EEKAKEY--TDTPVWIKASGQASDTIALHDRKDF---TTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYED 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 275 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEA--GKRQVPGAKVALQHNL-GIG 351
Cdd:PRK06064 298 LGFAKKGEGGKLAREGQTYIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAekGRQQVIGAGYGLTHNVgGTG 377
|
....*...
gi 302344762 352 GAVVVTLY 359
Cdd:PRK06064 378 HTAVVHIL 385
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
12-349 |
3.86e-59 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 200.07 E-value: 3.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYV-------------------------- 65
Cdd:PRK12578 1 RRVAVIGVGNSKF---GRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTayrgielypapivaeysgltgkvplr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 66 --------------------FGVAECVLALGFEKMSK----GSLGIKFSDRTIPTDKHvdllinKYGLSAhpvaPQMFGY 121
Cdd:PRK12578 78 veamcatglaasltaytavaSGLVDMAIAVGVDKMTEvdtsTSLAIGGRGGNYQWEYH------FYGTTF----PTYYAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK12578 148 YATRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 202 GLQSkAVEILAQEMMTDLpSSFEEKsiIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEG 281
Cdd:PRK12578 228 KIDS-PVWITGIGYANDY-AYVARR--GEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKG 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302344762 282 QGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAK-VALQHNLG 349
Cdd:PRK12578 304 KGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKLQQPLKKyIGLVHNVG 372
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
10-357 |
1.22e-53 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 185.74 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 10 TLRRVFVVGVGMTKFVKPGaensRDYPDLAEEAGKKALADAQIPYSAVdQACV----------GYVF------------- 66
Cdd:PRK06059 2 MPEPVYILGAGMHPWGKWG----RDFVEYGVVAARAALADAGLDWRDV-QLVVgadtirngypGFVAgatfaqalgwnga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 67 -------------------------GVAECVLALGFEKMSKGSLGIKFSDRtiPTDKhvDLLINKYGLSAHPVapqMFGY 121
Cdd:PRK06059 77 pvsssyaacasgsqalqsaraqilaGLCDVALVVGADTTPKGFFAPVGGER--PDDP--DWLRFHLIGATNPV---YFAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK06059 150 LARRRMDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSFARRH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 202 GLQSK-AVEILAQEMMT--------DLPSsFEEKSIIKMVGFDMS--KEAARKCYEKSGLTPNDIDVIELHDCFSTNELL 270
Cdd:PRK06059 230 LGSVAgVPSVRAISTVTprypqhlpELPD-IATDSTAAVPAPERVfkDQILDAAYAEAGIGPEDLSLAEVYDLSTALELD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 271 TYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGI 350
Cdd:PRK06059 309 WYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAGGRQVEGARVGITANQGL 388
|
410
....*....|
gi 302344762 351 ---GGAVVVT 357
Cdd:PRK06059 389 fghGSSVIVA 398
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
13-354 |
2.28e-48 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 171.28 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 13 RVFVVGVGMTKFVKPGAEnsrDYPDLAEEAGKKALADAQIPYSAVDQACVGyVF-------------------------- 66
Cdd:PRK07516 3 TASIVGWAHTPFGKLDAE---TLESLIVRVAREALAHAGIAAGDVDGIFLG-HFnagfspqdfpaslvlqadpalrfkpa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 67 -----------------------GVAECVLALGFEKMSkgslgikfsdrTIPTDKHVDLLIN-KYGLSAHPVA---PQMF 119
Cdd:PRK07516 79 trvenacatgsaavyaaldaieaGRARIVLVVGAEKMT-----------ATPTAEVGDILLGaSYLKEEGDTPggfAGVF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 120 GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKE----VFDFLTILQCCPTSDGAAAAILASE 195
Cdd:PRK07516 148 GRIAQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEFCRTVSEknplVAGPLRRTDCSLVSDGAAALVLADA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 196 AFVQKYglqSKAVEILAQEMMTD-LPSSFEEksiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 274
Cdd:PRK07516 228 ETARAL---QRAVRFRARAHVNDfLPLSRRD-----PLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 275 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGiGGAV 354
Cdd:PRK07516 300 MGLAPPGQGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAGGMQIPGAKLAGVFNMG-GAAV 378
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
12-349 |
3.52e-47 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 168.28 E-value: 3.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQI-----------------------------------PYSA 56
Cdd:PRK06157 7 DKVAILGMGCTKF---GERWDAGAEDLMVEAFLEALADAGIepkdidaawfgthydeigsgksgtplsralrlpniPVTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 57 VDQACV-------GYVFGVA----ECVLALGFEK-MSKGSLGIKFSDRTIPTDkhvdllinkyGLSAHPVAPQMFGYAGK 124
Cdd:PRK06157 84 VENFCAtgseafrGAVYAVAsgayDIALALGVEKlKDTGYGGLPVANPGTLAD----------MTMPNVTAPGNFAQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 125 EHMEKYGTKIEHF----AKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQK 200
Cdd:PRK06157 154 AYAAKYGVSREDLkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 201 YG----LQSKAVEILA---QEMMTDL--PSSFEEKSIikmvgfdmskeAARKCYEKSGLT-P-NDIDVIELHDCFSTNEL 269
Cdd:PRK06157 234 LGkkdpVYVKALQLAVsngWELQYNGwdGSYFPTTRI-----------AARKAYREAGITdPrEELSMAEVHDCFSITEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 270 LTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLG 349
Cdd:PRK06157 303 VTMEDLGLSERGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQLKNPRLALTHNLG 382
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
8-360 |
7.79e-43 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 157.38 E-value: 7.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 8 PATLRRVFVVGVGMTKFVKpgAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGY----------------------- 64
Cdd:PRK06365 12 KKKSRDVYMVAAGVTKFDK--ASPYMDFRERVKKAFDYAMNDAGLTLADIDGSVASYfsdhfqrqllagimvqdylglvp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 65 ------------------------VFGVAECVLALGFEKMSKgslgikfsdrtIPTDKHvdlliNKY-GLSA-----HPV 114
Cdd:PRK06365 90 kpskriegggatgglafqagyeeiASGRMDCVAVYGFETMSH-----------VNTWKG-----NEFiALASdtnfdYPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 115 APQMFGY---AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAI 191
Cdd:PRK06365 154 GGFYTGYyamMAVRHMYEFGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 192 LASEAfvQKYGLQSKAVEILAQEMMTD--------------LPSsfEEKSIIK------MVGFDMSKEAARKCYEKSGLT 251
Cdd:PRK06365 234 LASED--KAFEITDKPVLIKAIGTGSDtlrladrpfgevplLPN--ESPDDYKdlrypgVHSFRAGRMAAKEAYEMAGIT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 252 P--NDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLR 329
Cdd:PRK06365 310 DplNDLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQ 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 302344762 330 GEAGKR------QVPGAKVALQH-NLGIGGAVVVTLYK 360
Cdd:PRK06365 390 GRIKKHfhddylQVKNAKRGLIHsHAGTGTYVTVTILE 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
181-357 |
5.92e-37 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 136.80 E-value: 5.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 181 CPTSDGAAAAILASEAFVQKYGLQskaveilAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIEL 260
Cdd:cd00327 98 FVFGDGAAAAVVESEEHALRRGAH-------PQAEIVSTAATFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 261 HDCFSTNELLTYEALGLCPEGQGAtlvdrgdntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGK--RQVP 338
Cdd:cd00327 171 HGTGTPIGDAVELALGLDPDGVRS---------------PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPptPREP 235
|
170
....*....|....*....
gi 302344762 339 GAKVALQHNLGIGGAVVVT 357
Cdd:cd00327 236 RTVLLLGFGLGGTNAAVVL 254
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
14-357 |
9.97e-36 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 137.13 E-value: 9.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 14 VFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFG-------------------------- 67
Cdd:PRK06289 5 VWVLGGYQSDFARNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGelfagqghlgampatvhpalwgvpas 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 68 ----------VA-------------ECVLALGFEKMskgslgikfsdRTIPTDKHVDLL-----INKYGLSAHPVAPQMF 119
Cdd:PRK06289 85 rheaacasgsVAtlaamadlragryDVALVVGVELM-----------KTVPGDVAAEHLgaaawTGHEGQDARFPWPSMF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 120 GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-----FQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILAS 194
Cdd:PRK06289 154 ARVADEYDRRYGLDEEHLRAIAEINFANARRNPNAQtrgwaFPDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLAS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 195 EAFVQKYGLQSKAVEILAQEMMTdLPSSFEEKsIIKMVG----FDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELL 270
Cdd:PRK06289 234 DAYLRDYADARPIPRIKGWGHRT-APLGLEQK-LDRSAGdpyvLPHVRQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 271 TYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALqhNLGI 350
Cdd:PRK06289 312 AIDHIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDYQVEGAKTFG--TLNI 389
|
....*..
gi 302344762 351 GGAVVVT 357
Cdd:PRK06289 390 GGSTTTT 396
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
12-362 |
1.06e-35 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 136.78 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 12 RRVFVVGVGMTKFVKPGAENSrdYPDLAEEAGKKALADAQIPYSAVD--------------------------------- 58
Cdd:PRK08313 3 RLAAVLGTGQTKYVAKRQDVS--MAGLVREAIDRALADAGLTWDDIDavvvgkapdffegvmmpelfladalgatgkpli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 59 -----------QACVGYVF---GVAECVLALGFEKMSKGSLGIKFSdrtIPTDKHVDLLINKYGLSAHPVApqmfgyagk 124
Cdd:PRK08313 81 rvhtagsvggsTAVVAASLvqsGVYRRVLAVAWEKQSESNAMWALS---IPVPFTKPVGAGAGGYFAPHVR--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 125 EHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQF-QDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGL 203
Cdd:PRK08313 149 AYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLhQPDITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 204 QSKAVeILAQEMMTDlPSSFEEKSIIKMVGfdmSKEAARKCYEKSGLT-P-NDIDVIELHDCFSTNELLTYEALGLCPEG 281
Cdd:PRK08313 229 RPVAW-IHGTAMRTE-PLAFAGRDQVNPQA---GRDAAAALWKAAGITdPrDEIDVAEIYVPFSWFEPMWLENLGFAPEG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 282 QGATLVDRGDNTYGGKWVINPSGGLISkGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGiGGAVVVTLYKM 361
Cdd:PRK08313 304 EGWKLTEAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKAGEHQVDGARKALGHAYG-GGSQFFSMWVV 381
|
.
gi 302344762 362 G 362
Cdd:PRK08313 382 G 382
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
113-352 |
2.19e-34 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 133.23 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 113 PVAPqMFGYA--GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAA 190
Cdd:PRK06158 137 PVNP-VSAYAlaAARHMHQYGTTREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 191 ILASEAFVQkyGLQSKAVEILAQEMMTDlpssfeEKSIIKMVgfDMSKEAA----RKCYEKSGLTPNDIDVIELHDCFST 266
Cdd:PRK06158 216 VMVRADRAR--DLPRPPVYVLGAAAATW------HRQISSMP--DLTVTAAaesgPRAFAMAGLTPADIDVVELYDAFTI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 267 NELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPlGATGLAQCAELCWQLRGEAGKRQVPGAKVALQH 346
Cdd:PRK06158 286 NTILFLEDLGFCAKGEGGAFVEGGRIAPGGRLPVNTNGGGLSCVHP-GMYGLFLLIEAVRQLRGEAGERQVAGAEVALAH 364
|
....*.
gi 302344762 347 nlGIGG 352
Cdd:PRK06158 365 --GNGG 368
|
|
| SCP2 |
pfam02036 |
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ... |
408-494 |
5.27e-32 |
|
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.
Pssm-ID: 460423 [Multi-domain] Cd Length: 100 Bit Score: 118.13 E-value: 5.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 408 VKKIGG-IFAFKVKDGPGgkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMG 486
Cdd:pfam02036 15 LKKLNGkVIRFDLTDLGL----SLTLDLKDGGGRVLAGDEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDME 90
|
....*...
gi 302344762 487 LAMKLQNL 494
Cdd:pfam02036 91 LAQKLEGL 98
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
127-356 |
2.45e-28 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 116.00 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 127 MEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYglQSK 206
Cdd:PRK06066 154 MSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKL--TDD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 207 AVEILAQEMMTDlPSSFEEKSIIKMVgfdMSKEAARKCYEKSGLTP--NDIDVIELHDCFSTNELLTYEALGLCPEGQGA 284
Cdd:PRK06066 232 PVWIKGIGWSTE-SSNLETAELGKAN---YMRIAADMAYKMAGIESprKEVDAAEVDDRYSYKELQHIEALRLSEEPEKD 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302344762 285 TLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQvPGAKVALQHNL-GI---GGAVVV 356
Cdd:PRK06066 308 SLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQ-GKAERAVVASWrGIptlTGSVVV 382
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
12-338 |
6.79e-28 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 114.92 E-value: 6.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 12 RRVFVVGVGMTKFVKPGAENSRDypdLAEEAGKKALADAQIPYSAVDQACVGY--------------------------- 64
Cdd:PRK06065 9 KRVAVIGAGLTLFRRRLLETPQE---LAWEAASKALDEAGLELKDIDCVVIGSapdafdgvhmkgeylshgsggirkpvs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 65 -VF-------------------GVAECVLALGFEKMSKGSLGIKFSDRTIptdkhVDLLINKyglsahPVAPQM---FGY 121
Cdd:PRK06065 86 rVYvggatgvmtaiagwyhvasGLCQKVLAVAEEKMSPARPHPQAVFRYI-----WDPILEK------PLNPNLiwiFAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK06065 155 EMHRYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 202 glqskaveilaqemmTDLPSsfeeksIIKMVGFDMS---------------KEAARKCYEKSGLT-PN-DIDVIELHDCF 264
Cdd:PRK06065 235 ---------------TDTPV------WVEGVGWTLDntewpnrdlaypryvEFAARMAYKMAGIErPRkEIDVAEPYDPF 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302344762 265 STNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVP 338
Cdd:PRK06065 294 DYKELHHLEGLQLAKRGEAPKLLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGLMKVISIYWQLKGTAGKMQVK 367
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
129-352 |
8.61e-26 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 109.60 E-value: 8.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 129 KYGTKIEHF-----AKIGWKNHKHSVNNPYSQ-FQDEYSLDEV----------MASKEVFDFLTILQCCPTSDGAAAAIL 192
Cdd:PTZ00455 188 KYIQEHGHFtmedtARVAAKAYANGNKNPLAHmHTRKLSLEFCtgasdknpkfLGNETYKPFLRMTDCSQVSDGGAGLVL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 193 ASEAFVQKYGLQ---SKAVEILAQEM-MTDLPSSFEEKSiiKMVgfdMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNE 268
Cdd:PTZ00455 268 ASEEGLQKMGLSpndSRLVEIKSLACaSGNLYEDPPDAT--RMF---TSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 269 LLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAkVALQHNL 348
Cdd:PTZ00455 343 LLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQMKNI-PALGATL 421
|
....
gi 302344762 349 GIGG 352
Cdd:PTZ00455 422 NMGG 425
|
|
| PRK08142 |
PRK08142 |
thiolase domain-containing protein; |
112-353 |
3.04e-25 |
|
thiolase domain-containing protein;
Pssm-ID: 236164 [Multi-domain] Cd Length: 388 Bit Score: 107.10 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 112 HPVAPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGaaaai 191
Cdd:PRK08142 139 GPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDG----- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 192 laseafvqkyglqSKAVEILAQEMMTDLpssfeEKSIIKMVG------------FDMSKEAAR----KCYEKSGLTPNDI 255
Cdd:PRK08142 214 -------------GGALVVVRPEIARSL-----KRPLVKVLGageaikgqmggkVDLTYSGAAwsgpAAFAEAGVTPADI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 256 DVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYG-GKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAG- 333
Cdd:PRK08142 276 KYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHPANRGGMTKVIEAVRQLRGEAHp 355
|
250 260
....*....|....*....|
gi 302344762 334 KRQVPGAKVALQHnlGIGGA 353
Cdd:PRK08142 356 AVQVPNCDLALAH--GTGGL 373
|
|
| SCP2 |
COG3255 |
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism]; |
409-494 |
1.06e-24 |
|
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
Pssm-ID: 442486 [Multi-domain] Cd Length: 104 Bit Score: 98.05 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 409 KKIGGIFAFKVKDGPGGkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGLA 488
Cdd:COG3255 18 AGWDGVVQFVITGEGGG---AYYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLA 94
|
....*.
gi 302344762 489 MKLQNL 494
Cdd:COG3255 95 MKLMSL 100
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
16-340 |
2.48e-23 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 101.59 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 16 VVGVGMTKFVKpgaENSRDYPDLAEEAGKKALADA------------------------------------QIPY----- 54
Cdd:PRK07855 8 IVGIGATEFSK---NSGRSELRLACEAVLAALDDAglapsdvdglvtftmdtnpeiavaralgigelkffsRIHYgggaa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 55 -SAVDQACVGYVFGVAECVLAlgFEKMSKGSlGIKFS--DRTIPTDKHVDLLINK----YGLS--AHPVApqMFGyagKE 125
Cdd:PRK07855 85 cATVQQAAMAVATGVADVVVC--YRAFNERS-GMRFGqgQTGLAENPTSTGVDYGwsypHGLLtpAAWVA--MLA---RR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 126 HMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDE-YSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKygLQ 204
Cdd:PRK07855 157 YMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRpITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAERARD--LK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 205 SKAVEILA--------QEMMT----DLPSSFEEKSIikmvgfdmskeAARKCYEKSGLTPNDIDVIELHDCFSTNELLTY 272
Cdd:PRK07855 235 QRPAVIKAaaqgsgadQYMMTsyyrDDITGLPEMGL-----------VARQLWAQSGLGPADIDTAILYDHFTPFVLMQL 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344762 273 EALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLaqcAELCWQLRGEAgKRQVPGA 340
Cdd:PRK07855 304 EELGFCGRGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNGI---AEAVRQLRGTS-VNQVPGV 367
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
240-356 |
2.91e-12 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 68.27 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLA 319
Cdd:cd00751 290 AIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPE------------------KVNVNGGAIALGHPLGASGAR 351
|
90 100 110
....*....|....*....|....*....|....*..
gi 302344762 320 QCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 356
Cdd:cd00751 352 IVVTLLHELKRRGGRYGL----ATMCIGGGQGAAMVI 384
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
52-356 |
1.07e-11 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 66.67 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 52 IPYSAVDQAC------VGYVF-----GVAECVLALGFEKMSKGSLG--------IKFSDRtiPTDKHVDLLInkyGLSAH 112
Cdd:PRK06445 86 IPAMAVDRQCasslttVSIGAmeiatGMADIVIAGGVEHMTRTPMGdnphiepnPKLLTD--PKYIEYDLTT---GYVMG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 113 PVAPQMFGYAG--KEHMEKYGTKIEHFA----KIGW-----------KNHKHSVNNPYSQFQDEYSLDEVMASKEVFD-- 173
Cdd:PRK06445 161 LTAEKLAEEAGikREEMDRWSLRSHQLAakaiQEGYfkdeilpieveVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKpd 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 174 -FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVeilaqemmtdlpssfeeksiIKMVGFD------MSK---EAARK 243
Cdd:PRK06445 241 gVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAK--------------------IRSFGFAgvppaiMGKgpvPASKK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 244 CYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAE 323
Cdd:PRK06445 301 ALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPE------------------TVNIKGGAIAIGHPLGATGARIVGT 362
|
330 340 350
....*....|....*....|....*....|...
gi 302344762 324 LCWQLRGEAGKRQVPGAKVAlqhnLGIGGAVVV 356
Cdd:PRK06445 363 LARQLQIKGKDYGVATLCVG----GGQGGAVVL 391
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
240-356 |
1.38e-11 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 61.50 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLA 319
Cdd:pfam02803 27 AIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASGAR 88
|
90 100 110
....*....|....*....|....*....|....*..
gi 302344762 320 QCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 356
Cdd:pfam02803 89 ILVTLLHELKRRGGKYGL----ASLCIGGGQGVAMII 121
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
239-356 |
3.54e-11 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 64.94 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGL 318
Cdd:TIGR01930 289 PAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASGA 350
|
90 100 110
....*....|....*....|....*....|....*...
gi 302344762 319 AQCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 356
Cdd:TIGR01930 351 RIVTTLLHELKRRGGRYGL----ATMCIGGGQGAAVIL 384
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
240-317 |
7.72e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 57.59 E-value: 7.72e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHD------------------KVNVNGGAIAMGHPLGATG 364
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
240-335 |
1.25e-08 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 56.89 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlVDRGDNtyggkwvINPSGGLISKGHPLGATG-- 317
Cdd:PRK09050 302 ATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGL---------ADDDAR-------VNPNGGAIALGHPLGMSGar 365
|
90
....*....|....*...
gi 302344762 318 LAQCAELcwQLRGEAGKR 335
Cdd:PRK09050 366 LVLTALH--QLERTGGRY 381
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
237-348 |
4.92e-08 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 54.70 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 237 SKEAARKCyekSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlvdrGDNTyggkwVINPSGGLISkGHPLGAT 316
Cdd:PRK07937 252 TALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALGL------------GDKT-----KVNPSGGALA-ANPMFAA 310
|
90 100 110
....*....|....*....|....*....|....*
gi 302344762 317 GLAQCAELCWQ-LRGEAGkRQVPGAKV--ALQHNL 348
Cdd:PRK07937 311 GLERIGEAARHiWDGSAR-RALAHATSgpALQQNL 344
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
238-334 |
6.19e-08 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 54.62 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 238 KEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK09052 300 IEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPS------------------KVNPLGGAIALGHPLGATG 361
|
90
....*....|....*..
gi 302344762 318 LAQCAELCWQLRGEAGK 334
Cdd:PRK09052 362 AIRTATVVHGLRRTNLK 378
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
240-317 |
1.48e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 53.56 E-value: 1.48e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK07801 285 ATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAK------------------VNPNGGAIALGHPLGATG 344
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
240-317 |
1.86e-07 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 53.42 E-value: 1.86e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK09051 297 ATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAK------------------VNPNGSGISLGHPVGATG 356
|
|
| Alkyl_sulf_C |
pfam14864 |
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ... |
427-484 |
5.49e-07 |
|
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. Together with the N-terminal catalytic domain, this domain forms a hydrophobic chute and may recruit hydrophobic substrates.
Pssm-ID: 405542 [Multi-domain] Cd Length: 124 Bit Score: 48.34 E-value: 5.49e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302344762 427 EATWVVDVKNGkgsVL----PNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGN 484
Cdd:pfam14864 43 DEQYRLTLSNG---VLtyrkGRQADDADATLTLTRADLLALLLGKATLGKLIAAGKIKVEGD 101
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
246-321 |
1.54e-06 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 50.53 E-value: 1.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302344762 246 EKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGlAQC 321
Cdd:PLN02287 342 KAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEK------------------VNVNGGAIALGHPLGATG-ARC 398
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
181-356 |
2.25e-06 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 49.68 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 181 CPTSDGAAAAILASEAFVQKYGLQSKAvEILAQ-------EMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPN 253
Cdd:COG0183 246 SGINDGAAALLLMSEEAAKELGLKPLA-RIVAYavagvdpEIMGIGPV-----------------PATRKALARAGLTLD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 254 DIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAG 333
Cdd:COG0183 308 DIDLIEINEAFAAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGARILVTLLHELERRGG 369
|
170 180
....*....|....*....|...
gi 302344762 334 KRQVpgakVALQHNLGIGGAVVV 356
Cdd:COG0183 370 RYGL----ATMCIGGGQGIALII 388
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
185-317 |
2.38e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 49.77 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 185 DGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSsfeeksiikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCF 264
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPRA-RIVAMANMGDDPT----------LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAF 344
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 302344762 265 STNELLTYEALGLcpegqgatlvDRGDntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK06025 345 AVVAEKFIRDLDL----------DRDK--------VNVNGGAIALGHPIGATG 379
|
|
| BDS1 |
COG2015 |
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ... |
428-494 |
2.61e-06 |
|
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441618 [Multi-domain] Cd Length: 629 Bit Score: 49.84 E-value: 2.61e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302344762 428 ATWVVDVKNGkgsVLPN----SDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGLAMKLQNL 494
Cdd:COG2015 551 EKYLLELRNG---VLTYrkgpQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGDAAALARLLGL 618
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
239-356 |
2.65e-06 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 49.78 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatlVDRGDNTyggkwvINPSGGLISKGHPLGATGl 318
Cdd:PRK08131 300 EAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLG----------VDFDDPR------VNPNGGAIAVGHPLGASG- 362
|
90 100 110
....*....|....*....|....*....|....*...
gi 302344762 319 aqcAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVV 356
Cdd:PRK08131 363 ---ARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVI 397
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
240-317 |
4.88e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 48.83 E-value: 4.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302344762 240 AARKCYEKSGLTPNDIDVIELhdcfstNELLTYEALGLCPE-GQGATLVDRgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK06205 303 ATEKALARAGLTLDDIDLIEL------NEAFAAQVLAVLKEwGFGADDEER----------LNVNGSGISLGHPVGATG 365
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
161-317 |
7.13e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 48.46 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 161 SLDEVMASKEVF---DFLTILQCCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikm 231
Cdd:PRK07851 237 TYEKVSQLKPVFrpdGTVTAGNACPLNDGAAAVVIMSDTKARELGLTplarivSTGVSGLSPEIMGLGPV---------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 232 vgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcPEgqgatlvDRgdntyggkwvINPSGGLISKGH 311
Cdd:PRK07851 307 -------EASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGI-DE-------DK----------LNVSGGAIALGH 361
|
....*.
gi 302344762 312 PLGATG 317
Cdd:PRK07851 362 PFGMTG 367
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
14-159 |
7.91e-06 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 47.30 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 14 VFVVGVGMTKFVK-PGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF-------------------------- 66
Cdd:pfam00108 1 VVIVSAARTPFGSfGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLqagegqnparqaalkagipdsapavt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 67 ---------------------GVAECVLALGFEKMSKGSLGIKFSDR---TIPTDKHVDLLInKYGLSAHPVAPQMfGYA 122
Cdd:pfam00108 81 inkvcgsglkavylaaqsiasGDADVVLAGGVESMSHAPYALPTDARsglKHGDEKKHDLLI-PDGLTDAFNGYHM-GLT 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 302344762 123 GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDE 159
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGkFKDE 196
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
240-317 |
9.50e-06 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 47.84 E-value: 9.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK05790 296 AIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPE------------------KVNVNGGAIALGHPIGASG 355
|
|
| UbiJ |
COG3165 |
Ubiquinone biosynthesis protein UbiJ, contains SCP2 domain [Coenzyme transport and metabolism]; ... |
441-494 |
2.31e-05 |
|
Ubiquinone biosynthesis protein UbiJ, contains SCP2 domain [Coenzyme transport and metabolism];
Pssm-ID: 442398 Cd Length: 204 Bit Score: 45.23 E-value: 2.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 302344762 441 VLPNSDKKADCTITMADSDFLALMTGKmNPQSAFFQGKLKITGNMGLAMKLQNL 494
Cdd:COG3165 58 VLGAWEGEADCTLTGSLSALLRLADAQ-DLTALIASGELRIEGDAQLAQQLSRL 110
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
240-317 |
5.35e-05 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 45.34 E-value: 5.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatLVDRGDNTyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK08947 287 ATQKALKRAGLSISDIDVFELNEAFAAQSLPCLKDLG---------LLDKMDEK------VNLNGGAIALGHPLGCSG 349
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
239-338 |
6.62e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 45.27 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGL 318
Cdd:PRK06954 299 GAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEK------------------VNVNGGACALGHPIGASGA 360
|
90 100
....*....|....*....|
gi 302344762 319 AQCAELCWQLRGEAGKRQVP 338
Cdd:PRK06954 361 RILVTLIGALRARGGKRGVA 380
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
240-317 |
7.32e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 45.09 E-value: 7.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK08235 296 AINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPE------------------KVNVNGGAVALGHPIGASG 355
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
240-317 |
3.30e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 42.95 E-value: 3.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK05656 296 ATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAA------------------KVNVNGGAIALGHPIGASG 355
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
240-356 |
5.36e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 42.32 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALglcpegqgatlvdrgdntyggKW---VINPSGGLISKGHPLGAT 316
Cdd:PRK06633 295 ASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREM---------------------KWdmeKVNINGGAIAIGHPIGAS 353
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 302344762 317 GLAQCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 356
Cdd:PRK06633 354 GGRVLITLIHGLRRAKAKKGL----VTLCIGGGMGMAMCV 389
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
240-335 |
9.10e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 41.64 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLA 319
Cdd:PRK06504 293 ATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPER------------------LNVNGGAIALGHPLGASGTK 354
|
90
....*....|....*.
gi 302344762 320 QCAELCWQLRgEAGKR 335
Cdd:PRK06504 355 LMTTLVHALK-QRGKR 369
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
240-339 |
2.58e-03 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 40.08 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLA 319
Cdd:PLN02644 296 AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEK------------------VNVHGGAVSLGHPIGCSGAR 357
|
90 100
....*....|....*....|
gi 302344762 320 QCAELCWQLRGEAGKRQVPG 339
Cdd:PLN02644 358 ILVTLLGVLRSKNGKYGVAG 377
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
235-258 |
5.77e-03 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 38.68 E-value: 5.77e-03
10 20
....*....|....*....|....
gi 302344762 235 DMSKEAARKCYEKSGLTPNDIDVI 258
Cdd:cd00830 52 DLAVEAAKKALEDAGIDADDIDLI 75
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
183-317 |
6.81e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 38.96 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344762 183 TSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPNDID 256
Cdd:PRK07661 248 MSDGAAAVLLMDREKAESDGLKplakfrSFAVAGVPPEVMGIGPI-----------------AAIPKALKLAGLELSDIG 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302344762 257 VIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK07661 311 LFELNEAFASQSIQVIRELGLDEE------------------KVNVNGGAIALGHPLGCTG 353
|
|
| |
