|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
12-318 |
2.72e-178 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 499.81 E-value: 2.72e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------- 66
Cdd:PRK08256 1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYgdstsgqralyevgmtgipivnvnn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 67 ------------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHME 128
Cdd:PRK08256 79 ncstgstalflarqavrsGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 129 KYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKAV 208
Cdd:PRK08256 159 KYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 209 EILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVD 288
Cdd:PRK08256 238 EIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFID 317
|
330 340 350
....*....|....*....|....*....|
gi 2462512374 289 RGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK08256 318 DGDNTYGGRWVVNPSGGLLSKGHPLGATGL 347
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
17-336 |
1.51e-149 |
|
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: 426.91 E-value: 1.51e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 17 VGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYS----AVDQACVGYVF-------------------------- 66
Cdd:cd00826 1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLgagegqncaqqaamhagglqeapaig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 67 ---------------------GVAECVLALGFEKMSkgslgikFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKE 125
Cdd:cd00826 81 mnnlcgsglralalamqliagGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 126 HMEKYGTKIEHFAKIGWKN---HKHSVNNPYSQFQDEYSLDEVMASKEVFD---FLTILQCCPTSDGAAAAILASEAFVQ 199
Cdd:cd00826 154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 200 KYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCP 279
Cdd:cd00826 234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 280 EGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE--NDVRRSGILTKGP 336
Cdd:cd00826 314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAElcFELKGEAGKRQGA 372
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
17-323 |
8.42e-105 |
|
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: 312.66 E-value: 8.42e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 17 VGVGMTKFVKPGaenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------------ 66
Cdd:cd00829 1 VGVGMTPFGRRS---DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAggrfqsfpgaliaeylgllgkpatrveaag 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 67 ----------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLInkYGLSAhpvaPQMFGYAGKEHMEKY 130
Cdd:cd00829 78 asgsaavraaaaaiasGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPP--GGLTP----PALYALAARRYMHRY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 131 GTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqsKAVEI 210
Cdd:cd00829 152 GTTREDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTD--RPVWI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 211 LAQEMMTDLPSSFEEKSiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRG 290
Cdd:cd00829 230 LGVGAASDTPSLSERDD---FLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREG 306
|
330 340 350
....*....|....*....|....*....|...
gi 2462512374 291 DNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:cd00829 307 DTAIGGDLPVNTSGGLLSKGHPLGATGLAQAVE 339
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
11-323 |
1.77e-68 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 219.77 E-value: 1.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 11 LRRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQ-------------------------------------IP 53
Cdd:PRK06064 1 MRDVAIIGVGQTKF---GELWDVSLRDLAVEAGLEALEDAGidgkdidamyvgnmsaglfvsqehiaaliadyaglapIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 54 YSAVDQAC--------VGYVF---GVAECVLALGFEKMSKgslgikfsdrtIPTDKHVDLLI--------NKYGLSAhpv 114
Cdd:PRK06064 78 ATRVEAACasggaalrQAYLAvasGEADVVLAAGVEKMTD-----------VPTPDATEAIAragdyeweEFFGATF--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 115 aPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILAS 194
Cdd:PRK06064 144 -PGLYALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILAS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 195 EAFVQKYglQSKAVEILAQEMMTDLPSSFEEKSIikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 274
Cdd:PRK06064 223 EEKAKEY--TDTPVWIKASGQASDTIALHDRKDF---TTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYED 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462512374 275 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:PRK06064 298 LGFAKKGEGGKLAREGQTYIGGDIPVNPSGGLKAKGHPVGATGVSQAVE 346
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
12-318 |
2.73e-50 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 172.34 E-value: 2.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYV-------------------------- 65
Cdd:PRK12578 1 RRVAVIGVGNSKF---GRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTayrgielypapivaeysgltgkvplr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 66 --------------------FGVAECVLALGFEKMSK----GSLGIKFSDRTIPTDKHvdllinKYGLSAhpvaPQMFGY 121
Cdd:PRK12578 78 veamcatglaasltaytavaSGLVDMAIAVGVDKMTEvdtsTSLAIGGRGGNYQWEYH------FYGTTF----PTYYAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK12578 148 YATRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 202 GLQSkAVEILAQEMMTDLpSSFEEKsiIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEG 281
Cdd:PRK12578 228 KIDS-PVWITGIGYANDY-AYVARR--GEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKG 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462512374 282 QGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK12578 304 KGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGL 340
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
13-317 |
2.61e-40 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 146.25 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 13 RVFVVGVGMTKFVKPGAEnsrDYPDLAEEAGKKALADAQIPYSAVDQACVGyVF-------------------------- 66
Cdd:PRK07516 3 TASIVGWAHTPFGKLDAE---TLESLIVRVAREALAHAGIAAGDVDGIFLG-HFnagfspqdfpaslvlqadpalrfkpa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 67 -----------------------GVAECVLALGFEKMSkgslgikfsdrTIPTDKHVDLLIN-KYGLSAHPVA---PQMF 119
Cdd:PRK07516 79 trvenacatgsaavyaaldaieaGRARIVLVVGAEKMT-----------ATPTAEVGDILLGaSYLKEEGDTPggfAGVF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 120 GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKE----VFDFLTILQCCPTSDGAAAAILASE 195
Cdd:PRK07516 148 GRIAQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEFCRTVSEknplVAGPLRRTDCSLVSDGAAALVLADA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 196 AFVQKYglqSKAVEILAQEMMTD-LPSSFEEksiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 274
Cdd:PRK07516 228 ETARAL---QRAVRFRARAHVNDfLPLSRRD-----PLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEA 299
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2462512374 275 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK07516 300 MGLAPPGQGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATG 342
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
12-324 |
5.22e-37 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 137.47 E-value: 5.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQI-----------------------------------PYSA 56
Cdd:PRK06157 7 DKVAILGMGCTKF---GERWDAGAEDLMVEAFLEALADAGIepkdidaawfgthydeigsgksgtplsralrlpniPVTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 57 VDQACV-------GYVFGVA----ECVLALGFEK-MSKGSLGIKFSDRTIPTDkhvdllinkyGLSAHPVAPQMFGYAGK 124
Cdd:PRK06157 84 VENFCAtgseafrGAVYAVAsgayDIALALGVEKlKDTGYGGLPVANPGTLAD----------MTMPNVTAPGNFAQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 125 EHMEKYGTKIEHF----AKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQK 200
Cdd:PRK06157 154 AYAAKYGVSREDLkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 201 YG----LQSKAVEILA---QEMMT---DLpSSFEEKSIikmvgfdmskeAARKCYEKSGLT-P-NDIDVIELHDCFSTNE 268
Cdd:PRK06157 234 LGkkdpVYVKALQLAVsngWELQYngwDG-SYFPTTRI-----------AARKAYREAGITdPrEELSMAEVHDCFSITE 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462512374 269 LLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGEN 324
Cdd:PRK06157 302 LVTMEDLGLSERGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEM 357
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
8-318 |
5.70e-36 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 135.42 E-value: 5.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 8 PATLRRVFVVGVGMTKFVKpgAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGY----------------------- 64
Cdd:PRK06365 12 KKKSRDVYMVAAGVTKFDK--ASPYMDFRERVKKAFDYAMNDAGLTLADIDGSVASYfsdhfqrqllagimvqdylglvp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 65 ------------------------VFGVAECVLALGFEKMSKgslgikfsdrtIPTDKHvdlliNKY-GLSA-----HPV 114
Cdd:PRK06365 90 kpskriegggatgglafqagyeeiASGRMDCVAVYGFETMSH-----------VNTWKG-----NEFiALASdtnfdYPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 115 APQMFGY---AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAI 191
Cdd:PRK06365 154 GGFYTGYyamMAVRHMYEFGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 192 LASEAfvQKYGLQSKAVEILAQEMMTD--------------LPSsfEEKSIIK------MVGFDMSKEAARKCYEKSGLT 251
Cdd:PRK06365 234 LASED--KAFEITDKPVLIKAIGTGSDtlrladrpfgevplLPN--ESPDDYKdlrypgVHSFRAGRMAAKEAYEMAGIT 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 252 P--NDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK06365 310 DplNDLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGI 378
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
10-323 |
5.78e-35 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 131.81 E-value: 5.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 10 TLRRVFVVGVGMTKFVKPGaensRDYPDLAEEAGKKALADAQIPYSAVdQACV----------GYVF------------- 66
Cdd:PRK06059 2 MPEPVYILGAGMHPWGKWG----RDFVEYGVVAARAALADAGLDWRDV-QLVVgadtirngypGFVAgatfaqalgwnga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 67 -------------------------GVAECVLALGFEKMSKGSLGIKFSDRtiPTDKhvDLLINKYGLSAHPVapqMFGY 121
Cdd:PRK06059 77 pvsssyaacasgsqalqsaraqilaGLCDVALVVGADTTPKGFFAPVGGER--PDDP--DWLRFHLIGATNPV---YFAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK06059 150 LARRRMDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSFARRH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 202 GLQSK-AVEILAQEMMT--------DLPsSFEEKSIIKMVGFDMS--KEAARKCYEKSGLTPNDIDVIELHDCFSTNELL 270
Cdd:PRK06059 230 LGSVAgVPSVRAISTVTprypqhlpELP-DIATDSTAAVPAPERVfkDQILDAAYAEAGIGPEDLSLAEVYDLSTALELD 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462512374 271 TYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:PRK06059 309 WYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCE 361
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
14-321 |
1.39e-29 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 117.48 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 14 VFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFG-------------------------- 67
Cdd:PRK06289 5 VWVLGGYQSDFARNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGelfagqghlgampatvhpalwgvpas 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 68 ----------VA-------------ECVLALGFEKMskgslgikfsdRTIPTDKHVDLL-----INKYGLSAHPVAPQMF 119
Cdd:PRK06289 85 rheaacasgsVAtlaamadlragryDVALVVGVELM-----------KTVPGDVAAEHLgaaawTGHEGQDARFPWPSMF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 120 GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-----FQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILAS 194
Cdd:PRK06289 154 ARVADEYDRRYGLDEEHLRAIAEINFANARRNPNAQtrgwaFPDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLAS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 195 EAFVQKYGLQSKAVEILAQEMMTdLPSSFEEKsIIKMVG----FDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELL 270
Cdd:PRK06289 234 DAYLRDYADARPIPRIKGWGHRT-APLGLEQK-LDRSAGdpyvLPHVRQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2462512374 271 TYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNL 321
Cdd:PRK06289 312 AIDHIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRML 362
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
12-323 |
2.64e-26 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 107.89 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 12 RRVFVVGVGMTKFVKPGAENSrdYPDLAEEAGKKALADAQIPYSAVD--------------------------------- 58
Cdd:PRK08313 3 RLAAVLGTGQTKYVAKRQDVS--MAGLVREAIDRALADAGLTWDDIDavvvgkapdffegvmmpelfladalgatgkpli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 59 -----------QACVGYVF---GVAECVLALGFEKMSKGSLGIKFSdrtIPTDKHVDLLINKYGLSAHPVApqmfgyagk 124
Cdd:PRK08313 81 rvhtagsvggsTAVVAASLvqsGVYRRVLAVAWEKQSESNAMWALS---IPVPFTKPVGAGAGGYFAPHVR--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 125 EHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQF-QDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGL 203
Cdd:PRK08313 149 AYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLhQPDITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 204 QSKAVeILAQEMMTDlPSSFEEKSIIKMVGfdmSKEAARKCYEKSGLT-P-NDIDVIELHDCFSTNELLTYEALGLCPEG 281
Cdd:PRK08313 229 RPVAW-IHGTAMRTE-PLAFAGRDQVNPQA---GRDAAAALWKAAGITdPrDEIDVAEIYVPFSWFEPMWLENLGFAPEG 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2462512374 282 QGATLVDRGDNTYGGKWVINPSGGLISkGHPLGATGLKNLGE 323
Cdd:PRK08313 304 EGWKLTEAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAE 344
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
181-323 |
7.78e-26 |
|
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: 104.06 E-value: 7.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 181 CPTSDGAAAAILASEAFVQKYGLQskaveilAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIEL 260
Cdd:cd00327 98 FVFGDGAAAAVVESEEHALRRGAH-------PQAEIVSTAATFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEA 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462512374 261 HDCFSTNELLTYEALGLCPEGQGAtlvdrgdntyggkwvINPSGGLISKGHPLGATGLKNLGE 323
Cdd:cd00327 171 HGTGTPIGDAVELALGLDPDGVRS---------------PAVSATLIMTGHPLGAAGLAILDE 218
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
129-323 |
6.29e-24 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 101.89 E-value: 6.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 129 KYGTKIEHF-----AKIGWKNHKHSVNNPYSQ-FQDEYSLDEV----------MASKEVFDFLTILQCCPTSDGAAAAIL 192
Cdd:PTZ00455 188 KYIQEHGHFtmedtARVAAKAYANGNKNPLAHmHTRKLSLEFCtgasdknpkfLGNETYKPFLRMTDCSQVSDGGAGLVL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 193 ASEAFVQKYGLQ---SKAVEILAQEM-MTDLPSSFEEKSiiKMVgfdMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNE 268
Cdd:PTZ00455 268 ASEEGLQKMGLSpndSRLVEIKSLACaSGNLYEDPPDAT--RMF---TSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAE 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462512374 269 LLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:PTZ00455 343 LLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIME 397
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
113-318 |
4.37e-23 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 98.95 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 113 PVAPqMFGYA--GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGaaaa 190
Cdd:PRK06158 137 PVNP-VSAYAlaAARHMHQYGTTREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDG---- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 191 ilaseafvqkyglqSKAVEILAQEMMTDLP----------SSFEEKSIIKMVgfDMSKEAA----RKCYEKSGLTPNDID 256
Cdd:PRK06158 212 --------------AGAVVMVRADRARDLPrppvyvlgaaAATWHRQISSMP--DLTVTAAaesgPRAFAMAGLTPADID 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462512374 257 VIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPlGATGL 318
Cdd:PRK06158 276 VVELYDAFTINTILFLEDLGFCAKGEGGAFVEGGRIAPGGRLPVNTNGGGLSCVHP-GMYGL 336
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
127-323 |
9.45e-22 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 95.20 E-value: 9.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 127 MEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYglQSK 206
Cdd:PRK06066 154 MSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKL--TDD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 207 AVEILAQEMMTDlPSSFEEKSIIKMVgfdMSKEAARKCYEKSGLTP--NDIDVIELHDCFSTNELLTYEALGLCPEGQGA 284
Cdd:PRK06066 232 PVWIKGIGWSTE-SSNLETAELGKAN---YMRIAADMAYKMAGIESprKEVDAAEVDDRYSYKELQHIEALRLSEEPEKD 307
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462512374 285 TLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:PRK06066 308 SLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLD 346
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
16-308 |
1.30e-20 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 91.96 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 16 VVGVGMTKFVKpgaENSRDYPDLAEEAGKKALADA------------------------------------QIPY----- 54
Cdd:PRK07855 8 IVGIGATEFSK---NSGRSELRLACEAVLAALDDAglapsdvdglvtftmdtnpeiavaralgigelkffsRIHYgggaa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 55 -SAVDQACVGYVFGVAECVLAlgFEKMSKGSlGIKFS--DRTIPTDKHVDLLINK----YGLS--AHPVApqMFGyagKE 125
Cdd:PRK07855 85 cATVQQAAMAVATGVADVVVC--YRAFNERS-GMRFGqgQTGLAENPTSTGVDYGwsypHGLLtpAAWVA--MLA---RR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 126 HMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDE-YSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKygLQ 204
Cdd:PRK07855 157 YMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRpITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAERARD--LK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 205 SKAVEILA--------QEMMT----DLPSSFEEKSIikmvgfdmskeAARKCYEKSGLTPNDIDVIELHDCFSTNELLTY 272
Cdd:PRK07855 235 QRPAVIKAaaqgsgadQYMMTsyyrDDITGLPEMGL-----------VARQLWAQSGLGPADIDTAILYDHFTPFVLMQL 303
|
330 340 350
....*....|....*....|....*....|....*.
gi 2462512374 273 EALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLIS 308
Cdd:PRK07855 304 EELGFCGRGEAKDFIADGALELGGRLPINTHGGQLG 339
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
12-318 |
1.71e-18 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 85.65 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 12 RRVFVVGVGMTKFVKPGAENSRDypdLAEEAGKKALADAQIPYSAVDQACVGY--------------------------- 64
Cdd:PRK06065 9 KRVAVIGAGLTLFRRRLLETPQE---LAWEAASKALDEAGLELKDIDCVVIGSapdafdgvhmkgeylshgsggirkpvs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 65 -VF-------------------GVAECVLALGFEKMSKGSLGIKFSDRTIptdkhVDLLINKyglsahPVAPQM---FGY 121
Cdd:PRK06065 86 rVYvggatgvmtaiagwyhvasGLCQKVLAVAEEKMSPARPHPQAVFRYI-----WDPILEK------PLNPNLiwiFAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK06065 155 EMHRYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 202 glqskaveilaqemmTDLPssfeekSIIKMVGFDMS---------------KEAARKCYEKSGLT-PN-DIDVIELHDCF 264
Cdd:PRK06065 235 ---------------TDTP------VWVEGVGWTLDntewpnrdlaypryvEFAARMAYKMAGIErPRkEIDVAEPYDPF 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2462512374 265 STNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK06065 294 DYKELHHLEGLQLAKRGEAPKLLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGL 347
|
|
| PRK08142 |
PRK08142 |
thiolase domain-containing protein; |
112-312 |
3.97e-18 |
|
thiolase domain-containing protein;
Pssm-ID: 236164 [Multi-domain] Cd Length: 388 Bit Score: 84.75 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 112 HPVAPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGaaaai 191
Cdd:PRK08142 139 GPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDG----- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 192 laseafvqkyglqSKAVEILAQEMMTDLpssfeEKSIIKMVG------------FDMSKEAAR----KCYEKSGLTPNDI 255
Cdd:PRK08142 214 -------------GGALVVVRPEIARSL-----KRPLVKVLGageaikgqmggkVDLTYSGAAwsgpAAFAEAGVTPADI 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 256 DVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYG-GKWVINPSGGLISKGHP 312
Cdd:PRK08142 276 KYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHP 333
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
240-317 |
3.36e-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: 66.73 E-value: 3.36e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:cd00751 290 AIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPE------------------KVNVNGGAIALGHPLGASG 349
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
52-322 |
1.10e-11 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 65.51 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 52 IPYSAVDQAC------VGYVF-----GVAECVLALGFEKMSKGSLG--------IKFSDRtiPTDKHVDLLInkyGLSAH 112
Cdd:PRK06445 86 IPAMAVDRQCasslttVSIGAmeiatGMADIVIAGGVEHMTRTPMGdnphiepnPKLLTD--PKYIEYDLTT---GYVMG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 113 PVAPQMFGYAG--KEHMEKYGTKIEHFA----KIGW-----------KNHKHSVNNPYSQFQDEYSLDEVMASKEVFD-- 173
Cdd:PRK06445 161 LTAEKLAEEAGikREEMDRWSLRSHQLAakaiQEGYfkdeilpieveVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKpd 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 174 -FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVeilaqemmtdlpssfeeksiIKMVGFD------MSK---EAARK 243
Cdd:PRK06445 241 gVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAK--------------------IRSFGFAgvppaiMGKgpvPASKK 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 244 CYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLKNLG 322
Cdd:PRK06445 301 ALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPE------------------TVNIKGGAIAIGHPLGATGARIVG 361
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
240-317 |
2.31e-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: 60.35 E-value: 2.31e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:pfam02803 27 AIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASG 86
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
239-317 |
4.63e-10 |
|
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: 60.32 E-value: 4.63e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:TIGR01930 289 PAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASG 349
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
240-317 |
1.86e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 58.74 E-value: 1.86e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHD------------------KVNVNGGAIAMGHPLGATG 364
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
240-317 |
8.35e-09 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 56.50 E-value: 8.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlVDRGDNtyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK09050 302 ATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGL---------ADDDAR-------VNPNGGAIALGHPLGMSG 363
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
240-319 |
3.84e-08 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 54.33 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLK 319
Cdd:PRK07801 285 ATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAK------------------VNPNGGAIALGHPLGATGAK 346
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
240-317 |
4.78e-08 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 54.20 E-value: 4.78e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK09051 297 ATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAK------------------VNPNGSGISLGHPVGATG 356
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
238-317 |
9.02e-08 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 53.47 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 238 KEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK09052 300 IEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPS------------------KVNPLGGAIALGHPLGATG 361
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
237-323 |
7.90e-07 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 50.46 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 237 SKEAARKCyekSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlvdrGDNTyggkwVINPSGGLISkGHPLGAT 316
Cdd:PRK07937 252 TALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALGL------------GDKT-----KVNPSGGALA-ANPMFAA 310
|
....*..
gi 2462512374 317 GLKNLGE 323
Cdd:PRK07937 311 GLERIGE 317
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
185-333 |
9.21e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 50.16 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 185 DGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSsfeeksiikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCF 264
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPRA-RIVAMANMGDDPT----------LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAF 344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462512374 265 STNELLTYEALGLcpegqgatlvDRGDntyggkwvINPSGGLISKGHPLGATG-------LKNLGENDVRRsGILT 333
Cdd:PRK06025 345 AVVAEKFIRDLDL----------DRDK--------VNVNGGAIALGHPIGATGsiligtvLDELERRGLKR-GLVT 401
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
14-159 |
1.00e-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: 49.61 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 14 VFVVGVGMTKFVK-PGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF-------------------------- 66
Cdd:pfam00108 1 VVIVSAARTPFGSfGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLqagegqnparqaalkagipdsapavt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 67 ---------------------GVAECVLALGFEKMSKGSLGIKFSDR---TIPTDKHVDLLInKYGLSAHPVAPQMfGYA 122
Cdd:pfam00108 81 inkvcgsglkavylaaqsiasGDADVVLAGGVESMSHAPYALPTDARsglKHGDEKKHDLLI-PDGLTDAFNGYHM-GLT 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462512374 123 GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDE 159
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGkFKDE 196
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
181-333 |
1.16e-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: 50.06 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 181 CPTSDGAAAAILASEAFVQKYGLQSKAvEILAQ-------EMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPN 253
Cdd:COG0183 246 SGINDGAAALLLMSEEAAKELGLKPLA-RIVAYavagvdpEIMGIGPV-----------------PATRKALARAGLTLD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 254 DIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG-------LKNLGENDV 326
Cdd:COG0183 308 DIDLIEINEAFAAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGarilvtlLHELERRGG 369
|
....*..
gi 2462512374 327 RRsGILT 333
Cdd:COG0183 370 RY-GLAT 375
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
246-317 |
1.91e-06 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 49.38 E-value: 1.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462512374 246 EKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PLN02287 342 KAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEK------------------VNVNGGAIALGHPLGATG 395
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
240-330 |
2.01e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 49.22 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELhdcfstNELLTYEALGLCPE-GQGATLVDRgdntyggkwvINPSGGLISKGHPLGATG- 317
Cdd:PRK06205 303 ATEKALARAGLTLDDIDLIEL------NEAFAAQVLAVLKEwGFGADDEER----------LNVNGSGISLGHPVGATGg 366
|
90
....*....|....*
gi 2462512374 318 --LKNLGENDVRRSG 330
Cdd:PRK06205 367 riLATLLRELQRRQA 381
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
240-317 |
2.20e-06 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 49.00 E-value: 2.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK05790 296 AIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPE------------------KVNVNGGAIALGHPIGASG 355
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
239-317 |
2.51e-06 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 49.01 E-value: 2.51e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatlVDRGDNTyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK08131 300 EAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLG----------VDFDDPR------VNPNGGAIAVGHPLGASG 362
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
161-325 |
3.96e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 48.46 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 161 SLDEVMASKEVF---DFLTILQCCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikm 231
Cdd:PRK07851 237 TYEKVSQLKPVFrpdGTVTAGNACPLNDGAAAVVIMSDTKARELGLTplarivSTGVSGLSPEIMGLGPV---------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 232 vgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcPEgqgatlvDRgdntyggkwvINPSGGLISKGH 311
Cdd:PRK07851 307 -------EASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGI-DE-------DK----------LNVSGGAIALGH 361
|
170 180
....*....|....*....|.
gi 2462512374 312 PLGATG-------LKNLGEND 325
Cdd:PRK07851 362 PFGMTGaritttlLNNLQTHD 382
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
240-317 |
2.18e-05 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 45.73 E-value: 2.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatLVDRGDNTyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK08947 287 ATQKALKRAGLSISDIDVFELNEAFAAQSLPCLKDLG---------LLDKMDEK------VNLNGGAIALGHPLGCSG 349
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
240-317 |
3.06e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 45.47 E-value: 3.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK08235 296 AINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPE------------------KVNVNGGAVALGHPIGASG 355
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
240-321 |
4.90e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 44.88 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLK 319
Cdd:PRK05656 296 ATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAA------------------KVNVNGGAIALGHPIGASGCR 357
|
..
gi 2462512374 320 NL 321
Cdd:PRK05656 358 VL 359
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
240-319 |
1.34e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 43.56 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLK 319
Cdd:PRK06504 293 ATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPER------------------LNVNGGAIALGHPLGASGTK 354
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
240-317 |
6.64e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 41.17 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALglcpegqgatlvdrgdntyggKW---VINPSGGLISKGHPLGAT 316
Cdd:PRK06633 295 ASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREM---------------------KWdmeKVNINGGAIAIGHPIGAS 353
|
.
gi 2462512374 317 G 317
Cdd:PRK06633 354 G 354
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
183-319 |
7.50e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 41.27 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 183 TSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPNDID 256
Cdd:PRK07661 248 MSDGAAAVLLMDREKAESDGLKplakfrSFAVAGVPPEVMGIGPI-----------------AAIPKALKLAGLELSDIG 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462512374 257 VIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLK 319
Cdd:PRK07661 311 LFELNEAFASQSIQVIRELGLDEE------------------KVNVNGGAIALGHPLGCTGAK 355
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
240-322 |
1.38e-03 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 40.46 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLK 319
Cdd:PLN02644 296 AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEK------------------VNVHGGAVSLGHPIGCSGAR 357
|
...
gi 2462512374 320 NLG 322
Cdd:PLN02644 358 ILV 360
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
235-258 |
3.24e-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: 39.06 E-value: 3.24e-03
10 20
....*....|....*....|....
gi 2462512374 235 DMSKEAARKCYEKSGLTPNDIDVI 258
Cdd:cd00830 52 DLAVEAAKKALEDAGIDADDIDLI 75
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
235-258 |
7.30e-03 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 37.78 E-value: 7.30e-03
10 20
....*....|....*....|....
gi 2462512374 235 DMSKEAARKCYEKSGLTPNDIDVI 258
Cdd:COG0332 53 DLAVEAARKALEAAGIDPEDIDLI 76
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
184-317 |
9.32e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 37.56 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 184 SDGAAAAILASEAFVQKYGLQSKAVeILAQEMMTDLPSSFEEKSIikmvgfdmskEAARKCYEKSGLTPNDIDVIELHDC 263
Cdd:PRK06954 255 SDGAAALVMMRASTAKRLGLAPLAR-VVGHSTFAQAPSKFTTAPV----------GAIRKLFEKNGWRAAEVDLFEINEA 323
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462512374 264 FSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK06954 324 FAVVTMAAMKEHGLPHEK------------------VNVNGGACALGHPIGASG 359
|
|
|