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Conserved domains on  [gi|1845976712|ref|NP_001370058|]
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Golgi resident protein GCP60 [Caenorhabditis elegans]

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 ...
280-434 5.86e-79

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: 240.46  E-value: 5.86e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845976712 280 VGHGETVTVRVPTHENGSCLFWEFATDHYDIGFGVYFEWTVADSNQVSVHVsesddeedydealeaeqAEAGGGGGGAAG 359
Cdd:pfam13897   1 VGRGEVVTVRVPTHPEGSYLFWEFATDHYDIGFGVYFEWTDPTSTAVSVHV-----------------SESSDEEDEEEE 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845976712 360 QGGPGDVEAGAMQTrrvdpNKPRQDEIIPVYRRDCHEEVYAGSHRYPGRGIYLLKFDNSYSLWRSKTLYYRVYYS 434
Cdd:pfam13897  64 EENPGDVEAGSVNA-----NKPRLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRVYYT 133
ACBP pfam00887
Acyl CoA binding protein;
24-105 7.36e-12

Acyl CoA binding protein;


:

Pssm-ID: 459982  Cd Length: 76  Bit Score: 60.69  E-value: 7.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845976712  24 EECYKLAVQYYKKehvgKQEPVGYEDRIKLLSLSKQVQHGEISDEfdNAGWLDITGNDVNKAWRELGSLSRDEAMASFVF 103
Cdd:pfam00887   1 EEKFEAAAEFVKK----LKSKPSNEEKLELYGLYKQATVGDCNTP--RPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74

                  ..
gi 1845976712 104 LV 105
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 ...
280-434 5.86e-79

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: 240.46  E-value: 5.86e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845976712 280 VGHGETVTVRVPTHENGSCLFWEFATDHYDIGFGVYFEWTVADSNQVSVHVsesddeedydealeaeqAEAGGGGGGAAG 359
Cdd:pfam13897   1 VGRGEVVTVRVPTHPEGSYLFWEFATDHYDIGFGVYFEWTDPTSTAVSVHV-----------------SESSDEEDEEEE 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845976712 360 QGGPGDVEAGAMQTrrvdpNKPRQDEIIPVYRRDCHEEVYAGSHRYPGRGIYLLKFDNSYSLWRSKTLYYRVYYS 434
Cdd:pfam13897  64 EENPGDVEAGSVNA-----NKPRLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRVYYT 133
ACBP pfam00887
Acyl CoA binding protein;
24-105 7.36e-12

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 60.69  E-value: 7.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845976712  24 EECYKLAVQYYKKehvgKQEPVGYEDRIKLLSLSKQVQHGEISDEfdNAGWLDITGNDVNKAWRELGSLSRDEAMASFVF 103
Cdd:pfam00887   1 EEKFEAAAEFVKK----LKSKPSNEEKLELYGLYKQATVGDCNTP--RPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74

                  ..
gi 1845976712 104 LV 105
Cdd:pfam00887  75 LV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
48-110 1.42e-03

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: 37.69  E-value: 1.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845976712  48 EDRIKLLSLSKQVQHGEIsdEFDNAGWLDITGNDVNKAWRELGSLSRDEAMASFVFLVDRVCP 110
Cdd:cd00435    22 EEKLQLYSLYKQATVGDC--NTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEELIA 82
 
Name Accession Description Interval E-value
GOLD_2 pfam13897
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ...
280-434 5.86e-79

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: 240.46  E-value: 5.86e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845976712 280 VGHGETVTVRVPTHENGSCLFWEFATDHYDIGFGVYFEWTVADSNQVSVHVsesddeedydealeaeqAEAGGGGGGAAG 359
Cdd:pfam13897   1 VGRGEVVTVRVPTHPEGSYLFWEFATDHYDIGFGVYFEWTDPTSTAVSVHV-----------------SESSDEEDEEEE 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845976712 360 QGGPGDVEAGAMQTrrvdpNKPRQDEIIPVYRRDCHEEVYAGSHRYPGRGIYLLKFDNSYSLWRSKTLYYRVYYS 434
Cdd:pfam13897  64 EENPGDVEAGSVNA-----NKPRLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRVYYT 133
ACBP pfam00887
Acyl CoA binding protein;
24-105 7.36e-12

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 60.69  E-value: 7.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845976712  24 EECYKLAVQYYKKehvgKQEPVGYEDRIKLLSLSKQVQHGEISDEfdNAGWLDITGNDVNKAWRELGSLSRDEAMASFVF 103
Cdd:pfam00887   1 EEKFEAAAEFVKK----LKSKPSNEEKLELYGLYKQATVGDCNTP--RPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVE 74

                  ..
gi 1845976712 104 LV 105
Cdd:pfam00887  75 LV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
48-110 1.42e-03

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: 37.69  E-value: 1.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845976712  48 EDRIKLLSLSKQVQHGEIsdEFDNAGWLDITGNDVNKAWRELGSLSRDEAMASFVFLVDRVCP 110
Cdd:cd00435    22 EEKLQLYSLYKQATVGDC--NTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEELIA 82
 
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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