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Conserved domains on  [gi|55956775|ref|NP_001007099|]
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sterol carrier protein 2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08256 super family cl32282
lipid-transfer protein; Provisional
 12-317 1.71e-176

lipid-transfer protein; Provisional


The actual alignment was detected with superfamily member PRK08256:

Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 493.65  E-value: 1.71e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------- 66
Cdd:PRK08256   1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYgdstsgqralyevgmtgipivnvnn 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   67 ------------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHME 128
Cdd:PRK08256  79 ncstgstalflarqavrsGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHME 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  129 KYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKAV 208
Cdd:PRK08256 159 KYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRAV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  209 EILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVD 288
Cdd:PRK08256 238 EIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFID 317

                        330       340
                 ....*....|....*....|....*....
gi 55956775  289 RGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK08256 318 DGDNTYGGRWVVNPSGGLLSKGHPLGATG 346
 
Name Accession Description Interval E-value
PRK08256 PRK08256
lipid-transfer protein; Provisional
 12-317 1.71e-176

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 493.65  E-value: 1.71e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------- 66
Cdd:PRK08256   1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYgdstsgqralyevgmtgipivnvnn 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   67 ------------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHME 128
Cdd:PRK08256  79 ncstgstalflarqavrsGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHME 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  129 KYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKAV 208
Cdd:PRK08256 159 KYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRAV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  209 EILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVD 288
Cdd:PRK08256 238 EIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFID 317

                        330       340
                 ....*....|....*....|....*....
gi 55956775  289 RGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK08256 318 DGDNTYGGRWVVNPSGGLLSKGHPLGATG 346
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
 17-322 9.73e-148

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: 421.13  E-value: 9.73e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  17 VGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYS----AVDQACVGYVF-------------------------- 66
Cdd:cd00826   1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLgagegqncaqqaamhagglqeapaig 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  67 ---------------------GVAECVLALGFEKMSkgslgikFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKE 125
Cdd:cd00826  81 mnnlcgsglralalamqliagGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775 126 HMEKYGTKIEHFAKIGWKN---HKHSVNNPYSQFQDEYSLDEVMASKEVFD---FLTILQCCPTSDGAAAAILASEAFVQ 199
Cdd:cd00826 154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775 200 KYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCP 279
Cdd:cd00826 234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 55956775 280 EGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGGHSCS 322
Cdd:cd00826 314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICA 356
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 240-317 2.15e-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: 2.15e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775   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 ...
 239-318 2.86e-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: 60.70  E-value: 2.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGG 318
Cdd:TIGR01930 289 PAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASGA 350
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 181-318 9.01e-07

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: 9.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775 181 CPTSDGAAAAILASEAFVQKYGLQSKAvEILAQ-------EMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPN 253
Cdd:COG0183 246 SGINDGAAALLLMSEEAAKELGLKPLA-RIVAYavagvdpEIMGIGPV-----------------PATRKALARAGLTLD 307

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55956775 254 DIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGG 318
Cdd:COG0183 308 DIDLIEINEAFAAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGA 354
 
Name Accession Description Interval E-value
PRK08256 PRK08256
lipid-transfer protein; Provisional
 12-317 1.71e-176

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 493.65  E-value: 1.71e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------- 66
Cdd:PRK08256   1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYgdstsgqralyevgmtgipivnvnn 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   67 ------------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHME 128
Cdd:PRK08256  79 ncstgstalflarqavrsGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHME 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  129 KYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKAV 208
Cdd:PRK08256 159 KYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRAV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  209 EILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVD 288
Cdd:PRK08256 238 EIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFID 317

                        330       340
                 ....*....|....*....|....*....
gi 55956775  289 RGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK08256 318 DGDNTYGGRWVVNPSGGLLSKGHPLGATG 346
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
 17-322 9.73e-148

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: 421.13  E-value: 9.73e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  17 VGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYS----AVDQACVGYVF-------------------------- 66
Cdd:cd00826   1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLgagegqncaqqaamhagglqeapaig 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  67 ---------------------GVAECVLALGFEKMSkgslgikFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKE 125
Cdd:cd00826  81 mnnlcgsglralalamqliagGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775 126 HMEKYGTKIEHFAKIGWKN---HKHSVNNPYSQFQDEYSLDEVMASKEVFD---FLTILQCCPTSDGAAAAILASEAFVQ 199
Cdd:cd00826 154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775 200 KYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCP 279
Cdd:cd00826 234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 55956775 280 EGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGGHSCS 322
Cdd:cd00826 314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICA 356
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 17-319 1.36e-103

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: 308.04  E-value: 1.36e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  17 VGVGMTKFVKPGaenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------------ 66
Cdd:cd00829   1 VGVGMTPFGRRS---DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAggrfqsfpgaliaeylgllgkpatrveaag 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  67 ----------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLInkYGLSAhpvaPQMFGYAGKEHMEKY 130
Cdd:cd00829  78 asgsaavraaaaaiasGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPP--GGLTP----PALYALAARRYMHRY 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775 131 GTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqsKAVEI 210
Cdd:cd00829 152 GTTREDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTD--RPVWI 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775 211 LAQEMMTDLPSSFEEKSiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRG 290
Cdd:cd00829 230 LGVGAASDTPSLSERDD---FLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREG 306

                       330       340
                ....*....|....*....|....*....
gi 55956775 291 DNTYGGKWVINPSGGLISKGHPLGATGGH 319
Cdd:cd00829 307 DTAIGGDLPVNTSGGLLSKGHPLGATGLA 335
PRK06064 PRK06064
thiolase domain-containing protein;
11-317 6.21e-67

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 214.76  E-value: 6.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   11 LRRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQ-------------------------------------IP 53
Cdd:PRK06064   1 MRDVAIIGVGQTKF---GELWDVSLRDLAVEAGLEALEDAGidgkdidamyvgnmsaglfvsqehiaaliadyaglapIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   54 YSAVDQAC--------VGYVF---GVAECVLALGFEKMSKgslgikfsdrtIPTDKHVDLLI--------NKYGLSAhpv 114
Cdd:PRK06064  78 ATRVEAACasggaalrQAYLAvasGEADVVLAAGVEKMTD-----------VPTPDATEAIAragdyeweEFFGATF--- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  115 aPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILAS 194
Cdd:PRK06064 144 -PGLYALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILAS 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  195 EAFVQKYglQSKAVEILAQEMMTDLPSSFEEKSIikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 274
Cdd:PRK06064 223 EEKAKEY--TDTPVWIKASGQASDTIALHDRKDF---TTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYED 297

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 55956775  275 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK06064 298 LGFAKKGEGGKLAREGQTYIGGDIPVNPSGGLKAKGHPVGATG 340
PRK12578 PRK12578
thiolase domain-containing protein;
12-317 3.71e-50

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 171.18  E-value: 3.71e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYV-------------------------- 65
Cdd:PRK12578   1 RRVAVIGVGNSKF---GRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTayrgielypapivaeysgltgkvplr 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   66 --------------------FGVAECVLALGFEKMSK----GSLGIKFSDRTIPTDKHvdllinKYGLSAhpvaPQMFGY 121
Cdd:PRK12578  78 veamcatglaasltaytavaSGLVDMAIAVGVDKMTEvdtsTSLAIGGRGGNYQWEYH------FYGTTF----PTYYAL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK12578 148 YATRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKEL 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  202 GLQSkAVEILAQEMMTDLpSSFEEKsiIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEG 281
Cdd:PRK12578 228 KIDS-PVWITGIGYANDY-AYVARR--GEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKG 303

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 55956775  282 QGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK12578 304 KGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATG 339
PRK07516 PRK07516
thiolase domain-containing protein;
13-317 2.78e-40

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 145.09  E-value: 2.78e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   13 RVFVVGVGMTKFVKPGAEnsrDYPDLAEEAGKKALADAQIPYSAVDQACVGyVF-------------------------- 66
Cdd:PRK07516   3 TASIVGWAHTPFGKLDAE---TLESLIVRVAREALAHAGIAAGDVDGIFLG-HFnagfspqdfpaslvlqadpalrfkpa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   67 -----------------------GVAECVLALGFEKMSkgslgikfsdrTIPTDKHVDLLIN-KYGLSAHPVA---PQMF 119
Cdd:PRK07516  79 trvenacatgsaavyaaldaieaGRARIVLVVGAEKMT-----------ATPTAEVGDILLGaSYLKEEGDTPggfAGVF 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  120 GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKE----VFDFLTILQCCPTSDGAAAAILASE 195
Cdd:PRK07516 148 GRIAQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEFCRTVSEknplVAGPLRRTDCSLVSDGAAALVLADA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  196 AFVQKYglqSKAVEILAQEMMTD-LPSSFEEksiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 274
Cdd:PRK07516 228 ETARAL---QRAVRFRARAHVNDfLPLSRRD-----PLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEA 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 55956775  275 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK07516 300 MGLAPPGQGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATG 342
PRK06365 PRK06365
thiolase domain-containing protein;
8-317 1.39e-35

thiolase domain-containing protein;


Pssm-ID: 235785 [Multi-domain]  Cd Length: 430  Bit Score: 133.50  E-value: 1.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775    8 PATLRRVFVVGVGMTKFVKpgAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGY----------------------- 64
Cdd:PRK06365  12 KKKSRDVYMVAAGVTKFDK--ASPYMDFRERVKKAFDYAMNDAGLTLADIDGSVASYfsdhfqrqllagimvqdylglvp 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   65 ------------------------VFGVAECVLALGFEKMSKgslgikfsdrtIPTDKHvdlliNKY-GLSA-----HPV 114
Cdd:PRK06365  90 kpskriegggatgglafqagyeeiASGRMDCVAVYGFETMSH-----------VNTWKG-----NEFiALASdtnfdYPL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  115 APQMFGY---AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAI 191
Cdd:PRK06365 154 GGFYTGYyamMAVRHMYEFGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAI 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  192 LASEAfvQKYGLQSKAVEILAQEMMTD--------------LPSsfEEKSIIK------MVGFDMSKEAARKCYEKSGLT 251
Cdd:PRK06365 234 LASED--KAFEITDKPVLIKAIGTGSDtlrladrpfgevplLPN--ESPDDYKdlrypgVHSFRAGRMAAKEAYEMAGIT 309

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  252 P--NDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK06365 310 DplNDLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATG 377
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
 12-317 3.51e-35

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 131.69  E-value: 3.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQI-----------------------------------PYSA 56
Cdd:PRK06157   7 DKVAILGMGCTKF---GERWDAGAEDLMVEAFLEALADAGIepkdidaawfgthydeigsgksgtplsralrlpniPVTR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   57 VDQACV-------GYVFGVA----ECVLALGFEK-MSKGSLGIKFSDRTIPTDkhvdllinkyGLSAHPVAPQMFGYAGK 124
Cdd:PRK06157  84 VENFCAtgseafrGAVYAVAsgayDIALALGVEKlKDTGYGGLPVANPGTLAD----------MTMPNVTAPGNFAQLAS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  125 EHMEKYGTKIEHF----AKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQK 200
Cdd:PRK06157 154 AYAAKYGVSREDLkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  201 YGlQSKAVEILAQEMMTdlpSSFEEksiIKMVGFDMS-----KEAARKCYEKSGLT-P-NDIDVIELHDCFSTNELLTYE 273
Cdd:PRK06157 234 LG-KKDPVYVKALQLAV---SNGWE---LQYNGWDGSyfpttRIAARKAYREAGITdPrEELSMAEVHDCFSITELVTME 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 55956775  274 ALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK06157 307 DLGLSERGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASG 350
PRK06059 PRK06059
lipid-transfer protein; Provisional
 10-310 3.64e-35

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 131.42  E-value: 3.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   10 TLRRVFVVGVGMTKFVKPGaensRDYPDLAEEAGKKALADAQIPYSAVdQACV----------GYVF------------- 66
Cdd:PRK06059   2 MPEPVYILGAGMHPWGKWG----RDFVEYGVVAARAALADAGLDWRDV-QLVVgadtirngypGFVAgatfaqalgwnga 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   67 -------------------------GVAECVLALGFEKMSKGSLGIKFSDRtiPTDKhvDLLINKYGLSAHPVapqMFGY 121
Cdd:PRK06059  77 pvsssyaacasgsqalqsaraqilaGLCDVALVVGADTTPKGFFAPVGGER--PDDP--DWLRFHLIGATNPV---YFAL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK06059 150 LARRRMDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSFARRH 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  202 GLQSK-AVEILAQEMMT--------DLPsSFEEKSIIKMVGFDMS--KEAARKCYEKSGLTPNDIDVIELHDCFSTNELL 270
Cdd:PRK06059 230 LGSVAgVPSVRAISTVTprypqhlpELP-DIATDSTAAVPAPERVfkDQILDAAYAEAGIGPEDLSLAEVYDLSTALELD 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 55956775  271 TYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKG 310
Cdd:PRK06059 309 WYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFG 348
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
 14-317 1.21e-29

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 116.71  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   14 VFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFG-------------------------- 67
Cdd:PRK06289   5 VWVLGGYQSDFARNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGelfagqghlgampatvhpalwgvpas 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   68 ----------VA-------------ECVLALGFEKMskgslgikfsdRTIPTDKHVDLL-----INKYGLSAHPVAPQMF 119
Cdd:PRK06289  85 rheaacasgsVAtlaamadlragryDVALVVGVELM-----------KTVPGDVAAEHLgaaawTGHEGQDARFPWPSMF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  120 GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-----FQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILAS 194
Cdd:PRK06289 154 ARVADEYDRRYGLDEEHLRAIAEINFANARRNPNAQtrgwaFPDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLAS 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  195 EAFVQKYGLQSKAVEILAQEMMTdLPSSFEEKsIIKMVG----FDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELL 270
Cdd:PRK06289 234 DAYLRDYADARPIPRIKGWGHRT-APLGLEQK-LDRSAGdpyvLPHVRQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYL 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 55956775  271 TYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK06289 312 AIDHIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASG 358
PRK08313 PRK08313
thiolase domain-containing protein;
12-317 6.54e-26

thiolase domain-containing protein;


Pssm-ID: 181378 [Multi-domain]  Cd Length: 386  Bit Score: 105.97  E-value: 6.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   12 RRVFVVGVGMTKFVKPGAENSrdYPDLAEEAGKKALADAQIPYSAVD--------------------------------- 58
Cdd:PRK08313   3 RLAAVLGTGQTKYVAKRQDVS--MAGLVREAIDRALADAGLTWDDIDavvvgkapdffegvmmpelfladalgatgkpli 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   59 -----------QACVGYVF---GVAECVLALGFEKMSKGSLGIKFSdrtIPTDKHVDLLINKYGLSAHPVApqmfgyagk 124
Cdd:PRK08313  81 rvhtagsvggsTAVVAASLvqsGVYRRVLAVAWEKQSESNAMWALS---IPVPFTKPVGAGAGGYFAPHVR--------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  125 EHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQF-QDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGL 203
Cdd:PRK08313 149 AYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLhQPDITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  204 QSKAVeILAQEMMTDlPSSFEEKSIIKMVGfdmSKEAARKCYEKSGLT-P-NDIDVIELHDCFSTNELLTYEALGLCPEG 281
Cdd:PRK08313 229 RPVAW-IHGTAMRTE-PLAFAGRDQVNPQA---GRDAAAALWKAAGITdPrDEIDVAEIYVPFSWFEPMWLENLGFAPEG 303

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 55956775  282 QGATLVDRGDNTYGGKWVINPSGGLISkGHPLGATG 317
Cdd:PRK08313 304 EGWKLTEAGETAIGGRLPVNPSGGVLS-SNPIGASG 338
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 181-317 5.47e-25

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: 100.98  E-value: 5.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775 181 CPTSDGAAAAILASEAFVQKYGLQskaveilAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIEL 260
Cdd:cd00327  98 FVFGDGAAAAVVESEEHALRRGAH-------PQAEIVSTAATFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEA 170

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 55956775 261 HDCFSTNELLTYEALGLCPEGQGAtlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:cd00327 171 HGTGTPIGDAVELALGLDPDGVRS---------------PAVSATLIMTGHPLGAAG 212
PRK06158 PRK06158
thiolase; Provisional
 113-312 3.14e-23

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 98.56  E-value: 3.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  113 PVAPqMFGYA--GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAaa 190
Cdd:PRK06158 137 PVNP-VSAYAlaAARHMHQYGTTREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAG-- 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  191 ilaseafvqkyglqskAVEILAQEMMTDLP----------SSFEEKSIIKMVgfDMSKEAA----RKCYEKSGLTPNDID 256
Cdd:PRK06158 214 ----------------AVVMVRADRARDLPrppvyvlgaaAATWHRQISSMP--DLTVTAAaesgPRAFAMAGLTPADID 275

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 55956775  257 VIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHP 312
Cdd:PRK06158 276 VVELYDAFTINTILFLEDLGFCAKGEGGAFVEGGRIAPGGRLPVNTNGGGLSCVHP 331
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
 129-317 1.10e-22

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 97.66  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  129 KYGTKIEHF-----AKIGWKNHKHSVNNPYSQ-FQDEYSLDEV----------MASKEVFDFLTILQCCPTSDGAAAAIL 192
Cdd:PTZ00455 188 KYIQEHGHFtmedtARVAAKAYANGNKNPLAHmHTRKLSLEFCtgasdknpkfLGNETYKPFLRMTDCSQVSDGGAGLVL 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  193 ASEAFVQKYGLQ---SKAVEILAQEM-MTDLPSSFEEKSiiKMVgfdMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNE 268
Cdd:PTZ00455 268 ASEEGLQKMGLSpndSRLVEIKSLACaSGNLYEDPPDAT--RMF---TSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAE 342

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 55956775  269 LLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PTZ00455 343 LLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATG 391
PRK06066 PRK06066
thiolase domain-containing protein;
127-318 5.20e-22

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 95.20  E-value: 5.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  127 MEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYglQSK 206
Cdd:PRK06066 154 MSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKL--TDD 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  207 AVEILAQEMMTDlPSSFEEKSIIKMVgfdMSKEAARKCYEKSGLTP--NDIDVIELHDCFSTNELLTYEALGLCPEGQGA 284
Cdd:PRK06066 232 PVWIKGIGWSTE-SSNLETAELGKAN---YMRIAADMAYKMAGIESprKEVDAAEVDDRYSYKELQHIEALRLSEEPEKD 307

                        170       180       190
                 ....*....|....*....|....*....|....
gi 55956775  285 TLVDRGDNTYGGKWVINPSGGLISKGHPLGATGG 318
Cdd:PRK06066 308 SLLREGNFDPQGELPVNPSGGHLAKGVPLEASGL 341
PRK07855 PRK07855
lipid-transfer protein; Provisional
 16-308 6.87e-21

lipid-transfer protein; Provisional


Pssm-ID: 181147 [Multi-domain]  Cd Length: 386  Bit Score: 91.96  E-value: 6.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   16 VVGVGMTKFVKpgaENSRDYPDLAEEAGKKALADA------------------------------------QIPY----- 54
Cdd:PRK07855   8 IVGIGATEFSK---NSGRSELRLACEAVLAALDDAglapsdvdglvtftmdtnpeiavaralgigelkffsRIHYgggaa 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   55 -SAVDQACVGYVFGVAECVLAlgFEKMSKGSlGIKFS--DRTIPTDKHVDLLINK----YGLS--AHPVApqMFGyagKE 125
Cdd:PRK07855  85 cATVQQAAMAVATGVADVVVC--YRAFNERS-GMRFGqgQTGLAENPTSTGVDYGwsypHGLLtpAAWVA--MLA---RR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  126 HMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDE-YSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKygLQ 204
Cdd:PRK07855 157 YMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRpITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAERARD--LK 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  205 SKAVEILA--------QEMMT----DLPSSFEEKSIikmvgfdmskeAARKCYEKSGLTPNDIDVIELHDCFSTNELLTY 272
Cdd:PRK07855 235 QRPAVIKAaaqgsgadQYMMTsyyrDDITGLPEMGL-----------VARQLWAQSGLGPADIDTAILYDHFTPFVLMQL 303

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 55956775  273 EALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLIS 308
Cdd:PRK07855 304 EELGFCGRGEAKDFIADGALELGGRLPINTHGGQLG 339
PRK06065 PRK06065
thiolase domain-containing protein;
12-318 2.36e-18

thiolase domain-containing protein;


Pssm-ID: 180379 [Multi-domain]  Cd Length: 392  Bit Score: 84.88  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   12 RRVFVVGVGMTKFVKPGAENSRDypdLAEEAGKKALADAQIPYSAVDQACVGY--------------------------- 64
Cdd:PRK06065   9 KRVAVIGAGLTLFRRRLLETPQE---LAWEAASKALDEAGLELKDIDCVVIGSapdafdgvhmkgeylshgsggirkpvs 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   65 -VF-------------------GVAECVLALGFEKMSKGSLGIKFSDRTIptdkhVDLLINKyglsahPVAPQM---FGY 121
Cdd:PRK06065  86 rVYvggatgvmtaiagwyhvasGLCQKVLAVAEEKMSPARPHPQAVFRYI-----WDPILEK------PLNPNLiwiFAM 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK06065 155 EMHRYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRY 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  202 glqskaveilaqemmTDLPssfeekSIIKMVGFDMS---------------KEAARKCYEKSGLT-PN-DIDVIELHDCF 264
Cdd:PRK06065 235 ---------------TDTP------VWVEGVGWTLDntewpnrdlaypryvEFAARMAYKMAGIErPRkEIDVAEPYDPF 293

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55956775  265 STNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGG 318
Cdd:PRK06065 294 DYKELHHLEGLQLAKRGEAPKLLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGL 347
PRK08142 PRK08142
thiolase domain-containing protein;
112-312 3.05e-18

thiolase domain-containing protein;


Pssm-ID: 236164 [Multi-domain]  Cd Length: 388  Bit Score: 84.37  E-value: 3.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  112 HPVAPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGaaaai 191
Cdd:PRK08142 139 GPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDG----- 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  192 laseafvqkyglqSKAVEILAQEMMTDLpssfeEKSIIKMVG------------FDMSKEAAR----KCYEKSGLTPNDI 255
Cdd:PRK08142 214 -------------GGALVVVRPEIARSL-----KRPLVKVLGageaikgqmggkVDLTYSGAAwsgpAAFAEAGVTPADI 275

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  256 DVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYG-GKWVINPSGGLISKGHP 312
Cdd:PRK08142 276 KYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHP 333
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 240-318 2.35e-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: 67.12  E-value: 2.35e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55956775 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGG 318
Cdd:cd00751 290 AIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPE------------------KVNVNGGAIALGHPLGASGA 350
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
52-318 9.20e-12

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 65.13  E-value: 9.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   52 IPYSAVDQAC------VGYVF-----GVAECVLALGFEKMSKGSLG--------IKFSDRtiPTDKHVDLLInkyGLSAH 112
Cdd:PRK06445  86 IPAMAVDRQCasslttVSIGAmeiatGMADIVIAGGVEHMTRTPMGdnphiepnPKLLTD--PKYIEYDLTT---GYVMG 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  113 PVAPQMFGYAG--KEHMEKYGTKIEHFA----KIGW-----------KNHKHSVNNPYSQFQDEYSLDEVMASKEVFD-- 173
Cdd:PRK06445 161 LTAEKLAEEAGikREEMDRWSLRSHQLAakaiQEGYfkdeilpieveVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKpd 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  174 -FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVeilaqemmtdlpssfeeksiIKMVGFD------MSK---EAARK 243
Cdd:PRK06445 241 gVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAK--------------------IRSFGFAgvppaiMGKgpvPASKK 300

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55956775  244 CYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGG 318
Cdd:PRK06445 301 ALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPE------------------TVNIKGGAIAIGHPLGATGA 357
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 240-317 2.15e-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: 2.15e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775   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 ...
 239-318 2.86e-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: 60.70  E-value: 2.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775   239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGG 318
Cdd:TIGR01930 289 PAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASGA 350
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
240-318 1.55e-09

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 58.36  E-value: 1.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGG 318
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHD------------------KVNVNGGAIAMGHPLGATGA 365
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
 240-317 6.55e-09

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 56.50  E-value: 6.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlVDRGDNtyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK09050 302 ATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGL---------ADDDAR-------VNPNGGAIALGHPLGMSG 363
PRK09051 PRK09051
beta-ketothiolase BktB;
240-317 3.80e-08

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 54.20  E-value: 3.80e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK09051 297 ATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAK------------------VNPNGSGISLGHPVGATG 356
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
240-317 6.24e-08

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 53.56  E-value: 6.24e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK07801 285 ATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAK------------------VNPNGGAIALGHPLGATG 344
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
238-317 7.20e-08

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 53.47  E-value: 7.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  238 KEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK09052 300 IEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPS------------------KVNPLGGAIALGHPLGATG 361
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
240-318 5.45e-07

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 50.76  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  240 AARKCYEKSGLTPNDIDVIELhdcfstNELLTYEALGLCPE-GQGATLVDRgdntyggkwvINPSGGLISKGHPLGATGG 318
Cdd:PRK06205 303 ATEKALARAGLTLDDIDLIEL------NEAFAAQVLAVLKEwGFGADDEER----------LNVNGSGISLGHPVGATGG 366
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
185-317 7.46e-07

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 50.16  E-value: 7.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  185 DGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSsfeeksiikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCF 264
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPRA-RIVAMANMGDDPT----------LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAF 344

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55956775  265 STNELLTYEALGLcpegqgatlvDRGDntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK06025 345 AVVAEKFIRDLDL----------DRDK--------VNVNGGAIALGHPIGATG 379
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 181-318 9.01e-07

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: 9.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775 181 CPTSDGAAAAILASEAFVQKYGLQSKAvEILAQ-------EMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPN 253
Cdd:COG0183 246 SGINDGAAALLLMSEEAAKELGLKPLA-RIVAYavagvdpEIMGIGPV-----------------PATRKALARAGLTLD 307

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55956775 254 DIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGG 318
Cdd:COG0183 308 DIDLIEINEAFAAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGA 354
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 14-159 1.36e-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: 48.84  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775    14 VFVVGVGMTKFVK-PGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF-------------------------- 66
Cdd:pfam00108   1 VVIVSAARTPFGSfGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLqagegqnparqaalkagipdsapavt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775    67 ---------------------GVAECVLALGFEKMSKGSLGIKFSDR---TIPTDKHVDLLInKYGLSAHPVAPQMfGYA 122
Cdd:pfam00108  81 inkvcgsglkavylaaqsiasGDADVVLAGGVESMSHAPYALPTDARsglKHGDEKKHDLLI-PDGLTDAFNGYHM-GLT 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 55956775   123 GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDE 159
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGkFKDE 196
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
 246-317 1.55e-06

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 49.38  E-value: 1.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55956775  246 EKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PLN02287 342 KAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEK------------------VNVNGGAIALGHPLGATG 395
PRK05790 PRK05790
putative acyltransferase; Provisional
 240-317 2.00e-06

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 49.00  E-value: 2.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK05790 296 AIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPE------------------KVNVNGGAIALGHPIGASG 355
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
239-317 2.05e-06

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 49.01  E-value: 2.05e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55956775  239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatlVDRGDNTyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK08131 300 EAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLG----------VDFDDPR------VNPNGGAIAVGHPLGASG 362
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
161-317 3.64e-06

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 48.08  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  161 SLDEVMASKEVF---DFLTILQCCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikm 231
Cdd:PRK07851 237 TYEKVSQLKPVFrpdGTVTAGNACPLNDGAAAVVIMSDTKARELGLTplarivSTGVSGLSPEIMGLGPV---------- 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  232 vgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcPEgqgatlvDRgdntyggkwvINPSGGLISKGH 311
Cdd:PRK07851 307 -------EASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGI-DE-------DK----------LNVSGGAIALGH 361


                 ....*.
gi 55956775  312 PLGATG 317
Cdd:PRK07851 362 PFGMTG 367
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
240-318 1.57e-05

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 46.24  E-value: 1.57e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGG 318
Cdd:PRK08235 296 AINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPE------------------KVNVNGGAVALGHPIGASGA 356
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
 240-317 1.81e-05

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 45.73  E-value: 1.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatLVDRGDNTyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK08947 287 ATQKALKRAGLSISDIDVFELNEAFAAQSLPCLKDLG---------LLDKMDEK------VNLNGGAIALGHPLGCSG 349
PRK07937 PRK07937
lipid-transfer protein; Provisional
 237-317 5.11e-05

lipid-transfer protein; Provisional


Pssm-ID: 181173 [Multi-domain]  Cd Length: 352  Bit Score: 44.29  E-value: 5.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  237 SKEAARKCyekSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlvdrGDNTyggkwVINPSGGLISkGHPLGAT 316
Cdd:PRK07937 252 TALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALGL------------GDKT-----KVNPSGGALA-ANPMFAA 310


                 .
gi 55956775  317 G 317
Cdd:PRK07937 311 G 311
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
240-317 6.72e-05

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 44.11  E-value: 6.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK05656 296 ATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAA------------------KVNVNGGAIALGHPIGASG 355
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
240-318 8.91e-05

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 43.87  E-value: 8.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALglcpegqgatlvdrgdntyggKW---VINPSGGLISKGHPLGAT 316
Cdd:PRK06633 295 ASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREM---------------------KWdmeKVNINGGAIAIGHPIGAS 353


                 ..
gi 55956775  317 GG 318
Cdd:PRK06633 354 GG 355
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
240-317 4.16e-04

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 41.64  E-value: 4.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK06504 293 ATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPER------------------LNVNGGAIALGHPLGASG 352
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
 240-317 1.25e-03

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 40.08  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55956775  240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PLN02644 296 AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEK------------------VNVHGGAVSLGHPIGCSG 355
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
183-317 2.14e-03

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 39.35  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  183 TSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPNDID 256
Cdd:PRK07661 248 MSDGAAAVLLMDREKAESDGLKplakfrSFAVAGVPPEVMGIGPI-----------------AAIPKALKLAGLELSDIG 310

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55956775  257 VIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK07661 311 LFELNEAFASQSIQVIRELGLDEE------------------KVNVNGGAIALGHPLGCTG 353
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 235-258 2.77e-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: 39.06  E-value: 2.77e-03
                        10        20
                ....*....|....*....|....
gi 55956775 235 DMSKEAARKCYEKSGLTPNDIDVI 258
Cdd:cd00830  52 DLAVEAAKKALEDAGIDADDIDLI 75
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
246-318 3.21e-03

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 39.11  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956775  246 EKSGLTPNDIDVIELHDCFSTNELLT---YEALGLCPE--GQGATL--VDRGDntyggkwvINPSGGLISKGHPLGATGG 318
Cdd:PRK09268 320 ARNGLTLQDFDFYEIHEAFASQVLATlkaWEDEEYCRErlGLDAPLgsIDRSK--------LNVNGSSLAAGHPFAATGG 391
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 235-258 6.25e-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: 6.25e-03
                        10        20
                ....*....|....*....|....
gi 55956775 235 DMSKEAARKCYEKSGLTPNDIDVI 258
Cdd:COG0332  53 DLAVEAARKALEAAGIDPEDIDLI 76
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
235-258 9.41e-03

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 37.36  E-value: 9.41e-03
                         10        20
                 ....*....|....*....|....
gi 55956775  235 DMSKEAARKCYEKSGLTPNDIDVI 258
Cdd:PRK09352  54 DLATEAAKKALEAAGIDPEDIDLI 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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