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Conserved domains on  [gi|15826852|ref|NP_073572|]
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Golgi resident protein GCP60 [Homo sapiens]

Protein Classification

acyl-CoA-binding domain-containing protein( domain architecture ID 10468367)

acyl-CoA-binding domain-containing protein binds acyl-CoA esters and may play a role in housekeeping and/or trafficking

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GOLD_2 pfam13897
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ...
 397-527 3.69e-80

Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.


:

Pssm-ID: 464028  Cd Length: 133  Bit Score: 246.62  E-value: 3.69e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826852   397 VGRGEVVTVRVPTHEEGSYLFWEFATDNYDIGFGVYFEWTDSPNTAVSVHVS--ESSDDDEEEEENIGCEEKAKKNANKP 474
Cdd:pfam13897   1 VGRGEVVTVRVPTHPEGSYLFWEFATDHYDIGFGVYFEWTDPTSTAVSVHVSesSDEEDEEEEEENPGDVEAGSVNANKP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15826852   475 LLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKSVYYRVYYT 527
Cdd:pfam13897  81 RLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRVYYT 133
ACBP pfam00887
Acyl CoA binding protein;
84-165 2.84e-17

Acyl CoA binding protein;


:

Pssm-ID: 459982  Cd Length: 76  Bit Score: 76.48  E-value: 2.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826852    84 EELYGLALRFFKekdGKAFHPTYEEKLKLVALHKQVLMGPYNPdtcPEVGFFDVLGNDRRREWAALGNMSKEDAMVEFVK 163
Cdd:pfam00887   1 EEKFEAAAEFVK---KLKSKPSNEEKLELYGLYKQATVGDCNT---PRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74


                  ..
gi 15826852   164 LL 165
Cdd:pfam00887  75 LV 76
 
Name Accession Description Interval E-value
GOLD_2 pfam13897
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ...
 397-527 3.69e-80

Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.


Pssm-ID: 464028  Cd Length: 133  Bit Score: 246.62  E-value: 3.69e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826852   397 VGRGEVVTVRVPTHEEGSYLFWEFATDNYDIGFGVYFEWTDSPNTAVSVHVS--ESSDDDEEEEENIGCEEKAKKNANKP 474
Cdd:pfam13897   1 VGRGEVVTVRVPTHPEGSYLFWEFATDHYDIGFGVYFEWTDPTSTAVSVHVSesSDEEDEEEEEENPGDVEAGSVNANKP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15826852   475 LLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKSVYYRVYYT 527
Cdd:pfam13897  81 RLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRVYYT 133
ACBP pfam00887
Acyl CoA binding protein;
84-165 2.84e-17

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 76.48  E-value: 2.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826852    84 EELYGLALRFFKekdGKAFHPTYEEKLKLVALHKQVLMGPYNPdtcPEVGFFDVLGNDRRREWAALGNMSKEDAMVEFVK 163
Cdd:pfam00887   1 EEKFEAAAEFVK---KLKSKPSNEEKLELYGLYKQATVGDCNT---PRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74


                  ..
gi 15826852   164 LL 165
Cdd:pfam00887  75 LV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 104-175 2.28e-09

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 54.25  E-value: 2.28e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15826852 104 PTYEEKLKLVALHKQVLMGPYNPDtCPevGFFDVLGNDRRREWAALGNMSKEDAMVEFVKLLNRcchLFSTY 175
Cdd:cd00435  19 PSNEEKLQLYSLYKQATVGDCNTE-RP--GMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEE---LIAKY 84
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 102-165 5.99e-03

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 38.05  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826852    102 FHPTYEEKLKLVALHKQVLMGPYNPDTCPEVGFFD----------------VLGNDRRREWAALGNMSKEDAMVEFVKLL 165
Cdd:smart00295 111 LPCPEEEALLLAALALQAEFGDYDEELHDLRGELSlkrflpkqlldsrklkEWRERIVELHKELIGLSPEEAKLKYLELA 190
 
Name Accession Description Interval E-value
GOLD_2 pfam13897
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ...
 397-527 3.69e-80

Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.


Pssm-ID: 464028  Cd Length: 133  Bit Score: 246.62  E-value: 3.69e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826852   397 VGRGEVVTVRVPTHEEGSYLFWEFATDNYDIGFGVYFEWTDSPNTAVSVHVS--ESSDDDEEEEENIGCEEKAKKNANKP 474
Cdd:pfam13897   1 VGRGEVVTVRVPTHPEGSYLFWEFATDHYDIGFGVYFEWTDPTSTAVSVHVSesSDEEDEEEEEENPGDVEAGSVNANKP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15826852   475 LLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKSVYYRVYYT 527
Cdd:pfam13897  81 RLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRVYYT 133
ACBP pfam00887
Acyl CoA binding protein;
84-165 2.84e-17

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 76.48  E-value: 2.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826852    84 EELYGLALRFFKekdGKAFHPTYEEKLKLVALHKQVLMGPYNPdtcPEVGFFDVLGNDRRREWAALGNMSKEDAMVEFVK 163
Cdd:pfam00887   1 EEKFEAAAEFVK---KLKSKPSNEEKLELYGLYKQATVGDCNT---PRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74


                  ..
gi 15826852   164 LL 165
Cdd:pfam00887  75 LV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 104-175 2.28e-09

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 54.25  E-value: 2.28e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15826852 104 PTYEEKLKLVALHKQVLMGPYNPDtCPevGFFDVLGNDRRREWAALGNMSKEDAMVEFVKLLNRcchLFSTY 175
Cdd:cd00435  19 PSNEEKLQLYSLYKQATVGDCNTE-RP--GMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEE---LIAKY 84
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 102-165 5.99e-03

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 38.05  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15826852    102 FHPTYEEKLKLVALHKQVLMGPYNPDTCPEVGFFD----------------VLGNDRRREWAALGNMSKEDAMVEFVKLL 165
Cdd:smart00295 111 LPCPEEEALLLAALALQAEFGDYDEELHDLRGELSlkrflpkqlldsrklkEWRERIVELHKELIGLSPEEAKLKYLELA 190
 
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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