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Conserved domains on  [gi|45476581|ref|NP_035457|]
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sterol carrier protein 2 [Mus musculus]

Protein Classification

hydroxysteroid dehydrogenase-like protein 2( domain architecture ID 11483191)

hydroxysteroid dehydrogenase-like protein 2 (HSDL2) may be involved in in fatty acid metabolism, as well as in cholesterol metabolism and homeostasis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08256 PRK08256
lipid-transfer protein; Provisional
12-404 0e+00

lipid-transfer protein; Provisional


:

Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 719.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   12 RRVFVVGVGMTKFMKPGgeNSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHsLGLTGIPIINVN 91
Cdd:PRK08256   1 NKVFVAGVGMTPFEKPG--ASWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYGDSTSGQRALYE-VGMTGIPIVNVN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   92 NNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKEHM 171
Cdd:PRK08256  78 NNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  172 EKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLqSKA 251
Cdd:PRK08256 158 EKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  252 VEIVAQEMMTDLPSTFEEKSIIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLV 331
Cdd:PRK08256 237 VEIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFI 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45476581  332 DRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLYR 404
Cdd:PRK08256 317 DDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLGGACVVTLYQ 389
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
452-538 4.39e-32

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


:

Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 118.90  E-value: 4.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   452 VKKIGG-IFAFKVKDGPGgkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMG 530
Cdd:pfam02036  15 LKKLNGkVIRFDLTDLGL----SLTLDLKDGGGRVLAGDEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDME 90

                  ....*...
gi 45476581   531 LAMKLQNL 538
Cdd:pfam02036  91 LAQKLEGL 98
 
Name Accession Description Interval E-value
PRK08256 PRK08256
lipid-transfer protein; Provisional
12-404 0e+00

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 719.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   12 RRVFVVGVGMTKFMKPGgeNSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHsLGLTGIPIINVN 91
Cdd:PRK08256   1 NKVFVAGVGMTPFEKPG--ASWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYGDSTSGQRALYE-VGMTGIPIVNVN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   92 NNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKEHM 171
Cdd:PRK08256  78 NNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  172 EKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLqSKA 251
Cdd:PRK08256 158 EKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  252 VEIVAQEMMTDLPSTFEEKSIIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLV 331
Cdd:PRK08256 237 VEIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFI 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45476581  332 DRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLYR 404
Cdd:PRK08256 317 DDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLGGACVVTLYQ 389
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
17-403 0e+00

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: 594.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  17 VGVGMTKFMKPGGENSRDYPDMAKEAGQKALEDAQIPYS----AVEQACVGYVYGD---STSGQRAIYHSLGLTGIPIIN 89
Cdd:cd00826   1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLGAgegQNCAQQAAMHAGGLQEAPAIG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  90 VNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMErgsigtkFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKE 169
Cdd:cd00826  81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 170 HMEKYGTKVEHFAKIGWKN---HKHSVNNTYSQFQDEYSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQ 243
Cdd:cd00826 154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 244 QYGLQSKAVEIVAQEMMTDLPSTFEEKSIIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCP 323
Cdd:cd00826 234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 324 EGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLY 403
Cdd:cd00826 314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQGAGAGLALLCIGGGGGAAMCIES 393
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
452-538 4.39e-32

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 118.90  E-value: 4.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   452 VKKIGG-IFAFKVKDGPGgkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMG 530
Cdd:pfam02036  15 LKKLNGkVIRFDLTDLGL----SLTLDLKDGGGRVLAGDEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDME 90

                  ....*...
gi 45476581   531 LAMKLQNL 538
Cdd:pfam02036  91 LAQKLEGL 98
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
22-400 2.85e-29

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: 119.25  E-value: 2.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581    22 TKFMKPGGENSRDYP-DMAKEAGQKALEDAQIPYSAVEQACVGYVygDSTSGQR------AIYHSLGLTgIPIINVNNNC 94
Cdd:TIGR01930   7 TPIGKFGGSLKDVSAeDLGAAVIKELLERNPLDPELIDDVIFGNV--LQAGEQQniarqaALLAGLPES-VPAYTVNRQC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581    95 STGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKEHMEKY 174
Cdd:TIGR01930  84 ASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDARLKDLTDANTGLPMGVTAENLAKKY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   175 G-TKVE--HFA----KIGWKNHK-------------HSVNNTYSQFQDE-----YSLEEVMKSKPVFD---FLTILQCCP 226
Cdd:TIGR01930 164 GiSREEqdEYAlrshQRAAKAWEeglfkdeivpvtvKGRKGPVTVSSDEgirpnTTLEKLAKLKPAFDpdgTVTAGNSSP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   227 TSDGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFeeksiikvvGYdMSKEAARRCYEKSGLTPNDVDVIELHD 306
Cdd:TIGR01930 244 LNDGAAALLLMSEEKAKELGLTPLA-RIVSFAVAGVDPEIM---------GL-GPVPAIPKALKKAGLSISDIDLFEINE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   307 CFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakV 386
Cdd:TIGR01930 313 AFAAQVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGL----A 370
                         410
                  ....*....|....
gi 45476581   387 ALQHNLGLGGAVVV 400
Cdd:TIGR01930 371 TMCIGGGQGAAVIL 384
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
453-538 1.66e-24

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 97.67  E-value: 1.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 453 KKIGGIFAFKVKDGPGGkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMGLA 532
Cdd:COG3255  18 AGWDGVVQFVITGEGGG---AYYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLA 94

                ....*.
gi 45476581 533 MKLQNL 538
Cdd:COG3255  95 MKLMSL 100
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
12-400 1.31e-22

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: 99.76  E-value: 1.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  12 RRVFVVGVGMTKFMKPGGE-NSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVygdSTSGQ-----RAIYHSLGL-TG 84
Cdd:COG0183   2 REVVIVDAVRTPFGRFGGAlADVRADDLGAAVIKALLERAGLDPEAVDDVILGCV---LQAGQgqnpaRQAALLAGLpES 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  85 IPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFG 164
Cdd:COG0183  79 VPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMINPGLTDPYTGLSMGE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 165 YAgkEHM-EKYG-TKVE-------------------HFAK------IGWKNHKHSVNntysqfQDEY-----SLEEVMKS 212
Cdd:COG0183 159 TA--ENVaERYGiSREEqdafalrshqraaaaiaagRFDDeivpveVPDRKGEVVVD------RDEGprpdtTLEKLAKL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 213 KPVFD---FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAvEIVAQ-------EMMTDLPStfeeksiikvvgydmsk 282
Cdd:COG0183 231 KPAFKkdgTVTAGNASGINDGAAALLLMSEEAAKELGLKPLA-RIVAYavagvdpEIMGIGPV----------------- 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 283 EAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGL 362
Cdd:COG0183 293 PATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGA 354
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 45476581 363 AQCAELCWQLRGEAGKRQVpgakVALQHNLGLGGAVVV 400
Cdd:COG0183 355 RILVTLLHELERRGGRYGL----ATMCIGGGQGIALII 388
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
14-240 2.29e-18

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: 85.05  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581    14 VFVVGVGMTKFMKPGGeNSRDYP--DMAKEAGQKALEDAQIPYSAVEQACVGYVyGDSTSGQ---RAIYHSLGLT-GIPI 87
Cdd:pfam00108   1 VVIVSAARTPFGSFGG-SLKDVSavELGAEAIKAALERAGVDPEDVDEVIVGNV-LQAGEGQnpaRQAALKAGIPdSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581    88 INVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDR---TTPTDKHIEVLIdKYGLSAHPITPQMfG 164
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARsglKHGDEKKHDLLI-PDGLTDAFNGYHM-G 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   165 YAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQ-FQDE------------------------YSLEEVMKSKPVFD-- 217
Cdd:pfam00108 157 LTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGkFKDEivpvtvkgrkgkptvdkdegirppTTAEPLAKLKPAFDke 236
                         250       260
                  ....*....|....*....|....
gi 45476581   218 -FLTILQCCPTSDGAAAAILSSEE 240
Cdd:pfam00108 237 gTVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
PRK08256 PRK08256
lipid-transfer protein; Provisional
12-404 0e+00

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 719.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   12 RRVFVVGVGMTKFMKPGgeNSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHsLGLTGIPIINVN 91
Cdd:PRK08256   1 NKVFVAGVGMTPFEKPG--ASWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYGDSTSGQRALYE-VGMTGIPIVNVN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   92 NNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKEHM 171
Cdd:PRK08256  78 NNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  172 EKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLqSKA 251
Cdd:PRK08256 158 EKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  252 VEIVAQEMMTDLPSTFEEKSIIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLV 331
Cdd:PRK08256 237 VEIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFI 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45476581  332 DRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLYR 404
Cdd:PRK08256 317 DDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLGGACVVTLYQ 389
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
17-403 0e+00

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: 594.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  17 VGVGMTKFMKPGGENSRDYPDMAKEAGQKALEDAQIPYS----AVEQACVGYVYGD---STSGQRAIYHSLGLTGIPIIN 89
Cdd:cd00826   1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLGAgegQNCAQQAAMHAGGLQEAPAIG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  90 VNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMErgsigtkFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKE 169
Cdd:cd00826  81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 170 HMEKYGTKVEHFAKIGWKN---HKHSVNNTYSQFQDEYSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQ 243
Cdd:cd00826 154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 244 QYGLQSKAVEIVAQEMMTDLPSTFEEKSIIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCP 323
Cdd:cd00826 234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 324 EGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLY 403
Cdd:cd00826 314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQGAGAGLALLCIGGGGGAAMCIES 393
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
17-403 1.29e-163

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: 469.82  E-value: 1.29e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  17 VGVGMTKFMKPGGensRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGD---STSGQRAIYHsLGLTGIPIINVNNN 93
Cdd:cd00829   1 VGVGMTPFGRRSD---RSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGrfqSFPGALIAEY-LGLLGKPATRVEAA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  94 CSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIdkYGLSAhpitPQMFGYAGKEHMEK 173
Cdd:cd00829  77 GASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPP--GGLTP----PALYALAARRYMHR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 174 YGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLqsKAVE 253
Cdd:cd00829 151 YGTTREDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTD--RPVW 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 254 IVAQEMMTDLPSTFEEKSIikvVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDR 333
Cdd:cd00829 229 ILGVGAASDTPSLSERDDF---LSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVRE 305
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 334 GDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLY 403
Cdd:cd00829 306 GDTAIGGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGTGSAAVVTI 375
PRK06064 PRK06064
thiolase domain-containing protein;
11-404 1.01e-105

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 322.23  E-value: 1.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   11 LRRVFVVGVGMTKFmkpGGENSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAI------YhsLGLTG 84
Cdd:PRK06064   1 MRDVAIIGVGQTKF---GELWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIaaliadY--AGLAP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   85 IPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMergsigtkfsdrttpTDKHIEVLIDKYGLSAHPITPQMFG 164
Cdd:PRK06064  76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKM---------------TDVPTPDATEAIARAGDYEWEEFFG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  165 ------YA--GKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAIL 236
Cdd:PRK06064 141 atfpglYAliARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVIL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  237 SSEEFVQQYglQSKAVEIVAQEMMTDLPSTFEEKSIikvVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITY 316
Cdd:PRK06064 221 ASEEKAKEY--TDTPVWIKASGQASDTIALHDRKDF---TTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAY 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  317 EALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEA--GKRQVPGAKVALQHNL-G 393
Cdd:PRK06064 296 EDLGFAKKGEGGKLAREGQTYIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAekGRQQVIGAGYGLTHNVgG 375
                        410
                 ....*....|.
gi 45476581  394 LGGAVVVTLYR 404
Cdd:PRK06064 376 TGHTAVVHILS 386
PRK12578 PRK12578
thiolase domain-containing protein;
12-404 5.63e-80

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 255.54  E-value: 5.63e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   12 RRVFVVGVGMTKFmkpGGENSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRA--IYHSLGLTGIPIIN 89
Cdd:PRK12578   1 RRVAVIGVGNSKF---GRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPApiVAEYSGLTGKVPLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   90 VNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMergsigtkfSDRTTPTDKHIEVLIDKYGLSAH---PITPQMFGYA 166
Cdd:PRK12578  78 VEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKM---------TEVDTSTSLAIGGRGGNYQWEYHfygTTFPTYYALY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  167 GKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYG 246
Cdd:PRK12578 149 ATRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKELK 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  247 LQSkAVEIVAQEMMTDLPSTFEEksiIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQ 326
Cdd:PRK12578 229 IDS-PVWITGIGYANDYAYVARR---GEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKGK 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  327 GGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAK-VALQHNLGLGG--AVVVTLY 403
Cdd:PRK12578 305 GGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKLQQPLKKyIGLVHNVGGTGhfAYVMILR 384

                 .
gi 45476581  404 R 404
Cdd:PRK12578 385 R 385
PRK06059 PRK06059
lipid-transfer protein; Provisional
10-401 1.03e-72

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 237.35  E-value: 1.03e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   10 RLRRVFVVGVGMtkfmKPGGENSRDYPDMAKEAGQKALEDAQIPY---------SAVEQACVGYVYGdSTSGQraiyhSL 80
Cdd:PRK06059   2 MPEPVYILGAGM----HPWGKWGRDFVEYGVVAARAALADAGLDWrdvqlvvgaDTIRNGYPGFVAG-ATFAQ-----AL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   81 GLTGIPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDkhievlidkyGLSAHPI-- 158
Cdd:PRK06059  72 GWNGAPVSSSYAACASGSQALQSARAQILAGLCDVALVVGADTTPKGFFAPVGGERPDDPD----------WLRFHLIga 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  159 -TPQMFGYAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILS 237
Cdd:PRK06059 142 tNPVYFALLARRRMDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVA 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  238 SEEFVQQYGLQSK-AVEIVAQEMMT--------DLPsTFEEKSIIKVVGYDMS--KEAARRCYEKSGLTPNDVDVIELHD 306
Cdd:PRK06059 222 SKSFARRHLGSVAgVPSVRAISTVTprypqhlpELP-DIATDSTAAVPAPERVfkDQILDAAYAEAGIGPEDLSLAEVYD 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  307 CFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKV 386
Cdd:PRK06059 301 LSTALELDWYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAGGRQVEGARV 380
                        410
                 ....*....|....*...
gi 45476581  387 ALQHNLGL---GGAVVVT 401
Cdd:PRK06059 381 GITANQGLfghGSSVIVA 398
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
12-393 1.51e-65

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 218.36  E-value: 1.51e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   12 RRVFVVGVGMTKFmkpgGEN-SRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHS--LGLTGIPII 88
Cdd:PRK06157   7 DKVAILGMGCTKF----GERwDAGAEDLMVEAFLEALADAGIEPKDIDAAWFGTHYDEIGSGKSGTPLSraLRLPNIPVT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   89 NVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEK-MERGSIGTKFSDRTTPTDKHIEvlidkyGLSAhpitPQMFGYAG 167
Cdd:PRK06157  83 RVENFCATGSEAFRGAVYAVASGAYDIALALGVEKlKDTGYGGLPVANPGTLADMTMP------NVTA----PGNFAQLA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  168 KEHMEKYGTKVEHF----AKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQ 243
Cdd:PRK06157 153 SAYAAKYGVSREDLkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIAR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  244 QYG----LQSKAVEIVA---QEMMTDlpstfeeksiikvvGYDMS-----KEAARRCYEKSGLT-P-NDVDVIELHDCFS 309
Cdd:PRK06157 233 ALGkkdpVYVKALQLAVsngWELQYN--------------GWDGSyfpttRIAARKAYREAGITdPrEELSMAEVHDCFS 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  310 VNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQ 389
Cdd:PRK06157 299 ITELVTMEDLGLSERGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQLKNPRLALT 378

                 ....
gi 45476581  390 HNLG 393
Cdd:PRK06157 379 HNLG 382
PRK07516 PRK07516
thiolase domain-containing protein;
13-398 1.29e-62

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 210.19  E-value: 1.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   13 RVFVVGVGMTKFMKPGGEnsrDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYG----DSTSGQRAIYHSLGLTGIPII 88
Cdd:PRK07516   3 TASIVGWAHTPFGKLDAE---TLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAgfspQDFPASLVLQADPALRFKPAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   89 NVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERgsigtkfsdrtTPTDKHIEVLID-KYGLSAHPIT---PQMFG 164
Cdd:PRK07516  80 RVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTA-----------TPTAEVGDILLGaSYLKEEGDTPggfAGVFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  165 YAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLE---EVMKSKP-VFDFLTILQCCPTSDGAAAAILSSEE 240
Cdd:PRK07516 149 RIAQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEfcrTVSEKNPlVAGPLRRTDCSLVSDGAAALVLADAE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  241 FVQQYglqSKAVEIVAQEMMTD-LPstfeeksiikvvgydMSK------EAARRC----YEKSGLTPNDVDVIELHDCFS 309
Cdd:PRK07516 229 TARAL---QRAVRFRARAHVNDfLP---------------LSRrdplafEGPRRAwqraLAQAGVTLDDLSFVETHDCFT 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  310 VNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQ 389
Cdd:PRK07516 291 IAELIEYEAMGLAPPGQGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAGGMQIPGAKLAGV 370

                 ....*....
gi 45476581  390 HNLGlGGAV 398
Cdd:PRK07516 371 FNMG-GAAV 378
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
36-401 1.86e-61

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: 203.06  E-value: 1.86e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  36 PDMAKEAGQKALEDAQIPYSAVEQACVGYVYGD---STSGQRAIYHsLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGL 112
Cdd:cd00327   8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSgefSGAAGQLAYH-LGISGGPAYSVNQACATGLTALALAVQQVQNGK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 113 ANCVLALGFEKmergsigtkfsdrttptdkhievlidkyglsahpitpqmfgyagkehmekygtkvehfakigwknhkhs 192
Cdd:cd00327  87 ADIVLAGGSEE--------------------------------------------------------------------- 97
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 193 vnntysqfqdeysleevmkskpvfdfltilqcCPTSDGAAAAILSSEEFVQQYGlqskaveIVAQEMMTDLPSTFEEKSI 272
Cdd:cd00327  98 --------------------------------FVFGDGAAAAVVESEEHALRRG-------AHPQAEIVSTAATFDGASM 138
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 273 IKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGtlvdrgdntyggkwvINPSGGLIS 352
Cdd:cd00327 139 VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRS---------------PAVSATLIM 203
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 45476581 353 KGHPLGATGLAQCAELCWQLRGEAGK--RQVPGAKVALQHNLGLGGAVVVT 401
Cdd:cd00327 204 TGHPLGAAGLAILDELLLMLEHEFIPptPREPRTVLLLGFGLGGTNAAVVL 254
PRK06365 PRK06365
thiolase domain-containing protein;
6-402 1.96e-59

thiolase domain-containing protein;


Pssm-ID: 235785 [Multi-domain]  Cd Length: 430  Bit Score: 203.22  E-value: 1.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581    6 LKSPRLRR-VFVVGVGMTKFMKPGGENsrDYPDMAKEAGQKALEDAQIPYSAVEQACVGYV---YGDSTSGQRAIYHSLG 81
Cdd:PRK06365   9 LKMKKKSRdVYMVAAGVTKFDKASPYM--DFRERVKKAFDYAMNDAGLTLADIDGSVASYFsdhFQRQLLAGIMVQDYLG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   82 LTGIPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERgsigtkfsdrtTPTDKHIEVLidkyGLSA-----H 156
Cdd:PRK06365  87 LVPKPSKRIEGGGATGGLAFQAGYEEIASGRMDCVAVYGFETMSH-----------VNTWKGNEFI----ALASdtnfdY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  157 PITPQMFGY---AGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAA 233
Cdd:PRK06365 152 PLGGFYTGYyamMAVRHMYEFGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAAC 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  234 AILSSEEfvQQYGLQSKAVEIVAQEMMTD--------------LPStfEEKSIIK------VVGYDMSKEAARRCYEKSG 293
Cdd:PRK06365 232 AILASED--KAFEITDKPVLIKAIGTGSDtlrladrpfgevplLPN--ESPDDYKdlrypgVHSFRAGRMAAKEAYEMAG 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  294 LTP--NDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQ 371
Cdd:PRK06365 308 ITDplNDLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQ 387
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 45476581  372 LRGEAGKR------QVPGAKVALQH-NLGLGGAVVVTL 402
Cdd:PRK06365 388 LQGRIKKHfhddylQVKNAKRGLIHsHAGTGTYVTVTI 425
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
14-402 1.63e-47

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 170.25  E-value: 1.63e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   14 VFVVGVGMTKFMKPGGENSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQR------AIYHSlGLTGIPI 87
Cdd:PRK06289   5 VWVLGGYQSDFARNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGELFAGQGhlgampATVHP-ALWGVPA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   88 INVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMergsigtkfsdRTTPTDKHIEVL-----IDKYGLSAHPITPQM 162
Cdd:PRK06289  84 SRHEAACASGSVATLAAMADLRAGRYDVALVVGVELM-----------KTVPGDVAAEHLgaaawTGHEGQDARFPWPSM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  163 FGYAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQ-----FQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILS 237
Cdd:PRK06289 153 FARVADEYDRRYGLDEEHLRAIAEINFANARRNPNAQtrgwaFPDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  238 SEEFVQQY-------------------GLQSKAVEIVAQEMMtdLPSTfeeksiikvvgydmsKEAARRCYEKSGLTPND 298
Cdd:PRK06289 233 SDAYLRDYadarpiprikgwghrtaplGLEQKLDRSAGDPYV--LPHV---------------RQAVLDAYRRAGVGLDD 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  299 VDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGK 378
Cdd:PRK06289 296 LDGFEVHDCFTPSEYLAIDHIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGD 375
                        410       420
                 ....*....|....*....|....
gi 45476581  379 RQVPGAKVALQHNLGLGGAVVVTL 402
Cdd:PRK06289 376 YQVEGAKTFGTLNIGGSTTTTVSF 399
PRK08313 PRK08313
thiolase domain-containing protein;
12-397 2.95e-47

thiolase domain-containing protein;


Pssm-ID: 181378 [Multi-domain]  Cd Length: 386  Bit Score: 169.14  E-value: 2.95e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   12 RRVFVVGVGMTKFMKPGGENSrdYPDMAKEAGQKALEDAQIPYSAVEQACVGY---VYGDSTSGQRAIYHSLGLTGIPII 88
Cdd:PRK08313   3 RLAAVLGTGQTKYVAKRQDVS--MAGLVREAIDRALADAGLTWDDIDAVVVGKapdFFEGVMMPELFLADALGATGKPLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   89 NVNNNCSTG-STALFMAHqLIQGGLANCVLALGFEKMERGSigtkfsdrttptdkhievliDKYGLSAH-PITPQMFGYA 166
Cdd:PRK08313  81 RVHTAGSVGgSTAVVAAS-LVQSGVYRRVLAVAWEKQSESN--------------------AMWALSIPvPFTKPVGAGA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  167 G-------KEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQF-QDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSS 238
Cdd:PRK08313 140 GgyfaphvRAYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLhQPDITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  239 EEFVQQYGLQSKAVeIVAQEMMTDlPSTFEEKSiikVVGYDMSKEAARRCYEKSGLT-P-NDVDVIELHDCFSVNELITY 316
Cdd:PRK08313 220 EEAADAAAGRPVAW-IHGTAMRTE-PLAFAGRD---QVNPQAGRDAAAALWKAAGITdPrDEIDVAEIYVPFSWFEPMWL 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  317 EALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISkGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGlGG 396
Cdd:PRK08313 295 ENLGFAPEGEGWKLTEAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKAGEHQVDGARKALGHAYG-GG 372

                 .
gi 45476581  397 A 397
Cdd:PRK08313 373 S 373
PRK06158 PRK06158
thiolase; Provisional
37-396 1.25e-39

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 148.25  E-value: 1.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   37 DMAKEAGQKALEDAQIPYSAVEQACVGYVYgDSTSGQRAIYHslglTGIPIINVNNNCSTGSTalFMAH-----QLIQGG 111
Cdd:PRK06158  30 ELLAQAAHRALADAGLTMADVDGLFTASPD-DALWGLSVAEY----LGIRPRFVDGTMIGGSS--FLAHllpaaLALEAG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  112 LANCVL-ALGfekMERGSIGTKFSDRTTPTdkhievlidkygLSAHPITPQM----FGYAGKEHMEKYGTKVEHFAKIGW 186
Cdd:PRK06158 103 LCDVALiCYG---SNQRSAGGKLRSMLDPQ------------PYEAPYKPVNpvsaYALAAARHMHQYGTTREQLAEVAV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  187 KNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQqyGLQSKAVEIVAQEM------- 259
Cdd:PRK06158 168 AARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAVVMVRADRAR--DLPRPPVYVLGAAAatwhrqi 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  260 --MTDLPSTfeeksiikvvgydMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNT 337
Cdd:PRK06158 246 ssMPDLTVT-------------AAAESGPRAFAMAGLTPADIDVVELYDAFTINTILFLEDLGFCAKGEGGAFVEGGRIA 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 45476581  338 YGGKWVINPSGGLISKGHPlGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHnlGLGG 396
Cdd:PRK06158 313 PGGRLPVNTNGGGLSCVHP-GMYGLFLLIEAVRQLRGEAGERQVAGAEVALAH--GNGG 368
PRK06065 PRK06065
thiolase domain-containing protein;
12-382 9.66e-39

thiolase domain-containing protein;


Pssm-ID: 180379 [Multi-domain]  Cd Length: 392  Bit Score: 146.12  E-value: 9.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   12 RRVFVVGVGMTKFMKPGGENSRDypdMAKEAGQKALEDAQIPYSAVEQACVGYVyGDSTSG--QRAIYHSLGLTGI--PI 87
Cdd:PRK06065   9 KRVAVIGAGLTLFRRRLLETPQE---LAWEAASKALDEAGLELKDIDCVVIGSA-PDAFDGvhMKGEYLSHGSGGIrkPV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   88 INVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMErgsigtkfSDRTTPTD--KHI-EVLIDKyglsahPITPQM-- 162
Cdd:PRK06065  85 SRVYVGGATGVMTAIAGWYHVASGLCQKVLAVAEEKMS--------PARPHPQAvfRYIwDPILEK------PLNPNLiw 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  163 -FGYAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEF 241
Cdd:PRK06065 151 iFAMEMHRYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  242 VQQYglqskaveivaqemmTDLPSTfeeksiIKVVGYDMS---------------KEAARRCYEKSGLT-PN-DVDVIEL 304
Cdd:PRK06065 231 ARRY---------------TDTPVW------VEGVGWTLDntewpnrdlaypryvEFAARMAYKMAGIErPRkEIDVAEP 289
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45476581  305 HDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVP 382
Cdd:PRK06065 290 YDPFDYKELHHLEGLQLAKRGEAPKLLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGLMKVISIYWQLKGTAGKMQVK 367
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
10-396 4.19e-34

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 134.25  E-value: 4.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   10 RLRRVFVVGVGMTKFMKPGGEN--SRDYPDMAK-----------EAGQKALEDAQIPYSA--VEQACVGYVYGDSTSGQ- 73
Cdd:PTZ00455  10 AAKRVFVVGGHITPFVGKGSPLfiDKKHPDFGKkenktleellaTAIQGTLENTGLDGKAalVDKVVVGNFLGELFSSQg 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   74 ---RAIYHSLGLTGI-------PIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGS--IGTKFSDRTTptD 141
Cdd:PTZ00455  90 hlgPAAVGSLGQSGAsnallykPAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSarVGGDYLARAA--D 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  142 KHIEVLIDKYGLsahpitPQMFGYAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQ-FQDEYSLEEVMK---SKPVF- 216
Cdd:PTZ00455 168 YRRQRKLDDFTF------PCLFAKRMKYIQEHGHFTMEDTARVAAKAYANGNKNPLAHmHTRKLSLEFCTGasdKNPKFl 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  217 ------DFLTILQCCPTSDGAAAAILSSEEFVQQYGLQ---SKAVEIVAQE-----MMTDLPSTfeeksiikvvgYDM-- 280
Cdd:PTZ00455 242 gnetykPFLRMTDCSQVSDGGAGLVLASEEGLQKMGLSpndSRLVEIKSLAcasgnLYEDPPDA-----------TRMft 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  281 SKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGAT 360
Cdd:PTZ00455 311 SRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGAT 390
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 45476581  361 GLAQCAELCWQLRGEAGKRQVPGAkVALQHNLGLGG 396
Cdd:PTZ00455 391 GVKQIMEVYRQMKGQCGEYQMKNI-PALGATLNMGG 425
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
36-400 1.67e-32

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: 128.37  E-value: 1.67e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  36 PDMAKEAGQKALEDAQIPYSAVEQACVGYVYGdSTSGQ---RAIYHSLGL-TGIPIINVNNNCSTGSTALFMAHQLIQGG 111
Cdd:cd00751  23 DDLGAAVIKALLERAGLDPEEVDDVIMGNVLQ-AGEGQnpaRQAALLAGLpESVPATTVNRVCGSGLQAVALAAQSIAAG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 112 LANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAgkEHM-EKYG-TKVE---------- 179
Cdd:cd00751 102 EADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITA--ENVaEKYGiSREEqdefalrshq 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 180 ---------HFA------KIGWKNHKHSVNntysqfQDEY-----SLEEVMKSKPVFD---FLTILQCCPTSDGAAAAIL 236
Cdd:cd00751 180 raaaaqeagRFKdeivpvEVPGRKGPVVVD------RDEGprpdtTLEKLAKLKPAFKkdgTVTAGNASGINDGAAAVLL 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 237 SSEEFVQQYGLQSKAVeIVAQEmmtdlpstfeeksiikVVGYD---MSK---EAARRCYEKSGLTPNDVDVIELHDCFSV 310
Cdd:cd00751 254 MSEEKAKELGLKPLAR-IVGYA----------------VAGVDpaiMGIgpvPAIPKALKRAGLTLDDIDLIEINEAFAA 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 311 NELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQH 390
Cdd:cd00751 317 QALACLKELGLDPE------------------KVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGL----ATMCI 374
                       410
                ....*....|
gi 45476581 391 NLGLGGAVVV 400
Cdd:cd00751 375 GGGQGAAMVI 384
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
452-538 4.39e-32

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 118.90  E-value: 4.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   452 VKKIGG-IFAFKVKDGPGgkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMG 530
Cdd:pfam02036  15 LKKLNGkVIRFDLTDLGL----SLTLDLKDGGGRVLAGDEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDME 90

                  ....*...
gi 45476581   531 LAMKLQNL 538
Cdd:pfam02036  91 LAQKLEGL 98
PRK06066 PRK06066
thiolase domain-containing protein;
11-400 1.14e-31

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 126.02  E-value: 1.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   11 LRRVFVVGVGMTKFMKPGGENSrdYPDMAKEAGQKALEDAQI--PYSAVeqacvgyvygDS-TSGQRAIYHSLGLT---- 83
Cdd:PRK06066   3 LNRVAIVGIGWYGFRPTTPEVS--FREMMFEAASRAYKDAGNinPRRDV----------DSfISCQEDFWEGIAIAdefa 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   84 -----GI--PIINVnnncsTGSTALFMAH--QLIQGGLANCVLALGFEKmergsigtkfsdrttPTDkhIEVLIDKYGLS 154
Cdd:PRK06066  71 pdqigGAmrPTMTV-----AGDGLQGLAHavMHINSGLANVVVVEAHSK---------------PSD--ILTFSDVVKFA 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  155 AHPI------TPQMFGYAGKE---HMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCC 225
Cdd:PRK06066 129 MDPIyvrpigPPNPHFIAGLDavkFMSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIA 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  226 PTSDGAAAAILSSEEFVQQYglqskaveivaqemmTDLPStfeeksIIKVVGY--DMS-------------KEAARRCYE 290
Cdd:PRK06066 209 PFVDGAIVVVLASEEVAKKL---------------TDDPV------WIKGIGWstESSnletaelgkanymRIAADMAYK 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  291 KSGLTP--NDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAEL 368
Cdd:PRK06066 268 MAGIESprKEVDAAEVDDRYSYKELQHIEALRLSEEPEKDSLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDA 347
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 45476581  369 CWQLRGEAGKRQvPGAKVALQHNL----GLGGAVVV 400
Cdd:PRK06066 348 VEYLRGEAGARQ-GKAERAVVASWrgipTLTGSVVV 382
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
22-400 2.85e-29

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: 119.25  E-value: 2.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581    22 TKFMKPGGENSRDYP-DMAKEAGQKALEDAQIPYSAVEQACVGYVygDSTSGQR------AIYHSLGLTgIPIINVNNNC 94
Cdd:TIGR01930   7 TPIGKFGGSLKDVSAeDLGAAVIKELLERNPLDPELIDDVIFGNV--LQAGEQQniarqaALLAGLPES-VPAYTVNRQC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581    95 STGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKEHMEKY 174
Cdd:TIGR01930  84 ASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDARLKDLTDANTGLPMGVTAENLAKKY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   175 G-TKVE--HFA----KIGWKNHK-------------HSVNNTYSQFQDE-----YSLEEVMKSKPVFD---FLTILQCCP 226
Cdd:TIGR01930 164 GiSREEqdEYAlrshQRAAKAWEeglfkdeivpvtvKGRKGPVTVSSDEgirpnTTLEKLAKLKPAFDpdgTVTAGNSSP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   227 TSDGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFeeksiikvvGYdMSKEAARRCYEKSGLTPNDVDVIELHD 306
Cdd:TIGR01930 244 LNDGAAALLLMSEEKAKELGLTPLA-RIVSFAVAGVDPEIM---------GL-GPVPAIPKALKKAGLSISDIDLFEINE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   307 CFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakV 386
Cdd:TIGR01930 313 AFAAQVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGL----A 370
                         410
                  ....*....|....
gi 45476581   387 ALQHNLGLGGAVVV 400
Cdd:TIGR01930 371 TMCIGGGQGAAVIL 384
PRK08142 PRK08142
thiolase domain-containing protein;
156-397 2.32e-27

thiolase domain-containing protein;


Pssm-ID: 236164 [Multi-domain]  Cd Length: 388  Bit Score: 113.64  E-value: 2.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  156 HPITPQMFGYAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAI 235
Cdd:PRK08142 139 GPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDGGGALV 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  236 LSSEEfvqqyglqskaveiVAQEMmtdlpstfeEKSIIKVVGY------------DMSKEAAR----RCYEKSGLTPNDV 299
Cdd:PRK08142 219 VVRPE--------------IARSL---------KRPLVKVLGAgeaikgqmggkvDLTYSGAAwsgpAAFAEAGVTPADI 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  300 DVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYG-GKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAG- 377
Cdd:PRK08142 276 KYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHPANRGGMTKVIEAVRQLRGEAHp 355
                        250       260
                 ....*....|....*....|
gi 45476581  378 KRQVPGAKVALQHnlGLGGA 397
Cdd:PRK08142 356 AVQVPNCDLALAH--GTGGL 373
PRK07855 PRK07855
lipid-transfer protein; Provisional
16-384 2.81e-26

lipid-transfer protein; Provisional


Pssm-ID: 181147 [Multi-domain]  Cd Length: 386  Bit Score: 110.45  E-value: 2.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   16 VVGVGMTKFMKPGGENSRDypdMAKEAGQKALEDAQIPYSAVEqacvGYV-YGDSTSGQRAIYHSLG---LTGIPIINVN 91
Cdd:PRK07855   8 IVGIGATEFSKNSGRSELR---LACEAVLAALDDAGLAPSDVD----GLVtFTMDTNPEIAVARALGigeLKFFSRIHYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   92 NNCSTGSTA-LFMAhqlIQGGLANCVLAlgFEKMERGSiGTKFSDRTTPTDKHIEVLIDKYGLSAhP---ITP-QMFGYA 166
Cdd:PRK07855  81 GGAACATVQqAAMA---VATGVADVVVC--YRAFNERS-GMRFGQGQTGLAENPTSTGVDYGWSY-PhglLTPaAWVAML 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  167 GKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDE-YSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQy 245
Cdd:PRK07855 154 ARRYMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRpITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAERARD- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  246 gLQSKAVEIVA--------QEMMT----DLPSTFEEKSIikvvgydmskeAARRCYEKSGLTPNDVDVIELHDCFSVNEL 313
Cdd:PRK07855 233 -LKQRPAVIKAaaqgsgadQYMMTsyyrDDITGLPEMGL-----------VARQLWAQSGLGPADIDTAILYDHFTPFVL 300
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45476581  314 ITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLaqcAELCWQLRGEAgKRQVPGA 384
Cdd:PRK07855 301 MQLEELGFCGRGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNGI---AEAVRQLRGTS-VNQVPGV 367
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
453-538 1.66e-24

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 97.67  E-value: 1.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 453 KKIGGIFAFKVKDGPGGkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMGLA 532
Cdd:COG3255  18 AGWDGVVQFVITGEGGG---AYYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLA 94

                ....*.
gi 45476581 533 MKLQNL 538
Cdd:COG3255  95 MKLMSL 100
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
12-400 1.31e-22

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: 99.76  E-value: 1.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  12 RRVFVVGVGMTKFMKPGGE-NSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVygdSTSGQ-----RAIYHSLGL-TG 84
Cdd:COG0183   2 REVVIVDAVRTPFGRFGGAlADVRADDLGAAVIKALLERAGLDPEAVDDVILGCV---LQAGQgqnpaRQAALLAGLpES 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  85 IPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFG 164
Cdd:COG0183  79 VPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMINPGLTDPYTGLSMGE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 165 YAgkEHM-EKYG-TKVE-------------------HFAK------IGWKNHKHSVNntysqfQDEY-----SLEEVMKS 212
Cdd:COG0183 159 TA--ENVaERYGiSREEqdafalrshqraaaaiaagRFDDeivpveVPDRKGEVVVD------RDEGprpdtTLEKLAKL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 213 KPVFD---FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAvEIVAQ-------EMMTDLPStfeeksiikvvgydmsk 282
Cdd:COG0183 231 KPAFKkdgTVTAGNASGINDGAAALLLMSEEAAKELGLKPLA-RIVAYavagvdpEIMGIGPV----------------- 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581 283 EAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGL 362
Cdd:COG0183 293 PATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGA 354
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 45476581 363 AQCAELCWQLRGEAGKRQVpgakVALQHNLGLGGAVVV 400
Cdd:COG0183 355 RILVTLLHELERRGGRYGL----ATMCIGGGQGIALII 388
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
14-240 2.29e-18

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: 85.05  E-value: 2.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581    14 VFVVGVGMTKFMKPGGeNSRDYP--DMAKEAGQKALEDAQIPYSAVEQACVGYVyGDSTSGQ---RAIYHSLGLT-GIPI 87
Cdd:pfam00108   1 VVIVSAARTPFGSFGG-SLKDVSavELGAEAIKAALERAGVDPEDVDEVIVGNV-LQAGEGQnpaRQAALKAGIPdSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581    88 INVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDR---TTPTDKHIEVLIdKYGLSAHPITPQMfG 164
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARsglKHGDEKKHDLLI-PDGLTDAFNGYHM-G 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   165 YAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQ-FQDE------------------------YSLEEVMKSKPVFD-- 217
Cdd:pfam00108 157 LTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGkFKDEivpvtvkgrkgkptvdkdegirppTTAEPLAKLKPAFDke 236
                         250       260
                  ....*....|....*....|....
gi 45476581   218 -FLTILQCCPTSDGAAAAILSSEE 240
Cdd:pfam00108 237 gTVTAGNASPINDGAAAVLLMSES 260
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
85-400 3.69e-18

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 86.70  E-value: 3.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   85 IPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTkfsdrttptDKHIEV----LID-KY-------- 151
Cdd:PRK06445  86 IPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGD---------NPHIEPnpklLTDpKYieydlttg 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  152 ---GLSAHpitpQMFGYAG--KEHMEKYGTKVEHFA----KIGW-----------KNHKHSVNNTYSQFQDEYSLEEVMK 211
Cdd:PRK06445 157 yvmGLTAE----KLAEEAGikREEMDRWSLRSHQLAakaiQEGYfkdeilpieveVEGKKKVVDVDQSVRPDTSLEKLAK 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  212 SKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQQYGLQ--SKAVEI----VAQEMMTDLPSTfeeksiikvvgydmsk 282
Cdd:PRK06445 233 LPPAFKpdgVITAGNSSPLNSGASYVLLMSKKAVKKYGLKpmAKIRSFgfagVPPAIMGKGPVP---------------- 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  283 eAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGL 362
Cdd:PRK06445 297 -ASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPE------------------TVNIKGGAIAIGHPLGATGA 357
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 45476581  363 AQCAELCWQLRGEAGKRQVPGAKVAlqhnLGLGGAVVV 400
Cdd:PRK06445 358 RIVGTLARQLQIKGKDYGVATLCVG----GGQGGAVVL 391
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
11-402 3.65e-17

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 83.52  E-value: 3.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   11 LRRVFVVGVGMTKFMKPGGENSR-DYPDMAKEAGQKALEDAQIPYSAVEQACVGYVY----GDSTSGQrAIYHSLGLTGI 85
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGRSFSKiKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIqagvGQNPAGQ-AAYHAGLPFGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   86 PIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPtdKHIevLIDKYGLSAHPITPQMFGY 165
Cdd:PRK06366  80 TKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRWGP--KHL--LHKNYKIDDAMLVDGLIDA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  166 AGKEHM--------EKYGTKVEHFAKIGWKNHKHSVNNTYS-QFQDEY---------------SLEEVMKSKPVFD---F 218
Cdd:PRK06366 156 FYFEHMgvsaertaRKYGITREMADEYSVQSYERAIRATESgEFRNEIvpfndldrdegirktTMEDLAKLPPAFDkngI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  219 LTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPND 298
Cdd:PRK06366 236 LTAGNSAQLSDGGSALVMASEKAINEYGLKPIA-RITGYESASLDPLDFVEAPI----------PATRKLLEKQNKSIDY 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  299 VDVIELHDCFSVNELITYEALGLcpegqggtlvdrgDNTYggkwvINPSGGLISKGHPLGATGlaqcAELCWQLRGEAGK 378
Cdd:PRK06366 305 YDLVEHNEAFSIASIIVRDQLKI-------------DNER-----FNVNGGAVAIGHPIGNSG----SRIIVTLINALKT 362
                        410       420
                 ....*....|....*....|....
gi 45476581  379 RQVPGAKVALQHnlGLGGAVVVTL 402
Cdd:PRK06366 363 RHMKTGLATLCH--GGGGAHTLTL 384
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
37-378 6.74e-17

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 82.74  E-value: 6.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   37 DMAKEAGQKALedAQIP---YSAVEQACVGYVYGDSTSGQRAIYHSLGLTGIPI----INVNNNCSTGSTALFMAHQLIQ 109
Cdd:PRK09052  33 DLLAHVLRSAV--AQVPgldPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNsvggVTVNRFCASGLQAVAMAADRIR 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  110 GGLANCVLALGFEKMERGSI-GTKFSDRTTPTDKHIEVLI----------------------DKYGLSAH--PITPQMFG 164
Cdd:PRK09052 111 VGEADVMIAAGVESMSMVPMmGNKPSMSPAIFARDENVGIaygmgltaekvaeqwkvsredqDAFALESHqkAIAAQQAG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  165 YAGKEhMEKYgTKVEHFAKIgwkNHKHSVNNTYSQFQDE-----YSLEEVMKSKPVFDF---LTILQCCPTSDGAAAAIL 236
Cdd:PRK09052 191 EFKDE-ITPY-EITERFPDL---ATGEVDVKTRTVDLDEgpradTSLEGLAKLKPVFANkgsVTAGNSSQTSDGAGAVIL 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  237 SSEEFVQQYGLQ------SKAVEIVAQEMMTDLPstfeeksiikvvgydmsKEAARRCYEKSGLTPNDVDVIELHDCFSV 310
Cdd:PRK09052 266 VSEKALKQFNLTplarfvSFAVAGVPPEIMGIGP-----------------IEAIPAALKQAGLKQDDLDWIELNEAFAA 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45476581  311 NELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGK 378
Cdd:PRK09052 329 QSLAVIRDLGLDPS------------------KVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLK 378
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
11-361 5.88e-15

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 76.67  E-value: 5.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   11 LRRVFVVGVGMTKFMKPGGENSrdyPDMAKEAG----QKALEDAQIPYSAVEQACVGYVYgDSTSGQ---RAIYHSLGLT 83
Cdd:PRK08235   1 MSKTVIVSAARTPFGKFGGSLK---DVKATELGgiaiKEALERANVSAEDVEEVIMGTVL-QGGQGQipsRQAARAAGIP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   84 -GIPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKM-------ERGSIGTKFSDRT------------TPTDKH 143
Cdd:PRK08235  77 wEVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMsnapyilPGARWGYRMGDNEvidlmvadgltcAFSGVH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  144 IEV----LIDKYGLSAHpitpQMFGYAGKEHME-----KYGTKVEHFAKIGWKNHKhsvNNTYSQFQDE-----YSLEEV 209
Cdd:PRK08235 157 MGVyggeVAKELGISRE----AQDEWAYRSHQRavsahEEGRFEEEIVPVTIPQRK---GDPIVVAKDEaprkdTTIEKL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  210 MKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVeIVAQEMMTDLPSTFEeksiiKVVGYdmskeAAR 286
Cdd:PRK08235 230 AKLKPVFDktgTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLAT-ILAHTAIAVEAKDFP-----RTPGY-----AIN 298
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45476581  287 RCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 361
Cdd:PRK08235 299 ALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPE------------------KVNVNGGAVALGHPIGASG 355
PRK05790 PRK05790
putative acyltransferase; Provisional
36-361 3.52e-14

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 74.42  E-value: 3.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   36 PDMAKEAGQKALEDAQIPYSAVEQACVGYVYGdSTSGQRAIYHSLGLTGIPI----INVNNNCSTGSTALFMAHQLIQGG 111
Cdd:PRK05790  27 VELGAIVIKAALERAGVPPEQVDEVIMGQVLQ-AGAGQNPARQAALKAGLPVevpaLTINKVCGSGLKAVALAAQAIRAG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  112 LANCVLALGFEKMER------GS-IGTKFSDrTTPTDKHI-EVLIDKYglsahpiTPQMFGYAGKEHMEKYG-TKVE--H 180
Cdd:PRK05790 106 DADIVVAGGQESMSQaphvlpGSrWGQKMGD-VELVDTMIhDGLTDAF-------NGYHMGITAENLAEQYGiTREEqdE 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  181 F-------AKIGWKNHKHS---VNNTYSQ--------FQDEY-----SLEEVMKSKPVFD---FLTILQCCPTSDGAAAA 234
Cdd:PRK05790 178 FalasqqkAEAAIKAGRFKdeiVPVTIKQrkgdpvvvDTDEHprpdtTAESLAKLRPAFDkdgTVTAGNASGINDGAAAV 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  235 ILSSEEFVQQYGLQSKAvEIVAQemmtdlpstfeeksiiKVVGYDMSK------EAARRCYEKSGLTPNDVDVIELHDCF 308
Cdd:PRK05790 258 VVMSEAKAKELGLTPLA-RIVSY----------------AVAGVDPAImgigpvPAIRKALEKAGWSLADLDLIEINEAF 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45476581  309 SVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 361
Cdd:PRK05790 321 AAQALAVEKELGLDPE------------------KVNVNGGAIALGHPIGASG 355
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
12-405 9.58e-14

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 73.20  E-value: 9.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   12 RRVFVVGVGMT---KFMkpGGENSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYgDSTSGQR-AIYHSLGlTGIP- 86
Cdd:PLN02644   1 RDVCIVGVARTpigGFL--GSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVL-SANLGQApARQAALG-AGLPp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   87 ---IINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKME-------RGSIGTKFSDRTTP------------TDKHI 144
Cdd:PLN02644  77 stiCTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSnapkylpEARKGSRLGHDTVVdgmlkdglwdvyNDFGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  145 ----EVLIDKYGLS-----AHPITPQMFGYAGKE--HMEKYGTKVEHFAKIGwknhKHSVNNTYSQFQDEYSLEEVMKSK 213
Cdd:PLN02644 157 gvcaELCADQYSISreeqdAYAIQSYERAIAAQEagAFAWEIVPVEVPGGRG----RPSVIVDKDEGLGKFDPAKLRKLR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  214 PVFD----FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVEI----VAQ--EMMTDLPSTfeeksiikvvgydmske 283
Cdd:PLN02644 233 PSFKedggSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRgyadAAQapELFTTAPAL----------------- 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  284 AARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGqggtlvdrgdntyggkwvINPSGGLISKGHPLGATGLA 363
Cdd:PLN02644 296 AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEK------------------VNVHGGAVSLGHPIGCSGAR 357
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 45476581  364 QCAELCWQLRGEAGKRQVPGAkvalqHNlGLGGAVVVTLYRM 405
Cdd:PLN02644 358 ILVTLLGVLRSKNGKYGVAGI-----CN-GGGGASAIVVELM 393
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
11-361 2.01e-13

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 72.05  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   11 LRRVFVVGVGMTKFMKPGGENSRDYP-DMAKEAGQKALEDAQIPYSAVEQACVGYVygDSTSGQ-----RAIYHSLGLT- 83
Cdd:PRK07801   1 MAEAYIVDAVRTPVGKRKGGLAGVHPaDLGAHVLKGLVDRTGIDPAAVDDVIFGCV--DTIGPQagniaRTSWLAAGLPe 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   84 GIPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTK--------FSDRTTPTDKHIEvlidKYGlsA 155
Cdd:PRK07801  79 EVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAmtageqlgFTSPFAESKGWLH----RYG--D 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  156 HPITPqmfgYAGKEHM-EKYGTKVEHFAKIGWKNHKHSVNNTYS-QFQDEY---------------SLEEVMKSKPVFD- 217
Cdd:PRK07801 153 QEVSQ----FRGAELIaEKWGISREEMERFALESHRRAFAAIRAgRFDNEIvpvggvtvdegpretSLEKMAGLKPLVEg 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  218 -FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTP 296
Cdd:PRK07801 229 gRLTAAVASQISDGASAVLLASERAVKRHGLTPRA-RIHHLSVRGDDPVFMLTAPI----------PATRYALEKTGLSI 297
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45476581  297 NDVDVIELHDCFSVNELITYEALGLCPEGqggtlvdrgdntyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK07801 298 DDIDVVEINEAFAPVVLAWLKETGADPAK------------------VNPNGGAIALGHPLGATG 344
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
205-361 1.13e-12

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 69.65  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  205 SLEEVMKSKPVF---DFLTILQCCPTSDGAAAAILSSEEFVQQYGLQ------SKAVEIVAQEMMTDLPStfeeksiikv 275
Cdd:PRK07851 237 TYEKVSQLKPVFrpdGTVTAGNACPLNDGAAAVVIMSDTKARELGLTplarivSTGVSGLSPEIMGLGPV---------- 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  276 vgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLcPEgqggtlvDRgdntyggkwvINPSGGLISKGH 355
Cdd:PRK07851 307 -------EASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGI-DE-------DK----------LNVSGGAIALGH 361

                 ....*.
gi 45476581  356 PLGATG 361
Cdd:PRK07851 362 PFGMTG 367
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
201-379 2.98e-12

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 68.44  E-value: 2.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  201 QDEY-----SLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVEI------VAQEMMTDLPST 266
Cdd:PRK09050 222 RDEHprpetTLEALAKLKPVFRpdgTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILgmatagVEPRIMGIGPAP 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  267 feeksiikvvgydmskeAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLcpegqggtlVDRGDNtyggkwvINP 346
Cdd:PRK09050 302 -----------------ATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGL---------ADDDAR-------VNP 348
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 45476581  347 SGGLISKGHPLGATG--LAQCAELcwQLRGEAGKR 379
Cdd:PRK09050 349 NGGAIALGHPLGMSGarLVLTALH--QLERTGGRY 381
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
284-400 2.70e-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: 60.73  E-value: 2.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   284 AARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLA 363
Cdd:pfam02803  27 AIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASGAR 88
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 45476581   364 QCAELCWQLRGEAGKRQVpgakVALQHNLGLGGAVVV 400
Cdd:pfam02803  89 ILVTLLHELKRRGGKYGL----ASLCIGGGQGVAMII 121
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
37-138 2.87e-11

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: 64.75  E-value: 2.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  37 DMAKEAGQKALEDAQIPYSAVEQACVGYVYGD----STSGQraIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGL 112
Cdd:COG0332  53 DLAVEAARKALEAAGIDPEDIDLIIVATVTPDylfpSTACL--VQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQ 130
                        90       100
                ....*....|....*....|....*.
gi 45476581 113 ANCVLALGFEKMERgsiGTKFSDRTT 138
Cdd:COG0332 131 AKNVLVVGAETLSR---IVDWTDRST 153
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
82-361 4.63e-11

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 64.60  E-value: 4.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   82 LTGIPI----INVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMerGSIG-TKFSDRTTPTDKHIEVLIDKYGLSA- 155
Cdd:PRK08947  75 LAGIPHsvpaVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM--GHVPmNHGVDFHPGLSKNVAKAAGMMGLTAe 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  156 -----HPITPQM---FGYagKEHMEKYGTKVE-HFAKIGWKNHKHSVNNTYSQFQD------EYSLEEVMKSKPVFD--- 217
Cdd:PRK08947 153 mlgkmHGISREQqdaFAA--RSHQRAWAATQEgRFKNEIIPTEGHDADGVLKLFDYdevirpETTVEALAALRPAFDpvn 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  218 -FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVeIVAqemMTdlpstfeeksiikVVGYDMS------KEAARRCYE 290
Cdd:PRK08947 231 gTVTAGTSSALSDGASAMLVMSESRAKELGLKPRAR-IRS---MA-------------VAGCDPSimgygpVPATQKALK 293
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45476581  291 KSGLTPNDVDVIELHDCFSVNELITYEALGlcpegqggtLVDRGDNTyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK08947 294 RAGLSISDIDVFELNEAFAAQSLPCLKDLG---------LLDKMDEK------VNLNGGAIALGHPLGCSG 349
PRK07937 PRK07937
lipid-transfer protein; Provisional
11-392 5.65e-11

lipid-transfer protein; Provisional


Pssm-ID: 181173 [Multi-domain]  Cd Length: 352  Bit Score: 64.33  E-value: 5.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   11 LRRVFVVGVGMTKFMkPGGENSRDYPDMAKEAGQKALEDAQIPYSAVEQACVG---YVYGDSTSGQRAIyHSLGltGIPI 87
Cdd:PRK07937   1 MRDVAVVGFAQAPHV-RRTDGTTNGVEMLMPCFAELYAELGITKSDIGFWCSGssdYLAGRAFSFISAI-DSIG--AVPP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   88 INVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKmerGSIGTkfSDRTTPTDkhievlIDKYGLSahPITPQMFGYAG 167
Cdd:PRK07937  77 INESHVEMDAAWALYEAWVKLLTGEVDTALVYGFGK---SSAGT--LRRVLALQ------LDPYTVA--PLWPDSVSMAG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  168 ---KEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQfqDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEfvqq 244
Cdd:PRK07937 144 lqaRAGLDAGKWTEEQMAEVAARSRADARRNPSAE--PSISVDELLARPYFADPLRRHDIAPITDGAAAVVLAAGD---- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  245 yglqsKAVEIVAQEM------------------MTDLPSTfeeksiikvvgydmsKEAARRCyekSGLTPNDVDVIELHD 306
Cdd:PRK07937 218 -----RARELRERPAwitgiehriespslgardLTRSPST---------------ALAAEAA---TGGDAGGVDVAELHA 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  307 CFSVNELITYEALGLcpegqggtlvdrGDNTyggkwVINPSGGLISkGHPLGATGLAQCAELCWQ-LRGEAGkRQVPGAK 385
Cdd:PRK07937 275 PFTHQELILREALGL------------GDKT-----KVNPSGGALA-ANPMFAAGLERIGEAARHiWDGSAR-RALAHAT 335

                 ....*....
gi 45476581  386 V--ALQHNL 392
Cdd:PRK07937 336 SgpALQQNL 344
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
229-361 6.06e-11

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 64.41  E-value: 6.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  229 DGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCF 308
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPRA-RIVAMANMGDDPTLMLNAPV----------PAAKKVLAKAGLTKDDIDLWEINEAF 344
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45476581  309 SVNELITYEALGLcpegqggtlvDRGDntyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK06025 345 AVVAEKFIRDLDL----------DRDK--------VNVNGGAIALGHPIGATG 379
PRK09051 PRK09051
beta-ketothiolase BktB;
84-361 2.15e-10

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 62.67  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   84 GIPI----INVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSI-------GTKFSDrTTPTDKHIEVLIDKYG 152
Cdd:PRK09051  76 GVPQetpaFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYllpaarwGARMGD-AKLVDMMVGALHDPFG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  153 lsahpitpqmfgyagKEHM--------EKYGTKVEH---FAKIGWKNHKHSVNNTYSQFQ-----------------DEY 204
Cdd:PRK09051 155 ---------------TIHMgvtaenvaAKYGISREAqdaLALESHRRAAAAIAAGYFKDQivpveiktrkgevvfdtDEH 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  205 -----SLEEVMKSKPVF--DFLTIlqccpTS-------DGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFEEK 270
Cdd:PRK09051 220 vradtTLEDLAKLKPVFkkENGTV-----TAgnasginDGAAAVVLAEADAAEARGLKPLA-RLVGYAHAGVDPEYMGIG 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  271 SIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGqggtlvdrgdntyggkwvINPSGGL 350
Cdd:PRK09051 294 PV----------PATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAK------------------VNPNGSG 345
                        330
                 ....*....|.
gi 45476581  351 ISKGHPLGATG 361
Cdd:PRK09051 346 ISLGHPVGATG 356
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
36-400 4.32e-10

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 61.58  E-value: 4.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   36 PDMAKEAGQKALEDAQIPYSAVEQACVGYVYgDSTSGQRAIYHSLGLTGIPI----INVNNNCSTGSTALFMAHQLIQGG 111
Cdd:PRK06633  28 PMLAAHLIKDILQNSKIDPALVNEVILGQVI-TGGSGQNPARQTLIHAGIPKevpgYTINKVCGSGLKSVALAANSIMTG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  112 LANCVLALGFEKMERG------SIGTKFSDRTTPTDKHIEVLIDKY-----GLSAHPITPQmFGYAGKEHMEKYGTKVEH 180
Cdd:PRK06633 107 DNEIVIAGGQENMSLGmhgsyiRAGAKFGDIKMVDLMQYDGLTDVFsgvfmGITAENISKQ-FNISRQEQDEFALSSHKK 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  181 FAKIG----WKNH----KHSVNNTYSQF-QDE-----YSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQ 243
Cdd:PRK06633 186 AAKAQlagiFKDEilpiEVTIKKTTSLFdHDEtvrpdTSLEILSKLRPAFDkngVVTAGNASSINDGAACLMVVSEEALK 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  244 QYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALglcp 323
Cdd:PRK06633 266 KHNLTPLA-RIVSYASAGVDPSIMGTAPV----------PASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREM---- 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  324 egqggtlvdrgdntyggKW---VINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQHNLGLGGAVVV 400
Cdd:PRK06633 331 -----------------KWdmeKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGL----VTLCIGGGMGMAMCV 389
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
85-361 6.37e-10

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 61.05  E-value: 6.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   85 IPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGtkfSD-RTTPTDKhiEVLIDKY----GLSAHPIT 159
Cdd:PRK08242  82 VPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMG---SDgGAWAMDP--STNFPTYfvpqGISADLIA 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  160 pQMFGYaGKEHMEKYGTKVEHFAKIGWKNH--KHSV------NNTYSQFQDEY-----SLEEVMKSKPVFDFL------- 219
Cdd:PRK08242 157 -TKYGF-SREDVDAYAVESQQRAAAAWAEGyfAKSVvpvkdqNGLTILDHDEHmrpgtTMESLAKLKPSFAMMgemggfd 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  220 -TILQCCPT----------------SDGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPStfeeksiIKVVGydmSK 282
Cdd:PRK08242 235 aVALQKYPEverinhvhhagnssgiVDGAAAVLIGSEEAGKALGLKPRA-RIVATATIGSDPT-------IMLTG---PV 303
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45476581  283 EAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 361
Cdd:PRK08242 304 PATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHD------------------KVNVNGGAIAMGHPLGATG 364
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
37-138 7.56e-10

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: 60.25  E-value: 7.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  37 DMAKEAGQKALEDAQIpySAVEQACVgyVYGDSTSGQRA------IYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQG 110
Cdd:cd00830  52 DLAVEAAKKALEDAGI--DADDIDLI--IVATSTPDYLFpataclVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRS 127
                        90       100
                ....*....|....*....|....*...
gi 45476581 111 GLANCVLALGFEKMERgsiGTKFSDRTT 138
Cdd:cd00830 128 GGAKNVLVVGAETLSR---ILDWTDRST 152
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
22-400 1.47e-09

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 60.18  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   22 TKFMKPGGENSRDYPD-MAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHSLGLTGIPI----INVNNNCST 96
Cdd:PRK08131  12 SPFGRHAGALASVRPDdLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVtvpgQTVNRLCAS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   97 GSTALFMAHQLIQGGLANCVLALGFEKMER-----GSIGTKFSDRTTPTDKHI------EVLIDKYGLSAHPITPQ---- 161
Cdd:PRK08131  92 GLAAVIDAARAITCGEGDLYLAGGVESMSRapfvmGKAESAFSRDAKVFDTTIgarfpnPKIVAQYGNDSMPETGDnvaa 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  162 MFG--------YAGKEHMEKYGTKVEHF---------AKIGWKNHKHSVNntysqfQDEY-----SLEEVMKSKPVFD-- 217
Cdd:PRK08131 172 EFGisredadrFAAQSQAKYQAAKEEGFfadeitpieVPQGRKLPPKLVA------EDEHprpssTVEALTKLKPLFEgg 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  218 FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPStfeeksiIKVVGydmSKEAARRCYEKSGLTPN 297
Cdd:PRK08131 246 VVTAGNASGINDGAAALLIGSRAAGEKYGLKPMA-RILSSAAAGVEPR-------IMGIG---PVEAIKKALARAGLTLD 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  298 DVDVIELHDCFSVNELITYEALGlcpegqggtlVDRGDNTyggkwvINPSGGLISKGHPLGATGlaqcAELCWQLRGEAG 377
Cdd:PRK08131 315 DMDIIEINEAFASQVLGCLKGLG----------VDFDDPR------VNPNGGAIAVGHPLGASG----ARLALTAARELQ 374
                        410       420
                 ....*....|....*....|...
gi 45476581  378 KRQVPGAKVALQHNLGLGGAVVV 400
Cdd:PRK08131 375 RRGKRYAVVSLCIGVGQGLAMVI 397
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
42-361 4.00e-09

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 58.58  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   42 AGQKA-LEDAQIPYSAVEQ---ACVGYVYGDSTSGQRAIYHSLGL---TGIPIINVNnnCSTGSTALFMAHQLIQGGLAN 114
Cdd:PRK07850  32 AVQRAvLDRAGIDPGDVEQvigGCVTQAGEQSNNITRTAWLHAGLpyhVGATTIDCQ--CGSAQQANHLVAGLIAAGAID 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  115 CVLALGFEKMERGSIGTKFSDRTT---PTDKHI---------EVLIDKYGLSahpitpqmfgyagKEHMEKYGTKVEHFA 182
Cdd:PRK07850 110 VGIACGVEAMSRVPLGANAGPGRGlprPDSWDIdmpnqfeaaERIAKRRGIT-------------REDVDAFGLRSQRRA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  183 KIGWKNHK---------------------HSVNNTYSQFQDEYSLEEVMKSKPVFD--FLTILQCCPTSDGAAAAILSSE 239
Cdd:PRK07850 177 AQAWAEGRfdreispvqapvldeegqptgETRLVTRDQGLRDTTMEGLAGLKPVLEggIHTAGTSSQISDGAAAVLWMDE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  240 EFVQQYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSvnelityeAL 319
Cdd:PRK07850 257 DRARALGLRPRA-RIVAQALVGAEPYYHLDGPV----------QATAKVLEKAGMKIGDIDLVEINEAFA--------SV 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 45476581  320 GLCPEGQGGTLVDRgdntyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK07850 318 VLSWAQVHEPDMDK----------VNVNGGAIALGHPVGSTG 349
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
37-379 4.17e-09

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 58.59  E-value: 4.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   37 DMAKEAGQKALEDAQIPYSAVEQA---CVGYVYGDSTS-GQRAIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGL 112
Cdd:PRK06504  28 DLAAQVLDALVDRSGADPALIEDVimgCVSQVGEQATNvARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMSGT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  113 ANCVLALGFEKMERGSIGTKFSdrttptdkhievLIDKYGLsAHPITPQM--------FG-YAGKEHM-EKYGTKVEHFA 182
Cdd:PRK06504 108 MDIVIAAGVESMTRVPMGSPST------------LPAKNGL-GHYKSPGMeerypgiqFSqFTGAEMMaKKYGLSKDQLD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  183 KIGWKNHKHSVNNTYSQ-FQDEY-------------------------SLEEVMKSKPVFD-----FLTILQCCptsDGA 231
Cdd:PRK06504 175 EFALQSHQRAIAATQAGkFKAEIvpleitradgsgemhtvdegirfdaTLEGIAGVKLIAEggrltAATASQIC---DGA 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  232 AAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVN 311
Cdd:PRK06504 252 SGVMVVNERGLKALGVKPLA-RIHHMTVIGGDPVIMLEAPL----------PATERALKKAGMKIDDIDLYEVNEAFASV 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45476581  312 ELITYEALGLCPEGqggtlvdrgdntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRgEAGKR 379
Cdd:PRK06504 321 PLAWLKATGADPER------------------LNVNGGAIALGHPLGASGTKLMTTLVHALK-QRGKR 369
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
36-382 8.44e-09

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 57.59  E-value: 8.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   36 PDMAKEAGQKALEDAQIPYSAVEQACVGYVY----GDSTSGQRAIYHSLGLtGIPIINVNNNCSTGSTALFMAHQLIQGG 111
Cdd:PRK06954  32 PQLGAAAIAAAVERAGLKPEQIDEVVMGCVLpagqGQAPARQAALGAGLPL-SVGCTTVNKMCGSGMRAAMFAHDMLVAG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  112 LANCVLALGFEKME-------RGSIGTKFSDRTTPTDKHIEVLIDKYGLSahpitpQMFGYAGKEHMEKYGTKVEH---F 181
Cdd:PRK06954 111 SVDVIVAGGMESMTnapyllpKARGGMRMGHGQVLDHMFLDGLEDAYDKG------RLMGTFAEECAGEYGFTREAqdaF 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  182 AKIGWKNHKHSVNNTYSQFQ-----------------DE----YSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILS 237
Cdd:PRK06954 185 AIESLARAKRANEDGSFAWEiapvtvagkkgdtvidrDEqpfkANPEKIPTLKPAFSktgTVTAANSSSISDGAAALVMM 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  238 SEEFVQQYGLQSKAVeIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYE 317
Cdd:PRK06954 265 RASTAKRLGLAPLAR-VVGHSTFAQAPSKFTTAPV----------GAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMK 333
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45476581  318 ALGLCPEGqggtlvdrgdntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVP 382
Cdd:PRK06954 334 EHGLPHEK------------------VNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVA 380
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
205-368 1.41e-08

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 57.22  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  205 SLEEVMKSKPVFDF-----LTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVEIVAQEMMTDLpstfeeksiikVVGYD 279
Cdd:PRK09268 237 SLEKLAKLKPVFGKggratMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDF-----------VHGKE 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  280 ---MSKE-AARRCYEKSGLTPNDVDVIELHDCFSVNELIT---YEALGLCPE--GQGGTL--VDRGDntyggkwvINPSG 348
Cdd:PRK09268 306 gllMAPAyAVPRLLARNGLTLQDFDFYEIHEAFASQVLATlkaWEDEEYCRErlGLDAPLgsIDRSK--------LNVNG 377
                        170       180
                 ....*....|....*....|...
gi 45476581  349 GLISKGHPLGATG---LAQCAEL 368
Cdd:PRK09268 378 SSLAAGHPFAATGgriVATLAKL 400
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
47-365 1.62e-08

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 57.08  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   47 LEDAQIPYSAVEQACVGYVYGDSTsgQRAIYHSLG--LTGIP----IINVNNNCSTGSTALFMAHQLIQGGLANCVLALG 120
Cdd:PLN02287  83 VEKTGLNPSEVGDIVVGTVLAPGS--QRANECRMAafYAGFPetvpVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAG 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  121 FEKM------ERGSIGTKFSDRTTPTDKHIEVlidkyGLSAHPITpqmfgyagkehmEKYGTKVEHFAKIGWKNHKHSVN 194
Cdd:PLN02287 161 VESMttnpmaWEGGVNPRVESFSQAQDCLLPM-----GITSENVA------------ERFGVTREEQDQAAVESHRKAAA 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  195 NTYS-QFQDEY------------------------------SLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEE 240
Cdd:PLN02287 224 ATASgKFKDEIvpvhtkivdpktgeekpivisvddgirpntTLADLAKLKPVFKkngTTTAGNSSQVSDGAGAVLLMKRS 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  241 FVQQYGL------QSKAVEIVAQEMMTDLPSTfeekSIIKVVgydmskeaarrcyEKSGLTPNDVDVIELHDCFSVNELI 314
Cdd:PLN02287 304 VAMQKGLpilgvfRSFAAVGVDPAVMGIGPAV----AIPAAV-------------KAAGLELDDIDLFEINEAFASQFVY 366
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 45476581  315 TYEALGLCPEGqggtlvdrgdntyggkwvINPSGGLISKGHPLGATGlAQC 365
Cdd:PLN02287 367 CCKKLGLDPEK------------------VNVNGGAIALGHPLGATG-ARC 398
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
36-361 4.43e-08

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 55.28  E-value: 4.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   36 PDMAKEAGQKALEDAQIPYSAVEQACVGYVY----GDSTSGQRAIYHSLGLTgIPIINVNNNCSTGSTALFMAHQLIQGG 111
Cdd:PRK05656  27 VELGAAVIRRLLEQTGLDPAQVDEVILGQVLtagaGQNPARQAAIKAGLPHS-VPAMTLNKVCGSGLKALHLAAQAIRCG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  112 LANCVLALGFEKMERGS-----------------IGTKFSDR--TTPTDKHI----EVLIDKYGLS-----AHPITPQMF 163
Cdd:PRK05656 106 DAEVIIAGGQENMSLAPyvlpgartglrmghaqlVDSMITDGlwDAFNDYHMgitaENLVEKYGISreaqdAFAAASQQK 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  164 GYAGKEHmekyGTKVEHFAKIGWKNHKHS--VNNTYSQFQDEYSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSS 238
Cdd:PRK05656 186 AVAAIEA----GRFDDEITPILIPQRKGEplAFATDEQPRAGTTAESLAKLKPAFKkdgSVTAGNASSLNDGAAAVLLMS 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  239 EEFVQQYGLQSKAvEIVAQEMMTDLPStfeeksiIKVVGydmSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEA 318
Cdd:PRK05656 262 AAKAKALGLPVLA-KIAAYANAGVDPA-------IMGIG---PVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKE 330
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 45476581  319 LGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 361
Cdd:PRK05656 331 LGWDAA------------------KVNVNGGAIALGHPIGASG 355
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
85-402 2.95e-07

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 52.83  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   85 IPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMergSIGTKFSDRTTPTDKHIEVLIDKYglsahpitpQMFG 164
Cdd:PRK07661  81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESM---SLVPMMGHVVRPNPRLVEAAPEYY---------MGMG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  165 YAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQ-FQDEY---------------------------------SLEEVM 210
Cdd:PRK07661 149 HTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGkFADEIvpvdvtlrtvgennklqeetitfsqdegvradtTLEILG 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  211 KSKPVFDF---LTILQCCPTSDGAAAAILSSEEFVQQYGLQ------SKAVEIVAQEMMTDLPStfeeksiikvvgydms 281
Cdd:PRK07661 229 KLRPAFNVkgsVTAGNSSQMSDGAAAVLLMDREKAESDGLKplakfrSFAVAGVPPEVMGIGPI---------------- 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  282 kEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 361
Cdd:PRK07661 293 -AAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEE------------------KVNVNGGAIALGHPLGCTG 353
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 45476581  362 laqcAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTL 402
Cdd:PRK07661 354 ----AKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFEL 390
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
4-120 6.12e-07

"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.


Pssm-ID: 238423 [Multi-domain]  Cd Length: 324  Bit Score: 51.66  E-value: 6.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   4 VALKSPRLRRVFVVGVGmTKFMKPGGENSrdyPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIY--HSLG 81
Cdd:cd00827  21 LAEGLGVDPGKYTTGIG-QRHMAGDDEDV---PTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYlaELLG 96
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 45476581  82 LTGIPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALG 120
Cdd:cd00827  97 LTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVA 135
Alkyl_sulf_C pfam14864
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ...
471-528 9.42e-07

Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. Together with the N-terminal catalytic domain, this domain forms a hydrophobic chute and may recruit hydrophobic substrates.


Pssm-ID: 405542 [Multi-domain]  Cd Length: 124  Bit Score: 47.96  E-value: 9.42e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45476581   471 EATWVVDVKNGkgsVL----PNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGN 528
Cdd:pfam14864  43 DEQYRLTLSNG---VLtyrkGRQADDADATLTLTRADLLALLLGKATLGKLIAAGKIKVEGD 101
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
229-361 3.08e-06

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 49.60  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  229 DGAAAAILSSEEFVQQYGLQ------SKAVEIVAQEMMTdlpstfeeksiIKVVGydmskeAARRCYEKSGLTPNDVDVI 302
Cdd:PRK06205 259 DAAAACLVTTEDKAEELGLRplarlvSWAVAGVEPSRMG-----------IGPVP------ATEKALARAGLTLDDIDLI 321
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 45476581  303 ELHDCFSVNELITYEALGLCPEGqggtlVDRgdntyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK06205 322 ELNEAFAAQVLAVLKEWGFGADD-----EER----------LNVNGSGISLGHPVGATG 365
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
37-138 5.27e-06

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 48.53  E-value: 5.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   37 DMAKEAGQKALEDAQIPYSAVEQACVGYVYGD----STSGQraIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGL 112
Cdd:PRK09352  54 DLATEAAKKALEAAGIDPEDIDLIIVATTTPDyafpSTACL--VQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGA 131
                         90       100
                 ....*....|....*....|....*.
gi 45476581  113 ANCVLALGFEKMERgsIgTKFSDRTT 138
Cdd:PRK09352 132 YKNVLVIGAEKLSR--I-VDWTDRST 154
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
472-538 9.07e-06

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 48.30  E-value: 9.07e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45476581 472 ATWVVDVKNGkgsVLPN----SDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMGLAMKLQNL 538
Cdd:COG2015 551 EKYLLELRNG---VLTYrkgpQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGDAAALARLLGL 618
UbiJ COG3165
Ubiquinone biosynthesis protein UbiJ, contains SCP2 domain [Coenzyme transport and metabolism]; ...
485-538 1.42e-05

Ubiquinone biosynthesis protein UbiJ, contains SCP2 domain [Coenzyme transport and metabolism];


Pssm-ID: 442398  Cd Length: 204  Bit Score: 46.01  E-value: 1.42e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 45476581 485 VLPNSDKKADCTITMADSDLLALMTGKmNPQSAFFQGKLKIAGNMGLAMKLQNL 538
Cdd:COG3165  58 VLGAWEGEADCTLTGSLSALLRLADAQ-DLTALIASGELRIEGDAQLAQQLSRL 110
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
90-138 2.43e-04

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430064 [Multi-domain]  Cd Length: 80  Bit Score: 39.81  E-value: 2.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 45476581    90 VNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMergSIGTKFSDRTT 138
Cdd:pfam08545   3 INAACSGFVYALSTAAALIRSGRAKNVLVIGAETL---SKILDWTDRST 48
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
38-122 4.59e-04

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 42.53  E-value: 4.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  38 MAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIY--------------------------------HSLGLTGi 85
Cdd:cd00834  74 FALAAAEEALADAGLDPEELDPERIGVVIGSGIGGLATIEeayrallekgprrvspffvpmalpnmaagqvaIRLGLRG- 152
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 45476581  86 PIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFE 122
Cdd:cd00834 153 PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
42-122 7.90e-04

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 42.00  E-value: 7.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581  42 AGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHS--------------------------------LGLTGiPIIN 89
Cdd:COG0304  78 AAREALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAyrallekgprrvspffvpmmmpnmaaghvsirFGLKG-PNYT 156
                        90       100       110
                ....*....|....*....|....*....|...
gi 45476581  90 VNNNCSTGSTALFMAHQLIQGGLANCVLALGFE 122
Cdd:COG0304 157 VSTACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
PRK07204 PRK07204
beta-ketoacyl-ACP synthase III;
38-170 7.68e-03

beta-ketoacyl-ACP synthase III;


Pssm-ID: 235964  Cd Length: 329  Bit Score: 38.66  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45476581   38 MAKEAGQKALEDAQIPYSAVEQacvgyVYGDSTSGQRAI-------YHSLGL--TGIPIINVNNNCSTGSTALFMAHQLI 108
Cdd:PRK07204  55 MGAEAAKKAVEDAKLTLDDIDC-----IICASGTIQQAIpctasliQEQLGLqhSGIPCFDINSTCLSFITALDTISYAI 129
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45476581  109 QGGLANCVLALgfeKMERGSIGTKFSDRTTPT---DKHIEVLIDKYGLSAHPITPQMFGYAGKEH 170
Cdd:PRK07204 130 ECGRYKRVLII---SSEISSVGLNWGQNESCIlfgDGAAAVVITKGDHSSRILASHMETYSSGAH 191
 
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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