NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1129374802|ref|WP_075339461|]
View 

MULTISPECIES: acyl CoA:acetate/3-ketoacid CoA transferase [Staphylococcus]

Protein Classification

acyl CoA:acetate/3-ketoacid CoA transferase( domain architecture ID 11468716)

acyl CoA:acetate/3-ketoacid CoA transferase similar to Escherichia coli acetate CoA-transferase YdiF, which has broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
7-516 0e+00

Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];


:

Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 679.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802   7 KQITWHDLQHIIKDGDVIGLPALAVANLPAEVLRAVLAQHDTYHTPKDLTFILANDIHSlGAAPDLDDFIERRMIKRVIM 86
Cdd:COG4670     2 KIISAEEAAALIKDGDTVATSGFVGAGVPEELLKALEERFLETGHPRDLTLIHAAGQGD-GKGRGLDHLAHEGLVKRVIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  87 SILTASSKTAQAMKNNDIEAYFLPQGIIATHYRQSNQLLPGVITKIGLNTAVDPRYGGGKVNTRTTDDLVSLVTINDETY 166
Cdd:COG4670    81 GHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVDPRLEGGKLNERTTEDLVELVEIDGEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 167 LHYTFPSVDVALLRGTYADQQGNIYLTQEAYLSECYHVALNAKANHGKVIVQVKALVDDYQLKPNEVVIPGNLVDYVYVT 246
Cdd:COG4670   161 LFYKAFPIDVALIRGTTADEDGNLSMEHEALTLEVLAIAQAAKNSGGIVIAQVERIVKRGSLHPKDVKVPGILVDYVVVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 247 EDEkNHCQVIQSHYLPALSGEERIDGIPEPALPFNSRKLILRRAAQFLTYGDTISIGYGINNELSNLLHEECVEHDVQPI 326
Cdd:COG4670   241 PPE-DHMQTFSTQYNPAYSGEIRVPLSSLPPLPLDERKVIARRAAMELRPGAVVNLGIGIPEGVAAVAAEEGISDLITLT 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 327 LDVGIFGGFVGSREHFGMNYNADVRMPHDRAWDFIYNNGVSVAYLSFAEVDQYGNVNVSYFNDRLNGCGGFIDITQSVNK 406
Cdd:COG4670   320 VESGPIGGVPAGGLDFGAAVNAEAIIDQPDQFDFYDGGGLDIAFLGFAQVDRHGNVNVSKFGGRIAGCGGFINITQNAKK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 407 IIFSGTFVAGS-HVSCHNQRLNIETEGQNQKFVSDVSHIDFNAQYSQLLEQEVYFVTDRAVFELTNQGLKLIEIAPGLDL 485
Cdd:COG4670   400 VVFCGTFTAGGlKVEVEDGKLRILQEGKIKKFVKKVEQITFSGKYARERGQEVLYVTERAVFELTPEGLELTEIAPGIDL 479
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1129374802 486 HKDILNQMAFKPIIADHLKLIDTSIYKEKWG 516
Cdd:COG4670   480 ERDILAQMEFRPIIADDLKLMDARIFRDEPM 510
 
Name Accession Description Interval E-value
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
7-516 0e+00

Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 679.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802   7 KQITWHDLQHIIKDGDVIGLPALAVANLPAEVLRAVLAQHDTYHTPKDLTFILANDIHSlGAAPDLDDFIERRMIKRVIM 86
Cdd:COG4670     2 KIISAEEAAALIKDGDTVATSGFVGAGVPEELLKALEERFLETGHPRDLTLIHAAGQGD-GKGRGLDHLAHEGLVKRVIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  87 SILTASSKTAQAMKNNDIEAYFLPQGIIATHYRQSNQLLPGVITKIGLNTAVDPRYGGGKVNTRTTDDLVSLVTINDETY 166
Cdd:COG4670    81 GHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVDPRLEGGKLNERTTEDLVELVEIDGEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 167 LHYTFPSVDVALLRGTYADQQGNIYLTQEAYLSECYHVALNAKANHGKVIVQVKALVDDYQLKPNEVVIPGNLVDYVYVT 246
Cdd:COG4670   161 LFYKAFPIDVALIRGTTADEDGNLSMEHEALTLEVLAIAQAAKNSGGIVIAQVERIVKRGSLHPKDVKVPGILVDYVVVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 247 EDEkNHCQVIQSHYLPALSGEERIDGIPEPALPFNSRKLILRRAAQFLTYGDTISIGYGINNELSNLLHEECVEHDVQPI 326
Cdd:COG4670   241 PPE-DHMQTFSTQYNPAYSGEIRVPLSSLPPLPLDERKVIARRAAMELRPGAVVNLGIGIPEGVAAVAAEEGISDLITLT 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 327 LDVGIFGGFVGSREHFGMNYNADVRMPHDRAWDFIYNNGVSVAYLSFAEVDQYGNVNVSYFNDRLNGCGGFIDITQSVNK 406
Cdd:COG4670   320 VESGPIGGVPAGGLDFGAAVNAEAIIDQPDQFDFYDGGGLDIAFLGFAQVDRHGNVNVSKFGGRIAGCGGFINITQNAKK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 407 IIFSGTFVAGS-HVSCHNQRLNIETEGQNQKFVSDVSHIDFNAQYSQLLEQEVYFVTDRAVFELTNQGLKLIEIAPGLDL 485
Cdd:COG4670   400 VVFCGTFTAGGlKVEVEDGKLRILQEGKIKKFVKKVEQITFSGKYARERGQEVLYVTERAVFELTPEGLELTEIAPGIDL 479
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1129374802 486 HKDILNQMAFKPIIADHLKLIDTSIYKEKWG 516
Cdd:COG4670   480 ERDILAQMEFRPIIADDLKLMDARIFRDEPM 510
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
18-243 1.40e-36

Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.


Pssm-ID: 214882 [Multi-domain]  Cd Length: 212  Bit Score: 134.64  E-value: 1.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802   18 IKDGDVIGLPALAVANLPAEVLRAVLAQHdtyhtPKDLTFILANdihslgAAPDLDDFIERRMIKRVIMSILTASSKTAQ 97
Cdd:smart00882   9 IKDGDTVALGGFGGLPTPAALILALIRQG-----PKDLTLISEN------GGLGLGLLAGEGDVKKIIAGHVGLTPLLGR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802   98 AMKNNDIEAYFLPQGIIATHYRQSNQLLPGVITKIGLNTAVDPRYGGGKVNTRTTddlvslvtinDETYLHYTFPSVDVA 177
Cdd:smart00882  78 LYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYEGGKVRPFGM----------GGAYLLVPAIRPDVA 147
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1129374802  178 LLRGTYADQQGNIYLTQEAYLSECYHVALNAKanhgKVIVQVKALVDDYQLKPNEV--VIPGNLVDYV 243
Cdd:smart00882 148 LIRAHTADEFGNLVYEKEATSCGLPLTAAAAK----KVIVQVEEIVDLGVLDPDPVrlLIPGVLVDAV 211
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
7-248 6.95e-15

acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 73.63  E-value: 6.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802   7 KQITWHDLQHIIKDGDVIGLPALAVANLPAEVLRAVLAQhdtyhTPKDLTFIlANDIHSL--GAAPdlddFIERRMIKRV 84
Cdd:PRK09920    4 KLMTLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLES-----GVRDLTLI-ANDTAFVdtGIGP----LIVNGRVKKV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  85 IMSILTASSKTAQAMKNNDIEAYFLPQGIIATHYRQSNQLLPGVITKIGLNTAVDPryggGKvntrttddlvSLVTINDE 164
Cdd:PRK09920   74 IASHIGTNPETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEE----GK----------QTLTLDGK 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 165 TYLHYTFPSVDVALLRGTYADQQGNIyltqeaylseCYH---------VALNAKanhgKVIVQVKALVDDYQLKPNEVVI 235
Cdd:PRK09920  140 TWLLERPLRADLALIRAHRADTLGNL----------TYQlsarnfnplIALAAD----ITLVEPDELVETGELQPDHIVT 205
                         250
                  ....*....|...
gi 1129374802 236 PGNLVDYVYVTED 248
Cdd:PRK09920  206 PGAVIDHIIVSQE 218
CoA_trans pfam01144
Coenzyme A transferase;
18-245 3.23e-12

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 65.78  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  18 IKDGDVIGLPALAVANLPAEVLRAVLAQhdtyhTPKDLTFIlandiHSLGAAPDLDDFIERRMIKRVIMSI--LTASSKT 95
Cdd:pfam01144  12 IKDGMTVNVGGFGLIGIPETLIAALARS-----GVKDLTVI-----SNEAGVLGLGPLLLNGSVKKVIASYggETANPEF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  96 AQAMKNNDIEAYFLPQGIIATHYRQSNQLLP--GVITKIGLNTAVDPRygggkvntrttddlVSLVTINDETYLHYTFPS 173
Cdd:pfam01144  82 GRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPK--------------KRVPGFGGAMYLLEPALR 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129374802 174 VDVALLRGTYADQQGNIyltqeAYLSECYHVALNAKANHGKV-IVQVKALVDDYQLKPNEVVIPGNLVDYVYV 245
Cdd:pfam01144 148 ADVALIKASKADGEGNL-----VFRTTAPNFNGPAVAAAAKVtILEVEEIVEKGELLPLTVHTPGVLVDAVVE 215
 
Name Accession Description Interval E-value
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
7-516 0e+00

Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 679.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802   7 KQITWHDLQHIIKDGDVIGLPALAVANLPAEVLRAVLAQHDTYHTPKDLTFILANDIHSlGAAPDLDDFIERRMIKRVIM 86
Cdd:COG4670     2 KIISAEEAAALIKDGDTVATSGFVGAGVPEELLKALEERFLETGHPRDLTLIHAAGQGD-GKGRGLDHLAHEGLVKRVIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  87 SILTASSKTAQAMKNNDIEAYFLPQGIIATHYRQSNQLLPGVITKIGLNTAVDPRYGGGKVNTRTTDDLVSLVTINDETY 166
Cdd:COG4670    81 GHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVDPRLEGGKLNERTTEDLVELVEIDGEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 167 LHYTFPSVDVALLRGTYADQQGNIYLTQEAYLSECYHVALNAKANHGKVIVQVKALVDDYQLKPNEVVIPGNLVDYVYVT 246
Cdd:COG4670   161 LFYKAFPIDVALIRGTTADEDGNLSMEHEALTLEVLAIAQAAKNSGGIVIAQVERIVKRGSLHPKDVKVPGILVDYVVVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 247 EDEkNHCQVIQSHYLPALSGEERIDGIPEPALPFNSRKLILRRAAQFLTYGDTISIGYGINNELSNLLHEECVEHDVQPI 326
Cdd:COG4670   241 PPE-DHMQTFSTQYNPAYSGEIRVPLSSLPPLPLDERKVIARRAAMELRPGAVVNLGIGIPEGVAAVAAEEGISDLITLT 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 327 LDVGIFGGFVGSREHFGMNYNADVRMPHDRAWDFIYNNGVSVAYLSFAEVDQYGNVNVSYFNDRLNGCGGFIDITQSVNK 406
Cdd:COG4670   320 VESGPIGGVPAGGLDFGAAVNAEAIIDQPDQFDFYDGGGLDIAFLGFAQVDRHGNVNVSKFGGRIAGCGGFINITQNAKK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 407 IIFSGTFVAGS-HVSCHNQRLNIETEGQNQKFVSDVSHIDFNAQYSQLLEQEVYFVTDRAVFELTNQGLKLIEIAPGLDL 485
Cdd:COG4670   400 VVFCGTFTAGGlKVEVEDGKLRILQEGKIKKFVKKVEQITFSGKYARERGQEVLYVTERAVFELTPEGLELTEIAPGIDL 479
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1129374802 486 HKDILNQMAFKPIIADHLKLIDTSIYKEKWG 516
Cdd:COG4670   480 ERDILAQMEFRPIIADDLKLMDARIFRDEPM 510
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
18-243 1.40e-36

Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.


Pssm-ID: 214882 [Multi-domain]  Cd Length: 212  Bit Score: 134.64  E-value: 1.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802   18 IKDGDVIGLPALAVANLPAEVLRAVLAQHdtyhtPKDLTFILANdihslgAAPDLDDFIERRMIKRVIMSILTASSKTAQ 97
Cdd:smart00882   9 IKDGDTVALGGFGGLPTPAALILALIRQG-----PKDLTLISEN------GGLGLGLLAGEGDVKKIIAGHVGLTPLLGR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802   98 AMKNNDIEAYFLPQGIIATHYRQSNQLLPGVITKIGLNTAVDPRYGGGKVNTRTTddlvslvtinDETYLHYTFPSVDVA 177
Cdd:smart00882  78 LYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYEGGKVRPFGM----------GGAYLLVPAIRPDVA 147
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1129374802  178 LLRGTYADQQGNIYLTQEAYLSECYHVALNAKanhgKVIVQVKALVDDYQLKPNEV--VIPGNLVDYV 243
Cdd:smart00882 148 LIRAHTADEFGNLVYEKEATSCGLPLTAAAAK----KVIVQVEEIVDLGVLDPDPVrlLIPGVLVDAV 211
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
18-243 1.62e-19

Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 441394  Cd Length: 226  Bit Score: 87.45  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  18 IKDGDVIGLPALAVANLPAEVLRAVLAQHdtyhtPKDLTFIlANDihslGAAPDLDDFIERRMIKRVIMSILTA---SSK 94
Cdd:COG1788    15 VKDGMTIAIGGFGLCGIPMALIDELIRQG-----VKDLTLI-SNN----AGVDGLGLLIGAGQVKKVIASYVGGvglNPE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  95 TAQAMKNNDIEAYFLPQGIIATHYRQSNQLLPGVITKIGLNTAVdpryGGGKvntrttddlvSLVTINDETYLHYTFPSV 174
Cdd:COG1788    85 FRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDV----AEGK----------ETREIDGEEYVLEPALRA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1129374802 175 DVALLRGTYADQQGN--IYLTQEAYLSECyhvALNAKanhgKVIVQVKALVDDYQLKPNEVVIPGNLVDYV 243
Cdd:COG1788   151 DVALIHAQKADRAGNlvYRGTARNFNPLM---AMAAK----RVIVEVEEIVEVGELDPDAVVTPGIFVDAV 214
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
7-248 6.95e-15

acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 73.63  E-value: 6.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802   7 KQITWHDLQHIIKDGDVIGLPALAVANLPAEVLRAVLAQhdtyhTPKDLTFIlANDIHSL--GAAPdlddFIERRMIKRV 84
Cdd:PRK09920    4 KLMTLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLES-----GVRDLTLI-ANDTAFVdtGIGP----LIVNGRVKKV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  85 IMSILTASSKTAQAMKNNDIEAYFLPQGIIATHYRQSNQLLPGVITKIGLNTAVDPryggGKvntrttddlvSLVTINDE 164
Cdd:PRK09920   74 IASHIGTNPETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEE----GK----------QTLTLDGK 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 165 TYLHYTFPSVDVALLRGTYADQQGNIyltqeaylseCYH---------VALNAKanhgKVIVQVKALVDDYQLKPNEVVI 235
Cdd:PRK09920  140 TWLLERPLRADLALIRAHRADTLGNL----------TYQlsarnfnplIALAAD----ITLVEPDELVETGELQPDHIVT 205
                         250
                  ....*....|...
gi 1129374802 236 PGNLVDYVYVTED 248
Cdd:PRK09920  206 PGAVIDHIIVSQE 218
CoA_trans pfam01144
Coenzyme A transferase;
18-245 3.23e-12

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 65.78  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  18 IKDGDVIGLPALAVANLPAEVLRAVLAQhdtyhTPKDLTFIlandiHSLGAAPDLDDFIERRMIKRVIMSI--LTASSKT 95
Cdd:pfam01144  12 IKDGMTVNVGGFGLIGIPETLIAALARS-----GVKDLTVI-----SNEAGVLGLGPLLLNGSVKKVIASYggETANPEF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802  96 AQAMKNNDIEAYFLPQGIIATHYRQSNQLLP--GVITKIGLNTAVDPRygggkvntrttddlVSLVTINDETYLHYTFPS 173
Cdd:pfam01144  82 GRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPK--------------KRVPGFGGAMYLLEPALR 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129374802 174 VDVALLRGTYADQQGNIyltqeAYLSECYHVALNAKANHGKV-IVQVKALVDDYQLKPNEVVIPGNLVDYVYV 245
Cdd:pfam01144 148 ADVALIKASKADGEGNL-----VFRTTAPNFNGPAVAAAAKVtILEVEEIVEKGELLPLTVHTPGVLVDAVVE 215
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
279-504 6.58e-12

Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];


Pssm-ID: 441660  Cd Length: 235  Bit Score: 65.18  E-value: 6.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 279 PFNSRKLILRRAAQFLTYGDTISIGYGINNELSNLL---HE-ECVEHDVQPILDVGIFGgFVGSREHFGMNYNADVRMPH 354
Cdd:COG2057     1 AYTTRELMAVRAARELRDGEVVNLGIGLPTLAANLApltHApDVTLQSENGLLGPGPAP-LPGSVGDPDLINAGKQFFDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 355 DRAWDFIYNNGVSVAYLSFAEVDQYGNVNVSYFND------RLNGCGGFIDITQSVNKIIfsgtfVAGSHVschnqrlni 428
Cdd:COG2057    80 ADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIGDydkpgkRLPGMGGAMDLAAGAKRVI-----VVMEHS--------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129374802 429 etegqNQKFVSDVS------HIDfnaqysqlleQEVYFVTDRAVFELTNQ-GLKLIEIAPGLDLhKDILNQMAFKPIIAD 501
Cdd:COG2057   146 -----KRKFVEKCDlltgpgVVD----------GPRRVITDLAVFDFDPEkGLVLRELHPGVTV-EEVQENTGFELIVAD 209

                  ...
gi 1129374802 502 HLK 504
Cdd:COG2057   210 DVP 212
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH