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Conserved domains on  [gi|1441380651|ref|WP_114913431|]
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CoA transferase subunit A [Acidibrevibacterium fodinaquatile]

Protein Classification

CoA transferase subunit A( domain architecture ID 10004510)

CoA transferase subunit A is part of a complex that catalyzes the reversible transfer of CoA from one carboxylic acid to another

CATH:  3.40.1080.10
Gene Ontology:  GO:0008410
SCOP:  4001854

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
58-230 8.38e-40

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


:

Pssm-ID: 441394  Cd Length: 226  Bit Score: 137.91  E-value: 8.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651  58 DLLIGAGCVAEIETSAVslGEAGTAPRFVAALAAGTLTVRDATCPAIHTALQAAEKGVPFMPLRGVLGSDVlAHRPDWRV 137
Cdd:COG1788    60 GLLIGAGQVKKVIASYV--GGVGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDV-AEGKETRE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651 138 IDNpfaaepDPILLIPAVRPDFALFHAALADAAGNVWVGR--RRELATMAHAARDSFVTVERRISGNMLEDERLapgVIS 215
Cdd:COG1788   137 IDG------EEYVLEPALRADVALIHAQKADRAGNLVYRGtaRNFNPLMAMAAKRVIVEVEEIVEVGELDPDAV---VTP 207
                         170
                  ....*....|....*
gi 1441380651 216 GAYVTGIAHAPRGAA 230
Cdd:COG1788   208 GIFVDAVVEVPGGAR 222
 
Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
58-230 8.38e-40

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 137.91  E-value: 8.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651  58 DLLIGAGCVAEIETSAVslGEAGTAPRFVAALAAGTLTVRDATCPAIHTALQAAEKGVPFMPLRGVLGSDVlAHRPDWRV 137
Cdd:COG1788    60 GLLIGAGQVKKVIASYV--GGVGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDV-AEGKETRE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651 138 IDNpfaaepDPILLIPAVRPDFALFHAALADAAGNVWVGR--RRELATMAHAARDSFVTVERRISGNMLEDERLapgVIS 215
Cdd:COG1788   137 IDG------EEYVLEPALRADVALIHAQKADRAGNLVYRGtaRNFNPLMAMAAKRVIVEVEEIVEVGELDPDAV---VTP 207
                         170
                  ....*....|....*
gi 1441380651 216 GAYVTGIAHAPRGAA 230
Cdd:COG1788   208 GIFVDAVVEVPGGAR 222
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
6-197 1.52e-11

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: 62.22  E-value: 1.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651    6 SPDDLAARVPDGALIALPPDNSLGSVALALALIRRRARRLRLFCVPVGGFLADLLIGAGCVAEIETSAVslgeaGTAPRF 85
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGGLGLGLLAGEGDVKKIIAGHV-----GLTPLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651   86 VAALAAGTLTVRDATCPAIHTALQAAEKGVPFMPLRGVLGSDVLahRPDWRVIDNPFAAEpDPILLIPAVRPDFALFHAA 165
Cdd:smart00882  76 GRLYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVD--PRYEGGKVRPFGMG-GAYLLVPAIRPDVALIRAH 152
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1441380651  166 LADAAGNVWV---GRRRELATMAHAARDSFVTVER 197
Cdd:smart00882 153 TADEFGNLVYekeATSCGLPLTAAAAKKVIVQVEE 187
CoA_trans pfam01144
Coenzyme A transferase;
53-173 4.69e-03

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 37.28  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651  53 GGFLADLLIGAGCVAEIETSAVslGEAGTaPRFVAALAAGTLTVRDATCPAIHTALQAAEKGVPFMPLRGVLGSDVLAHr 132
Cdd:pfam01144  52 GVLGLGPLLLNGSVKKVIASYG--GETAN-PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPFEGFLTNTGIGTYVA- 127
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1441380651 133 PDWRVIDnpFAAEPDpiLLIPAVRPDFALFHAALADAAGNV 173
Cdd:pfam01144 128 PKKRVPG--FGGAMY--LLEPALRADVALIKASKADGEGNL 164
 
Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
58-230 8.38e-40

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 137.91  E-value: 8.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651  58 DLLIGAGCVAEIETSAVslGEAGTAPRFVAALAAGTLTVRDATCPAIHTALQAAEKGVPFMPLRGVLGSDVlAHRPDWRV 137
Cdd:COG1788    60 GLLIGAGQVKKVIASYV--GGVGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDV-AEGKETRE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651 138 IDNpfaaepDPILLIPAVRPDFALFHAALADAAGNVWVGR--RRELATMAHAARDSFVTVERRISGNMLEDERLapgVIS 215
Cdd:COG1788   137 IDG------EEYVLEPALRADVALIHAQKADRAGNLVYRGtaRNFNPLMAMAAKRVIVEVEEIVEVGELDPDAV---VTP 207
                         170
                  ....*....|....*
gi 1441380651 216 GAYVTGIAHAPRGAA 230
Cdd:COG1788   208 GIFVDAVVEVPGGAR 222
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
6-197 1.52e-11

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: 62.22  E-value: 1.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651    6 SPDDLAARVPDGALIALPPDNSLGSVALALALIRRRARRLRLFCVPVGGFLADLLIGAGCVAEIETSAVslgeaGTAPRF 85
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGGLGLGLLAGEGDVKKIIAGHV-----GLTPLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651   86 VAALAAGTLTVRDATCPAIHTALQAAEKGVPFMPLRGVLGSDVLahRPDWRVIDNPFAAEpDPILLIPAVRPDFALFHAA 165
Cdd:smart00882  76 GRLYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVD--PRYEGGKVRPFGMG-GAYLLVPAIRPDVALIRAH 152
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1441380651  166 LADAAGNVWV---GRRRELATMAHAARDSFVTVER 197
Cdd:smart00882 153 TADEFGNLVYekeATSCGLPLTAAAAKKVIVQVEE 187
CoA_trans pfam01144
Coenzyme A transferase;
53-173 4.69e-03

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 37.28  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441380651  53 GGFLADLLIGAGCVAEIETSAVslGEAGTaPRFVAALAAGTLTVRDATCPAIHTALQAAEKGVPFMPLRGVLGSDVLAHr 132
Cdd:pfam01144  52 GVLGLGPLLLNGSVKKVIASYG--GETAN-PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPFEGFLTNTGIGTYVA- 127
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1441380651 133 PDWRVIDnpFAAEPDpiLLIPAVRPDFALFHAALADAAGNV 173
Cdd:pfam01144 128 PKKRVPG--FGGAMY--LLEPALRADVALIKASKADGEGNL 164
 
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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