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Conserved domains on  [gi|504754531|ref|WP_014941633|]
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MULTISPECIES: OB-fold domain-containing protein [Mycobacterium]

Protein Classification

OB_aCoA_assoc and SCP-x_thiolase domain-containing protein( domain architecture ID 11446206)

protein containing domains DUF35_N, OB_aCoA_assoc, and SCP-x_thiolase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 164-532 1.30e-80

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: 256.81  E-value: 1.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 164 GIGRSATGRRLMVDPLSLTMDACLAAVADAGLELSDIDGLstYPGPVGMGMSEGGIAA-VEEALRIHPTWI----NGGmd 238
Cdd:cd00829    2 GVGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADIDAV--VVGNAAGGRFQSFPGAlIAEYLGLLGKPAtrveAAG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 239 lPGQGGAIIAAMMAVAAGLCRHVLCfrTVWESTYAALRLHGGGGRVSGPQ-QWSLPFGAASAANWIGVNANQYLHRYGAN 317
Cdd:cd00829   78 -ASGSAAVRAAAAAIASGLADVVLV--VGAEKMSDVPTGDEAGGRASDLEwEGPEPPGGLTPPALYALAARRYMHRYGTT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 318 RELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNASIGGDLPRPAIRCEAVGT 397
Cdd:cd00829  155 REDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTDRPVWILGVGA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 398 QVAERISWDQGTLTHEPQVIGQAAHLWSRTDLRPEDVDLALLYDGFTFNCVSWLEALGFCGFGEAQGWLDGGrRIALDGE 477
Cdd:cd00829  235 ASDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREG-DTAIGGD 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504754531 478 LPLNTHGGQLSEGRLH---GFGFLYEAVLQLRHQAGNRQVKDARTAVVSTGGGVPSGV 532
Cdd:cd00829  314 LPVNTSGGLLSKGHPLgatGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGTGSAA 371
COG1545 COG1545
Uncharacterized OB-fold protein, contains Zn-ribbon domain [General function prediction only];
14-128 5.71e-37

Uncharacterized OB-fold protein, contains Zn-ribbon domain [General function prediction only];


:

Pssm-ID: 441154 [Multi-domain]  Cd Length: 116  Bit Score: 132.71  E-value: 5.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531  14 FWTSGKDGHLRIQHCSECDTYVHPPVPICPSCRATSAEPAVVSGRATVVGYTVNAHPWLP-GFEPPYVIAVVALDEcaEV 92
Cdd:COG1545    1 FWRALAEGRLLGQRCPACGTVYFPPRPVCPHCGSEDLEWVELSGRGTVYSYTVVHRPPPPfEDEVPYVVALVELDE--GV 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504754531  93 RLTTNIVGCSPEEVHVGQRVSVRFDNID--DVWIPLFE 128
Cdd:COG1545   79 RVLGRLVGVDPEDVRIGMRVRVVFRPIDedGRTLPVFR 116
 
Name Accession Description Interval E-value
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 164-532 1.30e-80

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: 256.81  E-value: 1.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 164 GIGRSATGRRLMVDPLSLTMDACLAAVADAGLELSDIDGLstYPGPVGMGMSEGGIAA-VEEALRIHPTWI----NGGmd 238
Cdd:cd00829    2 GVGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADIDAV--VVGNAAGGRFQSFPGAlIAEYLGLLGKPAtrveAAG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 239 lPGQGGAIIAAMMAVAAGLCRHVLCfrTVWESTYAALRLHGGGGRVSGPQ-QWSLPFGAASAANWIGVNANQYLHRYGAN 317
Cdd:cd00829   78 -ASGSAAVRAAAAAIASGLADVVLV--VGAEKMSDVPTGDEAGGRASDLEwEGPEPPGGLTPPALYALAARRYMHRYGTT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 318 RELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNASIGGDLPRPAIRCEAVGT 397
Cdd:cd00829  155 REDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTDRPVWILGVGA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 398 QVAERISWDQGTLTHEPQVIGQAAHLWSRTDLRPEDVDLALLYDGFTFNCVSWLEALGFCGFGEAQGWLDGGrRIALDGE 477
Cdd:cd00829  235 ASDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREG-DTAIGGD 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504754531 478 LPLNTHGGQLSEGRLH---GFGFLYEAVLQLRHQAGNRQVKDARTAVVSTGGGVPSGV 532
Cdd:cd00829  314 LPVNTSGGLLSKGHPLgatGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGTGSAA 371
PRK07855 PRK07855
lipid-transfer protein; Provisional
 159-535 3.33e-74

lipid-transfer protein; Provisional


Pssm-ID: 181147 [Multi-domain]  Cd Length: 386  Bit Score: 240.27  E-value: 3.33e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 159 RSVISGIGRSATGRRLMVDPLSLTMDACLAAVADAGLELSDIDGLSTYPgpvgmgMSEGGIAAVEEAL---------RIH 229
Cdd:PRK07855   5 KAAIVGIGATEFSKNSGRSELRLACEAVLAALDDAGLAPSDVDGLVTFT------MDTNPEIAVARALgigelkffsRIH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 230 ptwINGGmdlpGQGGAIIAAMMAVAAGLCRHVLCFRTVWESTyaALRLHGGGGRVSGPQ-------QWSLPFGAASAANW 302
Cdd:PRK07855  79 ---YGGG----AACATVQQAAMAVATGVADVVVCYRAFNERS--GMRFGQGQTGLAENPtstgvdyGWSYPHGLLTPAAW 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 303 IGVNANQYLHRYGANRELFGMIAVNARRNAALNPSAI-YREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNASI 381
Cdd:PRK07855 150 VAMLARRYMHEYGATSEDFGRVAVADRKHAATNPKAWfYGRPITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAER 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 382 GGDLPRPAIRCEAvgtqVAERISWDQGTLT--HEPQVIG------QAAHLWSRTDLRPEDVDLALLYDGFTFNCVSWLEA 453
Cdd:PRK07855 230 ARDLKQRPAVIKA----AAQGSGADQYMMTsyYRDDITGlpemglVARQLWAQSGLGPADIDTAILYDHFTPFVLMQLEE 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 454 LGFCGFGEAQGWLDGGrRIALDGELPLNTHGGQLSEGRLHGFGFLYEAVLQLRHQAGNrQVKDARTAVVSTGGGVPSGVM 533
Cdd:PRK07855 306 LGFCGRGEAKDFIADG-ALELGGRLPINTHGGQLGEAYIHGMNGIAEAVRQLRGTSVN-QVPGVENVLVTAGTGVPTSGL 383


                 ..
gi 504754531 534 LL 535
Cdd:PRK07855 384 IL 385
COG1545 COG1545
Uncharacterized OB-fold protein, contains Zn-ribbon domain [General function prediction only];
14-128 5.71e-37

Uncharacterized OB-fold protein, contains Zn-ribbon domain [General function prediction only];


Pssm-ID: 441154 [Multi-domain]  Cd Length: 116  Bit Score: 132.71  E-value: 5.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531  14 FWTSGKDGHLRIQHCSECDTYVHPPVPICPSCRATSAEPAVVSGRATVVGYTVNAHPWLP-GFEPPYVIAVVALDEcaEV 92
Cdd:COG1545    1 FWRALAEGRLLGQRCPACGTVYFPPRPVCPHCGSEDLEWVELSGRGTVYSYTVVHRPPPPfEDEVPYVVALVELDE--GV 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504754531  93 RLTTNIVGCSPEEVHVGQRVSVRFDNID--DVWIPLFE 128
Cdd:COG1545   79 RVLGRLVGVDPEDVRIGMRVRVVFRPIDedGRTLPVFR 116
OB_aCoA_assoc pfam01796
DUF35 OB-fold domain, acyl-CoA-associated; The structure of a DUF35 representative reveals two ...
 55-117 6.28e-15

DUF35 OB-fold domain, acyl-CoA-associated; The structure of a DUF35 representative reveals two long N-terminal helices followed by a rubredoxin-like zinc ribbon domain and a C-terminal OB fold domain represented in this entry. OB-folds are frequently found to bind nucleic acids suggesting this domain might bind to DNA or RNA (Topsan http://www.topsan.org/). Genomic context shows it to be adjacent to acyl-CoA transferase (http:/www.microbesonline.org/).


Pssm-ID: 460333  Cd Length: 65  Bit Score: 69.17  E-value: 6.28e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504754531   55 VSGRATVVGYTVNAHPWL-PGFEPPYVIAVVALDEcaEVRLTTNIVGCSPEEVHVGQRVSVRFD 117
Cdd:pfam01796   4 LSGRGTVYSYTVVHRPPPgFADDVPYVVGLVELDE--GPRVMARLVGVDPDEVRIGMRVRAVFR 65
 
Name Accession Description Interval E-value
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 164-532 1.30e-80

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: 256.81  E-value: 1.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 164 GIGRSATGRRLMVDPLSLTMDACLAAVADAGLELSDIDGLstYPGPVGMGMSEGGIAA-VEEALRIHPTWI----NGGmd 238
Cdd:cd00829    2 GVGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADIDAV--VVGNAAGGRFQSFPGAlIAEYLGLLGKPAtrveAAG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 239 lPGQGGAIIAAMMAVAAGLCRHVLCfrTVWESTYAALRLHGGGGRVSGPQ-QWSLPFGAASAANWIGVNANQYLHRYGAN 317
Cdd:cd00829   78 -ASGSAAVRAAAAAIASGLADVVLV--VGAEKMSDVPTGDEAGGRASDLEwEGPEPPGGLTPPALYALAARRYMHRYGTT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 318 RELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNASIGGDLPRPAIRCEAVGT 397
Cdd:cd00829  155 REDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTDRPVWILGVGA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 398 QVAERISWDQGTLTHEPQVIGQAAHLWSRTDLRPEDVDLALLYDGFTFNCVSWLEALGFCGFGEAQGWLDGGrRIALDGE 477
Cdd:cd00829  235 ASDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREG-DTAIGGD 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504754531 478 LPLNTHGGQLSEGRLH---GFGFLYEAVLQLRHQAGNRQVKDARTAVVSTGGGVPSGV 532
Cdd:cd00829  314 LPVNTSGGLLSKGHPLgatGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGTGSAA 371
PRK07855 PRK07855
lipid-transfer protein; Provisional
 159-535 3.33e-74

lipid-transfer protein; Provisional


Pssm-ID: 181147 [Multi-domain]  Cd Length: 386  Bit Score: 240.27  E-value: 3.33e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 159 RSVISGIGRSATGRRLMVDPLSLTMDACLAAVADAGLELSDIDGLSTYPgpvgmgMSEGGIAAVEEAL---------RIH 229
Cdd:PRK07855   5 KAAIVGIGATEFSKNSGRSELRLACEAVLAALDDAGLAPSDVDGLVTFT------MDTNPEIAVARALgigelkffsRIH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 230 ptwINGGmdlpGQGGAIIAAMMAVAAGLCRHVLCFRTVWESTyaALRLHGGGGRVSGPQ-------QWSLPFGAASAANW 302
Cdd:PRK07855  79 ---YGGG----AACATVQQAAMAVATGVADVVVCYRAFNERS--GMRFGQGQTGLAENPtstgvdyGWSYPHGLLTPAAW 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 303 IGVNANQYLHRYGANRELFGMIAVNARRNAALNPSAI-YREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNASI 381
Cdd:PRK07855 150 VAMLARRYMHEYGATSEDFGRVAVADRKHAATNPKAWfYGRPITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAER 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 382 GGDLPRPAIRCEAvgtqVAERISWDQGTLT--HEPQVIG------QAAHLWSRTDLRPEDVDLALLYDGFTFNCVSWLEA 453
Cdd:PRK07855 230 ARDLKQRPAVIKA----AAQGSGADQYMMTsyYRDDITGlpemglVARQLWAQSGLGPADIDTAILYDHFTPFVLMQLEE 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 454 LGFCGFGEAQGWLDGGrRIALDGELPLNTHGGQLSEGRLHGFGFLYEAVLQLRHQAGNrQVKDARTAVVSTGGGVPSGVM 533
Cdd:PRK07855 306 LGFCGRGEAKDFIADG-ALELGGRLPINTHGGQLGEAYIHGMNGIAEAVRQLRGTSVN-QVPGVENVLVTAGTGVPTSGL 383


                 ..
gi 504754531 534 LL 535
Cdd:PRK07855 384 IL 385
PRK06158 PRK06158
thiolase; Provisional
 159-530 5.47e-62

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 208.35  E-value: 5.47e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 159 RSVISGIGRSATGRRLMVDPLSLTMDACLAAVADAGLELSDIDGLSTYPGPVGM-GMSeggiaaVEEALRIHPTWINGGM 237
Cdd:PRK06158   9 RTAIVGAATAGLGEAPGLSAMELLAQAAHRALADAGLTMADVDGLFTASPDDALwGLS------VAEYLGIRPRFVDGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 238 dlpgQGGAI-----IAAMMAVAAGLCRHVLCfrtvwesTYAALRLHGGGGRVS--GPQQWSLPFGAASAANWIGVNANQY 310
Cdd:PRK06158  83 ----IGGSSflahlLPAALALEAGLCDVALI-------CYGSNQRSAGGKLRSmlDPQPYEAPYKPVNPVSAYALAAARH 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 311 LHRYGANRELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNASIGGDLPRPAI 390
Cdd:PRK06158 152 MHQYGTTREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAVVMVRADRARDLPRPPV 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 391 RCEAVGTQVAERISWDQGTLTHEPQVI-GQAAhlWSRTDLRPEDVDLALLYDGFTFNCVSWLEALGFCGFGEAQGWLDGG 469
Cdd:PRK06158 232 YVLGAAAATWHRQISSMPDLTVTAAAEsGPRA--FAMAGLTPADIDVVELYDAFTINTILFLEDLGFCAKGEGGAFVEGG 309

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504754531 470 rRIALDGELPLNTHGGQLS--EGRLHGFGFLYEAVLQLRHQAGNRQVKDARTAVVSTGGGVPS 530
Cdd:PRK06158 310 -RIAPGGRLPVNTNGGGLScvHPGMYGLFLLIEAVRQLRGEAGERQVAGAEVALAHGNGGVLS 371
COG1545 COG1545
Uncharacterized OB-fold protein, contains Zn-ribbon domain [General function prediction only];
14-128 5.71e-37

Uncharacterized OB-fold protein, contains Zn-ribbon domain [General function prediction only];


Pssm-ID: 441154 [Multi-domain]  Cd Length: 116  Bit Score: 132.71  E-value: 5.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531  14 FWTSGKDGHLRIQHCSECDTYVHPPVPICPSCRATSAEPAVVSGRATVVGYTVNAHPWLP-GFEPPYVIAVVALDEcaEV 92
Cdd:COG1545    1 FWRALAEGRLLGQRCPACGTVYFPPRPVCPHCGSEDLEWVELSGRGTVYSYTVVHRPPPPfEDEVPYVVALVELDE--GV 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504754531  93 RLTTNIVGCSPEEVHVGQRVSVRFDNID--DVWIPLFE 128
Cdd:COG1545   79 RVLGRLVGVDPEDVRIGMRVRVVFRPIDedGRTLPVFR 116
PRK06064 PRK06064
thiolase domain-containing protein;
285-528 1.20e-31

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 126.16  E-value: 1.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 285 SGPQQWSLPFGAASAANWiGVNANQYLHRYGANRELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDC 364
Cdd:PRK06064 130 AGDYEWEEFFGATFPGLY-ALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDC 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 365 DVPCDGSIAVVVSNASIGGDLPRPAIRCEAVGtQVAERISW-DQGTLTHEPQVIGQAAHLWSRTDLRPEDVDLALLYDGF 443
Cdd:PRK06064 209 SPITDGAAAVILASEEKAKEYTDTPVWIKASG-QASDTIALhDRKDFTTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCF 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 444 TFNCVSWLEALGFCGFGEAQGWLDGGrRIALDGELPLNTHGGQLSEGrlH-----GFGFLYEAVLQLRHQA--GNRQVKD 516
Cdd:PRK06064 288 TIAEILAYEDLGFAKKGEGGKLAREG-QTYIGGDIPVNPSGGLKAKG--HpvgatGVSQAVEIVWQLRGEAekGRQQVIG 364

                        250
                 ....*....|..
gi 504754531 517 ARTAVVSTGGGV 528
Cdd:PRK06064 365 AGYGLTHNVGGT 376
PRK12578 PRK12578
thiolase domain-containing protein;
159-537 1.45e-30

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 123.03  E-value: 1.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 159 RSVISGIGRSATGRRLMVDPLSLTMDACLAAVADAGLELSDID----------GLSTYPGP--------VGMG------M 214
Cdd:PRK12578   2 RVAVIGVGNSKFGRRDDVSVQELAWESIKEALNDAGVSQTDIElvvvgstayrGIELYPAPivaeysglTGKVplrveaM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 215 SEGGIAAVEEALrihpTWINGGMdlpgqggaiiaammaVAAGLCRHVLCFRTVWESTYAALrlhggGGRvSGPQQWSLPF 294
Cdd:PRK12578  82 CATGLAASLTAY----TAVASGL---------------VDMAIAVGVDKMTEVDTSTSLAI-----GGR-GGNYQWEYHF 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 295 GAASAANWIGVNANQYLHRYGANRELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAV 374
Cdd:PRK12578 137 YGTTFPTYYALYATRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATA 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 375 VVSNA----SIGGDLPrpaIRCEAVG-----TQVAERISWDQGTLTHEpqvigQAAHLWSRTDLRPEDVDLALLYDGFTF 445
Cdd:PRK12578 217 IFASEekvkELKIDSP---VWITGIGyandyAYVARRGEWVGFKATQL-----AARQAYNMAKVTPNDIEVATVHDAFTI 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 446 NCVSWLEALGFCGFGEAQGWLDGGRRiALDGELPLNTHGGQLSEGR---LHGFGFLYEAVLQLRHQAGNRQV--KDARTA 520
Cdd:PRK12578 289 AEIMGYEDLGFTEKGKGGKFIEEGQS-EKGGKVGVNLFGGLKAKGHplgATGLSMIYEITKQLRDEAGKLQQplKKYIGL 367

                        410
                 ....*....|....*...
gi 504754531 521 VVSTGG-GVPSGVMLLHR 537
Cdd:PRK12578 368 VHNVGGtGHFAYVMILRR 385
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
 158-530 5.32e-28

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 115.90  E-value: 5.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 158 HRSVISGIGRSATGRRLMVDPLSLTMDACLAAVADAGLELSDIDG--LSTYPGPVGMGMSegGIAaVEEALRIHPTWIN- 234
Cdd:PRK06157   7 DKVAILGMGCTKFGERWDAGAEDLMVEAFLEALADAGIEPKDIDAawFGTHYDEIGSGKS--GTP-LSRALRLPNIPVTr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 235 ------GGMDlpgqggaiiaammavaaglcrhvlCFRTvweSTYAA---------------LRLHGGGG---RVSGPQQW 290
Cdd:PRK06157  84 venfcaTGSE------------------------AFRG---AVYAVasgaydialalgvekLKDTGYGGlpvANPGTLAD 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 291 -SLPFGAASAAnwIGVNANQYLHRYGANRE----LFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDCD 365
Cdd:PRK06157 137 mTMPNVTAPGN--FAQLASAYAAKYGVSREdlkrAMAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCC 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 366 VPCDGSIAVVVSNASIGGDL-PRPAIRCEAVGTQV-----AERISWDqGTLTHEPQVIGQAAHLWSRTDLRPEDVDLALL 439
Cdd:PRK06157 215 GVSDGAAAAIVTTPEIARALgKKDPVYVKALQLAVsngweLQYNGWD-GSYFPTTRIAARKAYREAGITDPREELSMAEV 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 440 YDGFTFNCVSWLEALGFCGFGEA-QGWLDGgrRIALDGELPLNTHGGQLSEGrlH-----GFGFLYEAVLQLRHQAGNRQ 513
Cdd:PRK06157 294 HDCFSITELVTMEDLGLSERGQAwRDVLDG--FFDADGGLPCQIDGGLKCFG--HpigasGLRMLYEMYLQLLGRAGERQ 369

                        410
                 ....*....|....*..
gi 504754531 514 VKDARTAVVSTGGGVPS 530
Cdd:PRK06157 370 LKNPRLALTHNLGGAPG 386
PRK08256 PRK08256
lipid-transfer protein; Provisional
 294-520 5.42e-28

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 115.77  E-value: 5.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 294 FGAAsaanwigvnANQYLHRYGANRELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDCDVPCDGSIA 373
Cdd:PRK08256 149 FGGA---------GREHMEKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAA 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 374 -VVVSNA-----SIGGDLprpAIRCEAVGTQVAEriSWDQGTLthePQVIG------QAAHLWSRTDLRPEDVDLALLYD 441
Cdd:PRK08256 220 aIVCSEEfarkhGLDRAV---EIVAQAMTTDTPS--TFDGRSM---IDLVGydmtraAAQQVYEQAGIGPEDIDVVELHD 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 442 GFTFNCVSWLEALGFCGFGEAQGWLDGGRrialdgelplNTHGGQ---------LSEGrlH-----GFGFLYEAVLQLRH 507
Cdd:PRK08256 292 CFSANELLTYEALGLCPEGEAEKFIDDGD----------NTYGGRwvvnpsgglLSKG--HplgatGLAQCAELTWQLRG 359

                        250
                 ....*....|...
gi 504754531 508 QAGNRQVKDARTA 520
Cdd:PRK08256 360 TAGARQVEGARLA 372
PRK06066 PRK06066
thiolase domain-containing protein;
304-530 1.15e-26

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 111.77  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 304 GVNANQYLHRYGANRELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNASIGG 383
Cdd:PRK06066 147 GLDAVKFMSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAK 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 384 DLPRPAIRCEAVGtqvaerisWDQGTLTHEPQVIGQAAHLWSRTDL--------RPE-DVDLALLYDGFTFNCVSWLEAL 454
Cdd:PRK06066 227 KLTDDPVWIKGIG--------WSTESSNLETAELGKANYMRIAADMaykmagieSPRkEVDAAEVDDRYSYKELQHIEAL 298

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504754531 455 GFCGFGEAQGWLDGGrRIALDGELPLNTHGGQLSEGRL---HGFGFLYEAVLQLRHQAGNRQvKDARTAVVSTGGGVPS 530
Cdd:PRK06066 299 RLSEEPEKDSLLREG-NFDPQGELPVNPSGGHLAKGVPleaSGLSLLLDAVEYLRGEAGARQ-GKAERAVVASWRGIPT 375
PRK08142 PRK08142
thiolase domain-containing protein;
279-531 5.70e-26

thiolase domain-containing protein;


Pssm-ID: 236164 [Multi-domain]  Cd Length: 388  Bit Score: 109.79  E-value: 5.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 279 GGGGRVSGPQ----QWSLPFGAASAaNWIGVNANQYLHRYGANRELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARP 354
Cdd:PRK08142 119 GTEPRNWGADapdaPFEAPYGPTTH-NLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPM 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 355 ITSPFGLYDCDVPCDGSIAVVVSNASIGGDLPRPAIRC----EAVGTQVAER--ISWDQGTLThEPQVIGQAAhlwsrtd 428
Cdd:PRK08142 198 IADPLHRLDCCVVTDGGGALVVVRPEIARSLKRPLVKVlgagEAIKGQMGGKvdLTYSGAAWS-GPAAFAEAG------- 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 429 LRPEDVDLALLYDGFTFNCVSWLEALGFCGFGEAQGWLDGGRRIALDGELPLNTHGGQLSE---GRLHGFGFLYEAVLQL 505
Cdd:PRK08142 270 VTPADIKYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGVGKLPFNTDGGGLCNnhpANRGGMTKVIEAVRQL 349

                        250       260
                 ....*....|....*....|....*...
gi 504754531 506 RHQAG-NRQVKDARTAVVS-TGGGVPSG 531
Cdd:PRK08142 350 RGEAHpAVQVPNCDLALAHgTGGLLGSR 377
PRK06059 PRK06059
lipid-transfer protein; Provisional
 185-526 2.14e-25

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 108.31  E-value: 2.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 185 ACLAAVADAGLELSDIDGLST-------YPGPVGMgmseggiAAVEEALRIHPTWINGGMDLPGQGGAIIAAMMAV-AAG 256
Cdd:PRK06059  30 AARAALADAGLDWRDVQLVVGadtirngYPGFVAG-------ATFAQALGWNGAPVSSSYAACASGSQALQSARAQiLAG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 257 LCRHVLCFRTvwESTYAALRLHGGGGRVSGP--QQWSLpFGAASAANWiGVNANQYLHRYGANRELFGMIAVNARRNAAL 334
Cdd:PRK06059 103 LCDVALVVGA--DTTPKGFFAPVGGERPDDPdwLRFHL-IGATNPVYF-ALLARRRMDLYGATVEDFAQVKVKNARHGLL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 335 NPSAIYREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNAS----IGGDLPRPaIRCEAVGTQ-------VAE-- 401
Cdd:PRK06059 179 NPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSfarrHLGSVAGV-PSVRAISTVtprypqhLPElp 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 402 RISWDQGTLTHEPQV-----IGQAAhlWSRTDLRPEDVDLALLYDGFTFNCVSWLEALGFCGFGEAQGWLDGGrRIALDG 476
Cdd:PRK06059 258 DIATDSTAAVPAPERvfkdqILDAA--YAEAGIGPEDLSLAEVYDLSTALELDWYEHLGLCPKGEAEALLRSG-ATTLGG 334

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504754531 477 ELPLNTHGGQLSEGR---LHGFGFLYEAVLQLRHQAGNRQVKDARTAVVSTGG 526
Cdd:PRK06059 335 RIPVNPSGGLACFGEaipAQAIAQVCELTWQLRGQAGGRQVEGARVGITANQG 387
PRK08313 PRK08313
thiolase domain-containing protein;
158-527 7.35e-25

thiolase domain-containing protein;


Pssm-ID: 181378 [Multi-domain]  Cd Length: 386  Bit Score: 106.35  E-value: 7.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 158 HRSVISGIGRSA-TGRRLMVDPLSLTMDACLAAVADAGLELSDIDGLSTYPGP---VGMGMSE----GGIAAVEEAL-RI 228
Cdd:PRK08313   3 RLAAVLGTGQTKyVAKRQDVSMAGLVREAIDRALADAGLTWDDIDAVVVGKAPdffEGVMMPElflaDALGATGKPLiRV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 229 HPTWINGGmdlpgqgGAIIAAMMAVAAGLCRHVLcfrTV-WESTYAALRLHGgggrVSGPQQWSLPFGAAsAANWIGVNA 307
Cdd:PRK08313  83 HTAGSVGG-------STAVVAASLVQSGVYRRVL---AVaWEKQSESNAMWA----LSIPVPFTKPVGAG-AGGYFAPHV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 308 NQYLHRYGANRELFGMIAVNARRNAALNPSAIYREP-MTMDDYLAARPITSPFgLYDCDVPC-DGSIAVVVSNASIGGDL 385
Cdd:PRK08313 148 RAYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLHQPdITLEKVMASQMLWDPI-RFDETCPSsDGACAVVIGDEEAADAA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 386 -PRPAIRCEAVGTQvAERISwDQGTLTHEPQV-IGQAAHLWSR---TDLRPEdVDLALLYDGFTFNCVSWLEALGFCGFG 460
Cdd:PRK08313 227 aGRPVAWIHGTAMR-TEPLA-FAGRDQVNPQAgRDAAAALWKAagiTDPRDE-IDVAEIYVPFSWFEPMWLENLGFAPEG 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 461 EaqGW-LDGGRRIALDGELPLNTHGGQLSEGRLHGFGFL--YEAVLQLRHQAGNRQVKDARTAVVSTGGG 527
Cdd:PRK08313 304 E--GWkLTEAGETAIGGRLPVNPSGGVLSSNPIGASGMIrfAEAALQVMGKAGEHQVDGARKALGHAYGG 371
PRK06065 PRK06065
thiolase domain-containing protein;
156-515 2.98e-17

thiolase domain-containing protein;


Pssm-ID: 180379 [Multi-domain]  Cd Length: 392  Bit Score: 83.72  E-value: 2.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 156 FEHRSVISGIGRSATGRRLMVDPLSLTMDACLAAVADAGLELSDIDGLSTYPGP--------VGMGMSEGGIAAVEEALR 227
Cdd:PRK06065   7 LNKRVAVIGAGLTLFRRRLLETPQELAWEAASKALDEAGLELKDIDCVVIGSAPdafdgvhmKGEYLSHGSGGIRKPVSR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 228 IHPTWINGGMdlpgqggAIIAAMMAVAAGLCRHVLcfrTVWESTYAALRLHggggrvsgPQQ-----WSLPFGAASAAN- 301
Cdd:PRK06065  87 VYVGGATGVM-------TAIAGWYHVASGLCQKVL---AVAEEKMSPARPH--------PQAvfryiWDPILEKPLNPNl 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 302 -WI-GVNANQYLHRYGANRELFGMIAVNARRNAALNPSAIYREPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNA 379
Cdd:PRK06065 149 iWIfAMEMHRYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASE 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 380 SIGGDLPRPAIRCEAVGTQVaERISWDQGTLTHePQVIGQAAHLWSRTD--LRP-EDVDLALLYDGFTFNCVSWLEALGF 456
Cdd:PRK06065 229 DLARRYTDTPVWVEGVGWTL-DNTEWPNRDLAY-PRYVEFAARMAYKMAgiERPrKEIDVAEPYDPFDYKELHHLEGLQL 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504754531 457 CGFGEA-----QGWLDggrriaLDGELPLNTHGGQLSEGR---LHGFGFLYEAVLQLRHQAGNRQVK 515
Cdd:PRK06065 307 AKRGEApkllkEGVFD------IDGDIPSSPSGGLLGVGNpiaAAGLMKVISIYWQLKGTAGKMQVK 367
OB_aCoA_assoc pfam01796
DUF35 OB-fold domain, acyl-CoA-associated; The structure of a DUF35 representative reveals two ...
 55-117 6.28e-15

DUF35 OB-fold domain, acyl-CoA-associated; The structure of a DUF35 representative reveals two long N-terminal helices followed by a rubredoxin-like zinc ribbon domain and a C-terminal OB fold domain represented in this entry. OB-folds are frequently found to bind nucleic acids suggesting this domain might bind to DNA or RNA (Topsan http://www.topsan.org/). Genomic context shows it to be adjacent to acyl-CoA transferase (http:/www.microbesonline.org/).


Pssm-ID: 460333  Cd Length: 65  Bit Score: 69.17  E-value: 6.28e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504754531   55 VSGRATVVGYTVNAHPWL-PGFEPPYVIAVVALDEcaEVRLTTNIVGCSPEEVHVGQRVSVRFD 117
Cdd:pfam01796   4 LSGRGTVYSYTVVHRPPPgFADDVPYVVGLVELDE--GPRVMARLVGVDPDEVRIGMRVRAVFR 65
PRK06365 PRK06365
thiolase domain-containing protein;
290-532 2.91e-14

thiolase domain-containing protein;


Pssm-ID: 235785 [Multi-domain]  Cd Length: 430  Bit Score: 74.95  E-value: 2.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 290 WSLPFGAASAAnWIGVNANQYLHRYGANRELFGMIAVNARRNAALNPSAiyREPM--TMDDYLAARPITSPFGLYDCDVP 367
Cdd:PRK06365 149 FDYPLGGFYTG-YYAMMAVRHMYEFGTTVEQLAKVSVKNHGNAIHNPFA--QSPMkiTVEDVRKSPMVSYPLTRLDVCAM 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 368 CDGSIAVVVSNASIGGDLPRPAIRCEAVGT-----QVAERISWDQGTLTHE----------PQVIG------QAAHLWSR 426
Cdd:PRK06365 226 SDGAACAILASEDKAFEITDKPVLIKAIGTgsdtlRLADRPFGEVPLLPNEspddykdlryPGVHSfragrmAAKEAYEM 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 427 TDLRP--EDVDLALLYDGFTFNCVSWLEALGFCGFGEAQGWLDGGRRiALDGELPLNTHGGQLSEGRLHGFGFLYEAVLQ 504
Cdd:PRK06365 306 AGITDplNDLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESGKP-ELPGKLPVNPSGGLLAAGHAVGATGIMQAVFM 384

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 504754531 505 L--------RHQAGNR-QVKDARTAVVSTGGGVPSGV 532
Cdd:PRK06365 385 FwqlqgrikKHFHDDYlQVKNAKRGLIHSHAGTGTYV 421
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
 307-527 2.99e-13

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 71.64  E-value: 2.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 307 ANQYLHRYGANRELFGMIAVNARRNAALNPSAIYR-----EPMTMDDYLAARPITSPFGLYDCDVPCDGSIAVVVSNASI 381
Cdd:PRK06289 157 ADEYDRRYGLDEEHLRAIAEINFANARRNPNAQTRgwafpDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLASDAY 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 382 GGDLP--RPAIRCEAVGTQVA-----ERISWDQGTLTHEPQVIGQAAHLWSRTDLRPEDVDLALLYDGFTFNCVSWLEAL 454
Cdd:PRK06289 237 LRDYAdaRPIPRIKGWGHRTAplgleQKLDRSAGDPYVLPHVRQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHI 316

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504754531 455 GFCGFGEAQGWLDGGrRIALDGELPLNTHGGQLSEGrlHGFG-----FLYEAVLQLRHQAGNRQVKDARTAVVSTGGG 527
Cdd:PRK06289 317 GLTGPGESWKAIENG-EIAIGGRLPINPSGGLIGGG--HPVGasgvrMLLDAAKQVTGTAGDYQVEGAKTFGTLNIGG 391
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
 304-536 1.28e-12

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: 69.44  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 304 GVNANQYLHRYGANRELFGMIAVNARR---NAALNPSAIYREPMTMDDYLAARPITSPFGLY---DCDVPCDGSIAVVVS 377
Cdd:cd00826  148 GQAGAEAAEKDGRFKDEFAKFGVKGRKgdiHSDADEYIQFGDEASLDEIAKLRPAFDKEDFLtagNACGLNDGAAAAILM 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 378 NASiggDLPRPAIRCEAVGTQVAERISwDQGTLTHEPQVIGQ---------AAHLWSRTDLRPEDVDLALLYDGFTFNCV 448
Cdd:cd00826  228 SEA---EAQKHGLQSKAREIQALEMIT-DMASTFEDKKVIKMvggdgpieaARKALEKAGLGIGDLDLIEAHDAFAANAC 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 449 SWLEALGFCGFGEAQGWLDGGRRiALDGELPLNTHGGQLSEGR---LHGFGFLYEAVLQLRHQAGNRQVKDARTAVVSTG 525
Cdd:cd00826  304 ATNEALGLCPEGQGGALVDRGDN-TYGGKSIINPNGGAIAIGHpigASGAAICAELCFELKGEAGKRQGAGAGLALLCIG 382

                        250
                 ....*....|.
gi 504754531 526 GGVPSGVMLLH 536
Cdd:cd00826  383 GGGGAAMCIES 393
PRK07516 PRK07516
thiolase domain-containing protein;
307-528 1.70e-09

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 59.58  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 307 ANQYLHRYGANRELFGMIAVNARRNAALNPSAIYREPMTMD---------DYLAArpitsPFGLYDCDVPCDGSIAVVVS 377
Cdd:PRK07516 151 AQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEfcrtvseknPLVAG-----PLRRTDCSLVSDGAAALVLA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 378 NASIGGDLPRpAIRCEAVGtQV---------------AERISWDQGtlthepqvIGQAAhlwsrtdLRPEDVDLALLYDG 442
Cdd:PRK07516 226 DAETARALQR-AVRFRARA-HVndflplsrrdplafeGPRRAWQRA--------LAQAG-------VTLDDLSFVETHDC 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 443 FTFNCVSWLEALGFCGFGEAQGWLDGGrRIALDGELPLNTHGGQLSEGrlH-----GFGFLYEAVLQLRHQAGNRQVKDA 517
Cdd:PRK07516 289 FTIAELIEYEAMGLAPPGQGARAIREG-WTAKDGKLPVNPSGGLKAKG--HpigatGVSMHVLAAMQLTGEAGGMQIPGA 365

                        250
                 ....*....|.
gi 504754531 518 RTAVVSTGGGV 528
Cdd:PRK07516 366 KLAGVFNMGGA 376
DUF35_N pfam12172
Rubredoxin-like zinc ribbon domain (DUF35_N); This domain has no known function and is found ...
 15-51 6.45e-08

Rubredoxin-like zinc ribbon domain (DUF35_N); This domain has no known function and is found in conserved hypothetical archaeal and bacterial proteins. The domain is duplicated in Swiss:O53566. The structure of a DUF35 representative reveals two long N-terminal helices followed by a rubredoxin-like zinc ribbon domain represented in this family and a C-terminal OB fold domain. Zinc is chelated by the four conserved cysteines in the alignment.


Pssm-ID: 463482  Cd Length: 37  Bit Score: 48.48  E-value: 6.45e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 504754531   15 WTSGKDGHLRIQHCSECDTYVHPPVPICPSCRATSAE 51
Cdd:pfam12172   1 WEALAEGRLVGQRCPDCGTVRFPPRAVCPHCGSRDLE 37
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
 420-523 3.33e-06

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 49.51  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504754531 420 AAHLWSRTDLRPEDVDLALLYDGFTFNCVSWLEALGFCGFGEAQGWLDGGrRIALDGELPLNTHGGQLSEGR---LHGFG 496
Cdd:PTZ00455 315 AQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYGHAKDLIRNG-ATALEGRIPVNTGGGLLSFGHpvgATGVK 393

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 504754531 497 FLYEAVLQLRHQAGNRQVK-------------DARTAVVS 523
Cdd:PTZ00455 394 QIMEVYRQMKGQCGEYQMKnipalgatlnmggDDKTAVST 433
 
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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